data_9BL3
# 
_entry.id   9BL3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BL3         pdb_00009bl3 10.2210/pdb9bl3/pdb 
WWPDB D_1000283636 ?            ?                   
# 
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 2024-11-13 
2 'Structure model' 1 1 2024-12-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BL3 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9BL2 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              jamie.rossjohn@monash.edu 
_pdbx_contact_author.name_first         Jamie 
_pdbx_contact_author.name_last          Rossjohn 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2020-7522 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Faoro, C.'    1 ? 
'Rossjohn, J.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            187 
_citation.language                  ? 
_citation.page_first                7008 
_citation.page_last                 ? 
_citation.title                     
'An archaic HLA class I receptor allele diversifies natural killer cell-driven immunity in First Nations peoples of Oceania.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2024.10.005 
_citation.pdbx_database_id_PubMed   39476840 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Loh, L.'             1  ? 
primary 'Saunders, P.M.'      2  ? 
primary 'Faoro, C.'           3  ? 
primary 'Font-Porterias, N.'  4  ? 
primary 'Nemat-Gorgani, N.'   5  ? 
primary 'Harrison, G.F.'      6  ? 
primary 'Sadeeq, S.'          7  ? 
primary 'Hensen, L.'          8  ? 
primary 'Wong, S.C.'          9  ? 
primary 'Widjaja, J.'         10 ? 
primary 'Clemens, E.B.'       11 ? 
primary 'Zhu, S.'             12 ? 
primary 'Kichula, K.M.'       13 ? 
primary 'Tao, S.'             14 ? 
primary 'Zhu, F.'             15 ? 
primary 'Montero-Martin, G.'  16 ? 
primary 'Fernandez-Vina, M.'  17 ? 
primary 'Guethlein, L.A.'     18 ? 
primary 'Vivian, J.P.'        19 ? 
primary 'Davies, J.'          20 ? 
primary 'Mentzer, A.J.'       21 ? 
primary 'Oppenheimer, S.J.'   22 ? 
primary 'Pomat, W.'           23 ? 
primary 'Ioannidis, A.G.'     24 ? 
primary 'Barberena-Jonas, C.' 25 ? 
primary 'Moreno-Estrada, A.'  26 ? 
primary 'Miller, A.'          27 ? 
primary 'Parham, P.'          28 ? 
primary 'Rossjohn, J.'        29 ? 
primary 'Tong, S.Y.C.'        30 ? 
primary 'Kedzierska, K.'      31 ? 
primary 'Brooks, A.G.'        32 ? 
primary 'Norman, P.J.'        33 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'HLA-B alpha chain (B*5703GB)'                  31811.285 1   ? ? ?                                      ? 
2 polymer     man Beta-2-microglobulin                            11879.356 1   ? ? 'UNP residues 21-119'                  ? 
3 polymer     syn 'Catenin alpha-1 peptide'                       1057.200  1   ? ? 'residues 850-859 (Uniprot numbering)' ? 
4 polymer     man 'Killer cell immunoglobulin-like receptor 3DL1' 33899.281 1   ? ? 'residues 1-299'                       ? 
5 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose        221.208   4   ? ? ?                                      ? 
6 water       nat water                                           18.015    385 ? ? ?                                      ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'MHC class I antigen, Human Leukocyte Antigen B*57:03'                          
3 'Alpha E-catenin,Cadherin-associated protein,Renal carcinoma antigen NY-REN-13' 
# 
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 
;GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYWDGETRNMKASAQTYRENLRI
ALRYYNQSEAGSHIIQVMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYL
EGLCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
;
;GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYWDGETRNMKASAQTYRENLRI
ALRYYNQSEAGSHIIQVMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYL
EGLCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
;
A ? 
2 'polypeptide(L)' no no 
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
;MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
;
B ? 
3 'polypeptide(L)' no no ASLNLPAVSW ASLNLPAVSW C ? 
4 'polypeptide(L)' no no 
;HMGGQDKPFLSAWPSAVVPRGGHVTLRCHYRHRFNNFMLYKEDRIHVPIFHGRLFQESFNMSPVTTAHAGNYTCRGSHPH
SPTGWSAASNPVVIMVTGNHRKPSLLAHPGPLVKSGERVILQCWSDIMFEHFFLHKEGISKDPSRLVGQIHDGVSKANFS
IGPMMFALAGTYRCYGSVTHTPYQLSAPSDPLDIVVTGPYEKPSLSAQPGPKVQAGESVTLSCSSRSSYDMYHLSREGGA
HERRLPAVRKVNRTFQADFPLGPATHGGTYRCFGSFRHSPYEWSDPSDPLLVSVTGNPSHHHHHH
;
;HMGGQDKPFLSAWPSAVVPRGGHVTLRCHYRHRFNNFMLYKEDRIHVPIFHGRLFQESFNMSPVTTAHAGNYTCRGSHPH
SPTGWSAASNPVVIMVTGNHRKPSLLAHPGPLVKSGERVILQCWSDIMFEHFFLHKEGISKDPSRLVGQIHDGVSKANFS
IGPMMFALAGTYRCYGSVTHTPYQLSAPSDPLDIVVTGPYEKPSLSAQPGPKVQAGESVTLSCSSRSSYDMYHLSREGGA
HERRLPAVRKVNRTFQADFPLGPATHGGTYRCFGSFRHSPYEWSDPSDPLLVSVTGNPSHHHHHH
;
G ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
6 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   SER n 
1 5   MET n 
1 6   ARG n 
1 7   TYR n 
1 8   PHE n 
1 9   TYR n 
1 10  THR n 
1 11  ALA n 
1 12  MET n 
1 13  SER n 
1 14  ARG n 
1 15  PRO n 
1 16  GLY n 
1 17  ARG n 
1 18  GLY n 
1 19  GLU n 
1 20  PRO n 
1 21  ARG n 
1 22  PHE n 
1 23  ILE n 
1 24  ALA n 
1 25  VAL n 
1 26  GLY n 
1 27  TYR n 
1 28  VAL n 
1 29  ASP n 
1 30  ASP n 
1 31  THR n 
1 32  GLN n 
1 33  PHE n 
1 34  VAL n 
1 35  ARG n 
1 36  PHE n 
1 37  ASP n 
1 38  SER n 
1 39  ASP n 
1 40  ALA n 
1 41  ALA n 
1 42  SER n 
1 43  PRO n 
1 44  ARG n 
1 45  MET n 
1 46  ALA n 
1 47  PRO n 
1 48  ARG n 
1 49  ALA n 
1 50  PRO n 
1 51  TRP n 
1 52  ILE n 
1 53  GLU n 
1 54  GLN n 
1 55  GLU n 
1 56  GLY n 
1 57  PRO n 
1 58  GLU n 
1 59  TYR n 
1 60  TRP n 
1 61  ASP n 
1 62  GLY n 
1 63  GLU n 
1 64  THR n 
1 65  ARG n 
1 66  ASN n 
1 67  MET n 
1 68  LYS n 
1 69  ALA n 
1 70  SER n 
1 71  ALA n 
1 72  GLN n 
1 73  THR n 
1 74  TYR n 
1 75  ARG n 
1 76  GLU n 
1 77  ASN n 
1 78  LEU n 
1 79  ARG n 
1 80  ILE n 
1 81  ALA n 
1 82  LEU n 
1 83  ARG n 
1 84  TYR n 
1 85  TYR n 
1 86  ASN n 
1 87  GLN n 
1 88  SER n 
1 89  GLU n 
1 90  ALA n 
1 91  GLY n 
1 92  SER n 
1 93  HIS n 
1 94  ILE n 
1 95  ILE n 
1 96  GLN n 
1 97  VAL n 
1 98  MET n 
1 99  TYR n 
1 100 GLY n 
1 101 CYS n 
1 102 ASP n 
1 103 VAL n 
1 104 GLY n 
1 105 PRO n 
1 106 ASP n 
1 107 GLY n 
1 108 ARG n 
1 109 LEU n 
1 110 LEU n 
1 111 ARG n 
1 112 GLY n 
1 113 HIS n 
1 114 ASN n 
1 115 GLN n 
1 116 TYR n 
1 117 ALA n 
1 118 TYR n 
1 119 ASP n 
1 120 GLY n 
1 121 LYS n 
1 122 ASP n 
1 123 TYR n 
1 124 ILE n 
1 125 ALA n 
1 126 LEU n 
1 127 ASN n 
1 128 GLU n 
1 129 ASP n 
1 130 LEU n 
1 131 SER n 
1 132 SER n 
1 133 TRP n 
1 134 THR n 
1 135 ALA n 
1 136 ALA n 
1 137 ASP n 
1 138 THR n 
1 139 ALA n 
1 140 ALA n 
1 141 GLN n 
1 142 ILE n 
1 143 THR n 
1 144 GLN n 
1 145 ARG n 
1 146 LYS n 
1 147 TRP n 
1 148 GLU n 
1 149 ALA n 
1 150 ALA n 
1 151 ARG n 
1 152 VAL n 
1 153 ALA n 
1 154 GLU n 
1 155 GLN n 
1 156 LEU n 
1 157 ARG n 
1 158 ALA n 
1 159 TYR n 
1 160 LEU n 
1 161 GLU n 
1 162 GLY n 
1 163 LEU n 
1 164 CYS n 
1 165 VAL n 
1 166 GLU n 
1 167 TRP n 
1 168 LEU n 
1 169 ARG n 
1 170 ARG n 
1 171 TYR n 
1 172 LEU n 
1 173 GLU n 
1 174 ASN n 
1 175 GLY n 
1 176 LYS n 
1 177 GLU n 
1 178 THR n 
1 179 LEU n 
1 180 GLN n 
1 181 ARG n 
1 182 ALA n 
1 183 ASP n 
1 184 PRO n 
1 185 PRO n 
1 186 LYS n 
1 187 THR n 
1 188 HIS n 
1 189 VAL n 
1 190 THR n 
1 191 HIS n 
1 192 HIS n 
1 193 PRO n 
1 194 ILE n 
1 195 SER n 
1 196 ASP n 
1 197 HIS n 
1 198 GLU n 
1 199 ALA n 
1 200 THR n 
1 201 LEU n 
1 202 ARG n 
1 203 CYS n 
1 204 TRP n 
1 205 ALA n 
1 206 LEU n 
1 207 GLY n 
1 208 PHE n 
1 209 TYR n 
1 210 PRO n 
1 211 ALA n 
1 212 GLU n 
1 213 ILE n 
1 214 THR n 
1 215 LEU n 
1 216 THR n 
1 217 TRP n 
1 218 GLN n 
1 219 ARG n 
1 220 ASP n 
1 221 GLY n 
1 222 GLU n 
1 223 ASP n 
1 224 GLN n 
1 225 THR n 
1 226 GLN n 
1 227 ASP n 
1 228 THR n 
1 229 GLU n 
1 230 LEU n 
1 231 VAL n 
1 232 GLU n 
1 233 THR n 
1 234 ARG n 
1 235 PRO n 
1 236 ALA n 
1 237 GLY n 
1 238 ASP n 
1 239 ARG n 
1 240 THR n 
1 241 PHE n 
1 242 GLN n 
1 243 LYS n 
1 244 TRP n 
1 245 ALA n 
1 246 ALA n 
1 247 VAL n 
1 248 VAL n 
1 249 VAL n 
1 250 PRO n 
1 251 SER n 
1 252 GLY n 
1 253 GLU n 
1 254 GLU n 
1 255 GLN n 
1 256 ARG n 
1 257 TYR n 
1 258 THR n 
1 259 CYS n 
1 260 HIS n 
1 261 VAL n 
1 262 GLN n 
1 263 HIS n 
1 264 GLU n 
1 265 GLY n 
1 266 LEU n 
1 267 PRO n 
1 268 LYS n 
1 269 PRO n 
1 270 LEU n 
1 271 THR n 
1 272 LEU n 
1 273 ARG n 
1 274 TRP n 
1 275 GLU n 
1 276 PRO n 
2 1   MET n 
2 2   ILE n 
2 3   GLN n 
2 4   ARG n 
2 5   THR n 
2 6   PRO n 
2 7   LYS n 
2 8   ILE n 
2 9   GLN n 
2 10  VAL n 
2 11  TYR n 
2 12  SER n 
2 13  ARG n 
2 14  HIS n 
2 15  PRO n 
2 16  ALA n 
2 17  GLU n 
2 18  ASN n 
2 19  GLY n 
2 20  LYS n 
2 21  SER n 
2 22  ASN n 
2 23  PHE n 
2 24  LEU n 
2 25  ASN n 
2 26  CYS n 
2 27  TYR n 
2 28  VAL n 
2 29  SER n 
2 30  GLY n 
2 31  PHE n 
2 32  HIS n 
2 33  PRO n 
2 34  SER n 
2 35  ASP n 
2 36  ILE n 
2 37  GLU n 
2 38  VAL n 
2 39  ASP n 
2 40  LEU n 
2 41  LEU n 
2 42  LYS n 
2 43  ASN n 
2 44  GLY n 
2 45  GLU n 
2 46  ARG n 
2 47  ILE n 
2 48  GLU n 
2 49  LYS n 
2 50  VAL n 
2 51  GLU n 
2 52  HIS n 
2 53  SER n 
2 54  ASP n 
2 55  LEU n 
2 56  SER n 
2 57  PHE n 
2 58  SER n 
2 59  LYS n 
2 60  ASP n 
2 61  TRP n 
2 62  SER n 
2 63  PHE n 
2 64  TYR n 
2 65  LEU n 
2 66  LEU n 
2 67  TYR n 
2 68  TYR n 
2 69  THR n 
2 70  GLU n 
2 71  PHE n 
2 72  THR n 
2 73  PRO n 
2 74  THR n 
2 75  GLU n 
2 76  LYS n 
2 77  ASP n 
2 78  GLU n 
2 79  TYR n 
2 80  ALA n 
2 81  CYS n 
2 82  ARG n 
2 83  VAL n 
2 84  ASN n 
2 85  HIS n 
2 86  VAL n 
2 87  THR n 
2 88  LEU n 
2 89  SER n 
2 90  GLN n 
2 91  PRO n 
2 92  LYS n 
2 93  ILE n 
2 94  VAL n 
2 95  LYS n 
2 96  TRP n 
2 97  ASP n 
2 98  ARG n 
2 99  ASP n 
2 100 MET n 
3 1   ALA n 
3 2   SER n 
3 3   LEU n 
3 4   ASN n 
3 5   LEU n 
3 6   PRO n 
3 7   ALA n 
3 8   VAL n 
3 9   SER n 
3 10  TRP n 
4 1   HIS n 
4 2   MET n 
4 3   GLY n 
4 4   GLY n 
4 5   GLN n 
4 6   ASP n 
4 7   LYS n 
4 8   PRO n 
4 9   PHE n 
4 10  LEU n 
4 11  SER n 
4 12  ALA n 
4 13  TRP n 
4 14  PRO n 
4 15  SER n 
4 16  ALA n 
4 17  VAL n 
4 18  VAL n 
4 19  PRO n 
4 20  ARG n 
4 21  GLY n 
4 22  GLY n 
4 23  HIS n 
4 24  VAL n 
4 25  THR n 
4 26  LEU n 
4 27  ARG n 
4 28  CYS n 
4 29  HIS n 
4 30  TYR n 
4 31  ARG n 
4 32  HIS n 
4 33  ARG n 
4 34  PHE n 
4 35  ASN n 
4 36  ASN n 
4 37  PHE n 
4 38  MET n 
4 39  LEU n 
4 40  TYR n 
4 41  LYS n 
4 42  GLU n 
4 43  ASP n 
4 44  ARG n 
4 45  ILE n 
4 46  HIS n 
4 47  VAL n 
4 48  PRO n 
4 49  ILE n 
4 50  PHE n 
4 51  HIS n 
4 52  GLY n 
4 53  ARG n 
4 54  LEU n 
4 55  PHE n 
4 56  GLN n 
4 57  GLU n 
4 58  SER n 
4 59  PHE n 
4 60  ASN n 
4 61  MET n 
4 62  SER n 
4 63  PRO n 
4 64  VAL n 
4 65  THR n 
4 66  THR n 
4 67  ALA n 
4 68  HIS n 
4 69  ALA n 
4 70  GLY n 
4 71  ASN n 
4 72  TYR n 
4 73  THR n 
4 74  CYS n 
4 75  ARG n 
4 76  GLY n 
4 77  SER n 
4 78  HIS n 
4 79  PRO n 
4 80  HIS n 
4 81  SER n 
4 82  PRO n 
4 83  THR n 
4 84  GLY n 
4 85  TRP n 
4 86  SER n 
4 87  ALA n 
4 88  ALA n 
4 89  SER n 
4 90  ASN n 
4 91  PRO n 
4 92  VAL n 
4 93  VAL n 
4 94  ILE n 
4 95  MET n 
4 96  VAL n 
4 97  THR n 
4 98  GLY n 
4 99  ASN n 
4 100 HIS n 
4 101 ARG n 
4 102 LYS n 
4 103 PRO n 
4 104 SER n 
4 105 LEU n 
4 106 LEU n 
4 107 ALA n 
4 108 HIS n 
4 109 PRO n 
4 110 GLY n 
4 111 PRO n 
4 112 LEU n 
4 113 VAL n 
4 114 LYS n 
4 115 SER n 
4 116 GLY n 
4 117 GLU n 
4 118 ARG n 
4 119 VAL n 
4 120 ILE n 
4 121 LEU n 
4 122 GLN n 
4 123 CYS n 
4 124 TRP n 
4 125 SER n 
4 126 ASP n 
4 127 ILE n 
4 128 MET n 
4 129 PHE n 
4 130 GLU n 
4 131 HIS n 
4 132 PHE n 
4 133 PHE n 
4 134 LEU n 
4 135 HIS n 
4 136 LYS n 
4 137 GLU n 
4 138 GLY n 
4 139 ILE n 
4 140 SER n 
4 141 LYS n 
4 142 ASP n 
4 143 PRO n 
4 144 SER n 
4 145 ARG n 
4 146 LEU n 
4 147 VAL n 
4 148 GLY n 
4 149 GLN n 
4 150 ILE n 
4 151 HIS n 
4 152 ASP n 
4 153 GLY n 
4 154 VAL n 
4 155 SER n 
4 156 LYS n 
4 157 ALA n 
4 158 ASN n 
4 159 PHE n 
4 160 SER n 
4 161 ILE n 
4 162 GLY n 
4 163 PRO n 
4 164 MET n 
4 165 MET n 
4 166 PHE n 
4 167 ALA n 
4 168 LEU n 
4 169 ALA n 
4 170 GLY n 
4 171 THR n 
4 172 TYR n 
4 173 ARG n 
4 174 CYS n 
4 175 TYR n 
4 176 GLY n 
4 177 SER n 
4 178 VAL n 
4 179 THR n 
4 180 HIS n 
4 181 THR n 
4 182 PRO n 
4 183 TYR n 
4 184 GLN n 
4 185 LEU n 
4 186 SER n 
4 187 ALA n 
4 188 PRO n 
4 189 SER n 
4 190 ASP n 
4 191 PRO n 
4 192 LEU n 
4 193 ASP n 
4 194 ILE n 
4 195 VAL n 
4 196 VAL n 
4 197 THR n 
4 198 GLY n 
4 199 PRO n 
4 200 TYR n 
4 201 GLU n 
4 202 LYS n 
4 203 PRO n 
4 204 SER n 
4 205 LEU n 
4 206 SER n 
4 207 ALA n 
4 208 GLN n 
4 209 PRO n 
4 210 GLY n 
4 211 PRO n 
4 212 LYS n 
4 213 VAL n 
4 214 GLN n 
4 215 ALA n 
4 216 GLY n 
4 217 GLU n 
4 218 SER n 
4 219 VAL n 
4 220 THR n 
4 221 LEU n 
4 222 SER n 
4 223 CYS n 
4 224 SER n 
4 225 SER n 
4 226 ARG n 
4 227 SER n 
4 228 SER n 
4 229 TYR n 
4 230 ASP n 
4 231 MET n 
4 232 TYR n 
4 233 HIS n 
4 234 LEU n 
4 235 SER n 
4 236 ARG n 
4 237 GLU n 
4 238 GLY n 
4 239 GLY n 
4 240 ALA n 
4 241 HIS n 
4 242 GLU n 
4 243 ARG n 
4 244 ARG n 
4 245 LEU n 
4 246 PRO n 
4 247 ALA n 
4 248 VAL n 
4 249 ARG n 
4 250 LYS n 
4 251 VAL n 
4 252 ASN n 
4 253 ARG n 
4 254 THR n 
4 255 PHE n 
4 256 GLN n 
4 257 ALA n 
4 258 ASP n 
4 259 PHE n 
4 260 PRO n 
4 261 LEU n 
4 262 GLY n 
4 263 PRO n 
4 264 ALA n 
4 265 THR n 
4 266 HIS n 
4 267 GLY n 
4 268 GLY n 
4 269 THR n 
4 270 TYR n 
4 271 ARG n 
4 272 CYS n 
4 273 PHE n 
4 274 GLY n 
4 275 SER n 
4 276 PHE n 
4 277 ARG n 
4 278 HIS n 
4 279 SER n 
4 280 PRO n 
4 281 TYR n 
4 282 GLU n 
4 283 TRP n 
4 284 SER n 
4 285 ASP n 
4 286 PRO n 
4 287 SER n 
4 288 ASP n 
4 289 PRO n 
4 290 LEU n 
4 291 LEU n 
4 292 VAL n 
4 293 SER n 
4 294 VAL n 
4 295 THR n 
4 296 GLY n 
4 297 ASN n 
4 298 PRO n 
4 299 SER n 
4 300 HIS n 
4 301 HIS n 
4 302 HIS n 
4 303 HIS n 
4 304 HIS n 
4 305 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 276 human ? HLA-B                      ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ?     
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? pET30 ? ? ? ? 
2 1 sample 'Biological sequence' 1 100 human ? 'B2M, CDABP0092, HDCMA22P' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ?     
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? pET30 ? ? ? ? 
4 1 sample 'Biological sequence' 1 305 human ? KIR3DL1                    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens'               9606   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?     ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       10 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   1   GLY GLY A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   MET 5   5   5   MET MET A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  MET 45  45  45  MET MET A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  TRP 51  51  51  TRP TRP A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  MET 67  67  67  MET MET A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 TRP 133 133 133 TRP TRP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 TRP 147 147 147 TRP TRP A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 CYS 164 164 164 CYS CYS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 HIS 188 188 188 HIS HIS A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 HIS 191 191 191 HIS HIS A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 CYS 203 203 203 CYS CYS A . n 
A 1 204 TRP 204 204 204 TRP TRP A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 TRP 217 217 217 TRP TRP A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 GLN 226 226 226 GLN GLN A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 ARG 239 239 239 ARG ARG A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 CYS 259 259 259 CYS CYS A . n 
A 1 260 HIS 260 260 260 HIS HIS A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 GLN 262 262 262 GLN GLN A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 LYS 268 268 268 LYS LYS A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 TRP 274 274 274 TRP TRP A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
B 2 1   MET 1   0   0   MET MET B . n 
B 2 2   ILE 2   1   1   ILE ILE B . n 
B 2 3   GLN 3   2   2   GLN GLN B . n 
B 2 4   ARG 4   3   3   ARG ARG B . n 
B 2 5   THR 5   4   4   THR THR B . n 
B 2 6   PRO 6   5   5   PRO PRO B . n 
B 2 7   LYS 7   6   6   LYS LYS B . n 
B 2 8   ILE 8   7   7   ILE ILE B . n 
B 2 9   GLN 9   8   8   GLN GLN B . n 
B 2 10  VAL 10  9   9   VAL VAL B . n 
B 2 11  TYR 11  10  10  TYR TYR B . n 
B 2 12  SER 12  11  11  SER SER B . n 
B 2 13  ARG 13  12  12  ARG ARG B . n 
B 2 14  HIS 14  13  13  HIS HIS B . n 
B 2 15  PRO 15  14  14  PRO PRO B . n 
B 2 16  ALA 16  15  15  ALA ALA B . n 
B 2 17  GLU 17  16  16  GLU GLU B . n 
B 2 18  ASN 18  17  17  ASN ASN B . n 
B 2 19  GLY 19  18  18  GLY GLY B . n 
B 2 20  LYS 20  19  19  LYS LYS B . n 
B 2 21  SER 21  20  20  SER SER B . n 
B 2 22  ASN 22  21  21  ASN ASN B . n 
B 2 23  PHE 23  22  22  PHE PHE B . n 
B 2 24  LEU 24  23  23  LEU LEU B . n 
B 2 25  ASN 25  24  24  ASN ASN B . n 
B 2 26  CYS 26  25  25  CYS CYS B . n 
B 2 27  TYR 27  26  26  TYR TYR B . n 
B 2 28  VAL 28  27  27  VAL VAL B . n 
B 2 29  SER 29  28  28  SER SER B . n 
B 2 30  GLY 30  29  29  GLY GLY B . n 
B 2 31  PHE 31  30  30  PHE PHE B . n 
B 2 32  HIS 32  31  31  HIS HIS B . n 
B 2 33  PRO 33  32  32  PRO PRO B . n 
B 2 34  SER 34  33  33  SER SER B . n 
B 2 35  ASP 35  34  34  ASP ASP B . n 
B 2 36  ILE 36  35  35  ILE ILE B . n 
B 2 37  GLU 37  36  36  GLU GLU B . n 
B 2 38  VAL 38  37  37  VAL VAL B . n 
B 2 39  ASP 39  38  38  ASP ASP B . n 
B 2 40  LEU 40  39  39  LEU LEU B . n 
B 2 41  LEU 41  40  40  LEU LEU B . n 
B 2 42  LYS 42  41  41  LYS LYS B . n 
B 2 43  ASN 43  42  42  ASN ASN B . n 
B 2 44  GLY 44  43  43  GLY GLY B . n 
B 2 45  GLU 45  44  44  GLU GLU B . n 
B 2 46  ARG 46  45  45  ARG ARG B . n 
B 2 47  ILE 47  46  46  ILE ILE B . n 
B 2 48  GLU 48  47  47  GLU GLU B . n 
B 2 49  LYS 49  48  48  LYS LYS B . n 
B 2 50  VAL 50  49  49  VAL VAL B . n 
B 2 51  GLU 51  50  50  GLU GLU B . n 
B 2 52  HIS 52  51  51  HIS HIS B . n 
B 2 53  SER 53  52  52  SER SER B . n 
B 2 54  ASP 54  53  53  ASP ASP B . n 
B 2 55  LEU 55  54  54  LEU LEU B . n 
B 2 56  SER 56  55  55  SER SER B . n 
B 2 57  PHE 57  56  56  PHE PHE B . n 
B 2 58  SER 58  57  57  SER SER B . n 
B 2 59  LYS 59  58  58  LYS LYS B . n 
B 2 60  ASP 60  59  59  ASP ASP B . n 
B 2 61  TRP 61  60  60  TRP TRP B . n 
B 2 62  SER 62  61  61  SER SER B . n 
B 2 63  PHE 63  62  62  PHE PHE B . n 
B 2 64  TYR 64  63  63  TYR TYR B . n 
B 2 65  LEU 65  64  64  LEU LEU B . n 
B 2 66  LEU 66  65  65  LEU LEU B . n 
B 2 67  TYR 67  66  66  TYR TYR B . n 
B 2 68  TYR 68  67  67  TYR TYR B . n 
B 2 69  THR 69  68  68  THR THR B . n 
B 2 70  GLU 70  69  69  GLU GLU B . n 
B 2 71  PHE 71  70  70  PHE PHE B . n 
B 2 72  THR 72  71  71  THR THR B . n 
B 2 73  PRO 73  72  72  PRO PRO B . n 
B 2 74  THR 74  73  73  THR THR B . n 
B 2 75  GLU 75  74  74  GLU GLU B . n 
B 2 76  LYS 76  75  75  LYS LYS B . n 
B 2 77  ASP 77  76  76  ASP ASP B . n 
B 2 78  GLU 78  77  77  GLU GLU B . n 
B 2 79  TYR 79  78  78  TYR TYR B . n 
B 2 80  ALA 80  79  79  ALA ALA B . n 
B 2 81  CYS 81  80  80  CYS CYS B . n 
B 2 82  ARG 82  81  81  ARG ARG B . n 
B 2 83  VAL 83  82  82  VAL VAL B . n 
B 2 84  ASN 84  83  83  ASN ASN B . n 
B 2 85  HIS 85  84  84  HIS HIS B . n 
B 2 86  VAL 86  85  85  VAL VAL B . n 
B 2 87  THR 87  86  86  THR THR B . n 
B 2 88  LEU 88  87  87  LEU LEU B . n 
B 2 89  SER 89  88  88  SER SER B . n 
B 2 90  GLN 90  89  89  GLN GLN B . n 
B 2 91  PRO 91  90  90  PRO PRO B . n 
B 2 92  LYS 92  91  91  LYS LYS B . n 
B 2 93  ILE 93  92  92  ILE ILE B . n 
B 2 94  VAL 94  93  93  VAL VAL B . n 
B 2 95  LYS 95  94  94  LYS LYS B . n 
B 2 96  TRP 96  95  95  TRP TRP B . n 
B 2 97  ASP 97  96  96  ASP ASP B . n 
B 2 98  ARG 98  97  97  ARG ARG B . n 
B 2 99  ASP 99  98  98  ASP ASP B . n 
B 2 100 MET 100 99  99  MET MET B . n 
C 3 1   ALA 1   1   1   ALA ALA C . n 
C 3 2   SER 2   2   2   SER SER C . n 
C 3 3   LEU 3   3   3   LEU LEU C . n 
C 3 4   ASN 4   4   4   ASN ASN C . n 
C 3 5   LEU 5   5   5   LEU LEU C . n 
C 3 6   PRO 6   6   6   PRO PRO C . n 
C 3 7   ALA 7   7   7   ALA ALA C . n 
C 3 8   VAL 8   8   8   VAL VAL C . n 
C 3 9   SER 9   9   9   SER SER C . n 
C 3 10  TRP 10  10  10  TRP TRP C . n 
D 4 1   HIS 1   1   ?   ?   ?   G . n 
D 4 2   MET 2   2   ?   ?   ?   G . n 
D 4 3   GLY 3   3   ?   ?   ?   G . n 
D 4 4   GLY 4   4   ?   ?   ?   G . n 
D 4 5   GLN 5   5   ?   ?   ?   G . n 
D 4 6   ASP 6   6   6   ASP ASP G . n 
D 4 7   LYS 7   7   7   LYS LYS G . n 
D 4 8   PRO 8   8   8   PRO PRO G . n 
D 4 9   PHE 9   9   9   PHE PHE G . n 
D 4 10  LEU 10  10  10  LEU LEU G . n 
D 4 11  SER 11  11  11  SER SER G . n 
D 4 12  ALA 12  12  12  ALA ALA G . n 
D 4 13  TRP 13  13  13  TRP TRP G . n 
D 4 14  PRO 14  14  14  PRO PRO G . n 
D 4 15  SER 15  15  15  SER SER G . n 
D 4 16  ALA 16  16  16  ALA ALA G . n 
D 4 17  VAL 17  17  17  VAL VAL G . n 
D 4 18  VAL 18  18  18  VAL VAL G . n 
D 4 19  PRO 19  19  19  PRO PRO G . n 
D 4 20  ARG 20  20  20  ARG ARG G . n 
D 4 21  GLY 21  21  21  GLY GLY G . n 
D 4 22  GLY 22  22  22  GLY GLY G . n 
D 4 23  HIS 23  23  23  HIS HIS G . n 
D 4 24  VAL 24  24  24  VAL VAL G . n 
D 4 25  THR 25  25  25  THR THR G . n 
D 4 26  LEU 26  26  26  LEU LEU G . n 
D 4 27  ARG 27  27  27  ARG ARG G . n 
D 4 28  CYS 28  28  28  CYS CYS G . n 
D 4 29  HIS 29  29  29  HIS HIS G . n 
D 4 30  TYR 30  30  30  TYR TYR G . n 
D 4 31  ARG 31  31  31  ARG ARG G . n 
D 4 32  HIS 32  32  32  HIS HIS G . n 
D 4 33  ARG 33  33  33  ARG ARG G . n 
D 4 34  PHE 34  34  34  PHE PHE G . n 
D 4 35  ASN 35  35  35  ASN ASN G . n 
D 4 36  ASN 36  36  36  ASN ASN G . n 
D 4 37  PHE 37  37  37  PHE PHE G . n 
D 4 38  MET 38  38  38  MET MET G . n 
D 4 39  LEU 39  39  39  LEU LEU G . n 
D 4 40  TYR 40  40  40  TYR TYR G . n 
D 4 41  LYS 41  41  41  LYS LYS G . n 
D 4 42  GLU 42  42  42  GLU GLU G . n 
D 4 43  ASP 43  43  43  ASP ASP G . n 
D 4 44  ARG 44  44  44  ARG ARG G . n 
D 4 45  ILE 45  45  45  ILE ILE G . n 
D 4 46  HIS 46  46  46  HIS HIS G . n 
D 4 47  VAL 47  47  47  VAL VAL G . n 
D 4 48  PRO 48  48  48  PRO PRO G . n 
D 4 49  ILE 49  49  49  ILE ILE G . n 
D 4 50  PHE 50  50  50  PHE PHE G . n 
D 4 51  HIS 51  51  51  HIS HIS G . n 
D 4 52  GLY 52  52  52  GLY GLY G . n 
D 4 53  ARG 53  53  53  ARG ARG G . n 
D 4 54  LEU 54  54  54  LEU LEU G . n 
D 4 55  PHE 55  55  55  PHE PHE G . n 
D 4 56  GLN 56  56  56  GLN GLN G . n 
D 4 57  GLU 57  57  57  GLU GLU G . n 
D 4 58  SER 58  58  58  SER SER G . n 
D 4 59  PHE 59  59  59  PHE PHE G . n 
D 4 60  ASN 60  60  60  ASN ASN G . n 
D 4 61  MET 61  61  61  MET MET G . n 
D 4 62  SER 62  62  62  SER SER G . n 
D 4 63  PRO 63  63  63  PRO PRO G . n 
D 4 64  VAL 64  64  64  VAL VAL G . n 
D 4 65  THR 65  65  65  THR THR G . n 
D 4 66  THR 66  66  66  THR THR G . n 
D 4 67  ALA 67  67  67  ALA ALA G . n 
D 4 68  HIS 68  68  68  HIS HIS G . n 
D 4 69  ALA 69  69  69  ALA ALA G . n 
D 4 70  GLY 70  70  70  GLY GLY G . n 
D 4 71  ASN 71  71  71  ASN ASN G . n 
D 4 72  TYR 72  72  72  TYR TYR G . n 
D 4 73  THR 73  73  73  THR THR G . n 
D 4 74  CYS 74  74  74  CYS CYS G . n 
D 4 75  ARG 75  75  75  ARG ARG G . n 
D 4 76  GLY 76  76  76  GLY GLY G . n 
D 4 77  SER 77  77  77  SER SER G . n 
D 4 78  HIS 78  78  78  HIS HIS G . n 
D 4 79  PRO 79  79  79  PRO PRO G . n 
D 4 80  HIS 80  80  80  HIS HIS G . n 
D 4 81  SER 81  81  81  SER SER G . n 
D 4 82  PRO 82  82  82  PRO PRO G . n 
D 4 83  THR 83  83  83  THR THR G . n 
D 4 84  GLY 84  84  84  GLY GLY G . n 
D 4 85  TRP 85  85  85  TRP TRP G . n 
D 4 86  SER 86  86  86  SER SER G . n 
D 4 87  ALA 87  87  87  ALA ALA G . n 
D 4 88  ALA 88  88  88  ALA ALA G . n 
D 4 89  SER 89  89  89  SER SER G . n 
D 4 90  ASN 90  90  90  ASN ASN G . n 
D 4 91  PRO 91  91  91  PRO PRO G . n 
D 4 92  VAL 92  92  92  VAL VAL G . n 
D 4 93  VAL 93  93  93  VAL VAL G . n 
D 4 94  ILE 94  94  94  ILE ILE G . n 
D 4 95  MET 95  95  95  MET MET G . n 
D 4 96  VAL 96  96  96  VAL VAL G . n 
D 4 97  THR 97  97  97  THR THR G . n 
D 4 98  GLY 98  98  98  GLY GLY G . n 
D 4 99  ASN 99  99  99  ASN ASN G . n 
D 4 100 HIS 100 100 100 HIS HIS G . n 
D 4 101 ARG 101 101 101 ARG ARG G . n 
D 4 102 LYS 102 102 102 LYS LYS G . n 
D 4 103 PRO 103 103 103 PRO PRO G . n 
D 4 104 SER 104 104 104 SER SER G . n 
D 4 105 LEU 105 105 105 LEU LEU G . n 
D 4 106 LEU 106 106 106 LEU LEU G . n 
D 4 107 ALA 107 107 107 ALA ALA G . n 
D 4 108 HIS 108 108 108 HIS HIS G . n 
D 4 109 PRO 109 109 109 PRO PRO G . n 
D 4 110 GLY 110 110 110 GLY GLY G . n 
D 4 111 PRO 111 111 111 PRO PRO G . n 
D 4 112 LEU 112 112 112 LEU LEU G . n 
D 4 113 VAL 113 113 113 VAL VAL G . n 
D 4 114 LYS 114 114 114 LYS LYS G . n 
D 4 115 SER 115 115 115 SER SER G . n 
D 4 116 GLY 116 116 116 GLY GLY G . n 
D 4 117 GLU 117 117 117 GLU GLU G . n 
D 4 118 ARG 118 118 118 ARG ARG G . n 
D 4 119 VAL 119 119 119 VAL VAL G . n 
D 4 120 ILE 120 120 120 ILE ILE G . n 
D 4 121 LEU 121 121 121 LEU LEU G . n 
D 4 122 GLN 122 122 122 GLN GLN G . n 
D 4 123 CYS 123 123 123 CYS CYS G . n 
D 4 124 TRP 124 124 124 TRP TRP G . n 
D 4 125 SER 125 125 125 SER SER G . n 
D 4 126 ASP 126 126 126 ASP ASP G . n 
D 4 127 ILE 127 127 127 ILE ILE G . n 
D 4 128 MET 128 128 128 MET MET G . n 
D 4 129 PHE 129 129 129 PHE PHE G . n 
D 4 130 GLU 130 130 130 GLU GLU G . n 
D 4 131 HIS 131 131 131 HIS HIS G . n 
D 4 132 PHE 132 132 132 PHE PHE G . n 
D 4 133 PHE 133 133 133 PHE PHE G . n 
D 4 134 LEU 134 134 134 LEU LEU G . n 
D 4 135 HIS 135 135 135 HIS HIS G . n 
D 4 136 LYS 136 136 136 LYS LYS G . n 
D 4 137 GLU 137 137 137 GLU GLU G . n 
D 4 138 GLY 138 138 138 GLY GLY G . n 
D 4 139 ILE 139 139 139 ILE ILE G . n 
D 4 140 SER 140 140 140 SER SER G . n 
D 4 141 LYS 141 141 141 LYS LYS G . n 
D 4 142 ASP 142 142 142 ASP ASP G . n 
D 4 143 PRO 143 143 143 PRO PRO G . n 
D 4 144 SER 144 144 144 SER SER G . n 
D 4 145 ARG 145 145 145 ARG ARG G . n 
D 4 146 LEU 146 146 146 LEU LEU G . n 
D 4 147 VAL 147 147 147 VAL VAL G . n 
D 4 148 GLY 148 148 148 GLY GLY G . n 
D 4 149 GLN 149 149 149 GLN GLN G . n 
D 4 150 ILE 150 150 150 ILE ILE G . n 
D 4 151 HIS 151 151 151 HIS HIS G . n 
D 4 152 ASP 152 152 152 ASP ASP G . n 
D 4 153 GLY 153 153 153 GLY GLY G . n 
D 4 154 VAL 154 154 154 VAL VAL G . n 
D 4 155 SER 155 155 155 SER SER G . n 
D 4 156 LYS 156 156 156 LYS LYS G . n 
D 4 157 ALA 157 157 157 ALA ALA G . n 
D 4 158 ASN 158 158 158 ASN ASN G . n 
D 4 159 PHE 159 159 159 PHE PHE G . n 
D 4 160 SER 160 160 160 SER SER G . n 
D 4 161 ILE 161 161 161 ILE ILE G . n 
D 4 162 GLY 162 162 162 GLY GLY G . n 
D 4 163 PRO 163 163 163 PRO PRO G . n 
D 4 164 MET 164 164 164 MET MET G . n 
D 4 165 MET 165 165 165 MET MET G . n 
D 4 166 PHE 166 166 166 PHE PHE G . n 
D 4 167 ALA 167 167 167 ALA ALA G . n 
D 4 168 LEU 168 168 168 LEU LEU G . n 
D 4 169 ALA 169 169 169 ALA ALA G . n 
D 4 170 GLY 170 170 170 GLY GLY G . n 
D 4 171 THR 171 171 171 THR THR G . n 
D 4 172 TYR 172 172 172 TYR TYR G . n 
D 4 173 ARG 173 173 173 ARG ARG G . n 
D 4 174 CYS 174 174 174 CYS CYS G . n 
D 4 175 TYR 175 175 175 TYR TYR G . n 
D 4 176 GLY 176 176 176 GLY GLY G . n 
D 4 177 SER 177 177 177 SER SER G . n 
D 4 178 VAL 178 178 178 VAL VAL G . n 
D 4 179 THR 179 179 179 THR THR G . n 
D 4 180 HIS 180 180 180 HIS HIS G . n 
D 4 181 THR 181 181 181 THR THR G . n 
D 4 182 PRO 182 182 182 PRO PRO G . n 
D 4 183 TYR 183 183 183 TYR TYR G . n 
D 4 184 GLN 184 184 184 GLN GLN G . n 
D 4 185 LEU 185 185 185 LEU LEU G . n 
D 4 186 SER 186 186 186 SER SER G . n 
D 4 187 ALA 187 187 187 ALA ALA G . n 
D 4 188 PRO 188 188 188 PRO PRO G . n 
D 4 189 SER 189 189 189 SER SER G . n 
D 4 190 ASP 190 190 190 ASP ASP G . n 
D 4 191 PRO 191 191 191 PRO PRO G . n 
D 4 192 LEU 192 192 192 LEU LEU G . n 
D 4 193 ASP 193 193 193 ASP ASP G . n 
D 4 194 ILE 194 194 194 ILE ILE G . n 
D 4 195 VAL 195 195 195 VAL VAL G . n 
D 4 196 VAL 196 196 196 VAL VAL G . n 
D 4 197 THR 197 197 197 THR THR G . n 
D 4 198 GLY 198 198 198 GLY GLY G . n 
D 4 199 PRO 199 199 199 PRO PRO G . n 
D 4 200 TYR 200 200 200 TYR TYR G . n 
D 4 201 GLU 201 201 201 GLU GLU G . n 
D 4 202 LYS 202 202 202 LYS LYS G . n 
D 4 203 PRO 203 203 203 PRO PRO G . n 
D 4 204 SER 204 204 204 SER SER G . n 
D 4 205 LEU 205 205 205 LEU LEU G . n 
D 4 206 SER 206 206 206 SER SER G . n 
D 4 207 ALA 207 207 207 ALA ALA G . n 
D 4 208 GLN 208 208 208 GLN GLN G . n 
D 4 209 PRO 209 209 209 PRO PRO G . n 
D 4 210 GLY 210 210 210 GLY GLY G . n 
D 4 211 PRO 211 211 211 PRO PRO G . n 
D 4 212 LYS 212 212 212 LYS LYS G . n 
D 4 213 VAL 213 213 213 VAL VAL G . n 
D 4 214 GLN 214 214 214 GLN GLN G . n 
D 4 215 ALA 215 215 215 ALA ALA G . n 
D 4 216 GLY 216 216 216 GLY GLY G . n 
D 4 217 GLU 217 217 217 GLU GLU G . n 
D 4 218 SER 218 218 218 SER SER G . n 
D 4 219 VAL 219 219 219 VAL VAL G . n 
D 4 220 THR 220 220 220 THR THR G . n 
D 4 221 LEU 221 221 221 LEU LEU G . n 
D 4 222 SER 222 222 222 SER SER G . n 
D 4 223 CYS 223 223 223 CYS CYS G . n 
D 4 224 SER 224 224 224 SER SER G . n 
D 4 225 SER 225 225 225 SER SER G . n 
D 4 226 ARG 226 226 226 ARG ARG G . n 
D 4 227 SER 227 227 227 SER SER G . n 
D 4 228 SER 228 228 228 SER SER G . n 
D 4 229 TYR 229 229 229 TYR TYR G . n 
D 4 230 ASP 230 230 230 ASP ASP G . n 
D 4 231 MET 231 231 231 MET MET G . n 
D 4 232 TYR 232 232 232 TYR TYR G . n 
D 4 233 HIS 233 233 233 HIS HIS G . n 
D 4 234 LEU 234 234 234 LEU LEU G . n 
D 4 235 SER 235 235 235 SER SER G . n 
D 4 236 ARG 236 236 236 ARG ARG G . n 
D 4 237 GLU 237 237 237 GLU GLU G . n 
D 4 238 GLY 238 238 238 GLY GLY G . n 
D 4 239 GLY 239 239 239 GLY GLY G . n 
D 4 240 ALA 240 240 ?   ?   ?   G . n 
D 4 241 HIS 241 241 241 HIS HIS G . n 
D 4 242 GLU 242 242 242 GLU GLU G . n 
D 4 243 ARG 243 243 243 ARG ARG G . n 
D 4 244 ARG 244 244 244 ARG ARG G . n 
D 4 245 LEU 245 245 245 LEU LEU G . n 
D 4 246 PRO 246 246 246 PRO PRO G . n 
D 4 247 ALA 247 247 247 ALA ALA G . n 
D 4 248 VAL 248 248 248 VAL VAL G . n 
D 4 249 ARG 249 249 249 ARG ARG G . n 
D 4 250 LYS 250 250 250 LYS LYS G . n 
D 4 251 VAL 251 251 251 VAL VAL G . n 
D 4 252 ASN 252 252 252 ASN ASN G . n 
D 4 253 ARG 253 253 253 ARG ARG G . n 
D 4 254 THR 254 254 254 THR THR G . n 
D 4 255 PHE 255 255 255 PHE PHE G . n 
D 4 256 GLN 256 256 256 GLN GLN G . n 
D 4 257 ALA 257 257 257 ALA ALA G . n 
D 4 258 ASP 258 258 258 ASP ASP G . n 
D 4 259 PHE 259 259 259 PHE PHE G . n 
D 4 260 PRO 260 260 260 PRO PRO G . n 
D 4 261 LEU 261 261 261 LEU LEU G . n 
D 4 262 GLY 262 262 262 GLY GLY G . n 
D 4 263 PRO 263 263 263 PRO PRO G . n 
D 4 264 ALA 264 264 264 ALA ALA G . n 
D 4 265 THR 265 265 265 THR THR G . n 
D 4 266 HIS 266 266 266 HIS HIS G . n 
D 4 267 GLY 267 267 267 GLY GLY G . n 
D 4 268 GLY 268 268 268 GLY GLY G . n 
D 4 269 THR 269 269 269 THR THR G . n 
D 4 270 TYR 270 270 270 TYR TYR G . n 
D 4 271 ARG 271 271 271 ARG ARG G . n 
D 4 272 CYS 272 272 272 CYS CYS G . n 
D 4 273 PHE 273 273 273 PHE PHE G . n 
D 4 274 GLY 274 274 274 GLY GLY G . n 
D 4 275 SER 275 275 275 SER SER G . n 
D 4 276 PHE 276 276 276 PHE PHE G . n 
D 4 277 ARG 277 277 277 ARG ARG G . n 
D 4 278 HIS 278 278 278 HIS HIS G . n 
D 4 279 SER 279 279 279 SER SER G . n 
D 4 280 PRO 280 280 280 PRO PRO G . n 
D 4 281 TYR 281 281 281 TYR TYR G . n 
D 4 282 GLU 282 282 282 GLU GLU G . n 
D 4 283 TRP 283 283 283 TRP TRP G . n 
D 4 284 SER 284 284 284 SER SER G . n 
D 4 285 ASP 285 285 285 ASP ASP G . n 
D 4 286 PRO 286 286 286 PRO PRO G . n 
D 4 287 SER 287 287 287 SER SER G . n 
D 4 288 ASP 288 288 288 ASP ASP G . n 
D 4 289 PRO 289 289 289 PRO PRO G . n 
D 4 290 LEU 290 290 290 LEU LEU G . n 
D 4 291 LEU 291 291 291 LEU LEU G . n 
D 4 292 VAL 292 292 292 VAL VAL G . n 
D 4 293 SER 293 293 293 SER SER G . n 
D 4 294 VAL 294 294 294 VAL VAL G . n 
D 4 295 THR 295 295 295 THR THR G . n 
D 4 296 GLY 296 296 ?   ?   ?   G . n 
D 4 297 ASN 297 297 ?   ?   ?   G . n 
D 4 298 PRO 298 298 ?   ?   ?   G . n 
D 4 299 SER 299 299 ?   ?   ?   G . n 
D 4 300 HIS 300 300 ?   ?   ?   G . n 
D 4 301 HIS 301 301 ?   ?   ?   G . n 
D 4 302 HIS 302 302 ?   ?   ?   G . n 
D 4 303 HIS 303 303 ?   ?   ?   G . n 
D 4 304 HIS 304 304 ?   ?   ?   G . n 
D 4 305 HIS 305 305 ?   ?   ?   G . 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 
E 5 NAG 1   401 401 NAG NAG G . 
F 5 NAG 1   402 402 NAG NAG G . 
G 5 NAG 1   403 403 NAG NAG G . 
H 5 NAG 1   404 404 NAG NAG G . 
I 6 HOH 1   301 301 HOH HOH A . 
I 6 HOH 2   302 302 HOH HOH A . 
I 6 HOH 3   303 303 HOH HOH A . 
I 6 HOH 4   304 304 HOH HOH A . 
I 6 HOH 5   305 305 HOH HOH A . 
I 6 HOH 6   306 306 HOH HOH A . 
I 6 HOH 7   307 307 HOH HOH A . 
I 6 HOH 8   308 308 HOH HOH A . 
I 6 HOH 9   309 309 HOH HOH A . 
I 6 HOH 10  310 310 HOH HOH A . 
I 6 HOH 11  311 311 HOH HOH A . 
I 6 HOH 12  312 312 HOH HOH A . 
I 6 HOH 13  313 313 HOH HOH A . 
I 6 HOH 14  314 314 HOH HOH A . 
I 6 HOH 15  315 315 HOH HOH A . 
I 6 HOH 16  316 316 HOH HOH A . 
I 6 HOH 17  317 317 HOH HOH A . 
I 6 HOH 18  318 318 HOH HOH A . 
I 6 HOH 19  319 319 HOH HOH A . 
I 6 HOH 20  320 320 HOH HOH A . 
I 6 HOH 21  321 321 HOH HOH A . 
I 6 HOH 22  322 322 HOH HOH A . 
I 6 HOH 23  323 323 HOH HOH A . 
I 6 HOH 24  324 324 HOH HOH A . 
I 6 HOH 25  325 325 HOH HOH A . 
I 6 HOH 26  326 326 HOH HOH A . 
I 6 HOH 27  327 327 HOH HOH A . 
I 6 HOH 28  328 328 HOH HOH A . 
I 6 HOH 29  329 329 HOH HOH A . 
I 6 HOH 30  330 330 HOH HOH A . 
I 6 HOH 31  331 331 HOH HOH A . 
I 6 HOH 32  332 332 HOH HOH A . 
I 6 HOH 33  333 333 HOH HOH A . 
I 6 HOH 34  334 334 HOH HOH A . 
I 6 HOH 35  335 335 HOH HOH A . 
I 6 HOH 36  336 336 HOH HOH A . 
I 6 HOH 37  337 337 HOH HOH A . 
I 6 HOH 38  338 338 HOH HOH A . 
I 6 HOH 39  339 339 HOH HOH A . 
I 6 HOH 40  340 340 HOH HOH A . 
I 6 HOH 41  341 341 HOH HOH A . 
I 6 HOH 42  342 342 HOH HOH A . 
I 6 HOH 43  343 343 HOH HOH A . 
I 6 HOH 44  344 344 HOH HOH A . 
I 6 HOH 45  345 345 HOH HOH A . 
I 6 HOH 46  346 346 HOH HOH A . 
I 6 HOH 47  347 347 HOH HOH A . 
I 6 HOH 48  348 348 HOH HOH A . 
I 6 HOH 49  349 349 HOH HOH A . 
I 6 HOH 50  350 350 HOH HOH A . 
I 6 HOH 51  351 351 HOH HOH A . 
I 6 HOH 52  352 352 HOH HOH A . 
I 6 HOH 53  353 353 HOH HOH A . 
I 6 HOH 54  354 354 HOH HOH A . 
I 6 HOH 55  355 355 HOH HOH A . 
I 6 HOH 56  356 356 HOH HOH A . 
I 6 HOH 57  357 357 HOH HOH A . 
I 6 HOH 58  358 358 HOH HOH A . 
I 6 HOH 59  359 359 HOH HOH A . 
I 6 HOH 60  360 360 HOH HOH A . 
I 6 HOH 61  361 361 HOH HOH A . 
I 6 HOH 62  362 362 HOH HOH A . 
I 6 HOH 63  363 363 HOH HOH A . 
I 6 HOH 64  364 364 HOH HOH A . 
I 6 HOH 65  365 365 HOH HOH A . 
I 6 HOH 66  366 366 HOH HOH A . 
I 6 HOH 67  367 367 HOH HOH A . 
I 6 HOH 68  368 368 HOH HOH A . 
I 6 HOH 69  369 369 HOH HOH A . 
I 6 HOH 70  370 370 HOH HOH A . 
I 6 HOH 71  371 371 HOH HOH A . 
I 6 HOH 72  372 372 HOH HOH A . 
I 6 HOH 73  373 373 HOH HOH A . 
I 6 HOH 74  374 374 HOH HOH A . 
I 6 HOH 75  375 375 HOH HOH A . 
I 6 HOH 76  376 376 HOH HOH A . 
I 6 HOH 77  377 377 HOH HOH A . 
I 6 HOH 78  378 378 HOH HOH A . 
I 6 HOH 79  379 379 HOH HOH A . 
I 6 HOH 80  380 380 HOH HOH A . 
I 6 HOH 81  381 381 HOH HOH A . 
I 6 HOH 82  382 382 HOH HOH A . 
I 6 HOH 83  383 383 HOH HOH A . 
I 6 HOH 84  384 384 HOH HOH A . 
I 6 HOH 85  385 385 HOH HOH A . 
I 6 HOH 86  386 386 HOH HOH A . 
I 6 HOH 87  387 387 HOH HOH A . 
I 6 HOH 88  388 388 HOH HOH A . 
I 6 HOH 89  389 389 HOH HOH A . 
I 6 HOH 90  390 390 HOH HOH A . 
I 6 HOH 91  391 391 HOH HOH A . 
I 6 HOH 92  392 392 HOH HOH A . 
I 6 HOH 93  393 393 HOH HOH A . 
I 6 HOH 94  394 394 HOH HOH A . 
I 6 HOH 95  395 395 HOH HOH A . 
I 6 HOH 96  396 396 HOH HOH A . 
I 6 HOH 97  397 397 HOH HOH A . 
I 6 HOH 98  398 398 HOH HOH A . 
I 6 HOH 99  399 399 HOH HOH A . 
I 6 HOH 100 400 400 HOH HOH A . 
I 6 HOH 101 401 401 HOH HOH A . 
I 6 HOH 102 402 402 HOH HOH A . 
I 6 HOH 103 403 403 HOH HOH A . 
I 6 HOH 104 404 404 HOH HOH A . 
I 6 HOH 105 405 405 HOH HOH A . 
I 6 HOH 106 406 406 HOH HOH A . 
I 6 HOH 107 407 407 HOH HOH A . 
I 6 HOH 108 408 408 HOH HOH A . 
I 6 HOH 109 409 409 HOH HOH A . 
I 6 HOH 110 410 410 HOH HOH A . 
I 6 HOH 111 411 411 HOH HOH A . 
I 6 HOH 112 412 412 HOH HOH A . 
I 6 HOH 113 413 413 HOH HOH A . 
I 6 HOH 114 414 414 HOH HOH A . 
I 6 HOH 115 415 415 HOH HOH A . 
I 6 HOH 116 416 416 HOH HOH A . 
I 6 HOH 117 417 417 HOH HOH A . 
I 6 HOH 118 418 418 HOH HOH A . 
I 6 HOH 119 419 419 HOH HOH A . 
I 6 HOH 120 420 420 HOH HOH A . 
I 6 HOH 121 421 421 HOH HOH A . 
I 6 HOH 122 422 422 HOH HOH A . 
I 6 HOH 123 423 423 HOH HOH A . 
I 6 HOH 124 424 424 HOH HOH A . 
I 6 HOH 125 425 425 HOH HOH A . 
I 6 HOH 126 426 426 HOH HOH A . 
I 6 HOH 127 427 427 HOH HOH A . 
I 6 HOH 128 428 428 HOH HOH A . 
I 6 HOH 129 429 429 HOH HOH A . 
I 6 HOH 130 430 430 HOH HOH A . 
I 6 HOH 131 431 431 HOH HOH A . 
I 6 HOH 132 432 432 HOH HOH A . 
I 6 HOH 133 433 433 HOH HOH A . 
I 6 HOH 134 434 434 HOH HOH A . 
I 6 HOH 135 435 435 HOH HOH A . 
I 6 HOH 136 436 436 HOH HOH A . 
I 6 HOH 137 437 437 HOH HOH A . 
I 6 HOH 138 438 438 HOH HOH A . 
I 6 HOH 139 439 439 HOH HOH A . 
I 6 HOH 140 440 440 HOH HOH A . 
I 6 HOH 141 441 441 HOH HOH A . 
I 6 HOH 142 442 442 HOH HOH A . 
I 6 HOH 143 443 443 HOH HOH A . 
I 6 HOH 144 444 444 HOH HOH A . 
I 6 HOH 145 445 445 HOH HOH A . 
I 6 HOH 146 446 446 HOH HOH A . 
I 6 HOH 147 447 447 HOH HOH A . 
I 6 HOH 148 448 448 HOH HOH A . 
I 6 HOH 149 449 449 HOH HOH A . 
I 6 HOH 150 450 450 HOH HOH A . 
I 6 HOH 151 451 451 HOH HOH A . 
I 6 HOH 152 452 452 HOH HOH A . 
I 6 HOH 153 453 453 HOH HOH A . 
I 6 HOH 154 454 454 HOH HOH A . 
I 6 HOH 155 455 455 HOH HOH A . 
I 6 HOH 156 456 456 HOH HOH A . 
I 6 HOH 157 457 457 HOH HOH A . 
I 6 HOH 158 458 458 HOH HOH A . 
I 6 HOH 159 459 459 HOH HOH A . 
I 6 HOH 160 460 460 HOH HOH A . 
I 6 HOH 161 461 461 HOH HOH A . 
I 6 HOH 162 462 462 HOH HOH A . 
I 6 HOH 163 463 463 HOH HOH A . 
I 6 HOH 164 464 464 HOH HOH A . 
I 6 HOH 165 465 465 HOH HOH A . 
I 6 HOH 166 466 466 HOH HOH A . 
I 6 HOH 167 467 467 HOH HOH A . 
I 6 HOH 168 468 468 HOH HOH A . 
I 6 HOH 169 469 469 HOH HOH A . 
I 6 HOH 170 470 470 HOH HOH A . 
I 6 HOH 171 471 471 HOH HOH A . 
I 6 HOH 172 472 472 HOH HOH A . 
I 6 HOH 173 473 473 HOH HOH A . 
I 6 HOH 174 474 474 HOH HOH A . 
I 6 HOH 175 475 475 HOH HOH A . 
I 6 HOH 176 476 476 HOH HOH A . 
I 6 HOH 177 477 477 HOH HOH A . 
I 6 HOH 178 478 478 HOH HOH A . 
I 6 HOH 179 479 479 HOH HOH A . 
I 6 HOH 180 480 480 HOH HOH A . 
I 6 HOH 181 481 481 HOH HOH A . 
I 6 HOH 182 482 482 HOH HOH A . 
I 6 HOH 183 483 483 HOH HOH A . 
I 6 HOH 184 484 484 HOH HOH A . 
J 6 HOH 1   101 101 HOH HOH B . 
J 6 HOH 2   102 102 HOH HOH B . 
J 6 HOH 3   103 103 HOH HOH B . 
J 6 HOH 4   104 104 HOH HOH B . 
J 6 HOH 5   105 105 HOH HOH B . 
J 6 HOH 6   106 106 HOH HOH B . 
J 6 HOH 7   107 107 HOH HOH B . 
J 6 HOH 8   108 108 HOH HOH B . 
J 6 HOH 9   109 109 HOH HOH B . 
J 6 HOH 10  110 110 HOH HOH B . 
J 6 HOH 11  111 111 HOH HOH B . 
J 6 HOH 12  112 112 HOH HOH B . 
J 6 HOH 13  113 113 HOH HOH B . 
J 6 HOH 14  114 114 HOH HOH B . 
J 6 HOH 15  115 115 HOH HOH B . 
J 6 HOH 16  116 116 HOH HOH B . 
J 6 HOH 17  117 117 HOH HOH B . 
J 6 HOH 18  118 118 HOH HOH B . 
J 6 HOH 19  119 119 HOH HOH B . 
J 6 HOH 20  120 120 HOH HOH B . 
J 6 HOH 21  121 121 HOH HOH B . 
J 6 HOH 22  122 122 HOH HOH B . 
J 6 HOH 23  123 123 HOH HOH B . 
J 6 HOH 24  124 124 HOH HOH B . 
J 6 HOH 25  125 125 HOH HOH B . 
J 6 HOH 26  126 126 HOH HOH B . 
J 6 HOH 27  127 127 HOH HOH B . 
J 6 HOH 28  128 128 HOH HOH B . 
J 6 HOH 29  129 129 HOH HOH B . 
J 6 HOH 30  130 130 HOH HOH B . 
J 6 HOH 31  131 131 HOH HOH B . 
J 6 HOH 32  132 132 HOH HOH B . 
J 6 HOH 33  133 133 HOH HOH B . 
J 6 HOH 34  134 134 HOH HOH B . 
J 6 HOH 35  135 135 HOH HOH B . 
J 6 HOH 36  136 136 HOH HOH B . 
J 6 HOH 37  137 137 HOH HOH B . 
J 6 HOH 38  138 138 HOH HOH B . 
J 6 HOH 39  139 139 HOH HOH B . 
J 6 HOH 40  140 140 HOH HOH B . 
J 6 HOH 41  141 141 HOH HOH B . 
J 6 HOH 42  142 142 HOH HOH B . 
J 6 HOH 43  143 143 HOH HOH B . 
J 6 HOH 44  144 144 HOH HOH B . 
J 6 HOH 45  145 145 HOH HOH B . 
J 6 HOH 46  146 146 HOH HOH B . 
J 6 HOH 47  147 147 HOH HOH B . 
J 6 HOH 48  148 148 HOH HOH B . 
K 6 HOH 1   101 101 HOH HOH C . 
K 6 HOH 2   102 102 HOH HOH C . 
K 6 HOH 3   103 103 HOH HOH C . 
K 6 HOH 4   104 104 HOH HOH C . 
K 6 HOH 5   105 105 HOH HOH C . 
K 6 HOH 6   106 106 HOH HOH C . 
K 6 HOH 7   107 107 HOH HOH C . 
K 6 HOH 8   108 108 HOH HOH C . 
K 6 HOH 9   109 109 HOH HOH C . 
L 6 HOH 1   501 501 HOH HOH G . 
L 6 HOH 2   502 502 HOH HOH G . 
L 6 HOH 3   503 503 HOH HOH G . 
L 6 HOH 4   504 504 HOH HOH G . 
L 6 HOH 5   505 505 HOH HOH G . 
L 6 HOH 6   506 506 HOH HOH G . 
L 6 HOH 7   507 507 HOH HOH G . 
L 6 HOH 8   508 508 HOH HOH G . 
L 6 HOH 9   509 509 HOH HOH G . 
L 6 HOH 10  510 510 HOH HOH G . 
L 6 HOH 11  511 511 HOH HOH G . 
L 6 HOH 12  512 512 HOH HOH G . 
L 6 HOH 13  513 513 HOH HOH G . 
L 6 HOH 14  514 514 HOH HOH G . 
L 6 HOH 15  515 515 HOH HOH G . 
L 6 HOH 16  516 516 HOH HOH G . 
L 6 HOH 17  517 517 HOH HOH G . 
L 6 HOH 18  518 518 HOH HOH G . 
L 6 HOH 19  519 519 HOH HOH G . 
L 6 HOH 20  520 520 HOH HOH G . 
L 6 HOH 21  521 521 HOH HOH G . 
L 6 HOH 22  522 522 HOH HOH G . 
L 6 HOH 23  523 523 HOH HOH G . 
L 6 HOH 24  524 524 HOH HOH G . 
L 6 HOH 25  525 525 HOH HOH G . 
L 6 HOH 26  526 526 HOH HOH G . 
L 6 HOH 27  527 527 HOH HOH G . 
L 6 HOH 28  528 528 HOH HOH G . 
L 6 HOH 29  529 529 HOH HOH G . 
L 6 HOH 30  530 530 HOH HOH G . 
L 6 HOH 31  531 531 HOH HOH G . 
L 6 HOH 32  532 532 HOH HOH G . 
L 6 HOH 33  533 533 HOH HOH G . 
L 6 HOH 34  534 534 HOH HOH G . 
L 6 HOH 35  535 535 HOH HOH G . 
L 6 HOH 36  536 536 HOH HOH G . 
L 6 HOH 37  537 537 HOH HOH G . 
L 6 HOH 38  538 538 HOH HOH G . 
L 6 HOH 39  539 539 HOH HOH G . 
L 6 HOH 40  540 540 HOH HOH G . 
L 6 HOH 41  541 541 HOH HOH G . 
L 6 HOH 42  542 542 HOH HOH G . 
L 6 HOH 43  543 543 HOH HOH G . 
L 6 HOH 44  544 544 HOH HOH G . 
L 6 HOH 45  545 545 HOH HOH G . 
L 6 HOH 46  546 546 HOH HOH G . 
L 6 HOH 47  547 547 HOH HOH G . 
L 6 HOH 48  548 548 HOH HOH G . 
L 6 HOH 49  549 549 HOH HOH G . 
L 6 HOH 50  550 550 HOH HOH G . 
L 6 HOH 51  551 551 HOH HOH G . 
L 6 HOH 52  552 552 HOH HOH G . 
L 6 HOH 53  553 553 HOH HOH G . 
L 6 HOH 54  554 554 HOH HOH G . 
L 6 HOH 55  555 555 HOH HOH G . 
L 6 HOH 56  556 556 HOH HOH G . 
L 6 HOH 57  557 557 HOH HOH G . 
L 6 HOH 58  558 558 HOH HOH G . 
L 6 HOH 59  559 559 HOH HOH G . 
L 6 HOH 60  560 560 HOH HOH G . 
L 6 HOH 61  561 561 HOH HOH G . 
L 6 HOH 62  562 562 HOH HOH G . 
L 6 HOH 63  563 563 HOH HOH G . 
L 6 HOH 64  564 564 HOH HOH G . 
L 6 HOH 65  565 565 HOH HOH G . 
L 6 HOH 66  566 566 HOH HOH G . 
L 6 HOH 67  567 567 HOH HOH G . 
L 6 HOH 68  568 568 HOH HOH G . 
L 6 HOH 69  569 569 HOH HOH G . 
L 6 HOH 70  570 570 HOH HOH G . 
L 6 HOH 71  571 571 HOH HOH G . 
L 6 HOH 72  572 572 HOH HOH G . 
L 6 HOH 73  573 573 HOH HOH G . 
L 6 HOH 74  574 574 HOH HOH G . 
L 6 HOH 75  575 575 HOH HOH G . 
L 6 HOH 76  576 576 HOH HOH G . 
L 6 HOH 77  577 577 HOH HOH G . 
L 6 HOH 78  578 578 HOH HOH G . 
L 6 HOH 79  579 579 HOH HOH G . 
L 6 HOH 80  580 580 HOH HOH G . 
L 6 HOH 81  581 581 HOH HOH G . 
L 6 HOH 82  582 582 HOH HOH G . 
L 6 HOH 83  583 583 HOH HOH G . 
L 6 HOH 84  584 584 HOH HOH G . 
L 6 HOH 85  585 585 HOH HOH G . 
L 6 HOH 86  586 586 HOH HOH G . 
L 6 HOH 87  587 587 HOH HOH G . 
L 6 HOH 88  588 588 HOH HOH G . 
L 6 HOH 89  589 589 HOH HOH G . 
L 6 HOH 90  590 590 HOH HOH G . 
L 6 HOH 91  591 591 HOH HOH G . 
L 6 HOH 92  592 592 HOH HOH G . 
L 6 HOH 93  593 593 HOH HOH G . 
L 6 HOH 94  594 594 HOH HOH G . 
L 6 HOH 95  595 595 HOH HOH G . 
L 6 HOH 96  596 596 HOH HOH G . 
L 6 HOH 97  597 597 HOH HOH G . 
L 6 HOH 98  598 598 HOH HOH G . 
L 6 HOH 99  599 599 HOH HOH G . 
L 6 HOH 100 600 600 HOH HOH G . 
L 6 HOH 101 601 601 HOH HOH G . 
L 6 HOH 102 602 602 HOH HOH G . 
L 6 HOH 103 603 603 HOH HOH G . 
L 6 HOH 104 604 604 HOH HOH G . 
L 6 HOH 105 605 605 HOH HOH G . 
L 6 HOH 106 606 606 HOH HOH G . 
L 6 HOH 107 607 607 HOH HOH G . 
L 6 HOH 108 608 608 HOH HOH G . 
L 6 HOH 109 609 609 HOH HOH G . 
L 6 HOH 110 610 610 HOH HOH G . 
L 6 HOH 111 611 611 HOH HOH G . 
L 6 HOH 112 612 612 HOH HOH G . 
L 6 HOH 113 613 613 HOH HOH G . 
L 6 HOH 114 614 614 HOH HOH G . 
L 6 HOH 115 615 615 HOH HOH G . 
L 6 HOH 116 616 616 HOH HOH G . 
L 6 HOH 117 617 617 HOH HOH G . 
L 6 HOH 118 618 618 HOH HOH G . 
L 6 HOH 119 619 619 HOH HOH G . 
L 6 HOH 120 620 620 HOH HOH G . 
L 6 HOH 121 621 621 HOH HOH G . 
L 6 HOH 122 622 622 HOH HOH G . 
L 6 HOH 123 623 623 HOH HOH G . 
L 6 HOH 124 624 624 HOH HOH G . 
L 6 HOH 125 625 625 HOH HOH G . 
L 6 HOH 126 626 626 HOH HOH G . 
L 6 HOH 127 627 627 HOH HOH G . 
L 6 HOH 128 628 628 HOH HOH G . 
L 6 HOH 129 629 629 HOH HOH G . 
L 6 HOH 130 630 630 HOH HOH G . 
L 6 HOH 131 631 631 HOH HOH G . 
L 6 HOH 132 632 632 HOH HOH G . 
L 6 HOH 133 633 633 HOH HOH G . 
L 6 HOH 134 634 634 HOH HOH G . 
L 6 HOH 135 635 635 HOH HOH G . 
L 6 HOH 136 636 636 HOH HOH G . 
L 6 HOH 137 637 637 HOH HOH G . 
L 6 HOH 138 638 638 HOH HOH G . 
L 6 HOH 139 639 639 HOH HOH G . 
L 6 HOH 140 640 640 HOH HOH G . 
L 6 HOH 141 641 641 HOH HOH G . 
L 6 HOH 142 642 642 HOH HOH G . 
L 6 HOH 143 643 643 HOH HOH G . 
L 6 HOH 144 644 644 HOH HOH G . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 79  ? CG  ? A ARG 79  CG  
2  1 Y 1 A ARG 79  ? CD  ? A ARG 79  CD  
3  1 Y 1 A ARG 79  ? NE  ? A ARG 79  NE  
4  1 Y 1 A ARG 79  ? CZ  ? A ARG 79  CZ  
5  1 Y 1 A ARG 79  ? NH1 ? A ARG 79  NH1 
6  1 Y 1 A ARG 79  ? NH2 ? A ARG 79  NH2 
7  1 Y 1 A ARG 83  ? CG  ? A ARG 83  CG  
8  1 Y 1 A ARG 83  ? CD  ? A ARG 83  CD  
9  1 Y 1 A ARG 83  ? NE  ? A ARG 83  NE  
10 1 Y 1 A ARG 83  ? CZ  ? A ARG 83  CZ  
11 1 Y 1 A ARG 83  ? NH1 ? A ARG 83  NH1 
12 1 Y 1 A ARG 83  ? NH2 ? A ARG 83  NH2 
13 1 Y 1 A GLU 89  ? CG  ? A GLU 89  CG  
14 1 Y 1 A GLU 89  ? CD  ? A GLU 89  CD  
15 1 Y 1 A GLU 89  ? OE1 ? A GLU 89  OE1 
16 1 Y 1 A GLU 89  ? OE2 ? A GLU 89  OE2 
17 1 Y 0 A ARG 151 ? CZ  ? A ARG 151 CZ  
18 1 Y 1 A LYS 186 ? CG  ? A LYS 186 CG  
19 1 Y 1 A LYS 186 ? CD  ? A LYS 186 CD  
20 1 Y 1 A LYS 186 ? CE  ? A LYS 186 CE  
21 1 Y 1 A LYS 186 ? NZ  ? A LYS 186 NZ  
22 1 Y 1 A GLU 222 ? CG  ? A GLU 222 CG  
23 1 Y 1 A GLU 222 ? CD  ? A GLU 222 CD  
24 1 Y 1 A GLU 222 ? OE1 ? A GLU 222 OE1 
25 1 Y 1 A GLU 222 ? OE2 ? A GLU 222 OE2 
26 1 Y 0 A SER 251 ? CA  B A SER 251 CA  
27 1 Y 0 A SER 251 ? CB  B A SER 251 CB  
28 1 Y 0 A SER 251 ? OG  B A SER 251 OG  
29 1 Y 1 B ILE 1   ? CG1 ? B ILE 2   CG1 
30 1 Y 1 B ILE 1   ? CG2 ? B ILE 2   CG2 
31 1 Y 1 B ILE 1   ? CD1 ? B ILE 2   CD1 
32 1 Y 1 B GLU 47  ? CG  ? B GLU 48  CG  
33 1 Y 1 B GLU 47  ? CD  ? B GLU 48  CD  
34 1 Y 1 B GLU 47  ? OE1 ? B GLU 48  OE1 
35 1 Y 1 B GLU 47  ? OE2 ? B GLU 48  OE2 
36 1 Y 1 B LYS 75  ? CG  ? B LYS 76  CG  
37 1 Y 1 B LYS 75  ? CD  ? B LYS 76  CD  
38 1 Y 1 B LYS 75  ? CE  ? B LYS 76  CE  
39 1 Y 1 B LYS 75  ? NZ  ? B LYS 76  NZ  
40 1 Y 1 B SER 88  ? OG  ? B SER 89  OG  
41 1 Y 1 B MET 99  ? CG  ? B MET 100 CG  
42 1 Y 1 B MET 99  ? SD  ? B MET 100 SD  
43 1 Y 1 B MET 99  ? CE  ? B MET 100 CE  
44 1 Y 1 G ARG 33  ? CG  ? D ARG 33  CG  
45 1 Y 1 G ARG 33  ? CD  ? D ARG 33  CD  
46 1 Y 1 G ARG 33  ? NE  ? D ARG 33  NE  
47 1 Y 1 G ARG 33  ? CZ  ? D ARG 33  CZ  
48 1 Y 1 G ARG 33  ? NH1 ? D ARG 33  NH1 
49 1 Y 1 G ARG 33  ? NH2 ? D ARG 33  NH2 
50 1 Y 1 G ASP 43  ? CG  ? D ASP 43  CG  
51 1 Y 1 G ASP 43  ? OD1 ? D ASP 43  OD1 
52 1 Y 1 G ASP 43  ? OD2 ? D ASP 43  OD2 
53 1 Y 1 G ARG 44  ? CG  ? D ARG 44  CG  
54 1 Y 1 G ARG 44  ? CD  ? D ARG 44  CD  
55 1 Y 1 G ARG 44  ? NE  ? D ARG 44  NE  
56 1 Y 1 G ARG 44  ? CZ  ? D ARG 44  CZ  
57 1 Y 1 G ARG 44  ? NH1 ? D ARG 44  NH1 
58 1 Y 1 G ARG 44  ? NH2 ? D ARG 44  NH2 
59 1 Y 1 G GLN 56  ? CG  ? D GLN 56  CG  
60 1 Y 1 G GLN 56  ? CD  ? D GLN 56  CD  
61 1 Y 1 G GLN 56  ? OE1 ? D GLN 56  OE1 
62 1 Y 1 G GLN 56  ? NE2 ? D GLN 56  NE2 
63 1 Y 1 G LYS 212 ? CG  ? D LYS 212 CG  
64 1 Y 1 G LYS 212 ? CD  ? D LYS 212 CD  
65 1 Y 1 G LYS 212 ? CE  ? D LYS 212 CE  
66 1 Y 1 G LYS 212 ? NZ  ? D LYS 212 NZ  
67 1 Y 1 G ARG 226 ? CG  ? D ARG 226 CG  
68 1 Y 1 G ARG 226 ? CD  ? D ARG 226 CD  
69 1 Y 1 G ARG 226 ? NE  ? D ARG 226 NE  
70 1 Y 1 G ARG 226 ? CZ  ? D ARG 226 CZ  
71 1 Y 1 G ARG 226 ? NH1 ? D ARG 226 NH1 
72 1 Y 1 G ARG 226 ? NH2 ? D ARG 226 NH2 
73 1 Y 1 G HIS 241 ? CG  ? D HIS 241 CG  
74 1 Y 1 G HIS 241 ? ND1 ? D HIS 241 ND1 
75 1 Y 1 G HIS 241 ? CD2 ? D HIS 241 CD2 
76 1 Y 1 G HIS 241 ? CE1 ? D HIS 241 CE1 
77 1 Y 1 G HIS 241 ? NE2 ? D HIS 241 NE2 
78 1 Y 1 G HIS 266 ? CG  ? D HIS 266 CG  
79 1 Y 1 G HIS 266 ? ND1 ? D HIS 266 ND1 
80 1 Y 1 G HIS 266 ? CD2 ? D HIS 266 CD2 
81 1 Y 1 G HIS 266 ? CE1 ? D HIS 266 CE1 
82 1 Y 1 G HIS 266 ? NE2 ? D HIS 266 NE2 
83 1 Y 1 G VAL 294 ? CG1 ? D VAL 294 CG1 
84 1 Y 1 G VAL 294 ? CG2 ? D VAL 294 CG2 
85 1 Y 1 G THR 295 ? OG1 ? D THR 295 OG1 
86 1 Y 1 G THR 295 ? CG2 ? D THR 295 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  95.564 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.163 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  109.016 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BL3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.769 
_cell.length_a_esd                 ? 
_cell.length_b                     60.784 
_cell.length_b_esd                 ? 
_cell.length_c                     65.042 
_cell.length_c_esd                 ? 
_cell.volume                       189283.256 
_cell.volume_esd                   ? 
_cell.Z_PDB                        1 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BL3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            'P 1' 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BL3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '16% PEG 3350, 2% tacsimate pH 5.0, 0.1 M tri-sodium citrate pH 5.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.953659 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.953659 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          37.40 
_reflns.entry_id                                       9BL3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               48.10 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     48382 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.054 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3548 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.850 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.463 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               49.05 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BL3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             48.10 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     48369 
_refine.ls_number_reflns_R_free                  2351 
_refine.ls_number_reflns_R_work                  46018 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.62 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1947 
_refine.ls_R_factor_R_free                       0.2289 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1930 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.9019 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2566 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        48.10 
_refine_hist.number_atoms_solvent             385 
_refine_hist.number_atoms_total               5775 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0073  ? 5592 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8957  ? 7625 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0548  ? 807  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0077  ? 997  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.1289 ? 2032 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.04  . . 124 2688 96.77 . . . . 0.3003 . . . . . . . . . . . 0.3282 
'X-RAY DIFFRACTION' 2.04 2.09  . . 143 2681 97.21 . . . . 0.2697 . . . . . . . . . . . 0.3106 
'X-RAY DIFFRACTION' 2.09 2.13  . . 137 2702 97.09 . . . . 0.2602 . . . . . . . . . . . 0.2982 
'X-RAY DIFFRACTION' 2.13 2.19  . . 164 2667 96.92 . . . . 0.2442 . . . . . . . . . . . 0.2771 
'X-RAY DIFFRACTION' 2.19 2.25  . . 131 2708 97.39 . . . . 0.2397 . . . . . . . . . . . 0.2959 
'X-RAY DIFFRACTION' 2.25 2.31  . . 138 2684 97.82 . . . . 0.2333 . . . . . . . . . . . 0.2670 
'X-RAY DIFFRACTION' 2.31 2.39  . . 130 2715 97.46 . . . . 0.2328 . . . . . . . . . . . 0.2491 
'X-RAY DIFFRACTION' 2.39 2.47  . . 145 2739 97.70 . . . . 0.2338 . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 2.47 2.57  . . 131 2706 97.63 . . . . 0.2401 . . . . . . . . . . . 0.2792 
'X-RAY DIFFRACTION' 2.57 2.69  . . 131 2689 97.85 . . . . 0.2355 . . . . . . . . . . . 0.3198 
'X-RAY DIFFRACTION' 2.69 2.83  . . 136 2727 97.38 . . . . 0.2337 . . . . . . . . . . . 0.2968 
'X-RAY DIFFRACTION' 2.83 3.01  . . 136 2721 98.14 . . . . 0.2292 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 3.01 3.24  . . 145 2737 98.19 . . . . 0.2127 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 3.24 3.57  . . 148 2674 97.85 . . . . 0.1859 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 3.57 4.08  . . 129 2765 98.20 . . . . 0.1594 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 4.08 5.14  . . 147 2684 97.52 . . . . 0.1368 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 5.14 48.10 . . 136 2731 98.49 . . . . 0.1627 . . . . . . . . . . . 0.1954 
# 
_struct.entry_id                     9BL3 
_struct.title                        'KIR3DL1*114 in complex with HLA-B*57:03 presenting the AW10 peptide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BL3 
_struct_keywords.text            'immunoglobulin fold, natural killer cell receptor, Kir, immune system' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP I3ZN84_HUMAN     I3ZN84     ? 1 
;GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYWDGETRNMKASAQTYRENLRI
ALRYYNQSEAGSHIIQVMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYL
EGLCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
;
25  
2 UNP B2MG_HUMAN       P61769     ? 2 
;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM
;
21  
3 UNP CTNA1_HUMAN      P35221     ? 3 ASLNLPAVSW 850 
4 UNP A0A5J6VN80_HUMAN A0A5J6VN80 ? 4 
;HMGGQDKPFLSAWPSAVVPRGGHVTLRCHYRHRFNNFMLYKEDRIHVPIFHGRLFQESFNMSPVTTAHAGNYTCRGSHPH
SPTGWSAASNPVVIMVTGNHRKPSLLAHPGPLVKSGERVILQCWSDIMFEHFFLHKEGISKDPSRLVGQIHDGVSKANFS
IGPMMFALAGTYRCYGSVTHTPYQLSAPSDPLDIVVTGPYEKPSLSAQPGPKVQAGESVTLSCSSRSSYDMYHLSREGGA
HERRLPAVRKVNRTFQADFPLGPATHGGTYRCFGSFRHSPYEWSDPSDPLLVSVTGNPS
;
22  
# 
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 9BL3 A 1 ? 276 ? I3ZN84     25  ? 300 ? 1 276 
2 2 9BL3 B 2 ? 100 ? P61769     21  ? 119 ? 1 99  
3 3 9BL3 C 1 ? 10  ? P35221     850 ? 859 ? 1 10  
4 4 9BL3 G 1 ? 299 ? A0A5J6VN80 22  ? 320 ? 1 299 
# 
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 
2 9BL3 MET B 1   ? UNP P61769     ? ? 'initiating methionine' 0   1 
4 9BL3 HIS G 300 ? UNP A0A5J6VN80 ? ? 'expression tag'        300 2 
4 9BL3 HIS G 301 ? UNP A0A5J6VN80 ? ? 'expression tag'        301 3 
4 9BL3 HIS G 302 ? UNP A0A5J6VN80 ? ? 'expression tag'        302 4 
4 9BL3 HIS G 303 ? UNP A0A5J6VN80 ? ? 'expression tag'        303 5 
4 9BL3 HIS G 304 ? UNP A0A5J6VN80 ? ? 'expression tag'        304 6 
4 9BL3 HIS G 305 ? UNP A0A5J6VN80 ? ? 'expression tag'        305 7 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 7520  ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  32350 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 49  ? GLU A 53  ? ALA A 49  GLU A 53  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 56  ? ASN A 86  ? GLY A 56  ASN A 86  1 ? 31 
HELX_P HELX_P3  AA3 ASP A 137 ? ALA A 150 ? ASP A 137 ALA A 150 1 ? 14 
HELX_P HELX_P4  AA4 ARG A 151 ? GLY A 162 ? ARG A 151 GLY A 162 1 ? 12 
HELX_P HELX_P5  AA5 GLY A 162 ? GLY A 175 ? GLY A 162 GLY A 175 1 ? 14 
HELX_P HELX_P6  AA6 GLY A 175 ? GLN A 180 ? GLY A 175 GLN A 180 1 ? 6  
HELX_P HELX_P7  AA7 GLU A 253 ? GLN A 255 ? GLU A 253 GLN A 255 5 ? 3  
HELX_P HELX_P8  AA8 PRO D 48  ? ARG D 53  ? PRO G 48  ARG G 53  1 ? 6  
HELX_P HELX_P9  AA9 THR D 65  ? ALA D 69  ? THR G 65  ALA G 69  5 ? 5  
HELX_P HELX_P10 AB1 MET D 165 ? ALA D 169 ? MET G 165 ALA G 169 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 101 SG  ? ? ? 1_555 A CYS 164 SG ? ? A CYS 101 A CYS 164 1_555 ? ? ? ? ? ? ? 2.085 ? ?               
disulf2 disulf ?   ? A CYS 203 SG  ? ? ? 1_555 A CYS 259 SG ? ? A CYS 203 A CYS 259 1_555 ? ? ? ? ? ? ? 2.016 ? ?               
disulf3 disulf ?   ? B CYS 26  SG  ? ? ? 1_555 B CYS 81  SG ? ? B CYS 25  B CYS 80  1_555 ? ? ? ? ? ? ? 2.011 ? ?               
disulf4 disulf ?   ? D CYS 28  SG  ? ? ? 1_555 D CYS 74  SG ? ? G CYS 28  G CYS 74  1_555 ? ? ? ? ? ? ? 2.056 ? ?               
disulf5 disulf ?   ? D CYS 123 SG  ? ? ? 1_555 D CYS 174 SG ? ? G CYS 123 G CYS 174 1_555 ? ? ? ? ? ? ? 2.055 ? ?               
disulf6 disulf ?   ? D CYS 223 SG  ? ? ? 1_555 D CYS 272 SG ? ? G CYS 223 G CYS 272 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
covale1 covale one ? D ASN 60  ND2 ? ? ? 1_555 G NAG .   C1 ? ? G ASN 60  G NAG 403 1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
covale2 covale one ? D ASN 71  ND2 ? ? ? 1_555 H NAG .   C1 ? ? G ASN 71  G NAG 404 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale3 covale one ? D ASN 158 ND2 ? ? ? 1_555 F NAG .   C1 ? ? G ASN 158 G NAG 402 1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
covale4 covale one ? D ASN 252 ND2 ? ? ? 1_555 E NAG .   C1 ? ? G ASN 252 G NAG 401 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG E .   ? ASN D 252 ? NAG G 401 ? 1_555 ASN G 252 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN D 158 ? NAG G 402 ? 1_555 ASN G 158 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG G .   ? ASN D 60  ? NAG G 403 ? 1_555 ASN G 60  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG H .   ? ASN D 71  ? NAG G 404 ? 1_555 ASN G 71  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  CYS A 101 ? CYS A 164 ? CYS A 101 ? 1_555 CYS A 164 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS A 203 ? CYS A 259 ? CYS A 203 ? 1_555 CYS A 259 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS B 26  ? CYS B 81  ? CYS B 25  ? 1_555 CYS B 80  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS D 28  ? CYS D 74  ? CYS G 28  ? 1_555 CYS G 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS D 123 ? CYS D 174 ? CYS G 123 ? 1_555 CYS G 174 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS D 223 ? CYS D 272 ? CYS G 223 ? 1_555 CYS G 272 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 209 A . ? TYR 209 A PRO 210 A ? PRO 210 A 1 -0.45 
2 HIS 32  B . ? HIS 31  B PRO 33  B ? PRO 32  B 1 4.23  
3 TRP 13  D . ? TRP 13  G PRO 14  D ? PRO 14  G 1 1.50  
4 SER 62  D . ? SER 62  G PRO 63  D ? PRO 63  G 1 -8.40 
5 HIS 108 D . ? HIS 108 G PRO 109 D ? PRO 109 G 1 3.04  
6 GLY 162 D . ? GLY 162 G PRO 163 D ? PRO 163 G 1 1.24  
7 GLY 198 D . ? GLY 198 G PRO 199 D ? PRO 199 G 1 9.80  
8 GLN 208 D . ? GLN 208 G PRO 209 D ? PRO 209 G 1 -0.01 
9 GLY 262 D . ? GLY 262 G PRO 263 D ? PRO 263 G 1 -4.60 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 3 ? 
AB4 ? 4 ? 
AB5 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 46  ? PRO A 47  ? ALA A 46  PRO A 47  
AA1 2 THR A 31  ? ASP A 37  ? THR A 31  ASP A 37  
AA1 3 ARG A 21  ? VAL A 28  ? ARG A 21  VAL A 28  
AA1 4 HIS A 3   ? MET A 12  ? HIS A 3   MET A 12  
AA1 5 ILE A 94  ? VAL A 103 ? ILE A 94  VAL A 103 
AA1 6 LEU A 109 ? TYR A 118 ? LEU A 109 TYR A 118 
AA1 7 LYS A 121 ? LEU A 126 ? LYS A 121 LEU A 126 
AA1 8 TRP A 133 ? ALA A 135 ? TRP A 133 ALA A 135 
AA2 1 LYS A 186 ? PRO A 193 ? LYS A 186 PRO A 193 
AA2 2 GLU A 198 ? PHE A 208 ? GLU A 198 PHE A 208 
AA2 3 PHE A 241 ? PRO A 250 ? PHE A 241 PRO A 250 
AA2 4 GLU A 229 ? LEU A 230 ? GLU A 229 LEU A 230 
AA3 1 LYS A 186 ? PRO A 193 ? LYS A 186 PRO A 193 
AA3 2 GLU A 198 ? PHE A 208 ? GLU A 198 PHE A 208 
AA3 3 PHE A 241 ? PRO A 250 ? PHE A 241 PRO A 250 
AA3 4 ARG A 234 ? PRO A 235 ? ARG A 234 PRO A 235 
AA4 1 GLU A 222 ? ASP A 223 ? GLU A 222 ASP A 223 
AA4 2 THR A 214 ? ARG A 219 ? THR A 214 ARG A 219 
AA4 3 TYR A 257 ? GLN A 262 ? TYR A 257 GLN A 262 
AA4 4 LEU A 270 ? LEU A 272 ? LEU A 270 LEU A 272 
AA5 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA5 2 ASN B 22  ? PHE B 31  ? ASN B 21  PHE B 30  
AA5 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA5 4 GLU B 51  ? HIS B 52  ? GLU B 50  HIS B 51  
AA6 1 LYS B 7   ? SER B 12  ? LYS B 6   SER B 11  
AA6 2 ASN B 22  ? PHE B 31  ? ASN B 21  PHE B 30  
AA6 3 PHE B 63  ? PHE B 71  ? PHE B 62  PHE B 70  
AA6 4 SER B 56  ? PHE B 57  ? SER B 55  PHE B 56  
AA7 1 GLU B 45  ? ARG B 46  ? GLU B 44  ARG B 45  
AA7 2 GLU B 37  ? LYS B 42  ? GLU B 36  LYS B 41  
AA7 3 TYR B 79  ? ASN B 84  ? TYR B 78  ASN B 83  
AA7 4 LYS B 92  ? LYS B 95  ? LYS B 91  LYS B 94  
AA8 1 PHE D 9   ? TRP D 13  ? PHE G 9   TRP G 13  
AA8 2 VAL D 24  ? HIS D 29  ? VAL G 24  HIS G 29  
AA8 3 PHE D 59  ? MET D 61  ? PHE G 59  MET G 61  
AA9 1 VAL D 17  ? PRO D 19  ? VAL G 17  PRO G 19  
AA9 2 VAL D 92  ? THR D 97  ? VAL G 92  THR G 97  
AA9 3 GLY D 70  ? GLY D 76  ? GLY G 70  GLY G 76  
AA9 4 PHE D 37  ? LYS D 41  ? PHE G 37  LYS G 41  
AB1 1 SER D 104 ? HIS D 108 ? SER G 104 HIS G 108 
AB1 2 VAL D 119 ? SER D 125 ? VAL G 119 SER G 125 
AB1 3 VAL D 154 ? ILE D 161 ? VAL G 154 ILE G 161 
AB1 4 GLN D 149 ? HIS D 151 ? GLN G 149 HIS G 151 
AB2 1 LEU D 112 ? LYS D 114 ? LEU G 112 LYS G 114 
AB2 2 LEU D 192 ? THR D 197 ? LEU G 192 THR G 197 
AB2 3 GLY D 170 ? SER D 177 ? GLY G 170 SER G 177 
AB2 4 HIS D 131 ? LYS D 136 ? HIS G 131 LYS G 136 
AB2 5 SER D 144 ? VAL D 147 ? SER G 144 VAL G 147 
AB3 1 LEU D 112 ? LYS D 114 ? LEU G 112 LYS G 114 
AB3 2 LEU D 192 ? THR D 197 ? LEU G 192 THR G 197 
AB3 3 GLU D 282 ? TRP D 283 ? GLU G 282 TRP G 283 
AB4 1 SER D 204 ? GLN D 208 ? SER G 204 GLN G 208 
AB4 2 THR D 220 ? SER D 225 ? THR G 220 SER G 225 
AB4 3 PHE D 255 ? PRO D 260 ? PHE G 255 PRO G 260 
AB4 4 VAL D 248 ? ARG D 249 ? VAL G 248 ARG G 249 
AB5 1 LYS D 212 ? VAL D 213 ? LYS G 212 VAL G 213 
AB5 2 LEU D 290 ? VAL D 294 ? LEU G 290 VAL G 294 
AB5 3 GLY D 267 ? SER D 275 ? GLY G 267 SER G 275 
AB5 4 MET D 231 ? ARG D 236 ? MET G 231 ARG G 236 
AB5 5 GLU D 242 ? PRO D 246 ? GLU G 242 PRO G 246 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 46  ? O ALA A 46  N ARG A 35  ? N ARG A 35  
AA1 2 3 O PHE A 33  ? O PHE A 33  N GLY A 26  ? N GLY A 26  
AA1 3 4 O ILE A 23  ? O ILE A 23  N THR A 10  ? N THR A 10  
AA1 4 5 N HIS A 3   ? N HIS A 3   O VAL A 103 ? O VAL A 103 
AA1 5 6 N ASP A 102 ? N ASP A 102 O LEU A 110 ? O LEU A 110 
AA1 6 7 N ASN A 114 ? N ASN A 114 O LEU A 126 ? O LEU A 126 
AA1 7 8 N ALA A 125 ? N ALA A 125 O THR A 134 ? O THR A 134 
AA2 1 2 N HIS A 192 ? N HIS A 192 O THR A 200 ? O THR A 200 
AA2 2 3 N CYS A 203 ? N CYS A 203 O ALA A 245 ? O ALA A 245 
AA2 3 4 O ALA A 246 ? O ALA A 246 N GLU A 229 ? N GLU A 229 
AA3 1 2 N HIS A 192 ? N HIS A 192 O THR A 200 ? O THR A 200 
AA3 2 3 N CYS A 203 ? N CYS A 203 O ALA A 245 ? O ALA A 245 
AA3 3 4 O GLN A 242 ? O GLN A 242 N ARG A 234 ? N ARG A 234 
AA4 1 2 O GLU A 222 ? O GLU A 222 N ARG A 219 ? N ARG A 219 
AA4 2 3 N THR A 216 ? N THR A 216 O HIS A 260 ? O HIS A 260 
AA4 3 4 N CYS A 259 ? N CYS A 259 O LEU A 272 ? O LEU A 272 
AA5 1 2 N LYS B 7   ? N LYS B 6   O SER B 29  ? O SER B 28  
AA5 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA5 3 4 O TYR B 68  ? O TYR B 67  N GLU B 51  ? N GLU B 50  
AA6 1 2 N LYS B 7   ? N LYS B 6   O SER B 29  ? O SER B 28  
AA6 2 3 N LEU B 24  ? N LEU B 23  O THR B 69  ? O THR B 68  
AA6 3 4 O TYR B 64  ? O TYR B 63  N SER B 56  ? N SER B 55  
AA7 1 2 O GLU B 45  ? O GLU B 44  N LYS B 42  ? N LYS B 41  
AA7 2 3 N ASP B 39  ? N ASP B 38  O ARG B 82  ? O ARG B 81  
AA7 3 4 N VAL B 83  ? N VAL B 82  O LYS B 92  ? O LYS B 91  
AA8 1 2 N SER D 11  ? N SER G 11  O ARG D 27  ? O ARG G 27  
AA8 2 3 N VAL D 24  ? N VAL G 24  O MET D 61  ? O MET G 61  
AA9 1 2 N VAL D 18  ? N VAL G 18  O MET D 95  ? O MET G 95  
AA9 2 3 O VAL D 92  ? O VAL G 92  N TYR D 72  ? N TYR G 72  
AA9 3 4 O THR D 73  ? O THR G 73  N TYR D 40  ? N TYR G 40  
AB1 1 2 N LEU D 106 ? N LEU G 106 O GLN D 122 ? O GLN G 122 
AB1 2 3 N LEU D 121 ? N LEU G 121 O PHE D 159 ? O PHE G 159 
AB1 3 4 O LYS D 156 ? O LYS G 156 N GLN D 149 ? N GLN G 149 
AB2 1 2 N VAL D 113 ? N VAL G 113 O VAL D 195 ? O VAL G 195 
AB2 2 3 O ILE D 194 ? O ILE G 194 N GLY D 170 ? N GLY G 170 
AB2 3 4 O ARG D 173 ? O ARG G 173 N HIS D 135 ? N HIS G 135 
AB2 4 5 N PHE D 132 ? N PHE G 132 O LEU D 146 ? O LEU G 146 
AB3 1 2 N VAL D 113 ? N VAL G 113 O VAL D 195 ? O VAL G 195 
AB3 2 3 N VAL D 196 ? N VAL G 196 O TRP D 283 ? O TRP G 283 
AB4 1 2 N SER D 206 ? N SER G 206 O SER D 222 ? O SER G 222 
AB4 2 3 N SER D 225 ? N SER G 225 O PHE D 255 ? O PHE G 255 
AB4 3 4 O GLN D 256 ? O GLN G 256 N VAL D 248 ? N VAL G 248 
AB5 1 2 N VAL D 213 ? N VAL G 213 O SER D 293 ? O SER G 293 
AB5 2 3 O LEU D 290 ? O LEU G 290 N TYR D 270 ? N TYR G 270 
AB5 3 4 O PHE D 273 ? O PHE G 273 N HIS D 233 ? N HIS G 233 
AB5 4 5 N TYR D 232 ? N TYR G 232 O LEU D 245 ? O LEU G 245 
# 
_pdbx_entry_details.entry_id                   9BL3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 29  ? ? 49.56   -119.51 
2 1 SER A 42  ? ? 54.80   70.05   
3 1 ASN A 114 ? ? -161.48 113.42  
4 1 SER A 195 ? ? -168.04 -161.89 
5 1 GLN A 224 ? ? -90.54  49.06   
6 1 TRP B 60  ? ? 80.10   -0.52   
7 1 HIS G 46  ? ? 69.41   -0.42   
8 1 SER G 186 ? ? -59.40  170.99  
9 1 ALA G 264 ? ? -164.12 38.97   
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
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 G HIS 1   ? D HIS 1   
2  1 Y 1 G MET 2   ? D MET 2   
3  1 Y 1 G GLY 3   ? D GLY 3   
4  1 Y 1 G GLY 4   ? D GLY 4   
5  1 Y 1 G GLN 5   ? D GLN 5   
6  1 Y 1 G ALA 240 ? D ALA 240 
7  1 Y 1 G GLY 296 ? D GLY 296 
8  1 Y 1 G ASN 297 ? D ASN 297 
9  1 Y 1 G PRO 298 ? D PRO 298 
10 1 Y 1 G SER 299 ? D SER 299 
11 1 Y 1 G HIS 300 ? D HIS 300 
12 1 Y 1 G HIS 301 ? D HIS 301 
13 1 Y 1 G HIS 302 ? D HIS 302 
14 1 Y 1 G HIS 303 ? D HIS 303 
15 1 Y 1 G HIS 304 ? D HIS 304 
16 1 Y 1 G HIS 305 ? D HIS 305 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAG C1   C N R 250 
NAG C2   C N R 251 
NAG C3   C N R 252 
NAG C4   C N S 253 
NAG C5   C N R 254 
NAG C6   C N N 255 
NAG C7   C N N 256 
NAG C8   C N N 257 
NAG N2   N N N 258 
NAG O1   O N N 259 
NAG O3   O N N 260 
NAG O4   O N N 261 
NAG O5   O N N 262 
NAG O6   O N N 263 
NAG O7   O N N 264 
NAG H1   H N N 265 
NAG H2   H N N 266 
NAG H3   H N N 267 
NAG H4   H N N 268 
NAG H5   H N N 269 
NAG H61  H N N 270 
NAG H62  H N N 271 
NAG H81  H N N 272 
NAG H82  H N N 273 
NAG H83  H N N 274 
NAG HN2  H N N 275 
NAG HO1  H N N 276 
NAG HO3  H N N 277 
NAG HO4  H N N 278 
NAG HO6  H N N 279 
PHE N    N N N 280 
PHE CA   C N S 281 
PHE C    C N N 282 
PHE O    O N N 283 
PHE CB   C N N 284 
PHE CG   C Y N 285 
PHE CD1  C Y N 286 
PHE CD2  C Y N 287 
PHE CE1  C Y N 288 
PHE CE2  C Y N 289 
PHE CZ   C Y N 290 
PHE OXT  O N N 291 
PHE H    H N N 292 
PHE H2   H N N 293 
PHE HA   H N N 294 
PHE HB2  H N N 295 
PHE HB3  H N N 296 
PHE HD1  H N N 297 
PHE HD2  H N N 298 
PHE HE1  H N N 299 
PHE HE2  H N N 300 
PHE HZ   H N N 301 
PHE HXT  H N N 302 
PRO N    N N N 303 
PRO CA   C N S 304 
PRO C    C N N 305 
PRO O    O N N 306 
PRO CB   C N N 307 
PRO CG   C N N 308 
PRO CD   C N N 309 
PRO OXT  O N N 310 
PRO H    H N N 311 
PRO HA   H N N 312 
PRO HB2  H N N 313 
PRO HB3  H N N 314 
PRO HG2  H N N 315 
PRO HG3  H N N 316 
PRO HD2  H N N 317 
PRO HD3  H N N 318 
PRO HXT  H N N 319 
SER N    N N N 320 
SER CA   C N S 321 
SER C    C N N 322 
SER O    O N N 323 
SER CB   C N N 324 
SER OG   O N N 325 
SER OXT  O N N 326 
SER H    H N N 327 
SER H2   H N N 328 
SER HA   H N N 329 
SER HB2  H N N 330 
SER HB3  H N N 331 
SER HG   H N N 332 
SER HXT  H N N 333 
THR N    N N N 334 
THR CA   C N S 335 
THR C    C N N 336 
THR O    O N N 337 
THR CB   C N R 338 
THR OG1  O N N 339 
THR CG2  C N N 340 
THR OXT  O N N 341 
THR H    H N N 342 
THR H2   H N N 343 
THR HA   H N N 344 
THR HB   H N N 345 
THR HG1  H N N 346 
THR HG21 H N N 347 
THR HG22 H N N 348 
THR HG23 H N N 349 
THR HXT  H N N 350 
TRP N    N N N 351 
TRP CA   C N S 352 
TRP C    C N N 353 
TRP O    O N N 354 
TRP CB   C N N 355 
TRP CG   C Y N 356 
TRP CD1  C Y N 357 
TRP CD2  C Y N 358 
TRP NE1  N Y N 359 
TRP CE2  C Y N 360 
TRP CE3  C Y N 361 
TRP CZ2  C Y N 362 
TRP CZ3  C Y N 363 
TRP CH2  C Y N 364 
TRP OXT  O N N 365 
TRP H    H N N 366 
TRP H2   H N N 367 
TRP HA   H N N 368 
TRP HB2  H N N 369 
TRP HB3  H N N 370 
TRP HD1  H N N 371 
TRP HE1  H N N 372 
TRP HE3  H N N 373 
TRP HZ2  H N N 374 
TRP HZ3  H N N 375 
TRP HH2  H N N 376 
TRP HXT  H N N 377 
TYR N    N N N 378 
TYR CA   C N S 379 
TYR C    C N N 380 
TYR O    O N N 381 
TYR CB   C N N 382 
TYR CG   C Y N 383 
TYR CD1  C Y N 384 
TYR CD2  C Y N 385 
TYR CE1  C Y N 386 
TYR CE2  C Y N 387 
TYR CZ   C Y N 388 
TYR OH   O N N 389 
TYR OXT  O N N 390 
TYR H    H N N 391 
TYR H2   H N N 392 
TYR HA   H N N 393 
TYR HB2  H N N 394 
TYR HB3  H N N 395 
TYR HD1  H N N 396 
TYR HD2  H N N 397 
TYR HE1  H N N 398 
TYR HE2  H N N 399 
TYR HH   H N N 400 
TYR HXT  H N N 401 
VAL N    N N N 402 
VAL CA   C N S 403 
VAL C    C N N 404 
VAL O    O N N 405 
VAL CB   C N N 406 
VAL CG1  C N N 407 
VAL CG2  C N N 408 
VAL OXT  O N N 409 
VAL H    H N N 410 
VAL H2   H N N 411 
VAL HA   H N N 412 
VAL HB   H N N 413 
VAL HG11 H N N 414 
VAL HG12 H N N 415 
VAL HG13 H N N 416 
VAL HG21 H N N 417 
VAL HG22 H N N 418 
VAL HG23 H N N 419 
VAL HXT  H N N 420 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAG C1  C2   sing N N 237 
NAG C1  O1   sing N N 238 
NAG C1  O5   sing N N 239 
NAG C1  H1   sing N N 240 
NAG C2  C3   sing N N 241 
NAG C2  N2   sing N N 242 
NAG C2  H2   sing N N 243 
NAG C3  C4   sing N N 244 
NAG C3  O3   sing N N 245 
NAG C3  H3   sing N N 246 
NAG C4  C5   sing N N 247 
NAG C4  O4   sing N N 248 
NAG C4  H4   sing N N 249 
NAG C5  C6   sing N N 250 
NAG C5  O5   sing N N 251 
NAG C5  H5   sing N N 252 
NAG C6  O6   sing N N 253 
NAG C6  H61  sing N N 254 
NAG C6  H62  sing N N 255 
NAG C7  C8   sing N N 256 
NAG C7  N2   sing N N 257 
NAG C7  O7   doub N N 258 
NAG C8  H81  sing N N 259 
NAG C8  H82  sing N N 260 
NAG C8  H83  sing N N 261 
NAG N2  HN2  sing N N 262 
NAG O1  HO1  sing N N 263 
NAG O3  HO3  sing N N 264 
NAG O4  HO4  sing N N 265 
NAG O6  HO6  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           2008981 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3VH8 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1' 
_space_group.name_Hall        'P 1' 
_space_group.IT_number        1 
_space_group.crystal_system   triclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BL3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019317 
_atom_sites.fract_transf_matrix[1][2]   0.006657 
_atom_sites.fract_transf_matrix[1][3]   0.003835 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017401 
_atom_sites.fract_transf_matrix[2][3]   0.002695 
_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]   0.015717 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 1   ? 5.38200   -35.51200 -33.78200 1.000 56.18568  ? 1   GLY A N   1 
ATOM   2    C CA  . GLY A 1 1   ? 4.47300   -34.61000 -33.09000 1.000 56.00935  ? 1   GLY A CA  1 
ATOM   3    C C   . GLY A 1 1   ? 4.01700   -33.39100 -33.88900 1.000 55.51981  ? 1   GLY A C   1 
ATOM   4    O O   . GLY A 1 1   ? 4.48800   -33.15800 -35.00200 1.000 55.75142  ? 1   GLY A O   1 
ATOM   5    N N   . SER A 1 2   ? 3.07900   -32.63800 -33.31300 1.000 48.18472  ? 2   SER A N   1 
ATOM   6    C CA  . SER A 1 2   ? 2.58900   -31.39700 -33.88900 1.000 48.84270  ? 2   SER A CA  1 
ATOM   7    C C   . SER A 1 2   ? 3.53800   -30.24300 -33.58200 1.000 47.61624  ? 2   SER A C   1 
ATOM   8    O O   . SER A 1 2   ? 4.34100   -30.29300 -32.65100 1.000 46.91352  ? 2   SER A O   1 
ATOM   9    C CB  . SER A 1 2   ? 1.19300   -31.06900 -33.36100 1.000 47.72941  ? 2   SER A CB  1 
ATOM   10   O OG  . SER A 1 2   ? 0.24400   -31.98700 -33.86500 1.000 49.07430  ? 2   SER A OG  1 
ATOM   11   N N   . HIS A 1 3   ? 3.43300   -29.18400 -34.38000 1.000 34.13041  ? 3   HIS A N   1 
ATOM   12   C CA  . HIS A 1 3   ? 4.35300   -28.07200 -34.22400 1.000 33.99092  ? 3   HIS A CA  1 
ATOM   13   C C   . HIS A 1 3   ? 3.64000   -26.77400 -34.54000 1.000 32.93026  ? 3   HIS A C   1 
ATOM   14   O O   . HIS A 1 3   ? 2.58400   -26.74700 -35.17400 1.000 32.83815  ? 3   HIS A O   1 
ATOM   15   C CB  . HIS A 1 3   ? 5.60200   -28.22900 -35.10800 1.000 33.74878  ? 3   HIS A CB  1 
ATOM   16   C CG  . HIS A 1 3   ? 6.43900   -29.42300 -34.76200 1.000 33.93038  ? 3   HIS A CG  1 
ATOM   17   N ND1 . HIS A 1 3   ? 7.29800   -29.44300 -33.68700 1.000 32.91447  ? 3   HIS A ND1 1 
ATOM   18   C CD2 . HIS A 1 3   ? 6.54900   -30.64100 -35.35000 1.000 34.58046  ? 3   HIS A CD2 1 
ATOM   19   C CE1 . HIS A 1 3   ? 7.90200   -30.61900 -33.62400 1.000 33.08291  ? 3   HIS A CE1 1 
ATOM   20   N NE2 . HIS A 1 3   ? 7.46500   -31.36400 -34.62100 1.000 33.95933  ? 3   HIS A NE2 1 
ATOM   21   N N   . SER A 1 4   ? 4.24900   -25.68500 -34.11000 1.000 36.52017  ? 4   SER A N   1 
ATOM   22   C CA  . SER A 1 4   ? 3.62000   -24.39400 -34.27000 1.000 36.04116  ? 4   SER A CA  1 
ATOM   23   C C   . SER A 1 4   ? 4.69000   -23.35200 -34.54400 1.000 35.16474  ? 4   SER A C   1 
ATOM   24   O O   . SER A 1 4   ? 5.85500   -23.51700 -34.17200 1.000 34.43571  ? 4   SER A O   1 
ATOM   25   C CB  . SER A 1 4   ? 2.83000   -24.02500 -33.01700 1.000 35.57269  ? 4   SER A CB  1 
ATOM   26   O OG  . SER A 1 4   ? 3.76000   -23.68200 -31.99900 1.000 35.05947  ? 4   SER A OG  1 
ATOM   27   N N   . MET A 1 5   ? 4.28400   -22.29700 -35.22900 1.000 37.73084  ? 5   MET A N   1 
ATOM   28   C CA  . MET A 1 5   ? 5.09100   -21.11100 -35.40700 1.000 35.61216  ? 5   MET A CA  1 
ATOM   29   C C   . MET A 1 5   ? 4.24200   -19.93500 -34.95100 1.000 34.98577  ? 5   MET A C   1 
ATOM   30   O O   . MET A 1 5   ? 3.04700   -19.88300 -35.25600 1.000 35.59637  ? 5   MET A O   1 
ATOM   31   C CB  . MET A 1 5   ? 5.52600   -20.92800 -36.88300 1.000 33.68825  ? 5   MET A CB  1 
ATOM   32   C CG  . MET A 1 5   ? 6.35200   -19.67300 -37.12600 1.000 31.32744  ? 5   MET A CG  1 
ATOM   33   S SD  . MET A 1 5   ? 7.23300   -19.67100 -38.71900 1.000 30.76158  ? 5   MET A SD  1 
ATOM   34   C CE  . MET A 1 5   ? 5.92500   -19.38900 -39.88000 1.000 30.85107  ? 5   MET A CE  1 
ATOM   35   N N   . ARG A 1 6   ? 4.85200   -19.00700 -34.20700 1.000 29.49564  ? 6   ARG A N   1 
ATOM   36   C CA  . ARG A 1 6   ? 4.17200   -17.78400 -33.79300 1.000 29.14560  ? 6   ARG A CA  1 
ATOM   37   C C   . ARG A 1 6   ? 5.09100   -16.58000 -33.97200 1.000 26.50844  ? 6   ARG A C   1 
ATOM   38   O O   . ARG A 1 6   ? 6.29800   -16.66900 -33.71000 1.000 25.10827  ? 6   ARG A O   1 
ATOM   39   C CB  . ARG A 1 6   ? 3.74700   -17.82500 -32.32600 1.000 29.72988  ? 6   ARG A CB  1 
ATOM   40   C CG  . ARG A 1 6   ? 2.72400   -18.88900 -31.97300 1.000 30.96424  ? 6   ARG A CG  1 
ATOM   41   C CD  . ARG A 1 6   ? 1.33000   -18.49100 -32.43700 1.000 31.45114  ? 6   ARG A CD  1 
ATOM   42   N NE  . ARG A 1 6   ? 0.37000   -19.45100 -31.92100 1.000 32.20912  ? 6   ARG A NE  1 
ATOM   43   C CZ  . ARG A 1 6   ? 0.15300   -20.64600 -32.45100 1.000 32.72761  ? 6   ARG A CZ  1 
ATOM   44   N NH1 . ARG A 1 6   ? 0.73500   -21.01800 -33.58300 1.000 32.74077  ? 6   ARG A NH1 1 
ATOM   45   N NH2 . ARG A 1 6   ? -0.64400  -21.50000 -31.81400 1.000 33.00659  ? 6   ARG A NH2 1 
ATOM   46   N N   . TYR A 1 7   ? 4.50200   -15.45300 -34.38200 1.000 31.08531  ? 7   TYR A N   1 
ATOM   47   C CA  . TYR A 1 7   ? 5.11700   -14.13800 -34.24700 1.000 29.54038  ? 7   TYR A CA  1 
ATOM   48   C C   . TYR A 1 7   ? 4.33800   -13.32200 -33.22800 1.000 30.21415  ? 7   TYR A C   1 
ATOM   49   O O   . TYR A 1 7   ? 3.10000   -13.33500 -33.22300 1.000 31.80118  ? 7   TYR A O   1 
ATOM   50   C CB  . TYR A 1 7   ? 5.16300   -13.37900 -35.57700 1.000 28.74292  ? 7   TYR A CB  1 
ATOM   51   C CG  . TYR A 1 7   ? 6.19100   -13.95100 -36.51100 1.000 28.46394  ? 7   TYR A CG  1 
ATOM   52   C CD1 . TYR A 1 7   ? 5.87700   -15.04300 -37.33500 1.000 29.35878  ? 7   TYR A CD1 1 
ATOM   53   C CD2 . TYR A 1 7   ? 7.49700   -13.44900 -36.53700 1.000 28.22180  ? 7   TYR A CD2 1 
ATOM   54   C CE1 . TYR A 1 7   ? 6.85100   -15.60000 -38.18200 1.000 29.27719  ? 7   TYR A CE1 1 
ATOM   55   C CE2 . TYR A 1 7   ? 8.46400   -13.99000 -37.38200 1.000 28.96137  ? 7   TYR A CE2 1 
ATOM   56   C CZ  . TYR A 1 7   ? 8.13200   -15.05100 -38.20200 1.000 29.17455  ? 7   TYR A CZ  1 
ATOM   57   O OH  . TYR A 1 7   ? 9.08900   -15.58600 -39.03100 1.000 30.22994  ? 7   TYR A OH  1 
ATOM   58   N N   . PHE A 1 8   ? 5.08100   -12.61800 -32.37200 1.000 28.76661  ? 8   PHE A N   1 
ATOM   59   C CA  . PHE A 1 8   ? 4.51700   -11.75300 -31.35400 1.000 29.36405  ? 8   PHE A CA  1 
ATOM   60   C C   . PHE A 1 8   ? 5.07800   -10.34400 -31.52500 1.000 28.50605  ? 8   PHE A C   1 
ATOM   61   O O   . PHE A 1 8   ? 6.30200   -10.14900 -31.52700 1.000 27.84281  ? 8   PHE A O   1 
ATOM   62   C CB  . PHE A 1 8   ? 4.83800   -12.26400 -29.95000 1.000 29.46406  ? 8   PHE A CB  1 
ATOM   63   C CG  . PHE A 1 8   ? 4.42500   -13.70700 -29.68400 1.000 30.84580  ? 8   PHE A CG  1 
ATOM   64   C CD1 . PHE A 1 8   ? 3.10200   -14.03500 -29.40200 1.000 32.15386  ? 8   PHE A CD1 1 
ATOM   65   C CD2 . PHE A 1 8   ? 5.36800   -14.72300 -29.68500 1.000 30.38259  ? 8   PHE A CD2 1 
ATOM   66   C CE1 . PHE A 1 8   ? 2.72600   -15.35200 -29.12000 1.000 32.92763  ? 8   PHE A CE1 1 
ATOM   67   C CE2 . PHE A 1 8   ? 4.99400   -16.04100 -29.40400 1.000 31.34850  ? 8   PHE A CE2 1 
ATOM   68   C CZ  . PHE A 1 8   ? 3.67000   -16.34800 -29.13700 1.000 32.67497  ? 8   PHE A CZ  1 
ATOM   69   N N   . TYR A 1 9   ? 4.18600   -9.36900  -31.65300 1.000 28.16390  ? 9   TYR A N   1 
ATOM   70   C CA  . TYR A 1 9   ? 4.55100   -7.96000  -31.74100 1.000 27.70332  ? 9   TYR A CA  1 
ATOM   71   C C   . TYR A 1 9   ? 4.13800   -7.22500  -30.47600 1.000 28.29023  ? 9   TYR A C   1 
ATOM   72   O O   . TYR A 1 9   ? 3.01300   -7.39300  -30.00300 1.000 29.69040  ? 9   TYR A O   1 
ATOM   73   C CB  . TYR A 1 9   ? 3.83800   -7.26300  -32.88700 1.000 28.30603  ? 9   TYR A CB  1 
ATOM   74   C CG  . TYR A 1 9   ? 4.07800   -7.78500  -34.27800 1.000 28.04810  ? 9   TYR A CG  1 
ATOM   75   C CD1 . TYR A 1 9   ? 5.09900   -8.67200  -34.55500 1.000 27.37697  ? 9   TYR A CD1 1 
ATOM   76   C CD2 . TYR A 1 9   ? 3.28800   -7.34600  -35.31700 1.000 28.72713  ? 9   TYR A CD2 1 
ATOM   77   C CE1 . TYR A 1 9   ? 5.30400   -9.13100  -35.84800 1.000 27.50067  ? 9   TYR A CE1 1 
ATOM   78   C CE2 . TYR A 1 9   ? 3.47600   -7.80900  -36.60900 1.000 28.86662  ? 9   TYR A CE2 1 
ATOM   79   C CZ  . TYR A 1 9   ? 4.49000   -8.69500  -36.86200 1.000 28.12179  ? 9   TYR A CZ  1 
ATOM   80   O OH  . TYR A 1 9   ? 4.68200   -9.13800  -38.14800 1.000 28.37182  ? 9   TYR A OH  1 
ATOM   81   N N   . THR A 1 10  ? 5.01000   -6.34800  -29.98300 1.000 27.83755  ? 10  THR A N   1 
ATOM   82   C CA  . THR A 1 10  ? 4.65300   -5.38800  -28.94500 1.000 28.52974  ? 10  THR A CA  1 
ATOM   83   C C   . THR A 1 10  ? 4.97400   -3.98800  -29.45400 1.000 28.99821  ? 10  THR A C   1 
ATOM   84   O O   . THR A 1 10  ? 6.12500   -3.69900  -29.79200 1.000 29.64303  ? 10  THR A O   1 
ATOM   85   C CB  . THR A 1 10  ? 5.40500   -5.68200  -27.65400 1.000 29.18245  ? 10  THR A CB  1 
ATOM   86   O OG1 . THR A 1 10  ? 5.14000   -7.04700  -27.25600 1.000 28.72713  ? 10  THR A OG1 1 
ATOM   87   C CG2 . THR A 1 10  ? 4.96600   -4.70000  -26.53300 1.000 29.87990  ? 10  THR A CG2 1 
ATOM   88   N N   . ALA A 1 11  ? 3.95500   -3.13700  -29.53900 1.000 30.94845  ? 11  ALA A N   1 
ATOM   89   C CA  . ALA A 1 11  ? 4.10300   -1.73800  -29.93400 1.000 31.86698  ? 11  ALA A CA  1 
ATOM   90   C C   . ALA A 1 11  ? 3.72000   -0.87500  -28.74200 1.000 32.69603  ? 11  ALA A C   1 
ATOM   91   O O   . ALA A 1 11  ? 2.60600   -1.00600  -28.21800 1.000 33.00133  ? 11  ALA A O   1 
ATOM   92   C CB  . ALA A 1 11  ? 3.21700   -1.41100  -31.13800 1.000 31.69591  ? 11  ALA A CB  1 
ATOM   93   N N   . MET A 1 12  ? 4.63800   -0.01600  -28.30600 1.000 42.06294  ? 12  MET A N   1 
ATOM   94   C CA  . MET A 1 12  ? 4.47100   0.73900   -27.07000 1.000 43.36836  ? 12  MET A CA  1 
ATOM   95   C C   . MET A 1 12  ? 4.69100   2.22600   -27.32400 1.000 44.72642  ? 12  MET A C   1 
ATOM   96   O O   . MET A 1 12  ? 5.67000   2.61500   -27.96800 1.000 45.82128  ? 12  MET A O   1 
ATOM   97   C CB  . MET A 1 12  ? 5.44900   0.24900   -25.99200 1.000 43.44205  ? 12  MET A CB  1 
ATOM   98   C CG  . MET A 1 12  ? 5.83300   -1.22600  -26.10300 1.000 43.10254  ? 12  MET A CG  1 
ATOM   99   S SD  . MET A 1 12  ? 7.25400   -1.67600  -25.08500 1.000 44.81853  ? 12  MET A SD  1 
ATOM   100  C CE  . MET A 1 12  ? 8.17200   -0.15000  -25.13700 1.000 44.67378  ? 12  MET A CE  1 
ATOM   101  N N   . SER A 1 13  ? 3.78400   3.04500   -26.80900 1.000 34.19884  ? 13  SER A N   1 
ATOM   102  C CA  . SER A 1 13  ? 3.99700   4.48000   -26.69900 1.000 35.44636  ? 13  SER A CA  1 
ATOM   103  C C   . SER A 1 13  ? 4.49400   4.79100   -25.29100 1.000 35.98326  ? 13  SER A C   1 
ATOM   104  O O   . SER A 1 13  ? 4.09000   4.14300   -24.31700 1.000 34.86471  ? 13  SER A O   1 
ATOM   105  C CB  . SER A 1 13  ? 2.71500   5.26300   -26.98900 1.000 36.08854  ? 13  SER A CB  1 
ATOM   106  O OG  . SER A 1 13  ? 1.70300   4.93500   -26.04700 1.000 36.05169  ? 13  SER A OG  1 
ATOM   107  N N   . ARG A 1 14  ? 5.40000   5.76100   -25.19100 1.000 41.02071  ? 14  ARG A N   1 
ATOM   108  C CA  . ARG A 1 14  ? 6.00100   6.13600   -23.91000 1.000 41.36022  ? 14  ARG A CA  1 
ATOM   109  C C   . ARG A 1 14  ? 6.35000   7.61800   -23.95600 1.000 41.97872  ? 14  ARG A C   1 
ATOM   110  O O   . ARG A 1 14  ? 7.52300   7.99800   -23.97400 1.000 42.64985  ? 14  ARG A O   1 
ATOM   111  C CB  . ARG A 1 14  ? 7.23000   5.27300   -23.63600 1.000 41.38917  ? 14  ARG A CB  1 
ATOM   112  C CG  . ARG A 1 14  ? 7.93300   4.94700   -24.92800 1.000 41.97609  ? 14  ARG A CG  1 
ATOM   113  C CD  . ARG A 1 14  ? 8.96400   3.85100   -24.79400 1.000 42.61564  ? 14  ARG A CD  1 
ATOM   114  N NE  . ARG A 1 14  ? 9.96500   3.97400   -25.84800 1.000 42.92883  ? 14  ARG A NE  1 
ATOM   115  C CZ  . ARG A 1 14  ? 11.16000  3.40900   -25.79800 1.000 42.91567  ? 14  ARG A CZ  1 
ATOM   116  N NH1 . ARG A 1 14  ? 11.51800  2.65100   -24.77000 1.000 43.39204  ? 14  ARG A NH1 1 
ATOM   117  N NH2 . ARG A 1 14  ? 12.01700  3.61200   -26.79500 1.000 42.71038  ? 14  ARG A NH2 1 
ATOM   118  N N   . PRO A 1 15  ? 5.33500   8.48600   -23.98500 1.000 36.34120  ? 15  PRO A N   1 
ATOM   119  C CA  . PRO A 1 15  ? 5.56300   9.91900   -24.22500 1.000 37.02023  ? 15  PRO A CA  1 
ATOM   120  C C   . PRO A 1 15  ? 6.54200   10.51100  -23.23000 1.000 37.85980  ? 15  PRO A C   1 
ATOM   121  O O   . PRO A 1 15  ? 6.36400   10.39800  -22.02000 1.000 37.43607  ? 15  PRO A O   1 
ATOM   122  C CB  . PRO A 1 15  ? 4.16900   10.53500  -24.05600 1.000 37.46502  ? 15  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 15  ? 3.21200   9.44000   -24.21200 1.000 36.43595  ? 15  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 15  ? 3.90300   8.15800   -23.85100 1.000 35.95957  ? 15  PRO A CD  1 
ATOM   125  N N   . GLY A 1 16  ? 7.57600   11.16600  -23.75700 1.000 34.95682  ? 16  GLY A N   1 
ATOM   126  C CA  . GLY A 1 16  ? 8.57100   11.82500  -22.94000 1.000 36.22540  ? 16  GLY A CA  1 
ATOM   127  C C   . GLY A 1 16  ? 9.65400   10.91500  -22.39900 1.000 36.48595  ? 16  GLY A C   1 
ATOM   128  O O   . GLY A 1 16  ? 10.63600  11.41900  -21.83400 1.000 38.88624  ? 16  GLY A O   1 
ATOM   129  N N   . ARG A 1 17  ? 9.51300   9.59800   -22.55000 1.000 48.24263  ? 17  ARG A N   1 
ATOM   130  C CA  . ARG A 1 17  ? 10.50500  8.63800   -22.08800 1.000 48.01892  ? 17  ARG A CA  1 
ATOM   131  C C   . ARG A 1 17  ? 11.26600  7.96700   -23.21500 1.000 48.47160  ? 17  ARG A C   1 
ATOM   132  O O   . ARG A 1 17  ? 12.39600  7.53000   -22.99900 1.000 48.54003  ? 17  ARG A O   1 
ATOM   133  C CB  . ARG A 1 17  ? 9.84600   7.55700   -21.21000 1.000 46.84509  ? 17  ARG A CB  1 
ATOM   134  C CG  . ARG A 1 17  ? 9.20600   8.12000   -19.93500 1.000 46.98984  ? 17  ARG A CG  1 
ATOM   135  C CD  . ARG A 1 17  ? 8.66900   7.04700   -18.99800 1.000 46.05552  ? 17  ARG A CD  1 
ATOM   136  N NE  . ARG A 1 17  ? 7.45300   6.39800   -19.48400 1.000 45.84234  ? 17  ARG A NE  1 
ATOM   137  C CZ  . ARG A 1 17  ? 7.41400   5.18000   -20.01300 1.000 45.94235  ? 17  ARG A CZ  1 
ATOM   138  N NH1 . ARG A 1 17  ? 8.52100   4.47500   -20.21700 1.000 45.40281  ? 17  ARG A NH1 1 
ATOM   139  N NH2 . ARG A 1 17  ? 6.23400   4.65200   -20.34400 1.000 44.70273  ? 17  ARG A NH2 1 
ATOM   140  N N   . GLY A 1 18  ? 10.68200  7.88300   -24.40600 1.000 36.81231  ? 18  GLY A N   1 
ATOM   141  C CA  . GLY A 1 18  ? 11.36400  7.32600   -25.56000 1.000 36.62018  ? 18  GLY A CA  1 
ATOM   142  C C   . GLY A 1 18  ? 10.50400  7.52400   -26.78800 1.000 35.73060  ? 18  GLY A C   1 
ATOM   143  O O   . GLY A 1 18  ? 9.37900   8.02100   -26.71200 1.000 35.68323  ? 18  GLY A O   1 
ATOM   144  N N   . GLU A 1 19  ? 11.05900  7.16000   -27.93400 1.000 47.47675  ? 19  GLU A N   1 
ATOM   145  C CA  . GLU A 1 19  ? 10.26700  7.12100   -29.14400 1.000 46.69507  ? 19  GLU A CA  1 
ATOM   146  C C   . GLU A 1 19  ? 9.30200   5.93500   -29.08700 1.000 45.88708  ? 19  GLU A C   1 
ATOM   147  O O   . GLU A 1 19  ? 9.56700   4.95000   -28.39600 1.000 45.93445  ? 19  GLU A O   1 
ATOM   148  C CB  . GLU A 1 19  ? 11.17500  6.98700   -30.36600 1.000 47.42148  ? 19  GLU A CB  1 
ATOM   149  C CG  . GLU A 1 19  ? 12.18800  8.10800   -30.53200 1.000 47.84784  ? 19  GLU A CG  1 
ATOM   150  C CD  . GLU A 1 19  ? 11.55200  9.42400   -30.92500 1.000 49.21906  ? 19  GLU A CD  1 
ATOM   151  O OE1 . GLU A 1 19  ? 10.31000  9.48600   -31.07000 1.000 48.61372  ? 19  GLU A OE1 1 
ATOM   152  O OE2 . GLU A 1 19  ? 12.30300  10.40300  -31.09400 1.000 50.08495  ? 19  GLU A OE2 1 
ATOM   153  N N   . PRO A 1 20  ? 8.17400   6.01100   -29.79100 1.000 40.46538  ? 20  PRO A N   1 
ATOM   154  C CA  . PRO A 1 20  ? 7.30900   4.83400   -29.91100 1.000 40.19429  ? 20  PRO A CA  1 
ATOM   155  C C   . PRO A 1 20  ? 8.13600   3.64700   -30.38200 1.000 39.89426  ? 20  PRO A C   1 
ATOM   156  O O   . PRO A 1 20  ? 8.96500   3.76800   -31.29100 1.000 39.43894  ? 20  PRO A O   1 
ATOM   157  C CB  . PRO A 1 20  ? 6.26900   5.26000   -30.95500 1.000 39.32577  ? 20  PRO A CB  1 
ATOM   158  C CG  . PRO A 1 20  ? 6.25500   6.71500   -30.88400 1.000 39.59685  ? 20  PRO A CG  1 
ATOM   159  C CD  . PRO A 1 20  ? 7.66400   7.13900   -30.58900 1.000 40.74173  ? 20  PRO A CD  1 
ATOM   160  N N   . ARG A 1 21  ? 7.95000   2.50900   -29.72200 1.000 43.70524  ? 21  ARG A N   1 
ATOM   161  C CA  . ARG A 1 21  ? 8.85200   1.37700   -29.86700 1.000 43.64471  ? 21  ARG A CA  1 
ATOM   162  C C   . ARG A 1 21  ? 8.09800   0.12500   -30.31500 1.000 42.74723  ? 21  ARG A C   1 
ATOM   163  O O   . ARG A 1 21  ? 7.02100   -0.18000  -29.78800 1.000 41.59972  ? 21  ARG A O   1 
ATOM   164  C CB  . ARG A 1 21  ? 9.56600   1.10400   -28.55200 1.000 43.77893  ? 21  ARG A CB  1 
ATOM   165  C CG  . ARG A 1 21  ? 10.43800  -0.11200  -28.59900 1.000 43.74209  ? 21  ARG A CG  1 
ATOM   166  C CD  . ARG A 1 21  ? 11.06200  -0.39600  -27.25200 1.000 44.02370  ? 21  ARG A CD  1 
ATOM   167  N NE  . ARG A 1 21  ? 11.98500  -1.51600  -27.34700 1.000 44.06844  ? 21  ARG A NE  1 
ATOM   168  C CZ  . ARG A 1 21  ? 12.53400  -2.11400  -26.30400 1.000 43.60786  ? 21  ARG A CZ  1 
ATOM   169  N NH1 . ARG A 1 21  ? 12.27700  -1.71200  -25.06600 1.000 44.38427  ? 21  ARG A NH1 1 
ATOM   170  N NH2 . ARG A 1 21  ? 13.35700  -3.14400  -26.50400 1.000 43.68682  ? 21  ARG A NH2 1 
ATOM   171  N N   . PHE A 1 22  ? 8.68700   -0.60800  -31.26700 1.000 34.94103  ? 22  PHE A N   1 
ATOM   172  C CA  . PHE A 1 22  ? 8.09500   -1.81800  -31.84800 1.000 33.04607  ? 22  PHE A CA  1 
ATOM   173  C C   . PHE A 1 22  ? 9.08400   -2.97000  -31.69600 1.000 33.69351  ? 22  PHE A C   1 
ATOM   174  O O   . PHE A 1 22  ? 10.23200  -2.87400  -32.15000 1.000 34.45676  ? 22  PHE A O   1 
ATOM   175  C CB  . PHE A 1 22  ? 7.73200   -1.58500  -33.32600 1.000 31.87751  ? 22  PHE A CB  1 
ATOM   176  C CG  . PHE A 1 22  ? 7.15800   -2.78900  -34.03600 1.000 29.99044  ? 22  PHE A CG  1 
ATOM   177  C CD1 . PHE A 1 22  ? 5.78800   -3.06100  -33.98100 1.000 28.75345  ? 22  PHE A CD1 1 
ATOM   178  C CD2 . PHE A 1 22  ? 7.97300   -3.62900  -34.78800 1.000 29.65356  ? 22  PHE A CD2 1 
ATOM   179  C CE1 . PHE A 1 22  ? 5.23200   -4.15400  -34.65900 1.000 28.12706  ? 22  PHE A CE1 1 
ATOM   180  C CE2 . PHE A 1 22  ? 7.43500   -4.71400  -35.46500 1.000 28.69028  ? 22  PHE A CE2 1 
ATOM   181  C CZ  . PHE A 1 22  ? 6.05500   -4.98300  -35.40200 1.000 28.02968  ? 22  PHE A CZ  1 
ATOM   182  N N   . ILE A 1 23  ? 8.64500   -4.03900  -31.04100 1.000 35.79640  ? 23  ILE A N   1 
ATOM   183  C CA  . ILE A 1 23  ? 9.44500   -5.22700  -30.77700 1.000 35.75955  ? 23  ILE A CA  1 
ATOM   184  C C   . ILE A 1 23  ? 8.69300   -6.41200  -31.36500 1.000 33.34610  ? 23  ILE A C   1 
ATOM   185  O O   . ILE A 1 23  ? 7.48100   -6.54600  -31.15300 1.000 32.06700  ? 23  ILE A O   1 
ATOM   186  C CB  . ILE A 1 23  ? 9.66400   -5.46100  -29.26500 1.000 35.79377  ? 23  ILE A CB  1 
ATOM   187  C CG1 . ILE A 1 23  ? 10.49200  -4.36400  -28.62200 1.000 37.26763  ? 23  ILE A CG1 1 
ATOM   188  C CG2 . ILE A 1 23  ? 10.36400  -6.81700  -28.99900 1.000 34.99893  ? 23  ILE A CG2 1 
ATOM   189  C CD1 . ILE A 1 23  ? 10.44900  -4.48900  -27.12500 1.000 37.77558  ? 23  ILE A CD1 1 
ATOM   190  N N   . ALA A 1 24  ? 9.40900   -7.27200  -32.08800 1.000 26.86375  ? 24  ALA A N   1 
ATOM   191  C CA  . ALA A 1 24  ? 8.81500   -8.46000  -32.68300 1.000 24.83719  ? 24  ALA A CA  1 
ATOM   192  C C   . ALA A 1 24  ? 9.70900   -9.64400  -32.35100 1.000 25.39515  ? 24  ALA A C   1 
ATOM   193  O O   . ALA A 1 24  ? 10.93500  -9.51700  -32.36100 1.000 27.54541  ? 24  ALA A O   1 
ATOM   194  C CB  . ALA A 1 24  ? 8.66800   -8.31800  -34.19600 1.000 24.77139  ? 24  ALA A CB  1 
ATOM   195  N N   . VAL A 1 25  ? 9.10700   -10.78700 -32.02100 1.000 29.36142  ? 25  VAL A N   1 
ATOM   196  C CA  . VAL A 1 25  ? 9.88100   -12.00500 -31.83600 1.000 29.44300  ? 25  VAL A CA  1 
ATOM   197  C C   . VAL A 1 25  ? 9.16700   -13.13300 -32.57600 1.000 28.61659  ? 25  VAL A C   1 
ATOM   198  O O   . VAL A 1 25  ? 7.94800   -13.11000 -32.75800 1.000 27.94546  ? 25  VAL A O   1 
ATOM   199  C CB  . VAL A 1 25  ? 10.12400  -12.33400 -30.33900 1.000 29.67987  ? 25  VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 25  ? 11.03900  -11.26300 -29.69100 1.000 30.99582  ? 25  VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 25  ? 8.83500   -12.43700 -29.56400 1.000 29.02453  ? 25  VAL A CG2 1 
ATOM   202  N N   . GLY A 1 26  ? 9.94700   -14.08300 -33.06300 1.000 30.87739  ? 26  GLY A N   1 
ATOM   203  C CA  . GLY A 1 26  ? 9.41400   -15.25400 -33.73900 1.000 30.59314  ? 26  GLY A CA  1 
ATOM   204  C C   . GLY A 1 26  ? 9.78700   -16.50400 -32.96600 1.000 30.92739  ? 26  GLY A C   1 
ATOM   205  O O   . GLY A 1 26  ? 10.90800  -16.61400 -32.45100 1.000 31.80381  ? 26  GLY A O   1 
ATOM   206  N N   . TYR A 1 27  ? 8.84600   -17.43400 -32.88400 1.000 30.86949  ? 27  TYR A N   1 
ATOM   207  C CA  . TYR A 1 27  ? 9.00600   -18.70500 -32.18600 1.000 31.60905  ? 27  TYR A CA  1 
ATOM   208  C C   . TYR A 1 27  ? 8.63600   -19.84900 -33.11800 1.000 32.77761  ? 27  TYR A C   1 
ATOM   209  O O   . TYR A 1 27  ? 7.67500   -19.74100 -33.87900 1.000 33.39085  ? 27  TYR A O   1 
ATOM   210  C CB  . TYR A 1 27  ? 8.10300   -18.78200 -30.94600 1.000 32.12490  ? 27  TYR A CB  1 
ATOM   211  C CG  . TYR A 1 27  ? 8.64500   -18.07900 -29.72400 1.000 31.75907  ? 27  TYR A CG  1 
ATOM   212  C CD1 . TYR A 1 27  ? 8.54200   -16.70200 -29.57900 1.000 31.16953  ? 27  TYR A CD1 1 
ATOM   213  C CD2 . TYR A 1 27  ? 9.23800   -18.80200 -28.70900 1.000 31.94067  ? 27  TYR A CD2 1 
ATOM   214  C CE1 . TYR A 1 27  ? 9.03700   -16.05800 -28.44800 1.000 31.12478  ? 27  TYR A CE1 1 
ATOM   215  C CE2 . TYR A 1 27  ? 9.72700   -18.18100 -27.57100 1.000 31.59326  ? 27  TYR A CE2 1 
ATOM   216  C CZ  . TYR A 1 27  ? 9.62900   -16.81000 -27.44600 1.000 31.68275  ? 27  TYR A CZ  1 
ATOM   217  O OH  . TYR A 1 27  ? 10.13100  -16.23600 -26.30100 1.000 31.99331  ? 27  TYR A OH  1 
ATOM   218  N N   . VAL A 1 28  ? 9.41300   -20.92600 -33.06700 1.000 28.01125  ? 28  VAL A N   1 
ATOM   219  C CA  . VAL A 1 28  ? 8.97000   -22.24900 -33.50000 1.000 29.41932  ? 28  VAL A CA  1 
ATOM   220  C C   . VAL A 1 28  ? 8.82000   -23.06800 -32.22700 1.000 30.26152  ? 28  VAL A C   1 
ATOM   221  O O   . VAL A 1 28  ? 9.78100   -23.19600 -31.46000 1.000 29.43774  ? 28  VAL A O   1 
ATOM   222  C CB  . VAL A 1 28  ? 9.95400   -22.91500 -34.47600 1.000 29.53512  ? 28  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 28  ? 9.51900   -24.36900 -34.75200 1.000 31.28007  ? 28  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 28  ? 10.02000  -22.13900 -35.79300 1.000 28.88504  ? 28  VAL A CG2 1 
ATOM   225  N N   . ASP A 1 29  ? 7.61000   -23.56500 -31.97700 1.000 33.73299  ? 29  ASP A N   1 
ATOM   226  C CA  . ASP A 1 29  ? 7.28500   -24.23000 -30.71300 1.000 34.79628  ? 29  ASP A CA  1 
ATOM   227  C C   . ASP A 1 29  ? 7.73100   -23.36800 -29.54400 1.000 32.83288  ? 29  ASP A C   1 
ATOM   228  O O   . ASP A 1 29  ? 7.30500   -22.21100 -29.43100 1.000 32.11701  ? 29  ASP A O   1 
ATOM   229  C CB  . ASP A 1 29  ? 7.92500   -25.61200 -30.65400 1.000 34.77259  ? 29  ASP A CB  1 
ATOM   230  C CG  . ASP A 1 29  ? 7.38900   -26.53400 -31.72200 1.000 36.62018  ? 29  ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 29  ? 6.18100   -26.44300 -32.02800 1.000 37.66767  ? 29  ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 29  ? 8.17800   -27.32300 -32.27900 1.000 37.29921  ? 29  ASP A OD2 1 
ATOM   233  N N   . ASP A 1 30  ? 8.62800   -23.88000 -28.70700 1.000 37.29921  ? 30  ASP A N   1 
ATOM   234  C CA  . ASP A 1 30  ? 9.08600   -23.12900 -27.54900 1.000 36.15433  ? 30  ASP A CA  1 
ATOM   235  C C   . ASP A 1 30  ? 10.42600  -22.42000 -27.77600 1.000 35.73850  ? 30  ASP A C   1 
ATOM   236  O O   . ASP A 1 30  ? 11.01400  -21.92300 -26.81600 1.000 35.05157  ? 30  ASP A O   1 
ATOM   237  C CB  . ASP A 1 30  ? 9.18000   -24.05300 -26.32500 1.000 36.74914  ? 30  ASP A CB  1 
ATOM   238  C CG  . ASP A 1 30  ? 7.82400   -24.63500 -25.92600 1.000 37.93086  ? 30  ASP A CG  1 
ATOM   239  O OD1 . ASP A 1 30  ? 6.85600   -23.84600 -25.82800 1.000 38.00719  ? 30  ASP A OD1 1 
ATOM   240  O OD2 . ASP A 1 30  ? 7.72100   -25.86300 -25.72300 1.000 38.42829  ? 30  ASP A OD2 1 
ATOM   241  N N   . THR A 1 31  ? 10.89700  -22.31700 -29.01900 1.000 30.01412  ? 31  THR A N   1 
ATOM   242  C CA  . THR A 1 31  ? 12.25000  -21.85500 -29.30700 1.000 29.60618  ? 31  THR A CA  1 
ATOM   243  C C   . THR A 1 31  ? 12.18200  -20.53400 -30.06500 1.000 29.34562  ? 31  THR A C   1 
ATOM   244  O O   . THR A 1 31  ? 11.65100  -20.48300 -31.17300 1.000 29.36668  ? 31  THR A O   1 
ATOM   245  C CB  . THR A 1 31  ? 13.01600  -22.91300 -30.11400 1.000 30.27731  ? 31  THR A CB  1 
ATOM   246  O OG1 . THR A 1 31  ? 13.20100  -24.07800 -29.30100 1.000 30.87739  ? 31  THR A OG1 1 
ATOM   247  C CG2 . THR A 1 31  ? 14.38800  -22.39300 -30.54100 1.000 30.67736  ? 31  THR A CG2 1 
ATOM   248  N N   . GLN A 1 32  ? 12.69900  -19.46500 -29.46100 1.000 30.80369  ? 32  GLN A N   1 
ATOM   249  C CA  . GLN A 1 32  ? 12.73600  -18.17700 -30.14700 1.000 30.75895  ? 32  GLN A CA  1 
ATOM   250  C C   . GLN A 1 32  ? 13.79000  -18.21800 -31.23900 1.000 31.94857  ? 32  GLN A C   1 
ATOM   251  O O   . GLN A 1 32  ? 14.90900  -18.67500 -31.01000 1.000 33.05396  ? 32  GLN A O   1 
ATOM   252  C CB  . GLN A 1 32  ? 13.04300  -17.03600 -29.17600 1.000 31.05372  ? 32  GLN A CB  1 
ATOM   253  C CG  . GLN A 1 32  ? 12.75800  -15.65500 -29.80100 1.000 30.94582  ? 32  GLN A CG  1 
ATOM   254  C CD  . GLN A 1 32  ? 13.49200  -14.52200 -29.10900 1.000 32.28545  ? 32  GLN A CD  1 
ATOM   255  O OE1 . GLN A 1 32  ? 13.83500  -14.61500 -27.94200 1.000 31.84856  ? 32  GLN A OE1 1 
ATOM   256  N NE2 . GLN A 1 32  ? 13.73700  -13.43400 -29.84400 1.000 33.12766  ? 32  GLN A NE2 1 
ATOM   257  N N   . PHE A 1 33  ? 13.44900  -17.75700 -32.43900 1.000 28.41656  ? 33  PHE A N   1 
ATOM   258  C CA  . PHE A 1 33  ? 14.44200  -17.83100 -33.50100 1.000 30.40365  ? 33  PHE A CA  1 
ATOM   259  C C   . PHE A 1 33  ? 14.77600  -16.51100 -34.19500 1.000 32.09332  ? 33  PHE A C   1 
ATOM   260  O O   . PHE A 1 33  ? 15.81200  -16.45900 -34.86400 1.000 34.58046  ? 33  PHE A O   1 
ATOM   261  C CB  . PHE A 1 33  ? 14.04000  -18.88500 -34.55400 1.000 30.43523  ? 33  PHE A CB  1 
ATOM   262  C CG  . PHE A 1 33  ? 12.86600  -18.51000 -35.40700 1.000 29.32457  ? 33  PHE A CG  1 
ATOM   263  C CD1 . PHE A 1 33  ? 11.56600  -18.65600 -34.93700 1.000 27.50330  ? 33  PHE A CD1 1 
ATOM   264  C CD2 . PHE A 1 33  ? 13.06000  -18.05700 -36.70100 1.000 30.25626  ? 33  PHE A CD2 1 
ATOM   265  C CE1 . PHE A 1 33  ? 10.49800  -18.31800 -35.71800 1.000 27.05851  ? 33  PHE A CE1 1 
ATOM   266  C CE2 . PHE A 1 33  ? 11.98800  -17.72000 -37.49900 1.000 28.99821  ? 33  PHE A CE2 1 
ATOM   267  C CZ  . PHE A 1 33  ? 10.70900  -17.84200 -37.01600 1.000 27.29538  ? 33  PHE A CZ  1 
ATOM   268  N N   . VAL A 1 34  ? 13.97300  -15.45100 -34.05000 1.000 27.72964  ? 34  VAL A N   1 
ATOM   269  C CA  . VAL A 1 34  ? 14.30800  -14.15100 -34.62200 1.000 29.41932  ? 34  VAL A CA  1 
ATOM   270  C C   . VAL A 1 34  ? 13.79600  -13.07200 -33.68100 1.000 28.37972  ? 34  VAL A C   1 
ATOM   271  O O   . VAL A 1 34  ? 12.93300  -13.31400 -32.83900 1.000 26.14261  ? 34  VAL A O   1 
ATOM   272  C CB  . VAL A 1 34  ? 13.72800  -13.90400 -36.04600 1.000 28.76924  ? 34  VAL A CB  1 
ATOM   273  C CG1 . VAL A 1 34  ? 14.37800  -14.79600 -37.10600 1.000 29.43248  ? 34  VAL A CG1 1 
ATOM   274  C CG2 . VAL A 1 34  ? 12.22600  -14.04700 -36.05900 1.000 25.88995  ? 34  VAL A CG2 1 
ATOM   275  N N   . ARG A 1 35  ? 14.32800  -11.86200 -33.84400 1.000 35.80429  ? 35  ARG A N   1 
ATOM   276  C CA  . ARG A 1 35  ? 13.84200  -10.70200 -33.11000 1.000 35.18843  ? 35  ARG A CA  1 
ATOM   277  C C   . ARG A 1 35  ? 14.05200  -9.45700  -33.96000 1.000 35.80956  ? 35  ARG A C   1 
ATOM   278  O O   . ARG A 1 35  ? 14.95000  -9.40700  -34.79900 1.000 36.25961  ? 35  ARG A O   1 
ATOM   279  C CB  . ARG A 1 35  ? 14.55500  -10.52200 -31.76900 1.000 34.90155  ? 35  ARG A CB  1 
ATOM   280  C CG  . ARG A 1 35  ? 16.03900  -10.22200 -31.93300 1.000 36.64124  ? 35  ARG A CG  1 
ATOM   281  C CD  . ARG A 1 35  ? 16.47600  -9.01000  -31.11800 1.000 37.37290  ? 35  ARG A CD  1 
ATOM   282  N NE  . ARG A 1 35  ? 17.92600  -8.84000  -31.14500 1.000 38.00982  ? 35  ARG A NE  1 
ATOM   283  C CZ  . ARG A 1 35  ? 18.74000  -9.04000  -30.11300 1.000 38.62305  ? 35  ARG A CZ  1 
ATOM   284  N NH1 . ARG A 1 35  ? 18.29500  -9.51700  -28.95800 1.000 36.86495  ? 35  ARG A NH1 1 
ATOM   285  N NH2 . ARG A 1 35  ? 20.03100  -8.72300  -30.23000 1.000 39.40999  ? 35  ARG A NH2 1 
ATOM   286  N N   . PHE A 1 36  ? 13.21700  -8.45100  -33.71000 1.000 30.36943  ? 36  PHE A N   1 
ATOM   287  C CA  . PHE A 1 36  ? 13.38400  -7.11100  -34.25100 1.000 30.88265  ? 36  PHE A CA  1 
ATOM   288  C C   . PHE A 1 36  ? 13.05700  -6.10800  -33.15000 1.000 31.23532  ? 36  PHE A C   1 
ATOM   289  O O   . PHE A 1 36  ? 12.07200  -6.27000  -32.42400 1.000 30.31153  ? 36  PHE A O   1 
ATOM   290  C CB  . PHE A 1 36  ? 12.48500  -6.89200  -35.47800 1.000 29.32194  ? 36  PHE A CB  1 
ATOM   291  C CG  . PHE A 1 36  ? 12.51300  -5.48500  -36.02100 1.000 29.46932  ? 36  PHE A CG  1 
ATOM   292  C CD1 . PHE A 1 36  ? 11.68800  -4.49600  -35.49200 1.000 29.31404  ? 36  PHE A CD1 1 
ATOM   293  C CD2 . PHE A 1 36  ? 13.34300  -5.15800  -37.07200 1.000 30.07992  ? 36  PHE A CD2 1 
ATOM   294  C CE1 . PHE A 1 36  ? 11.70900  -3.20200  -36.00500 1.000 29.49827  ? 36  PHE A CE1 1 
ATOM   295  C CE2 . PHE A 1 36  ? 13.35100  -3.85700  -37.60000 1.000 29.94833  ? 36  PHE A CE2 1 
ATOM   296  C CZ  . PHE A 1 36  ? 12.53600  -2.88900  -37.04900 1.000 30.04308  ? 36  PHE A CZ  1 
ATOM   297  N N   . ASP A 1 37  ? 13.87000  -5.06500  -33.03400 1.000 34.41465  ? 37  ASP A N   1 
ATOM   298  C CA  . ASP A 1 37  ? 13.65000  -4.04000  -32.01400 1.000 34.88576  ? 37  ASP A CA  1 
ATOM   299  C C   . ASP A 1 37  ? 13.93800  -2.68000  -32.63600 1.000 35.48847  ? 37  ASP A C   1 
ATOM   300  O O   . ASP A 1 37  ? 15.08600  -2.38900  -32.97700 1.000 35.88851  ? 37  ASP A O   1 
ATOM   301  C CB  . ASP A 1 37  ? 14.53700  -4.28500  -30.78900 1.000 35.07789  ? 37  ASP A CB  1 
ATOM   302  C CG  . ASP A 1 37  ? 14.30700  -3.27200  -29.66100 1.000 35.66217  ? 37  ASP A CG  1 
ATOM   303  O OD1 . ASP A 1 37  ? 13.57600  -2.26000  -29.82900 1.000 36.01484  ? 37  ASP A OD1 1 
ATOM   304  O OD2 . ASP A 1 37  ? 14.87400  -3.50300  -28.56500 1.000 35.96221  ? 37  ASP A OD2 1 
ATOM   305  N N   . SER A 1 38  ? 12.90100  -1.85700  -32.79300 1.000 35.97537  ? 38  SER A N   1 
ATOM   306  C CA  . SER A 1 38  ? 13.05700  -0.56800  -33.45100 1.000 36.13065  ? 38  SER A CA  1 
ATOM   307  C C   . SER A 1 38  ? 13.93200  0.39600   -32.65700 1.000 37.43607  ? 38  SER A C   1 
ATOM   308  O O   . SER A 1 38  ? 14.33200  1.42600   -33.20900 1.000 37.67031  ? 38  SER A O   1 
ATOM   309  C CB  . SER A 1 38  ? 11.69100  0.06500   -33.67900 1.000 35.32002  ? 38  SER A CB  1 
ATOM   310  O OG  . SER A 1 38  ? 11.06300  0.35900   -32.43100 1.000 36.05432  ? 38  SER A OG  1 
ATOM   311  N N   . ASP A 1 39  ? 14.23800  0.08700   -31.38800 1.000 53.63275  ? 39  ASP A N   1 
ATOM   312  C CA  . ASP A 1 39  ? 15.05600  0.97000   -30.56800 1.000 54.54601  ? 39  ASP A CA  1 
ATOM   313  C C   . ASP A 1 39  ? 16.53900  0.81200   -30.83500 1.000 55.31453  ? 39  ASP A C   1 
ATOM   314  O O   . ASP A 1 39  ? 17.29800  1.75800   -30.60900 1.000 56.71469  ? 39  ASP A O   1 
ATOM   315  C CB  . ASP A 1 39  ? 14.80100  0.73400   -29.08500 1.000 54.89079  ? 39  ASP A CB  1 
ATOM   316  C CG  . ASP A 1 39  ? 13.93800  1.80000   -28.48300 1.000 55.32505  ? 39  ASP A CG  1 
ATOM   317  O OD1 . ASP A 1 39  ? 13.21900  2.48100   -29.24600 1.000 55.82248  ? 39  ASP A OD1 1 
ATOM   318  O OD2 . ASP A 1 39  ? 13.97900  1.96000   -27.25100 1.000 56.29359  ? 39  ASP A OD2 1 
ATOM   319  N N   . ALA A 1 40  ? 16.97800  -0.35000  -31.30500 1.000 60.67043  ? 40  ALA A N   1 
ATOM   320  C CA  . ALA A 1 40  ? 18.38000  -0.48700  -31.67300 1.000 61.57580  ? 40  ALA A CA  1 
ATOM   321  C C   . ALA A 1 40  ? 18.78000  0.57100   -32.71100 1.000 61.59160  ? 40  ALA A C   1 
ATOM   322  O O   . ALA A 1 40  ? 17.94400  1.21800   -33.36000 1.000 61.02311  ? 40  ALA A O   1 
ATOM   323  C CB  . ALA A 1 40  ? 18.65000  -1.89100  -32.21400 1.000 61.64423  ? 40  ALA A CB  1 
ATOM   324  N N   . ALA A 1 41  ? 20.08600  0.78500   -32.82400 1.000 81.85192  ? 41  ALA A N   1 
ATOM   325  C CA  . ALA A 1 41  ? 20.61700  1.52500   -33.95500 1.000 82.12037  ? 41  ALA A CA  1 
ATOM   326  C C   . ALA A 1 41  ? 20.70300  0.58700   -35.15100 1.000 81.80191  ? 41  ALA A C   1 
ATOM   327  O O   . ALA A 1 41  ? 21.19400  -0.54300  -35.04000 1.000 80.36753  ? 41  ALA A O   1 
ATOM   328  C CB  . ALA A 1 41  ? 21.98400  2.12500   -33.61900 1.000 83.19155  ? 41  ALA A CB  1 
ATOM   329  N N   . SER A 1 42  ? 20.18900  1.05600   -36.29000 1.000 65.54207  ? 42  SER A N   1 
ATOM   330  C CA  . SER A 1 42  ? 19.99500  0.24200   -37.48600 1.000 64.94989  ? 42  SER A CA  1 
ATOM   331  C C   . SER A 1 42  ? 19.15700  -0.98300  -37.12300 1.000 64.12348  ? 42  SER A C   1 
ATOM   332  O O   . SER A 1 42  ? 19.67700  -2.10500  -37.05800 1.000 63.87082  ? 42  SER A O   1 
ATOM   333  C CB  . SER A 1 42  ? 21.33300  -0.17000  -38.09900 1.000 65.91053  ? 42  SER A CB  1 
ATOM   334  O OG  . SER A 1 42  ? 22.12300  0.97300   -38.35400 1.000 69.82679  ? 42  SER A OG  1 
ATOM   335  N N   . PRO A 1 43  ? 17.87300  -0.79700  -36.82700 1.000 43.54469  ? 43  PRO A N   1 
ATOM   336  C CA  . PRO A 1 43  ? 17.01500  -1.94100  -36.54300 1.000 42.02346  ? 43  PRO A CA  1 
ATOM   337  C C   . PRO A 1 43  ? 17.02700  -2.93700  -37.69100 1.000 41.97345  ? 43  PRO A C   1 
ATOM   338  O O   . PRO A 1 43  ? 17.02000  -2.56100  -38.86200 1.000 41.65499  ? 43  PRO A O   1 
ATOM   339  C CB  . PRO A 1 43  ? 15.63500  -1.30100  -36.37000 1.000 41.38654  ? 43  PRO A CB  1 
ATOM   340  C CG  . PRO A 1 43  ? 15.92200  0.05600   -35.88400 1.000 42.87883  ? 43  PRO A CG  1 
ATOM   341  C CD  . PRO A 1 43  ? 17.14800  0.48000   -36.67100 1.000 43.11306  ? 43  PRO A CD  1 
ATOM   342  N N   . ARG A 1 44  ? 17.05300  -4.21900  -37.34800 1.000 47.01353  ? 44  ARG A N   1 
ATOM   343  C CA  . ARG A 1 44  ? 16.88800  -5.24100  -38.36800 1.000 46.52137  ? 44  ARG A CA  1 
ATOM   344  C C   . ARG A 1 44  ? 16.46600  -6.54100  -37.71200 1.000 46.81351  ? 44  ARG A C   1 
ATOM   345  O O   . ARG A 1 44  ? 16.77200  -6.78800  -36.54500 1.000 46.42399  ? 44  ARG A O   1 
ATOM   346  C CB  . ARG A 1 44  ? 18.16800  -5.45700  -39.16600 1.000 47.44516  ? 44  ARG A CB  1 
ATOM   347  C CG  . ARG A 1 44  ? 19.31800  -5.95600  -38.36200 1.000 48.73479  ? 44  ARG A CG  1 
ATOM   348  C CD  . ARG A 1 44  ? 20.39900  -6.45300  -39.30200 1.000 50.34288  ? 44  ARG A CD  1 
ATOM   349  N NE  . ARG A 1 44  ? 20.46800  -5.62700  -40.50500 1.000 51.56408  ? 44  ARG A NE  1 
ATOM   350  C CZ  . ARG A 1 44  ? 20.36800  -6.08000  -41.75300 1.000 51.87990  ? 44  ARG A CZ  1 
ATOM   351  N NH1 . ARG A 1 44  ? 20.19800  -7.36700  -42.01800 1.000 51.87990  ? 44  ARG A NH1 1 
ATOM   352  N NH2 . ARG A 1 44  ? 20.45600  -5.21700  -42.76400 1.000 51.03770  ? 44  ARG A NH2 1 
ATOM   353  N N   . MET A 1 45  ? 15.75700  -7.36800  -38.48000 1.000 36.18855  ? 45  MET A N   1 
ATOM   354  C CA  . MET A 1 45  ? 15.47400  -8.71700  -38.02000 1.000 35.74902  ? 45  MET A CA  1 
ATOM   355  C C   . MET A 1 45  ? 16.79900  -9.44100  -37.83900 1.000 37.39922  ? 45  MET A C   1 
ATOM   356  O O   . MET A 1 45  ? 17.68100  -9.34900  -38.70000 1.000 37.67820  ? 45  MET A O   1 
ATOM   357  C CB  . MET A 1 45  ? 14.59600  -9.45500  -39.02300 1.000 34.98841  ? 45  MET A CB  1 
ATOM   358  C CG  . MET A 1 45  ? 14.00800  -10.76800 -38.44700 1.000 34.24884  ? 45  MET A CG  1 
ATOM   359  S SD  . MET A 1 45  ? 12.71300  -10.42200 -37.23300 1.000 33.31715  ? 45  MET A SD  1 
ATOM   360  C CE  . MET A 1 45  ? 11.24700  -10.80200 -38.21100 1.000 31.39061  ? 45  MET A CE  1 
ATOM   361  N N   . ALA A 1 46  ? 16.96700  -10.11000 -36.69800 1.000 31.81960  ? 46  ALA A N   1 
ATOM   362  C CA  . ALA A 1 46  ? 18.25500  -10.71200 -36.37600 1.000 32.95658  ? 46  ALA A CA  1 
ATOM   363  C C   . ALA A 1 46  ? 18.04300  -12.13100 -35.87800 1.000 32.92763  ? 46  ALA A C   1 
ATOM   364  O O   . ALA A 1 46  ? 16.99300  -12.43200 -35.29800 1.000 32.03542  ? 46  ALA A O   1 
ATOM   365  C CB  . ALA A 1 46  ? 19.01600  -9.89900  -35.31500 1.000 33.04870  ? 46  ALA A CB  1 
ATOM   366  N N   . PRO A 1 47  ? 19.00500  -13.02700 -36.10700 1.000 33.48296  ? 47  PRO A N   1 
ATOM   367  C CA  . PRO A 1 47  ? 18.82200  -14.42100 -35.68200 1.000 33.69878  ? 47  PRO A CA  1 
ATOM   368  C C   . PRO A 1 47  ? 18.90400  -14.55200 -34.16500 1.000 33.10923  ? 47  PRO A C   1 
ATOM   369  O O   . PRO A 1 47  ? 19.69600  -13.87400 -33.50900 1.000 32.95658  ? 47  PRO A O   1 
ATOM   370  C CB  . PRO A 1 47  ? 19.98100  -15.15300 -36.37200 1.000 34.70679  ? 47  PRO A CB  1 
ATOM   371  C CG  . PRO A 1 47  ? 21.00900  -14.13300 -36.57800 1.000 35.51215  ? 47  PRO A CG  1 
ATOM   372  C CD  . PRO A 1 47  ? 20.28700  -12.82700 -36.80900 1.000 34.34622  ? 47  PRO A CD  1 
ATOM   373  N N   . ARG A 1 48  ? 18.07900  -15.43400 -33.60800 1.000 41.95240  ? 48  ARG A N   1 
ATOM   374  C CA  . ARG A 1 48  ? 18.14100  -15.72800 -32.18000 1.000 40.64171  ? 48  ARG A CA  1 
ATOM   375  C C   . ARG A 1 48  ? 18.29800  -17.21000 -31.85900 1.000 40.71014  ? 48  ARG A C   1 
ATOM   376  O O   . ARG A 1 48  ? 18.35600  -17.56600 -30.67900 1.000 39.22312  ? 48  ARG A O   1 
ATOM   377  C CB  . ARG A 1 48  ? 16.90700  -15.16200 -31.46900 1.000 39.16785  ? 48  ARG A CB  1 
ATOM   378  C CG  . ARG A 1 48  ? 16.91600  -13.63000 -31.45100 1.000 39.70476  ? 48  ARG A CG  1 
ATOM   379  C CD  . ARG A 1 48  ? 18.17300  -13.07300 -30.76200 1.000 40.67330  ? 48  ARG A CD  1 
ATOM   380  N NE  . ARG A 1 48  ? 17.92700  -12.81400 -29.34800 1.000 39.49947  ? 48  ARG A NE  1 
ATOM   381  C CZ  . ARG A 1 48  ? 18.86100  -12.57700 -28.43700 1.000 40.10218  ? 48  ARG A CZ  1 
ATOM   382  N NH1 . ARG A 1 48  ? 20.14800  -12.55400 -28.74200 1.000 40.97597  ? 48  ARG A NH1 1 
ATOM   383  N NH2 . ARG A 1 48  ? 18.49500  -12.35500 -27.17700 1.000 39.58896  ? 48  ARG A NH2 1 
ATOM   384  N N   . ALA A 1 49  ? 18.39300  -18.06900 -32.87200 1.000 33.69088  ? 49  ALA A N   1 
ATOM   385  C CA  . ALA A 1 49  ? 18.68100  -19.48900 -32.75900 1.000 33.55139  ? 49  ALA A CA  1 
ATOM   386  C C   . ALA A 1 49  ? 19.68400  -19.84100 -33.84200 1.000 35.49899  ? 49  ALA A C   1 
ATOM   387  O O   . ALA A 1 49  ? 19.58100  -19.32800 -34.95700 1.000 36.55175  ? 49  ALA A O   1 
ATOM   388  C CB  . ALA A 1 49  ? 17.42000  -20.35500 -32.92100 1.000 32.35388  ? 49  ALA A CB  1 
ATOM   389  N N   . PRO A 1 50  ? 20.65600  -20.70300 -33.55200 1.000 34.45676  ? 50  PRO A N   1 
ATOM   390  C CA  . PRO A 1 50  ? 21.70400  -20.96200 -34.54500 1.000 35.51478  ? 50  PRO A CA  1 
ATOM   391  C C   . PRO A 1 50  ? 21.18800  -21.51100 -35.85800 1.000 36.56491  ? 50  PRO A C   1 
ATOM   392  O O   . PRO A 1 50  ? 21.79100  -21.23000 -36.90200 1.000 37.30710  ? 50  PRO A O   1 
ATOM   393  C CB  . PRO A 1 50  ? 22.61700  -21.96200 -33.82600 1.000 36.03327  ? 50  PRO A CB  1 
ATOM   394  C CG  . PRO A 1 50  ? 22.47500  -21.61300 -32.38000 1.000 34.68311  ? 50  PRO A CG  1 
ATOM   395  C CD  . PRO A 1 50  ? 21.00300  -21.25400 -32.22900 1.000 33.46980  ? 50  PRO A CD  1 
ATOM   396  N N   . TRP A 1 51  ? 20.08300  -22.26300 -35.85900 1.000 36.99654  ? 51  TRP A N   1 
ATOM   397  C CA  . TRP A 1 51  ? 19.68500  -22.91900 -37.09900 1.000 37.39659  ? 51  TRP A CA  1 
ATOM   398  C C   . TRP A 1 51  ? 19.06800  -21.96700 -38.11500 1.000 36.90969  ? 51  TRP A C   1 
ATOM   399  O O   . TRP A 1 51  ? 18.86200  -22.37000 -39.26300 1.000 37.19393  ? 51  TRP A O   1 
ATOM   400  C CB  . TRP A 1 51  ? 18.72100  -24.08500 -36.82300 1.000 36.40436  ? 51  TRP A CB  1 
ATOM   401  C CG  . TRP A 1 51  ? 17.61400  -23.76900 -35.88800 1.000 34.70416  ? 51  TRP A CG  1 
ATOM   402  C CD1 . TRP A 1 51  ? 17.55500  -24.07900 -34.56600 1.000 33.18556  ? 51  TRP A CD1 1 
ATOM   403  C CD2 . TRP A 1 51  ? 16.38600  -23.10400 -36.20300 1.000 33.14082  ? 51  TRP A CD2 1 
ATOM   404  N NE1 . TRP A 1 51  ? 16.37100  -23.63900 -34.03000 1.000 31.15637  ? 51  TRP A NE1 1 
ATOM   405  C CE2 . TRP A 1 51  ? 15.63900  -23.02700 -35.01100 1.000 31.05899  ? 51  TRP A CE2 1 
ATOM   406  C CE3 . TRP A 1 51  ? 15.86300  -22.53600 -37.36700 1.000 32.80920  ? 51  TRP A CE3 1 
ATOM   407  C CZ2 . TRP A 1 51  ? 14.38100  -22.42700 -34.95200 1.000 29.25877  ? 51  TRP A CZ2 1 
ATOM   408  C CZ3 . TRP A 1 51  ? 14.61000  -21.95100 -37.31300 1.000 30.89055  ? 51  TRP A CZ3 1 
ATOM   409  C CH2 . TRP A 1 51  ? 13.87600  -21.91200 -36.11400 1.000 29.14560  ? 51  TRP A CH2 1 
ATOM   410  N N   . ILE A 1 52  ? 18.76500  -20.72200 -37.74800 1.000 36.50701  ? 52  ILE A N   1 
ATOM   411  C CA  . ILE A 1 52  ? 18.31500  -19.76500 -38.75700 1.000 36.06222  ? 52  ILE A CA  1 
ATOM   412  C C   . ILE A 1 52  ? 19.47800  -18.95800 -39.34800 1.000 36.98865  ? 52  ILE A C   1 
ATOM   413  O O   . ILE A 1 52  ? 19.31000  -18.31500 -40.39900 1.000 36.89127  ? 52  ILE A O   1 
ATOM   414  C CB  . ILE A 1 52  ? 17.22300  -18.84700 -38.15900 1.000 35.30686  ? 52  ILE A CB  1 
ATOM   415  C CG1 . ILE A 1 52  ? 16.46200  -18.09100 -39.25900 1.000 34.41728  ? 52  ILE A CG1 1 
ATOM   416  C CG2 . ILE A 1 52  ? 17.81500  -17.85300 -37.17500 1.000 35.42530  ? 52  ILE A CG2 1 
ATOM   417  C CD1 . ILE A 1 52  ? 15.60500  -18.96600 -40.08300 1.000 33.43296  ? 52  ILE A CD1 1 
ATOM   418  N N   . GLU A 1 53  ? 20.67300  -19.02500 -38.75200 1.000 42.03136  ? 53  GLU A N   1 
ATOM   419  C CA  . GLU A 1 53  ? 21.73200  -18.08600 -39.10500 1.000 42.57879  ? 53  GLU A CA  1 
ATOM   420  C C   . GLU A 1 53  ? 22.24700  -18.26800 -40.52700 1.000 43.65787  ? 53  GLU A C   1 
ATOM   421  O O   . GLU A 1 53  ? 22.79000  -17.31300 -41.09100 1.000 43.13675  ? 53  GLU A O   1 
ATOM   422  C CB  . GLU A 1 53  ? 22.89700  -18.19600 -38.11200 1.000 42.98410  ? 53  GLU A CB  1 
ATOM   423  C CG  . GLU A 1 53  ? 22.46800  -17.87200 -36.70300 1.000 42.04451  ? 53  GLU A CG  1 
ATOM   424  C CD  . GLU A 1 53  ? 23.61000  -17.81200 -35.71900 1.000 43.12359  ? 53  GLU A CD  1 
ATOM   425  O OE1 . GLU A 1 53  ? 24.74800  -18.10700 -36.10100 1.000 44.29215  ? 53  GLU A OE1 1 
ATOM   426  O OE2 . GLU A 1 53  ? 23.36400  -17.46400 -34.54400 1.000 42.33666  ? 53  GLU A OE2 1 
ATOM   427  N N   . GLN A 1 54  ? 22.09300  -19.45200 -41.12600 1.000 43.99738  ? 54  GLN A N   1 
ATOM   428  C CA  . GLN A 1 54  ? 22.58000  -19.66600 -42.48000 1.000 44.42375  ? 54  GLN A CA  1 
ATOM   429  C C   . GLN A 1 54  ? 21.49800  -19.45500 -43.54000 1.000 43.87105  ? 54  GLN A C   1 
ATOM   430  O O   . GLN A 1 54  ? 21.67500  -19.89100 -44.67900 1.000 44.26320  ? 54  GLN A O   1 
ATOM   431  C CB  . GLN A 1 54  ? 23.20700  -21.05700 -42.61500 1.000 45.36070  ? 54  GLN A CB  1 
ATOM   432  C CG  . GLN A 1 54  ? 24.37700  -21.29600 -41.67500 1.000 46.09237  ? 54  GLN A CG  1 
ATOM   433  C CD  . GLN A 1 54  ? 25.52800  -20.32200 -41.88200 1.000 47.05301  ? 54  GLN A CD  1 
ATOM   434  O OE1 . GLN A 1 54  ? 25.77900  -19.85500 -42.99400 1.000 46.89510  ? 54  GLN A OE1 1 
ATOM   435  N NE2 . GLN A 1 54  ? 26.25800  -20.04400 -40.81200 1.000 46.79772  ? 54  GLN A NE2 1 
ATOM   436  N N   . GLU A 1 55  ? 20.38200  -18.80800 -43.19500 1.000 48.69531  ? 55  GLU A N   1 
ATOM   437  C CA  . GLU A 1 55  ? 19.53700  -18.22300 -44.22600 1.000 47.96891  ? 55  GLU A CA  1 
ATOM   438  C C   . GLU A 1 55  ? 20.27700  -17.07200 -44.88300 1.000 48.08471  ? 55  GLU A C   1 
ATOM   439  O O   . GLU A 1 55  ? 20.98100  -16.30400 -44.22100 1.000 48.36633  ? 55  GLU A O   1 
ATOM   440  C CB  . GLU A 1 55  ? 18.21700  -17.69500 -43.66000 1.000 46.84772  ? 55  GLU A CB  1 
ATOM   441  C CG  . GLU A 1 55  ? 17.32600  -18.71000 -43.03400 1.000 46.83719  ? 55  GLU A CG  1 
ATOM   442  C CD  . GLU A 1 55  ? 16.76100  -19.74200 -43.98900 1.000 46.43451  ? 55  GLU A CD  1 
ATOM   443  O OE1 . GLU A 1 55  ? 16.64500  -19.47800 -45.21800 1.000 45.18700  ? 55  GLU A OE1 1 
ATOM   444  O OE2 . GLU A 1 55  ? 16.40700  -20.82400 -43.48100 1.000 45.46071  ? 55  GLU A OE2 1 
ATOM   445  N N   . GLY A 1 56  ? 20.07600  -16.92700 -46.18400 1.000 50.97190  ? 56  GLY A N   1 
ATOM   446  C CA  . GLY A 1 56  ? 20.83100  -15.97900 -46.95400 1.000 50.52974  ? 56  GLY A CA  1 
ATOM   447  C C   . GLY A 1 56  ? 20.39300  -14.54800 -46.72300 1.000 49.92178  ? 56  GLY A C   1 
ATOM   448  O O   . GLY A 1 56  ? 19.43600  -14.27000 -45.98700 1.000 48.96377  ? 56  GLY A O   1 
ATOM   449  N N   . PRO A 1 57  ? 21.11200  -13.61500 -47.35700 1.000 47.94785  ? 57  PRO A N   1 
ATOM   450  C CA  . PRO A 1 57  ? 20.76800  -12.19100 -47.21300 1.000 47.22145  ? 57  PRO A CA  1 
ATOM   451  C C   . PRO A 1 57  ? 19.41300  -11.82700 -47.78500 1.000 47.56360  ? 57  PRO A C   1 
ATOM   452  O O   . PRO A 1 57  ? 18.82100  -10.84000 -47.33500 1.000 46.41346  ? 57  PRO A O   1 
ATOM   453  C CB  . PRO A 1 57  ? 21.90600  -11.47400 -47.95700 1.000 47.92417  ? 57  PRO A CB  1 
ATOM   454  C CG  . PRO A 1 57  ? 22.53600  -12.51700 -48.81500 1.000 49.36645  ? 57  PRO A CG  1 
ATOM   455  C CD  . PRO A 1 57  ? 22.38900  -13.79900 -48.06500 1.000 49.62700  ? 57  PRO A CD  1 
ATOM   456  N N   . GLU A 1 58  ? 18.88800  -12.58400 -48.75100 1.000 52.67737  ? 58  GLU A N   1 
ATOM   457  C CA  . GLU A 1 58  ? 17.54600  -12.27600 -49.23300 1.000 52.97214  ? 58  GLU A CA  1 
ATOM   458  C C   . GLU A 1 58  ? 16.50900  -12.50100 -48.13400 1.000 51.38248  ? 58  GLU A C   1 
ATOM   459  O O   . GLU A 1 58  ? 15.50000  -11.79000 -48.07500 1.000 50.31393  ? 58  GLU A O   1 
ATOM   460  C CB  . GLU A 1 58  ? 17.21900  -13.09600 -50.48700 1.000 55.25926  ? 58  GLU A CB  1 
ATOM   461  C CG  . GLU A 1 58  ? 16.91100  -14.57100 -50.24500 1.000 56.50414  ? 58  GLU A CG  1 
ATOM   462  C CD  . GLU A 1 58  ? 18.12300  -15.37200 -49.77100 1.000 57.27792  ? 58  GLU A CD  1 
ATOM   463  O OE1 . GLU A 1 58  ? 19.23700  -15.14600 -50.32300 1.000 57.61480  ? 58  GLU A OE1 1 
ATOM   464  O OE2 . GLU A 1 58  ? 17.95600  -16.21200 -48.83700 1.000 56.56731  ? 58  GLU A OE2 1 
ATOM   465  N N   . TYR A 1 59  ? 16.76400  -13.45400 -47.23500 1.000 39.89952  ? 59  TYR A N   1 
ATOM   466  C CA  . TYR A 1 59  ? 15.85700  -13.67800 -46.11400 1.000 38.70727  ? 59  TYR A CA  1 
ATOM   467  C C   . TYR A 1 59  ? 15.81600  -12.46500 -45.18600 1.000 36.88337  ? 59  TYR A C   1 
ATOM   468  O O   . TYR A 1 59  ? 14.73700  -11.93100 -44.89800 1.000 35.84640  ? 59  TYR A O   1 
ATOM   469  C CB  . TYR A 1 59  ? 16.27600  -14.93900 -45.35400 1.000 40.07059  ? 59  TYR A CB  1 
ATOM   470  C CG  . TYR A 1 59  ? 15.38100  -15.26400 -44.19000 1.000 38.55199  ? 59  TYR A CG  1 
ATOM   471  C CD1 . TYR A 1 59  ? 14.19100  -15.96500 -44.38300 1.000 38.97836  ? 59  TYR A CD1 1 
ATOM   472  C CD2 . TYR A 1 59  ? 15.71500  -14.87700 -42.90200 1.000 35.69112  ? 59  TYR A CD2 1 
ATOM   473  C CE1 . TYR A 1 59  ? 13.36600  -16.26700 -43.33700 1.000 37.25183  ? 59  TYR A CE1 1 
ATOM   474  C CE2 . TYR A 1 59  ? 14.87500  -15.17200 -41.82700 1.000 34.35675  ? 59  TYR A CE2 1 
ATOM   475  C CZ  . TYR A 1 59  ? 13.70700  -15.87200 -42.05400 1.000 35.47531  ? 59  TYR A CZ  1 
ATOM   476  O OH  . TYR A 1 59  ? 12.86100  -16.18000 -41.01900 1.000 34.64626  ? 59  TYR A OH  1 
ATOM   477  N N   . TRP A 1 60  ? 16.98500  -12.00900 -44.71600 1.000 39.44157  ? 60  TRP A N   1 
ATOM   478  C CA  . TRP A 1 60  ? 17.03700  -10.96900 -43.68500 1.000 37.70978  ? 60  TRP A CA  1 
ATOM   479  C C   . TRP A 1 60  ? 16.57600  -9.61100  -44.21100 1.000 37.94402  ? 60  TRP A C   1 
ATOM   480  O O   . TRP A 1 60  ? 15.93400  -8.84500  -43.47700 1.000 36.46227  ? 60  TRP A O   1 
ATOM   481  C CB  . TRP A 1 60  ? 18.45300  -10.87500 -43.11700 1.000 37.55187  ? 60  TRP A CB  1 
ATOM   482  C CG  . TRP A 1 60  ? 18.83300  -12.16000 -42.51900 1.000 37.54661  ? 60  TRP A CG  1 
ATOM   483  C CD1 . TRP A 1 60  ? 19.72300  -13.06900 -43.01500 1.000 38.67306  ? 60  TRP A CD1 1 
ATOM   484  C CD2 . TRP A 1 60  ? 18.27300  -12.73900 -41.33400 1.000 36.54649  ? 60  TRP A CD2 1 
ATOM   485  N NE1 . TRP A 1 60  ? 19.76400  -14.17400 -42.19400 1.000 38.42040  ? 60  TRP A NE1 1 
ATOM   486  C CE2 . TRP A 1 60  ? 18.88400  -13.99600 -41.15600 1.000 37.61240  ? 60  TRP A CE2 1 
ATOM   487  C CE3 . TRP A 1 60  ? 17.33300  -12.30300 -40.39100 1.000 35.23844  ? 60  TRP A CE3 1 
ATOM   488  C CZ2 . TRP A 1 60  ? 18.58200  -14.83100 -40.07000 1.000 37.83612  ? 60  TRP A CZ2 1 
ATOM   489  C CZ3 . TRP A 1 60  ? 17.02400  -13.14000 -39.31600 1.000 35.33055  ? 60  TRP A CZ3 1 
ATOM   490  C CH2 . TRP A 1 60  ? 17.65700  -14.38100 -39.16300 1.000 37.25183  ? 60  TRP A CH2 1 
ATOM   491  N N   . ASP A 1 61  ? 16.90300  -9.29600  -45.46900 1.000 45.46598  ? 61  ASP A N   1 
ATOM   492  C CA  . ASP A 1 61  ? 16.45400  -8.04400  -46.06500 1.000 45.84497  ? 61  ASP A CA  1 
ATOM   493  C C   . ASP A 1 61  ? 14.93100  -7.99600  -46.17100 1.000 45.17647  ? 61  ASP A C   1 
ATOM   494  O O   . ASP A 1 61  ? 14.31100  -6.97700  -45.85200 1.000 44.64219  ? 61  ASP A O   1 
ATOM   495  C CB  . ASP A 1 61  ? 17.10900  -7.86100  -47.44100 1.000 48.04787  ? 61  ASP A CB  1 
ATOM   496  C CG  . ASP A 1 61  ? 18.64800  -7.68800  -47.36400 1.000 49.98757  ? 61  ASP A CG  1 
ATOM   497  O OD1 . ASP A 1 61  ? 19.22800  -7.76900  -46.24900 1.000 49.04009  ? 61  ASP A OD1 1 
ATOM   498  O OD2 . ASP A 1 61  ? 19.28000  -7.47000  -48.43500 1.000 51.50881  ? 61  ASP A OD2 1 
ATOM   499  N N   . GLY A 1 62  ? 14.31500  -9.08900  -46.62400 1.000 41.40496  ? 62  GLY A N   1 
ATOM   500  C CA  . GLY A 1 62  ? 12.86100  -9.16800  -46.64900 1.000 40.46275  ? 62  GLY A CA  1 
ATOM   501  C C   . GLY A 1 62  ? 12.22800  -9.10400  -45.26700 1.000 38.09667  ? 62  GLY A C   1 
ATOM   502  O O   . GLY A 1 62  ? 11.19700  -8.46100  -45.08300 1.000 37.29658  ? 62  GLY A O   1 
ATOM   503  N N   . GLU A 1 63  ? 12.82000  -9.77800  -44.28100 1.000 35.59111  ? 63  GLU A N   1 
ATOM   504  C CA  . GLU A 1 63  ? 12.27700  -9.70400  -42.92500 1.000 34.18305  ? 63  GLU A CA  1 
ATOM   505  C C   . GLU A 1 63  ? 12.43900  -8.30100  -42.34200 1.000 34.08830  ? 63  GLU A C   1 
ATOM   506  O O   . GLU A 1 63  ? 11.50200  -7.75100  -41.75500 1.000 32.67760  ? 63  GLU A O   1 
ATOM   507  C CB  . GLU A 1 63  ? 12.95800  -10.73400 -42.02200 1.000 33.94881  ? 63  GLU A CB  1 
ATOM   508  C CG  . GLU A 1 63  ? 12.55400  -12.15700 -42.32100 1.000 34.61731  ? 63  GLU A CG  1 
ATOM   509  C CD  . GLU A 1 63  ? 11.06800  -12.30400 -42.54400 1.000 33.86459  ? 63  GLU A CD  1 
ATOM   510  O OE1 . GLU A 1 63  ? 10.32500  -12.33600 -41.54400 1.000 32.23544  ? 63  GLU A OE1 1 
ATOM   511  O OE2 . GLU A 1 63  ? 10.64200  -12.39200 -43.71000 1.000 34.51993  ? 63  GLU A OE2 1 
ATOM   512  N N   . THR A 1 64  ? 13.62100  -7.70200  -42.50700 1.000 34.25411  ? 64  THR A N   1 
ATOM   513  C CA  . THR A 1 64  ? 13.84200  -6.37100  -41.95800 1.000 33.72773  ? 64  THR A CA  1 
ATOM   514  C C   . THR A 1 64  ? 12.88800  -5.35100  -42.58000 1.000 34.11462  ? 64  THR A C   1 
ATOM   515  O O   . THR A 1 64  ? 12.27700  -4.55000  -41.85600 1.000 33.43559  ? 64  THR A O   1 
ATOM   516  C CB  . THR A 1 64  ? 15.31200  -5.98900  -42.13000 1.000 35.09368  ? 64  THR A CB  1 
ATOM   517  O OG1 . THR A 1 64  ? 16.09400  -6.82900  -41.26700 1.000 34.20673  ? 64  THR A OG1 1 
ATOM   518  C CG2 . THR A 1 64  ? 15.57400  -4.49700  -41.75000 1.000 35.97010  ? 64  THR A CG2 1 
ATOM   519  N N   . ARG A 1 65  ? 12.70600  -5.39800  -43.90800 1.000 43.74209  ? 65  ARG A N   1 
ATOM   520  C CA  . ARG A 1 65  ? 11.75400  -4.50400  -44.57100 1.000 44.19740  ? 65  ARG A CA  1 
ATOM   521  C C   . ARG A 1 65  ? 10.34000  -4.66800  -44.01300 1.000 42.66301  ? 65  ARG A C   1 
ATOM   522  O O   . ARG A 1 65  ? 9.65100   -3.67800  -43.73600 1.000 42.67091  ? 65  ARG A O   1 
ATOM   523  C CB  . ARG A 1 65  ? 11.76700  -4.75300  -46.07900 1.000 46.03710  ? 65  ARG A CB  1 
ATOM   524  C CG  . ARG A 1 65  ? 12.41800  -3.62600  -46.85700 1.000 48.47950  ? 65  ARG A CG  1 
ATOM   525  C CD  . ARG A 1 65  ? 12.53700  -3.89500  -48.36500 1.000 49.35065  ? 65  ARG A CD  1 
ATOM   526  N NE  . ARG A 1 65  ? 13.90000  -4.23100  -48.77800 1.000 50.57712  ? 65  ARG A NE  1 
ATOM   527  C CZ  . ARG A 1 65  ? 14.93100  -3.39700  -48.72200 1.000 51.71936  ? 65  ARG A CZ  1 
ATOM   528  N NH1 . ARG A 1 65  ? 14.80800  -2.17700  -48.21500 1.000 51.46670  ? 65  ARG A NH1 1 
ATOM   529  N NH2 . ARG A 1 65  ? 16.11700  -3.79000  -49.19700 1.000 52.24047  ? 65  ARG A NH2 1 
ATOM   530  N N   . ASN A 1 66  ? 9.88500   -5.91800  -43.86500 1.000 35.05420  ? 66  ASN A N   1 
ATOM   531  C CA  A ASN A 1 66  ? 8.56800   -6.15400  -43.29600 0.560 33.78826  ? 66  ASN A CA  1 
ATOM   532  C CA  B ASN A 1 66  ? 8.57700   -6.19100  -43.27000 0.440 33.75931  ? 66  ASN A CA  1 
ATOM   533  C C   . ASN A 1 66  ? 8.45400   -5.57200  -41.88400 1.000 32.63812  ? 66  ASN A C   1 
ATOM   534  O O   . ASN A 1 66  ? 7.44500   -4.94000  -41.55200 1.000 32.15912  ? 66  ASN A O   1 
ATOM   535  C CB  A ASN A 1 66  ? 8.27700   -7.65600  -43.29700 0.560 33.35400  ? 66  ASN A CB  1 
ATOM   536  C CB  B ASN A 1 66  ? 8.35100   -7.70000  -43.14900 0.440 33.25399  ? 66  ASN A CB  1 
ATOM   537  C CG  A ASN A 1 66  ? 6.82500   -7.96600  -43.07800 0.560 32.31177  ? 66  ASN A CG  1 
ATOM   538  C CG  B ASN A 1 66  ? 7.93200   -8.34000  -44.43200 0.440 34.70153  ? 66  ASN A CG  1 
ATOM   539  O OD1 A ASN A 1 66  ? 5.95300   -7.21000  -43.49300 0.560 33.17766  ? 66  ASN A OD1 1 
ATOM   540  O OD1 B ASN A 1 66  ? 7.77100   -7.67700  -45.45300 0.440 35.96747  ? 66  ASN A OD1 1 
ATOM   541  N ND2 A ASN A 1 66  ? 6.55200   -9.08400  -42.44400 0.560 31.91698  ? 66  ASN A ND2 1 
ATOM   542  N ND2 B ASN A 1 66  ? 7.74700   -9.65800  -44.39000 0.440 34.87260  ? 66  ASN A ND2 1 
ATOM   543  N N   . MET A 1 67  ? 9.46100   -5.77700  -41.03700 1.000 35.21212  ? 67  MET A N   1 
ATOM   544  C CA  . MET A 1 67  ? 9.36200   -5.26200  -39.66900 1.000 34.44624  ? 67  MET A CA  1 
ATOM   545  C C   . MET A 1 67  ? 9.35600   -3.73700  -39.64200 1.000 35.36477  ? 67  MET A C   1 
ATOM   546  O O   . MET A 1 67  ? 8.57600   -3.13000  -38.89800 1.000 34.38044  ? 67  MET A O   1 
ATOM   547  C CB  . MET A 1 67  ? 10.49400  -5.80800  -38.80800 1.000 33.56718  ? 67  MET A CB  1 
ATOM   548  C CG  . MET A 1 67  ? 10.42100  -7.28300  -38.52700 1.000 32.68550  ? 67  MET A CG  1 
ATOM   549  S SD  . MET A 1 67  ? 8.92500   -7.76600  -37.63400 1.000 31.16426  ? 67  MET A SD  1 
ATOM   550  C CE  . MET A 1 67  ? 7.82500   -8.19700  -38.95900 1.000 31.11689  ? 67  MET A CE  1 
ATOM   551  N N   . LYS A 1 68  ? 10.20400  -3.09700  -40.45800 1.000 39.11785  ? 68  LYS A N   1 
ATOM   552  C CA  . LYS A 1 68  ? 10.16800  -1.63800  -40.53100 1.000 39.94689  ? 68  LYS A CA  1 
ATOM   553  C C   . LYS A 1 68  ? 8.79600   -1.14700  -40.95500 1.000 39.74424  ? 68  LYS A C   1 
ATOM   554  O O   . LYS A 1 68  ? 8.28100   -0.17800  -40.39000 1.000 39.91531  ? 68  LYS A O   1 
ATOM   555  C CB  . LYS A 1 68  ? 11.23500  -1.11200  -41.49300 1.000 41.35759  ? 68  LYS A CB  1 
ATOM   556  C CG  . LYS A 1 68  ? 12.61600  -1.08900  -40.88400 1.000 42.21032  ? 68  LYS A CG  1 
ATOM   557  C CD  . LYS A 1 68  ? 13.53200  -0.14100  -41.63000 1.000 44.31321  ? 68  LYS A CD  1 
ATOM   558  C CE  . LYS A 1 68  ? 14.98500  -0.31400  -41.18500 1.000 44.95539  ? 68  LYS A CE  1 
ATOM   559  N NZ  . LYS A 1 68  ? 15.42000  0.61700   -40.11000 1.000 45.21332  ? 68  LYS A NZ  1 
ATOM   560  N N   . ALA A 1 69  ? 8.17400   -1.82300  -41.92900 1.000 36.83600  ? 69  ALA A N   1 
ATOM   561  C CA  . ALA A 1 69  ? 6.82300   -1.45600  -42.34600 1.000 36.87284  ? 69  ALA A CA  1 
ATOM   562  C C   . ALA A 1 69  ? 5.81400   -1.61600  -41.20400 1.000 35.34108  ? 69  ALA A C   1 
ATOM   563  O O   . ALA A 1 69  ? 4.99500   -0.72000  -40.96500 1.000 35.35950  ? 69  ALA A O   1 
ATOM   564  C CB  . ALA A 1 69  ? 6.39800   -2.28600  -43.55900 1.000 37.19130  ? 69  ALA A CB  1 
ATOM   565  N N   . SER A 1 70  ? 5.88100   -2.73000  -40.46300 1.000 36.88600  ? 70  SER A N   1 
ATOM   566  C CA  . SER A 1 70  ? 4.92400   -2.95300  -39.37800 1.000 35.52794  ? 70  SER A CA  1 
ATOM   567  C C   . SER A 1 70  ? 5.13800   -1.98800  -38.22700 1.000 36.17802  ? 70  SER A C   1 
ATOM   568  O O   . SER A 1 70  ? 4.17100   -1.58200  -37.57700 1.000 36.17276  ? 70  SER A O   1 
ATOM   569  C CB  . SER A 1 70  ? 4.99900   -4.40200  -38.86500 1.000 34.09356  ? 70  SER A CB  1 
ATOM   570  O OG  . SER A 1 70  ? 4.71000   -5.31000  -39.91100 1.000 34.29622  ? 70  SER A OG  1 
ATOM   571  N N   . ALA A 1 71  ? 6.39200   -1.63400  -37.93900 1.000 30.20099  ? 71  ALA A N   1 
ATOM   572  C CA  . ALA A 1 71  ? 6.65900   -0.61000  -36.93700 1.000 30.24836  ? 71  ALA A CA  1 
ATOM   573  C C   . ALA A 1 71  ? 5.98200   0.70800   -37.30400 1.000 31.36165  ? 71  ALA A C   1 
ATOM   574  O O   . ALA A 1 71  ? 5.40000   1.37700   -36.44000 1.000 31.36429  ? 71  ALA A O   1 
ATOM   575  C CB  . ALA A 1 71  ? 8.17100   -0.41100  -36.77100 1.000 30.78527  ? 71  ALA A CB  1 
ATOM   576  N N   . GLN A 1 72  ? 6.05500   1.10200   -38.58000 1.000 37.35974  ? 72  GLN A N   1 
ATOM   577  C CA  . GLN A 1 72  ? 5.35600   2.31300   -39.00800 1.000 38.14668  ? 72  GLN A CA  1 
ATOM   578  C C   . GLN A 1 72  ? 3.84400   2.14700   -38.88500 1.000 37.25447  ? 72  GLN A C   1 
ATOM   579  O O   . GLN A 1 72  ? 3.14300   3.04700   -38.40100 1.000 37.72558  ? 72  GLN A O   1 
ATOM   580  C CB  . GLN A 1 72  ? 5.74900   2.67800   -40.44700 1.000 39.89426  ? 72  GLN A CB  1 
ATOM   581  C CG  . GLN A 1 72  ? 4.91200   3.80500   -41.06100 1.000 41.90502  ? 72  GLN A CG  1 
ATOM   582  C CD  . GLN A 1 72  ? 5.42200   4.28400   -42.42800 1.000 43.92895  ? 72  GLN A CD  1 
ATOM   583  O OE1 . GLN A 1 72  ? 5.73200   3.47500   -43.31400 1.000 44.40006  ? 72  GLN A OE1 1 
ATOM   584  N NE2 . GLN A 1 72  ? 5.50100   5.59100   -42.60400 1.000 44.48691  ? 72  GLN A NE2 1 
ATOM   585  N N   . THR A 1 73  ? 3.32400   0.99800   -39.30900 1.000 32.75130  ? 73  THR A N   1 
ATOM   586  C CA  . THR A 1 73  ? 1.89600   0.72200   -39.14500 1.000 32.21702  ? 73  THR A CA  1 
ATOM   587  C C   . THR A 1 73  ? 1.45500   0.85400   -37.68600 1.000 31.65116  ? 73  THR A C   1 
ATOM   588  O O   . THR A 1 73  ? 0.51000   1.60000   -37.36400 1.000 31.84592  ? 73  THR A O   1 
ATOM   589  C CB  . THR A 1 73  ? 1.58700   -0.67400  -39.68200 1.000 31.88014  ? 73  THR A CB  1 
ATOM   590  O OG1 . THR A 1 73  ? 1.55900   -0.62500  -41.11300 1.000 32.96448  ? 73  THR A OG1 1 
ATOM   591  C CG2 . THR A 1 73  ? 0.26200   -1.18700  -39.12800 1.000 32.05911  ? 73  THR A CG2 1 
ATOM   592  N N   . TYR A 1 74  ? 2.14900   0.16600   -36.78800 1.000 34.49098  ? 74  TYR A N   1 
ATOM   593  C CA  . TYR A 1 74  ? 1.66200   0.07200   -35.42000 1.000 34.42781  ? 74  TYR A CA  1 
ATOM   594  C C   . TYR A 1 74  ? 1.93400   1.32600   -34.60200 1.000 35.46478  ? 74  TYR A C   1 
ATOM   595  O O   . TYR A 1 74  ? 1.16700   1.61100   -33.68400 1.000 36.00432  ? 74  TYR A O   1 
ATOM   596  C CB  . TYR A 1 74  ? 2.22200   -1.19100  -34.75700 1.000 33.64088  ? 74  TYR A CB  1 
ATOM   597  C CG  . TYR A 1 74  ? 1.30900   -2.32500  -35.15300 1.000 33.16187  ? 74  TYR A CG  1 
ATOM   598  C CD1 . TYR A 1 74  ? 0.09300   -2.49000  -34.51700 1.000 34.44360  ? 74  TYR A CD1 1 
ATOM   599  C CD2 . TYR A 1 74  ? 1.60800   -3.15100  -36.23000 1.000 32.47231  ? 74  TYR A CD2 1 
ATOM   600  C CE1 . TYR A 1 74  ? -0.79100  -3.48400  -34.91400 1.000 35.33582  ? 74  TYR A CE1 1 
ATOM   601  C CE2 . TYR A 1 74  ? 0.73300   -4.15600  -36.62800 1.000 33.34874  ? 74  TYR A CE2 1 
ATOM   602  C CZ  . TYR A 1 74  ? -0.46200  -4.30400  -35.96700 1.000 34.33833  ? 74  TYR A CZ  1 
ATOM   603  O OH  . TYR A 1 74  ? -1.35600  -5.27800  -36.33500 1.000 35.75692  ? 74  TYR A OH  1 
ATOM   604  N N   . ARG A 1 75  ? 2.95100   2.11700   -34.96400 1.000 42.43140  ? 75  ARG A N   1 
ATOM   605  C CA  . ARG A 1 75  ? 3.08600   3.45600   -34.40000 1.000 43.84473  ? 75  ARG A CA  1 
ATOM   606  C C   . ARG A 1 75  ? 1.82000   4.28500   -34.63600 1.000 43.89474  ? 75  ARG A C   1 
ATOM   607  O O   . ARG A 1 75  ? 1.34200   4.97600   -33.73200 1.000 44.98697  ? 75  ARG A O   1 
ATOM   608  C CB  . ARG A 1 75  ? 4.31900   4.13900   -35.00500 1.000 45.10541  ? 75  ARG A CB  1 
ATOM   609  C CG  . ARG A 1 75  ? 4.67800   5.48800   -34.44200 1.000 47.52412  ? 75  ARG A CG  1 
ATOM   610  C CD  . ARG A 1 75  ? 6.07300   5.95500   -34.94100 1.000 48.60583  ? 75  ARG A CD  1 
ATOM   611  N NE  . ARG A 1 75  ? 6.88900   4.84300   -35.43900 1.000 48.54003  ? 75  ARG A NE  1 
ATOM   612  C CZ  . ARG A 1 75  ? 7.41700   4.76600   -36.66200 1.000 49.21116  ? 75  ARG A CZ  1 
ATOM   613  N NH1 . ARG A 1 75  ? 7.28200   5.75200   -37.54300 1.000 49.92441  ? 75  ARG A NH1 1 
ATOM   614  N NH2 . ARG A 1 75  ? 8.10300   3.67300   -37.01000 1.000 47.02406  ? 75  ARG A NH2 1 
ATOM   615  N N   . GLU A 1 76  ? 1.24600   4.20500   -35.84000 1.000 35.84640  ? 76  GLU A N   1 
ATOM   616  C CA  . GLU A 1 76  ? 0.03500   4.96000   -36.13600 1.000 36.50174  ? 76  GLU A CA  1 
ATOM   617  C C   . GLU A 1 76  ? -1.21300  4.32800   -35.50500 1.000 35.47004  ? 76  GLU A C   1 
ATOM   618  O O   . GLU A 1 76  ? -2.12600  5.04400   -35.07600 1.000 36.03327  ? 76  GLU A O   1 
ATOM   619  C CB  . GLU A 1 76  ? -0.14200  5.08300   -37.64800 1.000 36.98865  ? 76  GLU A CB  1 
ATOM   620  C CG  . GLU A 1 76  ? -1.25500  6.03300   -38.01800 1.000 38.66779  ? 76  GLU A CG  1 
ATOM   621  C CD  . GLU A 1 76  ? -0.94600  7.48600   -37.63300 1.000 40.68646  ? 76  GLU A CD  1 
ATOM   622  O OE1 . GLU A 1 76  ? 0.24700   7.82900   -37.43100 1.000 40.45222  ? 76  GLU A OE1 1 
ATOM   623  O OE2 . GLU A 1 76  ? -1.90800  8.29300   -37.53700 1.000 41.81817  ? 76  GLU A OE2 1 
ATOM   624  N N   . ASN A 1 77  ? -1.29200  2.99600   -35.48300 1.000 32.44600  ? 77  ASN A N   1 
ATOM   625  C CA  . ASN A 1 77  ? -2.41100  2.33100   -34.81500 1.000 32.58285  ? 77  ASN A CA  1 
ATOM   626  C C   . ASN A 1 77  ? -2.52400  2.73600   -33.34700 1.000 32.69603  ? 77  ASN A C   1 
ATOM   627  O O   . ASN A 1 77  ? -3.63700  2.77900   -32.80100 1.000 33.29347  ? 77  ASN A O   1 
ATOM   628  C CB  . ASN A 1 77  ? -2.26500  0.81100   -34.94900 1.000 32.11438  ? 77  ASN A CB  1 
ATOM   629  C CG  . ASN A 1 77  ? -2.53200  0.33700   -36.37900 1.000 33.00396  ? 77  ASN A CG  1 
ATOM   630  O OD1 . ASN A 1 77  ? -3.34500  0.92100   -37.09100 1.000 33.85669  ? 77  ASN A OD1 1 
ATOM   631  N ND2 . ASN A 1 77  ? -1.82600  -0.71300  -36.80400 1.000 32.46705  ? 77  ASN A ND2 1 
ATOM   632  N N   . LEU A 1 78  ? -1.39800  3.06000   -32.70400 1.000 31.60116  ? 78  LEU A N   1 
ATOM   633  C CA  . LEU A 1 78  ? -1.44500  3.57000   -31.32900 1.000 34.51466  ? 78  LEU A CA  1 
ATOM   634  C C   . LEU A 1 78  ? -2.15500  4.91600   -31.26900 1.000 35.01999  ? 78  LEU A C   1 
ATOM   635  O O   . LEU A 1 78  ? -2.98500  5.15100   -30.38300 1.000 36.68861  ? 78  LEU A O   1 
ATOM   636  C CB  . LEU A 1 78  ? -0.03400  3.68200   -30.75100 1.000 36.05169  ? 78  LEU A CB  1 
ATOM   637  C CG  . LEU A 1 78  ? 0.64100   2.38100   -30.28400 1.000 36.44911  ? 78  LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 78  ? 2.13800   2.59200   -30.00500 1.000 36.23066  ? 78  LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 78  ? -0.05200  1.82700   -29.03700 1.000 38.96783  ? 78  LEU A CD2 1 
ATOM   640  N N   . ARG A 1 79  ? -1.85900  5.80300   -32.21800 1.000 33.85669  ? 79  ARG A N   1 
ATOM   641  C CA  . ARG A 1 79  ? -2.55000  7.08500   -32.28200 1.000 34.77785  ? 79  ARG A CA  1 
ATOM   642  C C   . ARG A 1 79  ? -4.03600  6.90100   -32.56900 1.000 33.67772  ? 79  ARG A C   1 
ATOM   643  O O   . ARG A 1 79  ? -4.88200  7.59300   -31.98200 1.000 34.48571  ? 79  ARG A O   1 
ATOM   644  C CB  . ARG A 1 79  ? -1.89300  7.97100   -33.35300 1.000 35.19896  ? 79  ARG A CB  1 
ATOM   645  N N   . ILE A 1 80  ? -4.36700  5.99400   -33.49300 1.000 35.44636  ? 80  ILE A N   1 
ATOM   646  C CA  . ILE A 1 80  ? -5.76300  5.67500   -33.78500 1.000 35.74113  ? 80  ILE A CA  1 
ATOM   647  C C   . ILE A 1 80  ? -6.46700  5.16000   -32.53100 1.000 36.14907  ? 80  ILE A C   1 
ATOM   648  O O   . ILE A 1 80  ? -7.56100  5.61700   -32.17700 1.000 36.65439  ? 80  ILE A O   1 
ATOM   649  C CB  . ILE A 1 80  ? -5.85100  4.65800   -34.94100 1.000 35.85167  ? 80  ILE A CB  1 
ATOM   650  C CG1 . ILE A 1 80  ? -5.30500  5.26700   -36.25500 1.000 36.65703  ? 80  ILE A CG1 1 
ATOM   651  C CG2 . ILE A 1 80  ? -7.28600  4.26500   -35.16100 1.000 37.60977  ? 80  ILE A CG2 1 
ATOM   652  C CD1 . ILE A 1 80  ? -5.15500  4.23800   -37.43900 1.000 36.94917  ? 80  ILE A CD1 1 
ATOM   653  N N   . ALA A 1 81  ? -5.84800  4.19900   -31.83800 1.000 37.61767  ? 81  ALA A N   1 
ATOM   654  C CA  . ALA A 1 81  ? -6.44700  3.68500   -30.60600 1.000 38.59673  ? 81  ALA A CA  1 
ATOM   655  C C   . ALA A 1 81  ? -6.71600  4.80100   -29.59900 1.000 40.66540  ? 81  ALA A C   1 
ATOM   656  O O   . ALA A 1 81  ? -7.70900  4.73900   -28.86400 1.000 42.01293  ? 81  ALA A O   1 
ATOM   657  C CB  . ALA A 1 81  ? -5.55000  2.61300   -29.99200 1.000 38.90466  ? 81  ALA A CB  1 
ATOM   658  N N   . LEU A 1 82  ? -5.86500  5.83900   -29.56900 1.000 38.40460  ? 82  LEU A N   1 
ATOM   659  C CA  . LEU A 1 82  ? -6.10600  6.97400   -28.67700 1.000 41.36022  ? 82  LEU A CA  1 
ATOM   660  C C   . LEU A 1 82  ? -7.44500  7.62900   -28.97100 1.000 39.83109  ? 82  LEU A C   1 
ATOM   661  O O   . LEU A 1 82  ? -8.19300  7.98200   -28.05000 1.000 42.08663  ? 82  LEU A O   1 
ATOM   662  C CB  . LEU A 1 82  ? -4.99000  8.01900   -28.80200 1.000 42.66564  ? 82  LEU A CB  1 
ATOM   663  C CG  . LEU A 1 82  ? -3.68500  7.79000   -28.04900 1.000 46.35819  ? 82  LEU A CG  1 
ATOM   664  C CD1 . LEU A 1 82  ? -2.77900  9.03600   -28.14500 1.000 46.30292  ? 82  LEU A CD1 1 
ATOM   665  C CD2 . LEU A 1 82  ? -3.93900  7.37900   -26.59100 1.000 51.01138  ? 82  LEU A CD2 1 
ATOM   666  N N   . ARG A 1 83  ? -7.76300  7.81400   -30.25000 1.000 40.23640  ? 83  ARG A N   1 
ATOM   667  C CA  . ARG A 1 83  ? -9.01800  8.47600   -30.58400 1.000 40.48907  ? 83  ARG A CA  1 
ATOM   668  C C   . ARG A 1 83  ? -10.20000 7.55300   -30.32000 1.000 40.66540  ? 83  ARG A C   1 
ATOM   669  O O   . ARG A 1 83  ? -11.25000 8.00300   -29.85300 1.000 41.03650  ? 83  ARG A O   1 
ATOM   670  C CB  . ARG A 1 83  ? -9.00300  8.94400   -32.04000 1.000 40.39168  ? 83  ARG A CB  1 
ATOM   671  N N   . TYR A 1 84  ? -10.04800 6.25800   -30.60500 1.000 42.09189  ? 84  TYR A N   1 
ATOM   672  C CA  . TYR A 1 84  ? -11.14900 5.32600   -30.36700 1.000 42.82356  ? 84  TYR A CA  1 
ATOM   673  C C   . TYR A 1 84  ? -11.58000 5.33800   -28.90500 1.000 43.51048  ? 84  TYR A C   1 
ATOM   674  O O   . TYR A 1 84  ? -12.78100 5.29700   -28.60300 1.000 44.23162  ? 84  TYR A O   1 
ATOM   675  C CB  . TYR A 1 84  ? -10.74700 3.90700   -30.77600 1.000 42.17611  ? 84  TYR A CB  1 
ATOM   676  C CG  . TYR A 1 84  ? -10.68800 3.63900   -32.26000 1.000 42.94199  ? 84  TYR A CG  1 
ATOM   677  C CD1 . TYR A 1 84  ? -11.14600 4.56600   -33.19400 1.000 44.46059  ? 84  TYR A CD1 1 
ATOM   678  C CD2 . TYR A 1 84  ? -10.19600 2.43600   -32.72700 1.000 43.46837  ? 84  TYR A CD2 1 
ATOM   679  C CE1 . TYR A 1 84  ? -11.09400 4.28800   -34.56300 1.000 45.67390  ? 84  TYR A CE1 1 
ATOM   680  C CE2 . TYR A 1 84  ? -10.14400 2.15100   -34.07500 1.000 45.07909  ? 84  TYR A CE2 1 
ATOM   681  C CZ  . TYR A 1 84  ? -10.58700 3.07000   -34.99100 1.000 45.99762  ? 84  TYR A CZ  1 
ATOM   682  O OH  . TYR A 1 84  ? -10.50100 2.74300   -36.32900 1.000 46.38714  ? 84  TYR A OH  1 
ATOM   683  N N   . TYR A 1 85  ? -10.62000 5.38200   -27.98300 1.000 42.45509  ? 85  TYR A N   1 
ATOM   684  C CA  . TYR A 1 85  ? -10.91800 5.32800   -26.55600 1.000 42.67617  ? 85  TYR A CA  1 
ATOM   685  C C   . TYR A 1 85  ? -10.89200 6.69300   -25.87700 1.000 44.47112  ? 85  TYR A C   1 
ATOM   686  O O   . TYR A 1 85  ? -11.06900 6.76100   -24.65900 1.000 44.38427  ? 85  TYR A O   1 
ATOM   687  C CB  . TYR A 1 85  ? -9.94400  4.37700   -25.85100 1.000 41.78922  ? 85  TYR A CB  1 
ATOM   688  C CG  . TYR A 1 85  ? -10.11600 2.91900   -26.26100 1.000 40.44432  ? 85  TYR A CG  1 
ATOM   689  C CD1 . TYR A 1 85  ? -11.11600 2.12600   -25.70400 1.000 40.11270  ? 85  TYR A CD1 1 
ATOM   690  C CD2 . TYR A 1 85  ? -9.27600  2.34400   -27.20200 1.000 39.66265  ? 85  TYR A CD2 1 
ATOM   691  C CE1 . TYR A 1 85  ? -11.27500 0.78200   -26.08500 1.000 38.76781  ? 85  TYR A CE1 1 
ATOM   692  C CE2 . TYR A 1 85  ? -9.41700  1.02300   -27.58000 1.000 38.21774  ? 85  TYR A CE2 1 
ATOM   693  C CZ  . TYR A 1 85  ? -10.40500 0.25000   -27.02200 1.000 37.78085  ? 85  TYR A CZ  1 
ATOM   694  O OH  . TYR A 1 85  ? -10.51800 -1.06400  -27.42900 1.000 36.57281  ? 85  TYR A OH  1 
ATOM   695  N N   . ASN A 1 86  ? -10.68300 7.77600   -26.62700 1.000 50.76398  ? 86  ASN A N   1 
ATOM   696  C CA  . ASN A 1 86  ? -10.75300 9.13200   -26.07700 1.000 51.89043  ? 86  ASN A CA  1 
ATOM   697  C C   . ASN A 1 86  ? -9.77700  9.29600   -24.90900 1.000 51.89833  ? 86  ASN A C   1 
ATOM   698  O O   . ASN A 1 86  ? -10.13200 9.75800   -23.82600 1.000 52.65105  ? 86  ASN A O   1 
ATOM   699  C CB  . ASN A 1 86  ? -12.18900 9.46400   -25.66200 1.000 52.54577  ? 86  ASN A CB  1 
ATOM   700  C CG  . ASN A 1 86  ? -12.58100 10.88500  -26.00300 1.000 54.45653  ? 86  ASN A CG  1 
ATOM   701  O OD1 . ASN A 1 86  ? -11.79800 11.64800  -26.57800 1.000 54.78288  ? 86  ASN A OD1 1 
ATOM   702  N ND2 . ASN A 1 86  ? -13.80400 11.25100  -25.65200 1.000 55.83827  ? 86  ASN A ND2 1 
ATOM   703  N N   . GLN A 1 87  ? -8.53500  8.88400   -25.14200 1.000 44.59745  ? 87  GLN A N   1 
ATOM   704  C CA  . GLN A 1 87  ? -7.46900  8.91200   -24.15400 1.000 44.77642  ? 87  GLN A CA  1 
ATOM   705  C C   . GLN A 1 87  ? -6.47000  10.02000  -24.48300 1.000 45.08172  ? 87  GLN A C   1 
ATOM   706  O O   . GLN A 1 87  ? -6.29800  10.39700  -25.64500 1.000 44.69220  ? 87  GLN A O   1 
ATOM   707  C CB  . GLN A 1 87  ? -6.74700  7.55700   -24.10300 1.000 43.23939  ? 87  GLN A CB  1 
ATOM   708  C CG  . GLN A 1 87  ? -7.64500  6.40100   -23.68200 1.000 42.30507  ? 87  GLN A CG  1 
ATOM   709  C CD  . GLN A 1 87  ? -7.01400  5.02300   -23.87900 1.000 40.36010  ? 87  GLN A CD  1 
ATOM   710  O OE1 . GLN A 1 87  ? -6.16400  4.81600   -24.75200 1.000 39.48895  ? 87  GLN A OE1 1 
ATOM   711  N NE2 . GLN A 1 87  ? -7.46100  4.06700   -23.08100 1.000 39.56790  ? 87  GLN A NE2 1 
ATOM   712  N N   . SER A 1 88  ? -5.78900  10.50500  -23.44800 1.000 51.49038  ? 88  SER A N   1 
ATOM   713  C CA  A SER A 1 88  ? -4.85800  11.61200  -23.59400 0.320 51.95623  ? 88  SER A CA  1 
ATOM   714  C CA  B SER A 1 88  ? -4.85400  11.61000  -23.59300 0.680 51.96149  ? 88  SER A CA  1 
ATOM   715  C C   . SER A 1 88  ? -3.61700  11.18800  -24.37600 1.000 49.59542  ? 88  SER A C   1 
ATOM   716  O O   . SER A 1 88  ? -3.24200  10.01500  -24.42300 1.000 48.60320  ? 88  SER A O   1 
ATOM   717  C CB  A SER A 1 88  ? -4.45200  12.14700  -22.21900 0.320 53.11689  ? 88  SER A CB  1 
ATOM   718  C CB  B SER A 1 88  ? -4.41900  12.13300  -22.22500 0.680 53.11163  ? 88  SER A CB  1 
ATOM   719  O OG  A SER A 1 88  ? -3.56900  13.24700  -22.33700 0.320 53.25639  ? 88  SER A OG  1 
ATOM   720  O OG  B SER A 1 88  ? -3.11300  12.67500  -22.31200 0.680 52.89582  ? 88  SER A OG  1 
ATOM   721  N N   . GLU A 1 89  ? -2.96600  12.17200  -24.98700 1.000 47.68203  ? 89  GLU A N   1 
ATOM   722  C CA  . GLU A 1 89  ? -1.72700  11.89700  -25.70100 1.000 45.83971  ? 89  GLU A CA  1 
ATOM   723  C C   . GLU A 1 89  ? -0.52200  11.82700  -24.76900 1.000 46.72139  ? 89  GLU A C   1 
ATOM   724  O O   . GLU A 1 89  ? 0.59200   11.56900  -25.24500 1.000 46.33187  ? 89  GLU A O   1 
ATOM   725  C CB  . GLU A 1 89  ? -1.50200  12.94900  -26.80000 1.000 46.50558  ? 89  GLU A CB  1 
ATOM   726  N N   . ALA A 1 90  ? -0.72400  11.99100  -23.45100 1.000 41.58130  ? 90  ALA A N   1 
ATOM   727  C CA  . ALA A 1 90  ? 0.35800   11.95600  -22.47400 1.000 42.45246  ? 90  ALA A CA  1 
ATOM   728  C C   . ALA A 1 90  ? 0.59500   10.57900  -21.86000 1.000 43.82894  ? 90  ALA A C   1 
ATOM   729  O O   . ALA A 1 90  ? 1.67600   10.34000  -21.31100 1.000 43.22097  ? 90  ALA A O   1 
ATOM   730  C CB  . ALA A 1 90  ? 0.07600   12.95600  -21.34600 1.000 44.02107  ? 90  ALA A CB  1 
ATOM   731  N N   . GLY A 1 91  ? -0.38700  9.67100   -21.91600 1.000 39.45999  ? 91  GLY A N   1 
ATOM   732  C CA  . GLY A 1 91  ? -0.23100  8.37700   -21.29800 1.000 38.95204  ? 91  GLY A CA  1 
ATOM   733  C C   . GLY A 1 91  ? 0.46800   7.38000   -22.20700 1.000 37.28079  ? 91  GLY A C   1 
ATOM   734  O O   . GLY A 1 91  ? 0.61700   7.59400   -23.41700 1.000 35.34634  ? 91  GLY A O   1 
ATOM   735  N N   . SER A 1 92  ? 0.89400   6.28100   -21.58600 1.000 39.57843  ? 92  SER A N   1 
ATOM   736  C CA  A SER A 1 92  ? 1.61900   5.20800   -22.25500 0.220 37.15972  ? 92  SER A CA  1 
ATOM   737  C CA  B SER A 1 92  ? 1.62000   5.20900   -22.25500 0.780 37.17288  ? 92  SER A CA  1 
ATOM   738  C C   . SER A 1 92  ? 0.68600   4.03000   -22.49200 1.000 34.58309  ? 92  SER A C   1 
ATOM   739  O O   . SER A 1 92  ? -0.00000  3.58200   -21.56600 1.000 34.27253  ? 92  SER A O   1 
ATOM   740  C CB  A SER A 1 92  ? 2.82200   4.76000   -21.42400 0.220 36.20434  ? 92  SER A CB  1 
ATOM   741  C CB  B SER A 1 92  ? 2.82100   4.76200   -21.42200 0.780 36.22803  ? 92  SER A CB  1 
ATOM   742  O OG  A SER A 1 92  ? 3.27600   3.48400   -21.84100 0.220 34.11198  ? 92  SER A OG  1 
ATOM   743  O OG  B SER A 1 92  ? 3.74500   5.82200   -21.27500 0.780 37.05181  ? 92  SER A OG  1 
ATOM   744  N N   . HIS A 1 93  ? 0.67000   3.52800   -23.72300 1.000 35.52794  ? 93  HIS A N   1 
ATOM   745  C CA  . HIS A 1 93  ? -0.22200  2.44400   -24.11200 1.000 32.88552  ? 93  HIS A CA  1 
ATOM   746  C C   . HIS A 1 93  ? 0.54300   1.36300   -24.87300 1.000 30.89318  ? 93  HIS A C   1 
ATOM   747  O O   . HIS A 1 93  ? 1.66700   1.57500   -25.34600 1.000 31.32218  ? 93  HIS A O   1 
ATOM   748  C CB  . HIS A 1 93  ? -1.38100  2.98300   -24.95200 1.000 32.62233  ? 93  HIS A CB  1 
ATOM   749  C CG  . HIS A 1 93  ? -2.18900  4.00800   -24.23000 1.000 35.68849  ? 93  HIS A CG  1 
ATOM   750  N ND1 . HIS A 1 93  ? -3.27600  3.68100   -23.45000 1.000 36.37805  ? 93  HIS A ND1 1 
ATOM   751  C CD2 . HIS A 1 93  ? -2.02300  5.34700   -24.10700 1.000 37.72558  ? 93  HIS A CD2 1 
ATOM   752  C CE1 . HIS A 1 93  ? -3.77100  4.78200   -22.91000 1.000 39.36261  ? 93  HIS A CE1 1 
ATOM   753  N NE2 . HIS A 1 93  ? -3.03600  5.80800   -23.30200 1.000 40.08112  ? 93  HIS A NE2 1 
ATOM   754  N N   . ILE A 1 94  ? -0.08700  0.19200   -25.00400 1.000 34.79101  ? 94  ILE A N   1 
ATOM   755  C CA  . ILE A 1 94  ? 0.56400   -0.95600  -25.62600 1.000 33.28820  ? 94  ILE A CA  1 
ATOM   756  C C   . ILE A 1 94  ? -0.42000  -1.69700  -26.52800 1.000 31.55642  ? 94  ILE A C   1 
ATOM   757  O O   . ILE A 1 94  ? -1.50400  -2.10300  -26.08500 1.000 31.84329  ? 94  ILE A O   1 
ATOM   758  C CB  . ILE A 1 94  ? 1.14200   -1.91300  -24.56900 1.000 33.53297  ? 94  ILE A CB  1 
ATOM   759  C CG1 . ILE A 1 94  ? 2.27200   -1.22600  -23.78300 1.000 35.04894  ? 94  ILE A CG1 1 
ATOM   760  C CG2 . ILE A 1 94  ? 1.60000   -3.22300  -25.23500 1.000 32.04332  ? 94  ILE A CG2 1 
ATOM   761  C CD1 . ILE A 1 94  ? 2.87300   -2.05700  -22.67000 1.000 35.07263  ? 94  ILE A CD1 1 
ATOM   762  N N   . ILE A 1 95  ? -0.03100  -1.88900  -27.79500 1.000 28.22970  ? 95  ILE A N   1 
ATOM   763  C CA  . ILE A 1 95  ? -0.68500  -2.85900  -28.67600 1.000 26.66899  ? 95  ILE A CA  1 
ATOM   764  C C   . ILE A 1 95  ? 0.12900   -4.14900  -28.72400 1.000 25.92153  ? 95  ILE A C   1 
ATOM   765  O O   . ILE A 1 95  ? 1.35700   -4.11400  -28.87200 1.000 26.84269  ? 95  ILE A O   1 
ATOM   766  C CB  . ILE A 1 95  ? -0.86300  -2.26700  -30.08700 1.000 26.57161  ? 95  ILE A CB  1 
ATOM   767  C CG1 . ILE A 1 95  ? -1.94200  -1.17700  -30.06400 1.000 28.35340  ? 95  ILE A CG1 1 
ATOM   768  C CG2 . ILE A 1 95  ? -1.20400  -3.36400  -31.11300 1.000 25.66360  ? 95  ILE A CG2 1 
ATOM   769  C CD1 . ILE A 1 95  ? -2.10800  -0.41200  -31.40000 1.000 29.01401  ? 95  ILE A CD1 1 
ATOM   770  N N   . GLN A 1 96  ? -0.55300  -5.30100  -28.66500 1.000 28.38498  ? 96  GLN A N   1 
ATOM   771  C CA  . GLN A 1 96  ? 0.11300   -6.58600  -28.84500 1.000 27.85597  ? 96  GLN A CA  1 
ATOM   772  C C   . GLN A 1 96  ? -0.55800  -7.37300  -29.96400 1.000 27.50067  ? 96  GLN A C   1 
ATOM   773  O O   . GLN A 1 96  ? -1.76700  -7.27800  -30.16600 1.000 28.24812  ? 96  GLN A O   1 
ATOM   774  C CB  . GLN A 1 96  ? 0.10500   -7.40100  -27.56400 1.000 28.57448  ? 96  GLN A CB  1 
ATOM   775  C CG  . GLN A 1 96  ? 1.10800   -6.87100  -26.53000 1.000 29.63250  ? 96  GLN A CG  1 
ATOM   776  C CD  . GLN A 1 96  ? 0.74000   -7.26500  -25.13500 1.000 30.07992  ? 96  GLN A CD  1 
ATOM   777  O OE1 . GLN A 1 96  ? -0.01200  -6.54800  -24.46500 1.000 30.30627  ? 96  GLN A OE1 1 
ATOM   778  N NE2 . GLN A 1 96  ? 1.26800   -8.39600  -24.66700 1.000 30.19836  ? 96  GLN A NE2 1 
ATOM   779  N N   . VAL A 1 97  ? 0.24400   -8.14000  -30.69400 1.000 25.96101  ? 97  VAL A N   1 
ATOM   780  C CA  . VAL A 1 97  ? -0.22100  -8.87900  -31.87000 1.000 26.40053  ? 97  VAL A CA  1 
ATOM   781  C C   . VAL A 1 97  ? 0.39000   -10.26000 -31.81300 1.000 27.11115  ? 97  VAL A C   1 
ATOM   782  O O   . VAL A 1 97  ? 1.58100   -10.40100 -31.52500 1.000 28.01389  ? 97  VAL A O   1 
ATOM   783  C CB  . VAL A 1 97  ? 0.17100   -8.22100  -33.21200 1.000 26.42159  ? 97  VAL A CB  1 
ATOM   784  C CG1 . VAL A 1 97  ? -0.46300  -9.04000  -34.37800 1.000 27.08483  ? 97  VAL A CG1 1 
ATOM   785  C CG2 . VAL A 1 97  ? -0.24200  -6.74600  -33.26200 1.000 25.96101  ? 97  VAL A CG2 1 
ATOM   786  N N   . MET A 1 98  ? -0.42900  -11.28100 -32.09100 1.000 28.56395  ? 98  MET A N   1 
ATOM   787  C CA  . MET A 1 98  ? 0.02800   -12.64700 -32.24100 1.000 29.96412  ? 98  MET A CA  1 
ATOM   788  C C   . MET A 1 98  ? -0.55000  -13.20200 -33.53400 1.000 30.98266  ? 98  MET A C   1 
ATOM   789  O O   . MET A 1 98  ? -1.70700  -12.93600 -33.86100 1.000 31.67485  ? 98  MET A O   1 
ATOM   790  C CB  . MET A 1 98  ? -0.40400  -13.50700 -31.03400 1.000 30.82475  ? 98  MET A CB  1 
ATOM   791  C CG  . MET A 1 98  ? -0.14600  -15.00500 -31.21000 1.000 32.95132  ? 98  MET A CG  1 
ATOM   792  S SD  . MET A 1 98  ? -1.46300  -15.89600 -32.11600 1.000 35.26212  ? 98  MET A SD  1 
ATOM   793  C CE  . MET A 1 98  ? -2.46500  -16.44100 -30.74200 1.000 35.41477  ? 98  MET A CE  1 
ATOM   794  N N   . TYR A 1 99  ? 0.26900   -13.93900 -34.28900 1.000 26.44001  ? 99  TYR A N   1 
ATOM   795  C CA  . TYR A 1 99  ? -0.26900  -14.76100 -35.37600 1.000 28.00336  ? 99  TYR A CA  1 
ATOM   796  C C   . TYR A 1 99  ? 0.61900   -15.98400 -35.58200 1.000 29.50617  ? 99  TYR A C   1 
ATOM   797  O O   . TYR A 1 99  ? 1.75600   -16.04800 -35.10800 1.000 29.55354  ? 99  TYR A O   1 
ATOM   798  C CB  . TYR A 1 99  ? -0.40700  -13.98300 -36.68600 1.000 27.25064  ? 99  TYR A CB  1 
ATOM   799  C CG  . TYR A 1 99  ? 0.87900   -13.38000 -37.18900 1.000 26.79532  ? 99  TYR A CG  1 
ATOM   800  C CD1 . TYR A 1 99  ? 1.72900   -14.09400 -38.03400 1.000 28.97453  ? 99  TYR A CD1 1 
ATOM   801  C CD2 . TYR A 1 99  ? 1.23100   -12.08800 -36.85500 1.000 25.55043  ? 99  TYR A CD2 1 
ATOM   802  C CE1 . TYR A 1 99  ? 2.90000   -13.53600 -38.51700 1.000 30.02202  ? 99  TYR A CE1 1 
ATOM   803  C CE2 . TYR A 1 99  ? 2.40300   -11.51800 -37.34200 1.000 26.82690  ? 99  TYR A CE2 1 
ATOM   804  C CZ  . TYR A 1 99  ? 3.23000   -12.24000 -38.15800 1.000 28.95347  ? 99  TYR A CZ  1 
ATOM   805  O OH  . TYR A 1 99  ? 4.39000   -11.66500 -38.60000 1.000 30.84054  ? 99  TYR A OH  1 
ATOM   806  N N   . GLY A 1 100 ? 0.09000   -16.94700 -36.32200 1.000 27.37433  ? 100 GLY A N   1 
ATOM   807  C CA  . GLY A 1 100 ? 0.87600   -18.09800 -36.70000 1.000 29.12191  ? 100 GLY A CA  1 
ATOM   808  C C   . GLY A 1 100 ? -0.02000  -19.28900 -36.98100 1.000 30.86159  ? 100 GLY A C   1 
ATOM   809  O O   . GLY A 1 100 ? -1.24700  -19.16500 -37.07300 1.000 31.04056  ? 100 GLY A O   1 
ATOM   810  N N   . CYS A 1 101 ? 0.63800   -20.43800 -37.15600 1.000 33.53034  ? 101 CYS A N   1 
ATOM   811  C CA  . CYS A 1 101 ? -0.00500  -21.64000 -37.65500 1.000 34.89103  ? 101 CYS A CA  1 
ATOM   812  C C   . CYS A 1 101 ? 0.42400   -22.84200 -36.81900 1.000 37.12814  ? 101 CYS A C   1 
ATOM   813  O O   . CYS A 1 101 ? 1.50200   -22.85000 -36.21500 1.000 37.75453  ? 101 CYS A O   1 
ATOM   814  C CB  . CYS A 1 101 ? 0.33600   -21.87500 -39.14200 1.000 35.10421  ? 101 CYS A CB  1 
ATOM   815  S SG  . CYS A 1 101 ? 2.09700   -21.59400 -39.60100 1.000 35.93589  ? 101 CYS A SG  1 
ATOM   816  N N   . ASP A 1 102 ? -0.44500  -23.85000 -36.78600 1.000 36.42805  ? 102 ASP A N   1 
ATOM   817  C CA  . ASP A 1 102 ? -0.15600  -25.15200 -36.19100 1.000 38.74149  ? 102 ASP A CA  1 
ATOM   818  C C   . ASP A 1 102 ? -0.15900  -26.19700 -37.29900 1.000 39.28366  ? 102 ASP A C   1 
ATOM   819  O O   . ASP A 1 102 ? -1.07600  -26.21600 -38.12700 1.000 38.60463  ? 102 ASP A O   1 
ATOM   820  C CB  . ASP A 1 102 ? -1.20400  -25.56700 -35.14100 1.000 38.98625  ? 102 ASP A CB  1 
ATOM   821  C CG  . ASP A 1 102 ? -1.42800  -24.52300 -34.04700 1.000 37.99666  ? 102 ASP A CG  1 
ATOM   822  O OD1 . ASP A 1 102 ? -0.53200  -23.71000 -33.76000 1.000 37.83875  ? 102 ASP A OD1 1 
ATOM   823  O OD2 . ASP A 1 102 ? -2.52800  -24.55200 -33.43600 1.000 37.30710  ? 102 ASP A OD2 1 
ATOM   824  N N   . VAL A 1 103 ? 0.83400   -27.08600 -37.30100 1.000 36.16486  ? 103 VAL A N   1 
ATOM   825  C CA  . VAL A 1 103 ? 0.85000   -28.16700 -38.28200 1.000 37.62030  ? 103 VAL A CA  1 
ATOM   826  C C   . VAL A 1 103 ? 0.94300   -29.50700 -37.56300 1.000 39.53632  ? 103 VAL A C   1 
ATOM   827  O O   . VAL A 1 103 ? 1.45500   -29.60400 -36.44300 1.000 39.96269  ? 103 VAL A O   1 
ATOM   828  C CB  . VAL A 1 103 ? 1.99300   -28.01800 -39.31100 1.000 37.70715  ? 103 VAL A CB  1 
ATOM   829  C CG1 . VAL A 1 103 ? 1.86900   -26.69900 -40.06400 1.000 36.38068  ? 103 VAL A CG1 1 
ATOM   830  C CG2 . VAL A 1 103 ? 3.35400   -28.15700 -38.63200 1.000 38.19932  ? 103 VAL A CG2 1 
ATOM   831  N N   . GLY A 1 104 ? 0.41500   -30.54600 -38.21100 1.000 51.12981  ? 104 GLY A N   1 
ATOM   832  C CA  . GLY A 1 104 ? 0.47500   -31.87900 -37.67100 1.000 52.25890  ? 104 GLY A CA  1 
ATOM   833  C C   . GLY A 1 104 ? 1.77100   -32.57400 -38.04200 1.000 54.20387  ? 104 GLY A C   1 
ATOM   834  O O   . GLY A 1 104 ? 2.68200   -31.96700 -38.62300 1.000 52.71422  ? 104 GLY A O   1 
ATOM   835  N N   . PRO A 1 105 ? 1.87600   -33.86700 -37.70600 1.000 60.59674  ? 105 PRO A N   1 
ATOM   836  C CA  . PRO A 1 105 ? 3.10700   -34.61400 -38.01800 1.000 60.95994  ? 105 PRO A CA  1 
ATOM   837  C C   . PRO A 1 105 ? 3.41800   -34.68700 -39.50000 1.000 61.26787  ? 105 PRO A C   1 
ATOM   838  O O   . PRO A 1 105 ? 4.59400   -34.78900 -39.87300 1.000 61.29682  ? 105 PRO A O   1 
ATOM   839  C CB  . PRO A 1 105 ? 2.82000   -36.00800 -37.43900 1.000 62.49434  ? 105 PRO A CB  1 
ATOM   840  C CG  . PRO A 1 105 ? 1.81700   -35.76200 -36.36000 1.000 62.35221  ? 105 PRO A CG  1 
ATOM   841  C CD  . PRO A 1 105 ? 0.95100   -34.65200 -36.86900 1.000 61.56001  ? 105 PRO A CD  1 
ATOM   842  N N   . ASP A 1 106 ? 2.40200   -34.65300 -40.35800 1.000 64.67618  ? 106 ASP A N   1 
ATOM   843  C CA  . ASP A 1 106 ? 2.61900   -34.59900 -41.79400 1.000 64.04715  ? 106 ASP A CA  1 
ATOM   844  C C   . ASP A 1 106 ? 2.99400   -33.20800 -42.28600 1.000 62.99966  ? 106 ASP A C   1 
ATOM   845  O O   . ASP A 1 106 ? 3.22500   -33.03500 -43.49100 1.000 62.81806  ? 106 ASP A O   1 
ATOM   846  C CB  . ASP A 1 106 ? 1.36600   -35.08100 -42.52500 1.000 64.62617  ? 106 ASP A CB  1 
ATOM   847  C CG  . ASP A 1 106 ? 0.11700   -34.34000 -42.08100 1.000 64.26034  ? 106 ASP A CG  1 
ATOM   848  O OD1 . ASP A 1 106 ? 0.23400   -33.38900 -41.26600 1.000 62.47591  ? 106 ASP A OD1 1 
ATOM   849  O OD2 . ASP A 1 106 ? -0.98200  -34.72000 -42.54400 1.000 64.12348  ? 106 ASP A OD2 1 
ATOM   850  N N   . GLY A 1 107 ? 3.05200   -32.21700 -41.39900 1.000 52.24047  ? 107 GLY A N   1 
ATOM   851  C CA  . GLY A 1 107 ? 3.39100   -30.87800 -41.81100 1.000 51.10350  ? 107 GLY A CA  1 
ATOM   852  C C   . GLY A 1 107 ? 2.25300   -30.09500 -42.42000 1.000 49.95599  ? 107 GLY A C   1 
ATOM   853  O O   . GLY A 1 107 ? 2.47400   -28.95300 -42.86000 1.000 48.71374  ? 107 GLY A O   1 
ATOM   854  N N   . ARG A 1 108 ? 1.04300   -30.65000 -42.44000 1.000 47.67940  ? 108 ARG A N   1 
ATOM   855  C CA  . ARG A 1 108 ? -0.09700  -29.94300 -42.99800 1.000 46.93721  ? 108 ARG A CA  1 
ATOM   856  C C   . ARG A 1 108 ? -0.75600  -29.05800 -41.93800 1.000 45.51598  ? 108 ARG A C   1 
ATOM   857  O O   . ARG A 1 108 ? -0.68000  -29.32200 -40.74200 1.000 46.15553  ? 108 ARG A O   1 
ATOM   858  C CB  . ARG A 1 108 ? -1.11000  -30.93100 -43.57900 1.000 47.57413  ? 108 ARG A CB  1 
ATOM   859  C CG  . ARG A 1 108 ? -0.61100  -31.70300 -44.82300 1.000 49.21906  ? 108 ARG A CG  1 
ATOM   860  C CD  . ARG A 1 108 ? -1.56400  -32.85300 -45.15600 1.000 50.65344  ? 108 ARG A CD  1 
ATOM   861  N NE  . ARG A 1 108 ? -1.38700  -33.44500 -46.48300 1.000 52.50630  ? 108 ARG A NE  1 
ATOM   862  C CZ  . ARG A 1 108 ? -2.35000  -33.52000 -47.39500 1.000 52.84844  ? 108 ARG A CZ  1 
ATOM   863  N NH1 . ARG A 1 108 ? -3.55800  -33.02200 -47.17000 1.000 52.87476  ? 108 ARG A NH1 1 
ATOM   864  N NH2 . ARG A 1 108 ? -2.10300  -34.12100 -48.55700 1.000 55.24610  ? 108 ARG A NH2 1 
ATOM   865  N N   . LEU A 1 109 ? -1.40500  -27.99900 -42.40100 1.000 40.59697  ? 109 LEU A N   1 
ATOM   866  C CA  . LEU A 1 109 ? -2.00400  -27.01400 -41.50900 1.000 39.92847  ? 109 LEU A CA  1 
ATOM   867  C C   . LEU A 1 109 ? -3.12300  -27.63000 -40.67200 1.000 40.64698  ? 109 LEU A C   1 
ATOM   868  O O   . LEU A 1 109 ? -3.98800  -28.33300 -41.19600 1.000 41.24179  ? 109 LEU A O   1 
ATOM   869  C CB  . LEU A 1 109 ? -2.55200  -25.84500 -42.32900 1.000 38.28354  ? 109 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 109 ? -3.30300  -24.81900 -41.48600 1.000 37.33079  ? 109 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 109 ? -2.33300  -24.06900 -40.62800 1.000 36.60702  ? 109 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 109 ? -4.10000  -23.87200 -42.34500 1.000 37.72821  ? 109 LEU A CD2 1 
ATOM   873  N N   . LEU A 1 110 ? -3.09800  -27.36500 -39.36500 1.000 39.53369  ? 110 LEU A N   1 
ATOM   874  C CA  . LEU A 1 110 ? -4.16300  -27.75800 -38.45000 1.000 40.22851  ? 110 LEU A CA  1 
ATOM   875  C C   . LEU A 1 110 ? -5.07200  -26.59000 -38.08600 1.000 39.27050  ? 110 LEU A C   1 
ATOM   876  O O   . LEU A 1 110 ? -6.29600  -26.74100 -38.08900 1.000 40.77857  ? 110 LEU A O   1 
ATOM   877  C CB  . LEU A 1 110 ? -3.57400  -28.37000 -37.17100 1.000 40.87069  ? 110 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 110 ? -2.90400  -29.74200 -37.26500 1.000 42.35508  ? 110 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 110 ? -2.28100  -30.05700 -35.90800 1.000 42.84461  ? 110 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 110 ? -3.87400  -30.84000 -37.70800 1.000 43.90790  ? 110 LEU A CD2 1 
ATOM   881  N N   . ARG A 1 111 ? -4.49600  -25.43800 -37.73200 1.000 47.87153  ? 111 ARG A N   1 
ATOM   882  C CA  . ARG A 1 111 ? -5.25600  -24.19400 -37.68500 1.000 46.99248  ? 111 ARG A CA  1 
ATOM   883  C C   . ARG A 1 111 ? -4.31400  -22.99900 -37.69400 1.000 45.36860  ? 111 ARG A C   1 
ATOM   884  O O   . ARG A 1 111 ? -3.11600  -23.11300 -37.42100 1.000 45.51072  ? 111 ARG A O   1 
ATOM   885  C CB  . ARG A 1 111 ? -6.19300  -24.09600 -36.47900 1.000 47.23461  ? 111 ARG A CB  1 
ATOM   886  C CG  . ARG A 1 111 ? -5.62000  -24.39700 -35.13100 1.000 47.24251  ? 111 ARG A CG  1 
ATOM   887  C CD  . ARG A 1 111 ? -6.70700  -24.10500 -34.07800 1.000 46.59243  ? 111 ARG A CD  1 
ATOM   888  N NE  . ARG A 1 111 ? -7.15900  -22.72900 -34.25500 1.000 46.09500  ? 111 ARG A NE  1 
ATOM   889  C CZ  . ARG A 1 111 ? -8.09100  -22.11400 -33.53500 1.000 45.01856  ? 111 ARG A CZ  1 
ATOM   890  N NH1 . ARG A 1 111 ? -8.74900  -22.73400 -32.56600 1.000 44.58429  ? 111 ARG A NH1 1 
ATOM   891  N NH2 . ARG A 1 111 ? -8.36400  -20.83300 -33.79300 1.000 44.59745  ? 111 ARG A NH2 1 
ATOM   892  N N   . GLY A 1 112 ? -4.89400  -21.85100 -38.03000 1.000 33.87511  ? 112 GLY A N   1 
ATOM   893  C CA  . GLY A 1 112 ? -4.19600  -20.57400 -38.04600 1.000 32.26966  ? 112 GLY A CA  1 
ATOM   894  C C   . GLY A 1 112 ? -4.67700  -19.69100 -36.91500 1.000 31.75381  ? 112 GLY A C   1 
ATOM   895  O O   . GLY A 1 112 ? -5.77900  -19.90200 -36.39300 1.000 32.55390  ? 112 GLY A O   1 
ATOM   896  N N   . HIS A 1 113 ? -3.87200  -18.70400 -36.52400 1.000 31.51430  ? 113 HIS A N   1 
ATOM   897  C CA  . HIS A 1 113 ? -4.22200  -17.83400 -35.41300 1.000 31.06425  ? 113 HIS A CA  1 
ATOM   898  C C   . HIS A 1 113 ? -3.84200  -16.40900 -35.76700 1.000 29.71935  ? 113 HIS A C   1 
ATOM   899  O O   . HIS A 1 113 ? -2.83400  -16.17900 -36.44600 1.000 28.54026  ? 113 HIS A O   1 
ATOM   900  C CB  . HIS A 1 113 ? -3.50400  -18.22600 -34.11500 1.000 30.83528  ? 113 HIS A CB  1 
ATOM   901  C CG  . HIS A 1 113 ? -3.67600  -19.66800 -33.72600 1.000 32.51969  ? 113 HIS A CG  1 
ATOM   902  N ND1 . HIS A 1 113 ? -4.55800  -20.07300 -32.74400 1.000 32.66971  ? 113 HIS A ND1 1 
ATOM   903  C CD2 . HIS A 1 113 ? -3.06000  -20.79200 -34.16300 1.000 33.86985  ? 113 HIS A CD2 1 
ATOM   904  C CE1 . HIS A 1 113 ? -4.48700  -21.38600 -32.59800 1.000 33.90143  ? 113 HIS A CE1 1 
ATOM   905  N NE2 . HIS A 1 113 ? -3.59200  -21.85000 -33.45500 1.000 35.45688  ? 113 HIS A NE2 1 
ATOM   906  N N   . ASN A 1 114 ? -4.65400  -15.46200 -35.30400 1.000 33.43296  ? 114 ASN A N   1 
ATOM   907  C CA  . ASN A 1 114 ? -4.29300  -14.05200 -35.38200 1.000 31.97225  ? 114 ASN A CA  1 
ATOM   908  C C   . ASN A 1 114 ? -5.17400  -13.31500 -34.38400 1.000 32.23544  ? 114 ASN A C   1 
ATOM   909  O O   . ASN A 1 114 ? -6.40100  -13.27300 -34.55200 1.000 33.11450  ? 114 ASN A O   1 
ATOM   910  C CB  . ASN A 1 114 ? -4.48100  -13.51500 -36.79200 1.000 31.60642  ? 114 ASN A CB  1 
ATOM   911  C CG  . ASN A 1 114 ? -4.01400  -12.07100 -36.93200 1.000 30.14572  ? 114 ASN A CG  1 
ATOM   912  O OD1 . ASN A 1 114 ? -3.07700  -11.61600 -36.25400 1.000 29.06401  ? 114 ASN A OD1 1 
ATOM   913  N ND2 . ASN A 1 114 ? -4.66500  -11.34700 -37.79100 1.000 30.40365  ? 114 ASN A ND2 1 
ATOM   914  N N   . GLN A 1 115 ? -4.55500  -12.77100 -33.34200 1.000 34.62784  ? 115 GLN A N   1 
ATOM   915  C CA  . GLN A 1 115 ? -5.26900  -12.08900 -32.27700 1.000 33.99092  ? 115 GLN A CA  1 
ATOM   916  C C   . GLN A 1 115 ? -4.54500  -10.79400 -31.95200 1.000 32.32493  ? 115 GLN A C   1 
ATOM   917  O O   . GLN A 1 115 ? -3.32100  -10.69700 -32.10600 1.000 30.67210  ? 115 GLN A O   1 
ATOM   918  C CB  . GLN A 1 115 ? -5.36700  -12.95700 -31.02200 1.000 33.69878  ? 115 GLN A CB  1 
ATOM   919  C CG  . GLN A 1 115 ? -5.95600  -14.33200 -31.27700 1.000 35.91746  ? 115 GLN A CG  1 
ATOM   920  C CD  . GLN A 1 115 ? -6.13300  -15.10200 -29.99200 1.000 36.25698  ? 115 GLN A CD  1 
ATOM   921  O OE1 . GLN A 1 115 ? -6.16900  -14.53100 -28.90100 1.000 37.36237  ? 115 GLN A OE1 1 
ATOM   922  N NE2 . GLN A 1 115 ? -6.23800  -16.41400 -30.11100 1.000 34.76206  ? 115 GLN A NE2 1 
ATOM   923  N N   . TYR A 1 116 ? -5.31900  -9.80600  -31.49900 1.000 30.44576  ? 116 TYR A N   1 
ATOM   924  C CA  . TYR A 1 116 ? -4.79500  -8.48500  -31.16900 1.000 29.59565  ? 116 TYR A CA  1 
ATOM   925  C C   . TYR A 1 116 ? -5.27800  -8.07500  -29.78800 1.000 29.27719  ? 116 TYR A C   1 
ATOM   926  O O   . TYR A 1 116 ? -6.38300  -8.42400  -29.37500 1.000 30.84054  ? 116 TYR A O   1 
ATOM   927  C CB  . TYR A 1 116 ? -5.23100  -7.40800  -32.19200 1.000 31.02740  ? 116 TYR A CB  1 
ATOM   928  C CG  . TYR A 1 116 ? -4.89300  -7.77300  -33.61300 1.000 31.28270  ? 116 TYR A CG  1 
ATOM   929  C CD1 . TYR A 1 116 ? -5.63800  -8.72600  -34.30400 1.000 31.97752  ? 116 TYR A CD1 1 
ATOM   930  C CD2 . TYR A 1 116 ? -3.82200  -7.17000  -34.27100 1.000 29.19297  ? 116 TYR A CD2 1 
ATOM   931  C CE1 . TYR A 1 116 ? -5.31500  -9.07300  -35.60300 1.000 31.60905  ? 116 TYR A CE1 1 
ATOM   932  C CE2 . TYR A 1 116 ? -3.50500  -7.50300  -35.59100 1.000 28.24286  ? 116 TYR A CE2 1 
ATOM   933  C CZ  . TYR A 1 116 ? -4.24200  -8.46700  -36.23100 1.000 29.84042  ? 116 TYR A CZ  1 
ATOM   934  O OH  . TYR A 1 116 ? -3.94500  -8.79300  -37.54000 1.000 29.55881  ? 116 TYR A OH  1 
ATOM   935  N N   . ALA A 1 117 ? -4.45000  -7.28400  -29.09700 1.000 27.39013  ? 117 ALA A N   1 
ATOM   936  C CA  . ALA A 1 117 ? -4.78400  -6.77400  -27.78000 1.000 28.20338  ? 117 ALA A CA  1 
ATOM   937  C C   . ALA A 1 117 ? -4.47900  -5.27800  -27.71100 1.000 28.30866  ? 117 ALA A C   1 
ATOM   938  O O   . ALA A 1 117 ? -3.55500  -4.79300  -28.37400 1.000 26.55055  ? 117 ALA A O   1 
ATOM   939  C CB  . ALA A 1 117 ? -3.99600  -7.48300  -26.72000 1.000 26.77426  ? 117 ALA A CB  1 
ATOM   940  N N   . TYR A 1 118 ? -5.23600  -4.56100  -26.87300 1.000 28.25602  ? 118 TYR A N   1 
ATOM   941  C CA  . TYR A 1 118 ? -4.92100  -3.17500  -26.54300 1.000 28.85609  ? 118 TYR A CA  1 
ATOM   942  C C   . TYR A 1 118 ? -4.87200  -3.05500  -25.03300 1.000 29.02716  ? 118 TYR A C   1 
ATOM   943  O O   . TYR A 1 118 ? -5.83400  -3.42900  -24.34100 1.000 29.72198  ? 118 TYR A O   1 
ATOM   944  C CB  . TYR A 1 118 ? -5.92600  -2.18200  -27.14300 1.000 31.29059  ? 118 TYR A CB  1 
ATOM   945  C CG  . TYR A 1 118 ? -5.55900  -0.70800  -26.89800 1.000 32.10911  ? 118 TYR A CG  1 
ATOM   946  C CD1 . TYR A 1 118 ? -4.34700  -0.18300  -27.33600 1.000 30.56156  ? 118 TYR A CD1 1 
ATOM   947  C CD2 . TYR A 1 118 ? -6.43900  0.14700   -26.25300 1.000 34.36991  ? 118 TYR A CD2 1 
ATOM   948  C CE1 . TYR A 1 118 ? -4.01200  1.16800   -27.11900 1.000 31.88803  ? 118 TYR A CE1 1 
ATOM   949  C CE2 . TYR A 1 118 ? -6.12400  1.49700   -26.04000 1.000 35.72534  ? 118 TYR A CE2 1 
ATOM   950  C CZ  . TYR A 1 118 ? -4.91700  1.99700   -26.47900 1.000 34.76206  ? 118 TYR A CZ  1 
ATOM   951  O OH  . TYR A 1 118 ? -4.60800  3.32800   -26.26100 1.000 36.33594  ? 118 TYR A OH  1 
ATOM   952  N N   . ASP A 1 119 ? -3.73100  -2.58400  -24.53200 1.000 35.13579  ? 119 ASP A N   1 
ATOM   953  C CA  . ASP A 1 119 ? -3.49600  -2.38200  -23.10000 1.000 36.47806  ? 119 ASP A CA  1 
ATOM   954  C C   . ASP A 1 119 ? -3.74200  -3.66700  -22.30400 1.000 35.23844  ? 119 ASP A C   1 
ATOM   955  O O   . ASP A 1 119 ? -4.27400  -3.65700  -21.18900 1.000 36.01748  ? 119 ASP A O   1 
ATOM   956  C CB  . ASP A 1 119 ? -4.32300  -1.20400  -22.57200 1.000 37.81769  ? 119 ASP A CB  1 
ATOM   957  C CG  . ASP A 1 119 ? -3.70100  0.17200   -22.95200 1.000 37.77295  ? 119 ASP A CG  1 
ATOM   958  O OD1 . ASP A 1 119 ? -2.48300  0.23200   -23.25300 1.000 36.64124  ? 119 ASP A OD1 1 
ATOM   959  O OD2 . ASP A 1 119 ? -4.42700  1.18600   -22.93200 1.000 38.57568  ? 119 ASP A OD2 1 
ATOM   960  N N   . GLY A 1 120 ? -3.30900  -4.78300  -22.87500 1.000 36.76493  ? 120 GLY A N   1 
ATOM   961  C CA  . GLY A 1 120 ? -3.34300  -6.05900  -22.20700 1.000 35.66480  ? 120 GLY A CA  1 
ATOM   962  C C   . GLY A 1 120 ? -4.67900  -6.76800  -22.21200 1.000 34.83049  ? 120 GLY A C   1 
ATOM   963  O O   . GLY A 1 120 ? -4.81100  -7.78000  -21.52700 1.000 34.15410  ? 120 GLY A O   1 
ATOM   964  N N   . LYS A 1 121 ? -5.67000  -6.26900  -22.94600 1.000 38.10983  ? 121 LYS A N   1 
ATOM   965  C CA  . LYS A 1 121 ? -6.98600  -6.88200  -23.02200 1.000 37.40448  ? 121 LYS A CA  1 
ATOM   966  C C   . LYS A 1 121 ? -7.27700  -7.24300  -24.46700 1.000 35.69902  ? 121 LYS A C   1 
ATOM   967  O O   . LYS A 1 121 ? -6.82600  -6.55500  -25.39000 1.000 35.42267  ? 121 LYS A O   1 
ATOM   968  C CB  . LYS A 1 121 ? -8.08300  -5.93400  -22.50900 1.000 39.48368  ? 121 LYS A CB  1 
ATOM   969  C CG  . LYS A 1 121 ? -7.86600  -5.44500  -21.07500 1.000 42.45772  ? 121 LYS A CG  1 
ATOM   970  C CD  . LYS A 1 121 ? -8.92200  -4.40500  -20.64300 1.000 44.97645  ? 121 LYS A CD  1 
ATOM   971  C CE  . LYS A 1 121 ? -9.86400  -4.00500  -21.79200 1.000 44.61588  ? 121 LYS A CE  1 
ATOM   972  N NZ  . LYS A 1 121 ? -11.05500 -4.92200  -21.86100 1.000 43.41573  ? 121 LYS A NZ  1 
ATOM   973  N N   . ASP A 1 122 ? -8.03400  -8.32100  -24.66100 1.000 37.07813  ? 122 ASP A N   1 
ATOM   974  C CA  . ASP A 1 122 ? -8.45300  -8.69500  -26.00500 1.000 35.69639  ? 122 ASP A CA  1 
ATOM   975  C C   . ASP A 1 122 ? -9.04900  -7.50100  -26.74000 1.000 36.28330  ? 122 ASP A C   1 
ATOM   976  O O   . ASP A 1 122 ? -9.85000  -6.74200  -26.18700 1.000 37.69399  ? 122 ASP A O   1 
ATOM   977  C CB  . ASP A 1 122 ? -9.47400  -9.82500  -25.97400 1.000 35.34108  ? 122 ASP A CB  1 
ATOM   978  C CG  . ASP A 1 122 ? -8.83000  -11.17700 -25.75000 1.000 34.92524  ? 122 ASP A CG  1 
ATOM   979  O OD1 . ASP A 1 122 ? -7.65000  -11.35600 -26.11000 1.000 34.07514  ? 122 ASP A OD1 1 
ATOM   980  O OD2 . ASP A 1 122 ? -9.50400  -12.06400 -25.23100 1.000 35.18053  ? 122 ASP A OD2 1 
ATOM   981  N N   . TYR A 1 123 ? -8.64400  -7.34200  -27.99700 1.000 27.72174  ? 123 TYR A N   1 
ATOM   982  C CA  . TYR A 1 123 ? -9.19200  -6.29500  -28.84800 1.000 28.35077  ? 123 TYR A CA  1 
ATOM   983  C C   . TYR A 1 123 ? -9.97300  -6.88600  -30.01500 1.000 26.93481  ? 123 TYR A C   1 
ATOM   984  O O   . TYR A 1 123 ? -11.18800 -6.72100  -30.08200 1.000 28.03494  ? 123 TYR A O   1 
ATOM   985  C CB  . TYR A 1 123 ? -8.07300  -5.36500  -29.34500 1.000 28.33761  ? 123 TYR A CB  1 
ATOM   986  C CG  . TYR A 1 123 ? -8.54400  -4.20000  -30.19100 1.000 28.65607  ? 123 TYR A CG  1 
ATOM   987  C CD1 . TYR A 1 123 ? -9.13100  -3.09600  -29.60900 1.000 31.22480  ? 123 TYR A CD1 1 
ATOM   988  C CD2 . TYR A 1 123 ? -8.38200  -4.20600  -31.57400 1.000 27.25327  ? 123 TYR A CD2 1 
ATOM   989  C CE1 . TYR A 1 123 ? -9.53000  -1.98000  -30.38600 1.000 32.10911  ? 123 TYR A CE1 1 
ATOM   990  C CE2 . TYR A 1 123 ? -8.80100  -3.11400  -32.37300 1.000 27.87176  ? 123 TYR A CE2 1 
ATOM   991  C CZ  . TYR A 1 123 ? -9.38800  -2.02000  -31.75800 1.000 30.39312  ? 123 TYR A CZ  1 
ATOM   992  O OH  . TYR A 1 123 ? -9.80600  -0.93100  -32.49200 1.000 31.28533  ? 123 TYR A OH  1 
ATOM   993  N N   . ILE A 1 124 ? -9.32400  -7.64100  -30.89900 1.000 29.56407  ? 124 ILE A N   1 
ATOM   994  C CA  . ILE A 1 124 ? -10.01800 -8.29000  -32.00300 1.000 28.89294  ? 124 ILE A CA  1 
ATOM   995  C C   . ILE A 1 124 ? -9.23200  -9.54600  -32.34900 1.000 27.89282  ? 124 ILE A C   1 
ATOM   996  O O   . ILE A 1 124 ? -8.02000  -9.62000  -32.11300 1.000 27.42960  ? 124 ILE A O   1 
ATOM   997  C CB  . ILE A 1 124 ? -10.16100 -7.32100  -33.21000 1.000 29.05875  ? 124 ILE A CB  1 
ATOM   998  C CG1 . ILE A 1 124 ? -11.14300 -7.85000  -34.26700 1.000 28.99821  ? 124 ILE A CG1 1 
ATOM   999  C CG2 . ILE A 1 124 ? -8.80200  -7.06200  -33.84800 1.000 27.95335  ? 124 ILE A CG2 1 
ATOM   1000 C CD1 . ILE A 1 124 ? -11.37200 -6.88200  -35.41800 1.000 30.17204  ? 124 ILE A CD1 1 
ATOM   1001 N N   . ALA A 1 125 ? -9.93500  -10.55000 -32.87800 1.000 29.94570  ? 125 ALA A N   1 
ATOM   1002 C CA  . ALA A 1 125 ? -9.32700  -11.83600 -33.20000 1.000 29.57460  ? 125 ALA A CA  1 
ATOM   1003 C C   . ALA A 1 125 ? -9.93000  -12.39700 -34.47800 1.000 29.57986  ? 125 ALA A C   1 
ATOM   1004 O O   . ALA A 1 125 ? -11.14000 -12.28600 -34.71100 1.000 30.30890  ? 125 ALA A O   1 
ATOM   1005 C CB  . ALA A 1 125 ? -9.50300  -12.85600 -32.05500 1.000 29.86148  ? 125 ALA A CB  1 
ATOM   1006 N N   . LEU A 1 126 ? -9.07900  -13.01400 -35.29200 1.000 30.96950  ? 126 LEU A N   1 
ATOM   1007 C CA  . LEU A 1 126 ? -9.54100  -13.77700 -36.44500 1.000 31.71170  ? 126 LEU A CA  1 
ATOM   1008 C C   . LEU A 1 126 ? -10.15800 -15.09500 -35.98600 1.000 32.53548  ? 126 LEU A C   1 
ATOM   1009 O O   . LEU A 1 126 ? -9.56800  -15.82000 -35.17800 1.000 32.25124  ? 126 LEU A O   1 
ATOM   1010 C CB  . LEU A 1 126 ? -8.37000  -14.04500 -37.39200 1.000 32.01173  ? 126 LEU A CB  1 
ATOM   1011 C CG  . LEU A 1 126 ? -8.62100  -14.74500 -38.73400 1.000 33.10660  ? 126 LEU A CG  1 
ATOM   1012 C CD1 . LEU A 1 126 ? -9.46200  -13.84100 -39.62200 1.000 33.71720  ? 126 LEU A CD1 1 
ATOM   1013 C CD2 . LEU A 1 126 ? -7.28200  -15.06500 -39.42600 1.000 33.91459  ? 126 LEU A CD2 1 
ATOM   1014 N N   . ASN A 1 127 ? -11.34000 -15.42500 -36.50700 1.000 32.80393  ? 127 ASN A N   1 
ATOM   1015 C CA  . ASN A 1 127 ? -11.99200 -16.66100 -36.09000 1.000 33.13555  ? 127 ASN A CA  1 
ATOM   1016 C C   . ASN A 1 127 ? -11.30100 -17.86800 -36.72000 1.000 33.74089  ? 127 ASN A C   1 
ATOM   1017 O O   . ASN A 1 127 ? -10.46900 -17.74000 -37.61900 1.000 33.86459  ? 127 ASN A O   1 
ATOM   1018 C CB  . ASN A 1 127 ? -13.47300 -16.63100 -36.45500 1.000 33.75931  ? 127 ASN A CB  1 
ATOM   1019 C CG  . ASN A 1 127 ? -14.20900 -15.50500 -35.75000 1.000 34.09093  ? 127 ASN A CG  1 
ATOM   1020 O OD1 . ASN A 1 127 ? -13.86000 -15.14000 -34.62000 1.000 33.31715  ? 127 ASN A OD1 1 
ATOM   1021 N ND2 . ASN A 1 127 ? -15.22500 -14.94200 -36.41100 1.000 34.33306  ? 127 ASN A ND2 1 
ATOM   1022 N N   . GLU A 1 128 ? -11.62900 -19.05300 -36.19500 1.000 36.30172  ? 128 GLU A N   1 
ATOM   1023 C CA  . GLU A 1 128 ? -11.05100 -20.30600 -36.68500 1.000 36.96496  ? 128 GLU A CA  1 
ATOM   1024 C C   . GLU A 1 128 ? -11.24600 -20.48800 -38.19200 1.000 37.90718  ? 128 GLU A C   1 
ATOM   1025 O O   . GLU A 1 128 ? -10.38600 -21.07700 -38.86000 1.000 38.31512  ? 128 GLU A O   1 
ATOM   1026 C CB  . GLU A 1 128 ? -11.66600 -21.49200 -35.92800 1.000 37.88875  ? 128 GLU A CB  1 
ATOM   1027 C CG  . GLU A 1 128 ? -10.86900 -22.79500 -36.02300 1.000 39.05731  ? 128 GLU A CG  1 
ATOM   1028 C CD  . GLU A 1 128 ? -11.43700 -23.92800 -35.16400 1.000 39.47579  ? 128 GLU A CD  1 
ATOM   1029 O OE1 . GLU A 1 128 ? -12.62200 -23.84200 -34.73000 1.000 38.93888  ? 128 GLU A OE1 1 
ATOM   1030 O OE2 . GLU A 1 128 ? -10.70900 -24.93800 -34.96200 1.000 40.35484  ? 128 GLU A OE2 1 
ATOM   1031 N N   . ASP A 1 129 ? -12.36100 -20.00000 -38.74500 1.000 35.95168  ? 129 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 129 ? -12.60000 -20.14400 -40.18100 1.000 36.66755  ? 129 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 129 ? -11.63500 -19.32300 -41.03400 1.000 36.80704  ? 129 ASP A C   1 
ATOM   1034 O O   . ASP A 1 129 ? -11.63200 -19.48600 -42.25500 1.000 37.73084  ? 129 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 129 ? -14.05500 -19.78800 -40.52800 1.000 37.33079  ? 129 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 129 ? -14.41900 -18.34700 -40.18700 1.000 36.99128  ? 129 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 129 ? -13.53200 -17.48700 -40.05000 1.000 36.48595  ? 129 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 129 ? -15.62600 -18.06500 -40.05500 1.000 37.35185  ? 129 ASP A OD2 1 
ATOM   1039 N N   . LEU A 1 130 ? -10.81300 -18.47000 -40.41700 1.000 31.37218  ? 130 LEU A N   1 
ATOM   1040 C CA  . LEU A 1 130 ? -9.84200  -17.59800 -41.08600 1.000 31.42745  ? 130 LEU A CA  1 
ATOM   1041 C C   . LEU A 1 130 ? -10.50700 -16.64700 -42.07100 1.000 32.18544  ? 130 LEU A C   1 
ATOM   1042 O O   . LEU A 1 130 ? -9.85900  -16.16700 -43.02100 1.000 32.35914  ? 130 LEU A O   1 
ATOM   1043 C CB  . LEU A 1 130 ? -8.74400  -18.40000 -41.80100 1.000 32.06174  ? 130 LEU A CB  1 
ATOM   1044 C CG  . LEU A 1 130 ? -8.04200  -19.47300 -40.98200 1.000 32.12490  ? 130 LEU A CG  1 
ATOM   1045 C CD1 . LEU A 1 130 ? -6.86200  -20.08100 -41.76700 1.000 33.15924  ? 130 LEU A CD1 1 
ATOM   1046 C CD2 . LEU A 1 130 ? -7.60300  -18.93400 -39.61400 1.000 31.41429  ? 130 LEU A CD2 1 
ATOM   1047 N N   . SER A 1 131 ? -11.79200 -16.34900 -41.88800 1.000 36.38331  ? 131 SER A N   1 
ATOM   1048 C CA  . SER A 1 131 ? -12.43500 -15.44600 -42.82900 1.000 37.33342  ? 131 SER A CA  1 
ATOM   1049 C C   . SER A 1 131 ? -13.41300 -14.49800 -42.15400 1.000 37.38080  ? 131 SER A C   1 
ATOM   1050 O O   . SER A 1 131 ? -14.10000 -13.75500 -42.85600 1.000 37.95718  ? 131 SER A O   1 
ATOM   1051 C CB  . SER A 1 131 ? -13.14200 -16.22900 -43.93900 1.000 38.70464  ? 131 SER A CB  1 
ATOM   1052 O OG  . SER A 1 131 ? -14.11400 -17.07400 -43.39700 1.000 38.68095  ? 131 SER A OG  1 
ATOM   1053 N N   . SER A 1 132 ? -13.48400 -14.48400 -40.82100 1.000 35.93852  ? 132 SER A N   1 
ATOM   1054 C CA  . SER A 1 132 ? -14.30900 -13.53000 -40.09400 1.000 35.97800  ? 132 SER A CA  1 
ATOM   1055 C C   . SER A 1 132 ? -13.57700 -13.11800 -38.81900 1.000 34.86997  ? 132 SER A C   1 
ATOM   1056 O O   . SER A 1 132 ? -12.58000 -13.73000 -38.42500 1.000 34.15146  ? 132 SER A O   1 
ATOM   1057 C CB  . SER A 1 132 ? -15.68900 -14.11900 -39.78200 1.000 36.32541  ? 132 SER A CB  1 
ATOM   1058 O OG  . SER A 1 132 ? -15.58600 -15.34900 -39.07300 1.000 36.01748  ? 132 SER A OG  1 
ATOM   1059 N N   . TRP A 1 133 ? -14.09100 -12.07600 -38.16100 1.000 29.77989  ? 133 TRP A N   1 
ATOM   1060 C CA  . TRP A 1 133 ? -13.47800 -11.52500 -36.96400 1.000 29.03243  ? 133 TRP A CA  1 
ATOM   1061 C C   . TRP A 1 133 ? -14.46100 -11.56100 -35.80600 1.000 29.19824  ? 133 TRP A C   1 
ATOM   1062 O O   . TRP A 1 133 ? -15.68100 -11.55100 -35.99700 1.000 30.22468  ? 133 TRP A O   1 
ATOM   1063 C CB  . TRP A 1 133 ? -13.01100 -10.06600 -37.18100 1.000 29.41142  ? 133 TRP A CB  1 
ATOM   1064 C CG  . TRP A 1 133 ? -12.17700 -9.91700  -38.40400 1.000 29.44564  ? 133 TRP A CG  1 
ATOM   1065 C CD1 . TRP A 1 133 ? -12.61700 -9.64700  -39.65600 1.000 30.72210  ? 133 TRP A CD1 1 
ATOM   1066 C CD2 . TRP A 1 133 ? -10.75800 -10.08300 -38.49800 1.000 28.49289  ? 133 TRP A CD2 1 
ATOM   1067 N NE1 . TRP A 1 133 ? -11.56100 -9.61600  -40.53600 1.000 30.85896  ? 133 TRP A NE1 1 
ATOM   1068 C CE2 . TRP A 1 133 ? -10.40400 -9.87800  -39.85100 1.000 29.42984  ? 133 TRP A CE2 1 
ATOM   1069 C CE3 . TRP A 1 133 ? -9.75400  -10.37500 -37.57300 1.000 26.95850  ? 133 TRP A CE3 1 
ATOM   1070 C CZ2 . TRP A 1 133 ? -9.08500  -9.94600  -40.30400 1.000 29.25877  ? 133 TRP A CZ2 1 
ATOM   1071 C CZ3 . TRP A 1 133 ? -8.42600  -10.44700 -38.02700 1.000 26.62161  ? 133 TRP A CZ3 1 
ATOM   1072 C CH2 . TRP A 1 133 ? -8.11400  -10.22700 -39.38400 1.000 27.81912  ? 133 TRP A CH2 1 
ATOM   1073 N N   . THR A 1 134 ? -13.91600 -11.61700 -34.59500 1.000 34.75417  ? 134 THR A N   1 
ATOM   1074 C CA  . THR A 1 134 ? -14.67900 -11.35200 -33.38300 1.000 35.45425  ? 134 THR A CA  1 
ATOM   1075 C C   . THR A 1 134 ? -14.05300 -10.15100 -32.70000 1.000 35.18843  ? 134 THR A C   1 
ATOM   1076 O O   . THR A 1 134 ? -12.85300 -10.15700 -32.40800 1.000 34.28043  ? 134 THR A O   1 
ATOM   1077 C CB  . THR A 1 134 ? -14.69400 -12.55900 -32.44800 1.000 35.42793  ? 134 THR A CB  1 
ATOM   1078 O OG1 . THR A 1 134 ? -15.27900 -13.65500 -33.14400 1.000 35.27002  ? 134 THR A OG1 1 
ATOM   1079 C CG2 . THR A 1 134 ? -15.57000 -12.25200 -31.24200 1.000 35.90694  ? 134 THR A CG2 1 
ATOM   1080 N N   . ALA A 1 135 ? -14.86800 -9.12500  -32.46000 1.000 35.30950  ? 135 ALA A N   1 
ATOM   1081 C CA  . ALA A 1 135 ? -14.42900 -7.88800  -31.84600 1.000 36.07538  ? 135 ALA A CA  1 
ATOM   1082 C C   . ALA A 1 135 ? -14.87600 -7.85900  -30.39300 1.000 37.14919  ? 135 ALA A C   1 
ATOM   1083 O O   . ALA A 1 135 ? -16.01800 -8.19500  -30.08800 1.000 37.23868  ? 135 ALA A O   1 
ATOM   1084 C CB  . ALA A 1 135 ? -15.00600 -6.68100  -32.58100 1.000 37.23078  ? 135 ALA A CB  1 
ATOM   1085 N N   . ALA A 1 136 ? -13.98000 -7.39800  -29.51200 1.000 39.45473  ? 136 ALA A N   1 
ATOM   1086 C CA  . ALA A 1 136 ? -14.20500 -7.44100  -28.07000 1.000 40.24956  ? 136 ALA A CA  1 
ATOM   1087 C C   . ALA A 1 136 ? -14.97300 -6.24000  -27.52600 1.000 42.84461  ? 136 ALA A C   1 
ATOM   1088 O O   . ALA A 1 136 ? -15.52000 -6.32800  -26.42600 1.000 43.30256  ? 136 ALA A O   1 
ATOM   1089 C CB  . ALA A 1 136 ? -12.86600 -7.52900  -27.33300 1.000 40.21798  ? 136 ALA A CB  1 
ATOM   1090 N N   . ASP A 1 137 ? -15.00000 -5.11000  -28.23300 1.000 39.82056  ? 137 ASP A N   1 
ATOM   1091 C CA  . ASP A 1 137 ? -15.73000 -3.94300  -27.74100 1.000 42.12084  ? 137 ASP A CA  1 
ATOM   1092 C C   . ASP A 1 137 ? -16.11400 -3.07700  -28.93800 1.000 42.91041  ? 137 ASP A C   1 
ATOM   1093 O O   . ASP A 1 137 ? -15.90000 -3.45900  -30.09400 1.000 41.84975  ? 137 ASP A O   1 
ATOM   1094 C CB  . ASP A 1 137 ? -14.90900 -3.18200  -26.68900 1.000 43.34730  ? 137 ASP A CB  1 
ATOM   1095 C CG  . ASP A 1 137 ? -13.51700 -2.77000  -27.19200 1.000 43.66839  ? 137 ASP A CG  1 
ATOM   1096 O OD1 . ASP A 1 137 ? -13.34600 -2.56800  -28.41300 1.000 42.62090  ? 137 ASP A OD1 1 
ATOM   1097 O OD2 . ASP A 1 137 ? -12.58500 -2.63900  -26.36000 1.000 44.07897  ? 137 ASP A OD2 1 
ATOM   1098 N N   . THR A 1 138 ? -16.68600 -1.89900  -28.65400 1.000 45.18173  ? 138 THR A N   1 
ATOM   1099 C CA  . THR A 1 138 ? -17.19300 -1.06300  -29.73700 1.000 45.80549  ? 138 THR A CA  1 
ATOM   1100 C C   . THR A 1 138 ? -16.07100 -0.37300  -30.50700 1.000 46.45031  ? 138 THR A C   1 
ATOM   1101 O O   . THR A 1 138 ? -16.25800 -0.03300  -31.68300 1.000 46.31345  ? 138 THR A O   1 
ATOM   1102 C CB  . THR A 1 138 ? -18.18500 -0.02600  -29.20300 1.000 47.67677  ? 138 THR A CB  1 
ATOM   1103 O OG1 . THR A 1 138 ? -17.62500 0.62000   -28.05500 1.000 49.95336  ? 138 THR A OG1 1 
ATOM   1104 C CG2 . THR A 1 138 ? -19.51200 -0.68400  -28.82200 1.000 47.30830  ? 138 THR A CG2 1 
ATOM   1105 N N   . ALA A 1 139 ? -14.91500 -0.14000  -29.87800 1.000 42.44193  ? 139 ALA A N   1 
ATOM   1106 C CA  . ALA A 1 139 ? -13.77200 0.37300   -30.62800 1.000 42.02083  ? 139 ALA A CA  1 
ATOM   1107 C C   . ALA A 1 139 ? -13.32000 -0.64300  -31.66000 1.000 39.15206  ? 139 ALA A C   1 
ATOM   1108 O O   . ALA A 1 139 ? -13.11900 -0.31100  -32.83500 1.000 38.33618  ? 139 ALA A O   1 
ATOM   1109 C CB  . ALA A 1 139 ? -12.61500 0.72100   -29.68600 1.000 41.84975  ? 139 ALA A CB  1 
ATOM   1110 N N   . ALA A 1 140 ? -13.17000 -1.89600  -31.22800 1.000 34.66995  ? 140 ALA A N   1 
ATOM   1111 C CA  . ALA A 1 140 ? -12.75900 -2.96600  -32.12600 1.000 31.95383  ? 140 ALA A CA  1 
ATOM   1112 C C   . ALA A 1 140 ? -13.79900 -3.23400  -33.20900 1.000 32.25124  ? 140 ALA A C   1 
ATOM   1113 O O   . ALA A 1 140 ? -13.44900 -3.73000  -34.28900 1.000 30.85896  ? 140 ALA A O   1 
ATOM   1114 C CB  . ALA A 1 140 ? -12.48500 -4.23500  -31.31800 1.000 30.00886  ? 140 ALA A CB  1 
ATOM   1115 N N   . GLN A 1 141 ? -15.07600 -2.91500  -32.95000 1.000 36.83600  ? 141 GLN A N   1 
ATOM   1116 C CA  . GLN A 1 141 ? -16.08100 -3.03300  -34.00100 1.000 37.49134  ? 141 GLN A CA  1 
ATOM   1117 C C   . GLN A 1 141 ? -15.80800 -2.06800  -35.15000 1.000 38.35723  ? 141 GLN A C   1 
ATOM   1118 O O   . GLN A 1 141 ? -16.12900 -2.37200  -36.29900 1.000 38.38092  ? 141 GLN A O   1 
ATOM   1119 C CB  . GLN A 1 141 ? -17.48400 -2.82200  -33.42600 1.000 38.76781  ? 141 GLN A CB  1 
ATOM   1120 C CG  . GLN A 1 141 ? -17.88500 -3.96900  -32.51500 1.000 37.64925  ? 141 GLN A CG  1 
ATOM   1121 C CD  . GLN A 1 141 ? -19.30300 -3.87600  -31.99000 1.000 39.53369  ? 141 GLN A CD  1 
ATOM   1122 O OE1 . GLN A 1 141 ? -19.91900 -2.81800  -31.99200 1.000 41.62604  ? 141 GLN A OE1 1 
ATOM   1123 N NE2 . GLN A 1 141 ? -19.84200 -5.01500  -31.55500 1.000 39.80214  ? 141 GLN A NE2 1 
ATOM   1124 N N   . ILE A 1 142 ? -15.20600 -0.91500  -34.87100 1.000 37.60188  ? 142 ILE A N   1 
ATOM   1125 C CA  . ILE A 1 142 ? -14.77900 -0.03700  -35.95500 1.000 37.93350  ? 142 ILE A CA  1 
ATOM   1126 C C   . ILE A 1 142 ? -13.70800 -0.72700  -36.79100 1.000 36.10170  ? 142 ILE A C   1 
ATOM   1127 O O   . ILE A 1 142 ? -13.80400 -0.79500  -38.02400 1.000 36.28593  ? 142 ILE A O   1 
ATOM   1128 C CB  . ILE A 1 142 ? -14.27300 1.30500   -35.40800 1.000 38.41513  ? 142 ILE A CB  1 
ATOM   1129 C CG1 . ILE A 1 142 ? -15.32300 1.96300   -34.50100 1.000 40.32589  ? 142 ILE A CG1 1 
ATOM   1130 C CG2 . ILE A 1 142 ? -13.88900 2.21600   -36.58400 1.000 37.54134  ? 142 ILE A CG2 1 
ATOM   1131 C CD1 . ILE A 1 142 ? -14.80500 3.20500   -33.79800 1.000 40.89438  ? 142 ILE A CD1 1 
ATOM   1132 N N   . THR A 1 143 ? -12.67600 -1.25600  -36.12200 1.000 35.35950  ? 143 THR A N   1 
ATOM   1133 C CA  . THR A 1 143 ? -11.61100 -1.97200  -36.81500 1.000 32.80920  ? 143 THR A CA  1 
ATOM   1134 C C   . THR A 1 143 ? -12.16600 -3.11800  -37.65500 1.000 33.03554  ? 143 THR A C   1 
ATOM   1135 O O   . THR A 1 143 ? -11.77600 -3.28800  -38.81800 1.000 33.22767  ? 143 THR A O   1 
ATOM   1136 C CB  . THR A 1 143 ? -10.60000 -2.45900  -35.79100 1.000 31.08531  ? 143 THR A CB  1 
ATOM   1137 O OG1 . THR A 1 143 ? -10.03600 -1.31600  -35.13200 1.000 31.67485  ? 143 THR A OG1 1 
ATOM   1138 C CG2 . THR A 1 143 ? -9.48900  -3.27200  -36.43500 1.000 28.88241  ? 143 THR A CG2 1 
ATOM   1139 N N   . GLN A 1 144 ? -13.11900 -3.87400  -37.10200 1.000 35.72007  ? 144 GLN A N   1 
ATOM   1140 C CA  . GLN A 1 144 ? -13.74600 -4.96300  -37.84500 1.000 35.45425  ? 144 GLN A CA  1 
ATOM   1141 C C   . GLN A 1 144 ? -14.41300 -4.46400  -39.12000 1.000 37.13866  ? 144 GLN A C   1 
ATOM   1142 O O   . GLN A 1 144 ? -14.26300 -5.07500  -40.18100 1.000 37.12287  ? 144 GLN A O   1 
ATOM   1143 C CB  . GLN A 1 144 ? -14.76800 -5.68200  -36.96500 1.000 35.00683  ? 144 GLN A CB  1 
ATOM   1144 C CG  . GLN A 1 144 ? -15.59700 -6.76100  -37.67900 1.000 35.23844  ? 144 GLN A CG  1 
ATOM   1145 C CD  . GLN A 1 144 ? -16.45600 -7.53400  -36.70000 1.000 35.03052  ? 144 GLN A CD  1 
ATOM   1146 O OE1 . GLN A 1 144 ? -16.38500 -7.29100  -35.49300 1.000 35.07263  ? 144 GLN A OE1 1 
ATOM   1147 N NE2 . GLN A 1 144 ? -17.26600 -8.46600  -37.20200 1.000 35.13316  ? 144 GLN A NE2 1 
ATOM   1148 N N   . ARG A 1 145 ? -15.13900 -3.35600  -39.03800 1.000 39.25471  ? 145 ARG A N   1 
ATOM   1149 C CA  . ARG A 1 145 ? -15.81000 -2.79000  -40.23400 1.000 40.36010  ? 145 ARG A CA  1 
ATOM   1150 C C   . ARG A 1 145 ? -14.75100 -2.43500  -41.28500 1.000 39.99690  ? 145 ARG A C   1 
ATOM   1151 O O   . ARG A 1 145 ? -14.95400 -2.76000  -42.45300 1.000 39.71266  ? 145 ARG A O   1 
ATOM   1152 C CB  . ARG A 1 145 ? -16.70100 -1.61900  -39.82100 1.000 41.27337  ? 145 ARG A CB  1 
ATOM   1153 C CG  . ARG A 1 145 ? -17.81000 -2.01400  -38.86000 1.000 41.88923  ? 145 ARG A CG  1 
ATOM   1154 C CD  . ARG A 1 145 ? -18.86700 -0.94800  -38.68100 1.000 44.55271  ? 145 ARG A CD  1 
ATOM   1155 N NE  . ARG A 1 145 ? -18.50700 0.08600   -37.72500 1.000 44.58429  ? 145 ARG A NE  1 
ATOM   1156 C CZ  . ARG A 1 145 ? -18.27100 1.34400   -38.05800 1.000 45.34491  ? 145 ARG A CZ  1 
ATOM   1157 N NH1 . ARG A 1 145 ? -18.34700 1.70900   -39.32500 1.000 44.63956  ? 145 ARG A NH1 1 
ATOM   1158 N NH2 . ARG A 1 145 ? -17.95800 2.22800   -37.13100 1.000 46.33450  ? 145 ARG A NH2 1 
ATOM   1159 N N   . LYS A 1 146 ? -13.64400 -1.84000  -40.85900 1.000 37.31237  ? 146 LYS A N   1 
ATOM   1160 C CA  . LYS A 1 146 ? -12.58300 -1.49000  -41.80500 1.000 36.12275  ? 146 LYS A CA  1 
ATOM   1161 C C   . LYS A 1 146 ? -11.94600 -2.73600  -42.41200 1.000 35.56479  ? 146 LYS A C   1 
ATOM   1162 O O   . LYS A 1 146 ? -11.71800 -2.80000  -43.62100 1.000 35.10947  ? 146 LYS A O   1 
ATOM   1163 C CB  . LYS A 1 146 ? -11.51800 -0.63000  -41.11300 1.000 34.75943  ? 146 LYS A CB  1 
ATOM   1164 C CG  . LYS A 1 146 ? -12.02700 0.73300   -40.66900 1.000 35.72007  ? 146 LYS A CG  1 
ATOM   1165 C CD  . LYS A 1 146 ? -10.96200 1.49200   -39.87300 1.000 34.70416  ? 146 LYS A CD  1 
ATOM   1166 C CE  . LYS A 1 146 ? -9.99800  2.21900   -40.77600 1.000 33.64614  ? 146 LYS A CE  1 
ATOM   1167 N NZ  . LYS A 1 146 ? -9.00800  3.08900   -40.03300 1.000 32.64339  ? 146 LYS A NZ  1 
ATOM   1168 N N   . TRP A 1 147 ? -11.64500 -3.73700  -41.58400 1.000 36.56754  ? 147 TRP A N   1 
ATOM   1169 C CA  . TRP A 1 147 ? -10.98400 -4.93100  -42.10200 1.000 35.80429  ? 147 TRP A CA  1 
ATOM   1170 C C   . TRP A 1 147 ? -11.91700 -5.75700  -42.97200 1.000 35.81482  ? 147 TRP A C   1 
ATOM   1171 O O   . TRP A 1 147 ? -11.45500 -6.46900  -43.87100 1.000 35.49636  ? 147 TRP A O   1 
ATOM   1172 C CB  . TRP A 1 147 ? -10.44200 -5.77600  -40.95400 1.000 33.22767  ? 147 TRP A CB  1 
ATOM   1173 C CG  . TRP A 1 147 ? -9.32700  -5.12300  -40.23000 1.000 31.72222  ? 147 TRP A CG  1 
ATOM   1174 C CD1 . TRP A 1 147 ? -8.76200  -3.88500  -40.50700 1.000 31.50641  ? 147 TRP A CD1 1 
ATOM   1175 C CD2 . TRP A 1 147 ? -8.59200  -5.65900  -39.13000 1.000 29.30088  ? 147 TRP A CD2 1 
ATOM   1176 N NE1 . TRP A 1 147 ? -7.75000  -3.63200  -39.62500 1.000 29.41668  ? 147 TRP A NE1 1 
ATOM   1177 C CE2 . TRP A 1 147 ? -7.61600  -4.70600  -38.77600 1.000 28.25339  ? 147 TRP A CE2 1 
ATOM   1178 C CE3 . TRP A 1 147 ? -8.66200  -6.85900  -38.40800 1.000 28.64028  ? 147 TRP A CE3 1 
ATOM   1179 C CZ2 . TRP A 1 147 ? -6.73600  -4.89900  -37.70200 1.000 26.90849  ? 147 TRP A CZ2 1 
ATOM   1180 C CZ3 . TRP A 1 147 ? -7.78200  -7.05500  -37.34700 1.000 27.14536  ? 147 TRP A CZ3 1 
ATOM   1181 C CH2 . TRP A 1 147 ? -6.82500  -6.07400  -37.01100 1.000 26.65583  ? 147 TRP A CH2 1 
ATOM   1182 N N   . GLU A 1 148 ? -13.22300 -5.68500  -42.72100 1.000 35.48057  ? 148 GLU A N   1 
ATOM   1183 C CA  . GLU A 1 148 ? -14.17200 -6.32300  -43.62800 1.000 36.00695  ? 148 GLU A CA  1 
ATOM   1184 C C   . GLU A 1 148 ? -14.19800 -5.59800  -44.96200 1.000 36.58860  ? 148 GLU A C   1 
ATOM   1185 O O   . GLU A 1 148 ? -14.18600 -6.23200  -46.02100 1.000 36.67545  ? 148 GLU A O   1 
ATOM   1186 C CB  . GLU A 1 148 ? -15.57300 -6.37200  -42.99700 1.000 36.33330  ? 148 GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 148 ? -15.62300 -7.33200  -41.79300 1.000 35.24633  ? 148 GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 148 ? -16.92700 -7.30900  -41.00100 0.830 35.90430  ? 148 GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 148 ? -17.73100 -6.36500  -41.11900 1.000 37.43344  ? 148 GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 148 ? -17.13900 -8.24000  -40.21500 0.820 34.83312  ? 148 GLU A OE2 1 
ATOM   1191 N N   . ALA A 1 149 ? -14.20800 -4.26300  -44.93200 1.000 32.46442  ? 149 ALA A N   1 
ATOM   1192 C CA  . ALA A 1 149 ? -14.28600 -3.51600  -46.18100 1.000 33.10397  ? 149 ALA A CA  1 
ATOM   1193 C C   . ALA A 1 149 ? -13.01300 -3.66700  -47.01100 1.000 32.49074  ? 149 ALA A C   1 
ATOM   1194 O O   . ALA A 1 149 ? -13.06500 -3.56000  -48.24400 1.000 33.76457  ? 149 ALA A O   1 
ATOM   1195 C CB  . ALA A 1 149 ? -14.58900 -2.05000  -45.89200 1.000 33.65404  ? 149 ALA A CB  1 
ATOM   1196 N N   . ALA A 1 150 ? -11.88100 -3.93000  -46.36500 1.000 38.05983  ? 150 ALA A N   1 
ATOM   1197 C CA  . ALA A 1 150 ? -10.59800 -4.11500  -47.03000 1.000 37.23868  ? 150 ALA A CA  1 
ATOM   1198 C C   . ALA A 1 150 ? -10.26900 -5.57400  -47.28200 1.000 37.25973  ? 150 ALA A C   1 
ATOM   1199 O O   . ALA A 1 150 ? -9.19400  -5.85800  -47.81300 1.000 36.61755  ? 150 ALA A O   1 
ATOM   1200 C CB  . ALA A 1 150 ? -9.46600  -3.50200  -46.19600 1.000 36.39910  ? 150 ALA A CB  1 
ATOM   1201 N N   . ARG A 1 151 ? -11.14700 -6.49800  -46.87200 1.000 43.60523  ? 151 ARG A N   1 
ATOM   1202 C CA  . ARG A 1 151 ? -10.93200 -7.94000  -47.02100 1.000 43.42626  ? 151 ARG A CA  1 
ATOM   1203 C C   . ARG A 1 151 ? -9.60400  -8.37100  -46.39900 1.000 42.55247  ? 151 ARG A C   1 
ATOM   1204 O O   . ARG A 1 151 ? -8.80900  -9.09400  -46.99900 1.000 42.25243  ? 151 ARG A O   1 
ATOM   1205 C CB  . ARG A 1 151 ? -11.01500 -8.35700  -48.49500 1.000 44.05002  ? 151 ARG A CB  1 
ATOM   1206 C CG  . ARG A 1 151 ? -12.42100 -8.37700  -49.08200 1.000 45.92393  ? 151 ARG A CG  1 
ATOM   1207 C CD  . ARG A 1 151 ? -12.88800 -7.02000  -49.57200 1.000 46.68454  ? 151 ARG A CD  1 
ATOM   1208 N NE  . ARG A 1 151 ? -14.02300 -7.12500  -50.49200 1.000 48.28474  ? 151 ARG A NE  1 
ATOM   1209 C CZ  . ARG A 1 151 ? -15.30200 -7.03900  -50.13800 0.000 47.80310  ? 151 ARG A CZ  1 
ATOM   1210 N NH1 . ARG A 1 151 ? -15.67200 -6.82600  -48.88200 1.000 47.17145  ? 151 ARG A NH1 1 
ATOM   1211 N NH2 . ARG A 1 151 ? -16.23700 -7.17300  -51.06700 1.000 49.11642  ? 151 ARG A NH2 1 
ATOM   1212 N N   . VAL A 1 152 ? -9.37200  -7.93800  -45.16000 1.000 35.78587  ? 152 VAL A N   1 
ATOM   1213 C CA  . VAL A 1 152 ? -8.10800  -8.26100  -44.50900 1.000 35.33845  ? 152 VAL A CA  1 
ATOM   1214 C C   . VAL A 1 152 ? -8.02800  -9.75500  -44.16800 1.000 34.83312  ? 152 VAL A C   1 
ATOM   1215 O O   . VAL A 1 152 ? -6.93500  -10.34300 -44.16700 1.000 34.14357  ? 152 VAL A O   1 
ATOM   1216 C CB  . VAL A 1 152 ? -7.90400  -7.37200  -43.26600 1.000 34.67521  ? 152 VAL A CB  1 
ATOM   1217 C CG1 . VAL A 1 152 ? -6.66100  -7.79900  -42.48900 1.000 32.51969  ? 152 VAL A CG1 1 
ATOM   1218 C CG2 . VAL A 1 152 ? -7.76000  -5.91300  -43.67700 1.000 34.35675  ? 152 VAL A CG2 1 
ATOM   1219 N N   . ALA A 1 153 ? -9.15900  -10.40200 -43.89600 1.000 34.34886  ? 153 ALA A N   1 
ATOM   1220 C CA  . ALA A 1 153 ? -9.10000  -11.82100 -43.55600 1.000 34.03303  ? 153 ALA A CA  1 
ATOM   1221 C C   . ALA A 1 153 ? -8.49800  -12.64000 -44.69800 1.000 34.46992  ? 153 ALA A C   1 
ATOM   1222 O O   . ALA A 1 153 ? -7.70300  -13.55100 -44.44900 1.000 34.26463  ? 153 ALA A O   1 
ATOM   1223 C CB  . ALA A 1 153 ? -10.49200 -12.35500 -43.19700 1.000 34.01987  ? 153 ALA A CB  1 
ATOM   1224 N N   . GLU A 1 154 ? -8.86100  -12.32400 -45.95100 1.000 43.49469  ? 154 GLU A N   1 
ATOM   1225 C CA  . GLU A 1 154 ? -8.33300  -13.04800 -47.11000 1.000 43.97633  ? 154 GLU A CA  1 
ATOM   1226 C C   . GLU A 1 154 ? -6.81100  -13.04600 -47.12500 1.000 43.48942  ? 154 GLU A C   1 
ATOM   1227 O O   . GLU A 1 154 ? -6.18400  -14.05200 -47.47800 1.000 43.96053  ? 154 GLU A O   1 
ATOM   1228 C CB  . GLU A 1 154 ? -8.85800  -12.43700 -48.41300 1.000 44.81590  ? 154 GLU A CB  1 
ATOM   1229 C CG  . GLU A 1 154 ? -10.36100 -12.47800 -48.60700 1.000 46.14501  ? 154 GLU A CG  1 
ATOM   1230 C CD  . GLU A 1 154 ? -10.81300 -11.94500 -49.97000 1.000 48.33474  ? 154 GLU A CD  1 
ATOM   1231 O OE1 . GLU A 1 154 ? -10.04100 -11.21600 -50.65300 1.000 47.91627  ? 154 GLU A OE1 1 
ATOM   1232 O OE2 . GLU A 1 154 ? -11.96200 -12.25500 -50.36200 1.000 49.75333  ? 154 GLU A OE2 1 
ATOM   1233 N N   . GLN A 1 155 ? -6.20100  -11.91300 -46.75500 1.000 44.98171  ? 155 GLN A N   1 
ATOM   1234 C CA  . GLN A 1 155 ? -4.74300  -11.81500 -46.72200 1.000 44.73431  ? 155 GLN A CA  1 
ATOM   1235 C C   . GLN A 1 155 ? -4.14800  -12.64700 -45.59200 1.000 44.08423  ? 155 GLN A C   1 
ATOM   1236 O O   . GLN A 1 155 ? -3.12000  -13.30800 -45.78100 1.000 44.32637  ? 155 GLN A O   1 
ATOM   1237 C CB  . GLN A 1 155 ? -4.31500  -10.35700 -46.57800 1.000 44.23425  ? 155 GLN A CB  1 
ATOM   1238 C CG  . GLN A 1 155 ? -4.69200  -9.48800  -47.75400 1.000 44.97381  ? 155 GLN A CG  1 
ATOM   1239 C CD  . GLN A 1 155 ? -4.66700  -8.03500  -47.38200 1.000 44.47375  ? 155 GLN A CD  1 
ATOM   1240 O OE1 . GLN A 1 155 ? -3.64200  -7.51600  -46.94300 1.000 43.96580  ? 155 GLN A OE1 1 
ATOM   1241 N NE2 . GLN A 1 155 ? -5.80500  -7.37100  -47.51600 1.000 44.77379  ? 155 GLN A NE2 1 
ATOM   1242 N N   . LEU A 1 156 ? -4.77200  -12.61500 -44.40500 1.000 33.18029  ? 156 LEU A N   1 
ATOM   1243 C CA  . LEU A 1 156 ? -4.33600  -13.49100 -43.32700 1.000 32.65918  ? 156 LEU A CA  1 
ATOM   1244 C C   . LEU A 1 156 ? -4.46400  -14.94500 -43.73700 1.000 33.50402  ? 156 LEU A C   1 
ATOM   1245 O O   . LEU A 1 156 ? -3.56800  -15.75800 -43.46900 1.000 33.43559  ? 156 LEU A O   1 
ATOM   1246 C CB  . LEU A 1 156 ? -5.15400  -13.24200 -42.05400 1.000 31.70380  ? 156 LEU A CB  1 
ATOM   1247 C CG  . LEU A 1 156 ? -4.52000  -12.34200 -40.98800 1.000 30.66683  ? 156 LEU A CG  1 
ATOM   1248 C CD1 . LEU A 1 156 ? -3.31800  -13.02100 -40.38000 1.000 30.78001  ? 156 LEU A CD1 1 
ATOM   1249 C CD2 . LEU A 1 156 ? -4.13200  -10.96300 -41.55000 1.000 30.60367  ? 156 LEU A CD2 1 
ATOM   1250 N N   A ARG A 1 157 ? -5.58200  -15.30000 -44.38100 0.520 31.76170  ? 157 ARG A N   1 
ATOM   1251 N N   B ARG A 1 157 ? -5.57500  -15.29200 -44.38600 0.480 31.76697  ? 157 ARG A N   1 
ATOM   1252 C CA  A ARG A 1 157 ? -5.81800  -16.69300 -44.74800 0.520 32.54864  ? 157 ARG A CA  1 
ATOM   1253 C CA  B ARG A 1 157 ? -5.82000  -16.67900 -44.75200 0.480 32.52758  ? 157 ARG A CA  1 
ATOM   1254 C C   A ARG A 1 157 ? -4.79500  -17.16600 -45.77400 0.520 33.34347  ? 157 ARG A C   1 
ATOM   1255 C C   B ARG A 1 157 ? -4.79800  -17.16200 -45.77300 0.480 33.33558  ? 157 ARG A C   1 
ATOM   1256 O O   A ARG A 1 157 ? -4.26300  -18.27900 -45.66200 0.520 33.69878  ? 157 ARG A O   1 
ATOM   1257 O O   B ARG A 1 157 ? -4.27200  -18.27700 -45.65800 0.480 33.70404  ? 157 ARG A O   1 
ATOM   1258 C CB  A ARG A 1 157 ? -7.24500  -16.86400 -45.27700 0.520 32.81446  ? 157 ARG A CB  1 
ATOM   1259 C CB  B ARG A 1 157 ? -7.23800  -16.81600 -45.29200 0.480 32.80920  ? 157 ARG A CB  1 
ATOM   1260 C CG  A ARG A 1 157 ? -7.60100  -18.29100 -45.70600 0.520 33.58297  ? 157 ARG A CG  1 
ATOM   1261 C CG  B ARG A 1 157 ? -7.70600  -18.23400 -45.47300 0.480 33.39874  ? 157 ARG A CG  1 
ATOM   1262 C CD  A ARG A 1 157 ? -9.07700  -18.46800 -46.09400 0.520 34.06461  ? 157 ARG A CD  1 
ATOM   1263 C CD  B ARG A 1 157 ? -9.20500  -18.28200 -45.66900 0.480 33.59087  ? 157 ARG A CD  1 
ATOM   1264 N NE  A ARG A 1 157 ? -9.33700  -19.82700 -46.56800 0.520 35.16737  ? 157 ARG A NE  1 
ATOM   1265 N NE  B ARG A 1 157 ? -9.62500  -17.81700 -46.98600 0.480 34.36465  ? 157 ARG A NE  1 
ATOM   1266 C CZ  A ARG A 1 157 ? -10.52700 -20.32900 -46.89600 0.520 35.70691  ? 157 ARG A CZ  1 
ATOM   1267 C CZ  B ARG A 1 157 ? -10.19200 -16.64200 -47.22600 0.480 34.48308  ? 157 ARG A CZ  1 
ATOM   1268 N NH1 A ARG A 1 157 ? -11.64700 -19.62900 -46.76300 0.520 34.83839  ? 157 ARG A NH1 1 
ATOM   1269 N NH1 B ARG A 1 157 ? -10.36900 -15.74400 -46.26300 0.480 33.41453  ? 157 ARG A NH1 1 
ATOM   1270 N NH2 A ARG A 1 157 ? -10.59500 -21.56700 -47.37200 0.520 35.58848  ? 157 ARG A NH2 1 
ATOM   1271 N NH2 B ARG A 1 157 ? -10.58300 -16.35400 -48.46200 0.480 35.38056  ? 157 ARG A NH2 1 
ATOM   1272 N N   . ALA A 1 158 ? -4.48200  -16.32000 -46.76100 1.000 30.35101  ? 158 ALA A N   1 
ATOM   1273 C CA  . ALA A 1 158 ? -3.49700  -16.69600 -47.76900 1.000 31.38534  ? 158 ALA A CA  1 
ATOM   1274 C C   . ALA A 1 158 ? -2.14700  -16.96500 -47.13300 1.000 31.35113  ? 158 ALA A C   1 
ATOM   1275 O O   . ALA A 1 158 ? -1.45000  -17.91500 -47.51200 1.000 32.68813  ? 158 ALA A O   1 
ATOM   1276 C CB  . ALA A 1 158 ? -3.38200  -15.59900 -48.82200 1.000 31.66959  ? 158 ALA A CB  1 
ATOM   1277 N N   . TYR A 1 159 ? -1.77500  -16.15600 -46.14000 1.000 29.17455  ? 159 TYR A N   1 
ATOM   1278 C CA  . TYR A 1 159 ? -0.51100  -16.36000 -45.44500 1.000 29.44300  ? 159 TYR A CA  1 
ATOM   1279 C C   . TYR A 1 159 ? -0.55100  -17.62000 -44.58700 1.000 29.77725  ? 159 TYR A C   1 
ATOM   1280 O O   . TYR A 1 159 ? 0.36300   -18.45400 -44.64000 1.000 30.68789  ? 159 TYR A O   1 
ATOM   1281 C CB  . TYR A 1 159 ? -0.19700  -15.14600 -44.57800 1.000 28.70871  ? 159 TYR A CB  1 
ATOM   1282 C CG  . TYR A 1 159 ? 0.89900   -15.38000 -43.58300 1.000 29.25877  ? 159 TYR A CG  1 
ATOM   1283 C CD1 . TYR A 1 159 ? 2.23400   -15.33800 -43.97600 1.000 30.60367  ? 159 TYR A CD1 1 
ATOM   1284 C CD2 . TYR A 1 159 ? 0.60700   -15.65800 -42.25800 1.000 28.30603  ? 159 TYR A CD2 1 
ATOM   1285 C CE1 . TYR A 1 159 ? 3.24700   -15.52900 -43.07000 1.000 31.13794  ? 159 TYR A CE1 1 
ATOM   1286 C CE2 . TYR A 1 159 ? 1.60400   -15.86400 -41.34600 1.000 28.80609  ? 159 TYR A CE2 1 
ATOM   1287 C CZ  . TYR A 1 159 ? 2.93000   -15.80900 -41.74500 1.000 30.25363  ? 159 TYR A CZ  1 
ATOM   1288 O OH  . TYR A 1 159 ? 3.93500   -16.02000 -40.82100 1.000 30.72210  ? 159 TYR A OH  1 
ATOM   1289 N N   . LEU A 1 160 ? -1.60500  -17.76900 -43.78800 1.000 31.45904  ? 160 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 160 ? -1.68100  -18.90500 -42.87600 1.000 31.85645  ? 160 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 160 ? -1.70100  -20.23200 -43.63700 1.000 33.23556  ? 160 LEU A C   1 
ATOM   1292 O O   . LEU A 1 160 ? -1.01900  -21.17700 -43.24400 1.000 34.31201  ? 160 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 160 ? -2.89900  -18.75100 -41.97000 1.000 30.77737  ? 160 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 160 ? -2.79100  -17.52400 -41.04400 1.000 29.92201  ? 160 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 160 ? -4.10500  -17.24500 -40.35900 1.000 29.00348  ? 160 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 160 ? -1.68200  -17.66900 -40.00200 1.000 29.91411  ? 160 LEU A CD2 1 
ATOM   1297 N N   . GLU A 1 161 ? -2.43300  -20.30700 -44.75500 1.000 37.90718  ? 161 GLU A N   1 
ATOM   1298 C CA  . GLU A 1 161 ? -2.45900  -21.53200 -45.55600 1.000 39.18891  ? 161 GLU A CA  1 
ATOM   1299 C C   . GLU A 1 161 ? -1.17100  -21.74000 -46.34300 1.000 40.30483  ? 161 GLU A C   1 
ATOM   1300 O O   . GLU A 1 161 ? -0.85000  -22.88000 -46.69100 1.000 41.11809  ? 161 GLU A O   1 
ATOM   1301 C CB  . GLU A 1 161 ? -3.61300  -21.51500 -46.55800 1.000 39.17838  ? 161 GLU A CB  1 
ATOM   1302 C CG  . GLU A 1 161 ? -5.01900  -21.38700 -46.01900 1.000 39.27050  ? 161 GLU A CG  1 
ATOM   1303 C CD  . GLU A 1 161 ? -6.04800  -21.27000 -47.14900 1.000 39.40736  ? 161 GLU A CD  1 
ATOM   1304 O OE1 . GLU A 1 161 ? -5.66100  -21.08100 -48.33800 1.000 39.90742  ? 161 GLU A OE1 1 
ATOM   1305 O OE2 . GLU A 1 161 ? -7.25300  -21.36400 -46.87300 1.000 39.27313  ? 161 GLU A OE2 1 
ATOM   1306 N N   . GLY A 1 162 ? -0.44400  -20.66400 -46.64700 1.000 36.05432  ? 162 GLY A N   1 
ATOM   1307 C CA  . GLY A 1 162 ? 0.69100   -20.74500 -47.55100 1.000 37.49923  ? 162 GLY A CA  1 
ATOM   1308 C C   . GLY A 1 162 ? 2.04300   -20.56800 -46.88100 1.000 37.84927  ? 162 GLY A C   1 
ATOM   1309 O O   . GLY A 1 162 ? 2.61400   -21.53500 -46.37000 1.000 37.99666  ? 162 GLY A O   1 
ATOM   1310 N N   . LEU A 1 163 ? 2.56800   -19.33700 -46.88100 1.000 34.95156  ? 163 LEU A N   1 
ATOM   1311 C CA  . LEU A 1 163 ? 3.92600   -19.10500 -46.39400 1.000 34.64363  ? 163 LEU A CA  1 
ATOM   1312 C C   . LEU A 1 163 ? 4.10900   -19.57400 -44.95500 1.000 32.74866  ? 163 LEU A C   1 
ATOM   1313 O O   . LEU A 1 163 ? 5.18200   -20.08600 -44.59500 1.000 31.82224  ? 163 LEU A O   1 
ATOM   1314 C CB  . LEU A 1 163 ? 4.28200   -17.62300 -46.52400 1.000 35.67796  ? 163 LEU A CB  1 
ATOM   1315 C CG  . LEU A 1 163 ? 4.50600   -17.17400 -47.96800 1.000 38.20195  ? 163 LEU A CG  1 
ATOM   1316 C CD1 . LEU A 1 163 ? 4.71700   -15.65900 -48.05300 1.000 37.07550  ? 163 LEU A CD1 1 
ATOM   1317 C CD2 . LEU A 1 163 ? 5.69800   -17.91600 -48.52900 1.000 38.51778  ? 163 LEU A CD2 1 
ATOM   1318 N N   . CYS A 1 164 ? 3.08800   -19.39400 -44.11100 1.000 41.04439  ? 164 CYS A N   1 
ATOM   1319 C CA  . CYS A 1 164 ? 3.24400   -19.76700 -42.71200 1.000 38.70727  ? 164 CYS A CA  1 
ATOM   1320 C C   . CYS A 1 164 ? 3.60900   -21.24100 -42.58400 1.000 36.94917  ? 164 CYS A C   1 
ATOM   1321 O O   . CYS A 1 164 ? 4.62200   -21.58100 -41.96900 1.000 35.71744  ? 164 CYS A O   1 
ATOM   1322 C CB  . CYS A 1 164 ? 1.98100   -19.44200 -41.90900 1.000 37.91244  ? 164 CYS A CB  1 
ATOM   1323 S SG  . CYS A 1 164 ? 2.24800   -19.56900 -40.07200 1.000 35.30160  ? 164 CYS A SG  1 
ATOM   1324 N N   . VAL A 1 165 ? 2.82900   -22.13000 -43.20300 1.000 37.74400  ? 165 VAL A N   1 
ATOM   1325 C CA  A VAL A 1 165 ? 3.14700   -23.54500 -43.05500 0.380 36.19908  ? 165 VAL A CA  1 
ATOM   1326 C CA  B VAL A 1 165 ? 3.10300   -23.56600 -43.11700 0.620 36.27803  ? 165 VAL A CA  1 
ATOM   1327 C C   . VAL A 1 165 ? 4.38800   -23.91000 -43.85800 1.000 37.49397  ? 165 VAL A C   1 
ATOM   1328 O O   . VAL A 1 165 ? 5.17100   -24.76300 -43.42300 1.000 36.20960  ? 165 VAL A O   1 
ATOM   1329 C CB  A VAL A 1 165 ? 1.94300   -24.43400 -43.42000 0.380 36.07275  ? 165 VAL A CB  1 
ATOM   1330 C CB  B VAL A 1 165 ? 1.91100   -24.37100 -43.67000 0.620 36.51227  ? 165 VAL A CB  1 
ATOM   1331 C CG1 A VAL A 1 165 ? 0.78800   -24.15000 -42.48200 0.380 35.27528  ? 165 VAL A CG1 1 
ATOM   1332 C CG1 B VAL A 1 165 ? 2.21800   -25.85900 -43.67000 0.620 35.87009  ? 165 VAL A CG1 1 
ATOM   1333 C CG2 A VAL A 1 165 ? 1.51400   -24.24700 -44.86600 0.380 37.94139  ? 165 VAL A CG2 1 
ATOM   1334 C CG2 B VAL A 1 165 ? 0.65000   -24.09400 -42.87100 0.620 35.82272  ? 165 VAL A CG2 1 
ATOM   1335 N N   . GLU A 1 166 ? 4.61100   -23.26600 -45.01200 1.000 37.84138  ? 166 GLU A N   1 
ATOM   1336 C CA  . GLU A 1 166 ? 5.78100   -23.60500 -45.81500 1.000 39.66528  ? 166 GLU A CA  1 
ATOM   1337 C C   . GLU A 1 166 ? 7.07100   -23.27200 -45.06600 1.000 39.36261  ? 166 GLU A C   1 
ATOM   1338 O O   . GLU A 1 166 ? 7.98900   -24.09600 -45.00900 1.000 39.41262  ? 166 GLU A O   1 
ATOM   1339 C CB  . GLU A 1 166 ? 5.69700   -22.91100 -47.18400 1.000 41.60499  ? 166 GLU A CB  1 
ATOM   1340 C CG  . GLU A 1 166 ? 4.57000   -23.51300 -48.07200 1.000 42.86040  ? 166 GLU A CG  1 
ATOM   1341 C CD  . GLU A 1 166 ? 3.93100   -22.53900 -49.07900 1.000 45.36597  ? 166 GLU A CD  1 
ATOM   1342 O OE1 . GLU A 1 166 ? 4.35400   -21.36500 -49.17700 1.000 45.69495  ? 166 GLU A OE1 1 
ATOM   1343 O OE2 . GLU A 1 166 ? 2.98200   -22.96400 -49.78400 1.000 45.67916  ? 166 GLU A OE2 1 
ATOM   1344 N N   . TRP A 1 167 ? 7.13500   -22.09600 -44.43100 1.000 30.15098  ? 167 TRP A N   1 
ATOM   1345 C CA  . TRP A 1 167 ? 8.33800   -21.72400 -43.68800 1.000 30.09308  ? 167 TRP A CA  1 
ATOM   1346 C C   . TRP A 1 167 ? 8.48700   -22.54000 -42.41400 1.000 27.75333  ? 167 TRP A C   1 
ATOM   1347 O O   . TRP A 1 167 ? 9.60600   -22.88400 -42.01400 1.000 28.08758  ? 167 TRP A O   1 
ATOM   1348 C CB  . TRP A 1 167 ? 8.32000   -20.23300 -43.35300 1.000 30.80896  ? 167 TRP A CB  1 
ATOM   1349 C CG  . TRP A 1 167 ? 8.86700   -19.42700 -44.45800 1.000 33.75931  ? 167 TRP A CG  1 
ATOM   1350 C CD1 . TRP A 1 167 ? 8.18000   -18.61600 -45.30300 1.000 35.23054  ? 167 TRP A CD1 1 
ATOM   1351 C CD2 . TRP A 1 167 ? 10.23000  -19.39700 -44.87800 1.000 34.64889  ? 167 TRP A CD2 1 
ATOM   1352 N NE1 . TRP A 1 167 ? 9.04600   -18.04600 -46.22000 1.000 35.94115  ? 167 TRP A NE1 1 
ATOM   1353 C CE2 . TRP A 1 167 ? 10.31200  -18.51000 -45.97400 1.000 35.70428  ? 167 TRP A CE2 1 
ATOM   1354 C CE3 . TRP A 1 167 ? 11.39600  -20.00700 -44.41300 1.000 34.40149  ? 167 TRP A CE3 1 
ATOM   1355 C CZ2 . TRP A 1 167 ? 11.51800  -18.22700 -46.62200 1.000 35.95431  ? 167 TRP A CZ2 1 
ATOM   1356 C CZ3 . TRP A 1 167 ? 12.59600  -19.72200 -45.04600 1.000 35.34634  ? 167 TRP A CZ3 1 
ATOM   1357 C CH2 . TRP A 1 167 ? 12.64700  -18.84900 -46.15300 1.000 35.69639  ? 167 TRP A CH2 1 
ATOM   1358 N N   . LEU A 1 168 ? 7.37900   -22.82500 -41.73600 1.000 34.60941  ? 168 LEU A N   1 
ATOM   1359 C CA  . LEU A 1 168 ? 7.47500   -23.64400 -40.53200 1.000 32.22228  ? 168 LEU A CA  1 
ATOM   1360 C C   . LEU A 1 168 ? 8.06000   -25.01800 -40.86100 1.000 32.74077  ? 168 LEU A C   1 
ATOM   1361 O O   . LEU A 1 168 ? 8.93100   -25.52100 -40.13700 1.000 32.73287  ? 168 LEU A O   1 
ATOM   1362 C CB  . LEU A 1 168 ? 6.10700   -23.76700 -39.87100 1.000 29.91148  ? 168 LEU A CB  1 
ATOM   1363 C CG  . LEU A 1 168 ? 6.05700   -24.75700 -38.70200 1.000 27.81649  ? 168 LEU A CG  1 
ATOM   1364 C CD1 . LEU A 1 168 ? 7.05400   -24.38700 -37.63400 1.000 26.65583  ? 168 LEU A CD1 1 
ATOM   1365 C CD2 . LEU A 1 168 ? 4.63700   -24.81500 -38.09100 1.000 26.82164  ? 168 LEU A CD2 1 
ATOM   1366 N N   . ARG A 1 169 ? 7.62800   -25.61900 -41.97100 1.000 42.20243  ? 169 ARG A N   1 
ATOM   1367 C CA  . ARG A 1 169 ? 8.23300   -26.87600 -42.40200 1.000 42.78671  ? 169 ARG A CA  1 
ATOM   1368 C C   . ARG A 1 169 ? 9.72200   -26.70000 -42.68200 1.000 44.83432  ? 169 ARG A C   1 
ATOM   1369 O O   . ARG A 1 169 ? 10.53100  -27.56500 -42.32700 1.000 44.91065  ? 169 ARG A O   1 
ATOM   1370 C CB  . ARG A 1 169 ? 7.51800   -27.43300 -43.63900 1.000 43.54206  ? 169 ARG A CB  1 
ATOM   1371 C CG  . ARG A 1 169 ? 6.06000   -27.89500 -43.42200 1.000 42.44193  ? 169 ARG A CG  1 
ATOM   1372 C CD  . ARG A 1 169 ? 5.55300   -28.70400 -44.64300 1.000 44.78169  ? 169 ARG A CD  1 
ATOM   1373 N NE  . ARG A 1 169 ? 5.88100   -28.01800 -45.89600 1.000 46.68981  ? 169 ARG A NE  1 
ATOM   1374 C CZ  . ARG A 1 169 ? 5.00000   -27.40700 -46.68000 1.000 47.80047  ? 169 ARG A CZ  1 
ATOM   1375 N NH1 . ARG A 1 169 ? 3.70500   -27.41300 -46.39800 1.000 47.62150  ? 169 ARG A NH1 1 
ATOM   1376 N NH2 . ARG A 1 169 ? 5.42700   -26.77900 -47.77800 1.000 49.08746  ? 169 ARG A NH2 1 
ATOM   1377 N N   . ARG A 1 170 ? 10.11000  -25.57800 -43.31000 1.000 34.78049  ? 170 ARG A N   1 
ATOM   1378 C CA  . ARG A 1 170 ? 11.53200  -25.32700 -43.54900 1.000 37.35448  ? 170 ARG A CA  1 
ATOM   1379 C C   . ARG A 1 170 ? 12.30800  -25.14300 -42.24500 1.000 37.14393  ? 170 ARG A C   1 
ATOM   1380 O O   . ARG A 1 170 ? 13.40300  -25.68900 -42.09200 1.000 37.87823  ? 170 ARG A O   1 
ATOM   1381 C CB  . ARG A 1 170 ? 11.71500  -24.11300 -44.45600 1.000 38.90466  ? 170 ARG A CB  1 
ATOM   1382 C CG  . ARG A 1 170 ? 11.56700  -24.43000 -45.94400 1.000 39.68371  ? 170 ARG A CG  1 
ATOM   1383 C CD  . ARG A 1 170 ? 12.02200  -23.25300 -46.81600 1.000 42.05241  ? 170 ARG A CD  1 
ATOM   1384 N NE  . ARG A 1 170 ? 10.99700  -22.22200 -46.86200 1.000 42.43140  ? 170 ARG A NE  1 
ATOM   1385 C CZ  . ARG A 1 170 ? 9.96700   -22.25300 -47.69500 1.000 42.59195  ? 170 ARG A CZ  1 
ATOM   1386 N NH1 . ARG A 1 170 ? 9.84900   -23.20300 -48.60400 1.000 42.23138  ? 170 ARG A NH1 1 
ATOM   1387 N NH2 . ARG A 1 170 ? 9.01900   -21.32700 -47.59000 1.000 41.98924  ? 170 ARG A NH2 1 
ATOM   1388 N N   . TYR A 1 171 ? 11.76600  -24.39100 -41.28900 1.000 31.04846  ? 171 TYR A N   1 
ATOM   1389 C CA  . TYR A 1 171 ? 12.48600  -24.19500 -40.02900 1.000 31.08794  ? 171 TYR A CA  1 
ATOM   1390 C C   . TYR A 1 171 ? 12.62000  -25.50800 -39.26000 1.000 30.31679  ? 171 TYR A C   1 
ATOM   1391 O O   . TYR A 1 171 ? 13.64700  -25.75600 -38.62300 1.000 31.87751  ? 171 TYR A O   1 
ATOM   1392 C CB  . TYR A 1 171 ? 11.79000  -23.14600 -39.16800 1.000 28.27707  ? 171 TYR A CB  1 
ATOM   1393 C CG  . TYR A 1 171 ? 11.68700  -21.76700 -39.80100 1.000 29.41405  ? 171 TYR A CG  1 
ATOM   1394 C CD1 . TYR A 1 171 ? 12.68000  -21.26600 -40.63300 1.000 32.71971  ? 171 TYR A CD1 1 
ATOM   1395 C CD2 . TYR A 1 171 ? 10.57300  -20.97800 -39.56800 1.000 26.28999  ? 171 TYR A CD2 1 
ATOM   1396 C CE1 . TYR A 1 171 ? 12.56700  -19.98700 -41.20100 1.000 32.51179  ? 171 TYR A CE1 1 
ATOM   1397 C CE2 . TYR A 1 171 ? 10.44700  -19.72400 -40.11100 1.000 26.72426  ? 171 TYR A CE2 1 
ATOM   1398 C CZ  . TYR A 1 171 ? 11.43500  -19.23300 -40.92900 1.000 29.40616  ? 171 TYR A CZ  1 
ATOM   1399 O OH  . TYR A 1 171 ? 11.26300  -17.97800 -41.46900 1.000 28.87188  ? 171 TYR A OH  1 
ATOM   1400 N N   . LEU A 1 172 ? 11.59200  -26.36100 -39.31100 1.000 37.38606  ? 172 LEU A N   1 
ATOM   1401 C CA  . LEU A 1 172 ? 11.66600  -27.64100 -38.62000 1.000 36.10959  ? 172 LEU A CA  1 
ATOM   1402 C C   . LEU A 1 172 ? 12.75800  -28.51700 -39.21800 1.000 38.27038  ? 172 LEU A C   1 
ATOM   1403 O O   . LEU A 1 172 ? 13.44000  -29.24500 -38.49000 1.000 38.89414  ? 172 LEU A O   1 
ATOM   1404 C CB  . LEU A 1 172 ? 10.31200  -28.35400 -38.67200 1.000 33.33294  ? 172 LEU A CB  1 
ATOM   1405 C CG  . LEU A 1 172 ? 9.25400   -27.67200 -37.80300 1.000 30.75632  ? 172 LEU A CG  1 
ATOM   1406 C CD1 . LEU A 1 172 ? 7.84800   -28.10800 -38.18300 1.000 29.44300  ? 172 LEU A CD1 1 
ATOM   1407 C CD2 . LEU A 1 172 ? 9.52500   -27.95100 -36.33700 1.000 29.50880  ? 172 LEU A CD2 1 
ATOM   1408 N N   . GLU A 1 173 ? 12.94800  -28.45300 -40.54100 1.000 41.32864  ? 173 GLU A N   1 
ATOM   1409 C CA  . GLU A 1 173 ? 14.08500  -29.13100 -41.15200 1.000 42.57879  ? 173 GLU A CA  1 
ATOM   1410 C C   . GLU A 1 173 ? 15.40000  -28.51200 -40.70100 1.000 44.43954  ? 173 GLU A C   1 
ATOM   1411 O O   . GLU A 1 173 ? 16.33100  -29.23300 -40.33100 1.000 45.45019  ? 173 GLU A O   1 
ATOM   1412 C CB  . GLU A 1 173 ? 14.00100  -29.07500 -42.67700 1.000 43.87895  ? 173 GLU A CB  1 
ATOM   1413 C CG  . GLU A 1 173 ? 12.96700  -29.93500 -43.33200 1.000 43.37889  ? 173 GLU A CG  1 
ATOM   1414 C CD  . GLU A 1 173 ? 13.03200  -29.83800 -44.85800 1.000 45.50546  ? 173 GLU A CD  1 
ATOM   1415 O OE1 . GLU A 1 173 ? 13.25300  -28.71100 -45.38800 1.000 45.72654  ? 173 GLU A OE1 1 
ATOM   1416 O OE2 . GLU A 1 173 ? 12.87300  -30.89000 -45.53300 1.000 46.38188  ? 173 GLU A OE2 1 
ATOM   1417 N N   . ASN A 1 174 ? 15.50500  -27.16800 -40.75800 1.000 38.34144  ? 174 ASN A N   1 
ATOM   1418 C CA  . ASN A 1 174 ? 16.76900  -26.51200 -40.42000 1.000 39.49684  ? 174 ASN A CA  1 
ATOM   1419 C C   . ASN A 1 174 ? 17.22400  -26.88600 -39.02300 1.000 39.44420  ? 174 ASN A C   1 
ATOM   1420 O O   . ASN A 1 174 ? 18.41000  -27.12300 -38.79300 1.000 40.11270  ? 174 ASN A O   1 
ATOM   1421 C CB  . ASN A 1 174 ? 16.65200  -24.98900 -40.50300 1.000 39.85478  ? 174 ASN A CB  1 
ATOM   1422 C CG  . ASN A 1 174 ? 16.51200  -24.48100 -41.91400 1.000 40.39958  ? 174 ASN A CG  1 
ATOM   1423 O OD1 . ASN A 1 174 ? 16.86200  -25.15200 -42.87600 1.000 40.61276  ? 174 ASN A OD1 1 
ATOM   1424 N ND2 . ASN A 1 174 ? 16.00000  -23.27600 -42.04000 1.000 41.13388  ? 174 ASN A ND2 1 
ATOM   1425 N N   . GLY A 1 175 ? 16.30200  -26.90500 -38.07400 1.000 35.46478  ? 175 GLY A N   1 
ATOM   1426 C CA  . GLY A 1 175 ? 16.66000  -27.16200 -36.70000 1.000 35.59374  ? 175 GLY A CA  1 
ATOM   1427 C C   . GLY A 1 175 ? 16.16400  -28.50700 -36.21300 1.000 34.35938  ? 175 GLY A C   1 
ATOM   1428 O O   . GLY A 1 175 ? 15.83900  -28.65800 -35.03200 1.000 33.67246  ? 175 GLY A O   1 
ATOM   1429 N N   . LYS A 1 176 ? 16.13100  -29.50300 -37.09800 1.000 42.51299  ? 176 LYS A N   1 
ATOM   1430 C CA  . LYS A 1 176 ? 15.53500  -30.78600 -36.73000 1.000 40.84437  ? 176 LYS A CA  1 
ATOM   1431 C C   . LYS A 1 176 ? 16.16700  -31.36200 -35.46900 1.000 41.15757  ? 176 LYS A C   1 
ATOM   1432 O O   . LYS A 1 176 ? 15.46500  -31.75700 -34.53000 1.000 39.17575  ? 176 LYS A O   1 
ATOM   1433 C CB  . LYS A 1 176 ? 15.65600  -31.77800 -37.87800 1.000 40.92596  ? 176 LYS A CB  1 
ATOM   1434 C CG  . LYS A 1 176 ? 14.99300  -33.10000 -37.54200 1.000 39.00731  ? 176 LYS A CG  1 
ATOM   1435 C CD  . LYS A 1 176 ? 14.92900  -34.01700 -38.71300 1.000 40.27851  ? 176 LYS A CD  1 
ATOM   1436 C CE  . LYS A 1 176 ? 14.23200  -35.31600 -38.29400 1.000 40.87332  ? 176 LYS A CE  1 
ATOM   1437 N NZ  . LYS A 1 176 ? 14.20900  -36.32700 -39.35900 1.000 43.51048  ? 176 LYS A NZ  1 
ATOM   1438 N N   . GLU A 1 177 ? 17.49800  -31.38300 -35.42000 1.000 54.89079  ? 177 GLU A N   1 
ATOM   1439 C CA  . GLU A 1 177 ? 18.22500  -32.02200 -34.33700 1.000 55.43559  ? 177 GLU A CA  1 
ATOM   1440 C C   . GLU A 1 177 ? 18.03500  -31.32300 -32.99400 1.000 56.30149  ? 177 GLU A C   1 
ATOM   1441 O O   . GLU A 1 177 ? 18.42000  -31.89300 -31.96800 1.000 56.17516  ? 177 GLU A O   1 
ATOM   1442 C CB  . GLU A 1 177 ? 19.71400  -32.10800 -34.70000 1.000 57.35161  ? 177 GLU A CB  1 
ATOM   1443 C CG  . GLU A 1 177 ? 20.01500  -32.69600 -36.11000 1.000 57.97800  ? 177 GLU A CG  1 
ATOM   1444 C CD  . GLU A 1 177 ? 19.80700  -31.70000 -37.28400 1.000 59.80191  ? 177 GLU A CD  1 
ATOM   1445 O OE1 . GLU A 1 177 ? 19.60100  -30.47700 -37.03100 1.000 58.98076  ? 177 GLU A OE1 1 
ATOM   1446 O OE2 . GLU A 1 177 ? 19.84200  -32.14500 -38.46700 1.000 58.84653  ? 177 GLU A OE2 1 
ATOM   1447 N N   . THR A 1 178 ? 17.45100  -30.11600 -32.96000 1.000 38.36776  ? 178 THR A N   1 
ATOM   1448 C CA  . THR A 1 178 ? 17.06300  -29.51500 -31.68500 1.000 38.85992  ? 178 THR A CA  1 
ATOM   1449 C C   . THR A 1 178 ? 15.56600  -29.30200 -31.55200 1.000 36.59649  ? 178 THR A C   1 
ATOM   1450 O O   . THR A 1 178 ? 15.03900  -29.35900 -30.43800 1.000 34.77785  ? 178 THR A O   1 
ATOM   1451 C CB  . THR A 1 178 ? 17.76000  -28.15900 -31.45000 1.000 40.14429  ? 178 THR A CB  1 
ATOM   1452 O OG1 . THR A 1 178 ? 17.44000  -27.23600 -32.50600 1.000 39.94953  ? 178 THR A OG1 1 
ATOM   1453 C CG2 . THR A 1 178 ? 19.26800  -28.34500 -31.34000 1.000 40.47854  ? 178 THR A CG2 1 
ATOM   1454 N N   . LEU A 1 179 ? 14.86900  -29.01600 -32.65000 1.000 41.87871  ? 179 LEU A N   1 
ATOM   1455 C CA  . LEU A 1 179 ? 13.44300  -28.73300 -32.56600 1.000 37.41238  ? 179 LEU A CA  1 
ATOM   1456 C C   . LEU A 1 179 ? 12.61200  -29.99900 -32.45600 1.000 34.85681  ? 179 LEU A C   1 
ATOM   1457 O O   . LEU A 1 179 ? 11.53500  -29.97200 -31.86100 1.000 31.23796  ? 179 LEU A O   1 
ATOM   1458 C CB  . LEU A 1 179 ? 12.98800  -27.93600 -33.79300 1.000 37.03076  ? 179 LEU A CB  1 
ATOM   1459 C CG  . LEU A 1 179 ? 13.56800  -26.52700 -33.91200 1.000 38.46777  ? 179 LEU A CG  1 
ATOM   1460 C CD1 . LEU A 1 179 ? 13.04700  -25.86400 -35.17900 1.000 37.96245  ? 179 LEU A CD1 1 
ATOM   1461 C CD2 . LEU A 1 179 ? 13.22600  -25.71200 -32.66100 1.000 35.37266  ? 179 LEU A CD2 1 
ATOM   1462 N N   . GLN A 1 180 ? 13.04500  -31.09300 -33.06700 1.000 40.51802  ? 180 GLN A N   1 
ATOM   1463 C CA  . GLN A 1 180 ? 12.23600  -32.30400 -33.09100 1.000 38.82571  ? 180 GLN A CA  1 
ATOM   1464 C C   . GLN A 1 180 ? 12.87100  -33.44700 -32.31900 1.000 39.30471  ? 180 GLN A C   1 
ATOM   1465 O O   . GLN A 1 180 ? 12.55900  -34.60100 -32.59800 1.000 38.89151  ? 180 GLN A O   1 
ATOM   1466 C CB  . GLN A 1 180 ? 11.96700  -32.76400 -34.52800 1.000 39.10206  ? 180 GLN A CB  1 
ATOM   1467 C CG  . GLN A 1 180 ? 11.43800  -31.67100 -35.44100 1.000 38.41776  ? 180 GLN A CG  1 
ATOM   1468 C CD  . GLN A 1 180 ? 11.09600  -32.22200 -36.78100 1.000 39.05995  ? 180 GLN A CD  1 
ATOM   1469 O OE1 . GLN A 1 180 ? 10.41800  -33.23200 -36.86700 1.000 38.70464  ? 180 GLN A OE1 1 
ATOM   1470 N NE2 . GLN A 1 180 ? 11.60000  -31.60000 -37.84400 1.000 40.72330  ? 180 GLN A NE2 1 
ATOM   1471 N N   . ARG A 1 181 ? 13.78600  -33.16800 -31.39900 1.000 64.39983  ? 181 ARG A N   1 
ATOM   1472 C CA  . ARG A 1 181 ? 14.32700  -34.19500 -30.51500 1.000 65.08938  ? 181 ARG A CA  1 
ATOM   1473 C C   . ARG A 1 181 ? 13.96200  -33.78300 -29.10200 1.000 64.42351  ? 181 ARG A C   1 
ATOM   1474 O O   . ARG A 1 181 ? 14.53500  -32.83500 -28.55800 1.000 67.37913  ? 181 ARG A O   1 
ATOM   1475 C CB  . ARG A 1 181 ? 15.83700  -34.36900 -30.67100 1.000 68.25292  ? 181 ARG A CB  1 
ATOM   1476 C CG  . ARG A 1 181 ? 16.28600  -34.92800 -32.02400 1.000 69.35305  ? 181 ARG A CG  1 
ATOM   1477 C CD  . ARG A 1 181 ? 15.89700  -36.39400 -32.24600 1.000 68.86089  ? 181 ARG A CD  1 
ATOM   1478 N NE  . ARG A 1 181 ? 14.75800  -36.53400 -33.15200 1.000 68.05026  ? 181 ARG A NE  1 
ATOM   1479 C CZ  . ARG A 1 181 ? 14.84600  -36.64900 -34.47200 1.000 68.98985  ? 181 ARG A CZ  1 
ATOM   1480 N NH1 . ARG A 1 181 ? 16.01800  -36.64900 -35.09300 1.000 71.79019  ? 181 ARG A NH1 1 
ATOM   1481 N NH2 . ARG A 1 181 ? 13.72800  -36.76500 -35.18900 1.000 68.25029  ? 181 ARG A NH2 1 
ATOM   1482 N N   . ALA A 1 182 ? 12.99700  -34.47800 -28.52500 1.000 37.80190  ? 182 ALA A N   1 
ATOM   1483 C CA  . ALA A 1 182 ? 12.55800  -34.17000 -27.17600 1.000 36.80704  ? 182 ALA A CA  1 
ATOM   1484 C C   . ALA A 1 182 ? 13.65300  -34.55100 -26.18300 1.000 39.65212  ? 182 ALA A C   1 
ATOM   1485 O O   . ALA A 1 182 ? 14.13600  -35.68400 -26.20500 1.000 40.70225  ? 182 ALA A O   1 
ATOM   1486 C CB  . ALA A 1 182 ? 11.26500  -34.91800 -26.89100 1.000 33.88038  ? 182 ALA A CB  1 
ATOM   1487 N N   . ASP A 1 183 ? 14.09000  -33.59000 -25.35800 1.000 37.08076  ? 183 ASP A N   1 
ATOM   1488 C CA  . ASP A 1 183 ? 15.05500  -33.86700 -24.28800 1.000 40.20482  ? 183 ASP A CA  1 
ATOM   1489 C C   . ASP A 1 183 ? 14.31500  -34.18900 -23.00000 1.000 38.30986  ? 183 ASP A C   1 
ATOM   1490 O O   . ASP A 1 183 ? 13.56500  -33.33600 -22.51100 1.000 36.57807  ? 183 ASP A O   1 
ATOM   1491 C CB  . ASP A 1 183 ? 15.95900  -32.66900 -24.04600 1.000 43.28940  ? 183 ASP A CB  1 
ATOM   1492 C CG  . ASP A 1 183 ? 16.88200  -32.37300 -25.21300 1.000 46.54769  ? 183 ASP A CG  1 
ATOM   1493 O OD1 . ASP A 1 183 ? 17.21200  -33.30200 -25.99100 1.000 46.58716  ? 183 ASP A OD1 1 
ATOM   1494 O OD2 . ASP A 1 183 ? 17.29700  -31.19900 -25.33800 1.000 48.36633  ? 183 ASP A OD2 1 
ATOM   1495 N N   . PRO A 1 184 ? 14.48400  -35.37300 -22.41000 1.000 35.48847  ? 184 PRO A N   1 
ATOM   1496 C CA  . PRO A 1 184 ? 13.70100  -35.71700 -21.22700 1.000 33.71720  ? 184 PRO A CA  1 
ATOM   1497 C C   . PRO A 1 184 ? 14.19000  -34.94200 -20.01400 1.000 35.96484  ? 184 PRO A C   1 
ATOM   1498 O O   . PRO A 1 184 ? 15.35000  -34.49400 -19.97300 1.000 39.61791  ? 184 PRO A O   1 
ATOM   1499 C CB  . PRO A 1 184 ? 13.92300  -37.22800 -21.06900 1.000 34.00934  ? 184 PRO A CB  1 
ATOM   1500 C CG  . PRO A 1 184 ? 15.22300  -37.49500 -21.74300 1.000 36.23592  ? 184 PRO A CG  1 
ATOM   1501 C CD  . PRO A 1 184 ? 15.38300  -36.47200 -22.82500 1.000 36.68598  ? 184 PRO A CD  1 
ATOM   1502 N N   . PRO A 1 185 ? 13.34200  -34.74300 -19.00900 1.000 36.69914  ? 185 PRO A N   1 
ATOM   1503 C CA  . PRO A 1 185 ? 13.80400  -34.07700 -17.78900 1.000 38.74938  ? 185 PRO A CA  1 
ATOM   1504 C C   . PRO A 1 185 ? 14.67700  -34.99100 -16.94300 1.000 42.01030  ? 185 PRO A C   1 
ATOM   1505 O O   . PRO A 1 185 ? 14.48300  -36.20700 -16.89100 1.000 40.74699  ? 185 PRO A O   1 
ATOM   1506 C CB  . PRO A 1 185 ? 12.50400  -33.72300 -17.06000 1.000 34.96998  ? 185 PRO A CB  1 
ATOM   1507 C CG  . PRO A 1 185 ? 11.51700  -34.75600 -17.53700 1.000 32.44600  ? 185 PRO A CG  1 
ATOM   1508 C CD  . PRO A 1 185 ? 11.91900  -35.13900 -18.93700 1.000 32.66971  ? 185 PRO A CD  1 
ATOM   1509 N N   . LYS A 1 186 ? 15.67900  -34.39100 -16.30400 1.000 37.99140  ? 186 LYS A N   1 
ATOM   1510 C CA  . LYS A 1 186 ? 16.38700  -35.04200 -15.21000 1.000 40.02848  ? 186 LYS A CA  1 
ATOM   1511 C C   . LYS A 1 186 ? 15.61300  -34.74300 -13.92800 1.000 39.48631  ? 186 LYS A C   1 
ATOM   1512 O O   . LYS A 1 186 ? 15.19000  -33.60200 -13.71300 1.000 38.75991  ? 186 LYS A O   1 
ATOM   1513 C CB  . LYS A 1 186 ? 17.83400  -34.55000 -15.12500 1.000 42.25243  ? 186 LYS A CB  1 
ATOM   1514 N N   . THR A 1 187 ? 15.38800  -35.77000 -13.10200 1.000 41.44181  ? 187 THR A N   1 
ATOM   1515 C CA  . THR A 1 187 ? 14.42900  -35.67900 -12.00900 1.000 40.13902  ? 187 THR A CA  1 
ATOM   1516 C C   . THR A 1 187 ? 15.01500  -36.13300 -10.67500 1.000 42.44193  ? 187 THR A C   1 
ATOM   1517 O O   . THR A 1 187 ? 15.89100  -37.00100 -10.62100 1.000 43.56312  ? 187 THR A O   1 
ATOM   1518 C CB  . THR A 1 187 ? 13.18500  -36.52000 -12.31000 1.000 36.99391  ? 187 THR A CB  1 
ATOM   1519 O OG1 . THR A 1 187 ? 13.58600  -37.85900 -12.61500 1.000 37.21499  ? 187 THR A OG1 1 
ATOM   1520 C CG2 . THR A 1 187 ? 12.41000  -35.93900 -13.49400 1.000 33.74878  ? 187 THR A CG2 1 
ATOM   1521 N N   . HIS A 1 188 ? 14.50900  -35.53400 -9.59300  1.000 38.18616  ? 188 HIS A N   1 
ATOM   1522 C CA  . HIS A 1 188 ? 14.81500  -35.98000 -8.23600  1.000 39.53895  ? 188 HIS A CA  1 
ATOM   1523 C C   . HIS A 1 188 ? 13.82700  -35.33500 -7.27100  1.000 38.63358  ? 188 HIS A C   1 
ATOM   1524 O O   . HIS A 1 188 ? 13.07800  -34.41700 -7.62600  1.000 37.24131  ? 188 HIS A O   1 
ATOM   1525 C CB  . HIS A 1 188 ? 16.25600  -35.64800 -7.83400  1.000 42.04451  ? 188 HIS A CB  1 
ATOM   1526 C CG  . HIS A 1 188 ? 16.49900  -34.18700 -7.62600  1.000 42.77618  ? 188 HIS A CG  1 
ATOM   1527 N ND1 . HIS A 1 188 ? 16.73500  -33.31300 -8.66700  1.000 42.75513  ? 188 HIS A ND1 1 
ATOM   1528 C CD2 . HIS A 1 188 ? 16.54100  -33.44300 -6.49400  1.000 43.11833  ? 188 HIS A CD2 1 
ATOM   1529 C CE1 . HIS A 1 188 ? 16.91400  -32.09500 -8.18500  1.000 42.61300  ? 188 HIS A CE1 1 
ATOM   1530 N NE2 . HIS A 1 188 ? 16.80100  -32.14600 -6.86900  1.000 43.12096  ? 188 HIS A NE2 1 
ATOM   1531 N N   . VAL A 1 189 ? 13.85600  -35.81400 -6.03000  1.000 42.61564  ? 189 VAL A N   1 
ATOM   1532 C CA  . VAL A 1 189 ? 12.95200  -35.36600 -4.98100  1.000 42.48930  ? 189 VAL A CA  1 
ATOM   1533 C C   . VAL A 1 189 ? 13.78900  -34.85900 -3.81500  1.000 45.10804  ? 189 VAL A C   1 
ATOM   1534 O O   . VAL A 1 189 ? 14.72800  -35.53500 -3.37600  1.000 46.73981  ? 189 VAL A O   1 
ATOM   1535 C CB  . VAL A 1 189 ? 12.00500  -36.49500 -4.53000  1.000 40.90227  ? 189 VAL A CB  1 
ATOM   1536 C CG1 . VAL A 1 189 ? 11.05700  -35.99800 -3.43200  1.000 40.73120  ? 189 VAL A CG1 1 
ATOM   1537 C CG2 . VAL A 1 189 ? 11.21600  -37.03300 -5.71300  1.000 38.38881  ? 189 VAL A CG2 1 
ATOM   1538 N N   . THR A 1 190 ? 13.45700  -33.67200 -3.32000  1.000 44.07897  ? 190 THR A N   1 
ATOM   1539 C CA  . THR A 1 190 ? 14.09200  -33.13900 -2.12600  1.000 45.20805  ? 190 THR A CA  1 
ATOM   1540 C C   . THR A 1 190 ? 13.07900  -33.08300 -0.99300  1.000 44.72642  ? 190 THR A C   1 
ATOM   1541 O O   . THR A 1 190 ? 11.86200  -33.15900 -1.20500  1.000 43.23150  ? 190 THR A O   1 
ATOM   1542 C CB  . THR A 1 190 ? 14.67600  -31.74300 -2.35700  1.000 46.04236  ? 190 THR A CB  1 
ATOM   1543 O OG1 . THR A 1 190 ? 13.61500  -30.81800 -2.64900  1.000 44.61324  ? 190 THR A OG1 1 
ATOM   1544 C CG2 . THR A 1 190 ? 15.65700  -31.77800 -3.50700  1.000 45.59494  ? 190 THR A CG2 1 
ATOM   1545 N N   . HIS A 1 191 ? 13.61300  -32.92200 0.21200   1.000 46.52400  ? 191 HIS A N   1 
ATOM   1546 C CA  . HIS A 1 191 ? 12.87600  -33.01700 1.46100   1.000 46.68454  ? 191 HIS A CA  1 
ATOM   1547 C C   . HIS A 1 191 ? 13.34600  -31.87800 2.34900   1.000 47.89522  ? 191 HIS A C   1 
ATOM   1548 O O   . HIS A 1 191 ? 14.55700  -31.69400 2.51400   1.000 48.94534  ? 191 HIS A O   1 
ATOM   1549 C CB  . HIS A 1 191 ? 13.15100  -34.37800 2.12500   1.000 47.35831  ? 191 HIS A CB  1 
ATOM   1550 C CG  . HIS A 1 191 ? 12.43200  -34.61300 3.42100   1.000 47.78204  ? 191 HIS A CG  1 
ATOM   1551 N ND1 . HIS A 1 191 ? 12.86500  -34.09200 4.62200   1.000 49.67964  ? 191 HIS A ND1 1 
ATOM   1552 C CD2 . HIS A 1 191 ? 11.34200  -35.36400 3.71200   1.000 46.73192  ? 191 HIS A CD2 1 
ATOM   1553 C CE1 . HIS A 1 191 ? 12.06100  -34.49100 5.59400   1.000 49.06115  ? 191 HIS A CE1 1 
ATOM   1554 N NE2 . HIS A 1 191 ? 11.13100  -35.27000 5.07100   1.000 47.60834  ? 191 HIS A NE2 1 
ATOM   1555 N N   . HIS A 1 192 ? 12.40900  -31.10700 2.90700   1.000 54.12228  ? 192 HIS A N   1 
ATOM   1556 C CA  . HIS A 1 192 ? 12.79300  -30.15700 3.93500   1.000 55.28294  ? 192 HIS A CA  1 
ATOM   1557 C C   . HIS A 1 192 ? 11.70900  -30.05700 5.00200   1.000 55.26715  ? 192 HIS A C   1 
ATOM   1558 O O   . HIS A 1 192 ? 10.52300  -29.87200 4.66800   1.000 53.81435  ? 192 HIS A O   1 
ATOM   1559 C CB  . HIS A 1 192 ? 13.09700  -28.78000 3.34400   1.000 55.43559  ? 192 HIS A CB  1 
ATOM   1560 C CG  . HIS A 1 192 ? 14.26000  -28.79100 2.39600   1.000 56.58310  ? 192 HIS A CG  1 
ATOM   1561 N ND1 . HIS A 1 192 ? 14.10300  -28.78700 1.02400   1.000 56.09357  ? 192 HIS A ND1 1 
ATOM   1562 C CD2 . HIS A 1 192 ? 15.59500  -28.87900 2.62100   1.000 57.29371  ? 192 HIS A CD2 1 
ATOM   1563 C CE1 . HIS A 1 192 ? 15.29100  -28.82400 0.44400   1.000 55.77511  ? 192 HIS A CE1 1 
ATOM   1564 N NE2 . HIS A 1 192 ? 16.21300  -28.88200 1.39100   1.000 57.09895  ? 192 HIS A NE2 1 
ATOM   1565 N N   . PRO A 1 193 ? 12.07800  -30.16600 6.27500   1.000 56.91472  ? 193 PRO A N   1 
ATOM   1566 C CA  . PRO A 1 193 ? 11.08700  -30.02700 7.34400   1.000 57.57532  ? 193 PRO A CA  1 
ATOM   1567 C C   . PRO A 1 193 ? 10.57700  -28.60300 7.41500   1.000 58.59387  ? 193 PRO A C   1 
ATOM   1568 O O   . PRO A 1 193 ? 11.29900  -27.64900 7.12300   1.000 58.85706  ? 193 PRO A O   1 
ATOM   1569 C CB  . PRO A 1 193 ? 11.86700  -30.39500 8.61900   1.000 60.45198  ? 193 PRO A CB  1 
ATOM   1570 C CG  . PRO A 1 193 ? 13.20000  -30.93300 8.15100   1.000 61.03890  ? 193 PRO A CG  1 
ATOM   1571 C CD  . PRO A 1 193 ? 13.44200  -30.31700 6.80000   1.000 59.40186  ? 193 PRO A CD  1 
ATOM   1572 N N   . ILE A 1 194 ? 9.30700   -28.47000 7.79100   1.000 64.56564  ? 194 ILE A N   1 
ATOM   1573 C CA  . ILE A 1 194 ? 8.72000   -27.17100 8.10300   1.000 65.86316  ? 194 ILE A CA  1 
ATOM   1574 C C   . ILE A 1 194 ? 8.34300   -27.05100 9.56300   1.000 69.99787  ? 194 ILE A C   1 
ATOM   1575 O O   . ILE A 1 194 ? 7.96400   -25.95100 10.00000  1.000 72.62976  ? 194 ILE A O   1 
ATOM   1576 C CB  . ILE A 1 194 ? 7.49200   -26.87200 7.21600   1.000 64.56827  ? 194 ILE A CB  1 
ATOM   1577 C CG1 . ILE A 1 194 ? 6.27000   -27.63800 7.72800   1.000 64.97095  ? 194 ILE A CG1 1 
ATOM   1578 C CG2 . ILE A 1 194 ? 7.77800   -27.25600 5.78600   1.000 61.71793  ? 194 ILE A CG2 1 
ATOM   1579 C CD1 . ILE A 1 194 ? 5.05600   -27.49900 6.83800   1.000 63.50761  ? 194 ILE A CD1 1 
ATOM   1580 N N   . SER A 1 195 ? 8.43700   -28.14000 10.33200  1.000 60.72307  ? 195 SER A N   1 
ATOM   1581 C CA  . SER A 1 195 ? 8.14600   -28.15500 11.75700  1.000 64.37351  ? 195 SER A CA  1 
ATOM   1582 C C   . SER A 1 195 ? 8.65200   -29.47800 12.32000  1.000 64.12348  ? 195 SER A C   1 
ATOM   1583 O O   . SER A 1 195 ? 9.46100   -30.15900 11.68100  1.000 61.92585  ? 195 SER A O   1 
ATOM   1584 C CB  . SER A 1 195 ? 6.64800   -27.98400 12.01300  1.000 64.92094  ? 195 SER A CB  1 
ATOM   1585 O OG  . SER A 1 195 ? 5.91900   -29.07900 11.48900  1.000 61.76793  ? 195 SER A OG  1 
ATOM   1586 N N   . ASP A 1 196 ? 8.18300   -29.87400 13.49600  1.000 68.89773  ? 196 ASP A N   1 
ATOM   1587 C CA  . ASP A 1 196 ? 8.54600   -31.17800 14.02900  1.000 68.72929  ? 196 ASP A CA  1 
ATOM   1588 C C   . ASP A 1 196 ? 7.55400   -32.27200 13.63900  1.000 65.95791  ? 196 ASP A C   1 
ATOM   1589 O O   . ASP A 1 196 ? 7.65300   -33.39500 14.14900  1.000 66.12372  ? 196 ASP A O   1 
ATOM   1590 C CB  . ASP A 1 196 ? 8.68800   -31.10900 15.55700  1.000 73.15614  ? 196 ASP A CB  1 
ATOM   1591 C CG  . ASP A 1 196 ? 10.15400  -31.10700 16.01700  1.000 75.73013  ? 196 ASP A CG  1 
ATOM   1592 O OD1 . ASP A 1 196 ? 11.04900  -31.49400 15.22700  1.000 73.32984  ? 196 ASP A OD1 1 
ATOM   1593 O OD2 . ASP A 1 196 ? 10.40900  -30.73200 17.18300  1.000 80.17540  ? 196 ASP A OD2 1 
ATOM   1594 N N   . HIS A 1 197 ? 6.58400   -31.97000 12.77100  1.000 61.46000  ? 197 HIS A N   1 
ATOM   1595 C CA  . HIS A 1 197 ? 5.65100   -32.99500 12.32200  1.000 59.18604  ? 197 HIS A CA  1 
ATOM   1596 C C   . HIS A 1 197 ? 5.21000   -32.83200 10.87100  1.000 55.84091  ? 197 HIS A C   1 
ATOM   1597 O O   . HIS A 1 197 ? 4.35300   -33.60100 10.42000  1.000 54.27493  ? 197 HIS A O   1 
ATOM   1598 C CB  . HIS A 1 197 ? 4.40100   -33.05000 13.22900  1.000 61.52053  ? 197 HIS A CB  1 
ATOM   1599 C CG  . HIS A 1 197 ? 3.62600   -31.77100 13.27600  1.000 63.22337  ? 197 HIS A CG  1 
ATOM   1600 N ND1 . HIS A 1 197 ? 3.82700   -30.81600 14.25000  1.000 66.95803  ? 197 HIS A ND1 1 
ATOM   1601 C CD2 . HIS A 1 197 ? 2.64800   -31.28900 12.47400  1.000 62.10218  ? 197 HIS A CD2 1 
ATOM   1602 C CE1 . HIS A 1 197 ? 3.01600   -29.79400 14.03600  1.000 68.07922  ? 197 HIS A CE1 1 
ATOM   1603 N NE2 . HIS A 1 197 ? 2.29500   -30.05300 12.96000  1.000 65.12623  ? 197 HIS A NE2 1 
ATOM   1604 N N   . GLU A 1 198 ? 5.75800   -31.87200 10.12300  1.000 53.39061  ? 198 GLU A N   1 
ATOM   1605 C CA  . GLU A 1 198 ? 5.46000   -31.74300 8.70400   1.000 52.30364  ? 198 GLU A CA  1 
ATOM   1606 C C   . GLU A 1 198 ? 6.74000   -31.43700 7.93900   1.000 50.75872  ? 198 GLU A C   1 
ATOM   1607 O O   . GLU A 1 198 ? 7.64500   -30.76900 8.44800   1.000 49.80071  ? 198 GLU A O   1 
ATOM   1608 C CB  . GLU A 1 198 ? 4.41400   -30.64900 8.42000   1.000 53.14848  ? 198 GLU A CB  1 
ATOM   1609 C CG  . GLU A 1 198 ? 2.97500   -31.02500 8.78500   1.000 55.99882  ? 198 GLU A CG  1 
ATOM   1610 C CD  . GLU A 1 198 ? 1.96200   -29.95400 8.38000   1.000 57.25950  ? 198 GLU A CD  1 
ATOM   1611 O OE1 . GLU A 1 198 ? 2.05200   -28.81800 8.89200   1.000 56.90682  ? 198 GLU A OE1 1 
ATOM   1612 O OE2 . GLU A 1 198 ? 1.07600   -30.24800 7.54500   1.000 58.44122  ? 198 GLU A OE2 1 
ATOM   1613 N N   . ALA A 1 199 ? 6.80100   -31.94100 6.70600   1.000 45.75022  ? 199 ALA A N   1 
ATOM   1614 C CA  . ALA A 1 199 ? 7.91600   -31.69700 5.80800   1.000 43.95790  ? 199 ALA A CA  1 
ATOM   1615 C C   . ALA A 1 199 ? 7.37900   -31.46900 4.40300   1.000 43.54733  ? 199 ALA A C   1 
ATOM   1616 O O   . ALA A 1 199 ? 6.28000   -31.91500 4.05800   1.000 44.64483  ? 199 ALA A O   1 
ATOM   1617 C CB  . ALA A 1 199 ? 8.91300   -32.86700 5.80900   1.000 43.19465  ? 199 ALA A CB  1 
ATOM   1618 N N   . THR A 1 200 ? 8.17200   -30.75900 3.59600   1.000 40.78910  ? 200 THR A N   1 
ATOM   1619 C CA  . THR A 1 200 ? 7.88600   -30.55400 2.18600   1.000 40.65751  ? 200 THR A CA  1 
ATOM   1620 C C   . THR A 1 200 ? 8.64800   -31.56600 1.34500   1.000 39.62317  ? 200 THR A C   1 
ATOM   1621 O O   . THR A 1 200 ? 9.86400   -31.70100 1.48300   1.000 38.57041  ? 200 THR A O   1 
ATOM   1622 C CB  . THR A 1 200 ? 8.27200   -29.14500 1.74400   1.000 40.04954  ? 200 THR A CB  1 
ATOM   1623 O OG1 . THR A 1 200 ? 7.58500   -28.18900 2.55900   1.000 41.24705  ? 200 THR A OG1 1 
ATOM   1624 C CG2 . THR A 1 200 ? 7.88700   -28.94200 0.27900   1.000 40.30483  ? 200 THR A CG2 1 
ATOM   1625 N N   . LEU A 1 201 ? 7.93000   -32.27600 0.48600   1.000 37.12024  ? 201 LEU A N   1 
ATOM   1626 C CA  . LEU A 1 201 ? 8.52600   -33.02800 -0.61200  1.000 35.52005  ? 201 LEU A CA  1 
ATOM   1627 C C   . LEU A 1 201 ? 8.42000   -32.18000 -1.87500  1.000 35.32266  ? 201 LEU A C   1 
ATOM   1628 O O   . LEU A 1 201 ? 7.34700   -31.63400 -2.16300  1.000 37.08866  ? 201 LEU A O   1 
ATOM   1629 C CB  . LEU A 1 201 ? 7.81900   -34.36800 -0.81600  1.000 36.49385  ? 201 LEU A CB  1 
ATOM   1630 C CG  . LEU A 1 201 ? 7.87900   -35.32300 0.38500   1.000 37.12024  ? 201 LEU A CG  1 
ATOM   1631 C CD1 . LEU A 1 201 ? 7.12400   -36.61800 0.10500   1.000 38.10457  ? 201 LEU A CD1 1 
ATOM   1632 C CD2 . LEU A 1 201 ? 9.33800   -35.62400 0.71300   1.000 35.96221  ? 201 LEU A CD2 1 
ATOM   1633 N N   . ARG A 1 202 ? 9.53000   -32.05200 -2.61100  1.000 41.02597  ? 202 ARG A N   1 
ATOM   1634 C CA  . ARG A 1 202 ? 9.56600   -31.26100 -3.84100  1.000 39.98901  ? 202 ARG A CA  1 
ATOM   1635 C C   . ARG A 1 202 ? 10.11900  -32.11800 -4.97100  1.000 38.26511  ? 202 ARG A C   1 
ATOM   1636 O O   . ARG A 1 202 ? 11.24000  -32.63500 -4.88200  1.000 37.25973  ? 202 ARG A O   1 
ATOM   1637 C CB  . ARG A 1 202 ? 10.39800  -29.98200 -3.67300  1.000 39.51263  ? 202 ARG A CB  1 
ATOM   1638 C CG  . ARG A 1 202 ? 10.44100  -29.11500 -4.95500  1.000 38.40987  ? 202 ARG A CG  1 
ATOM   1639 C CD  . ARG A 1 202 ? 11.13400  -27.76300 -4.73600  1.000 38.55199  ? 202 ARG A CD  1 
ATOM   1640 N NE  . ARG A 1 202 ? 10.31800  -26.85500 -3.94600  1.000 39.59948  ? 202 ARG A NE  1 
ATOM   1641 C CZ  . ARG A 1 202 ? 10.54100  -26.57400 -2.67100  1.000 41.24705  ? 202 ARG A CZ  1 
ATOM   1642 N NH1 . ARG A 1 202 ? 11.58700  -27.06800 -2.02900  1.000 40.80752  ? 202 ARG A NH1 1 
ATOM   1643 N NH2 . ARG A 1 202 ? 9.69700   -25.77100 -2.02400  1.000 41.47076  ? 202 ARG A NH2 1 
ATOM   1644 N N   . CYS A 1 203 ? 9.32600   -32.28100 -6.02000  1.000 40.00743  ? 203 CYS A N   1 
ATOM   1645 C CA  . CYS A 1 203 ? 9.70200   -33.07100 -7.17700  1.000 38.90466  ? 203 CYS A CA  1 
ATOM   1646 C C   . CYS A 1 203 ? 10.26600  -32.15500 -8.25400  1.000 36.74651  ? 203 CYS A C   1 
ATOM   1647 O O   . CYS A 1 203 ? 9.60400   -31.20300 -8.65700  1.000 37.31763  ? 203 CYS A O   1 
ATOM   1648 C CB  . CYS A 1 203 ? 8.48800   -33.81200 -7.71700  1.000 41.71816  ? 203 CYS A CB  1 
ATOM   1649 S SG  . CYS A 1 203 ? 8.89900   -34.98600 -8.95300  1.000 41.18915  ? 203 CYS A SG  1 
ATOM   1650 N N   . TRP A 1 204 ? 11.47600  -32.43900 -8.71100  1.000 38.89414  ? 204 TRP A N   1 
ATOM   1651 C CA  . TRP A 1 204 ? 12.19700  -31.55700 -9.62200  1.000 37.34132  ? 204 TRP A CA  1 
ATOM   1652 C C   . TRP A 1 204 ? 12.26600  -32.15600 -11.01900 1.000 36.68335  ? 204 TRP A C   1 
ATOM   1653 O O   . TRP A 1 204 ? 12.54300  -33.34500 -11.16700 1.000 36.88074  ? 204 TRP A O   1 
ATOM   1654 C CB  . TRP A 1 204 ? 13.62300  -31.31900 -9.12300  1.000 37.08603  ? 204 TRP A CB  1 
ATOM   1655 C CG  . TRP A 1 204 ? 13.71600  -30.37600 -8.00500  1.000 38.02298  ? 204 TRP A CG  1 
ATOM   1656 C CD1 . TRP A 1 204 ? 13.65400  -30.66500 -6.67400  1.000 39.28366  ? 204 TRP A CD1 1 
ATOM   1657 C CD2 . TRP A 1 204 ? 13.90000  -28.96700 -8.10700  1.000 38.84939  ? 204 TRP A CD2 1 
ATOM   1658 N NE1 . TRP A 1 204 ? 13.78400  -29.50700 -5.93900  1.000 40.76278  ? 204 TRP A NE1 1 
ATOM   1659 C CE2 . TRP A 1 204 ? 13.93700  -28.45500 -6.80000  1.000 40.06796  ? 204 TRP A CE2 1 
ATOM   1660 C CE3 . TRP A 1 204 ? 14.02400  -28.08000 -9.18600  1.000 38.62305  ? 204 TRP A CE3 1 
ATOM   1661 C CZ2 . TRP A 1 204 ? 14.10000  -27.10100 -6.53800  1.000 41.31285  ? 204 TRP A CZ2 1 
ATOM   1662 C CZ3 . TRP A 1 204 ? 14.19100  -26.72200 -8.91400  1.000 40.18377  ? 204 TRP A CZ3 1 
ATOM   1663 C CH2 . TRP A 1 204 ? 14.22900  -26.25400 -7.60800  1.000 41.33390  ? 204 TRP A CH2 1 
ATOM   1664 N N   . ALA A 1 205 ? 12.09800  -31.31000 -12.04400 1.000 29.51933  ? 205 ALA A N   1 
ATOM   1665 C CA  . ALA A 1 205 ? 12.31200  -31.71600 -13.43400 1.000 29.41142  ? 205 ALA A CA  1 
ATOM   1666 C C   . ALA A 1 205 ? 13.16400  -30.65400 -14.10900 1.000 28.21917  ? 205 ALA A C   1 
ATOM   1667 O O   . ALA A 1 205 ? 12.77200  -29.48700 -14.13600 1.000 27.69806  ? 205 ALA A O   1 
ATOM   1668 C CB  . ALA A 1 205 ? 10.98600  -31.88600 -14.17900 1.000 30.82475  ? 205 ALA A CB  1 
ATOM   1669 N N   . LEU A 1 206 ? 14.34200  -31.04200 -14.59900 1.000 33.09081  ? 206 LEU A N   1 
ATOM   1670 C CA  . LEU A 1 206 ? 15.32200  -30.08000 -15.07900 1.000 32.77761  ? 206 LEU A CA  1 
ATOM   1671 C C   . LEU A 1 206 ? 15.80200  -30.46700 -16.46600 1.000 32.87763  ? 206 LEU A C   1 
ATOM   1672 O O   . LEU A 1 206 ? 15.96500  -31.64700 -16.77400 1.000 33.52244  ? 206 LEU A O   1 
ATOM   1673 C CB  . LEU A 1 206 ? 16.54700  -29.98400 -14.15900 1.000 33.17503  ? 206 LEU A CB  1 
ATOM   1674 C CG  . LEU A 1 206 ? 16.30500  -29.66600 -12.68200 1.000 33.82774  ? 206 LEU A CG  1 
ATOM   1675 C CD1 . LEU A 1 206 ? 17.62600  -29.68900 -11.91900 1.000 34.50414  ? 206 LEU A CD1 1 
ATOM   1676 C CD2 . LEU A 1 206 ? 15.62600  -28.32100 -12.53200 1.000 34.25411  ? 206 LEU A CD2 1 
ATOM   1677 N N   . GLY A 1 207 ? 16.06200  -29.45300 -17.28300 1.000 32.77498  ? 207 GLY A N   1 
ATOM   1678 C CA  . GLY A 1 207 ? 16.73300  -29.67800 -18.55000 1.000 33.73036  ? 207 GLY A CA  1 
ATOM   1679 C C   . GLY A 1 207 ? 15.89600  -30.31300 -19.64000 1.000 34.06724  ? 207 GLY A C   1 
ATOM   1680 O O   . GLY A 1 207 ? 16.44100  -31.01400 -20.49900 1.000 35.84377  ? 207 GLY A O   1 
ATOM   1681 N N   . PHE A 1 208 ? 14.58800  -30.09900 -19.64300 1.000 27.77965  ? 208 PHE A N   1 
ATOM   1682 C CA  . PHE A 1 208 ? 13.73000  -30.76300 -20.60600 1.000 29.22982  ? 208 PHE A CA  1 
ATOM   1683 C C   . PHE A 1 208 ? 13.30100  -29.79300 -21.70100 1.000 28.89031  ? 208 PHE A C   1 
ATOM   1684 O O   . PHE A 1 208 ? 13.20900  -28.59000 -21.48000 1.000 27.28748  ? 208 PHE A O   1 
ATOM   1685 C CB  . PHE A 1 208 ? 12.48400  -31.38500 -19.94500 1.000 30.31942  ? 208 PHE A CB  1 
ATOM   1686 C CG  . PHE A 1 208 ? 11.65400  -30.41200 -19.14800 1.000 28.83767  ? 208 PHE A CG  1 
ATOM   1687 C CD1 . PHE A 1 208 ? 11.94000  -30.16800 -17.80000 1.000 27.90071  ? 208 PHE A CD1 1 
ATOM   1688 C CD2 . PHE A 1 208 ? 10.57200  -29.77100 -19.71900 1.000 28.18233  ? 208 PHE A CD2 1 
ATOM   1689 C CE1 . PHE A 1 208 ? 11.17600  -29.27700 -17.05500 1.000 27.14799  ? 208 PHE A CE1 1 
ATOM   1690 C CE2 . PHE A 1 208 ? 9.80600   -28.87800 -18.98200 1.000 27.68227  ? 208 PHE A CE2 1 
ATOM   1691 C CZ  . PHE A 1 208 ? 10.10900  -28.62800 -17.64800 1.000 27.41118  ? 208 PHE A CZ  1 
ATOM   1692 N N   . TYR A 1 209 ? 13.00200  -30.35000 -22.87700 1.000 32.35125  ? 209 TYR A N   1 
ATOM   1693 C CA  . TYR A 1 209 ? 12.46700  -29.65300 -24.04300 1.000 32.11174  ? 209 TYR A CA  1 
ATOM   1694 C C   . TYR A 1 209 ? 11.56000  -30.64100 -24.75900 1.000 33.71194  ? 209 TYR A C   1 
ATOM   1695 O O   . TYR A 1 209 ? 11.94600  -31.80600 -24.89900 1.000 36.12538  ? 209 TYR A O   1 
ATOM   1696 C CB  . TYR A 1 209 ? 13.55900  -29.17800 -25.00600 1.000 33.51191  ? 209 TYR A CB  1 
ATOM   1697 C CG  . TYR A 1 209 ? 12.98400  -28.35500 -26.13000 1.000 33.48296  ? 209 TYR A CG  1 
ATOM   1698 C CD1 . TYR A 1 209 ? 12.80300  -26.98800 -25.98100 1.000 33.99618  ? 209 TYR A CD1 1 
ATOM   1699 C CD2 . TYR A 1 209 ? 12.58100  -28.94800 -27.31000 1.000 34.84628  ? 209 TYR A CD2 1 
ATOM   1700 C CE1 . TYR A 1 209 ? 12.26100  -26.21500 -27.00400 1.000 34.78312  ? 209 TYR A CE1 1 
ATOM   1701 C CE2 . TYR A 1 209 ? 12.04000  -28.19700 -28.34100 1.000 35.73060  ? 209 TYR A CE2 1 
ATOM   1702 C CZ  . TYR A 1 209 ? 11.88300  -26.82900 -28.17300 1.000 35.45425  ? 209 TYR A CZ  1 
ATOM   1703 O OH  . TYR A 1 209 ? 11.33700  -26.08200 -29.17400 1.000 36.49385  ? 209 TYR A OH  1 
ATOM   1704 N N   . PRO A 1 210 ? 10.37300  -30.23100 -25.22900 1.000 38.50462  ? 210 PRO A N   1 
ATOM   1705 C CA  . PRO A 1 210 ? 9.76300   -28.90000 -25.15300 1.000 37.28605  ? 210 PRO A CA  1 
ATOM   1706 C C   . PRO A 1 210 ? 9.20000   -28.62400 -23.76300 1.000 36.08064  ? 210 PRO A C   1 
ATOM   1707 O O   . PRO A 1 210 ? 9.40500   -29.43900 -22.86600 1.000 36.35962  ? 210 PRO A O   1 
ATOM   1708 C CB  . PRO A 1 210 ? 8.65500   -28.95300 -26.21400 1.000 38.41776  ? 210 PRO A CB  1 
ATOM   1709 C CG  . PRO A 1 210 ? 8.30400   -30.38400 -26.33600 1.000 39.93637  ? 210 PRO A CG  1 
ATOM   1710 C CD  . PRO A 1 210 ? 9.53800   -31.18000 -25.98900 1.000 40.58118  ? 210 PRO A CD  1 
ATOM   1711 N N   . ALA A 1 211 ? 8.52900   -27.47900 -23.59200 1.000 33.61982  ? 211 ALA A N   1 
ATOM   1712 C CA  . ALA A 1 211 ? 8.18000   -27.01800 -22.25500 1.000 33.40927  ? 211 ALA A CA  1 
ATOM   1713 C C   . ALA A 1 211 ? 7.01400   -27.79600 -21.66100 1.000 34.26463  ? 211 ALA A C   1 
ATOM   1714 O O   . ALA A 1 211 ? 6.92500   -27.90800 -20.43100 1.000 34.36201  ? 211 ALA A O   1 
ATOM   1715 C CB  . ALA A 1 211 ? 7.84700   -25.52600 -22.27100 1.000 33.40401  ? 211 ALA A CB  1 
ATOM   1716 N N   . GLU A 1 212 ? 6.11900   -28.32300 -22.49900 1.000 41.84975  ? 212 GLU A N   1 
ATOM   1717 C CA  . GLU A 1 212 ? 4.99000   -29.09500 -22.00000 1.000 43.35257  ? 212 GLU A CA  1 
ATOM   1718 C C   . GLU A 1 212 ? 5.46500   -30.23300 -21.09800 1.000 44.13687  ? 212 GLU A C   1 
ATOM   1719 O O   . GLU A 1 212 ? 6.37400   -30.99000 -21.44700 1.000 44.21846  ? 212 GLU A O   1 
ATOM   1720 C CB  . GLU A 1 212 ? 4.17100   -29.64500 -23.17100 1.000 44.72905  ? 212 GLU A CB  1 
ATOM   1721 C CG  . GLU A 1 212 ? 3.09300   -30.64500 -22.76600 1.000 46.29239  ? 212 GLU A CG  1 
ATOM   1722 C CD  . GLU A 1 212 ? 1.96500   -30.00500 -21.97000 1.000 47.56360  ? 212 GLU A CD  1 
ATOM   1723 O OE1 . GLU A 1 212 ? 1.50100   -28.91100 -22.37000 1.000 47.33989  ? 212 GLU A OE1 1 
ATOM   1724 O OE2 . GLU A 1 212 ? 1.52700   -30.59600 -20.94500 1.000 48.79532  ? 212 GLU A OE2 1 
ATOM   1725 N N   . ILE A 1 213 ? 4.86000   -30.33000 -19.91700 1.000 31.13531  ? 213 ILE A N   1 
ATOM   1726 C CA  . ILE A 1 213 ? 5.20700   -31.38000 -18.95800 1.000 32.37757  ? 213 ILE A CA  1 
ATOM   1727 C C   . ILE A 1 213 ? 4.05900   -31.49400 -17.97300 1.000 34.34886  ? 213 ILE A C   1 
ATOM   1728 O O   . ILE A 1 213 ? 3.31700   -30.53500 -17.76000 1.000 34.21463  ? 213 ILE A O   1 
ATOM   1729 C CB  . ILE A 1 213 ? 6.56100   -31.08600 -18.25500 1.000 31.44061  ? 213 ILE A CB  1 
ATOM   1730 C CG1 . ILE A 1 213 ? 7.01900   -32.29800 -17.42400 1.000 33.59087  ? 213 ILE A CG1 1 
ATOM   1731 C CG2 . ILE A 1 213 ? 6.48000   -29.80000 -17.41700 1.000 30.40628  ? 213 ILE A CG2 1 
ATOM   1732 C CD1 . ILE A 1 213 ? 8.50800   -32.34300 -17.10000 1.000 32.42231  ? 213 ILE A CD1 1 
ATOM   1733 N N   . THR A 1 214 ? 3.87000   -32.69500 -17.41500 1.000 40.39958  ? 214 THR A N   1 
ATOM   1734 C CA  . THR A 1 214 ? 2.94100   -32.90200 -16.30300 1.000 41.94450  ? 214 THR A CA  1 
ATOM   1735 C C   . THR A 1 214 ? 3.70700   -33.48500 -15.12500 1.000 43.26045  ? 214 THR A C   1 
ATOM   1736 O O   . THR A 1 214 ? 4.28200   -34.57400 -15.23500 1.000 43.28940  ? 214 THR A O   1 
ATOM   1737 C CB  . THR A 1 214 ? 1.79300   -33.83700 -16.67500 1.000 42.47615  ? 214 THR A CB  1 
ATOM   1738 O OG1 . THR A 1 214 ? 1.10000   -33.34000 -17.82200 1.000 41.65499  ? 214 THR A OG1 1 
ATOM   1739 C CG2 . THR A 1 214 ? 0.79900   -33.95000 -15.50600 1.000 44.27899  ? 214 THR A CG2 1 
ATOM   1740 N N   . LEU A 1 215 ? 3.70700   -32.76300 -14.00600 1.000 38.08088  ? 215 LEU A N   1 
ATOM   1741 C CA  . LEU A 1 215 ? 4.23100   -33.24100 -12.73000 1.000 39.76003  ? 215 LEU A CA  1 
ATOM   1742 C C   . LEU A 1 215 ? 3.06700   -33.38600 -11.76700 1.000 41.27337  ? 215 LEU A C   1 
ATOM   1743 O O   . LEU A 1 215 ? 2.36700   -32.40600 -11.49500 1.000 41.55761  ? 215 LEU A O   1 
ATOM   1744 C CB  . LEU A 1 215 ? 5.24400   -32.26400 -12.13100 1.000 39.85215  ? 215 LEU A CB  1 
ATOM   1745 C CG  . LEU A 1 215 ? 6.57000   -31.93500 -12.79800 1.000 37.25710  ? 215 LEU A CG  1 
ATOM   1746 C CD1 . LEU A 1 215 ? 7.32900   -30.91100 -11.93600 1.000 33.71194  ? 215 LEU A CD1 1 
ATOM   1747 C CD2 . LEU A 1 215 ? 7.37100   -33.20500 -12.93400 1.000 35.69902  ? 215 LEU A CD2 1 
ATOM   1748 N N   . THR A 1 216 ? 2.88200   -34.58000 -11.21500 1.000 44.20793  ? 216 THR A N   1 
ATOM   1749 C CA  . THR A 1 216 ? 1.84600   -34.77900 -10.21300 1.000 45.53441  ? 216 THR A CA  1 
ATOM   1750 C C   . THR A 1 216 ? 2.41400   -35.51400 -9.00500  1.000 46.04763  ? 216 THR A C   1 
ATOM   1751 O O   . THR A 1 216 ? 3.34400   -36.32400 -9.11100  1.000 44.62114  ? 216 THR A O   1 
ATOM   1752 C CB  . THR A 1 216 ? 0.62500   -35.56500 -10.76900 1.000 46.25818  ? 216 THR A CB  1 
ATOM   1753 O OG1 . THR A 1 216 ? 1.05400   -36.82300 -11.30400 1.000 45.48440  ? 216 THR A OG1 1 
ATOM   1754 C CG2 . THR A 1 216 ? -0.09000  -34.77800 -11.84600 1.000 45.03961  ? 216 THR A CG2 1 
ATOM   1755 N N   . TRP A 1 217 ? 1.84600   -35.21100 -7.84800  1.000 42.31034  ? 217 TRP A N   1 
ATOM   1756 C CA  . TRP A 1 217 ? 2.07800   -35.98100 -6.64100  1.000 42.31297  ? 217 TRP A CA  1 
ATOM   1757 C C   . TRP A 1 217 ? 0.87000   -36.86800 -6.40800  1.000 44.23688  ? 217 TRP A C   1 
ATOM   1758 O O   . TRP A 1 217 ? -0.27100  -36.41000 -6.53500  1.000 45.31070  ? 217 TRP A O   1 
ATOM   1759 C CB  . TRP A 1 217 ? 2.30000   -35.06800 -5.43800  1.000 43.13412  ? 217 TRP A CB  1 
ATOM   1760 C CG  . TRP A 1 217 ? 3.71200   -34.60800 -5.29700  1.000 41.36812  ? 217 TRP A CG  1 
ATOM   1761 C CD1 . TRP A 1 217 ? 4.21300   -33.38100 -5.61100  1.000 40.87069  ? 217 TRP A CD1 1 
ATOM   1762 C CD2 . TRP A 1 217 ? 4.80700   -35.37600 -4.80000  1.000 39.83372  ? 217 TRP A CD2 1 
ATOM   1763 N NE1 . TRP A 1 217 ? 5.55800   -33.33700 -5.34700  1.000 39.09942  ? 217 TRP A NE1 1 
ATOM   1764 C CE2 . TRP A 1 217 ? 5.94600   -34.54500 -4.83300  1.000 37.92297  ? 217 TRP A CE2 1 
ATOM   1765 C CE3 . TRP A 1 217 ? 4.93400   -36.68300 -4.31100  1.000 39.03363  ? 217 TRP A CE3 1 
ATOM   1766 C CZ2 . TRP A 1 217 ? 7.19800   -34.98300 -4.42000  1.000 35.53847  ? 217 TRP A CZ2 1 
ATOM   1767 C CZ3 . TRP A 1 217 ? 6.17800   -37.12100 -3.91400  1.000 37.34921  ? 217 TRP A CZ3 1 
ATOM   1768 C CH2 . TRP A 1 217 ? 7.29800   -36.27000 -3.96600  1.000 35.34634  ? 217 TRP A CH2 1 
ATOM   1769 N N   . GLN A 1 218 ? 1.12200   -38.13800 -6.09200  1.000 57.48847  ? 218 GLN A N   1 
ATOM   1770 C CA  . GLN A 1 218 ? 0.09400   -39.05200 -5.63100  1.000 58.61755  ? 218 GLN A CA  1 
ATOM   1771 C C   . GLN A 1 218 ? 0.41100   -39.48000 -4.20800  1.000 59.14657  ? 218 GLN A C   1 
ATOM   1772 O O   . GLN A 1 218 ? 1.57200   -39.50400 -3.78900  1.000 57.45689  ? 218 GLN A O   1 
ATOM   1773 C CB  . GLN A 1 218 ? -0.02200  -40.31800 -6.51300  1.000 58.15697  ? 218 GLN A CB  1 
ATOM   1774 C CG  . GLN A 1 218 ? -0.68300  -40.12300 -7.86700  1.000 58.90969  ? 218 GLN A CG  1 
ATOM   1775 C CD  . GLN A 1 218 ? -0.66000  -41.39000 -8.72000  1.000 58.32278  ? 218 GLN A CD  1 
ATOM   1776 O OE1 . GLN A 1 218 ? -0.55500  -42.50200 -8.20200  1.000 58.87285  ? 218 GLN A OE1 1 
ATOM   1777 N NE2 . GLN A 1 218 ? -0.74600  -41.22200 -10.03400 1.000 57.55953  ? 218 GLN A NE2 1 
ATOM   1778 N N   . ARG A 1 219 ? -0.63600  -39.83400 -3.47300  1.000 67.99763  ? 219 ARG A N   1 
ATOM   1779 C CA  . ARG A 1 219 ? -0.50100  -40.46600 -2.17100  1.000 67.90814  ? 219 ARG A CA  1 
ATOM   1780 C C   . ARG A 1 219 ? -1.44300  -41.65300 -2.15500  1.000 69.12934  ? 219 ARG A C   1 
ATOM   1781 O O   . ARG A 1 219 ? -2.65100  -41.48300 -2.33800  1.000 70.26369  ? 219 ARG A O   1 
ATOM   1782 C CB  . ARG A 1 219 ? -0.82900  -39.49800 -1.04200  1.000 68.95037  ? 219 ARG A CB  1 
ATOM   1783 C CG  . ARG A 1 219 ? -0.94600  -40.17400 0.30300   1.000 69.77152  ? 219 ARG A CG  1 
ATOM   1784 C CD  . ARG A 1 219 ? -1.54600  -39.21300 1.28400   1.000 71.04273  ? 219 ARG A CD  1 
ATOM   1785 N NE  . ARG A 1 219 ? -2.93800  -39.53300 1.56000   1.000 74.25890  ? 219 ARG A NE  1 
ATOM   1786 C CZ  . ARG A 1 219 ? -3.68600  -38.88000 2.43800   1.000 75.86173  ? 219 ARG A CZ  1 
ATOM   1787 N NH1 . ARG A 1 219 ? -3.21000  -37.84600 3.11200   1.000 75.16428  ? 219 ARG A NH1 1 
ATOM   1788 N NH2 . ARG A 1 219 ? -4.93800  -39.28000 2.65100   1.000 79.46479  ? 219 ARG A NH2 1 
ATOM   1789 N N   . ASP A 1 220 ? -0.88900  -42.84900 -1.96200  1.000 72.96928  ? 220 ASP A N   1 
ATOM   1790 C CA  . ASP A 1 220 ? -1.64300  -44.09000 -2.13400  1.000 77.51193  ? 220 ASP A CA  1 
ATOM   1791 C C   . ASP A 1 220 ? -2.35200  -44.11100 -3.48500  1.000 78.44362  ? 220 ASP A C   1 
ATOM   1792 O O   . ASP A 1 220 ? -3.44700  -44.66400 -3.63200  1.000 82.68886  ? 220 ASP A O   1 
ATOM   1793 C CB  . ASP A 1 220 ? -2.63800  -44.30000 -0.98900  1.000 81.16499  ? 220 ASP A CB  1 
ATOM   1794 C CG  . ASP A 1 220 ? -1.96100  -44.35900 0.36000   1.000 81.05446  ? 220 ASP A CG  1 
ATOM   1795 O OD1 . ASP A 1 220 ? -0.71300  -44.46700 0.40100   1.000 78.29360  ? 220 ASP A OD1 1 
ATOM   1796 O OD2 . ASP A 1 220 ? -2.67900  -44.29300 1.38100   1.000 84.72595  ? 220 ASP A OD2 1 
ATOM   1797 N N   . GLY A 1 221 ? -1.73100  -43.48000 -4.48000  1.000 76.60655  ? 221 GLY A N   1 
ATOM   1798 C CA  . GLY A 1 221 ? -2.28200  -43.41900 -5.81000  1.000 76.58550  ? 221 GLY A CA  1 
ATOM   1799 C C   . GLY A 1 221 ? -3.30000  -42.32600 -6.04600  1.000 76.94607  ? 221 GLY A C   1 
ATOM   1800 O O   . GLY A 1 221 ? -3.69900  -42.11900 -7.20100  1.000 77.09345  ? 221 GLY A O   1 
ATOM   1801 N N   . GLU A 1 222 ? -3.73700  -41.62300 -5.00500  1.000 98.70394  ? 222 GLU A N   1 
ATOM   1802 C CA  . GLU A 1 222 ? -4.74500  -40.58400 -5.16000  1.000 99.80144  ? 222 GLU A CA  1 
ATOM   1803 C C   . GLU A 1 222 ? -4.09300  -39.27000 -5.57000  1.000 97.86963  ? 222 GLU A C   1 
ATOM   1804 O O   . GLU A 1 222 ? -3.06500  -38.87100 -5.01500  1.000 97.14849  ? 222 GLU A O   1 
ATOM   1805 C CB  . GLU A 1 222 ? -5.52700  -40.40300 -3.85700  1.000 103.08078 ? 222 GLU A CB  1 
ATOM   1806 N N   . ASP A 1 223 ? -4.69500  -38.54800 -6.50900  1.000 89.60811  ? 223 ASP A N   1 
ATOM   1807 C CA  . ASP A 1 223 ? -4.00100  -37.32200 -6.97900  1.000 88.41323  ? 223 ASP A CA  1 
ATOM   1808 C C   . ASP A 1 223 ? -4.17000  -36.20200 -5.95200  1.000 88.70011  ? 223 ASP A C   1 
ATOM   1809 O O   . ASP A 1 223 ? -5.31600  -35.83400 -5.65100  1.000 89.68444  ? 223 ASP A O   1 
ATOM   1810 C CB  . ASP A 1 223 ? -4.44300  -36.90100 -8.38000  1.000 88.50008  ? 223 ASP A CB  1 
ATOM   1811 C CG  . ASP A 1 223 ? -3.28200  -36.70900 -9.33600  1.000 87.31836  ? 223 ASP A CG  1 
ATOM   1812 O OD1 . ASP A 1 223 ? -2.35100  -35.96400 -8.98000  1.000 86.18665  ? 223 ASP A OD1 1 
ATOM   1813 O OD2 . ASP A 1 223 ? -3.31900  -37.30700 -10.42800 1.000 86.64986  ? 223 ASP A OD2 1 
ATOM   1814 N N   . GLN A 1 224 ? -3.05400  -35.66300 -5.47900  1.000 66.76853  ? 224 GLN A N   1 
ATOM   1815 C CA  . GLN A 1 224 ? -3.09000  -34.56400 -4.49100  1.000 67.41335  ? 224 GLN A CA  1 
ATOM   1816 C C   . GLN A 1 224 ? -3.09900  -33.24100 -5.24000  1.000 66.41323  ? 224 GLN A C   1 
ATOM   1817 O O   . GLN A 1 224 ? -2.32900  -32.36000 -4.86000  1.000 66.22899  ? 224 GLN A O   1 
ATOM   1818 C CB  . GLN A 1 224 ? -1.85700  -34.68600 -3.60400  1.000 66.39743  ? 224 GLN A CB  1 
ATOM   1819 C CG  . GLN A 1 224 ? -1.63300  -36.09500 -3.08600  1.000 66.80801  ? 224 GLN A CG  1 
ATOM   1820 C CD  . GLN A 1 224 ? -2.78500  -36.49500 -2.20200  1.000 69.16092  ? 224 GLN A CD  1 
ATOM   1821 O OE1 . GLN A 1 224 ? -3.62800  -37.30400 -2.57800  1.000 69.33726  ? 224 GLN A OE1 1 
ATOM   1822 N NE2 . GLN A 1 224 ? -2.83900  -35.90300 -1.02200  1.000 69.41885  ? 224 GLN A NE2 1 
ATOM   1823 N N   . THR A 1 225 ? -3.97300  -33.08900 -6.23600  1.000 104.21776 ? 225 THR A N   1 
ATOM   1824 C CA  . THR A 1 225 ? -3.89300  -31.88100 -7.05600  1.000 102.86233 ? 225 THR A CA  1 
ATOM   1825 C C   . THR A 1 225 ? -4.15200  -30.61800 -6.23800  1.000 102.47281 ? 225 THR A C   1 
ATOM   1826 O O   . THR A 1 225 ? -3.50100  -29.58800 -6.45300  1.000 101.49375 ? 225 THR A O   1 
ATOM   1827 C CB  . THR A 1 225 ? -4.86400  -31.98800 -8.23600  1.000 102.96761 ? 225 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 225 ? -4.50000  -33.11500 -9.04500  1.000 101.86484 ? 225 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 225 ? -4.85000  -30.72600 -9.09200  1.000 102.75179 ? 225 THR A CG2 1 
ATOM   1830 N N   . GLN A 1 226 ? -5.07500  -30.68100 -5.27700  1.000 100.18306 ? 226 GLN A N   1 
ATOM   1831 C CA  . GLN A 1 226 ? -5.40500  -29.48400 -4.50600  1.000 100.25939 ? 226 GLN A CA  1 
ATOM   1832 C C   . GLN A 1 226 ? -4.28800  -29.11400 -3.52900  1.000 99.81460  ? 226 GLN A C   1 
ATOM   1833 O O   . GLN A 1 226 ? -4.03000  -27.92700 -3.29700  1.000 98.33811  ? 226 GLN A O   1 
ATOM   1834 C CB  . GLN A 1 226 ? -6.72900  -29.68100 -3.76600  1.000 102.25963 ? 226 GLN A CB  1 
ATOM   1835 C CG  . GLN A 1 226 ? -7.95900  -29.81100 -4.66900  1.000 104.00984 ? 226 GLN A CG  1 
ATOM   1836 C CD  . GLN A 1 226 ? -8.46700  -28.47500 -5.20100  1.000 105.91796 ? 226 GLN A CD  1 
ATOM   1837 O OE1 . GLN A 1 226 ? -7.87900  -27.42300 -4.94900  1.000 104.27303 ? 226 GLN A OE1 1 
ATOM   1838 N NE2 . GLN A 1 226 ? -9.57100  -28.51600 -5.94000  1.000 108.98938 ? 226 GLN A NE2 1 
ATOM   1839 N N   . ASP A 1 227 ? -3.61700  -30.10500 -2.94600  1.000 72.92716  ? 227 ASP A N   1 
ATOM   1840 C CA  . ASP A 1 227 ? -2.55800  -29.84700 -1.97700  1.000 72.37184  ? 227 ASP A CA  1 
ATOM   1841 C C   . ASP A 1 227 ? -1.18900  -29.63700 -2.62700  1.000 70.38739  ? 227 ASP A C   1 
ATOM   1842 O O   . ASP A 1 227 ? -0.20700  -29.41100 -1.91200  1.000 68.95300  ? 227 ASP A O   1 
ATOM   1843 C CB  . ASP A 1 227 ? -2.48500  -30.99500 -0.95700  1.000 73.92728  ? 227 ASP A CB  1 
ATOM   1844 C CG  . ASP A 1 227 ? -3.72000  -31.06800 -0.05300  1.000 76.67761  ? 227 ASP A CG  1 
ATOM   1845 O OD1 . ASP A 1 227 ? -4.24000  -29.99900 0.33200   1.000 76.95133  ? 227 ASP A OD1 1 
ATOM   1846 O OD2 . ASP A 1 227 ? -4.16900  -32.19100 0.28000   1.000 78.09621  ? 227 ASP A OD2 1 
ATOM   1847 N N   . THR A 1 228 ? -1.10400  -29.68600 -3.95700  1.000 54.29862  ? 228 THR A N   1 
ATOM   1848 C CA  . THR A 1 228 ? 0.16300   -29.56600 -4.66700  1.000 52.49050  ? 228 THR A CA  1 
ATOM   1849 C C   . THR A 1 228 ? 0.42100   -28.10700 -5.01700  1.000 49.89019  ? 228 THR A C   1 
ATOM   1850 O O   . THR A 1 228 ? -0.47600  -27.41100 -5.50100  1.000 49.74807  ? 228 THR A O   1 
ATOM   1851 C CB  . THR A 1 228 ? 0.16000   -30.42100 -5.93700  1.000 52.47208  ? 228 THR A CB  1 
ATOM   1852 O OG1 . THR A 1 228 ? 0.06400   -31.80500 -5.58800  1.000 54.02753  ? 228 THR A OG1 1 
ATOM   1853 C CG2 . THR A 1 228 ? 1.43300   -30.20900 -6.74500  1.000 50.56133  ? 228 THR A CG2 1 
ATOM   1854 N N   . GLU A 1 229 ? 1.63200   -27.64600 -4.73400  1.000 57.54637  ? 229 GLU A N   1 
ATOM   1855 C CA  . GLU A 1 229 ? 2.11300   -26.35100 -5.18900  1.000 54.95133  ? 229 GLU A CA  1 
ATOM   1856 C C   . GLU A 1 229 ? 2.99100   -26.57000 -6.41400  1.000 53.72749  ? 229 GLU A C   1 
ATOM   1857 O O   . GLU A 1 229 ? 4.01200   -27.26000 -6.33600  1.000 53.54326  ? 229 GLU A O   1 
ATOM   1858 C CB  . GLU A 1 229 ? 2.90000   -25.64000 -4.09200  1.000 54.58812  ? 229 GLU A CB  1 
ATOM   1859 C CG  . GLU A 1 229 ? 3.83100   -24.57300 -4.63800  1.000 52.55104  ? 229 GLU A CG  1 
ATOM   1860 C CD  . GLU A 1 229 ? 4.52600   -23.78400 -3.54100  1.000 52.45366  ? 229 GLU A CD  1 
ATOM   1861 O OE1 . GLU A 1 229 ? 4.97300   -24.41200 -2.54600  1.000 53.31692  ? 229 GLU A OE1 1 
ATOM   1862 O OE2 . GLU A 1 229 ? 4.61800   -22.53900 -3.68200  1.000 52.01939  ? 229 GLU A OE2 1 
ATOM   1863 N N   . LEU A 1 230 ? 2.59200   -25.98900 -7.54000  1.000 46.60822  ? 230 LEU A N   1 
ATOM   1864 C CA  . LEU A 1 230 ? 3.31400   -26.11600 -8.80100  1.000 44.86854  ? 230 LEU A CA  1 
ATOM   1865 C C   . LEU A 1 230 ? 3.83800   -24.74300 -9.20600  1.000 42.93146  ? 230 LEU A C   1 
ATOM   1866 O O   . LEU A 1 230 ? 3.06700   -23.78500 -9.27500  1.000 42.76302  ? 230 LEU A O   1 
ATOM   1867 C CB  . LEU A 1 230 ? 2.40400   -26.66200 -9.90800  1.000 45.77917  ? 230 LEU A CB  1 
ATOM   1868 C CG  . LEU A 1 230 ? 1.80000   -28.06600 -9.91600  1.000 48.93745  ? 230 LEU A CG  1 
ATOM   1869 C CD1 . LEU A 1 230 ? 0.52100   -28.06200 -10.74400 1.000 49.45330  ? 230 LEU A CD1 1 
ATOM   1870 C CD2 . LEU A 1 230 ? 2.77200   -29.07300 -10.50000 1.000 48.65057  ? 230 LEU A CD2 1 
ATOM   1871 N N   . VAL A 1 231 ? 5.12100   -24.63900 -9.49100  1.000 39.46263  ? 231 VAL A N   1 
ATOM   1872 C CA  . VAL A 1 231 ? 5.61700   -23.36900 -10.01600 1.000 37.70189  ? 231 VAL A CA  1 
ATOM   1873 C C   . VAL A 1 231 ? 5.42000   -23.34000 -11.51600 1.000 36.68861  ? 231 VAL A C   1 
ATOM   1874 O O   . VAL A 1 231 ? 5.36400   -24.37400 -12.19000 1.000 36.80441  ? 231 VAL A O   1 
ATOM   1875 C CB  . VAL A 1 231 ? 7.09800   -23.09400 -9.69200  1.000 36.74651  ? 231 VAL A CB  1 
ATOM   1876 C CG1 . VAL A 1 231 ? 7.22800   -22.42600 -8.33100  1.000 38.25722  ? 231 VAL A CG1 1 
ATOM   1877 C CG2 . VAL A 1 231 ? 7.91400   -24.36300 -9.84400  1.000 35.78061  ? 231 VAL A CG2 1 
ATOM   1878 N N   . GLU A 1 232 ? 5.35600   -22.11900 -12.04000 1.000 39.33366  ? 232 GLU A N   1 
ATOM   1879 C CA  . GLU A 1 232 ? 5.34800   -21.90800 -13.47000 1.000 38.69938  ? 232 GLU A CA  1 
ATOM   1880 C C   . GLU A 1 232 ? 6.59600   -22.51800 -14.09600 1.000 37.40975  ? 232 GLU A C   1 
ATOM   1881 O O   . GLU A 1 232 ? 7.69900   -22.40100 -13.56100 1.000 37.28868  ? 232 GLU A O   1 
ATOM   1882 C CB  . GLU A 1 232 ? 5.26400   -20.40400 -13.75100 1.000 38.71517  ? 232 GLU A CB  1 
ATOM   1883 C CG  . GLU A 1 232 ? 5.32800   -20.05800 -15.21400 1.000 39.19154  ? 232 GLU A CG  1 
ATOM   1884 C CD  . GLU A 1 232 ? 5.15400   -18.59100 -15.45200 1.000 39.51263  ? 232 GLU A CD  1 
ATOM   1885 O OE1 . GLU A 1 232 ? 5.20800   -17.82000 -14.47600 1.000 39.91268  ? 232 GLU A OE1 1 
ATOM   1886 O OE2 . GLU A 1 232 ? 4.94300   -18.20000 -16.63200 1.000 39.87847  ? 232 GLU A OE2 1 
ATOM   1887 N N   . THR A 1 233 ? 6.40800   -23.20800 -15.21600 1.000 34.95945  ? 233 THR A N   1 
ATOM   1888 C CA  . THR A 1 233 ? 7.54400   -23.71500 -15.97900 1.000 34.49098  ? 233 THR A CA  1 
ATOM   1889 C C   . THR A 1 233 ? 8.44800   -22.54700 -16.35800 1.000 34.51466  ? 233 THR A C   1 
ATOM   1890 O O   . THR A 1 233 ? 7.97100   -21.47800 -16.74400 1.000 34.70153  ? 233 THR A O   1 
ATOM   1891 C CB  . THR A 1 233 ? 7.05800   -24.44900 -17.23300 1.000 33.88564  ? 233 THR A CB  1 
ATOM   1892 O OG1 . THR A 1 233 ? 6.20200   -25.53100 -16.84900 1.000 34.90945  ? 233 THR A OG1 1 
ATOM   1893 C CG2 . THR A 1 233 ? 8.23200   -25.00500 -18.01900 1.000 32.98817  ? 233 THR A CG2 1 
ATOM   1894 N N   . ARG A 1 234 ? 9.75400   -22.74200 -16.22700 1.000 31.05372  ? 234 ARG A N   1 
ATOM   1895 C CA  . ARG A 1 234 ? 10.65800  -21.61000 -16.34700 1.000 32.07227  ? 234 ARG A CA  1 
ATOM   1896 C C   . ARG A 1 234 ? 11.83100  -21.96100 -17.25000 1.000 33.32242  ? 234 ARG A C   1 
ATOM   1897 O O   . ARG A 1 234 ? 12.25300  -23.12400 -17.31700 1.000 32.29598  ? 234 ARG A O   1 
ATOM   1898 C CB  . ARG A 1 234 ? 11.17100  -21.18300 -14.96100 1.000 33.05923  ? 234 ARG A CB  1 
ATOM   1899 C CG  . ARG A 1 234 ? 12.12800  -22.16400 -14.33000 1.000 33.19082  ? 234 ARG A CG  1 
ATOM   1900 C CD  . ARG A 1 234 ? 12.18200  -21.98700 -12.82500 1.000 33.57771  ? 234 ARG A CD  1 
ATOM   1901 N NE  . ARG A 1 234 ? 13.23800  -22.80000 -12.23400 1.000 34.30674  ? 234 ARG A NE  1 
ATOM   1902 C CZ  . ARG A 1 234 ? 13.48500  -22.87300 -10.93600 1.000 34.93050  ? 234 ARG A CZ  1 
ATOM   1903 N NH1 . ARG A 1 234 ? 12.77000  -22.18600 -10.05800 1.000 34.79101  ? 234 ARG A NH1 1 
ATOM   1904 N NH2 . ARG A 1 234 ? 14.46700  -23.65600 -10.50700 1.000 34.91471  ? 234 ARG A NH2 1 
ATOM   1905 N N   . PRO A 1 235 ? 12.37600  -20.97300 -17.96300 1.000 30.83264  ? 235 PRO A N   1 
ATOM   1906 C CA  . PRO A 1 235 ? 13.49000  -21.25000 -18.87600 1.000 31.94594  ? 235 PRO A CA  1 
ATOM   1907 C C   . PRO A 1 235 ? 14.81900  -21.33600 -18.13600 1.000 31.43535  ? 235 PRO A C   1 
ATOM   1908 O O   . PRO A 1 235 ? 15.12100  -20.52900 -17.25400 1.000 31.93541  ? 235 PRO A O   1 
ATOM   1909 C CB  . PRO A 1 235 ? 13.46000  -20.04800 -19.83500 1.000 33.75668  ? 235 PRO A CB  1 
ATOM   1910 C CG  . PRO A 1 235 ? 12.93200  -18.91600 -18.95400 1.000 32.84341  ? 235 PRO A CG  1 
ATOM   1911 C CD  . PRO A 1 235 ? 11.91400  -19.57400 -18.05200 1.000 31.21690  ? 235 PRO A CD  1 
ATOM   1912 N N   . ALA A 1 236 ? 15.61500  -22.34000 -18.49600 1.000 33.14608  ? 236 ALA A N   1 
ATOM   1913 C CA  . ALA A 1 236 ? 16.94700  -22.47100 -17.92900 1.000 33.18819  ? 236 ALA A CA  1 
ATOM   1914 C C   . ALA A 1 236 ? 17.94000  -21.48300 -18.53400 1.000 34.72785  ? 236 ALA A C   1 
ATOM   1915 O O   . ALA A 1 236 ? 18.94200  -21.16000 -17.89500 1.000 34.71206  ? 236 ALA A O   1 
ATOM   1916 C CB  . ALA A 1 236 ? 17.45600  -23.90700 -18.10700 1.000 31.68275  ? 236 ALA A CB  1 
ATOM   1917 N N   . GLY A 1 237 ? 17.66500  -20.96400 -19.71900 1.000 38.15194  ? 237 GLY A N   1 
ATOM   1918 C CA  . GLY A 1 237 ? 18.57600  -20.07300 -20.41100 1.000 39.79688  ? 237 GLY A CA  1 
ATOM   1919 C C   . GLY A 1 237 ? 19.34500  -20.72000 -21.54300 1.000 40.53381  ? 237 GLY A C   1 
ATOM   1920 O O   . GLY A 1 237 ? 19.97000  -20.00100 -22.33700 1.000 42.26296  ? 237 GLY A O   1 
ATOM   1921 N N   . ASP A 1 238 ? 19.31000  -22.05100 -21.64200 1.000 41.62868  ? 238 ASP A N   1 
ATOM   1922 C CA  . ASP A 1 238 ? 19.97700  -22.81500 -22.68700 1.000 42.25770  ? 238 ASP A CA  1 
ATOM   1923 C C   . ASP A 1 238 ? 18.98900  -23.48800 -23.63700 1.000 42.21822  ? 238 ASP A C   1 
ATOM   1924 O O   . ASP A 1 238 ? 19.34200  -24.47900 -24.27500 1.000 42.57089  ? 238 ASP A O   1 
ATOM   1925 C CB  . ASP A 1 238 ? 20.89000  -23.87000 -22.05900 1.000 41.01808  ? 238 ASP A CB  1 
ATOM   1926 C CG  . ASP A 1 238 ? 20.15000  -24.77700 -21.07400 1.000 39.72318  ? 238 ASP A CG  1 
ATOM   1927 O OD1 . ASP A 1 238 ? 18.89400  -24.73900 -21.02200 1.000 38.64674  ? 238 ASP A OD1 1 
ATOM   1928 O OD2 . ASP A 1 238 ? 20.82800  -25.52400 -20.33800 1.000 39.30734  ? 238 ASP A OD2 1 
ATOM   1929 N N   . ARG A 1 239 ? 17.75900  -22.97900 -23.72700 1.000 34.20936  ? 239 ARG A N   1 
ATOM   1930 C CA  . ARG A 1 239 ? 16.67000  -23.56500 -24.50400 1.000 34.09356  ? 239 ARG A CA  1 
ATOM   1931 C C   . ARG A 1 239 ? 16.14000  -24.87000 -23.90300 1.000 32.06700  ? 239 ARG A C   1 
ATOM   1932 O O   . ARG A 1 239 ? 15.48200  -25.65000 -24.60000 1.000 31.94330  ? 239 ARG A O   1 
ATOM   1933 C CB  . ARG A 1 239 ? 17.05300  -23.77500 -25.98400 1.000 36.05432  ? 239 ARG A CB  1 
ATOM   1934 C CG  . ARG A 1 239 ? 17.47700  -22.45100 -26.67700 1.000 39.08627  ? 239 ARG A CG  1 
ATOM   1935 C CD  . ARG A 1 239 ? 17.69300  -22.54400 -28.19500 1.000 41.39180  ? 239 ARG A CD  1 
ATOM   1936 N NE  . ARG A 1 239 ? 18.16300  -21.26400 -28.73600 1.000 43.97633  ? 239 ARG A NE  1 
ATOM   1937 C CZ  . ARG A 1 239 ? 19.43200  -20.87700 -28.76000 1.000 46.13448  ? 239 ARG A CZ  1 
ATOM   1938 N NH1 . ARG A 1 239 ? 20.40200  -21.66600 -28.32600 1.000 45.76075  ? 239 ARG A NH1 1 
ATOM   1939 N NH2 . ARG A 1 239 ? 19.74000  -19.66500 -29.22500 1.000 46.71876  ? 239 ARG A NH2 1 
ATOM   1940 N N   . THR A 1 240 ? 16.39000  -25.13300 -22.62700 1.000 35.99116  ? 240 THR A N   1 
ATOM   1941 C CA  . THR A 1 240 ? 15.61200  -26.11900 -21.89400 1.000 33.82248  ? 240 THR A CA  1 
ATOM   1942 C C   . THR A 1 240 ? 14.77500  -25.41100 -20.83000 1.000 33.12502  ? 240 THR A C   1 
ATOM   1943 O O   . THR A 1 240 ? 14.83800  -24.19000 -20.66000 1.000 34.49098  ? 240 THR A O   1 
ATOM   1944 C CB  . THR A 1 240 ? 16.49200  -27.19500 -21.24900 1.000 33.37242  ? 240 THR A CB  1 
ATOM   1945 O OG1 . THR A 1 240 ? 17.36100  -26.61500 -20.27000 1.000 33.97249  ? 240 THR A OG1 1 
ATOM   1946 C CG2 . THR A 1 240 ? 17.30000  -27.94000 -22.30100 1.000 35.39372  ? 240 THR A CG2 1 
ATOM   1947 N N   . PHE A 1 241 ? 13.98200  -26.20500 -20.10300 1.000 30.80106  ? 241 PHE A N   1 
ATOM   1948 C CA  . PHE A 1 241 ? 13.03900  -25.68100 -19.13200 1.000 30.78001  ? 241 PHE A CA  1 
ATOM   1949 C C   . PHE A 1 241 ? 13.17100  -26.45600 -17.82200 1.000 30.25889  ? 241 PHE A C   1 
ATOM   1950 O O   . PHE A 1 241 ? 13.83300  -27.49300 -17.75100 1.000 29.81147  ? 241 PHE A O   1 
ATOM   1951 C CB  . PHE A 1 241 ? 11.60600  -25.74100 -19.67600 1.000 30.28521  ? 241 PHE A CB  1 
ATOM   1952 C CG  . PHE A 1 241 ? 11.37600  -24.86000 -20.88600 1.000 31.51694  ? 241 PHE A CG  1 
ATOM   1953 C CD1 . PHE A 1 241 ? 11.67700  -25.31400 -22.16000 1.000 31.76170  ? 241 PHE A CD1 1 
ATOM   1954 C CD2 . PHE A 1 241 ? 10.85900  -23.59300 -20.74400 1.000 32.84868  ? 241 PHE A CD2 1 
ATOM   1955 C CE1 . PHE A 1 241 ? 11.47800  -24.50000 -23.27600 1.000 33.28557  ? 241 PHE A CE1 1 
ATOM   1956 C CE2 . PHE A 1 241 ? 10.65700  -22.78500 -21.84600 1.000 34.12251  ? 241 PHE A CE2 1 
ATOM   1957 C CZ  . PHE A 1 241 ? 10.95000  -23.25100 -23.11600 1.000 34.38044  ? 241 PHE A CZ  1 
ATOM   1958 N N   . GLN A 1 242 ? 12.53900  -25.91400 -16.78000 1.000 29.29562  ? 242 GLN A N   1 
ATOM   1959 C CA  . GLN A 1 242 ? 12.62500  -26.39700 -15.40700 1.000 29.40616  ? 242 GLN A CA  1 
ATOM   1960 C C   . GLN A 1 242 ? 11.24600  -26.24800 -14.78200 1.000 29.79041  ? 242 GLN A C   1 
ATOM   1961 O O   . GLN A 1 242 ? 10.49900  -25.32000 -15.10700 1.000 30.09308  ? 242 GLN A O   1 
ATOM   1962 C CB  . GLN A 1 242 ? 13.65600  -25.61100 -14.55200 1.000 31.28796  ? 242 GLN A CB  1 
ATOM   1963 C CG  . GLN A 1 242 ? 15.08900  -25.55700 -15.09400 1.000 31.20637  ? 242 GLN A CG  1 
ATOM   1964 C CD  . GLN A 1 242 ? 16.05800  -24.80200 -14.16200 1.000 32.24860  ? 242 GLN A CD  1 
ATOM   1965 O OE1 . GLN A 1 242 ? 15.64800  -24.21800 -13.16200 1.000 33.37242  ? 242 GLN A OE1 1 
ATOM   1966 N NE2 . GLN A 1 242 ? 17.34400  -24.83900 -14.48500 1.000 32.16965  ? 242 GLN A NE2 1 
ATOM   1967 N N   . LYS A 1 243 ? 10.90600  -27.17600 -13.88300 1.000 26.91112  ? 243 LYS A N   1 
ATOM   1968 C CA  . LYS A 1 243 ? 9.66100   -27.06800 -13.13600 1.000 27.73754  ? 243 LYS A CA  1 
ATOM   1969 C C   . LYS A 1 243 ? 9.82100   -27.89000 -11.86400 1.000 28.77977  ? 243 LYS A C   1 
ATOM   1970 O O   . LYS A 1 243 ? 10.64500  -28.80000 -11.80500 1.000 28.61396  ? 243 LYS A O   1 
ATOM   1971 C CB  . LYS A 1 243 ? 8.47800   -27.56900 -13.97900 1.000 29.03506  ? 243 LYS A CB  1 
ATOM   1972 C CG  . LYS A 1 243 ? 7.11100   -27.10400 -13.52100 1.000 31.05372  ? 243 LYS A CG  1 
ATOM   1973 C CD  . LYS A 1 243 ? 6.04000   -27.77900 -14.36000 1.000 32.88815  ? 243 LYS A CD  1 
ATOM   1974 C CE  . LYS A 1 243 ? 4.63600   -27.24400 -14.07100 1.000 34.05935  ? 243 LYS A CE  1 
ATOM   1975 N NZ  . LYS A 1 243 ? 4.46900   -25.81500 -14.41100 1.000 32.22755  ? 243 LYS A NZ  1 
ATOM   1976 N N   . TRP A 1 244 ? 9.05500   -27.55000 -10.83500 1.000 31.36955  ? 244 TRP A N   1 
ATOM   1977 C CA  . TRP A 1 244 ? 8.95800   -28.43100 -9.68000  1.000 32.93816  ? 244 TRP A CA  1 
ATOM   1978 C C   . TRP A 1 244 ? 7.53700   -28.42600 -9.15000  1.000 36.28856  ? 244 TRP A C   1 
ATOM   1979 O O   . TRP A 1 244 ? 6.73900   -27.53100 -9.44400  1.000 36.47016  ? 244 TRP A O   1 
ATOM   1980 C CB  . TRP A 1 244 ? 9.95800   -28.08200 -8.54800  1.000 32.73287  ? 244 TRP A CB  1 
ATOM   1981 C CG  . TRP A 1 244 ? 9.98100   -26.66700 -7.99000  1.000 33.21451  ? 244 TRP A CG  1 
ATOM   1982 C CD1 . TRP A 1 244 ? 10.94400  -25.71700 -8.22900  1.000 32.60654  ? 244 TRP A CD1 1 
ATOM   1983 C CD2 . TRP A 1 244 ? 9.04400   -26.05800 -7.07700  1.000 34.27516  ? 244 TRP A CD2 1 
ATOM   1984 N NE1 . TRP A 1 244 ? 10.66100  -24.56300 -7.53500  1.000 33.64877  ? 244 TRP A NE1 1 
ATOM   1985 C CE2 . TRP A 1 244 ? 9.51000   -24.74700 -6.81200  1.000 34.90155  ? 244 TRP A CE2 1 
ATOM   1986 C CE3 . TRP A 1 244 ? 7.87500   -26.49800 -6.44600  1.000 36.63071  ? 244 TRP A CE3 1 
ATOM   1987 C CZ2 . TRP A 1 244 ? 8.84100   -23.87100 -5.95300  1.000 35.47004  ? 244 TRP A CZ2 1 
ATOM   1988 C CZ3 . TRP A 1 244 ? 7.19800   -25.62300 -5.61300  1.000 37.95455  ? 244 TRP A CZ3 1 
ATOM   1989 C CH2 . TRP A 1 244 ? 7.68600   -24.32300 -5.36700  1.000 36.99128  ? 244 TRP A CH2 1 
ATOM   1990 N N   . ALA A 1 245 ? 7.23300   -29.45300 -8.36000  1.000 30.14835  ? 245 ALA A N   1 
ATOM   1991 C CA  . ALA A 1 245 ? 5.94400   -29.59100 -7.69800  1.000 33.57771  ? 245 ALA A CA  1 
ATOM   1992 C C   . ALA A 1 245 ? 6.19200   -30.03800 -6.26500  1.000 34.44624  ? 245 ALA A C   1 
ATOM   1993 O O   . ALA A 1 245 ? 6.99400   -30.95000 -6.03700  1.000 33.58824  ? 245 ALA A O   1 
ATOM   1994 C CB  . ALA A 1 245 ? 5.07200   -30.60300 -8.43500  1.000 36.69651  ? 245 ALA A CB  1 
ATOM   1995 N N   . ALA A 1 246 ? 5.52500   -29.38900 -5.29900  1.000 34.93577  ? 246 ALA A N   1 
ATOM   1996 C CA  . ALA A 1 246 ? 5.72900   -29.68300 -3.88400  1.000 35.23844  ? 246 ALA A CA  1 
ATOM   1997 C C   . ALA A 1 246 ? 4.41600   -29.99100 -3.17900  1.000 37.05181  ? 246 ALA A C   1 
ATOM   1998 O O   . ALA A 1 246 ? 3.37600   -29.39600 -3.48300  1.000 37.74400  ? 246 ALA A O   1 
ATOM   1999 C CB  . ALA A 1 246 ? 6.40000   -28.52100 -3.13900  1.000 33.62245  ? 246 ALA A CB  1 
ATOM   2000 N N   . VAL A 1 247 ? 4.49200   -30.89400 -2.20300  1.000 37.15445  ? 247 VAL A N   1 
ATOM   2001 C CA  . VAL A 1 247 ? 3.39000   -31.18900 -1.29700  1.000 38.47567  ? 247 VAL A CA  1 
ATOM   2002 C C   . VAL A 1 247 ? 3.91600   -31.17900 0.13100   1.000 38.15194  ? 247 VAL A C   1 
ATOM   2003 O O   . VAL A 1 247 ? 5.09100   -31.46800 0.38500   1.000 36.83073  ? 247 VAL A O   1 
ATOM   2004 C CB  . VAL A 1 247 ? 2.71400   -32.53900 -1.62400  1.000 39.97848  ? 247 VAL A CB  1 
ATOM   2005 C CG1 . VAL A 1 247 ? 2.06200   -32.45300 -2.98300  1.000 41.29969  ? 247 VAL A CG1 1 
ATOM   2006 C CG2 . VAL A 1 247 ? 3.73800   -33.69100 -1.58800  1.000 38.64674  ? 247 VAL A CG2 1 
ATOM   2007 N N   . VAL A 1 248 ? 3.03500   -30.82200 1.06400   1.000 42.60511  ? 248 VAL A N   1 
ATOM   2008 C CA  . VAL A 1 248 ? 3.34600   -30.88000 2.48200   1.000 42.84461  ? 248 VAL A CA  1 
ATOM   2009 C C   . VAL A 1 248 ? 2.80900   -32.19600 3.02700   1.000 44.33953  ? 248 VAL A C   1 
ATOM   2010 O O   . VAL A 1 248 ? 1.64700   -32.56100 2.78800   1.000 46.11342  ? 248 VAL A O   1 
ATOM   2011 C CB  . VAL A 1 248 ? 2.75600   -29.67500 3.22600   1.000 43.54996  ? 248 VAL A CB  1 
ATOM   2012 C CG1 . VAL A 1 248 ? 3.11200   -29.72900 4.72700   1.000 45.26332  ? 248 VAL A CG1 1 
ATOM   2013 C CG2 . VAL A 1 248 ? 3.26100   -28.40600 2.61000   1.000 42.04451  ? 248 VAL A CG2 1 
ATOM   2014 N N   . VAL A 1 249 ? 3.66500   -32.93000 3.72700   1.000 45.07646  ? 249 VAL A N   1 
ATOM   2015 C CA  . VAL A 1 249 ? 3.33000   -34.28000 4.14600   1.000 46.17396  ? 249 VAL A CA  1 
ATOM   2016 C C   . VAL A 1 249 ? 3.57600   -34.41100 5.64500   1.000 48.05839  ? 249 VAL A C   1 
ATOM   2017 O O   . VAL A 1 249 ? 4.48800   -33.76600 6.18700   1.000 47.24514  ? 249 VAL A O   1 
ATOM   2018 C CB  . VAL A 1 249 ? 4.14300   -35.31400 3.35600   1.000 44.88433  ? 249 VAL A CB  1 
ATOM   2019 C CG1 . VAL A 1 249 ? 4.02300   -35.05200 1.84900   1.000 44.25794  ? 249 VAL A CG1 1 
ATOM   2020 C CG2 . VAL A 1 249 ? 5.58900   -35.27400 3.77700   1.000 43.11043  ? 249 VAL A CG2 1 
ATOM   2021 N N   . PRO A 1 250 ? 2.77600   -35.20500 6.35200   1.000 51.47459  ? 250 PRO A N   1 
ATOM   2022 C CA  . PRO A 1 250 ? 3.10300   -35.51400 7.74700   1.000 53.66433  ? 250 PRO A CA  1 
ATOM   2023 C C   . PRO A 1 250 ? 4.43700   -36.23900 7.82000   1.000 52.61683  ? 250 PRO A C   1 
ATOM   2024 O O   . PRO A 1 250 ? 4.72600   -37.13800 7.02000   1.000 51.80884  ? 250 PRO A O   1 
ATOM   2025 C CB  . PRO A 1 250 ? 1.94600   -36.41400 8.20700   1.000 57.48584  ? 250 PRO A CB  1 
ATOM   2026 C CG  . PRO A 1 250 ? 0.83800   -36.15100 7.21500   1.000 57.44899  ? 250 PRO A CG  1 
ATOM   2027 C CD  . PRO A 1 250 ? 1.51600   -35.82400 5.91100   1.000 53.39851  ? 250 PRO A CD  1 
ATOM   2028 N N   . SER A 1 251 ? 5.26200   -35.82300 8.77400   1.000 68.30819  ? 251 SER A N   1 
ATOM   2029 C CA  A SER A 1 251 ? 6.53800   -36.48800 8.98100   1.000 67.81339  ? 251 SER A CA  1 
ATOM   2030 C CA  B SER A 1 251 ? 6.54000   -36.48600 8.99200   0.000 67.77918  ? 251 SER A CA  1 
ATOM   2031 C C   . SER A 1 251 ? 6.30900   -37.96000 9.29400   1.000 69.11881  ? 251 SER A C   1 
ATOM   2032 O O   . SER A 1 251 ? 5.44500   -38.31100 10.09800  1.000 71.06905  ? 251 SER A O   1 
ATOM   2033 C CB  A SER A 1 251 ? 7.31700   -35.79500 10.09900  1.000 67.51336  ? 251 SER A CB  1 
ATOM   2034 C CB  B SER A 1 251 ? 7.29800   -35.81400 10.13600  0.000 67.54494  ? 251 SER A CB  1 
ATOM   2035 O OG  A SER A 1 251 ? 7.86000   -34.57300 9.61200   1.000 66.84486  ? 251 SER A OG  1 
ATOM   2036 O OG  B SER A 1 251 ? 7.61600   -34.47200 9.81200   0.000 66.70010  ? 251 SER A OG  1 
ATOM   2037 N N   . GLY A 1 252 ? 7.06500   -38.82200 8.62300   1.000 59.82823  ? 252 GLY A N   1 
ATOM   2038 C CA  . GLY A 1 252 ? 6.88500   -40.24600 8.75800   1.000 61.63897  ? 252 GLY A CA  1 
ATOM   2039 C C   . GLY A 1 252 ? 5.98900   -40.87300 7.71200   1.000 61.84163  ? 252 GLY A C   1 
ATOM   2040 O O   . GLY A 1 252 ? 5.96900   -42.10200 7.60000   1.000 63.84976  ? 252 GLY A O   1 
ATOM   2041 N N   . GLU A 1 253 ? 5.26200   -40.07600 6.92800   1.000 55.74616  ? 253 GLU A N   1 
ATOM   2042 C CA  . GLU A 1 253 ? 4.39200   -40.60200 5.88400   1.000 56.00408  ? 253 GLU A CA  1 
ATOM   2043 C C   . GLU A 1 253 ? 4.96100   -40.39200 4.48800   1.000 52.97214  ? 253 GLU A C   1 
ATOM   2044 O O   . GLU A 1 253 ? 4.24300   -40.59700 3.50600   1.000 53.55379  ? 253 GLU A O   1 
ATOM   2045 C CB  . GLU A 1 253 ? 2.99600   -39.97900 5.98700   1.000 57.09369  ? 253 GLU A CB  1 
ATOM   2046 C CG  . GLU A 1 253 ? 2.14700   -40.54500 7.15800   1.000 61.64160  ? 253 GLU A CG  1 
ATOM   2047 C CD  . GLU A 1 253 ? 0.79000   -39.86800 7.28500   1.000 63.23390  ? 253 GLU A CD  1 
ATOM   2048 O OE1 . GLU A 1 253 ? 0.33500   -39.23200 6.30800   1.000 61.79425  ? 253 GLU A OE1 1 
ATOM   2049 O OE2 . GLU A 1 253 ? 0.18400   -39.94600 8.36700   1.000 66.65273  ? 253 GLU A OE2 1 
ATOM   2050 N N   . GLU A 1 254 ? 6.24200   -40.02400 4.38300   1.000 54.51443  ? 254 GLU A N   1 
ATOM   2051 C CA  . GLU A 1 254 ? 6.84300   -39.70900 3.08600   1.000 53.10374  ? 254 GLU A CA  1 
ATOM   2052 C C   . GLU A 1 254 ? 6.73800   -40.88000 2.11600   1.000 53.77224  ? 254 GLU A C   1 
ATOM   2053 O O   . GLU A 1 254 ? 6.48500   -40.68200 0.92100   1.000 53.21164  ? 254 GLU A O   1 
ATOM   2054 C CB  . GLU A 1 254 ? 8.30700   -39.31200 3.26700   1.000 51.75621  ? 254 GLU A CB  1 
ATOM   2055 C CG  . GLU A 1 254 ? 8.53100   -37.95200 3.89700   1.000 51.14561  ? 254 GLU A CG  1 
ATOM   2056 C CD  . GLU A 1 254 ? 8.54500   -37.98400 5.42400   1.000 52.51945  ? 254 GLU A CD  1 
ATOM   2057 O OE1 . GLU A 1 254 ? 8.22700   -39.03100 6.02600   1.000 52.89582  ? 254 GLU A OE1 1 
ATOM   2058 O OE2 . GLU A 1 254 ? 8.88200   -36.93400 6.02100   1.000 52.14573  ? 254 GLU A OE2 1 
ATOM   2059 N N   . GLN A 1 255 ? 6.90300   -42.11100 2.61700   1.000 59.80454  ? 255 GLN A N   1 
ATOM   2060 C CA  . GLN A 1 255 ? 6.82400   -43.29000 1.76200   1.000 60.43883  ? 255 GLN A CA  1 
ATOM   2061 C C   . GLN A 1 255 ? 5.48600   -43.39600 1.04100   1.000 60.78887  ? 255 GLN A C   1 
ATOM   2062 O O   . GLN A 1 255 ? 5.41200   -44.04800 -0.00100  1.000 62.08639  ? 255 GLN A O   1 
ATOM   2063 C CB  . GLN A 1 255 ? 7.06200   -44.57100 2.58100   1.000 64.04978  ? 255 GLN A CB  1 
ATOM   2064 C CG  . GLN A 1 255 ? 8.47600   -44.73300 3.16000   1.000 64.80777  ? 255 GLN A CG  1 
ATOM   2065 C CD  . GLN A 1 255 ? 8.55100   -45.78800 4.26400   1.000 69.07144  ? 255 GLN A CD  1 
ATOM   2066 O OE1 . GLN A 1 255 ? 8.24600   -45.51100 5.42500   1.000 69.52676  ? 255 GLN A OE1 1 
ATOM   2067 N NE2 . GLN A 1 255 ? 8.96100   -46.99800 3.90500   1.000 71.09010  ? 255 GLN A NE2 1 
ATOM   2068 N N   . ARG A 1 256 ? 4.43200   -42.75800 1.55100   1.000 58.20435  ? 256 ARG A N   1 
ATOM   2069 C CA  . ARG A 1 256 ? 3.13300   -42.83600 0.89200   1.000 59.54135  ? 256 ARG A CA  1 
ATOM   2070 C C   . ARG A 1 256 ? 3.06400   -42.02600 -0.39600  1.000 59.60188  ? 256 ARG A C   1 
ATOM   2071 O O   . ARG A 1 256 ? 2.12400   -42.21200 -1.17500  1.000 60.64938  ? 256 ARG A O   1 
ATOM   2072 C CB  . ARG A 1 256 ? 2.03700   -42.35600 1.83600   1.000 61.65476  ? 256 ARG A CB  1 
ATOM   2073 C CG  . ARG A 1 256 ? 1.74100   -43.32400 2.97400   1.000 64.91568  ? 256 ARG A CG  1 
ATOM   2074 C CD  . ARG A 1 256 ? 0.88200   -42.66500 4.02700   1.000 66.76327  ? 256 ARG A CD  1 
ATOM   2075 N NE  . ARG A 1 256 ? -0.55100  -42.82000 3.79200   1.000 70.31633  ? 256 ARG A NE  1 
ATOM   2076 C CZ  . ARG A 1 256 ? -1.43100  -41.82600 3.81800   1.000 70.77428  ? 256 ARG A CZ  1 
ATOM   2077 N NH1 . ARG A 1 256 ? -1.04900  -40.56600 3.98700   1.000 67.62127  ? 256 ARG A NH1 1 
ATOM   2078 N NH2 . ARG A 1 256 ? -2.73000  -42.10700 3.71300   1.000 74.37734  ? 256 ARG A NH2 1 
ATOM   2079 N N   . TYR A 1 257 ? 4.02100   -41.14300 -0.64100  1.000 50.13759  ? 257 TYR A N   1 
ATOM   2080 C CA  . TYR A 1 257 ? 3.91300   -40.15100 -1.70100  1.000 49.78492  ? 257 TYR A CA  1 
ATOM   2081 C C   . TYR A 1 257 ? 4.81000   -40.52700 -2.87100  1.000 47.72151  ? 257 TYR A C   1 
ATOM   2082 O O   . TYR A 1 257 ? 5.96900   -40.90500 -2.68000  1.000 46.69507  ? 257 TYR A O   1 
ATOM   2083 C CB  . TYR A 1 257 ? 4.26200   -38.74800 -1.17900  1.000 49.49278  ? 257 TYR A CB  1 
ATOM   2084 C CG  . TYR A 1 257 ? 3.21800   -38.18000 -0.24300  1.000 51.29562  ? 257 TYR A CG  1 
ATOM   2085 C CD1 . TYR A 1 257 ? 3.19300   -38.53800 1.09700   1.000 51.68778  ? 257 TYR A CD1 1 
ATOM   2086 C CD2 . TYR A 1 257 ? 2.24600   -37.30200 -0.70200  1.000 52.60368  ? 257 TYR A CD2 1 
ATOM   2087 C CE1 . TYR A 1 257 ? 2.24400   -38.03100 1.95500   1.000 53.58274  ? 257 TYR A CE1 1 
ATOM   2088 C CE2 . TYR A 1 257 ? 1.28800   -36.79100 0.15300   1.000 54.52759  ? 257 TYR A CE2 1 
ATOM   2089 C CZ  . TYR A 1 257 ? 1.29300   -37.15900 1.48400   1.000 54.73288  ? 257 TYR A CZ  1 
ATOM   2090 O OH  . TYR A 1 257 ? 0.35100   -36.65700 2.35500   1.000 56.35413  ? 257 TYR A OH  1 
ATOM   2091 N N   . THR A 1 258 ? 4.27000   -40.42800 -4.07600  1.000 45.92130  ? 258 THR A N   1 
ATOM   2092 C CA  . THR A 1 258 ? 5.03000   -40.67400 -5.28800  1.000 44.87643  ? 258 THR A CA  1 
ATOM   2093 C C   . THR A 1 258 ? 4.84300   -39.49200 -6.21700  1.000 44.72642  ? 258 THR A C   1 
ATOM   2094 O O   . THR A 1 258 ? 3.73900   -38.95600 -6.33700  1.000 46.67402  ? 258 THR A O   1 
ATOM   2095 C CB  . THR A 1 258 ? 4.59300   -41.97400 -6.00200  1.000 45.20805  ? 258 THR A CB  1 
ATOM   2096 O OG1 . THR A 1 258 ? 3.18400   -41.93400 -6.25400  1.000 46.97932  ? 258 THR A OG1 1 
ATOM   2097 C CG2 . THR A 1 258 ? 4.91800   -43.19100 -5.16400  1.000 47.47411  ? 258 THR A CG2 1 
ATOM   2098 N N   . CYS A 1 259 ? 5.92800   -39.07500 -6.85400  1.000 43.54469  ? 259 CYS A N   1 
ATOM   2099 C CA  . CYS A 1 259 ? 5.87500   -38.04200 -7.87400  1.000 43.56312  ? 259 CYS A CA  1 
ATOM   2100 C C   . CYS A 1 259 ? 5.80600   -38.70500 -9.24300  1.000 43.59733  ? 259 CYS A C   1 
ATOM   2101 O O   . CYS A 1 259 ? 6.52600   -39.67600 -9.50800  1.000 42.34718  ? 259 CYS A O   1 
ATOM   2102 C CB  . CYS A 1 259 ? 7.08900   -37.11100 -7.79300  1.000 41.69974  ? 259 CYS A CB  1 
ATOM   2103 S SG  . CYS A 1 259 ? 7.12200   -35.91400 -9.16600  1.000 41.89450  ? 259 CYS A SG  1 
ATOM   2104 N N   . HIS A 1 260 ? 4.92200   -38.20600 -10.09800 1.000 43.53154  ? 260 HIS A N   1 
ATOM   2105 C CA  . HIS A 1 260 ? 4.74200   -38.76400 -11.43100 1.000 43.41836  ? 260 HIS A CA  1 
ATOM   2106 C C   . HIS A 1 260 ? 5.11100   -37.70100 -12.44900 1.000 42.28928  ? 260 HIS A C   1 
ATOM   2107 O O   . HIS A 1 260 ? 4.73200   -36.53600 -12.29900 1.000 43.08938  ? 260 HIS A O   1 
ATOM   2108 C CB  . HIS A 1 260 ? 3.31100   -39.26500 -11.63500 1.000 44.41059  ? 260 HIS A CB  1 
ATOM   2109 C CG  . HIS A 1 260 ? 2.92700   -40.33300 -10.66500 1.000 45.31070  ? 260 HIS A CG  1 
ATOM   2110 N ND1 . HIS A 1 260 ? 2.80800   -41.65900 -11.02400 1.000 46.12658  ? 260 HIS A ND1 1 
ATOM   2111 C CD2 . HIS A 1 260 ? 2.68600   -40.27800 -9.33400  1.000 46.20554  ? 260 HIS A CD2 1 
ATOM   2112 C CE1 . HIS A 1 260 ? 2.46400   -42.37200 -9.96300  1.000 46.80298  ? 260 HIS A CE1 1 
ATOM   2113 N NE2 . HIS A 1 260 ? 2.40900   -41.55800 -8.92000  1.000 47.08459  ? 260 HIS A NE2 1 
ATOM   2114 N N   . VAL A 1 261 ? 5.87700   -38.10100 -13.46000 1.000 42.00767  ? 261 VAL A N   1 
ATOM   2115 C CA  . VAL A 1 261 ? 6.40900   -37.18700 -14.46600 1.000 40.89174  ? 261 VAL A CA  1 
ATOM   2116 C C   . VAL A 1 261 ? 6.03900   -37.71200 -15.84700 1.000 40.79436  ? 261 VAL A C   1 
ATOM   2117 O O   . VAL A 1 261 ? 6.32700   -38.87100 -16.18100 1.000 40.54697  ? 261 VAL A O   1 
ATOM   2118 C CB  . VAL A 1 261 ? 7.93300   -37.02900 -14.34000 1.000 39.19944  ? 261 VAL A CB  1 
ATOM   2119 C CG1 . VAL A 1 261 ? 8.43400   -35.94600 -15.30300 1.000 37.57293  ? 261 VAL A CG1 1 
ATOM   2120 C CG2 . VAL A 1 261 ? 8.33500   -36.72300 -12.87700 1.000 38.60200  ? 261 VAL A CG2 1 
ATOM   2121 N N   . GLN A 1 262 ? 5.39100   -36.86700 -16.64200 1.000 42.86830  ? 262 GLN A N   1 
ATOM   2122 C CA  . GLN A 1 262 ? 5.08300   -37.18400 -18.02900 1.000 43.22097  ? 262 GLN A CA  1 
ATOM   2123 C C   . GLN A 1 262 ? 5.73800   -36.14900 -18.92000 1.000 41.77080  ? 262 GLN A C   1 
ATOM   2124 O O   . GLN A 1 262 ? 5.61700   -34.94600 -18.66700 1.000 41.21284  ? 262 GLN A O   1 
ATOM   2125 C CB  . GLN A 1 262 ? 3.58800   -37.21200 -18.28200 1.000 43.45258  ? 262 GLN A CB  1 
ATOM   2126 C CG  . GLN A 1 262 ? 2.89800   -38.33900 -17.53600 1.000 44.87643  ? 262 GLN A CG  1 
ATOM   2127 C CD  . GLN A 1 262 ? 1.42300   -38.08900 -17.40800 1.000 46.52663  ? 262 GLN A CD  1 
ATOM   2128 O OE1 . GLN A 1 262 ? 0.64000   -38.50700 -18.25500 1.000 47.32146  ? 262 GLN A OE1 1 
ATOM   2129 N NE2 . GLN A 1 262 ? 1.03300   -37.37800 -16.35400 1.000 47.00827  ? 262 GLN A NE2 1 
ATOM   2130 N N   . HIS A 1 263 ? 6.42900   -36.62400 -19.95300 1.000 38.68622  ? 263 HIS A N   1 
ATOM   2131 C CA  . HIS A 1 263 ? 7.11000   -35.72600 -20.86600 1.000 37.97034  ? 263 HIS A CA  1 
ATOM   2132 C C   . HIS A 1 263 ? 7.36600   -36.46000 -22.16200 1.000 38.22564  ? 263 HIS A C   1 
ATOM   2133 O O   . HIS A 1 263 ? 7.64800   -37.66100 -22.16900 1.000 38.89677  ? 263 HIS A O   1 
ATOM   2134 C CB  . HIS A 1 263 ? 8.43300   -35.18700 -20.30500 1.000 36.62808  ? 263 HIS A CB  1 
ATOM   2135 C CG  . HIS A 1 263 ? 9.03800   -34.11000 -21.15400 1.000 35.38845  ? 263 HIS A CG  1 
ATOM   2136 N ND1 . HIS A 1 263 ? 9.87900   -34.37900 -22.21500 1.000 35.85956  ? 263 HIS A ND1 1 
ATOM   2137 C CD2 . HIS A 1 263 ? 8.88600   -32.76400 -21.12900 1.000 34.01724  ? 263 HIS A CD2 1 
ATOM   2138 C CE1 . HIS A 1 263 ? 10.24300  -33.24400 -22.78600 1.000 34.60415  ? 263 HIS A CE1 1 
ATOM   2139 N NE2 . HIS A 1 263 ? 9.64700   -32.24900 -22.15200 1.000 33.21977  ? 263 HIS A NE2 1 
ATOM   2140 N N   . GLU A 1 264 ? 7.29100   -35.70200 -23.25600 1.000 48.39001  ? 264 GLU A N   1 
ATOM   2141 C CA  . GLU A 1 264 ? 7.45500   -36.27100 -24.58500 1.000 48.92692  ? 264 GLU A CA  1 
ATOM   2142 C C   . GLU A 1 264 ? 8.75700   -37.04700 -24.72100 1.000 49.49278  ? 264 GLU A C   1 
ATOM   2143 O O   . GLU A 1 264 ? 8.80300   -38.04800 -25.43800 1.000 50.43236  ? 264 GLU A O   1 
ATOM   2144 C CB  . GLU A 1 264 ? 7.38600   -35.14800 -25.61500 1.000 48.69531  ? 264 GLU A CB  1 
ATOM   2145 C CG  . GLU A 1 264 ? 7.09000   -35.61700 -27.00100 1.000 50.42973  ? 264 GLU A CG  1 
ATOM   2146 C CD  . GLU A 1 264 ? 7.04200   -34.46600 -27.98400 1.000 50.21918  ? 264 GLU A CD  1 
ATOM   2147 O OE1 . GLU A 1 264 ? 6.86300   -33.31400 -27.53500 1.000 48.35053  ? 264 GLU A OE1 1 
ATOM   2148 O OE2 . GLU A 1 264 ? 7.17400   -34.72800 -29.20300 1.000 51.22719  ? 264 GLU A OE2 1 
ATOM   2149 N N   . GLY A 1 265 ? 9.81600   -36.61600 -24.03500 1.000 44.04212  ? 265 GLY A N   1 
ATOM   2150 C CA  . GLY A 1 265 ? 11.11400  -37.26200 -24.11900 1.000 44.50534  ? 265 GLY A CA  1 
ATOM   2151 C C   . GLY A 1 265 ? 11.25700  -38.52300 -23.30200 1.000 44.79748  ? 265 GLY A C   1 
ATOM   2152 O O   . GLY A 1 265 ? 12.27800  -39.20300 -23.40800 1.000 44.91065  ? 265 GLY A O   1 
ATOM   2153 N N   . LEU A 1 266 ? 10.26400  -38.84100 -22.47400 1.000 45.27385  ? 266 LEU A N   1 
ATOM   2154 C CA  . LEU A 1 266 ? 10.26100  -40.07800 -21.71800 1.000 45.50546  ? 266 LEU A CA  1 
ATOM   2155 C C   . LEU A 1 266 ? 9.47200   -41.11500 -22.49900 1.000 47.13460  ? 266 LEU A C   1 
ATOM   2156 O O   . LEU A 1 266 ? 8.31900   -40.84700 -22.87800 1.000 47.67677  ? 266 LEU A O   1 
ATOM   2157 C CB  . LEU A 1 266 ? 9.64700   -39.86400 -20.34200 1.000 45.17910  ? 266 LEU A CB  1 
ATOM   2158 C CG  . LEU A 1 266 ? 10.39600  -38.92100 -19.39900 1.000 44.14477  ? 266 LEU A CG  1 
ATOM   2159 C CD1 . LEU A 1 266 ? 9.51500   -38.48700 -18.24400 1.000 44.33689  ? 266 LEU A CD1 1 
ATOM   2160 C CD2 . LEU A 1 266 ? 11.65700  -39.56800 -18.87100 1.000 43.54469  ? 266 LEU A CD2 1 
ATOM   2161 N N   . PRO A 1 267 ? 10.04300  -42.28400 -22.79700 1.000 49.10589  ? 267 PRO A N   1 
ATOM   2162 C CA  . PRO A 1 267 ? 9.24700   -43.30300 -23.48800 1.000 50.66923  ? 267 PRO A CA  1 
ATOM   2163 C C   . PRO A 1 267 ? 8.13300   -43.84000 -22.60900 1.000 51.61935  ? 267 PRO A C   1 
ATOM   2164 O O   . PRO A 1 267 ? 7.08900   -44.24900 -23.12700 1.000 53.68275  ? 267 PRO A O   1 
ATOM   2165 C CB  . PRO A 1 267 ? 10.28200  -44.37700 -23.84300 1.000 52.65631  ? 267 PRO A CB  1 
ATOM   2166 C CG  . PRO A 1 267 ? 11.30600  -44.26300 -22.73300 1.000 51.72989  ? 267 PRO A CG  1 
ATOM   2167 C CD  . PRO A 1 267 ? 11.34000  -42.80700 -22.31900 1.000 48.56372  ? 267 PRO A CD  1 
ATOM   2168 N N   . LYS A 1 268 ? 8.31600   -43.83100 -21.29400 1.000 50.18760  ? 268 LYS A N   1 
ATOM   2169 C CA  . LYS A 1 268 ? 7.27600   -44.19500 -20.34100 1.000 50.77714  ? 268 LYS A CA  1 
ATOM   2170 C C   . LYS A 1 268 ? 7.24400   -43.14500 -19.24400 1.000 49.08483  ? 268 LYS A C   1 
ATOM   2171 O O   . LYS A 1 268 ? 8.27800   -42.53900 -18.93200 1.000 47.56623  ? 268 LYS A O   1 
ATOM   2172 C CB  . LYS A 1 268 ? 7.51400   -45.58100 -19.71900 1.000 53.04847  ? 268 LYS A CB  1 
ATOM   2173 C CG  . LYS A 1 268 ? 7.49100   -46.74200 -20.70600 1.000 57.46215  ? 268 LYS A CG  1 
ATOM   2174 C CD  . LYS A 1 268 ? 7.75000   -48.04900 -19.98900 1.000 61.38894  ? 268 LYS A CD  1 
ATOM   2175 C CE  . LYS A 1 268 ? 8.11800   -49.15100 -20.96500 1.000 65.80789  ? 268 LYS A CE  1 
ATOM   2176 N NZ  . LYS A 1 268 ? 8.44600   -50.39700 -20.23200 1.000 69.99787  ? 268 LYS A NZ  1 
ATOM   2177 N N   . PRO A 1 269 ? 6.08100   -42.90200 -18.63800 1.000 50.51922  ? 269 PRO A N   1 
ATOM   2178 C CA  . PRO A 1 269 ? 6.04300   -41.97300 -17.50300 1.000 49.90335  ? 269 PRO A CA  1 
ATOM   2179 C C   . PRO A 1 269 ? 6.88700   -42.50400 -16.35500 1.000 49.71386  ? 269 PRO A C   1 
ATOM   2180 O O   . PRO A 1 269 ? 7.01200   -43.71800 -16.15700 1.000 49.99547  ? 269 PRO A O   1 
ATOM   2181 C CB  . PRO A 1 269 ? 4.55800   -41.91500 -17.12400 1.000 50.96401  ? 269 PRO A CB  1 
ATOM   2182 C CG  . PRO A 1 269 ? 3.82600   -42.59800 -18.19800 1.000 52.24047  ? 269 PRO A CG  1 
ATOM   2183 C CD  . PRO A 1 269 ? 4.78200   -43.57100 -18.84100 1.000 52.83791  ? 269 PRO A CD  1 
ATOM   2184 N N   . LEU A 1 270 ? 7.47700   -41.57400 -15.61500 1.000 56.79365  ? 270 LEU A N   1 
ATOM   2185 C CA  . LEU A 1 270 ? 8.34600   -41.85900 -14.48100 1.000 56.30675  ? 270 LEU A CA  1 
ATOM   2186 C C   . LEU A 1 270 ? 7.59300   -41.72800 -13.16500 1.000 57.19633  ? 270 LEU A C   1 
ATOM   2187 O O   . LEU A 1 270 ? 6.77500   -40.81900 -12.98900 1.000 58.00959  ? 270 LEU A O   1 
ATOM   2188 C CB  . LEU A 1 270 ? 9.53600   -40.89400 -14.43600 1.000 55.18293  ? 270 LEU A CB  1 
ATOM   2189 C CG  . LEU A 1 270 ? 10.62900  -41.02000 -15.49000 1.000 54.41442  ? 270 LEU A CG  1 
ATOM   2190 C CD1 . LEU A 1 270 ? 11.69700  -39.99700 -15.16400 1.000 53.04057  ? 270 LEU A CD1 1 
ATOM   2191 C CD2 . LEU A 1 270 ? 11.18800  -42.44000 -15.47800 1.000 54.81973  ? 270 LEU A CD2 1 
ATOM   2192 N N   . THR A 1 271 ? 7.91500   -42.60900 -12.22900 1.000 59.04919  ? 271 THR A N   1 
ATOM   2193 C CA  . THR A 1 271 ? 7.44800   -42.50500 -10.85600 1.000 59.97298  ? 271 THR A CA  1 
ATOM   2194 C C   . THR A 1 271 ? 8.65200   -42.34800 -9.93600  1.000 59.34922  ? 271 THR A C   1 
ATOM   2195 O O   . THR A 1 271 ? 9.62000   -43.11000 -10.03000 1.000 57.88852  ? 271 THR A O   1 
ATOM   2196 C CB  . THR A 1 271 ? 6.63100   -43.73100 -10.46800 1.000 61.92585  ? 271 THR A CB  1 
ATOM   2197 O OG1 . THR A 1 271 ? 5.51000   -43.86400 -11.36200 1.000 62.60487  ? 271 THR A OG1 1 
ATOM   2198 C CG2 . THR A 1 271 ? 6.14700   -43.61200 -9.02900  1.000 62.46538  ? 271 THR A CG2 1 
ATOM   2199 N N   . LEU A 1 272 ? 8.58900   -41.36300 -9.05300  1.000 56.45151  ? 272 LEU A N   1 
ATOM   2200 C CA  . LEU A 1 272 ? 9.69100   -41.05800 -8.16400  1.000 55.70405  ? 272 LEU A CA  1 
ATOM   2201 C C   . LEU A 1 272 ? 9.20500   -41.06400 -6.72900  1.000 55.94881  ? 272 LEU A C   1 
ATOM   2202 O O   . LEU A 1 272 ? 8.06800   -40.68500 -6.43900  1.000 57.67007  ? 272 LEU A O   1 
ATOM   2203 C CB  . LEU A 1 272 ? 10.30700  -39.68900 -8.45800  1.000 54.22229  ? 272 LEU A CB  1 
ATOM   2204 C CG  . LEU A 1 272 ? 10.94000  -39.43900 -9.81400  1.000 53.49589  ? 272 LEU A CG  1 
ATOM   2205 C CD1 . LEU A 1 272 ? 11.76800  -38.18600 -9.69800  1.000 52.30364  ? 272 LEU A CD1 1 
ATOM   2206 C CD2 . LEU A 1 272 ? 11.78600  -40.65000 -10.21500 1.000 53.74855  ? 272 LEU A CD2 1 
ATOM   2207 N N   . ARG A 1 273 ? 10.09300  -41.46800 -5.83300  1.000 70.12157  ? 273 ARG A N   1 
ATOM   2208 C CA  . ARG A 1 273 ? 9.86800   -41.31800 -4.40800  1.000 71.05326  ? 273 ARG A CA  1 
ATOM   2209 C C   . ARG A 1 273 ? 11.14600  -40.81700 -3.75700  1.000 69.48201  ? 273 ARG A C   1 
ATOM   2210 O O   . ARG A 1 273 ? 12.24700  -40.98900 -4.28300  1.000 68.50558  ? 273 ARG A O   1 
ATOM   2211 C CB  . ARG A 1 273 ? 9.41600   -42.62900 -3.76900  1.000 72.41921  ? 273 ARG A CB  1 
ATOM   2212 C CG  . ARG A 1 273 ? 10.11100  -43.84800 -4.32900  1.000 73.77727  ? 273 ARG A CG  1 
ATOM   2213 C CD  . ARG A 1 273 ? 9.87900   -45.03900 -3.43300  1.000 76.17755  ? 273 ARG A CD  1 
ATOM   2214 N NE  . ARG A 1 273 ? 8.47900   -45.15000 -3.03900  1.000 78.27254  ? 273 ARG A NE  1 
ATOM   2215 C CZ  . ARG A 1 273 ? 7.53900   -45.74900 -3.76100  1.000 79.72798  ? 273 ARG A CZ  1 
ATOM   2216 N NH1 . ARG A 1 273 ? 7.80300   -46.25100 -4.96000  1.000 79.84642  ? 273 ARG A NH1 1 
ATOM   2217 N NH2 . ARG A 1 273 ? 6.30700   -45.85400 -3.26400  1.000 80.68862  ? 273 ARG A NH2 1 
ATOM   2218 N N   . TRP A 1 274 ? 10.98500  -40.17900 -2.60900  1.000 54.17228  ? 274 TRP A N   1 
ATOM   2219 C CA  . TRP A 1 274 ? 12.11600  -39.69500 -1.84300  1.000 53.55379  ? 274 TRP A CA  1 
ATOM   2220 C C   . TRP A 1 274 ? 12.66000  -40.78000 -0.91700  1.000 53.90120  ? 274 TRP A C   1 
ATOM   2221 O O   . TRP A 1 274 ? 11.90000  -41.55900 -0.34000  1.000 55.16714  ? 274 TRP A O   1 
ATOM   2222 C CB  . TRP A 1 274 ? 11.70400  -38.47800 -1.03300  1.000 53.72486  ? 274 TRP A CB  1 
ATOM   2223 C CG  . TRP A 1 274 ? 12.78300  -37.99900 -0.17400  1.000 53.45904  ? 274 TRP A CG  1 
ATOM   2224 C CD1 . TRP A 1 274 ? 13.84500  -37.21000 -0.53600  1.000 52.99056  ? 274 TRP A CD1 1 
ATOM   2225 C CD2 . TRP A 1 274 ? 12.93300  -38.27100 1.20700   1.000 54.37757  ? 274 TRP A CD2 1 
ATOM   2226 N NE1 . TRP A 1 274 ? 14.65100  -36.98300 0.55400   1.000 53.18532  ? 274 TRP A NE1 1 
ATOM   2227 C CE2 . TRP A 1 274 ? 14.10800  -37.62200 1.63600   1.000 54.04069  ? 274 TRP A CE2 1 
ATOM   2228 C CE3 . TRP A 1 274 ? 12.18800  -39.00300 2.13100   1.000 55.13293  ? 274 TRP A CE3 1 
ATOM   2229 C CZ2 . TRP A 1 274 ? 14.54700  -37.68300 2.93700   1.000 54.20650  ? 274 TRP A CZ2 1 
ATOM   2230 C CZ3 . TRP A 1 274 ? 12.62700  -39.06000 3.41700   1.000 55.51718  ? 274 TRP A CZ3 1 
ATOM   2231 C CH2 . TRP A 1 274 ? 13.79600  -38.40400 3.81200   1.000 55.66720  ? 274 TRP A CH2 1 
ATOM   2232 N N   . GLU A 1 275 ? 13.98800  -40.80900 -0.77200  1.000 64.27613  ? 275 GLU A N   1 
ATOM   2233 C CA  . GLU A 1 275 ? 14.67100  -41.73100 0.11000   1.000 66.55535  ? 275 GLU A CA  1 
ATOM   2234 C C   . GLU A 1 275 ? 15.79600  -40.98000 0.81000   1.000 66.49745  ? 275 GLU A C   1 
ATOM   2235 O O   . GLU A 1 275 ? 16.57000  -40.27200 0.14400   1.000 65.44206  ? 275 GLU A O   1 
ATOM   2236 C CB  . GLU A 1 275 ? 15.24200  -42.93000 -0.64700  1.000 68.91616  ? 275 GLU A CB  1 
ATOM   2237 C CG  . GLU A 1 275 ? 14.20700  -43.79200 -1.34800  1.000 69.63466  ? 275 GLU A CG  1 
ATOM   2238 C CD  . GLU A 1 275 ? 14.84200  -44.80400 -2.27900  1.000 71.93231  ? 275 GLU A CD  1 
ATOM   2239 O OE1 . GLU A 1 275 ? 15.72300  -45.56700 -1.82500  1.000 75.15375  ? 275 GLU A OE1 1 
ATOM   2240 O OE2 . GLU A 1 275 ? 14.47000  -44.81800 -3.46900  1.000 70.61110  ? 275 GLU A OE2 1 
ATOM   2241 N N   . PRO A 1 276 ? 15.93200  -41.12700 2.13400   1.000 57.47268  ? 276 PRO A N   1 
ATOM   2242 C CA  . PRO A 1 276 ? 17.02600  -40.53800 2.91600   1.000 58.69651  ? 276 PRO A CA  1 
ATOM   2243 C C   . PRO A 1 276 ? 18.41400  -40.82100 2.33300   1.000 59.64136  ? 276 PRO A C   1 
ATOM   2244 O O   . PRO A 1 276 ? 19.05900  -39.84300 1.94700   1.000 58.69388  ? 276 PRO A O   1 
ATOM   2245 C CB  . PRO A 1 276 ? 16.87700  -41.21300 4.28700   1.000 61.34420  ? 276 PRO A CB  1 
ATOM   2246 C CG  . PRO A 1 276 ? 15.44100  -41.53800 4.38000   1.000 60.67833  ? 276 PRO A CG  1 
ATOM   2247 C CD  . PRO A 1 276 ? 14.99100  -41.87600 2.98200   1.000 58.77547  ? 276 PRO A CD  1 
ATOM   2248 N N   . MET B 2 1   ? -6.39600  1.00800   -16.68600 1.000 95.20878  ? 0   MET B N   1 
ATOM   2249 C CA  . MET B 2 1   ? -5.84300  -0.09600  -17.45800 1.000 93.46384  ? 0   MET B CA  1 
ATOM   2250 C C   . MET B 2 1   ? -5.69300  -1.35600  -16.62200 1.000 94.56134  ? 0   MET B C   1 
ATOM   2251 O O   . MET B 2 1   ? -5.60600  -1.29700  -15.39300 1.000 93.26381  ? 0   MET B O   1 
ATOM   2252 C CB  . MET B 2 1   ? -4.48700  0.28500   -18.04300 1.000 99.54351  ? 0   MET B CB  1 
ATOM   2253 C CG  . MET B 2 1   ? -4.56000  1.04700   -19.35000 1.000 100.41467 ? 0   MET B CG  1 
ATOM   2254 S SD  . MET B 2 1   ? -3.05000  1.97500   -19.67000 1.000 96.97742  ? 0   MET B SD  1 
ATOM   2255 C CE  . MET B 2 1   ? -1.84600  0.99000   -18.78300 1.000 91.85312  ? 0   MET B CE  1 
ATOM   2256 N N   . ILE B 2 2   ? -5.65500  -2.49900  -17.30400 1.000 99.78565  ? 1   ILE B N   1 
ATOM   2257 C CA  . ILE B 2 2   ? -5.36800  -3.76800  -16.64500 1.000 98.78816  ? 1   ILE B CA  1 
ATOM   2258 C C   . ILE B 2 2   ? -3.88300  -3.78100  -16.29800 1.000 94.84821  ? 1   ILE B C   1 
ATOM   2259 O O   . ILE B 2 2   ? -3.02700  -3.78900  -17.18700 1.000 92.31896  ? 1   ILE B O   1 
ATOM   2260 C CB  . ILE B 2 2   ? -5.74600  -4.96000  -17.52900 1.000 99.73827  ? 1   ILE B CB  1 
ATOM   2261 N N   . GLN B 2 3   ? -3.57000  -3.76300  -15.00700 1.000 73.58777  ? 2   GLN B N   1 
ATOM   2262 C CA  . GLN B 2 3   ? -2.19300  -3.79400  -14.54000 1.000 66.37638  ? 2   GLN B CA  1 
ATOM   2263 C C   . GLN B 2 3   ? -1.98000  -5.06800  -13.73700 1.000 60.78624  ? 2   GLN B C   1 
ATOM   2264 O O   . GLN B 2 3   ? -2.79400  -5.40500  -12.87300 1.000 61.20734  ? 2   GLN B O   1 
ATOM   2265 C CB  . GLN B 2 3   ? -1.86200  -2.55600  -13.70200 1.000 64.81567  ? 2   GLN B CB  1 
ATOM   2266 C CG  . GLN B 2 3   ? -2.15200  -1.25000  -14.42700 1.000 68.96353  ? 2   GLN B CG  1 
ATOM   2267 C CD  . GLN B 2 3   ? -1.21300  -0.12600  -14.02900 1.000 65.79210  ? 2   GLN B CD  1 
ATOM   2268 O OE1 . GLN B 2 3   ? -0.83300  0.00100   -12.86600 1.000 63.04440  ? 2   GLN B OE1 1 
ATOM   2269 N NE2 . GLN B 2 3   ? -0.83100  0.70100   -15.00700 1.000 65.49733  ? 2   GLN B NE2 1 
ATOM   2270 N N   . ARG B 2 4   ? -0.88600  -5.77000  -14.02800 1.000 61.58896  ? 3   ARG B N   1 
ATOM   2271 C CA  . ARG B 2 4   ? -0.58800  -7.06200  -13.42100 1.000 55.04871  ? 3   ARG B CA  1 
ATOM   2272 C C   . ARG B 2 4   ? 0.82600   -7.04500  -12.85600 1.000 47.19250  ? 3   ARG B C   1 
ATOM   2273 O O   . ARG B 2 4   ? 1.76700   -6.64000  -13.54200 1.000 43.74735  ? 3   ARG B O   1 
ATOM   2274 C CB  . ARG B 2 4   ? -0.75200  -8.18900  -14.44000 1.000 54.58549  ? 3   ARG B CB  1 
ATOM   2275 C CG  . ARG B 2 4   ? -2.19800  -8.59200  -14.66400 1.000 61.78899  ? 3   ARG B CG  1 
ATOM   2276 C CD  . ARG B 2 4   ? -2.35400  -9.46900  -15.88800 1.000 62.97860  ? 3   ARG B CD  1 
ATOM   2277 N NE  . ARG B 2 4   ? -2.56200  -8.66100  -17.08400 1.000 69.41095  ? 3   ARG B NE  1 
ATOM   2278 C CZ  . ARG B 2 4   ? -2.84600  -9.14900  -18.28500 1.000 69.51360  ? 3   ARG B CZ  1 
ATOM   2279 N NH1 . ARG B 2 4   ? -2.95600  -10.45000 -18.49400 1.000 65.09201  ? 3   ARG B NH1 1 
ATOM   2280 N NH2 . ARG B 2 4   ? -3.02500  -8.30800  -19.30100 1.000 70.79796  ? 3   ARG B NH2 1 
ATOM   2281 N N   . THR B 2 5   ? 0.97200   -7.48600  -11.61900 1.000 52.83791  ? 4   THR B N   1 
ATOM   2282 C CA  . THR B 2 5   ? 2.25600   -7.40700  -10.94600 1.000 47.00300  ? 4   THR B CA  1 
ATOM   2283 C C   . THR B 2 5   ? 3.10500   -8.62300  -11.32700 1.000 42.51299  ? 4   THR B C   1 
ATOM   2284 O O   . THR B 2 5   ? 2.56600   -9.66700  -11.69500 1.000 43.03411  ? 4   THR B O   1 
ATOM   2285 C CB  . THR B 2 5   ? 2.03700   -7.30900  -9.42700  1.000 48.70847  ? 4   THR B CB  1 
ATOM   2286 O OG1 . THR B 2 5   ? 3.21200   -6.80500  -8.77400  1.000 47.40305  ? 4   THR B OG1 1 
ATOM   2287 C CG2 . THR B 2 5   ? 1.65400   -8.65900  -8.81700  1.000 47.76889  ? 4   THR B CG2 1 
ATOM   2288 N N   . PRO B 2 6   ? 4.43500   -8.49700  -11.34900 1.000 42.93673  ? 5   PRO B N   1 
ATOM   2289 C CA  . PRO B 2 6   ? 5.25400   -9.60300  -11.86500 1.000 40.41537  ? 5   PRO B CA  1 
ATOM   2290 C C   . PRO B 2 6   ? 5.39500   -10.73900 -10.87200 1.000 40.34431  ? 5   PRO B C   1 
ATOM   2291 O O   . PRO B 2 6   ? 5.46700   -10.52400 -9.66000  1.000 41.04439  ? 5   PRO B O   1 
ATOM   2292 C CB  . PRO B 2 6   ? 6.61500   -8.95300  -12.12600 1.000 38.62832  ? 5   PRO B CB  1 
ATOM   2293 C CG  . PRO B 2 6   ? 6.65400   -7.76900  -11.21300 1.000 41.41549  ? 5   PRO B CG  1 
ATOM   2294 C CD  . PRO B 2 6   ? 5.23400   -7.27800  -11.13000 1.000 42.81040  ? 5   PRO B CD  1 
ATOM   2295 N N   . LYS B 2 7   ? 5.42200   -11.96000 -11.39800 1.000 45.37123  ? 6   LYS B N   1 
ATOM   2296 C CA  . LYS B 2 7   ? 5.91700   -13.10300 -10.64700 1.000 44.72378  ? 6   LYS B CA  1 
ATOM   2297 C C   . LYS B 2 7   ? 7.42000   -13.19100 -10.85800 1.000 41.91029  ? 6   LYS B C   1 
ATOM   2298 O O   . LYS B 2 7   ? 7.92900   -12.81600 -11.91500 1.000 41.29442  ? 6   LYS B O   1 
ATOM   2299 C CB  . LYS B 2 7   ? 5.24800   -14.40300 -11.10100 1.000 47.03459  ? 6   LYS B CB  1 
ATOM   2300 C CG  . LYS B 2 7   ? 3.73400   -14.42400 -10.91400 1.000 51.84043  ? 6   LYS B CG  1 
ATOM   2301 C CD  . LYS B 2 7   ? 3.13200   -15.76600 -11.33400 1.000 56.83050  ? 6   LYS B CD  1 
ATOM   2302 C CE  . LYS B 2 7   ? 2.92900   -15.86200 -12.85000 1.000 57.15685  ? 6   LYS B CE  1 
ATOM   2303 N NZ  . LYS B 2 7   ? 1.62500   -15.25300 -13.25000 1.000 59.63610  ? 6   LYS B NZ  1 
ATOM   2304 N N   . ILE B 2 8   ? 8.12800   -13.70300 -9.85400  1.000 35.63322  ? 7   ILE B N   1 
ATOM   2305 C CA  . ILE B 2 8   ? 9.58800   -13.68900 -9.84900  1.000 34.99630  ? 7   ILE B CA  1 
ATOM   2306 C C   . ILE B 2 8   ? 10.10200  -15.05100 -9.41500  1.000 35.12263  ? 7   ILE B C   1 
ATOM   2307 O O   . ILE B 2 8   ? 9.71100   -15.54700 -8.35700  1.000 35.22528  ? 7   ILE B O   1 
ATOM   2308 C CB  . ILE B 2 8   ? 10.15000  -12.62000 -8.88700  1.000 36.70966  ? 7   ILE B CB  1 
ATOM   2309 C CG1 . ILE B 2 8   ? 9.55900   -11.24100 -9.17900  1.000 37.52292  ? 7   ILE B CG1 1 
ATOM   2310 C CG2 . ILE B 2 8   ? 11.66500  -12.56400 -9.00100  1.000 37.83875  ? 7   ILE B CG2 1 
ATOM   2311 C CD1 . ILE B 2 8   ? 9.78000   -10.22900 -8.05100  1.000 39.10995  ? 7   ILE B CD1 1 
ATOM   2312 N N   . GLN B 2 9   ? 11.02100  -15.62600 -10.19100 1.000 30.35364  ? 8   GLN B N   1 
ATOM   2313 C CA  . GLN B 2 9   ? 11.74600  -16.83600 -9.79600  1.000 30.53261  ? 8   GLN B CA  1 
ATOM   2314 C C   . GLN B 2 9   ? 13.24100  -16.59000 -9.95400  1.000 32.38809  ? 8   GLN B C   1 
ATOM   2315 O O   . GLN B 2 9   ? 13.67500  -16.05300 -10.98000 1.000 32.96711  ? 8   GLN B O   1 
ATOM   2316 C CB  . GLN B 2 9   ? 11.33100  -18.04400 -10.64900 1.000 29.68514  ? 8   GLN B CB  1 
ATOM   2317 C CG  . GLN B 2 9   ? 9.92900   -18.56200 -10.34100 1.000 30.74842  ? 8   GLN B CG  1 
ATOM   2318 C CD  . GLN B 2 9   ? 9.70500   -19.99800 -10.80600 1.000 31.88540  ? 8   GLN B CD  1 
ATOM   2319 O OE1 . GLN B 2 9   ? 10.27200  -20.94800 -10.24700 1.000 31.98015  ? 8   GLN B OE1 1 
ATOM   2320 N NE2 . GLN B 2 9   ? 8.87700   -20.16100 -11.82200 1.000 33.39874  ? 8   GLN B NE2 1 
ATOM   2321 N N   . VAL B 2 10  ? 14.02400  -16.96100 -8.94300  1.000 33.21188  ? 9   VAL B N   1 
ATOM   2322 C CA  A VAL B 2 10  ? 15.47900  -16.84900 -8.97900  0.740 36.38857  ? 9   VAL B CA  1 
ATOM   2323 C CA  B VAL B 2 10  ? 15.47600  -16.85200 -8.98500  0.260 36.35962  ? 9   VAL B CA  1 
ATOM   2324 C C   . VAL B 2 10  ? 16.06500  -18.24100 -8.80400  1.000 36.84126  ? 9   VAL B C   1 
ATOM   2325 O O   . VAL B 2 10  ? 15.69200  -18.96400 -7.87100  1.000 36.36225  ? 9   VAL B O   1 
ATOM   2326 C CB  A VAL B 2 10  ? 16.01300  -15.89900 -7.89000  0.740 39.10995  ? 9   VAL B CB  1 
ATOM   2327 C CB  B VAL B 2 10  ? 15.99500  -15.87500 -7.91700  0.260 38.99941  ? 9   VAL B CB  1 
ATOM   2328 C CG1 A VAL B 2 10  ? 17.47700  -15.53400 -8.16000  0.740 42.48141  ? 9   VAL B CG1 1 
ATOM   2329 C CG1 B VAL B 2 10  ? 15.40000  -14.54300 -8.17200  0.260 39.00731  ? 9   VAL B CG1 1 
ATOM   2330 C CG2 A VAL B 2 10  ? 15.14100  -14.65900 -7.78700  0.740 38.64937  ? 9   VAL B CG2 1 
ATOM   2331 C CG2 B VAL B 2 10  ? 15.60200  -16.32000 -6.52400  0.260 38.92572  ? 9   VAL B CG2 1 
ATOM   2332 N N   . TYR B 2 11  ? 16.99100  -18.60900 -9.68200  1.000 36.42542  ? 10  TYR B N   1 
ATOM   2333 C CA  . TYR B 2 11  ? 17.47700  -19.98200 -9.71800  1.000 36.87284  ? 10  TYR B CA  1 
ATOM   2334 C C   . TYR B 2 11  ? 18.69600  -20.05600 -10.62300 1.000 39.71792  ? 10  TYR B C   1 
ATOM   2335 O O   . TYR B 2 11  ? 19.01300  -19.11300 -11.35200 1.000 40.66803  ? 10  TYR B O   1 
ATOM   2336 C CB  . TYR B 2 11  ? 16.38100  -20.92500 -10.21700 1.000 33.90407  ? 10  TYR B CB  1 
ATOM   2337 C CG  . TYR B 2 11  ? 15.81500  -20.50100 -11.56400 1.000 31.74854  ? 10  TYR B CG  1 
ATOM   2338 C CD1 . TYR B 2 11  ? 14.84000  -19.52300 -11.65500 1.000 30.00360  ? 10  TYR B CD1 1 
ATOM   2339 C CD2 . TYR B 2 11  ? 16.24200  -21.10500 -12.72900 1.000 32.03279  ? 10  TYR B CD2 1 
ATOM   2340 C CE1 . TYR B 2 11  ? 14.32900  -19.11800 -12.88600 1.000 28.59553  ? 10  TYR B CE1 1 
ATOM   2341 C CE2 . TYR B 2 11  ? 15.73500  -20.72600 -13.96000 1.000 30.54314  ? 10  TYR B CE2 1 
ATOM   2342 C CZ  . TYR B 2 11  ? 14.77500  -19.74100 -14.02900 1.000 28.74292  ? 10  TYR B CZ  1 
ATOM   2343 O OH  . TYR B 2 11  ? 14.29600  -19.37200 -15.24900 1.000 27.50593  ? 10  TYR B OH  1 
ATOM   2344 N N   . SER B 2 12  ? 19.37200  -21.19700 -10.58100 1.000 40.29957  ? 11  SER B N   1 
ATOM   2345 C CA  . SER B 2 12  ? 20.54200  -21.39400 -11.41800 1.000 42.81566  ? 11  SER B CA  1 
ATOM   2346 C C   . SER B 2 12  ? 20.18000  -22.23700 -12.63500 1.000 41.97345  ? 11  SER B C   1 
ATOM   2347 O O   . SER B 2 12  ? 19.21100  -23.00400 -12.62200 1.000 38.98362  ? 11  SER B O   1 
ATOM   2348 C CB  . SER B 2 12  ? 21.69100  -22.03900 -10.63600 1.000 45.39755  ? 11  SER B CB  1 
ATOM   2349 O OG  . SER B 2 12  ? 21.27500  -23.20500 -9.94900  1.000 44.71589  ? 11  SER B OG  1 
ATOM   2350 N N   . ARG B 2 13  ? 20.95500  -22.06200 -13.71000 1.000 43.54733  ? 12  ARG B N   1 
ATOM   2351 C CA  . ARG B 2 13  ? 20.74200  -22.88000 -14.89800 1.000 46.08447  ? 12  ARG B CA  1 
ATOM   2352 C C   . ARG B 2 13  ? 20.97500  -24.35000 -14.59300 1.000 48.28210  ? 12  ARG B C   1 
ATOM   2353 O O   . ARG B 2 13  ? 20.20700  -25.21300 -15.02900 1.000 47.52412  ? 12  ARG B O   1 
ATOM   2354 C CB  . ARG B 2 13  ? 21.65700  -22.43500 -16.03700 1.000 47.72151  ? 12  ARG B CB  1 
ATOM   2355 C CG  . ARG B 2 13  ? 21.53300  -23.34400 -17.27100 1.000 51.57724  ? 12  ARG B CG  1 
ATOM   2356 C CD  . ARG B 2 13  ? 22.47700  -22.94100 -18.38500 1.000 54.48811  ? 12  ARG B CD  1 
ATOM   2357 N NE  . ARG B 2 13  ? 22.20400  -21.58900 -18.85200 1.000 49.90862  ? 12  ARG B NE  1 
ATOM   2358 C CZ  . ARG B 2 13  ? 22.98400  -20.91300 -19.68500 1.000 50.51922  ? 12  ARG B CZ  1 
ATOM   2359 N NH1 . ARG B 2 13  ? 24.07800  -21.45100 -20.19800 1.000 54.62234  ? 12  ARG B NH1 1 
ATOM   2360 N NH2 . ARG B 2 13  ? 22.66300  -19.66000 -20.00200 1.000 46.83719  ? 12  ARG B NH2 1 
ATOM   2361 N N   . HIS B 2 14  ? 22.03000  -24.65300 -13.85300 1.000 48.95061  ? 13  HIS B N   1 
ATOM   2362 C CA  . HIS B 2 14  ? 22.39100  -26.00900 -13.47300 1.000 50.60870  ? 13  HIS B CA  1 
ATOM   2363 C C   . HIS B 2 14  ? 22.36600  -26.13300 -11.95400 1.000 48.86902  ? 13  HIS B C   1 
ATOM   2364 O O   . HIS B 2 14  ? 22.39400  -25.11900 -11.24500 1.000 47.78731  ? 13  HIS B O   1 
ATOM   2365 C CB  . HIS B 2 14  ? 23.78600  -26.37400 -14.00900 1.000 54.57760  ? 13  HIS B CB  1 
ATOM   2366 C CG  . HIS B 2 14  ? 23.90100  -26.30700 -15.50300 1.000 56.79628  ? 13  HIS B CG  1 
ATOM   2367 N ND1 . HIS B 2 14  ? 24.82400  -25.50800 -16.14300 1.000 60.20459  ? 13  HIS B ND1 1 
ATOM   2368 C CD2 . HIS B 2 14  ? 23.22100  -26.95100 -16.48100 1.000 57.48321  ? 13  HIS B CD2 1 
ATOM   2369 C CE1 . HIS B 2 14  ? 24.70000  -25.65400 -17.45100 1.000 62.02059  ? 13  HIS B CE1 1 
ATOM   2370 N NE2 . HIS B 2 14  ? 23.73400  -26.52300 -17.68200 1.000 60.92046  ? 13  HIS B NE2 1 
ATOM   2371 N N   . PRO B 2 15  ? 22.28600  -27.35700 -11.42100 1.000 52.22995  ? 14  PRO B N   1 
ATOM   2372 C CA  . PRO B 2 15  ? 22.46700  -27.55200 -9.97400  1.000 51.97992  ? 14  PRO B CA  1 
ATOM   2373 C C   . PRO B 2 15  ? 23.75400  -26.90600 -9.48300  1.000 54.52233  ? 14  PRO B C   1 
ATOM   2374 O O   . PRO B 2 15  ? 24.84200  -27.16200 -10.00600 1.000 56.97788  ? 14  PRO B O   1 
ATOM   2375 C CB  . PRO B 2 15  ? 22.51300  -29.07700 -9.82700  1.000 52.60631  ? 14  PRO B CB  1 
ATOM   2376 C CG  . PRO B 2 15  ? 21.71900  -29.58100 -10.96000 1.000 51.67988  ? 14  PRO B CG  1 
ATOM   2377 C CD  . PRO B 2 15  ? 21.92000  -28.61400 -12.10100 1.000 51.76147  ? 14  PRO B CD  1 
ATOM   2378 N N   . ALA B 2 16  ? 23.62000  -26.06800 -8.46200  1.000 61.85742  ? 15  ALA B N   1 
ATOM   2379 C CA  . ALA B 2 16  ? 24.73800  -25.26000 -8.00300  1.000 62.71278  ? 15  ALA B CA  1 
ATOM   2380 C C   . ALA B 2 16  ? 25.78200  -26.11200 -7.29700  1.000 64.96042  ? 15  ALA B C   1 
ATOM   2381 O O   . ALA B 2 16  ? 25.45900  -27.01800 -6.52400  1.000 65.06043  ? 15  ALA B O   1 
ATOM   2382 C CB  . ALA B 2 16  ? 24.23900  -24.16200 -7.06800  1.000 61.25208  ? 15  ALA B CB  1 
ATOM   2383 N N   . GLU B 2 17  ? 27.04800  -25.82300 -7.58000  1.000 69.51623  ? 16  GLU B N   1 
ATOM   2384 C CA  . GLU B 2 17  ? 28.17100  -26.46200 -6.90700  1.000 71.32171  ? 16  GLU B CA  1 
ATOM   2385 C C   . GLU B 2 17  ? 29.21400  -25.39200 -6.63300  1.000 70.68479  ? 16  GLU B C   1 
ATOM   2386 O O   . GLU B 2 17  ? 29.61600  -24.67400 -7.55500  1.000 70.61899  ? 16  GLU B O   1 
ATOM   2387 C CB  . GLU B 2 17  ? 28.76100  -27.59700 -7.75600  1.000 73.39038  ? 16  GLU B CB  1 
ATOM   2388 C CG  . GLU B 2 17  ? 29.99800  -28.25200 -7.15400  1.000 77.56719  ? 16  GLU B CG  1 
ATOM   2389 C CD  . GLU B 2 17  ? 30.35800  -29.58500 -7.81400  1.000 81.36239  ? 16  GLU B CD  1 
ATOM   2390 O OE1 . GLU B 2 17  ? 29.71400  -29.95600 -8.82400  1.000 80.40438  ? 16  GLU B OE1 1 
ATOM   2391 O OE2 . GLU B 2 17  ? 31.27900  -30.26300 -7.31300  1.000 84.07587  ? 16  GLU B OE2 1 
ATOM   2392 N N   . ASN B 2 18  ? 29.63100  -25.26900 -5.37100  1.000 71.39803  ? 17  ASN B N   1 
ATOM   2393 C CA  . ASN B 2 18  ? 30.58600  -24.23000 -4.99900  1.000 71.29802  ? 17  ASN B CA  1 
ATOM   2394 C C   . ASN B 2 18  ? 31.88400  -24.39300 -5.78000  1.000 73.67989  ? 17  ASN B C   1 
ATOM   2395 O O   . ASN B 2 18  ? 32.49400  -25.46500 -5.77200  1.000 76.22493  ? 17  ASN B O   1 
ATOM   2396 C CB  . ASN B 2 18  ? 30.85600  -24.26400 -3.49400  1.000 71.60069  ? 17  ASN B CB  1 
ATOM   2397 C CG  . ASN B 2 18  ? 29.74700  -23.61000 -2.69200  1.000 68.93721  ? 17  ASN B CG  1 
ATOM   2398 O OD1 . ASN B 2 18  ? 29.00300  -22.78300 -3.20900  1.000 67.14752  ? 17  ASN B OD1 1 
ATOM   2399 N ND2 . ASN B 2 18  ? 29.63500  -23.97400 -1.42600  1.000 70.21895  ? 17  ASN B ND2 1 
ATOM   2400 N N   . GLY B 2 19  ? 32.28600  -23.33300 -6.48200  1.000 73.90886  ? 18  GLY B N   1 
ATOM   2401 C CA  . GLY B 2 19  ? 33.49800  -23.34700 -7.27200  1.000 76.86448  ? 18  GLY B CA  1 
ATOM   2402 C C   . GLY B 2 19  ? 33.32000  -23.67800 -8.73900  1.000 77.88039  ? 18  GLY B C   1 
ATOM   2403 O O   . GLY B 2 19  ? 34.30000  -23.60700 -9.49200  1.000 80.58071  ? 18  GLY B O   1 
ATOM   2404 N N   . LYS B 2 20  ? 32.11300  -24.03000 -9.17300  1.000 73.39301  ? 19  LYS B N   1 
ATOM   2405 C CA  . LYS B 2 20  ? 31.84900  -24.39700 -10.55700 1.000 74.66422  ? 19  LYS B CA  1 
ATOM   2406 C C   . LYS B 2 20  ? 31.07300  -23.27700 -11.22900 1.000 72.42710  ? 19  LYS B C   1 
ATOM   2407 O O   . LYS B 2 20  ? 30.08400  -22.78600 -10.67500 1.000 69.78995  ? 19  LYS B O   1 
ATOM   2408 C CB  . LYS B 2 20  ? 31.06400  -25.70800 -10.64900 1.000 76.25651  ? 19  LYS B CB  1 
ATOM   2409 C CG  . LYS B 2 20  ? 31.75300  -26.90500 -10.01200 1.000 78.21201  ? 19  LYS B CG  1 
ATOM   2410 C CD  . LYS B 2 20  ? 33.06900  -27.23900 -10.69900 1.000 82.25460  ? 19  LYS B CD  1 
ATOM   2411 C CE  . LYS B 2 20  ? 33.93600  -28.15600 -9.83200  1.000 85.57605  ? 19  LYS B CE  1 
ATOM   2412 N NZ  . LYS B 2 20  ? 33.26700  -29.45400 -9.51100  1.000 86.74987  ? 19  LYS B NZ  1 
ATOM   2413 N N   . SER B 2 21  ? 31.52200  -22.87800 -12.41600 1.000 56.61995  ? 20  SER B N   1 
ATOM   2414 C CA  . SER B 2 21  ? 30.84500  -21.81300 -13.14000 1.000 60.45725  ? 20  SER B CA  1 
ATOM   2415 C C   . SER B 2 21  ? 29.41700  -22.23300 -13.46600 1.000 62.00480  ? 20  SER B C   1 
ATOM   2416 O O   . SER B 2 21  ? 29.13900  -23.40500 -13.73000 1.000 53.53537  ? 20  SER B O   1 
ATOM   2417 C CB  . SER B 2 21  ? 31.61100  -21.46500 -14.42000 1.000 58.94391  ? 20  SER B CB  1 
ATOM   2418 O OG  . SER B 2 21  ? 31.14800  -20.24900 -14.98300 1.000 70.64268  ? 20  SER B OG  1 
ATOM   2419 N N   . ASN B 2 22  ? 28.51000  -21.26500 -13.43900 1.000 55.77511  ? 21  ASN B N   1 
ATOM   2420 C CA  . ASN B 2 22  ? 27.09100  -21.52700 -13.60100 1.000 49.91388  ? 21  ASN B CA  1 
ATOM   2421 C C   . ASN B 2 22  ? 26.45700  -20.27600 -14.19600 1.000 57.35161  ? 21  ASN B C   1 
ATOM   2422 O O   . ASN B 2 22  ? 27.15200  -19.35500 -14.63800 1.000 55.78300  ? 21  ASN B O   1 
ATOM   2423 C CB  . ASN B 2 22  ? 26.47400  -21.91900 -12.24900 1.000 46.54769  ? 21  ASN B CB  1 
ATOM   2424 C CG  . ASN B 2 22  ? 25.24700  -22.80400 -12.38700 1.000 56.15147  ? 21  ASN B CG  1 
ATOM   2425 O OD1 . ASN B 2 22  ? 24.48500  -22.69100 -13.34900 1.000 47.59518  ? 21  ASN B OD1 1 
ATOM   2426 N ND2 . ASN B 2 22  ? 25.04100  -23.68600 -11.40300 1.000 40.16534  ? 21  ASN B ND2 1 
ATOM   2427 N N   . PHE B 2 23  ? 25.13100  -20.23800 -14.19200 1.000 51.21404  ? 22  PHE B N   1 
ATOM   2428 C CA  . PHE B 2 23  ? 24.38600  -19.07000 -14.62200 1.000 40.40221  ? 22  PHE B CA  1 
ATOM   2429 C C   . PHE B 2 23  ? 23.30900  -18.77300 -13.59400 1.000 44.61851  ? 22  PHE B C   1 
ATOM   2430 O O   . PHE B 2 23  ? 22.57100  -19.67800 -13.19600 1.000 41.70500  ? 22  PHE B O   1 
ATOM   2431 C CB  . PHE B 2 23  ? 23.75500  -19.29600 -15.99500 1.000 41.46550  ? 22  PHE B CB  1 
ATOM   2432 C CG  . PHE B 2 23  ? 24.70100  -19.08900 -17.14700 1.000 44.86327  ? 22  PHE B CG  1 
ATOM   2433 C CD1 . PHE B 2 23  ? 25.51700  -20.12000 -17.59200 1.000 45.04487  ? 22  PHE B CD1 1 
ATOM   2434 C CD2 . PHE B 2 23  ? 24.75500  -17.86300 -17.79600 1.000 46.33977  ? 22  PHE B CD2 1 
ATOM   2435 C CE1 . PHE B 2 23  ? 26.37200  -19.92300 -18.66600 1.000 50.74556  ? 22  PHE B CE1 1 
ATOM   2436 C CE2 . PHE B 2 23  ? 25.60000  -17.66300 -18.87500 1.000 54.37757  ? 22  PHE B CE2 1 
ATOM   2437 C CZ  . PHE B 2 23  ? 26.40600  -18.69300 -19.31100 1.000 42.42351  ? 22  PHE B CZ  1 
ATOM   2438 N N   . LEU B 2 24  ? 23.20200  -17.51100 -13.19200 1.000 39.24155  ? 23  LEU B N   1 
ATOM   2439 C CA  . LEU B 2 24  ? 22.17000  -17.07000 -12.26300 1.000 42.29191  ? 23  LEU B CA  1 
ATOM   2440 C C   . LEU B 2 24  ? 21.03500  -16.42500 -13.04800 1.000 41.81028  ? 23  LEU B C   1 
ATOM   2441 O O   . LEU B 2 24  ? 21.26800  -15.51000 -13.85000 1.000 41.68921  ? 23  LEU B O   1 
ATOM   2442 C CB  . LEU B 2 24  ? 22.73700  -16.08800 -11.24000 1.000 39.42578  ? 23  LEU B CB  1 
ATOM   2443 C CG  . LEU B 2 24  ? 21.72900  -15.45000 -10.27600 1.000 43.65787  ? 23  LEU B CG  1 
ATOM   2444 C CD1 . LEU B 2 24  ? 21.11900  -16.51000 -9.34200  1.000 39.48631  ? 23  LEU B CD1 1 
ATOM   2445 C CD2 . LEU B 2 24  ? 22.37100  -14.31400 -9.48200  1.000 41.93661  ? 23  LEU B CD2 1 
ATOM   2446 N N   . ASN B 2 25  ? 19.81500  -16.90100 -12.81800 1.000 36.26224  ? 24  ASN B N   1 
ATOM   2447 C CA  . ASN B 2 25  ? 18.65200  -16.49600 -13.59200 1.000 31.63011  ? 24  ASN B CA  1 
ATOM   2448 C C   . ASN B 2 25  ? 17.64900  -15.79600 -12.69800 1.000 35.75955  ? 24  ASN B C   1 
ATOM   2449 O O   . ASN B 2 25  ? 17.43700  -16.19600 -11.55700 1.000 37.57556  ? 24  ASN B O   1 
ATOM   2450 C CB  . ASN B 2 25  ? 17.95500  -17.70600 -14.25200 1.000 34.37254  ? 24  ASN B CB  1 
ATOM   2451 C CG  . ASN B 2 25  ? 18.80100  -18.36100 -15.31000 1.000 43.11306  ? 24  ASN B CG  1 
ATOM   2452 O OD1 . ASN B 2 25  ? 19.59200  -17.70100 -15.98400 1.000 42.92883  ? 24  ASN B OD1 1 
ATOM   2453 N ND2 . ASN B 2 25  ? 18.64300  -19.67700 -15.46400 1.000 43.32362  ? 24  ASN B ND2 1 
ATOM   2454 N N   . CYS B 2 26  ? 17.00000  -14.77700 -13.22800 1.000 29.50880  ? 25  CYS B N   1 
ATOM   2455 C CA  . CYS B 2 26  ? 15.82900  -14.20700 -12.57600 1.000 35.31739  ? 25  CYS B CA  1 
ATOM   2456 C C   . CYS B 2 26  ? 14.74500  -14.14900 -13.63400 1.000 37.04392  ? 25  CYS B C   1 
ATOM   2457 O O   . CYS B 2 26  ? 14.84300  -13.38800 -14.60300 1.000 36.77283  ? 25  CYS B O   1 
ATOM   2458 C CB  . CYS B 2 26  ? 16.10700  -12.83100 -11.97000 1.000 36.28856  ? 25  CYS B CB  1 
ATOM   2459 S SG  . CYS B 2 26  ? 14.63300  -12.04000 -11.29300 1.000 43.82368  ? 25  CYS B SG  1 
ATOM   2460 N N   . TYR B 2 27  ? 13.73300  -14.98200 -13.47800 1.000 29.92727  ? 26  TYR B N   1 
ATOM   2461 C CA  . TYR B 2 27  ? 12.67500  -15.07000 -14.46700 1.000 25.68992  ? 26  TYR B CA  1 
ATOM   2462 C C   . TYR B 2 27  ? 11.51200  -14.23600 -13.95800 1.000 31.75907  ? 26  TYR B C   1 
ATOM   2463 O O   . TYR B 2 27  ? 11.04300  -14.44500 -12.83400 1.000 32.61180  ? 26  TYR B O   1 
ATOM   2464 C CB  . TYR B 2 27  ? 12.27800  -16.52600 -14.69800 1.000 28.87188  ? 26  TYR B CB  1 
ATOM   2465 C CG  . TYR B 2 27  ? 11.18900  -16.71900 -15.72100 1.000 31.53010  ? 26  TYR B CG  1 
ATOM   2466 C CD1 . TYR B 2 27  ? 11.31100  -16.18700 -17.01800 1.000 27.11378  ? 26  TYR B CD1 1 
ATOM   2467 C CD2 . TYR B 2 27  ? 10.04400  -17.44400 -15.40600 1.000 33.67246  ? 26  TYR B CD2 1 
ATOM   2468 C CE1 . TYR B 2 27  ? 10.29700  -16.39200 -17.97000 1.000 29.82726  ? 26  TYR B CE1 1 
ATOM   2469 C CE2 . TYR B 2 27  ? 9.04200   -17.66500 -16.34800 1.000 33.39874  ? 26  TYR B CE2 1 
ATOM   2470 C CZ  . TYR B 2 27  ? 9.17300   -17.12200 -17.62700 1.000 32.89079  ? 26  TYR B CZ  1 
ATOM   2471 O OH  . TYR B 2 27  ? 8.17700   -17.33000 -18.54700 1.000 35.13316  ? 26  TYR B OH  1 
ATOM   2472 N N   . VAL B 2 28  ? 11.10400  -13.24300 -14.74400 1.000 29.74567  ? 27  VAL B N   1 
ATOM   2473 C CA  . VAL B 2 28  ? 9.97100   -12.38200 -14.41700 1.000 32.91974  ? 27  VAL B CA  1 
ATOM   2474 C C   . VAL B 2 28  ? 8.88200   -12.61400 -15.45100 1.000 33.03554  ? 27  VAL B C   1 
ATOM   2475 O O   . VAL B 2 28  ? 9.16300   -12.68200 -16.65500 1.000 34.78049  ? 27  VAL B O   1 
ATOM   2476 C CB  . VAL B 2 28  ? 10.36500  -10.88800 -14.36500 1.000 34.36201  ? 27  VAL B CB  1 
ATOM   2477 C CG1 . VAL B 2 28  ? 11.24400  -10.60700 -13.15100 1.000 35.69639  ? 27  VAL B CG1 1 
ATOM   2478 C CG2 . VAL B 2 28  ? 11.10000  -10.49600 -15.62000 1.000 39.37841  ? 27  VAL B CG2 1 
ATOM   2479 N N   . SER B 2 29  ? 7.63800   -12.73700 -14.98200 1.000 31.86961  ? 28  SER B N   1 
ATOM   2480 C CA  . SER B 2 29  ? 6.53900   -13.11600 -15.86200 1.000 30.69315  ? 28  SER B CA  1 
ATOM   2481 C C   . SER B 2 29  ? 5.22000   -12.62100 -15.29200 1.000 35.21212  ? 28  SER B C   1 
ATOM   2482 O O   . SER B 2 29  ? 5.13600   -12.18000 -14.14100 1.000 36.62018  ? 28  SER B O   1 
ATOM   2483 C CB  . SER B 2 29  ? 6.47600   -14.63500 -16.05100 1.000 35.95694  ? 28  SER B CB  1 
ATOM   2484 O OG  . SER B 2 29  ? 6.22200   -15.25400 -14.79500 1.000 35.96484  ? 28  SER B OG  1 
ATOM   2485 N N   . GLY B 2 30  ? 4.18000   -12.71500 -16.12200 1.000 31.13268  ? 29  GLY B N   1 
ATOM   2486 C CA  . GLY B 2 30  ? 2.83500   -12.35800 -15.72700 1.000 30.74579  ? 29  GLY B CA  1 
ATOM   2487 C C   . GLY B 2 30  ? 2.58100   -10.88400 -15.50000 1.000 36.75441  ? 29  GLY B C   1 
ATOM   2488 O O   . GLY B 2 30  ? 1.56000   -10.53400 -14.91300 1.000 35.77271  ? 29  GLY B O   1 
ATOM   2489 N N   . PHE B 2 31  ? 3.45300   -9.99600  -15.96700 1.000 33.26715  ? 30  PHE B N   1 
ATOM   2490 C CA  . PHE B 2 31  ? 3.28300   -8.58500  -15.65700 1.000 34.99104  ? 30  PHE B CA  1 
ATOM   2491 C C   . PHE B 2 31  ? 2.78500   -7.79300  -16.85900 1.000 35.03315  ? 30  PHE B C   1 
ATOM   2492 O O   . PHE B 2 31  ? 2.97600   -8.17800  -18.01500 1.000 31.00372  ? 30  PHE B O   1 
ATOM   2493 C CB  . PHE B 2 31  ? 4.57600   -7.97700  -15.11600 1.000 28.81661  ? 30  PHE B CB  1 
ATOM   2494 C CG  . PHE B 2 31  ? 5.76800   -8.13200  -16.02800 1.000 37.13866  ? 30  PHE B CG  1 
ATOM   2495 C CD1 . PHE B 2 31  ? 6.51600   -9.30400  -16.03100 1.000 34.36201  ? 30  PHE B CD1 1 
ATOM   2496 C CD2 . PHE B 2 31  ? 6.15500   -7.09600  -16.85700 1.000 33.11713  ? 30  PHE B CD2 1 
ATOM   2497 C CE1 . PHE B 2 31  ? 7.63100   -9.44800  -16.87000 1.000 30.17993  ? 30  PHE B CE1 1 
ATOM   2498 C CE2 . PHE B 2 31  ? 7.26300   -7.22500  -17.69000 1.000 33.53034  ? 30  PHE B CE2 1 
ATOM   2499 C CZ  . PHE B 2 31  ? 8.00200   -8.41200  -17.69100 1.000 35.24633  ? 30  PHE B CZ  1 
ATOM   2500 N N   . HIS B 2 32  ? 2.13200   -6.66700  -16.56000 1.000 34.35675  ? 31  HIS B N   1 
ATOM   2501 C CA  . HIS B 2 32  ? 1.64500   -5.73100  -17.56400 1.000 35.24896  ? 31  HIS B CA  1 
ATOM   2502 C C   . HIS B 2 32  ? 1.48100   -4.38200  -16.89000 1.000 36.57544  ? 31  HIS B C   1 
ATOM   2503 O O   . HIS B 2 32  ? 0.86300   -4.30700  -15.82200 1.000 37.19657  ? 31  HIS B O   1 
ATOM   2504 C CB  . HIS B 2 32  ? 0.31700   -6.20200  -18.15700 1.000 35.57005  ? 31  HIS B CB  1 
ATOM   2505 C CG  . HIS B 2 32  ? 0.15200   -5.85100  -19.59800 1.000 36.28067  ? 31  HIS B CG  1 
ATOM   2506 N ND1 . HIS B 2 32  ? -0.18600  -4.58300  -20.01800 1.000 36.61755  ? 31  HIS B ND1 1 
ATOM   2507 C CD2 . HIS B 2 32  ? 0.25700   -6.60700  -20.71400 1.000 36.02537  ? 31  HIS B CD2 1 
ATOM   2508 C CE1 . HIS B 2 32  ? -0.26000  -4.57000  -21.33700 1.000 36.90969  ? 31  HIS B CE1 1 
ATOM   2509 N NE2 . HIS B 2 32  ? 0.01000   -5.78300  -21.78400 1.000 36.62808  ? 31  HIS B NE2 1 
ATOM   2510 N N   . PRO B 2 33  ? 1.98100   -3.28100  -17.47000 1.000 37.83348  ? 32  PRO B N   1 
ATOM   2511 C CA  . PRO B 2 33  ? 2.63700   -3.12800  -18.76800 1.000 38.83097  ? 32  PRO B CA  1 
ATOM   2512 C C   . PRO B 2 33  ? 4.04800   -3.69500  -18.76700 1.000 39.84425  ? 32  PRO B C   1 
ATOM   2513 O O   . PRO B 2 33  ? 4.44300   -4.31400  -17.78200 1.000 38.53357  ? 32  PRO B O   1 
ATOM   2514 C CB  . PRO B 2 33  ? 2.64100   -1.60700  -18.98700 1.000 41.45497  ? 32  PRO B CB  1 
ATOM   2515 C CG  . PRO B 2 33  ? 2.57200   -1.02500  -17.64600 1.000 42.33666  ? 32  PRO B CG  1 
ATOM   2516 C CD  . PRO B 2 33  ? 1.75000   -1.97900  -16.81700 1.000 39.50210  ? 32  PRO B CD  1 
ATOM   2517 N N   . SER B 2 34  ? 4.79800   -3.47000  -19.84900 1.000 32.95658  ? 33  SER B N   1 
ATOM   2518 C CA  . SER B 2 34  ? 6.04700   -4.19300  -20.06400 1.000 33.81984  ? 33  SER B CA  1 
ATOM   2519 C C   . SER B 2 34  ? 7.26200   -3.52600  -19.43900 1.000 38.88098  ? 33  SER B C   1 
ATOM   2520 O O   . SER B 2 34  ? 8.26600   -4.21200  -19.21400 1.000 38.47830  ? 33  SER B O   1 
ATOM   2521 C CB  . SER B 2 34  ? 6.30300   -4.36800  -21.55700 1.000 34.41728  ? 33  SER B CB  1 
ATOM   2522 O OG  . SER B 2 34  ? 6.43200   -3.11300  -22.16200 1.000 40.34957  ? 33  SER B OG  1 
ATOM   2523 N N   . ASP B 2 35  ? 7.22300   -2.21500  -19.19400 1.000 47.02669  ? 34  ASP B N   1 
ATOM   2524 C CA  . ASP B 2 35  ? 8.33700   -1.57300  -18.51600 1.000 50.70082  ? 34  ASP B CA  1 
ATOM   2525 C C   . ASP B 2 35  ? 8.57800   -2.26300  -17.17800 1.000 47.75309  ? 34  ASP B C   1 
ATOM   2526 O O   . ASP B 2 35  ? 7.65900   -2.41500  -16.37000 1.000 43.78157  ? 34  ASP B O   1 
ATOM   2527 C CB  . ASP B 2 35  ? 8.06100   -0.08100  -18.30000 1.000 51.91149  ? 34  ASP B CB  1 
ATOM   2528 C CG  . ASP B 2 35  ? 8.17100   0.73200   -19.57500 1.000 54.78815  ? 34  ASP B CG  1 
ATOM   2529 O OD1 . ASP B 2 35  ? 8.40200   0.14500   -20.65800 1.000 54.40126  ? 34  ASP B OD1 1 
ATOM   2530 O OD2 . ASP B 2 35  ? 8.02700   1.96800   -19.50000 1.000 55.80143  ? 34  ASP B OD2 1 
ATOM   2531 N N   . ILE B 2 36  ? 9.81100   -2.70400  -16.95800 1.000 43.81052  ? 35  ILE B N   1 
ATOM   2532 C CA  . ILE B 2 36  ? 10.17800  -3.36200  -15.71500 1.000 41.61288  ? 35  ILE B CA  1 
ATOM   2533 C C   . ILE B 2 36  ? 11.67400  -3.18800  -15.53400 1.000 45.18436  ? 35  ILE B C   1 
ATOM   2534 O O   . ILE B 2 36  ? 12.43000  -3.09100  -16.50700 1.000 47.63992  ? 35  ILE B O   1 
ATOM   2535 C CB  . ILE B 2 36  ? 9.75900   -4.85200  -15.71800 1.000 36.79389  ? 35  ILE B CB  1 
ATOM   2536 C CG1 . ILE B 2 36  ? 9.92700   -5.48800  -14.33900 1.000 33.00659  ? 35  ILE B CG1 1 
ATOM   2537 C CG2 . ILE B 2 36  ? 10.51900  -5.64400  -16.76100 1.000 36.76493  ? 35  ILE B CG2 1 
ATOM   2538 C CD1 . ILE B 2 36  ? 9.11700   -6.79300  -14.26400 1.000 28.59553  ? 35  ILE B CD1 1 
ATOM   2539 N N   . GLU B 2 37  ? 12.09000  -3.09700  -14.27600 1.000 52.58788  ? 36  GLU B N   1 
ATOM   2540 C CA  . GLU B 2 37  ? 13.49000  -2.97000  -13.90900 1.000 54.83552  ? 36  GLU B CA  1 
ATOM   2541 C C   . GLU B 2 37  ? 13.87700  -4.21100  -13.12700 1.000 52.49840  ? 36  GLU B C   1 
ATOM   2542 O O   . GLU B 2 37  ? 13.22200  -4.55300  -12.13500 1.000 49.15589  ? 36  GLU B O   1 
ATOM   2543 C CB  . GLU B 2 37  ? 13.73000  -1.70800  -13.08500 1.000 55.35401  ? 36  GLU B CB  1 
ATOM   2544 C CG  . GLU B 2 37  ? 15.15500  -1.21500  -13.15500 1.000 59.93877  ? 36  GLU B CG  1 
ATOM   2545 C CD  . GLU B 2 37  ? 15.31800  0.13700   -12.50100 1.000 65.24993  ? 36  GLU B CD  1 
ATOM   2546 O OE1 . GLU B 2 37  ? 14.40100  0.98000   -12.65400 1.000 66.20267  ? 36  GLU B OE1 1 
ATOM   2547 O OE2 . GLU B 2 37  ? 16.35000  0.34900   -11.82100 1.000 68.57138  ? 36  GLU B OE2 1 
ATOM   2548 N N   . VAL B 2 38  ? 14.92300  -4.88700  -13.58100 1.000 47.83468  ? 37  VAL B N   1 
ATOM   2549 C CA  . VAL B 2 38  ? 15.38000  -6.12500  -12.97400 1.000 45.95814  ? 37  VAL B CA  1 
ATOM   2550 C C   . VAL B 2 38  ? 16.87700  -6.01800  -12.77200 1.000 49.11378  ? 37  VAL B C   1 
ATOM   2551 O O   . VAL B 2 38  ? 17.61900  -5.73400  -13.71900 1.000 50.70345  ? 37  VAL B O   1 
ATOM   2552 C CB  . VAL B 2 38  ? 15.04600  -7.35000  -13.83300 1.000 42.23664  ? 37  VAL B CB  1 
ATOM   2553 C CG1 . VAL B 2 38  ? 15.66100  -8.58200  -13.21800 1.000 38.94414  ? 37  VAL B CG1 1 
ATOM   2554 C CG2 . VAL B 2 38  ? 13.53900  -7.49200  -13.98600 1.000 38.09930  ? 37  VAL B CG2 1 
ATOM   2555 N N   . ASP B 2 39  ? 17.31600  -6.24600  -11.54200 1.000 52.73527  ? 38  ASP B N   1 
ATOM   2556 C CA  . ASP B 2 39  ? 18.72300  -6.27000  -11.19300 1.000 54.83289  ? 38  ASP B CA  1 
ATOM   2557 C C   . ASP B 2 39  ? 19.04500  -7.58200  -10.50700 1.000 52.03782  ? 38  ASP B C   1 
ATOM   2558 O O   . ASP B 2 39  ? 18.28900  -8.04000  -9.64900  1.000 48.44528  ? 38  ASP B O   1 
ATOM   2559 C CB  . ASP B 2 39  ? 19.07400  -5.10600  -10.27300 1.000 55.09871  ? 38  ASP B CB  1 
ATOM   2560 C CG  . ASP B 2 39  ? 19.05100  -3.77900  -11.00200 1.000 58.18329  ? 38  ASP B CG  1 
ATOM   2561 O OD1 . ASP B 2 39  ? 19.56500  -3.72400  -12.13500 1.000 59.23342  ? 38  ASP B OD1 1 
ATOM   2562 O OD2 . ASP B 2 39  ? 18.52200  -2.79800  -10.44300 1.000 60.61516  ? 38  ASP B OD2 1 
ATOM   2563 N N   . LEU B 2 40  ? 20.17400  -8.16800  -10.88200 1.000 53.11689  ? 39  LEU B N   1 
ATOM   2564 C CA  . LEU B 2 40  ? 20.74000  -9.29300  -10.15900 1.000 51.14824  ? 39  LEU B CA  1 
ATOM   2565 C C   . LEU B 2 40  ? 21.73100  -8.76400  -9.12800  1.000 53.00372  ? 39  LEU B C   1 
ATOM   2566 O O   . LEU B 2 40  ? 22.61600  -7.96600  -9.45700  1.000 55.26978  ? 39  LEU B O   1 
ATOM   2567 C CB  . LEU B 2 40  ? 21.40900  -10.26800 -11.13200 1.000 49.60858  ? 39  LEU B CB  1 
ATOM   2568 C CG  . LEU B 2 40  ? 20.41300  -10.87700 -12.13100 1.000 45.85023  ? 39  LEU B CG  1 
ATOM   2569 C CD1 . LEU B 2 40  ? 20.99300  -12.02700 -12.92500 1.000 40.32589  ? 39  LEU B CD1 1 
ATOM   2570 C CD2 . LEU B 2 40  ? 19.20000  -11.35200 -11.39000 1.000 40.74436  ? 39  LEU B CD2 1 
ATOM   2571 N N   . LEU B 2 41  ? 21.56800  -9.18400  -7.87700  1.000 48.95324  ? 40  LEU B N   1 
ATOM   2572 C CA  . LEU B 2 41  ? 22.36600  -8.64200  -6.78700  1.000 50.22971  ? 40  LEU B CA  1 
ATOM   2573 C C   . LEU B 2 41  ? 23.32500  -9.69200  -6.25000  1.000 49.67175  ? 40  LEU B C   1 
ATOM   2574 O O   . LEU B 2 41  ? 22.95000  -10.85800 -6.06500  1.000 46.28713  ? 40  LEU B O   1 
ATOM   2575 C CB  . LEU B 2 41  ? 21.49300  -8.14700  -5.63500  1.000 50.39815  ? 40  LEU B CB  1 
ATOM   2576 C CG  . LEU B 2 41  ? 20.37700  -7.12700  -5.83500  1.000 52.49577  ? 40  LEU B CG  1 
ATOM   2577 C CD1 . LEU B 2 41  ? 19.90800  -6.71800  -4.44800  1.000 54.74604  ? 40  LEU B CD1 1 
ATOM   2578 C CD2 . LEU B 2 41  ? 20.82000  -5.91700  -6.64600  1.000 56.32254  ? 40  LEU B CD2 1 
ATOM   2579 N N   . LYS B 2 42  ? 24.55900  -9.26800  -5.99400  1.000 51.06928  ? 41  LYS B N   1 
ATOM   2580 C CA  . LYS B 2 42  ? 25.54300  -10.07000 -5.27300  1.000 51.11929  ? 41  LYS B CA  1 
ATOM   2581 C C   . LYS B 2 42  ? 25.87400  -9.33400  -3.98700  1.000 55.63825  ? 41  LYS B C   1 
ATOM   2582 O O   . LYS B 2 42  ? 26.45600  -8.24400  -4.02500  1.000 60.80992  ? 41  LYS B O   1 
ATOM   2583 C CB  . LYS B 2 42  ? 26.80100  -10.30900 -6.10500  1.000 52.41681  ? 41  LYS B CB  1 
ATOM   2584 C CG  . LYS B 2 42  ? 27.84800  -11.12300 -5.37500  1.000 52.68526  ? 41  LYS B CG  1 
ATOM   2585 C CD  . LYS B 2 42  ? 29.13700  -11.24500 -6.16800  1.000 55.07502  ? 41  LYS B CD  1 
ATOM   2586 C CE  . LYS B 2 42  ? 30.13000  -12.11700 -5.42300  1.000 55.13293  ? 41  LYS B CE  1 
ATOM   2587 N NZ  . LYS B 2 42  ? 31.45300  -12.18300 -6.09500  1.000 58.41227  ? 41  LYS B NZ  1 
ATOM   2588 N N   . ASN B 2 43  ? 25.50200  -9.93200  -2.85400  1.000 54.15386  ? 42  ASN B N   1 
ATOM   2589 C CA  . ASN B 2 43  ? 25.73700  -9.33800  -1.53800  1.000 56.06462  ? 42  ASN B CA  1 
ATOM   2590 C C   . ASN B 2 43  ? 25.15000  -7.93400  -1.49200  1.000 56.25411  ? 42  ASN B C   1 
ATOM   2591 O O   . ASN B 2 43  ? 25.75300  -6.99700  -0.96600  1.000 58.95707  ? 42  ASN B O   1 
ATOM   2592 C CB  . ASN B 2 43  ? 27.23000  -9.33000  -1.17600  1.000 59.72032  ? 42  ASN B CB  1 
ATOM   2593 C CG  . ASN B 2 43  ? 27.81500  -10.74000 -1.03100  1.000 60.16511  ? 42  ASN B CG  1 
ATOM   2594 O OD1 . ASN B 2 43  ? 27.12800  -11.67200 -0.60900  1.000 58.32541  ? 42  ASN B OD1 1 
ATOM   2595 N ND2 . ASN B 2 43  ? 29.07600  -10.89700 -1.40300  1.000 63.07598  ? 42  ASN B ND2 1 
ATOM   2596 N N   . GLY B 2 44  ? 23.96600  -7.78900  -2.08700  1.000 56.31465  ? 43  GLY B N   1 
ATOM   2597 C CA  . GLY B 2 44  ? 23.28300  -6.51800  -2.16000  1.000 57.83851  ? 43  GLY B CA  1 
ATOM   2598 C C   . GLY B 2 44  ? 23.73700  -5.58500  -3.26400  1.000 61.47579  ? 43  GLY B C   1 
ATOM   2599 O O   . GLY B 2 44  ? 23.09000  -4.55100  -3.47600  1.000 62.00743  ? 43  GLY B O   1 
ATOM   2600 N N   . GLU B 2 45  ? 24.81600  -5.90100  -3.97500  1.000 60.65464  ? 44  GLU B N   1 
ATOM   2601 C CA  . GLU B 2 45  ? 25.37000  -4.99500  -4.97300  1.000 63.87082  ? 44  GLU B CA  1 
ATOM   2602 C C   . GLU B 2 45  ? 24.99100  -5.46900  -6.36900  1.000 64.50510  ? 44  GLU B C   1 
ATOM   2603 O O   . GLU B 2 45  ? 25.09600  -6.66100  -6.68200  1.000 61.92848  ? 44  GLU B O   1 
ATOM   2604 C CB  . GLU B 2 45  ? 26.89100  -4.87400  -4.83500  1.000 65.76315  ? 44  GLU B CB  1 
ATOM   2605 C CG  . GLU B 2 45  ? 27.33400  -3.98000  -3.68500  1.000 67.74233  ? 44  GLU B CG  1 
ATOM   2606 C CD  . GLU B 2 45  ? 28.84400  -3.78000  -3.61800  1.000 72.03232  ? 44  GLU B CD  1 
ATOM   2607 O OE1 . GLU B 2 45  ? 29.55200  -4.16900  -4.57200  1.000 73.51408  ? 44  GLU B OE1 1 
ATOM   2608 O OE2 . GLU B 2 45  ? 29.32800  -3.23000  -2.60700  1.000 74.63790  ? 44  GLU B OE2 1 
ATOM   2609 N N   . ARG B 2 46  ? 24.54400  -4.53100  -7.20000  1.000 61.98901  ? 45  ARG B N   1 
ATOM   2610 C CA  . ARG B 2 46  ? 24.10400  -4.86800  -8.54700  1.000 63.06019  ? 45  ARG B CA  1 
ATOM   2611 C C   . ARG B 2 46  ? 25.25400  -5.46000  -9.35000  1.000 63.66290  ? 45  ARG B C   1 
ATOM   2612 O O   . ARG B 2 46  ? 26.35300  -4.90700  -9.38500  1.000 66.25005  ? 45  ARG B O   1 
ATOM   2613 C CB  . ARG B 2 46  ? 23.55000  -3.62200  -9.23600  1.000 64.76303  ? 45  ARG B CB  1 
ATOM   2614 C CG  . ARG B 2 46  ? 22.98100  -3.88400  -10.61200 1.000 66.62904  ? 45  ARG B CG  1 
ATOM   2615 C CD  . ARG B 2 46  ? 22.31800  -2.64400  -11.17600 1.000 67.86866  ? 45  ARG B CD  1 
ATOM   2616 N NE  . ARG B 2 46  ? 23.27200  -1.56300  -11.36400 1.000 71.83230  ? 45  ARG B NE  1 
ATOM   2617 C CZ  . ARG B 2 46  ? 23.93400  -1.34200  -12.49100 1.000 75.23007  ? 45  ARG B CZ  1 
ATOM   2618 N NH1 . ARG B 2 46  ? 23.76200  -2.11200  -13.55600 1.000 75.25113  ? 45  ARG B NH1 1 
ATOM   2619 N NH2 . ARG B 2 46  ? 24.78600  -0.32100  -12.55100 1.000 77.68300  ? 45  ARG B NH2 1 
ATOM   2620 N N   . ILE B 2 47  ? 25.00600  -6.60600  -9.96400  1.000 62.49170  ? 46  ILE B N   1 
ATOM   2621 C CA  . ILE B 2 47  ? 25.96700  -7.21400  -10.87800 1.000 63.08125  ? 46  ILE B CA  1 
ATOM   2622 C C   . ILE B 2 47  ? 25.89000  -6.49000  -12.21600 1.000 68.10817  ? 46  ILE B C   1 
ATOM   2623 O O   . ILE B 2 47  ? 24.79900  -6.14700  -12.68800 1.000 68.18186  ? 46  ILE B O   1 
ATOM   2624 C CB  . ILE B 2 47  ? 25.68000  -8.71900  -11.02800 1.000 59.70453  ? 46  ILE B CB  1 
ATOM   2625 C CG1 . ILE B 2 47  ? 25.93200  -9.44100  -9.70100  1.000 55.22241  ? 46  ILE B CG1 1 
ATOM   2626 C CG2 . ILE B 2 47  ? 26.47200  -9.33400  -12.20200 1.000 59.54398  ? 46  ILE B CG2 1 
ATOM   2627 C CD1 . ILE B 2 47  ? 25.08400  -10.69000 -9.52900  1.000 51.06402  ? 46  ILE B CD1 1 
ATOM   2628 N N   . GLU B 2 48  ? 27.05500  -6.25000  -12.82900 1.000 61.88374  ? 47  GLU B N   1 
ATOM   2629 C CA  . GLU B 2 48  ? 27.14300  -5.37000  -13.99400 1.000 65.04464  ? 47  GLU B CA  1 
ATOM   2630 C C   . GLU B 2 48  ? 26.69900  -6.05800  -15.28400 1.000 63.61289  ? 47  GLU B C   1 
ATOM   2631 O O   . GLU B 2 48  ? 25.81200  -5.56200  -15.98400 1.000 64.19717  ? 47  GLU B O   1 
ATOM   2632 C CB  . GLU B 2 48  ? 28.57300  -4.83700  -14.14000 1.000 70.92693  ? 47  GLU B CB  1 
ATOM   2633 N N   . LYS B 2 49  ? 27.30900  -7.19500  -15.62400 1.000 89.71602  ? 48  LYS B N   1 
ATOM   2634 C CA  . LYS B 2 49  ? 27.13600  -7.79700  -16.95200 1.000 91.66625  ? 48  LYS B CA  1 
ATOM   2635 C C   . LYS B 2 49  ? 25.90800  -8.71400  -16.98700 1.000 88.54483  ? 48  LYS B C   1 
ATOM   2636 O O   . LYS B 2 49  ? 25.99800  -9.92700  -17.17900 1.000 85.41024  ? 48  LYS B O   1 
ATOM   2637 C CB  . LYS B 2 49  ? 28.39700  -8.55100  -17.35400 1.000 90.13712  ? 48  LYS B CB  1 
ATOM   2638 C CG  . LYS B 2 49  ? 29.61000  -7.66000  -17.56700 1.000 94.01127  ? 48  LYS B CG  1 
ATOM   2639 C CD  . LYS B 2 49  ? 29.34200  -6.65800  -18.67200 1.000 98.36179  ? 48  LYS B CD  1 
ATOM   2640 C CE  . LYS B 2 49  ? 30.60400  -5.93600  -19.10300 1.000 103.24922 ? 48  LYS B CE  1 
ATOM   2641 N NZ  . LYS B 2 49  ? 30.36200  -5.14600  -20.34200 1.000 106.95756 ? 48  LYS B NZ  1 
ATOM   2642 N N   . VAL B 2 50  ? 24.73500  -8.10100  -16.83500 1.000 55.58561  ? 49  VAL B N   1 
ATOM   2643 C CA  . VAL B 2 50  ? 23.46500  -8.82100  -16.85500 1.000 50.95874  ? 49  VAL B CA  1 
ATOM   2644 C C   . VAL B 2 50  ? 22.80200  -8.64000  -18.21300 1.000 53.64064  ? 49  VAL B C   1 
ATOM   2645 O O   . VAL B 2 50  ? 22.59300  -7.50900  -18.66700 1.000 56.06725  ? 49  VAL B O   1 
ATOM   2646 C CB  . VAL B 2 50  ? 22.52700  -8.34000  -15.73800 1.000 48.51898  ? 49  VAL B CB  1 
ATOM   2647 C CG1 . VAL B 2 50  ? 21.19900  -9.05500  -15.84500 1.000 44.48691  ? 49  VAL B CG1 1 
ATOM   2648 C CG2 . VAL B 2 50  ? 23.14900  -8.60200  -14.36800 1.000 48.45844  ? 49  VAL B CG2 1 
ATOM   2649 N N   . GLU B 2 51  ? 22.43400  -9.74500  -18.84000 1.000 56.74365  ? 50  GLU B N   1 
ATOM   2650 C CA  . GLU B 2 51  ? 21.68900  -9.72100  -20.08800 1.000 57.35688  ? 50  GLU B CA  1 
ATOM   2651 C C   . GLU B 2 51  ? 20.26500  -10.20300 -19.84600 1.000 50.99296  ? 50  GLU B C   1 
ATOM   2652 O O   . GLU B 2 51  ? 19.93700  -10.76300 -18.79400 1.000 45.79233  ? 50  GLU B O   1 
ATOM   2653 C CB  . GLU B 2 51  ? 22.38500  -10.58300 -21.14000 1.000 60.81255  ? 50  GLU B CB  1 
ATOM   2654 C CG  . GLU B 2 51  ? 23.87500  -10.35000 -21.19200 1.000 65.31046  ? 50  GLU B CG  1 
ATOM   2655 C CD  . GLU B 2 51  ? 24.56100  -11.22300 -22.21300 1.000 66.81591  ? 50  GLU B CD  1 
ATOM   2656 O OE1 . GLU B 2 51  ? 24.28700  -11.04800 -23.41900 1.000 70.92693  ? 50  GLU B OE1 1 
ATOM   2657 O OE2 . GLU B 2 51  ? 25.36300  -12.09100 -21.80400 1.000 60.37303  ? 50  GLU B OE2 1 
ATOM   2658 N N   . HIS B 2 52  ? 19.40500  -9.96300  -20.82900 1.000 53.29850  ? 51  HIS B N   1 
ATOM   2659 C CA  . HIS B 2 52  ? 18.04500  -10.45200 -20.72100 1.000 46.57137  ? 51  HIS B CA  1 
ATOM   2660 C C   . HIS B 2 52  ? 17.53600  -10.86000 -22.09300 1.000 46.60032  ? 51  HIS B C   1 
ATOM   2661 O O   . HIS B 2 52  ? 18.02400  -10.40300 -23.13300 1.000 50.69818  ? 51  HIS B O   1 
ATOM   2662 C CB  . HIS B 2 52  ? 17.10000  -9.42100  -20.09300 1.000 42.75513  ? 51  HIS B CB  1 
ATOM   2663 C CG  . HIS B 2 52  ? 16.95200  -8.16700  -20.89200 1.000 44.32374  ? 51  HIS B CG  1 
ATOM   2664 N ND1 . HIS B 2 52  ? 16.19400  -8.09700  -22.03900 1.000 43.69471  ? 51  HIS B ND1 1 
ATOM   2665 C CD2 . HIS B 2 52  ? 17.47200  -6.93000  -20.70900 1.000 47.35305  ? 51  HIS B CD2 1 
ATOM   2666 C CE1 . HIS B 2 52  ? 16.25400  -6.87200  -22.53300 1.000 47.14513  ? 51  HIS B CE1 1 
ATOM   2667 N NE2 . HIS B 2 52  ? 17.02100  -6.14300  -21.74100 1.000 48.96113  ? 51  HIS B NE2 1 
ATOM   2668 N N   . SER B 2 53  ? 16.53600  -11.73800 -22.06300 1.000 39.49158  ? 52  SER B N   1 
ATOM   2669 C CA  . SER B 2 53  ? 15.90000  -12.21300 -23.27500 1.000 38.07299  ? 52  SER B CA  1 
ATOM   2670 C C   . SER B 2 53  ? 15.07700  -11.09300 -23.89900 1.000 37.37290  ? 52  SER B C   1 
ATOM   2671 O O   . SER B 2 53  ? 14.79700  -10.06500 -23.27300 1.000 37.63609  ? 52  SER B O   1 
ATOM   2672 C CB  . SER B 2 53  ? 15.02100  -13.43200 -22.96700 1.000 35.95168  ? 52  SER B CB  1 
ATOM   2673 O OG  . SER B 2 53  ? 13.93400  -13.05100 -22.14300 1.000 34.03829  ? 52  SER B OG  1 
ATOM   2674 N N   . ASP B 2 54  ? 14.67800  -11.30700 -25.14800 1.000 40.23640  ? 53  ASP B N   1 
ATOM   2675 C CA  . ASP B 2 54  ? 13.81600  -10.36300 -25.84000 1.000 39.49947  ? 53  ASP B CA  1 
ATOM   2676 C C   . ASP B 2 54  ? 12.39500  -10.42600 -25.29800 1.000 37.34921  ? 53  ASP B C   1 
ATOM   2677 O O   . ASP B 2 54  ? 11.86200  -11.51300 -25.03500 1.000 35.77271  ? 53  ASP B O   1 
ATOM   2678 C CB  . ASP B 2 54  ? 13.78600  -10.67100 -27.33100 1.000 38.84676  ? 53  ASP B CB  1 
ATOM   2679 C CG  . ASP B 2 54  ? 15.15800  -10.67800 -27.94300 1.000 41.18125  ? 53  ASP B CG  1 
ATOM   2680 O OD1 . ASP B 2 54  ? 15.95600  -9.76700  -27.63000 1.000 43.11043  ? 53  ASP B OD1 1 
ATOM   2681 O OD2 . ASP B 2 54  ? 15.45200  -11.60200 -28.72900 1.000 41.31022  ? 53  ASP B OD2 1 
ATOM   2682 N N   . LEU B 2 55  ? 11.76600  -9.25500  -25.21000 1.000 32.89868  ? 54  LEU B N   1 
ATOM   2683 C CA  . LEU B 2 55  ? 10.41700  -9.13600  -24.67900 1.000 31.01688  ? 54  LEU B CA  1 
ATOM   2684 C C   . LEU B 2 55  ? 9.42600   -9.97200  -25.48200 1.000 29.73514  ? 54  LEU B C   1 
ATOM   2685 O O   . LEU B 2 55  ? 9.34800   -9.86200  -26.71800 1.000 30.37206  ? 54  LEU B O   1 
ATOM   2686 C CB  . LEU B 2 55  ? 9.97600   -7.67600  -24.69600 1.000 31.74065  ? 54  LEU B CB  1 
ATOM   2687 C CG  . LEU B 2 55  ? 8.62500   -7.48200  -24.01300 1.000 30.59051  ? 54  LEU B CG  1 
ATOM   2688 C CD1 . LEU B 2 55  ? 8.82100   -7.44900  -22.49800 1.000 31.24585  ? 54  LEU B CD1 1 
ATOM   2689 C CD2 . LEU B 2 55  ? 7.96200   -6.21200  -24.49700 1.000 31.26954  ? 54  LEU B CD2 1 
ATOM   2690 N N   . SER B 2 56  ? 8.68700   -10.83000 -24.77400 1.000 33.98302  ? 55  SER B N   1 
ATOM   2691 C CA  . SER B 2 56  ? 7.63800   -11.64000 -25.36900 1.000 33.16977  ? 55  SER B CA  1 
ATOM   2692 C C   . SER B 2 56  ? 6.49100   -11.70500 -24.37500 1.000 32.28545  ? 55  SER B C   1 
ATOM   2693 O O   . SER B 2 56  ? 6.58300   -11.15100 -23.27300 1.000 32.14859  ? 55  SER B O   1 
ATOM   2694 C CB  . SER B 2 56  ? 8.16200   -13.04000 -25.73200 1.000 34.43044  ? 55  SER B CB  1 
ATOM   2695 O OG  . SER B 2 56  ? 7.24100   -13.72700 -26.57900 1.000 35.02262  ? 55  SER B OG  1 
ATOM   2696 N N   . PHE B 2 57  ? 5.42200   -12.42400 -24.73800 1.000 28.45868  ? 56  PHE B N   1 
ATOM   2697 C CA  . PHE B 2 57  ? 4.25200   -12.47600 -23.87300 1.000 28.26655  ? 56  PHE B CA  1 
ATOM   2698 C C   . PHE B 2 57  ? 3.47600   -13.77600 -24.06300 1.000 28.83767  ? 56  PHE B C   1 
ATOM   2699 O O   . PHE B 2 57  ? 3.60500   -14.47700 -25.07500 1.000 29.33510  ? 56  PHE B O   1 
ATOM   2700 C CB  . PHE B 2 57  ? 3.33900   -11.24900 -24.08800 1.000 27.90335  ? 56  PHE B CB  1 
ATOM   2701 C CG  . PHE B 2 57  ? 2.90300   -11.04200 -25.52100 1.000 27.97967  ? 56  PHE B CG  1 
ATOM   2702 C CD1 . PHE B 2 57  ? 1.83600   -11.77700 -26.05400 1.000 28.25076  ? 56  PHE B CD1 1 
ATOM   2703 C CD2 . PHE B 2 57  ? 3.52900   -10.09500 -26.32200 1.000 28.10337  ? 56  PHE B CD2 1 
ATOM   2704 C CE1 . PHE B 2 57  ? 1.42500   -11.58300 -27.36200 1.000 28.55079  ? 56  PHE B CE1 1 
ATOM   2705 C CE2 . PHE B 2 57  ? 3.12800   -9.89300  -27.63700 1.000 28.52447  ? 56  PHE B CE2 1 
ATOM   2706 C CZ  . PHE B 2 57  ? 2.06600   -10.63600 -28.15700 1.000 28.69555  ? 56  PHE B CZ  1 
ATOM   2707 N N   . SER B 2 58  ? 2.68100   -14.09600 -23.03500 1.000 33.13818  ? 57  SER B N   1 
ATOM   2708 C CA  . SER B 2 58  ? 1.89200   -15.31100 -22.92400 1.000 34.45150  ? 57  SER B CA  1 
ATOM   2709 C C   . SER B 2 58  ? 0.52700   -15.11200 -23.56200 1.000 34.82523  ? 57  SER B C   1 
ATOM   2710 O O   . SER B 2 58  ? 0.12900   -13.99700 -23.90900 1.000 34.00145  ? 57  SER B O   1 
ATOM   2711 C CB  . SER B 2 58  ? 1.72500   -15.70500 -21.45000 1.000 34.53835  ? 57  SER B CB  1 
ATOM   2712 O OG  . SER B 2 58  ? 2.97900   -15.78200 -20.81100 1.000 34.60152  ? 57  SER B OG  1 
ATOM   2713 N N   . LYS B 2 59  ? -0.22700  -16.21000 -23.65900 1.000 41.18389  ? 58  LYS B N   1 
ATOM   2714 C CA  . LYS B 2 59  ? -1.52500  -16.13800 -24.32000 1.000 41.57341  ? 58  LYS B CA  1 
ATOM   2715 C C   . LYS B 2 59  ? -2.48800  -15.17800 -23.62700 1.000 40.60487  ? 58  LYS B C   1 
ATOM   2716 O O   . LYS B 2 59  ? -3.38600  -14.64600 -24.28600 1.000 40.94438  ? 58  LYS B O   1 
ATOM   2717 C CB  . LYS B 2 59  ? -2.13000  -17.53300 -24.43100 1.000 43.08411  ? 58  LYS B CB  1 
ATOM   2718 C CG  . LYS B 2 59  ? -1.36600  -18.44300 -25.40300 1.000 45.03172  ? 58  LYS B CG  1 
ATOM   2719 C CD  . LYS B 2 59  ? -1.27400  -17.83500 -26.81900 1.000 46.31608  ? 58  LYS B CD  1 
ATOM   2720 C CE  . LYS B 2 59  ? -0.95400  -18.91300 -27.89200 1.000 47.86100  ? 58  LYS B CE  1 
ATOM   2721 N NZ  . LYS B 2 59  ? -0.26000  -18.41000 -29.14900 1.000 46.81088  ? 58  LYS B NZ  1 
ATOM   2722 N N   . ASP B 2 60  ? -2.30100  -14.90600 -22.33700 1.000 37.93086  ? 59  ASP B N   1 
ATOM   2723 C CA  . ASP B 2 60  ? -3.13100  -13.92800 -21.64100 1.000 38.27038  ? 59  ASP B CA  1 
ATOM   2724 C C   . ASP B 2 60  ? -2.61000  -12.49900 -21.78000 1.000 37.50186  ? 59  ASP B C   1 
ATOM   2725 O O   . ASP B 2 60  ? -3.14000  -11.59900 -21.12000 1.000 37.90191  ? 59  ASP B O   1 
ATOM   2726 C CB  . ASP B 2 60  ? -3.27900  -14.30800 -20.15200 1.000 38.94414  ? 59  ASP B CB  1 
ATOM   2727 C CG  . ASP B 2 60  ? -1.96600  -14.17200 -19.35600 1.000 38.64674  ? 59  ASP B CG  1 
ATOM   2728 O OD1 . ASP B 2 60  ? -0.90600  -13.81800 -19.93000 1.000 37.01760  ? 59  ASP B OD1 1 
ATOM   2729 O OD2 . ASP B 2 60  ? -1.99300  -14.42000 -18.13800 1.000 38.79676  ? 59  ASP B OD2 1 
ATOM   2730 N N   . TRP B 2 61  ? -1.58800  -12.28000 -22.61300 1.000 30.64052  ? 60  TRP B N   1 
ATOM   2731 C CA  . TRP B 2 61  ? -0.97100  -11.00000 -22.99000 1.000 29.97465  ? 60  TRP B CA  1 
ATOM   2732 C C   . TRP B 2 61  ? 0.00800   -10.49100 -21.93400 1.000 29.79305  ? 60  TRP B C   1 
ATOM   2733 O O   . TRP B 2 61  ? 0.62700   -9.45800  -22.15500 1.000 29.71672  ? 60  TRP B O   1 
ATOM   2734 C CB  . TRP B 2 61  ? -2.00700  -9.90500  -23.30800 1.000 30.80106  ? 60  TRP B CB  1 
ATOM   2735 C CG  . TRP B 2 61  ? -3.03000  -10.34800 -24.32900 1.000 31.13794  ? 60  TRP B CG  1 
ATOM   2736 C CD1 . TRP B 2 61  ? -4.33200  -10.69200 -24.09400 1.000 32.33546  ? 60  TRP B CD1 1 
ATOM   2737 C CD2 . TRP B 2 61  ? -2.82400  -10.51000 -25.74400 1.000 30.65368  ? 60  TRP B CD2 1 
ATOM   2738 N NE1 . TRP B 2 61  ? -4.94900  -11.06400 -25.26900 1.000 32.43284  ? 60  TRP B NE1 1 
ATOM   2739 C CE2 . TRP B 2 61  ? -4.04200  -10.96700 -26.29300 1.000 31.65380  ? 60  TRP B CE2 1 
ATOM   2740 C CE3 . TRP B 2 61  ? -1.72500  -10.33500 -26.59000 1.000 30.01412  ? 60  TRP B CE3 1 
ATOM   2741 C CZ2 . TRP B 2 61  ? -4.20100  -11.22000 -27.66000 1.000 32.29861  ? 60  TRP B CZ2 1 
ATOM   2742 C CZ3 . TRP B 2 61  ? -1.88300  -10.58300 -27.94200 1.000 30.70631  ? 60  TRP B CZ3 1 
ATOM   2743 C CH2 . TRP B 2 61  ? -3.11800  -11.03400 -28.46600 1.000 31.98541  ? 60  TRP B CH2 1 
ATOM   2744 N N   . SER B 2 62  ? 0.20900   -11.18900 -20.82200 1.000 34.32517  ? 61  SER B N   1 
ATOM   2745 C CA  . SER B 2 62  ? 1.19300   -10.72000 -19.86200 1.000 34.27516  ? 61  SER B CA  1 
ATOM   2746 C C   . SER B 2 62  ? 2.60500   -11.04600 -20.34300 1.000 33.55402  ? 61  SER B C   1 
ATOM   2747 O O   . SER B 2 62  ? 2.84100   -12.05300 -21.02500 1.000 33.22240  ? 61  SER B O   1 
ATOM   2748 C CB  . SER B 2 62  ? 0.95200   -11.32700 -18.48900 1.000 35.09368  ? 61  SER B CB  1 
ATOM   2749 O OG  . SER B 2 62  ? 1.11200   -12.72300 -18.53300 1.000 35.10158  ? 61  SER B OG  1 
ATOM   2750 N N   . PHE B 2 63  ? 3.54600   -10.17200 -19.98300 1.000 31.63537  ? 62  PHE B N   1 
ATOM   2751 C CA  . PHE B 2 63  ? 4.90900   -10.27200 -20.48600 1.000 28.89557  ? 62  PHE B CA  1 
ATOM   2752 C C   . PHE B 2 63  ? 5.77000   -11.20200 -19.63800 1.000 27.40065  ? 62  PHE B C   1 
ATOM   2753 O O   . PHE B 2 63  ? 5.52700   -11.43300 -18.43500 1.000 28.32971  ? 62  PHE B O   1 
ATOM   2754 C CB  . PHE B 2 63  ? 5.56700   -8.89100  -20.55200 1.000 30.65104  ? 62  PHE B CB  1 
ATOM   2755 C CG  . PHE B 2 63  ? 4.89200   -7.96600  -21.48900 1.000 32.31177  ? 62  PHE B CG  1 
ATOM   2756 C CD1 . PHE B 2 63  ? 5.15900   -8.02700  -22.86400 1.000 30.40365  ? 62  PHE B CD1 1 
ATOM   2757 C CD2 . PHE B 2 63  ? 3.97400   -7.03800  -21.02500 1.000 36.15433  ? 62  PHE B CD2 1 
ATOM   2758 C CE1 . PHE B 2 63  ? 4.52600   -7.18600  -23.73200 1.000 31.66695  ? 62  PHE B CE1 1 
ATOM   2759 C CE2 . PHE B 2 63  ? 3.33600   -6.19500  -21.89300 1.000 36.82810  ? 62  PHE B CE2 1 
ATOM   2760 C CZ  . PHE B 2 63  ? 3.60600   -6.26100  -23.25800 1.000 34.17778  ? 62  PHE B CZ  1 
ATOM   2761 N N   . TYR B 2 64  ? 6.83800   -11.69100 -20.26100 1.000 30.48787  ? 63  TYR B N   1 
ATOM   2762 C CA  . TYR B 2 64  ? 7.84800   -12.40500 -19.50200 1.000 29.72988  ? 63  TYR B CA  1 
ATOM   2763 C C   . TYR B 2 64  ? 9.22300   -12.09900 -20.07300 1.000 29.56933  ? 63  TYR B C   1 
ATOM   2764 O O   . TYR B 2 64  ? 9.38000   -11.84200 -21.27900 1.000 29.35089  ? 63  TYR B O   1 
ATOM   2765 C CB  . TYR B 2 64  ? 7.59200   -13.92300 -19.48700 1.000 29.36931  ? 63  TYR B CB  1 
ATOM   2766 C CG  . TYR B 2 64  ? 7.61800   -14.58200 -20.84300 1.000 29.82989  ? 63  TYR B CG  1 
ATOM   2767 C CD1 . TYR B 2 64  ? 8.81900   -14.99300 -21.42600 1.000 30.15625  ? 63  TYR B CD1 1 
ATOM   2768 C CD2 . TYR B 2 64  ? 6.43800   -14.80200 -21.54500 1.000 30.90107  ? 63  TYR B CD2 1 
ATOM   2769 C CE1 . TYR B 2 64  ? 8.82600   -15.61300 -22.70600 1.000 31.35113  ? 63  TYR B CE1 1 
ATOM   2770 C CE2 . TYR B 2 64  ? 6.43600   -15.41400 -22.79800 1.000 32.06174  ? 63  TYR B CE2 1 
ATOM   2771 C CZ  . TYR B 2 64  ? 7.63600   -15.82400 -23.36600 1.000 32.19070  ? 63  TYR B CZ  1 
ATOM   2772 O OH  . TYR B 2 64  ? 7.61600   -16.42600 -24.61000 1.000 33.87775  ? 63  TYR B OH  1 
ATOM   2773 N N   . LEU B 2 65  ? 10.21500  -12.13500 -19.18300 1.000 31.61432  ? 64  LEU B N   1 
ATOM   2774 C CA  . LEU B 2 65  ? 11.62100  -11.87500 -19.47400 1.000 32.74603  ? 64  LEU B CA  1 
ATOM   2775 C C   . LEU B 2 65  ? 12.51100  -12.75200 -18.59800 1.000 32.79077  ? 64  LEU B C   1 
ATOM   2776 O O   . LEU B 2 65  ? 12.22800  -12.95100 -17.41400 1.000 32.23281  ? 64  LEU B O   1 
ATOM   2777 C CB  . LEU B 2 65  ? 12.00100  -10.41000 -19.20200 1.000 35.01999  ? 64  LEU B CB  1 
ATOM   2778 C CG  . LEU B 2 65  ? 11.43600  -9.32800  -20.09900 1.000 36.62808  ? 64  LEU B CG  1 
ATOM   2779 C CD1 . LEU B 2 65  ? 11.81400  -7.96900  -19.55100 1.000 40.44432  ? 64  LEU B CD1 1 
ATOM   2780 C CD2 . LEU B 2 65  ? 11.97600  -9.52500  -21.52600 1.000 36.53070  ? 64  LEU B CD2 1 
ATOM   2781 N N   . LEU B 2 66  ? 13.61300  -13.23000 -19.16500 1.000 29.26140  ? 65  LEU B N   1 
ATOM   2782 C CA  . LEU B 2 66  ? 14.65400  -13.90800 -18.40000 1.000 30.49050  ? 65  LEU B CA  1 
ATOM   2783 C C   . LEU B 2 66  ? 15.89000  -13.01400 -18.34900 1.000 32.94342  ? 65  LEU B C   1 
ATOM   2784 O O   . LEU B 2 66  ? 16.37800  -12.58500 -19.40000 1.000 34.41465  ? 65  LEU B O   1 
ATOM   2785 C CB  . LEU B 2 66  ? 15.01600  -15.25200 -19.03500 1.000 31.93278  ? 65  LEU B CB  1 
ATOM   2786 C CG  . LEU B 2 66  ? 16.16400  -15.93200 -18.29300 1.000 34.09093  ? 65  LEU B CG  1 
ATOM   2787 C CD1 . LEU B 2 66  ? 15.68700  -16.36800 -16.90600 1.000 32.66444  ? 65  LEU B CD1 1 
ATOM   2788 C CD2 . LEU B 2 66  ? 16.71100  -17.09800 -19.09600 1.000 37.42554  ? 65  LEU B CD2 1 
ATOM   2789 N N   . TYR B 2 67  ? 16.35300  -12.70600 -17.13600 1.000 33.80142  ? 66  TYR B N   1 
ATOM   2790 C CA  . TYR B 2 67  ? 17.59900  -11.99100 -16.86900 1.000 36.82810  ? 66  TYR B CA  1 
ATOM   2791 C C   . TYR B 2 67  ? 18.63300  -12.98800 -16.36100 1.000 38.27564  ? 66  TYR B C   1 
ATOM   2792 O O   . TYR B 2 67  ? 18.31000  -13.85700 -15.54000 1.000 36.47806  ? 66  TYR B O   1 
ATOM   2793 C CB  . TYR B 2 67  ? 17.39800  -10.88600 -15.82300 1.000 37.18604  ? 66  TYR B CB  1 
ATOM   2794 C CG  . TYR B 2 67  ? 16.66100  -9.67900  -16.34300 1.000 38.37302  ? 66  TYR B CG  1 
ATOM   2795 C CD1 . TYR B 2 67  ? 15.28400  -9.71400  -16.53900 1.000 36.16486  ? 66  TYR B CD1 1 
ATOM   2796 C CD2 . TYR B 2 67  ? 17.33800  -8.49900  -16.64400 1.000 41.98135  ? 66  TYR B CD2 1 
ATOM   2797 C CE1 . TYR B 2 67  ? 14.60400  -8.60900  -17.04300 1.000 38.11510  ? 66  TYR B CE1 1 
ATOM   2798 C CE2 . TYR B 2 67  ? 16.66300  -7.39200  -17.13000 1.000 43.10254  ? 66  TYR B CE2 1 
ATOM   2799 C CZ  . TYR B 2 67  ? 15.29700  -7.45700  -17.33000 1.000 42.03925  ? 66  TYR B CZ  1 
ATOM   2800 O OH  . TYR B 2 67  ? 14.60600  -6.35700  -17.80500 1.000 43.13675  ? 66  TYR B OH  1 
ATOM   2801 N N   . TYR B 2 68  ? 19.85300  -12.87700 -16.87600 1.000 33.62245  ? 67  TYR B N   1 
ATOM   2802 C CA  . TYR B 2 68  ? 20.86900  -13.89400 -16.53600 1.000 35.18580  ? 67  TYR B CA  1 
ATOM   2803 C C   . TYR B 2 68  ? 22.29000  -13.33100 -16.53400 1.000 39.28629  ? 67  TYR B C   1 
ATOM   2804 O O   . TYR B 2 68  ? 22.55300  -12.35300 -17.24400 1.000 41.56814  ? 67  TYR B O   1 
ATOM   2805 C CB  . TYR B 2 68  ? 20.78500  -15.04500 -17.53700 1.000 36.35436  ? 67  TYR B CB  1 
ATOM   2806 C CG  . TYR B 2 68  ? 20.87600  -14.63600 -18.98400 1.000 39.47579  ? 67  TYR B CG  1 
ATOM   2807 C CD1 . TYR B 2 68  ? 19.77300  -14.14400 -19.65900 1.000 36.55965  ? 67  TYR B CD1 1 
ATOM   2808 C CD2 . TYR B 2 68  ? 22.06600  -14.74500 -19.67900 1.000 44.57377  ? 67  TYR B CD2 1 
ATOM   2809 C CE1 . TYR B 2 68  ? 19.85100  -13.76300 -20.98600 1.000 39.04416  ? 67  TYR B CE1 1 
ATOM   2810 C CE2 . TYR B 2 68  ? 22.16200  -14.37300 -21.00800 1.000 47.28988  ? 67  TYR B CE2 1 
ATOM   2811 C CZ  . TYR B 2 68  ? 21.05000  -13.88000 -21.66500 1.000 44.09739  ? 67  TYR B CZ  1 
ATOM   2812 O OH  . TYR B 2 68  ? 21.14000  -13.51300 -22.97400 1.000 44.49481  ? 67  TYR B OH  1 
ATOM   2813 N N   . THR B 2 69  ? 23.16900  -13.95400 -15.75100 1.000 46.28450  ? 68  THR B N   1 
ATOM   2814 C CA  . THR B 2 69  ? 24.59900  -13.56800 -15.70800 1.000 49.09010  ? 68  THR B CA  1 
ATOM   2815 C C   . THR B 2 69  ? 25.39000  -14.80000 -15.29100 1.000 50.35341  ? 68  THR B C   1 
ATOM   2816 O O   . THR B 2 69  ? 24.87600  -15.57700 -14.48100 1.000 48.21631  ? 68  THR B O   1 
ATOM   2817 C CB  . THR B 2 69  ? 24.88400  -12.42600 -14.73000 1.000 48.67952  ? 68  THR B CB  1 
ATOM   2818 O OG1 . THR B 2 69  ? 26.28200  -12.15500 -14.78800 1.000 50.96401  ? 68  THR B OG1 1 
ATOM   2819 C CG2 . THR B 2 69  ? 24.48300  -12.74800 -13.30900 1.000 45.80023  ? 68  THR B CG2 1 
ATOM   2820 N N   . GLU B 2 70  ? 26.57800  -14.97400 -15.85400 1.000 60.33618  ? 69  GLU B N   1 
ATOM   2821 C CA  . GLU B 2 70  ? 27.45400  -16.09800 -15.45100 1.000 61.71003  ? 69  GLU B CA  1 
ATOM   2822 C C   . GLU B 2 70  ? 27.97300  -15.80500 -14.04900 1.000 59.98877  ? 69  GLU B C   1 
ATOM   2823 O O   . GLU B 2 70  ? 28.31000  -14.65500 -13.78100 1.000 60.43883  ? 69  GLU B O   1 
ATOM   2824 C CB  . GLU B 2 70  ? 28.60300  -16.29100 -16.43800 1.000 66.18688  ? 69  GLU B CB  1 
ATOM   2825 C CG  . GLU B 2 70  ? 29.13200  -17.70900 -16.48200 1.000 68.50295  ? 69  GLU B CG  1 
ATOM   2826 C CD  . GLU B 2 70  ? 29.83600  -18.07700 -17.77700 1.000 73.25352  ? 69  GLU B CD  1 
ATOM   2827 O OE1 . GLU B 2 70  ? 30.09700  -17.16600 -18.58400 1.000 74.55104  ? 69  GLU B OE1 1 
ATOM   2828 O OE2 . GLU B 2 70  ? 30.12100  -19.27000 -17.97400 1.000 75.56696  ? 69  GLU B OE2 1 
ATOM   2829 N N   . PHE B 2 71  ? 28.00400  -16.82200 -13.20000 1.000 55.14082  ? 70  PHE B N   1 
ATOM   2830 C CA  . PHE B 2 71  ? 28.42900  -16.64900 -11.79400 1.000 54.16439  ? 70  PHE B CA  1 
ATOM   2831 C C   . PHE B 2 71  ? 29.04300  -17.94500 -11.28200 1.000 55.21715  ? 70  PHE B C   1 
ATOM   2832 O O   . PHE B 2 71  ? 28.66100  -19.02200 -11.75900 1.000 55.65404  ? 70  PHE B O   1 
ATOM   2833 C CB  . PHE B 2 71  ? 27.24900  -16.23600 -10.91300 1.000 50.59291  ? 70  PHE B CB  1 
ATOM   2834 C CG  . PHE B 2 71  ? 26.39600  -17.34000 -10.35100 1.000 49.06378  ? 70  PHE B CG  1 
ATOM   2835 C CD1 . PHE B 2 71  ? 25.83300  -18.30200 -11.17200 1.000 49.07694  ? 70  PHE B CD1 1 
ATOM   2836 C CD2 . PHE B 2 71  ? 26.11800  -17.38300 -8.99600  1.000 47.63729  ? 70  PHE B CD2 1 
ATOM   2837 C CE1 . PHE B 2 71  ? 25.03700  -19.30200 -10.64200 1.000 47.72941  ? 70  PHE B CE1 1 
ATOM   2838 C CE2 . PHE B 2 71  ? 25.31500  -18.38000 -8.46900  1.000 46.37925  ? 70  PHE B CE2 1 
ATOM   2839 C CZ  . PHE B 2 71  ? 24.77900  -19.33800 -9.29300  1.000 46.64243  ? 70  PHE B CZ  1 
ATOM   2840 N N   . THR B 2 72  ? 30.00700  -17.82700 -10.37100 1.000 60.37829  ? 71  THR B N   1 
ATOM   2841 C CA  . THR B 2 72  ? 30.58400  -19.02500 -9.71800  1.000 60.63622  ? 71  THR B CA  1 
ATOM   2842 C C   . THR B 2 72  ? 30.12500  -18.97800 -8.26400  1.000 58.90180  ? 71  THR B C   1 
ATOM   2843 O O   . THR B 2 72  ? 30.66900  -18.17400 -7.50300  1.000 58.99655  ? 71  THR B O   1 
ATOM   2844 C CB  . THR B 2 72  ? 32.10600  -19.07100 -9.87000  1.000 63.79186  ? 71  THR B CB  1 
ATOM   2845 O OG1 . THR B 2 72  ? 32.41400  -19.00300 -11.26100 1.000 66.03160  ? 71  THR B OG1 1 
ATOM   2846 C CG2 . THR B 2 72  ? 32.70700  -20.32400 -9.27300  1.000 63.92872  ? 71  THR B CG2 1 
ATOM   2847 N N   . PRO B 2 73  ? 29.11700  -19.76800 -7.85900  1.000 55.75142  ? 72  PRO B N   1 
ATOM   2848 C CA  . PRO B 2 73  ? 28.58800  -19.67900 -6.49400  1.000 65.06833  ? 72  PRO B CA  1 
ATOM   2849 C C   . PRO B 2 73  ? 29.62200  -20.08600 -5.45400  1.000 70.43213  ? 72  PRO B C   1 
ATOM   2850 O O   . PRO B 2 73  ? 30.43900  -20.98400 -5.67300  1.000 69.23199  ? 72  PRO B O   1 
ATOM   2851 C CB  . PRO B 2 73  ? 27.39800  -20.64400 -6.51300  1.000 69.57150  ? 72  PRO B CB  1 
ATOM   2852 C CG  . PRO B 2 73  ? 27.73400  -21.62100 -7.58400  1.000 61.71793  ? 72  PRO B CG  1 
ATOM   2853 C CD  . PRO B 2 73  ? 28.48500  -20.85600 -8.62900  1.000 53.10110  ? 72  PRO B CD  1 
ATOM   2854 N N   . THR B 2 74  ? 29.59200  -19.39000 -4.32300  1.000 71.44278  ? 73  THR B N   1 
ATOM   2855 C CA  . THR B 2 74  ? 30.38500  -19.73200 -3.15300  1.000 74.91951  ? 73  THR B CA  1 
ATOM   2856 C C   . THR B 2 74  ? 29.45300  -19.79400 -1.95300  1.000 79.40952  ? 73  THR B C   1 
ATOM   2857 O O   . THR B 2 74  ? 28.31200  -19.32600 -2.00600  1.000 79.60428  ? 73  THR B O   1 
ATOM   2858 C CB  . THR B 2 74  ? 31.50200  -18.71200 -2.89000  1.000 69.52149  ? 73  THR B CB  1 
ATOM   2859 O OG1 . THR B 2 74  ? 30.93000  -17.50400 -2.37100  1.000 67.79497  ? 73  THR B OG1 1 
ATOM   2860 C CG2 . THR B 2 74  ? 32.26400  -18.39200 -4.17200  1.000 63.33128  ? 73  THR B CG2 1 
ATOM   2861 N N   . GLU B 2 75  ? 29.93900  -20.37000 -0.85200  1.000 78.56468  ? 74  GLU B N   1 
ATOM   2862 C CA  . GLU B 2 75  ? 29.10200  -20.38400 0.33900   1.000 81.99404  ? 74  GLU B CA  1 
ATOM   2863 C C   . GLU B 2 75  ? 29.06000  -19.01400 1.00100   1.000 79.93853  ? 74  GLU B C   1 
ATOM   2864 O O   . GLU B 2 75  ? 28.08200  -18.68200 1.67800   1.000 81.83350  ? 74  GLU B O   1 
ATOM   2865 C CB  . GLU B 2 75  ? 29.58300  -21.44400 1.32900   1.000 85.97873  ? 74  GLU B CB  1 
ATOM   2866 C CG  . GLU B 2 75  ? 28.49000  -21.84500 2.31100   1.000 90.57928  ? 74  GLU B CG  1 
ATOM   2867 C CD  . GLU B 2 75  ? 27.15300  -22.09600 1.60900   1.000 92.37950  ? 74  GLU B CD  1 
ATOM   2868 O OE1 . GLU B 2 75  ? 26.98200  -23.18600 1.01400   1.000 92.81902  ? 74  GLU B OE1 1 
ATOM   2869 O OE2 . GLU B 2 75  ? 26.28100  -21.19500 1.63800   1.000 91.89523  ? 74  GLU B OE2 1 
ATOM   2870 N N   . LYS B 2 76  ? 30.09700  -18.20000 0.80300   1.000 87.14992  ? 75  LYS B N   1 
ATOM   2871 C CA  . LYS B 2 76  ? 30.14600  -16.88400 1.42300   1.000 84.20746  ? 75  LYS B CA  1 
ATOM   2872 C C   . LYS B 2 76  ? 29.22200  -15.86700 0.75600   1.000 80.47544  ? 75  LYS B C   1 
ATOM   2873 O O   . LYS B 2 76  ? 28.88500  -14.85700 1.38700   1.000 80.36227  ? 75  LYS B O   1 
ATOM   2874 C CB  . LYS B 2 76  ? 31.58400  -16.36000 1.40800   1.000 83.59950  ? 75  LYS B CB  1 
ATOM   2875 N N   . ASP B 2 77  ? 28.79700  -16.10800 -0.48700  1.000 74.84582  ? 76  ASP B N   1 
ATOM   2876 C CA  . ASP B 2 77  ? 28.09600  -15.11000 -1.28700  1.000 69.27146  ? 76  ASP B CA  1 
ATOM   2877 C C   . ASP B 2 77  ? 26.59300  -15.36300 -1.32700  1.000 70.84270  ? 76  ASP B C   1 
ATOM   2878 O O   . ASP B 2 77  ? 26.13900  -16.50200 -1.46600  1.000 75.84594  ? 76  ASP B O   1 
ATOM   2879 C CB  . ASP B 2 77  ? 28.64600  -15.07200 -2.71300  1.000 64.15243  ? 76  ASP B CB  1 
ATOM   2880 C CG  . ASP B 2 77  ? 30.08300  -14.58100 -2.76800  1.000 63.62079  ? 76  ASP B CG  1 
ATOM   2881 O OD1 . ASP B 2 77  ? 30.41700  -13.61700 -2.04300  1.000 67.13173  ? 76  ASP B OD1 1 
ATOM   2882 O OD2 . ASP B 2 77  ? 30.88200  -15.16600 -3.53300  1.000 61.33104  ? 76  ASP B OD2 1 
ATOM   2883 N N   . GLU B 2 78  ? 25.83600  -14.27500 -1.21900  1.000 68.68718  ? 77  GLU B N   1 
ATOM   2884 C CA  . GLU B 2 78  ? 24.38200  -14.28000 -1.20200  1.000 69.04249  ? 77  GLU B CA  1 
ATOM   2885 C C   . GLU B 2 78  ? 23.87800  -13.56900 -2.45500  1.000 63.54709  ? 77  GLU B C   1 
ATOM   2886 O O   . GLU B 2 78  ? 24.27600  -12.43200 -2.72600  1.000 62.11534  ? 77  GLU B O   1 
ATOM   2887 C CB  . GLU B 2 78  ? 23.86600  -13.58600 0.06800   1.000 72.07706  ? 77  GLU B CB  1 
ATOM   2888 C CG  . GLU B 2 78  ? 24.46000  -14.12900 1.38600   1.000 77.47771  ? 77  GLU B CG  1 
ATOM   2889 C CD  . GLU B 2 78  ? 25.20800  -13.07600 2.22600   1.000 81.61768  ? 77  GLU B CD  1 
ATOM   2890 O OE1 . GLU B 2 78  ? 25.33300  -11.90700 1.79700   1.000 80.48333  ? 77  GLU B OE1 1 
ATOM   2891 O OE2 . GLU B 2 78  ? 25.67900  -13.41900 3.33600   1.000 86.09190  ? 77  GLU B OE2 1 
ATOM   2892 N N   . TYR B 2 79  ? 23.01100  -14.23400 -3.22100  1.000 48.25315  ? 78  TYR B N   1 
ATOM   2893 C CA  . TYR B 2 79  ? 22.49800  -13.69000 -4.47000  1.000 46.36345  ? 78  TYR B CA  1 
ATOM   2894 C C   . TYR B 2 79  ? 21.00300  -13.43100 -4.36000  1.000 46.07131  ? 78  TYR B C   1 
ATOM   2895 O O   . TYR B 2 79  ? 20.29200  -14.11900 -3.61700  1.000 44.82906  ? 78  TYR B O   1 
ATOM   2896 C CB  . TYR B 2 79  ? 22.78300  -14.63900 -5.64000  1.000 43.88947  ? 78  TYR B CB  1 
ATOM   2897 C CG  . TYR B 2 79  ? 24.25900  -14.72100 -5.96100  1.000 45.33965  ? 78  TYR B CG  1 
ATOM   2898 C CD1 . TYR B 2 79  ? 24.86000  -13.77500 -6.78000  1.000 46.44241  ? 78  TYR B CD1 1 
ATOM   2899 C CD2 . TYR B 2 79  ? 25.05900  -15.71700 -5.41500  1.000 46.45557  ? 78  TYR B CD2 1 
ATOM   2900 C CE1 . TYR B 2 79  ? 26.21200  -13.82600 -7.07000  1.000 48.10840  ? 78  TYR B CE1 1 
ATOM   2901 C CE2 . TYR B 2 79  ? 26.42700  -15.77300 -5.69300  1.000 48.41370  ? 78  TYR B CE2 1 
ATOM   2902 C CZ  . TYR B 2 79  ? 26.99300  -14.82200 -6.52900  1.000 49.40856  ? 78  TYR B CZ  1 
ATOM   2903 O OH  . TYR B 2 79  ? 28.34000  -14.85800 -6.82800  1.000 51.59566  ? 78  TYR B OH  1 
ATOM   2904 N N   . ALA B 2 80  ? 20.53100  -12.43300 -5.11100  1.000 45.91340  ? 79  ALA B N   1 
ATOM   2905 C CA  . ALA B 2 80  ? 19.10600  -12.13300 -5.14800  1.000 45.43176  ? 79  ALA B CA  1 
ATOM   2906 C C   . ALA B 2 80  ? 18.75900  -11.47300 -6.47700  1.000 44.42901  ? 79  ALA B C   1 
ATOM   2907 O O   . ALA B 2 80  ? 19.63700  -11.10700 -7.25900  1.000 44.62377  ? 79  ALA B O   1 
ATOM   2908 C CB  . ALA B 2 80  ? 18.69200  -11.24000 -3.97500  1.000 48.66636  ? 79  ALA B CB  1 
ATOM   2909 N N   . CYS B 2 81  ? 17.45700  -11.33100 -6.71700  1.000 52.62736  ? 80  CYS B N   1 
ATOM   2910 C CA  . CYS B 2 81  ? 16.93100  -10.54800 -7.82200  1.000 52.44576  ? 80  CYS B CA  1 
ATOM   2911 C C   . CYS B 2 81  ? 16.08600  -9.41500  -7.26200  1.000 55.46981  ? 80  CYS B C   1 
ATOM   2912 O O   . CYS B 2 81  ? 15.30700  -9.62200  -6.32700  1.000 55.78827  ? 80  CYS B O   1 
ATOM   2913 C CB  . CYS B 2 81  ? 16.09600  -11.41800 -8.76700  1.000 50.27971  ? 80  CYS B CB  1 
ATOM   2914 S SG  . CYS B 2 81  ? 15.34100  -10.56100 -10.12900 1.000 51.32457  ? 80  CYS B SG  1 
ATOM   2915 N N   . ARG B 2 82  ? 16.26100  -8.21500  -7.82400  1.000 50.89294  ? 81  ARG B N   1 
ATOM   2916 C CA  . ARG B 2 82  ? 15.54500  -7.01200  -7.40100  1.000 53.31955  ? 81  ARG B CA  1 
ATOM   2917 C C   . ARG B 2 82  ? 14.69200  -6.51000  -8.55700  1.000 53.46431  ? 81  ARG B C   1 
ATOM   2918 O O   . ARG B 2 82  ? 15.22000  -6.19200  -9.62500  1.000 52.83265  ? 81  ARG B O   1 
ATOM   2919 C CB  . ARG B 2 82  ? 16.51200  -5.91500  -6.94300  1.000 56.34360  ? 81  ARG B CB  1 
ATOM   2920 C CG  . ARG B 2 82  ? 15.82400  -4.60900  -6.54600  1.000 59.61241  ? 81  ARG B CG  1 
ATOM   2921 C CD  . ARG B 2 82  ? 16.81600  -3.60700  -5.96400  1.000 63.60236  ? 81  ARG B CD  1 
ATOM   2922 N NE  . ARG B 2 82  ? 17.83300  -3.24700  -6.94300  1.000 64.32350  ? 81  ARG B NE  1 
ATOM   2923 C CZ  . ARG B 2 82  ? 19.03500  -2.77900  -6.64100  1.000 66.56061  ? 81  ARG B CZ  1 
ATOM   2924 N NH1 . ARG B 2 82  ? 19.40700  -2.59100  -5.38800  1.000 69.12671  ? 81  ARG B NH1 1 
ATOM   2925 N NH2 . ARG B 2 82  ? 19.88700  -2.49900  -7.62200  1.000 66.64483  ? 81  ARG B NH2 1 
ATOM   2926 N N   . VAL B 2 83  ? 13.37900  -6.43100  -8.34100  1.000 46.63980  ? 82  VAL B N   1 
ATOM   2927 C CA  . VAL B 2 83  ? 12.42600  -6.09500  -9.39500  1.000 46.01341  ? 82  VAL B CA  1 
ATOM   2928 C C   . VAL B 2 83  ? 11.61500  -4.87500  -8.97200  1.000 49.71649  ? 82  VAL B C   1 
ATOM   2929 O O   . VAL B 2 83  ? 11.13400  -4.80800  -7.83700  1.000 49.77965  ? 82  VAL B O   1 
ATOM   2930 C CB  . VAL B 2 83  ? 11.48600  -7.27800  -9.70100  1.000 43.67103  ? 82  VAL B CB  1 
ATOM   2931 C CG1 . VAL B 2 83  ? 10.55400  -6.94100  -10.85700 1.000 42.44983  ? 82  VAL B CG1 1 
ATOM   2932 C CG2 . VAL B 2 83  ? 12.28900  -8.55000  -10.01200 1.000 40.41537  ? 82  VAL B CG2 1 
ATOM   2933 N N   . ASN B 2 84  ? 11.44600  -3.92200  -9.89200  1.000 53.78013  ? 83  ASN B N   1 
ATOM   2934 C CA  . ASN B 2 84  ? 10.54400  -2.79700  -9.68500  1.000 57.02263  ? 83  ASN B CA  1 
ATOM   2935 C C   . ASN B 2 84  ? 9.65900   -2.63300  -10.91600 1.000 57.37530  ? 83  ASN B C   1 
ATOM   2936 O O   . ASN B 2 84  ? 10.08000  -2.88900  -12.04700 1.000 56.09357  ? 83  ASN B O   1 
ATOM   2937 C CB  . ASN B 2 84  ? 11.31600  -1.50100  -9.37900  1.000 58.88338  ? 83  ASN B CB  1 
ATOM   2938 C CG  . ASN B 2 84  ? 10.44700  -0.42600  -8.70900  1.000 61.75740  ? 83  ASN B CG  1 
ATOM   2939 O OD1 . ASN B 2 84  ? 9.27700   -0.64300  -8.39200  1.000 61.24945  ? 83  ASN B OD1 1 
ATOM   2940 N ND2 . ASN B 2 84  ? 11.03600  0.74200   -8.49200  1.000 65.06570  ? 83  ASN B ND2 1 
ATOM   2941 N N   . HIS B 2 85  ? 8.42700   -2.19200  -10.67500 1.000 53.41167  ? 84  HIS B N   1 
ATOM   2942 C CA  . HIS B 2 85  ? 7.34600   -2.19300  -11.65100 1.000 52.93529  ? 84  HIS B CA  1 
ATOM   2943 C C   . HIS B 2 85  ? 6.28700   -1.21800  -11.14300 1.000 56.13568  ? 84  HIS B C   1 
ATOM   2944 O O   . HIS B 2 85  ? 6.18000   -0.99100  -9.93000  1.000 56.35149  ? 84  HIS B O   1 
ATOM   2945 C CB  . HIS B 2 85  ? 6.78900   -3.61700  -11.80500 1.000 47.64255  ? 84  HIS B CB  1 
ATOM   2946 C CG  . HIS B 2 85  ? 5.84400   -3.79400  -12.94600 1.000 45.74759  ? 84  HIS B CG  1 
ATOM   2947 N ND1 . HIS B 2 85  ? 4.48100   -3.89300  -12.77400 1.000 44.56850  ? 84  HIS B ND1 1 
ATOM   2948 C CD2 . HIS B 2 85  ? 6.06600   -3.91500  -14.27600 1.000 44.07371  ? 84  HIS B CD2 1 
ATOM   2949 C CE1 . HIS B 2 85  ? 3.90300   -4.06200  -13.95100 1.000 42.13400  ? 84  HIS B CE1 1 
ATOM   2950 N NE2 . HIS B 2 85  ? 4.84400   -4.07500  -14.87700 1.000 41.74448  ? 84  HIS B NE2 1 
ATOM   2951 N N   . VAL B 2 86  ? 5.50400   -0.64100  -12.06300 1.000 58.08328  ? 85  VAL B N   1 
ATOM   2952 C CA  . VAL B 2 86  ? 4.49700   0.33400   -11.63200 1.000 60.14669  ? 85  VAL B CA  1 
ATOM   2953 C C   . VAL B 2 86  ? 3.54600   -0.25200  -10.59900 1.000 58.35437  ? 85  VAL B C   1 
ATOM   2954 O O   . VAL B 2 86  ? 3.05300   0.46500   -9.72200  1.000 59.62294  ? 85  VAL B O   1 
ATOM   2955 C CB  . VAL B 2 86  ? 3.70500   0.88700   -12.82800 1.000 61.15207  ? 85  VAL B CB  1 
ATOM   2956 C CG1 . VAL B 2 86  ? 4.62500   1.65800   -13.75000 1.000 62.20746  ? 85  VAL B CG1 1 
ATOM   2957 C CG2 . VAL B 2 86  ? 2.97100   -0.22300  -13.53500 1.000 57.83325  ? 85  VAL B CG2 1 
ATOM   2958 N N   . THR B 2 87  ? 3.26000   -1.55200  -10.68400 1.000 61.27050  ? 86  THR B N   1 
ATOM   2959 C CA  . THR B 2 87  ? 2.37400   -2.17200  -9.70800  1.000 58.12539  ? 86  THR B CA  1 
ATOM   2960 C C   . THR B 2 87  ? 3.01600   -2.32200  -8.33400  1.000 59.47029  ? 86  THR B C   1 
ATOM   2961 O O   . THR B 2 87  ? 2.33600   -2.77400  -7.40400  1.000 59.98614  ? 86  THR B O   1 
ATOM   2962 C CB  . THR B 2 87  ? 1.91300   -3.54200  -10.21000 1.000 52.81160  ? 86  THR B CB  1 
ATOM   2963 O OG1 . THR B 2 87  ? 3.05200   -4.38800  -10.37900 1.000 50.85347  ? 86  THR B OG1 1 
ATOM   2964 C CG2 . THR B 2 87  ? 1.18800   -3.39900  -11.54500 1.000 51.99571  ? 86  THR B CG2 1 
ATOM   2965 N N   . LEU B 2 88  ? 4.28500   -1.95200  -8.16900  1.000 57.88326  ? 87  LEU B N   1 
ATOM   2966 C CA  . LEU B 2 88  ? 5.00300   -2.14000  -6.91400  1.000 58.58597  ? 87  LEU B CA  1 
ATOM   2967 C C   . LEU B 2 88  ? 5.36200   -0.77900  -6.34600  1.000 63.85766  ? 87  LEU B C   1 
ATOM   2968 O O   . LEU B 2 88  ? 6.02700   0.02000   -7.01900  1.000 65.95791  ? 87  LEU B O   1 
ATOM   2969 C CB  . LEU B 2 88  ? 6.26300   -2.98200  -7.12500  1.000 56.13568  ? 87  LEU B CB  1 
ATOM   2970 C CG  . LEU B 2 88  ? 6.02600   -4.47100  -7.39600  1.000 52.46155  ? 87  LEU B CG  1 
ATOM   2971 C CD1 . LEU B 2 88  ? 7.22000   -5.13100  -8.09900  1.000 50.19023  ? 87  LEU B CD1 1 
ATOM   2972 C CD2 . LEU B 2 88  ? 5.69400   -5.20000  -6.09000  1.000 52.40892  ? 87  LEU B CD2 1 
ATOM   2973 N N   . SER B 2 89  ? 4.91100   -0.50900  -5.11500  1.000 65.92106  ? 88  SER B N   1 
ATOM   2974 C CA  . SER B 2 89  ? 5.32100   0.72000   -4.44400  1.000 70.56636  ? 88  SER B CA  1 
ATOM   2975 C C   . SER B 2 89  ? 6.81900   0.72200   -4.17700  1.000 69.93207  ? 88  SER B C   1 
ATOM   2976 O O   . SER B 2 89  ? 7.46300   1.77500   -4.22900  1.000 72.20339  ? 88  SER B O   1 
ATOM   2977 C CB  . SER B 2 89  ? 4.54800   0.90200   -3.13200  1.000 73.30089  ? 88  SER B CB  1 
ATOM   2978 N N   . GLN B 2 90  ? 7.39400   -0.44400  -3.91200  1.000 68.79772  ? 89  GLN B N   1 
ATOM   2979 C CA  . GLN B 2 90  ? 8.78800   -0.52700  -3.52000  1.000 69.68204  ? 89  GLN B CA  1 
ATOM   2980 C C   . GLN B 2 90  ? 9.42800   -1.71800  -4.21200  1.000 65.30783  ? 89  GLN B C   1 
ATOM   2981 O O   . GLN B 2 90  ? 8.74000   -2.69400  -4.53100  1.000 62.20483  ? 89  GLN B O   1 
ATOM   2982 C CB  . GLN B 2 90  ? 8.92500   -0.66100  -1.99700  1.000 71.77966  ? 89  GLN B CB  1 
ATOM   2983 C CG  . GLN B 2 90  ? 8.44500   0.56700   -1.22500  1.000 77.24874  ? 89  GLN B CG  1 
ATOM   2984 C CD  . GLN B 2 90  ? 9.32900   1.79900   -1.42700  1.000 80.62019  ? 89  GLN B CD  1 
ATOM   2985 O OE1 . GLN B 2 90  ? 10.43300  1.71400   -1.96800  1.000 78.65680  ? 89  GLN B OE1 1 
ATOM   2986 N NE2 . GLN B 2 90  ? 8.84300   2.94900   -0.97200  1.000 84.39696  ? 89  GLN B NE2 1 
ATOM   2987 N N   . PRO B 2 91  ? 10.73500  -1.66100  -4.46200  1.000 60.45198  ? 90  PRO B N   1 
ATOM   2988 C CA  . PRO B 2 91  ? 11.39800  -2.76700  -5.16400  1.000 56.53309  ? 90  PRO B CA  1 
ATOM   2989 C C   . PRO B 2 91  ? 11.29700  -4.07300  -4.37500  1.000 54.85921  ? 90  PRO B C   1 
ATOM   2990 O O   . PRO B 2 91  ? 11.46400  -4.09600  -3.15600  1.000 57.16738  ? 90  PRO B O   1 
ATOM   2991 C CB  . PRO B 2 91  ? 12.85000  -2.28600  -5.28100  1.000 57.98327  ? 90  PRO B CB  1 
ATOM   2992 C CG  . PRO B 2 91  ? 12.79100  -0.80800  -5.11100  1.000 62.02323  ? 90  PRO B CG  1 
ATOM   2993 C CD  . PRO B 2 91  ? 11.66100  -0.55600  -4.16600  1.000 64.10242  ? 90  PRO B CD  1 
ATOM   2994 N N   . LYS B 2 92  ? 11.03400  -5.16800  -5.08800  1.000 53.16427  ? 91  LYS B N   1 
ATOM   2995 C CA  . LYS B 2 92  ? 10.85100  -6.48300  -4.47600  1.000 51.00612  ? 91  LYS B CA  1 
ATOM   2996 C C   . LYS B 2 92  ? 12.09800  -7.34200  -4.67800  1.000 49.71649  ? 91  LYS B C   1 
ATOM   2997 O O   . LYS B 2 92  ? 12.52100  -7.56600  -5.81600  1.000 49.45856  ? 91  LYS B O   1 
ATOM   2998 C CB  . LYS B 2 92  ? 9.62000   -7.17800  -5.05800  1.000 50.21392  ? 91  LYS B CB  1 
ATOM   2999 C CG  . LYS B 2 92  ? 9.25600   -8.47000  -4.34000  1.000 50.34025  ? 91  LYS B CG  1 
ATOM   3000 C CD  . LYS B 2 92  ? 7.98100   -9.08000  -4.87800  1.000 53.46431  ? 91  LYS B CD  1 
ATOM   3001 C CE  . LYS B 2 92  ? 7.71000   -10.43200 -4.19100  1.000 57.00947  ? 91  LYS B CE  1 
ATOM   3002 N NZ  . LYS B 2 92  ? 6.63100   -11.21200 -4.86200  1.000 62.19693  ? 91  LYS B NZ  1 
ATOM   3003 N N   . ILE B 2 93  ? 12.68000  -7.81900  -3.57700  1.000 53.83803  ? 92  ILE B N   1 
ATOM   3004 C CA  . ILE B 2 93  ? 13.90500  -8.61700  -3.59100  1.000 52.99056  ? 92  ILE B CA  1 
ATOM   3005 C C   . ILE B 2 93  ? 13.55600  -10.07800 -3.32400  1.000 52.28258  ? 92  ILE B C   1 
ATOM   3006 O O   . ILE B 2 93  ? 12.91800  -10.39500 -2.31300  1.000 52.48787  ? 92  ILE B O   1 
ATOM   3007 C CB  . ILE B 2 93  ? 14.91800  -8.12100  -2.54400  1.000 56.87787  ? 92  ILE B CB  1 
ATOM   3008 C CG1 . ILE B 2 93  ? 15.17000  -6.61800  -2.67300  1.000 59.50187  ? 92  ILE B CG1 1 
ATOM   3009 C CG2 . ILE B 2 93  ? 16.21100  -8.93100  -2.64600  1.000 57.05421  ? 92  ILE B CG2 1 
ATOM   3010 C CD1 . ILE B 2 93  ? 16.49200  -6.27400  -3.33200  1.000 61.98638  ? 92  ILE B CD1 1 
ATOM   3011 N N   . VAL B 2 94  ? 13.98800  -10.96900 -4.21700  1.000 45.25279  ? 93  VAL B N   1 
ATOM   3012 C CA  . VAL B 2 94  ? 13.84200  -12.40600 -4.01900  1.000 45.99762  ? 93  VAL B CA  1 
ATOM   3013 C C   . VAL B 2 94  ? 15.22800  -13.02400 -3.90800  1.000 46.14237  ? 93  VAL B C   1 
ATOM   3014 O O   . VAL B 2 94  ? 16.04000  -12.93300 -4.84000  1.000 45.43966  ? 93  VAL B O   1 
ATOM   3015 C CB  . VAL B 2 94  ? 13.03700  -13.07000 -5.14200  1.000 46.17922  ? 93  VAL B CB  1 
ATOM   3016 C CG1 . VAL B 2 94  ? 12.94100  -14.55400 -4.88000  1.000 49.52436  ? 93  VAL B CG1 1 
ATOM   3017 C CG2 . VAL B 2 94  ? 11.65500  -12.47300 -5.21200  1.000 47.18987  ? 93  VAL B CG2 1 
ATOM   3018 N N   . LYS B 2 95  ? 15.48700  -13.65800 -2.77700  1.000 48.89797  ? 94  LYS B N   1 
ATOM   3019 C CA  . LYS B 2 95  ? 16.77700  -14.27000 -2.52800  1.000 49.69806  ? 94  LYS B CA  1 
ATOM   3020 C C   . LYS B 2 95  ? 16.89500  -15.58400 -3.27800  1.000 51.14561  ? 94  LYS B C   1 
ATOM   3021 O O   . LYS B 2 95  ? 15.91400  -16.31700 -3.44400  1.000 53.80908  ? 94  LYS B O   1 
ATOM   3022 C CB  . LYS B 2 95  ? 16.97500  -14.50000 -1.03000  1.000 52.40892  ? 94  LYS B CB  1 
ATOM   3023 C CG  . LYS B 2 95  ? 17.64100  -13.33200 -0.31300  1.000 54.20124  ? 94  LYS B CG  1 
ATOM   3024 C CD  . LYS B 2 95  ? 19.12500  -13.23900 -0.68800  1.000 56.45940  ? 94  LYS B CD  1 
ATOM   3025 C CE  . LYS B 2 95  ? 19.88800  -12.28700 0.22900   1.000 61.39420  ? 94  LYS B CE  1 
ATOM   3026 N NZ  . LYS B 2 95  ? 19.81000  -10.84000 -0.18600  1.000 60.88625  ? 94  LYS B NZ  1 
ATOM   3027 N N   . TRP B 2 96  ? 18.10500  -15.87800 -3.73600  1.000 45.64758  ? 95  TRP B N   1 
ATOM   3028 C CA  . TRP B 2 96  ? 18.35700  -17.16400 -4.36800  1.000 45.62652  ? 95  TRP B CA  1 
ATOM   3029 C C   . TRP B 2 96  ? 18.50800  -18.20600 -3.26900  1.000 48.07682  ? 95  TRP B C   1 
ATOM   3030 O O   . TRP B 2 96  ? 19.39800  -18.09800 -2.41800  1.000 50.47184  ? 95  TRP B O   1 
ATOM   3031 C CB  . TRP B 2 96  ? 19.59900  -17.11600 -5.25000  1.000 46.08447  ? 95  TRP B CB  1 
ATOM   3032 C CG  . TRP B 2 96  ? 19.95500  -18.43300 -5.83900  1.000 46.68718  ? 95  TRP B CG  1 
ATOM   3033 C CD1 . TRP B 2 96  ? 19.12500  -19.28600 -6.51700  1.000 46.50558  ? 95  TRP B CD1 1 
ATOM   3034 C CD2 . TRP B 2 96  ? 21.24100  -19.06000 -5.82300  1.000 48.96903  ? 95  TRP B CD2 1 
ATOM   3035 N NE1 . TRP B 2 96  ? 19.81300  -20.40900 -6.90300  1.000 50.68502  ? 95  TRP B NE1 1 
ATOM   3036 C CE2 . TRP B 2 96  ? 21.11500  -20.29300 -6.49900  1.000 50.87452  ? 95  TRP B CE2 1 
ATOM   3037 C CE3 . TRP B 2 96  ? 22.48500  -18.70000 -5.29900  1.000 51.54302  ? 95  TRP B CE3 1 
ATOM   3038 C CZ2 . TRP B 2 96  ? 22.18300  -21.16400 -6.66600  1.000 55.69615  ? 95  TRP B CZ2 1 
ATOM   3039 C CZ3 . TRP B 2 96  ? 23.54700  -19.57400 -5.46000  1.000 54.06438  ? 95  TRP B CZ3 1 
ATOM   3040 C CH2 . TRP B 2 96  ? 23.39000  -20.78900 -6.13800  1.000 56.08304  ? 95  TRP B CH2 1 
ATOM   3041 N N   . ASP B 2 97  ? 17.62100  -19.19500 -3.27500  1.000 48.42949  ? 96  ASP B N   1 
ATOM   3042 C CA  . ASP B 2 97  ? 17.65000  -20.30400 -2.32800  1.000 52.59052  ? 96  ASP B CA  1 
ATOM   3043 C C   . ASP B 2 97  ? 18.21400  -21.53000 -3.03200  1.000 57.32529  ? 96  ASP B C   1 
ATOM   3044 O O   . ASP B 2 97  ? 17.51300  -22.19100 -3.80400  1.000 61.30209  ? 96  ASP B O   1 
ATOM   3045 C CB  . ASP B 2 97  ? 16.25500  -20.59100 -1.78900  1.000 56.65942  ? 96  ASP B CB  1 
ATOM   3046 C CG  . ASP B 2 97  ? 16.26500  -21.56700 -0.62900  1.000 60.29407  ? 96  ASP B CG  1 
ATOM   3047 O OD1 . ASP B 2 97  ? 17.15600  -22.45000 -0.56800  1.000 61.92321  ? 96  ASP B OD1 1 
ATOM   3048 O OD2 . ASP B 2 97  ? 15.36700  -21.44300 0.23200   1.000 59.85718  ? 96  ASP B OD2 1 
ATOM   3049 N N   . ARG B 2 98  ? 19.45300  -21.86300 -2.70600  1.000 84.01270  ? 97  ARG B N   1 
ATOM   3050 C CA  . ARG B 2 98  ? 20.14200  -23.02700 -3.31000  1.000 89.11595  ? 97  ARG B CA  1 
ATOM   3051 C C   . ARG B 2 98  ? 19.39700  -24.31800 -2.93700  1.000 95.05877  ? 97  ARG B C   1 
ATOM   3052 O O   . ARG B 2 98  ? 19.08500  -25.08400 -3.86600  1.000 98.82501  ? 97  ARG B O   1 
ATOM   3053 C CB  . ARG B 2 98  ? 21.60500  -22.98500 -2.84700  1.000 88.06582  ? 97  ARG B CB  1 
ATOM   3054 C CG  . ARG B 2 98  ? 22.22200  -21.59800 -2.93900  1.000 82.51516  ? 97  ARG B CG  1 
ATOM   3055 C CD  . ARG B 2 98  ? 23.65700  -21.54000 -2.46400  1.000 83.92059  ? 97  ARG B CD  1 
ATOM   3056 N NE  . ARG B 2 98  ? 24.41800  -22.69200 -2.91200  1.000 88.05003  ? 97  ARG B NE  1 
ATOM   3057 C CZ  . ARG B 2 98  ? 25.71900  -22.67900 -3.15900  1.000 89.93447  ? 97  ARG B CZ  1 
ATOM   3058 N NH1 . ARG B 2 98  ? 26.41400  -21.56700 -3.00600  1.000 88.98172  ? 97  ARG B NH1 1 
ATOM   3059 N NH2 . ARG B 2 98  ? 26.32100  -23.78100 -3.56300  1.000 93.08748  ? 97  ARG B NH2 1 
ATOM   3060 N N   . ASP B 2 99  ? 19.05800  -24.51300 -1.66100  1.000 98.17230  ? 98  ASP B N   1 
ATOM   3061 C CA  . ASP B 2 99  ? 18.26300  -25.68900 -1.21800  1.000 102.46755 ? 98  ASP B CA  1 
ATOM   3062 C C   . ASP B 2 99  ? 17.02700  -25.90200 -2.10300  1.000 102.80970 ? 98  ASP B C   1 
ATOM   3063 O O   . ASP B 2 99  ? 16.74000  -27.07400 -2.39000  1.000 103.65717 ? 98  ASP B O   1 
ATOM   3064 C CB  . ASP B 2 99  ? 17.79800  -25.53300 0.23000   1.000 103.06762 ? 98  ASP B CB  1 
ATOM   3065 C CG  . ASP B 2 99  ? 18.80800  -24.84100 1.12900   1.000 100.02252 ? 98  ASP B CG  1 
ATOM   3066 O OD1 . ASP B 2 99  ? 19.96400  -25.30200 1.18000   1.000 98.10650  ? 98  ASP B OD1 1 
ATOM   3067 O OD2 . ASP B 2 99  ? 18.42900  -23.84800 1.77200   1.000 99.11452  ? 98  ASP B OD2 1 
ATOM   3068 N N   . MET B 2 100 ? 16.33900  -24.83200 -2.52200  1.000 115.17170 ? 99  MET B N   1 
ATOM   3069 C CA  . MET B 2 100 ? 15.07800  -24.95100 -3.31600  1.000 114.54794 ? 99  MET B CA  1 
ATOM   3070 C C   . MET B 2 100 ? 14.22900  -23.67500 -3.20800  1.000 113.98735 ? 99  MET B C   1 
ATOM   3071 O O   . MET B 2 100 ? 13.33400  -23.48400 -4.05700  1.000 112.16871 ? 99  MET B O   1 
ATOM   3072 C CB  . MET B 2 100 ? 14.25000  -26.12200 -2.79900  1.000 112.12923 ? 99  MET B CB  1 
ATOM   3073 N N   . ALA C 3 1   ? 8.78700   -17.19100 -41.54600 1.000 33.91986  ? 1   ALA C N   1 
ATOM   3074 C CA  . ALA C 3 1   ? 8.88500   -15.82900 -42.07000 1.000 39.21523  ? 1   ALA C CA  1 
ATOM   3075 C C   . ALA C 3 1   ? 7.62800   -15.01100 -41.74500 1.000 39.03100  ? 1   ALA C C   1 
ATOM   3076 O O   . ALA C 3 1   ? 6.52000   -15.52500 -41.76500 1.000 34.92261  ? 1   ALA C O   1 
ATOM   3077 C CB  . ALA C 3 1   ? 9.12700   -15.85800 -43.57200 1.000 42.81566  ? 1   ALA C CB  1 
ATOM   3078 N N   . SER C 3 2   ? 7.82000   -13.72800 -41.47400 1.000 33.14871  ? 2   SER C N   1 
ATOM   3079 C CA  . SER C 3 2   ? 6.76000   -12.89600 -40.93400 1.000 32.49863  ? 2   SER C CA  1 
ATOM   3080 C C   . SER C 3 2   ? 5.70800   -12.56000 -41.99100 1.000 33.60666  ? 2   SER C C   1 
ATOM   3081 O O   . SER C 3 2   ? 5.93400   -12.66500 -43.19700 1.000 35.88588  ? 2   SER C O   1 
ATOM   3082 C CB  . SER C 3 2   ? 7.35200   -11.61100 -40.35500 1.000 36.29646  ? 2   SER C CB  1 
ATOM   3083 O OG  . SER C 3 2   ? 8.10900   -10.89700 -41.32300 1.000 43.12622  ? 2   SER C OG  1 
ATOM   3084 N N   . LEU C 3 3   ? 4.54800   -12.12500 -41.50400 1.000 35.54110  ? 3   LEU C N   1 
ATOM   3085 C CA  . LEU C 3 3   ? 3.43000   -11.71800 -42.34000 1.000 35.90430  ? 3   LEU C CA  1 
ATOM   3086 C C   . LEU C 3 3   ? 3.63100   -10.28800 -42.83600 1.000 43.26571  ? 3   LEU C C   1 
ATOM   3087 O O   . LEU C 3 3   ? 3.89900   -9.37600  -42.04700 1.000 47.06617  ? 3   LEU C O   1 
ATOM   3088 C CB  . LEU C 3 3   ? 2.14200   -11.81700 -41.53500 1.000 32.39073  ? 3   LEU C CB  1 
ATOM   3089 C CG  . LEU C 3 3   ? 0.89500   -11.12800 -42.07100 1.000 33.38295  ? 3   LEU C CG  1 
ATOM   3090 C CD1 . LEU C 3 3   ? 0.18400   -11.94800 -43.08400 1.000 33.26188  ? 3   LEU C CD1 1 
ATOM   3091 C CD2 . LEU C 3 3   ? -0.02600  -10.81900 -40.86900 1.000 31.87751  ? 3   LEU C CD2 1 
ATOM   3092 N N   . ASN C 3 4   ? 3.49000   -10.09200 -44.13700 1.000 50.27708  ? 4   ASN C N   1 
ATOM   3093 C CA  . ASN C 3 4   ? 3.64900   -8.77600  -44.74900 1.000 54.67761  ? 4   ASN C CA  1 
ATOM   3094 C C   . ASN C 3 4   ? 2.25900   -8.19300  -44.99100 1.000 53.65643  ? 4   ASN C C   1 
ATOM   3095 O O   . ASN C 3 4   ? 1.57200   -8.57500  -45.94000 1.000 51.65093  ? 4   ASN C O   1 
ATOM   3096 C CB  . ASN C 3 4   ? 4.46200   -8.88000  -46.03500 1.000 55.74353  ? 4   ASN C CB  1 
ATOM   3097 C CG  . ASN C 3 4   ? 4.51600   -7.57100  -46.79100 1.000 58.04380  ? 4   ASN C CG  1 
ATOM   3098 O OD1 . ASN C 3 4   ? 5.11500   -6.59500  -46.32900 1.000 58.97812  ? 4   ASN C OD1 1 
ATOM   3099 N ND2 . ASN C 3 4   ? 3.88600   -7.54000  -47.96500 1.000 58.47806  ? 4   ASN C ND2 1 
ATOM   3100 N N   . LEU C 3 5   ? 1.83600   -7.26900  -44.12600 1.000 61.88900  ? 5   LEU C N   1 
ATOM   3101 C CA  . LEU C 3 5   ? 0.47700   -6.74600  -44.23200 1.000 61.49685  ? 5   LEU C CA  1 
ATOM   3102 C C   . LEU C 3 5   ? 0.49200   -5.34700  -44.82500 1.000 64.83672  ? 5   LEU C C   1 
ATOM   3103 O O   . LEU C 3 5   ? 0.72900   -4.36500  -44.10200 1.000 65.09991  ? 5   LEU C O   1 
ATOM   3104 C CB  . LEU C 3 5   ? -0.21400  -6.74600  -42.86900 1.000 58.79652  ? 5   LEU C CB  1 
ATOM   3105 C CG  . LEU C 3 5   ? -1.65600  -7.26600  -42.90200 1.000 55.68562  ? 5   LEU C CG  1 
ATOM   3106 C CD1 . LEU C 3 5   ? -1.87900  -8.34700  -43.96700 1.000 52.91687  ? 5   LEU C CD1 1 
ATOM   3107 C CD2 . LEU C 3 5   ? -2.03200  -7.79400  -41.54400 1.000 50.90347  ? 5   LEU C CD2 1 
ATOM   3108 N N   . PRO C 3 6   ? 0.22300   -5.19800  -46.12400 1.000 100.92789 ? 6   PRO C N   1 
ATOM   3109 C CA  . PRO C 3 6   ? 0.32300   -3.88100  -46.76200 1.000 102.10172 ? 6   PRO C CA  1 
ATOM   3110 C C   . PRO C 3 6   ? -0.79200  -2.96700  -46.28200 1.000 101.82273 ? 6   PRO C C   1 
ATOM   3111 O O   . PRO C 3 6   ? -1.97500  -3.26000  -46.47500 1.000 100.57785 ? 6   PRO C O   1 
ATOM   3112 C CB  . PRO C 3 6   ? 0.18500   -4.19500  -48.25900 1.000 101.34373 ? 6   PRO C CB  1 
ATOM   3113 C CG  . PRO C 3 6   ? 0.18000   -5.69600  -48.37700 1.000 98.64867  ? 6   PRO C CG  1 
ATOM   3114 C CD  . PRO C 3 6   ? -0.28500  -6.21200  -47.05900 1.000 98.13545  ? 6   PRO C CD  1 
ATOM   3115 N N   . ALA C 3 7   ? -0.40400  -1.87100  -45.63000 1.000 57.89642  ? 7   ALA C N   1 
ATOM   3116 C CA  . ALA C 3 7   ? -1.24100  -0.68300  -45.50000 1.000 58.44122  ? 7   ALA C CA  1 
ATOM   3117 C C   . ALA C 3 7   ? -2.46200  -0.88500  -44.60600 1.000 56.43308  ? 7   ALA C C   1 
ATOM   3118 O O   . ALA C 3 7   ? -3.43200  -0.12800  -44.71700 1.000 56.50678  ? 7   ALA C O   1 
ATOM   3119 C CB  . ALA C 3 7   ? -1.69000  -0.19800  -46.87900 1.000 58.14908  ? 7   ALA C CB  1 
ATOM   3120 N N   . VAL C 3 8   ? -2.43900  -1.87600  -43.71800 1.000 49.12957  ? 8   VAL C N   1 
ATOM   3121 C CA  . VAL C 3 8   ? -3.59600  -2.21000  -42.88600 1.000 47.12407  ? 8   VAL C CA  1 
ATOM   3122 C C   . VAL C 3 8   ? -3.60400  -1.34200  -41.63200 1.000 46.74245  ? 8   VAL C C   1 
ATOM   3123 O O   . VAL C 3 8   ? -2.63200  -1.32700  -40.87000 1.000 46.00025  ? 8   VAL C O   1 
ATOM   3124 C CB  . VAL C 3 8   ? -3.59400  -3.70300  -42.50900 1.000 44.75800  ? 8   VAL C CB  1 
ATOM   3125 C CG1 . VAL C 3 8   ? -4.69500  -3.98600  -41.50800 1.000 41.72079  ? 8   VAL C CG1 1 
ATOM   3126 C CG2 . VAL C 3 8   ? -3.79500  -4.56600  -43.75400 1.000 43.88947  ? 8   VAL C CG2 1 
ATOM   3127 N N   . SER C 3 9   ? -4.71100  -0.64300  -41.39700 1.000 41.86291  ? 9   SER C N   1 
ATOM   3128 C CA  . SER C 3 9   ? -4.87400  0.19700   -40.22100 1.000 41.08651  ? 9   SER C CA  1 
ATOM   3129 C C   . SER C 3 9   ? -5.95200  -0.35200  -39.30200 1.000 39.54158  ? 9   SER C C   1 
ATOM   3130 O O   . SER C 3 9   ? -6.91700  -0.95900  -39.76000 1.000 39.22576  ? 9   SER C O   1 
ATOM   3131 C CB  . SER C 3 9   ? -5.28200  1.61100   -40.60300 1.000 42.09189  ? 9   SER C CB  1 
ATOM   3132 O OG  . SER C 3 9   ? -6.57700  1.59400   -41.14500 1.000 42.43667  ? 9   SER C OG  1 
ATOM   3133 N N   . TRP C 3 10  ? -5.82100  -0.05500  -38.01200 1.000 48.27158  ? 10  TRP C N   1 
ATOM   3134 C CA  . TRP C 3 10  ? -6.91600  -0.27700  -37.06200 1.000 45.11594  ? 10  TRP C CA  1 
ATOM   3135 C C   . TRP C 3 10  ? -8.04000  0.69500   -37.33500 1.000 46.87404  ? 10  TRP C C   1 
ATOM   3136 O O   . TRP C 3 10  ? -7.83300  1.63900   -38.08900 1.000 49.23485  ? 10  TRP C O   1 
ATOM   3137 C CB  . TRP C 3 10  ? -6.45900  -0.11600  -35.62000 1.000 40.84174  ? 10  TRP C CB  1 
ATOM   3138 C CG  . TRP C 3 10  ? -5.70200  -1.25800  -35.13000 1.000 39.51263  ? 10  TRP C CG  1 
ATOM   3139 C CD1 . TRP C 3 10  ? -4.99600  -2.15200  -35.87500 1.000 40.54960  ? 10  TRP C CD1 1 
ATOM   3140 C CD2 . TRP C 3 10  ? -5.56800  -1.66400  -33.76700 1.000 37.58345  ? 10  TRP C CD2 1 
ATOM   3141 N NE1 . TRP C 3 10  ? -4.41400  -3.09300  -35.05600 1.000 38.62042  ? 10  TRP C NE1 1 
ATOM   3142 C CE2 . TRP C 3 10  ? -4.74400  -2.81300  -33.75300 1.000 37.42817  ? 10  TRP C CE2 1 
ATOM   3143 C CE3 . TRP C 3 10  ? -6.06300  -1.17300  -32.55400 1.000 37.08603  ? 10  TRP C CE3 1 
ATOM   3144 C CZ2 . TRP C 3 10  ? -4.41600  -3.48600  -32.57400 1.000 36.98865  ? 10  TRP C CZ2 1 
ATOM   3145 C CZ3 . TRP C 3 10  ? -5.72600  -1.85000  -31.37100 1.000 37.44660  ? 10  TRP C CZ3 1 
ATOM   3146 C CH2 . TRP C 3 10  ? -4.91300  -2.98300  -31.39700 1.000 37.77821  ? 10  TRP C CH2 1 
ATOM   3147 O OXT . TRP C 3 10  ? -9.15300  0.55700   -36.81600 1.000 43.81315  ? 10  TRP C OXT 1 
ATOM   3148 N N   . ASP D 4 6   ? 24.66700  6.21500   -21.28300 1.000 56.49362  ? 6   ASP G N   1 
ATOM   3149 C CA  . ASP D 4 6   ? 24.20700  7.09100   -20.20000 1.000 64.94726  ? 6   ASP G CA  1 
ATOM   3150 C C   . ASP D 4 6   ? 23.63500  8.39200   -20.76200 1.000 66.66062  ? 6   ASP G C   1 
ATOM   3151 O O   . ASP D 4 6   ? 24.05800  9.49000   -20.38300 1.000 61.61528  ? 6   ASP G O   1 
ATOM   3152 C CB  . ASP D 4 6   ? 25.34500  7.40500   -19.22200 1.000 65.20782  ? 6   ASP G CB  1 
ATOM   3153 C CG  . ASP D 4 6   ? 24.83700  7.85500   -17.86200 1.000 57.91484  ? 6   ASP G CG  1 
ATOM   3154 O OD1 . ASP D 4 6   ? 24.17000  7.05300   -17.17800 1.000 72.96401  ? 6   ASP G OD1 1 
ATOM   3155 O OD2 . ASP D 4 6   ? 25.10800  9.00300   -17.47300 1.000 69.70573  ? 6   ASP G OD2 1 
ATOM   3156 N N   . LYS D 4 7   ? 22.66300  8.24400   -21.66200 1.000 57.63849  ? 7   LYS G N   1 
ATOM   3157 C CA  . LYS D 4 7   ? 22.05800  9.31200   -22.44300 1.000 56.51730  ? 7   LYS G CA  1 
ATOM   3158 C C   . LYS D 4 7   ? 20.66200  9.62000   -21.93700 1.000 54.49074  ? 7   LYS G C   1 
ATOM   3159 O O   . LYS D 4 7   ? 19.83700  8.70300   -21.83400 1.000 55.01449  ? 7   LYS G O   1 
ATOM   3160 C CB  . LYS D 4 7   ? 21.97500  8.90800   -23.91800 1.000 56.62521  ? 7   LYS G CB  1 
ATOM   3161 C CG  . LYS D 4 7   ? 23.09800  9.38800   -24.79300 1.000 58.69125  ? 7   LYS G CG  1 
ATOM   3162 C CD  . LYS D 4 7   ? 22.54800  9.87300   -26.13600 1.000 59.34133  ? 7   LYS G CD  1 
ATOM   3163 C CE  . LYS D 4 7   ? 21.95100  8.75200   -26.96600 1.000 57.90431  ? 7   LYS G CE  1 
ATOM   3164 N NZ  . LYS D 4 7   ? 21.35600  9.27600   -28.23700 1.000 56.91735  ? 7   LYS G NZ  1 
ATOM   3165 N N   . PRO D 4 8   ? 20.34600  10.87000  -21.62900 1.000 42.60774  ? 8   PRO G N   1 
ATOM   3166 C CA  . PRO D 4 8   ? 18.94500  11.23500  -21.41400 1.000 41.04703  ? 8   PRO G CA  1 
ATOM   3167 C C   . PRO D 4 8   ? 18.17800  11.22000  -22.73000 1.000 39.66528  ? 8   PRO G C   1 
ATOM   3168 O O   . PRO D 4 8   ? 18.75100  11.29600  -23.82400 1.000 39.46263  ? 8   PRO G O   1 
ATOM   3169 C CB  . PRO D 4 8   ? 19.01300  12.65100  -20.83200 1.000 40.73383  ? 8   PRO G CB  1 
ATOM   3170 C CG  . PRO D 4 8   ? 20.45800  12.85700  -20.41800 1.000 42.18664  ? 8   PRO G CG  1 
ATOM   3171 C CD  . PRO D 4 8   ? 21.27200  11.97800  -21.33100 1.000 42.23664  ? 8   PRO G CD  1 
ATOM   3172 N N   . PHE D 4 9   ? 16.85500  11.11700  -22.61100 1.000 45.47124  ? 9   PHE G N   1 
ATOM   3173 C CA  . PHE D 4 9   ? 15.97100  11.22500  -23.76100 1.000 43.10517  ? 9   PHE G CA  1 
ATOM   3174 C C   . PHE D 4 9   ? 15.27300  12.57500  -23.71600 1.000 41.04439  ? 9   PHE G C   1 
ATOM   3175 O O   . PHE D 4 9   ? 14.48300  12.84100  -22.80100 1.000 40.76015  ? 9   PHE G O   1 
ATOM   3176 C CB  . PHE D 4 9   ? 14.92800  10.11400  -23.82700 1.000 42.66038  ? 9   PHE G CB  1 
ATOM   3177 C CG  . PHE D 4 9   ? 13.96700  10.29700  -24.97600 1.000 40.26272  ? 9   PHE G CG  1 
ATOM   3178 C CD1 . PHE D 4 9   ? 14.37100  10.02400  -26.27000 1.000 40.88122  ? 9   PHE G CD1 1 
ATOM   3179 C CD2 . PHE D 4 9   ? 12.68700  10.79800  -24.76700 1.000 38.91256  ? 9   PHE G CD2 1 
ATOM   3180 C CE1 . PHE D 4 9   ? 13.51500  10.22100  -27.33400 1.000 39.69950  ? 9   PHE G CE1 1 
ATOM   3181 C CE2 . PHE D 4 9   ? 11.82400  11.00100  -25.82700 1.000 37.46239  ? 9   PHE G CE2 1 
ATOM   3182 C CZ  . PHE D 4 9   ? 12.23500  10.70800  -27.11400 1.000 37.95455  ? 9   PHE G CZ  1 
ATOM   3183 N N   . LEU D 4 10  ? 15.55200  13.40200  -24.72200 1.000 35.10684  ? 10  LEU G N   1 
ATOM   3184 C CA  . LEU D 4 10  ? 15.02500  14.75100  -24.83900 1.000 33.23293  ? 10  LEU G CA  1 
ATOM   3185 C C   . LEU D 4 10  ? 13.84900  14.77200  -25.80500 1.000 31.54852  ? 10  LEU G C   1 
ATOM   3186 O O   . LEU D 4 10  ? 13.88200  14.12800  -26.85900 1.000 32.44073  ? 10  LEU G O   1 
ATOM   3187 C CB  . LEU D 4 10  ? 16.12900  15.70100  -25.33300 1.000 33.24609  ? 10  LEU G CB  1 
ATOM   3188 C CG  . LEU D 4 10  ? 15.82300  17.18200  -25.47300 1.000 31.51430  ? 10  LEU G CG  1 
ATOM   3189 C CD1 . LEU D 4 10  ? 15.58800  17.76100  -24.07300 1.000 31.98015  ? 10  LEU G CD1 1 
ATOM   3190 C CD2 . LEU D 4 10  ? 17.01600  17.90900  -26.17000 1.000 32.81972  ? 10  LEU G CD2 1 
ATOM   3191 N N   . SER D 4 11  ? 12.80900  15.51600  -25.45900 1.000 39.93110  ? 11  SER G N   1 
ATOM   3192 C CA  . SER D 4 11  ? 11.67800  15.58600  -26.36400 1.000 39.65475  ? 11  SER G CA  1 
ATOM   3193 C C   . SER D 4 11  ? 10.96500  16.91500  -26.18900 1.000 38.99415  ? 11  SER G C   1 
ATOM   3194 O O   . SER D 4 11  ? 11.06400  17.57100  -25.14600 1.000 39.76266  ? 11  SER G O   1 
ATOM   3195 C CB  . SER D 4 11  ? 10.70900  14.41000  -26.15100 1.000 39.63896  ? 11  SER G CB  1 
ATOM   3196 O OG  . SER D 4 11  ? 10.17600  14.44200  -24.84600 1.000 40.86543  ? 11  SER G OG  1 
ATOM   3197 N N   . ALA D 4 12  ? 10.24700  17.30300  -27.24100 1.000 38.81255  ? 12  ALA G N   1 
ATOM   3198 C CA  . ALA D 4 12  ? 9.48500   18.54300  -27.26900 1.000 38.86782  ? 12  ALA G CA  1 
ATOM   3199 C C   . ALA D 4 12  ? 8.00800   18.21500  -27.39200 1.000 40.29430  ? 12  ALA G C   1 
ATOM   3200 O O   . ALA D 4 12  ? 7.62200   17.32600  -28.15800 1.000 40.07323  ? 12  ALA G O   1 
ATOM   3201 C CB  . ALA D 4 12  ? 9.91900   19.45000  -28.43000 1.000 38.89151  ? 12  ALA G CB  1 
ATOM   3202 N N   . TRP D 4 13  ? 7.17700   18.92500  -26.63500 1.000 50.03231  ? 13  TRP G N   1 
ATOM   3203 C CA  . TRP D 4 13  ? 5.77500   18.61500  -26.67400 1.000 51.63777  ? 13  TRP G CA  1 
ATOM   3204 C C   . TRP D 4 13  ? 4.95200   19.89500  -26.67500 1.000 52.59315  ? 13  TRP G C   1 
ATOM   3205 O O   . TRP D 4 13  ? 5.25300   20.82300  -25.91700 1.000 53.85383  ? 13  TRP G O   1 
ATOM   3206 C CB  . TRP D 4 13  ? 5.37200   17.72200  -25.48300 1.000 52.26942  ? 13  TRP G CB  1 
ATOM   3207 C CG  . TRP D 4 13  ? 4.12800   16.92700  -25.77300 1.000 53.69854  ? 13  TRP G CG  1 
ATOM   3208 C CD1 . TRP D 4 13  ? 4.06000   15.66400  -26.29700 1.000 52.83002  ? 13  TRP G CD1 1 
ATOM   3209 C CD2 . TRP D 4 13  ? 2.77400   17.36200  -25.59400 1.000 55.58561  ? 13  TRP G CD2 1 
ATOM   3210 N NE1 . TRP D 4 13  ? 2.74000   15.27700  -26.43300 1.000 54.11701  ? 13  TRP G NE1 1 
ATOM   3211 C CE2 . TRP D 4 13  ? 1.93400   16.31000  -26.02200 1.000 55.54087  ? 13  TRP G CE2 1 
ATOM   3212 C CE3 . TRP D 4 13  ? 2.18900   18.54400  -25.12100 1.000 56.73575  ? 13  TRP G CE3 1 
ATOM   3213 C CZ2 . TRP D 4 13  ? 0.54100   16.39800  -25.97500 1.000 57.14369  ? 13  TRP G CZ2 1 
ATOM   3214 C CZ3 . TRP D 4 13  ? 0.80600   18.63000  -25.07600 1.000 58.73336  ? 13  TRP G CZ3 1 
ATOM   3215 C CH2 . TRP D 4 13  ? -0.00300  17.56300  -25.50300 1.000 58.76494  ? 13  TRP G CH2 1 
ATOM   3216 N N   . PRO D 4 14  ? 3.88800   19.96500  -27.49200 1.000 43.23413  ? 14  PRO G N   1 
ATOM   3217 C CA  . PRO D 4 14  ? 3.38800   18.91500  -28.39100 1.000 43.06306  ? 14  PRO G CA  1 
ATOM   3218 C C   . PRO D 4 14  ? 4.08200   18.79600  -29.74200 1.000 42.73144  ? 14  PRO G C   1 
ATOM   3219 O O   . PRO D 4 14  ? 3.85100   17.81700  -30.46500 1.000 42.32876  ? 14  PRO G O   1 
ATOM   3220 C CB  . PRO D 4 14  ? 1.93200   19.32600  -28.61500 1.000 45.74233  ? 14  PRO G CB  1 
ATOM   3221 C CG  . PRO D 4 14  ? 1.96200   20.80700  -28.53200 1.000 46.97142  ? 14  PRO G CG  1 
ATOM   3222 C CD  . PRO D 4 14  ? 2.97500   21.12200  -27.45000 1.000 45.96077  ? 14  PRO G CD  1 
ATOM   3223 N N   . SER D 4 15  ? 4.87800   19.78900  -30.10800 1.000 41.35233  ? 15  SER G N   1 
ATOM   3224 C CA  . SER D 4 15  ? 5.49300   19.78700  -31.43100 1.000 41.89713  ? 15  SER G CA  1 
ATOM   3225 C C   . SER D 4 15  ? 6.75600   20.62400  -31.41700 1.000 41.01808  ? 15  SER G C   1 
ATOM   3226 O O   . SER D 4 15  ? 6.74000   21.76000  -30.93900 1.000 40.91806  ? 15  SER G O   1 
ATOM   3227 C CB  . SER D 4 15  ? 4.53700   20.33500  -32.48800 1.000 44.07371  ? 15  SER G CB  1 
ATOM   3228 O OG  . SER D 4 15  ? 5.14500   20.25800  -33.76000 1.000 44.72115  ? 15  SER G OG  1 
ATOM   3229 N N   . ALA D 4 16  ? 7.83300   20.06200  -31.96300 1.000 36.29119  ? 16  ALA G N   1 
ATOM   3230 C CA  . ALA D 4 16  ? 9.09100   20.78600  -32.10800 1.000 36.84652  ? 16  ALA G CA  1 
ATOM   3231 C C   . ALA D 4 16  ? 8.98700   21.89600  -33.15000 1.000 38.32302  ? 16  ALA G C   1 
ATOM   3232 O O   . ALA D 4 16  ? 9.77300   22.84900  -33.12400 1.000 38.11510  ? 16  ALA G O   1 
ATOM   3233 C CB  . ALA D 4 16  ? 10.20700  19.80800  -32.48300 1.000 37.17025  ? 16  ALA G CB  1 
ATOM   3234 N N   . VAL D 4 17  ? 8.05900   21.76200  -34.09000 1.000 32.40652  ? 17  VAL G N   1 
ATOM   3235 C CA  . VAL D 4 17  ? 7.72800   22.81100  -35.04400 1.000 33.58561  ? 17  VAL G CA  1 
ATOM   3236 C C   . VAL D 4 17  ? 6.60400   23.60800  -34.41000 1.000 34.18568  ? 17  VAL G C   1 
ATOM   3237 O O   . VAL D 4 17  ? 5.49000   23.10300  -34.25400 1.000 35.43846  ? 17  VAL G O   1 
ATOM   3238 C CB  . VAL D 4 17  ? 7.30500   22.23300  -36.39900 1.000 34.52519  ? 17  VAL G CB  1 
ATOM   3239 C CG1 . VAL D 4 17  ? 6.96700   23.36400  -37.37000 1.000 35.09105  ? 17  VAL G CG1 1 
ATOM   3240 C CG2 . VAL D 4 17  ? 8.41300   21.33200  -36.95600 1.000 33.91196  ? 17  VAL G CG2 1 
ATOM   3241 N N   . VAL D 4 18  ? 6.89900   24.83800  -34.01700 1.000 33.56455  ? 18  VAL G N   1 
ATOM   3242 C CA  . VAL D 4 18  ? 5.95800   25.58400  -33.19100 1.000 34.05671  ? 18  VAL G CA  1 
ATOM   3243 C C   . VAL D 4 18  ? 5.82600   26.99800  -33.73800 1.000 34.12778  ? 18  VAL G C   1 
ATOM   3244 O O   . VAL D 4 18  ? 6.83200   27.61500  -34.12600 1.000 33.33031  ? 18  VAL G O   1 
ATOM   3245 C CB  . VAL D 4 18  ? 6.40500   25.59400  -31.72000 1.000 32.79341  ? 18  VAL G CB  1 
ATOM   3246 C CG1 . VAL D 4 18  ? 7.78500   26.27500  -31.55200 1.000 30.85107  ? 18  VAL G CG1 1 
ATOM   3247 C CG2 . VAL D 4 18  ? 5.36300   26.26600  -30.85600 1.000 35.43320  ? 18  VAL G CG2 1 
ATOM   3248 N N   . PRO D 4 19  ? 4.61200   27.53900  -33.79800 1.000 39.55211  ? 19  PRO G N   1 
ATOM   3249 C CA  . PRO D 4 19  ? 4.45400   28.92500  -34.23600 1.000 39.15733  ? 19  PRO G CA  1 
ATOM   3250 C C   . PRO D 4 19  ? 5.00900   29.87000  -33.20100 1.000 38.39408  ? 19  PRO G C   1 
ATOM   3251 O O   . PRO D 4 19  ? 4.92700   29.62200  -31.99200 1.000 38.71780  ? 19  PRO G O   1 
ATOM   3252 C CB  . PRO D 4 19  ? 2.93800   29.08800  -34.37800 1.000 41.86291  ? 19  PRO G CB  1 
ATOM   3253 C CG  . PRO D 4 19  ? 2.37400   28.05300  -33.45500 1.000 44.35005  ? 19  PRO G CG  1 
ATOM   3254 C CD  . PRO D 4 19  ? 3.31400   26.88800  -33.54800 1.000 43.08411  ? 19  PRO G CD  1 
ATOM   3255 N N   . ARG D 4 20  ? 5.58700   30.96200  -33.68800 1.000 38.77307  ? 20  ARG G N   1 
ATOM   3256 C CA  . ARG D 4 20  ? 5.91100   32.05800  -32.79600 1.000 38.89677  ? 20  ARG G CA  1 
ATOM   3257 C C   . ARG D 4 20  ? 4.64900   32.49900  -32.07000 1.000 40.78910  ? 20  ARG G C   1 
ATOM   3258 O O   . ARG D 4 20  ? 3.57900   32.59600  -32.67200 1.000 41.19178  ? 20  ARG G O   1 
ATOM   3259 C CB  . ARG D 4 20  ? 6.51900   33.21100  -33.57700 1.000 39.63107  ? 20  ARG G CB  1 
ATOM   3260 C CG  . ARG D 4 20  ? 7.28300   34.10800  -32.70400 1.000 40.42590  ? 20  ARG G CG  1 
ATOM   3261 C CD  . ARG D 4 20  ? 7.97000   35.18800  -33.48100 1.000 41.75237  ? 20  ARG G CD  1 
ATOM   3262 N NE  . ARG D 4 20  ? 7.17800   36.39900  -33.42200 1.000 44.23162  ? 20  ARG G NE  1 
ATOM   3263 C CZ  . ARG D 4 20  ? 6.56400   36.93900  -34.46200 1.000 44.75010  ? 20  ARG G CZ  1 
ATOM   3264 N NH1 . ARG D 4 20  ? 6.60200   36.37100  -35.65800 1.000 44.41848  ? 20  ARG G NH1 1 
ATOM   3265 N NH2 . ARG D 4 20  ? 5.91300   38.08300  -34.30200 1.000 46.19501  ? 20  ARG G NH2 1 
ATOM   3266 N N   . GLY D 4 21  ? 4.77100   32.72900  -30.75900 1.000 37.88612  ? 21  GLY G N   1 
ATOM   3267 C CA  . GLY D 4 21  ? 3.62500   32.97200  -29.91100 1.000 39.40736  ? 21  GLY G CA  1 
ATOM   3268 C C   . GLY D 4 21  ? 2.94000   31.71900  -29.38800 1.000 40.71278  ? 21  GLY G C   1 
ATOM   3269 O O   . GLY D 4 21  ? 2.04300   31.82600  -28.53800 1.000 42.63406  ? 21  GLY G O   1 
ATOM   3270 N N   . GLY D 4 22  ? 3.34600   30.54100  -29.84000 1.000 35.80692  ? 22  GLY G N   1 
ATOM   3271 C CA  . GLY D 4 22  ? 2.79200   29.29400  -29.34600 1.000 37.49134  ? 22  GLY G CA  1 
ATOM   3272 C C   . GLY D 4 22  ? 3.44100   28.84700  -28.05300 1.000 36.71756  ? 22  GLY G C   1 
ATOM   3273 O O   . GLY D 4 22  ? 3.89400   29.65800  -27.24200 1.000 36.59386  ? 22  GLY G O   1 
ATOM   3274 N N   . HIS D 4 23  ? 3.49400   27.53500  -27.84900 1.000 42.64459  ? 23  HIS G N   1 
ATOM   3275 C CA  . HIS D 4 23  ? 4.20600   27.01600  -26.69400 1.000 41.75501  ? 23  HIS G CA  1 
ATOM   3276 C C   . HIS D 4 23  ? 4.80400   25.66000  -27.02900 1.000 39.76529  ? 23  HIS G C   1 
ATOM   3277 O O   . HIS D 4 23  ? 4.21900   24.86600  -27.76900 1.000 39.65212  ? 23  HIS G O   1 
ATOM   3278 C CB  . HIS D 4 23  ? 3.29800   26.91300  -25.46300 1.000 43.94474  ? 23  HIS G CB  1 
ATOM   3279 C CG  . HIS D 4 23  ? 2.14600   25.96700  -25.62500 1.000 44.06318  ? 23  HIS G CG  1 
ATOM   3280 N ND1 . HIS D 4 23  ? 2.27300   24.60400  -25.46000 1.000 42.91304  ? 23  HIS G ND1 1 
ATOM   3281 C CD2 . HIS D 4 23  ? 0.84200   26.19000  -25.91800 1.000 45.86339  ? 23  HIS G CD2 1 
ATOM   3282 C CE1 . HIS D 4 23  ? 1.09700   24.02700  -25.64200 1.000 43.20255  ? 23  HIS G CE1 1 
ATOM   3283 N NE2 . HIS D 4 23  ? 0.21100   24.96600  -25.92100 1.000 45.38702  ? 23  HIS G NE2 1 
ATOM   3284 N N   . VAL D 4 24  ? 5.98000   25.40500  -26.47000 1.000 44.65009  ? 24  VAL G N   1 
ATOM   3285 C CA  . VAL D 4 24  ? 6.60400   24.09500  -26.55500 1.000 42.10768  ? 24  VAL G CA  1 
ATOM   3286 C C   . VAL D 4 24  ? 7.32300   23.82600  -25.24200 1.000 42.69459  ? 24  VAL G C   1 
ATOM   3287 O O   . VAL D 4 24  ? 7.92500   24.72500  -24.64800 1.000 44.86854  ? 24  VAL G O   1 
ATOM   3288 C CB  . VAL D 4 24  ? 7.55000   24.00200  -27.76700 1.000 39.00468  ? 24  VAL G CB  1 
ATOM   3289 C CG1 . VAL D 4 24  ? 8.65300   25.06500  -27.68000 1.000 38.37829  ? 24  VAL G CG1 1 
ATOM   3290 C CG2 . VAL D 4 24  ? 8.10900   22.58800  -27.91300 1.000 36.96759  ? 24  VAL G CG2 1 
ATOM   3291 N N   . THR D 4 25  ? 7.21000   22.59900  -24.75900 1.000 46.14764  ? 25  THR G N   1 
ATOM   3292 C CA  . THR D 4 25  ? 7.90300   22.16200  -23.56100 1.000 47.33462  ? 25  THR G CA  1 
ATOM   3293 C C   . THR D 4 25  ? 9.00400   21.18900  -23.95700 1.000 44.12898  ? 25  THR G C   1 
ATOM   3294 O O   . THR D 4 25  ? 8.74400   20.22400  -24.68400 1.000 42.50510  ? 25  THR G O   1 
ATOM   3295 C CB  . THR D 4 25  ? 6.91500   21.51100  -22.59400 1.000 48.75321  ? 25  THR G CB  1 
ATOM   3296 O OG1 . THR D 4 25  ? 5.96300   22.49600  -22.16900 1.000 50.79556  ? 25  THR G OG1 1 
ATOM   3297 C CG2 . THR D 4 25  ? 7.62200   20.92800  -21.38100 1.000 49.97968  ? 25  THR G CG2 1 
ATOM   3298 N N   . LEU D 4 26  ? 10.23000  21.45700  -23.50900 1.000 39.19154  ? 26  LEU G N   1 
ATOM   3299 C CA  . LEU D 4 26  ? 11.31500  20.48800  -23.61900 1.000 37.16498  ? 26  LEU G CA  1 
ATOM   3300 C C   . LEU D 4 26  ? 11.34500  19.64300  -22.35000 1.000 40.07323  ? 26  LEU G C   1 
ATOM   3301 O O   . LEU D 4 26  ? 11.37100  20.17700  -21.23700 1.000 43.95001  ? 26  LEU G O   1 
ATOM   3302 C CB  . LEU D 4 26  ? 12.66800  21.17400  -23.83000 1.000 36.54912  ? 26  LEU G CB  1 
ATOM   3303 C CG  . LEU D 4 26  ? 13.02700  21.56900  -25.27000 1.000 32.93816  ? 26  LEU G CG  1 
ATOM   3304 C CD1 . LEU D 4 26  ? 14.34600  22.35200  -25.36500 1.000 32.41441  ? 26  LEU G CD1 1 
ATOM   3305 C CD2 . LEU D 4 26  ? 13.07400  20.30500  -26.10800 1.000 31.74065  ? 26  LEU G CD2 1 
ATOM   3306 N N   . ARG D 4 27  ? 11.31300  18.32800  -22.51200 1.000 48.02418  ? 27  ARG G N   1 
ATOM   3307 C CA  . ARG D 4 27  ? 11.44500  17.41500  -21.39000 1.000 50.17180  ? 27  ARG G CA  1 
ATOM   3308 C C   . ARG D 4 27  ? 12.75000  16.64600  -21.51100 1.000 49.82966  ? 27  ARG G C   1 
ATOM   3309 O O   . ARG D 4 27  ? 13.14900  16.24900  -22.61000 1.000 47.10038  ? 27  ARG G O   1 
ATOM   3310 C CB  . ARG D 4 27  ? 10.25400  16.45600  -21.32600 1.000 49.31381  ? 27  ARG G CB  1 
ATOM   3311 C CG  . ARG D 4 27  ? 9.31200   16.78000  -20.19700 1.000 52.79580  ? 27  ARG G CG  1 
ATOM   3312 C CD  . ARG D 4 27  ? 8.17000   15.77800  -20.10600 1.000 51.87464  ? 27  ARG G CD  1 
ATOM   3313 N NE  . ARG D 4 27  ? 7.45100   15.65600  -21.37000 1.000 50.04547  ? 27  ARG G NE  1 
ATOM   3314 C CZ  . ARG D 4 27  ? 6.43700   14.82500  -21.57000 1.000 50.41657  ? 27  ARG G CZ  1 
ATOM   3315 N NH1 . ARG D 4 27  ? 6.00300   14.02400  -20.60800 1.000 50.92453  ? 27  ARG G NH1 1 
ATOM   3316 N NH2 . ARG D 4 27  ? 5.84300   14.80000  -22.76600 1.000 48.02418  ? 27  ARG G NH2 1 
ATOM   3317 N N   . CYS D 4 28  ? 13.41200  16.44400  -20.37400 1.000 41.52340  ? 28  CYS G N   1 
ATOM   3318 C CA  . CYS D 4 28  ? 14.65700  15.68600  -20.29000 1.000 42.51826  ? 28  CYS G CA  1 
ATOM   3319 C C   . CYS D 4 28  ? 14.43500  14.54400  -19.30500 1.000 43.94474  ? 28  CYS G C   1 
ATOM   3320 O O   . CYS D 4 28  ? 14.27000  14.77700  -18.10100 1.000 46.66875  ? 28  CYS G O   1 
ATOM   3321 C CB  . CYS D 4 28  ? 15.81200  16.58700  -19.85400 1.000 44.97118  ? 28  CYS G CB  1 
ATOM   3322 S SG  . CYS D 4 28  ? 17.48000  15.84100  -19.83900 1.000 45.60020  ? 28  CYS G SG  1 
ATOM   3323 N N   . HIS D 4 29  ? 14.39900  13.31900  -19.81900 1.000 39.00468  ? 29  HIS G N   1 
ATOM   3324 C CA  . HIS D 4 29  ? 14.15300  12.13400  -19.01700 1.000 40.01796  ? 29  HIS G CA  1 
ATOM   3325 C C   . HIS D 4 29  ? 15.45600  11.36000  -18.88100 1.000 42.02872  ? 29  HIS G C   1 
ATOM   3326 O O   . HIS D 4 29  ? 16.08900  11.02300  -19.88900 1.000 40.95228  ? 29  HIS G O   1 
ATOM   3327 C CB  . HIS D 4 29  ? 13.07400  11.26100  -19.65100 1.000 39.20470  ? 29  HIS G CB  1 
ATOM   3328 C CG  . HIS D 4 29  ? 12.68000  10.08700  -18.80800 1.000 42.93936  ? 29  HIS G CG  1 
ATOM   3329 N ND1 . HIS D 4 29  ? 13.16000  8.81400   -19.03100 1.000 44.45270  ? 29  HIS G ND1 1 
ATOM   3330 C CD2 . HIS D 4 29  ? 11.85700  9.99600   -17.73800 1.000 46.08710  ? 29  HIS G CD2 1 
ATOM   3331 C CE1 . HIS D 4 29  ? 12.64500  7.98800   -18.13800 1.000 48.28210  ? 29  HIS G CE1 1 
ATOM   3332 N NE2 . HIS D 4 29  ? 11.85600  8.68200   -17.33800 1.000 49.42435  ? 29  HIS G NE2 1 
ATOM   3333 N N   . TYR D 4 30  ? 15.83600  11.05700  -17.64000 1.000 46.53979  ? 30  TYR G N   1 
ATOM   3334 C CA  . TYR D 4 30  ? 17.13800  10.47100  -17.35200 1.000 47.89785  ? 30  TYR G CA  1 
ATOM   3335 C C   . TYR D 4 30  ? 17.06300  9.79300   -15.99500 1.000 50.39552  ? 30  TYR G C   1 
ATOM   3336 O O   . TYR D 4 30  ? 16.67700  10.43100  -15.01000 1.000 50.96401  ? 30  TYR G O   1 
ATOM   3337 C CB  . TYR D 4 30  ? 18.24200  11.54900  -17.36700 1.000 48.60320  ? 30  TYR G CB  1 
ATOM   3338 C CG  . TYR D 4 30  ? 19.59800  11.04200  -16.93300 1.000 49.70333  ? 30  TYR G CG  1 
ATOM   3339 C CD1 . TYR D 4 30  ? 20.30000  10.13400  -17.71000 1.000 49.21906  ? 30  TYR G CD1 1 
ATOM   3340 C CD2 . TYR D 4 30  ? 20.17800  11.47600  -15.74800 1.000 51.17456  ? 30  TYR G CD2 1 
ATOM   3341 C CE1 . TYR D 4 30  ? 21.54600  9.66700   -17.32100 1.000 50.68239  ? 30  TYR G CE1 1 
ATOM   3342 C CE2 . TYR D 4 30  ? 21.42800  11.01200  -15.34300 1.000 51.85885  ? 30  TYR G CE2 1 
ATOM   3343 C CZ  . TYR D 4 30  ? 22.10700  10.10600  -16.13500 1.000 51.95623  ? 30  TYR G CZ  1 
ATOM   3344 O OH  . TYR D 4 30  ? 23.34600  9.63500   -15.74500 1.000 52.85634  ? 30  TYR G OH  1 
ATOM   3345 N N   . ARG D 4 31  ? 17.41100  8.50600   -15.95600 1.000 70.52688  ? 31  ARG G N   1 
ATOM   3346 C CA  . ARG D 4 31  ? 17.37700  7.69700   -14.73600 1.000 72.77978  ? 31  ARG G CA  1 
ATOM   3347 C C   . ARG D 4 31  ? 16.03500  7.83000   -14.01200 1.000 73.01928  ? 31  ARG G C   1 
ATOM   3348 O O   . ARG D 4 31  ? 15.96600  8.12400   -12.81500 1.000 74.24574  ? 31  ARG G O   1 
ATOM   3349 C CB  . ARG D 4 31  ? 18.55100  8.05000   -13.81800 1.000 74.42998  ? 31  ARG G CB  1 
ATOM   3350 C CG  . ARG D 4 31  ? 19.89200  7.92400   -14.52400 1.000 74.41155  ? 31  ARG G CG  1 
ATOM   3351 C CD  . ARG D 4 31  ? 21.07200  7.79100   -13.57400 1.000 75.93542  ? 31  ARG G CD  1 
ATOM   3352 N NE  . ARG D 4 31  ? 21.13200  8.85800   -12.57900 1.000 77.99883  ? 31  ARG G NE  1 
ATOM   3353 C CZ  . ARG D 4 31  ? 21.29300  8.65500   -11.27600 1.000 80.61756  ? 31  ARG G CZ  1 
ATOM   3354 N NH1 . ARG D 4 31  ? 21.41800  7.43600   -10.77700 1.000 81.27027  ? 31  ARG G NH1 1 
ATOM   3355 N NH2 . ARG D 4 31  ? 21.34300  9.70300   -10.45600 1.000 80.55966  ? 31  ARG G NH2 1 
ATOM   3356 N N   . HIS D 4 32  ? 14.95400  7.62400   -14.77500 1.000 81.50188  ? 32  HIS G N   1 
ATOM   3357 C CA  . HIS D 4 32  ? 13.58200  7.59900   -14.25200 1.000 81.32817  ? 32  HIS G CA  1 
ATOM   3358 C C   . HIS D 4 32  ? 13.20400  8.91100   -13.56200 1.000 81.53609  ? 32  HIS G C   1 
ATOM   3359 O O   . HIS D 4 32  ? 12.50100  8.91400   -12.55000 1.000 82.29408  ? 32  HIS G O   1 
ATOM   3360 C CB  . HIS D 4 32  ? 13.37000  6.40900   -13.30200 1.000 83.07312  ? 32  HIS G CB  1 
ATOM   3361 C CG  . HIS D 4 32  ? 13.76200  5.08800   -13.88800 1.000 83.64950  ? 32  HIS G CG  1 
ATOM   3362 N ND1 . HIS D 4 32  ? 15.05300  4.60500   -13.83600 1.000 85.01019  ? 32  HIS G ND1 1 
ATOM   3363 C CD2 . HIS D 4 32  ? 13.03600  4.15400   -14.54600 1.000 84.26010  ? 32  HIS G CD2 1 
ATOM   3364 C CE1 . HIS D 4 32  ? 15.10300  3.42500   -14.43000 1.000 84.80754  ? 32  HIS G CE1 1 
ATOM   3365 N NE2 . HIS D 4 32  ? 13.89200  3.12800   -14.87000 1.000 84.62330  ? 32  HIS G NE2 1 
ATOM   3366 N N   . ARG D 4 33  ? 13.65500  10.03800  -14.11500 1.000 68.09764  ? 33  ARG G N   1 
ATOM   3367 C CA  . ARG D 4 33  ? 13.36100  11.33600  -13.52200 1.000 68.75561  ? 33  ARG G CA  1 
ATOM   3368 C C   . ARG D 4 33  ? 13.29600  12.39300  -14.61500 1.000 66.98961  ? 33  ARG G C   1 
ATOM   3369 O O   . ARG D 4 33  ? 13.95900  12.27900  -15.64800 1.000 65.67630  ? 33  ARG G O   1 
ATOM   3370 C CB  . ARG D 4 33  ? 14.40900  11.72700  -12.47000 1.000 71.51910  ? 33  ARG G CB  1 
ATOM   3371 N N   . PHE D 4 34  ? 12.49700  13.43400  -14.37000 1.000 68.24239  ? 34  PHE G N   1 
ATOM   3372 C CA  . PHE D 4 34  ? 12.33200  14.53900  -15.30700 1.000 67.28965  ? 34  PHE G CA  1 
ATOM   3373 C C   . PHE D 4 34  ? 12.94300  15.84300  -14.79200 1.000 68.87668  ? 34  PHE G C   1 
ATOM   3374 O O   . PHE D 4 34  ? 12.57800  16.92500  -15.26600 1.000 68.42926  ? 34  PHE G O   1 
ATOM   3375 C CB  . PHE D 4 34  ? 10.84700  14.74200  -15.62400 1.000 65.27362  ? 34  PHE G CB  1 
ATOM   3376 C CG  . PHE D 4 34  ? 10.31100  13.80400  -16.67100 1.000 62.73647  ? 34  PHE G CG  1 
ATOM   3377 C CD1 . PHE D 4 34  ? 10.56600  14.02700  -18.01700 1.000 60.37040  ? 34  PHE G CD1 1 
ATOM   3378 C CD2 . PHE D 4 34  ? 9.53300   12.71100  -16.31400 1.000 62.79437  ? 34  PHE G CD2 1 
ATOM   3379 C CE1 . PHE D 4 34  ? 10.06900  13.17200  -18.98700 1.000 58.50701  ? 34  PHE G CE1 1 
ATOM   3380 C CE2 . PHE D 4 34  ? 9.02100   11.84400  -17.28300 1.000 60.93362  ? 34  PHE G CE2 1 
ATOM   3381 C CZ  . PHE D 4 34  ? 9.29700   12.07700  -18.62200 1.000 58.56755  ? 34  PHE G CZ  1 
ATOM   3382 N N   . ASN D 4 35  ? 13.87100  15.76400  -13.84200 1.000 67.15542  ? 35  ASN G N   1 
ATOM   3383 C CA  . ASN D 4 35  ? 14.34800  16.93200  -13.11700 1.000 68.75824  ? 35  ASN G CA  1 
ATOM   3384 C C   . ASN D 4 35  ? 15.87100  16.97700  -13.10700 1.000 68.66876  ? 35  ASN G C   1 
ATOM   3385 O O   . ASN D 4 35  ? 16.55200  16.02800  -13.50600 1.000 68.58717  ? 35  ASN G O   1 
ATOM   3386 C CB  . ASN D 4 35  ? 13.82100  16.92600  -11.67600 1.000 70.17684  ? 35  ASN G CB  1 
ATOM   3387 C CG  . ASN D 4 35  ? 14.00800  15.58700  -11.00700 1.000 70.40581  ? 35  ASN G CG  1 
ATOM   3388 O OD1 . ASN D 4 35  ? 13.37800  14.60500  -11.39400 1.000 69.87154  ? 35  ASN G OD1 1 
ATOM   3389 N ND2 . ASN D 4 35  ? 14.87600  15.53200  -10.00500 1.000 72.23234  ? 35  ASN G ND2 1 
ATOM   3390 N N   . ASN D 4 36  ? 16.39100  18.11100  -12.63500 1.000 68.75298  ? 36  ASN G N   1 
ATOM   3391 C CA  . ASN D 4 36  ? 17.81900  18.33000  -12.41100 1.000 68.30556  ? 36  ASN G CA  1 
ATOM   3392 C C   . ASN D 4 36  ? 18.62900  18.05100  -13.67800 1.000 66.99224  ? 36  ASN G C   1 
ATOM   3393 O O   . ASN D 4 36  ? 19.40100  17.09900  -13.76300 1.000 66.30269  ? 36  ASN G O   1 
ATOM   3394 C CB  . ASN D 4 36  ? 18.31600  17.47700  -11.24200 1.000 70.41634  ? 36  ASN G CB  1 
ATOM   3395 C CG  . ASN D 4 36  ? 17.82500  17.98600  -9.89700  1.000 71.46646  ? 36  ASN G CG  1 
ATOM   3396 O OD1 . ASN D 4 36  ? 17.58600  19.19100  -9.71700  1.000 71.02957  ? 36  ASN G OD1 1 
ATOM   3397 N ND2 . ASN D 4 36  ? 17.67100  17.06900  -8.94000  1.000 72.56923  ? 36  ASN G ND2 1 
ATOM   3398 N N   . PHE D 4 37  ? 18.42800  18.92200  -14.66600 1.000 51.59566  ? 37  PHE G N   1 
ATOM   3399 C CA  . PHE D 4 37  ? 19.14600  18.82600  -15.92400 1.000 48.62162  ? 37  PHE G CA  1 
ATOM   3400 C C   . PHE D 4 37  ? 19.51200  20.21600  -16.42000 1.000 47.12407  ? 37  PHE G C   1 
ATOM   3401 O O   . PHE D 4 37  ? 18.93100  21.22500  -16.00300 1.000 47.62150  ? 37  PHE G O   1 
ATOM   3402 C CB  . PHE D 4 37  ? 18.32600  18.08900  -16.98700 1.000 48.22947  ? 37  PHE G CB  1 
ATOM   3403 C CG  . PHE D 4 37  ? 17.10200  18.83800  -17.46300 1.000 47.69256  ? 37  PHE G CG  1 
ATOM   3404 C CD1 . PHE D 4 37  ? 15.88600  18.70000  -16.80200 1.000 49.68754  ? 37  PHE G CD1 1 
ATOM   3405 C CD2 . PHE D 4 37  ? 17.15600  19.63900  -18.60000 1.000 45.33438  ? 37  PHE G CD2 1 
ATOM   3406 C CE1 . PHE D 4 37  ? 14.75200  19.37300  -17.25800 1.000 49.41645  ? 37  PHE G CE1 1 
ATOM   3407 C CE2 . PHE D 4 37  ? 16.02000  20.30600  -19.06700 1.000 44.85801  ? 37  PHE G CE2 1 
ATOM   3408 C CZ  . PHE D 4 37  ? 14.82200  20.17200  -18.39400 1.000 47.23987  ? 37  PHE G CZ  1 
ATOM   3409 N N   . MET D 4 38  ? 20.48600  20.26100  -17.32400 1.000 59.80454  ? 38  MET G N   1 
ATOM   3410 C CA  . MET D 4 38  ? 20.86300  21.49500  -17.99400 1.000 58.71493  ? 38  MET G CA  1 
ATOM   3411 C C   . MET D 4 38  ? 20.68800  21.33600  -19.50000 1.000 55.63562  ? 38  MET G C   1 
ATOM   3412 O O   . MET D 4 38  ? 20.72300  20.22200  -20.03200 1.000 55.23031  ? 38  MET G O   1 
ATOM   3413 C CB  . MET D 4 38  ? 22.31700  21.90700  -17.65100 1.000 58.84916  ? 38  MET G CB  1 
ATOM   3414 C CG  . MET D 4 38  ? 22.50100  22.40100  -16.20700 1.000 60.36776  ? 38  MET G CG  1 
ATOM   3415 S SD  . MET D 4 38  ? 24.14800  23.04200  -15.82900 1.000 61.59423  ? 38  MET G SD  1 
ATOM   3416 C CE  . MET D 4 38  ? 25.11200  21.55000  -16.06800 1.000 62.35484  ? 38  MET G CE  1 
ATOM   3417 N N   . LEU D 4 39  ? 20.48700  22.46700  -20.17900 1.000 49.66122  ? 39  LEU G N   1 
ATOM   3418 C CA  . LEU D 4 39  ? 20.29300  22.51700  -21.62100 1.000 47.51622  ? 39  LEU G CA  1 
ATOM   3419 C C   . LEU D 4 39  ? 21.47600  23.18500  -22.30300 1.000 47.16618  ? 39  LEU G C   1 
ATOM   3420 O O   . LEU D 4 39  ? 22.13200  24.05500  -21.73300 1.000 48.89797  ? 39  LEU G O   1 
ATOM   3421 C CB  . LEU D 4 39  ? 19.01200  23.27400  -21.99000 1.000 46.95037  ? 39  LEU G CB  1 
ATOM   3422 C CG  . LEU D 4 39  ? 17.74400  22.42600  -21.88700 1.000 46.28186  ? 39  LEU G CG  1 
ATOM   3423 C CD1 . LEU D 4 39  ? 16.50200  23.29200  -21.97500 1.000 46.50294  ? 39  LEU G CD1 1 
ATOM   3424 C CD2 . LEU D 4 39  ? 17.75300  21.38300  -22.98100 1.000 43.84210  ? 39  LEU G CD2 1 
ATOM   3425 N N   . TYR D 4 40  ? 21.72800  22.77200  -23.53800 1.000 50.07179  ? 40  TYR G N   1 
ATOM   3426 C CA  . TYR D 4 40  ? 22.83400  23.27000  -24.33200 1.000 50.82188  ? 40  TYR G CA  1 
ATOM   3427 C C   . TYR D 4 40  ? 22.35500  23.42700  -25.76900 1.000 50.78240  ? 40  TYR G C   1 
ATOM   3428 O O   . TYR D 4 40  ? 21.51400  22.66200  -26.24100 1.000 50.14812  ? 40  TYR G O   1 
ATOM   3429 C CB  . TYR D 4 40  ? 24.04300  22.32100  -24.28400 1.000 53.40904  ? 40  TYR G CB  1 
ATOM   3430 C CG  . TYR D 4 40  ? 24.55800  21.97000  -22.89900 1.000 54.53285  ? 40  TYR G CG  1 
ATOM   3431 C CD1 . TYR D 4 40  ? 23.95100  20.97700  -22.12800 1.000 54.43811  ? 40  TYR G CD1 1 
ATOM   3432 C CD2 . TYR D 4 40  ? 25.67300  22.61300  -22.38000 1.000 55.49086  ? 40  TYR G CD2 1 
ATOM   3433 C CE1 . TYR D 4 40  ? 24.43700  20.65100  -20.86900 1.000 55.68826  ? 40  TYR G CE1 1 
ATOM   3434 C CE2 . TYR D 4 40  ? 26.17000  22.29900  -21.12500 1.000 56.89103  ? 40  TYR G CE2 1 
ATOM   3435 C CZ  . TYR D 4 40  ? 25.55000  21.32000  -20.37300 1.000 57.20423  ? 40  TYR G CZ  1 
ATOM   3436 O OH  . TYR D 4 40  ? 26.05900  21.02400  -19.12700 1.000 59.08340  ? 40  TYR G OH  1 
ATOM   3437 N N   . LYS D 4 41  ? 22.89100  24.42500  -26.46200 1.000 57.44110  ? 41  LYS G N   1 
ATOM   3438 C CA  . LYS D 4 41  ? 22.60300  24.63900  -27.87100 1.000 57.50689  ? 41  LYS G CA  1 
ATOM   3439 C C   . LYS D 4 41  ? 23.80700  24.23900  -28.71500 1.000 59.73611  ? 41  LYS G C   1 
ATOM   3440 O O   . LYS D 4 41  ? 24.95300  24.33900  -28.27500 1.000 61.48369  ? 41  LYS G O   1 
ATOM   3441 C CB  . LYS D 4 41  ? 22.22200  26.09400  -28.13200 1.000 56.90156  ? 41  LYS G CB  1 
ATOM   3442 C CG  . LYS D 4 41  ? 20.77800  26.43900  -27.74800 1.000 55.19346  ? 41  LYS G CG  1 
ATOM   3443 C CD  . LYS D 4 41  ? 20.41900  27.84500  -28.25700 1.000 55.76721  ? 41  LYS G CD  1 
ATOM   3444 C CE  . LYS D 4 41  ? 18.97200  28.21200  -27.95800 1.000 54.25914  ? 41  LYS G CE  1 
ATOM   3445 N NZ  . LYS D 4 41  ? 18.86200  29.66900  -27.66900 1.000 55.17767  ? 41  LYS G NZ  1 
ATOM   3446 N N   . GLU D 4 42  ? 23.54000  23.79500  -29.94400 1.000 52.84844  ? 42  GLU G N   1 
ATOM   3447 C CA  . GLU D 4 42  ? 24.57500  23.12900  -30.73600 1.000 56.11989  ? 42  GLU G CA  1 
ATOM   3448 C C   . GLU D 4 42  ? 25.79300  24.02300  -30.97700 1.000 56.95420  ? 42  GLU G C   1 
ATOM   3449 O O   . GLU D 4 42  ? 26.93700  23.56600  -30.86800 1.000 58.75704  ? 42  GLU G O   1 
ATOM   3450 C CB  . GLU D 4 42  ? 24.00700  22.65800  -32.07600 1.000 56.59100  ? 42  GLU G CB  1 
ATOM   3451 C CG  . GLU D 4 42  ? 25.05900  21.92800  -32.91400 1.000 59.33869  ? 42  GLU G CG  1 
ATOM   3452 C CD  . GLU D 4 42  ? 24.74900  21.86700  -34.40200 1.000 60.64411  ? 42  GLU G CD  1 
ATOM   3453 O OE1 . GLU D 4 42  ? 23.64100  22.28500  -34.81900 1.000 58.62019  ? 42  GLU G OE1 1 
ATOM   3454 O OE2 . GLU D 4 42  ? 25.63600  21.39100  -35.14900 1.000 62.69436  ? 42  GLU G OE2 1 
ATOM   3455 N N   . ASP D 4 43  ? 25.57400  25.29400  -31.33900 1.000 75.56959  ? 43  ASP G N   1 
ATOM   3456 C CA  . ASP D 4 43  ? 26.70500  26.15800  -31.69200 1.000 79.99380  ? 43  ASP G CA  1 
ATOM   3457 C C   . ASP D 4 43  ? 27.64100  26.39300  -30.50900 1.000 81.46766  ? 43  ASP G C   1 
ATOM   3458 O O   . ASP D 4 43  ? 28.85500  26.53400  -30.69900 1.000 85.04704  ? 43  ASP G O   1 
ATOM   3459 C CB  . ASP D 4 43  ? 26.20500  27.49700  -32.24400 1.000 80.96234  ? 43  ASP G CB  1 
ATOM   3460 N N   . ARG D 4 44  ? 27.10400  26.42800  -29.29000 1.000 87.35521  ? 44  ARG G N   1 
ATOM   3461 C CA  . ARG D 4 44  ? 27.87400  26.62100  -28.05900 1.000 88.83170  ? 44  ARG G CA  1 
ATOM   3462 C C   . ARG D 4 44  ? 27.64900  25.41300  -27.14300 1.000 86.48669  ? 44  ARG G C   1 
ATOM   3463 O O   . ARG D 4 44  ? 26.80800  25.43800  -26.23800 1.000 84.60488  ? 44  ARG G O   1 
ATOM   3464 C CB  . ARG D 4 44  ? 27.46500  27.94200  -27.38200 1.000 88.78170  ? 44  ARG G CB  1 
ATOM   3465 N N   . ILE D 4 45  ? 28.40700  24.34600  -27.38300 1.000 82.77045  ? 45  ILE G N   1 
ATOM   3466 C CA  . ILE D 4 45  ? 28.30800  23.12600  -26.59000 1.000 82.82046  ? 45  ILE G CA  1 
ATOM   3467 C C   . ILE D 4 45  ? 29.24100  23.24800  -25.39300 1.000 84.48645  ? 45  ILE G C   1 
ATOM   3468 O O   . ILE D 4 45  ? 30.24400  23.96700  -25.44400 1.000 87.75789  ? 45  ILE G O   1 
ATOM   3469 C CB  . ILE D 4 45  ? 28.63500  21.88500  -27.45200 1.000 85.12336  ? 45  ILE G CB  1 
ATOM   3470 C CG1 . ILE D 4 45  ? 28.44500  20.59200  -26.64900 1.000 86.25245  ? 45  ILE G CG1 1 
ATOM   3471 C CG2 . ILE D 4 45  ? 30.04900  21.98200  -28.01900 1.000 87.29205  ? 45  ILE G CG2 1 
ATOM   3472 C CD1 . ILE D 4 45  ? 29.09100  19.36600  -27.28200 1.000 88.99225  ? 45  ILE G CD1 1 
ATOM   3473 N N   . HIS D 4 46  ? 28.90300  22.55400  -24.30100 1.000 104.38883 ? 46  HIS G N   1 
ATOM   3474 C CA  . HIS D 4 46  ? 29.60000  22.55300  -23.01000 1.000 105.68372 ? 46  HIS G CA  1 
ATOM   3475 C C   . HIS D 4 46  ? 29.46800  23.87400  -22.25500 1.000 106.12325 ? 46  HIS G C   1 
ATOM   3476 O O   . HIS D 4 46  ? 30.02100  23.99800  -21.15300 1.000 107.89978 ? 46  HIS G O   1 
ATOM   3477 C CB  . HIS D 4 46  ? 31.09500  22.20500  -23.12900 1.000 109.41838 ? 46  HIS G CB  1 
ATOM   3478 C CG  . HIS D 4 46  ? 31.36600  20.76600  -23.44300 1.000 110.45535 ? 46  HIS G CG  1 
ATOM   3479 N ND1 . HIS D 4 46  ? 31.35200  20.26700  -24.72800 1.000 111.67128 ? 46  HIS G ND1 1 
ATOM   3480 C CD2 . HIS D 4 46  ? 31.67300  19.72000  -22.63900 1.000 111.82130 ? 46  HIS G CD2 1 
ATOM   3481 C CE1 . HIS D 4 46  ? 31.63200  18.97600  -24.70200 1.000 113.29779 ? 46  HIS G CE1 1 
ATOM   3482 N NE2 . HIS D 4 46  ? 31.83100  18.61900  -23.44600 1.000 113.58994 ? 46  HIS G NE2 1 
ATOM   3483 N N   . VAL D 4 47  ? 28.77500  24.86700  -22.80700 1.000 97.43537  ? 47  VAL G N   1 
ATOM   3484 C CA  . VAL D 4 47  ? 28.35600  26.06400  -22.09300 1.000 97.46169  ? 47  VAL G CA  1 
ATOM   3485 C C   . VAL D 4 47  ? 26.83600  25.99000  -21.92500 1.000 93.94021  ? 47  VAL G C   1 
ATOM   3486 O O   . VAL D 4 47  ? 26.09400  26.17800  -22.90100 1.000 91.61625  ? 47  VAL G O   1 
ATOM   3487 C CB  . VAL D 4 47  ? 28.76800  27.34900  -22.82000 1.000 99.78302  ? 47  VAL G CB  1 
ATOM   3488 C CG1 . VAL D 4 47  ? 28.20000  28.56300  -22.09700 1.000 105.82321 ? 47  VAL G CG1 1 
ATOM   3489 C CG2 . VAL D 4 47  ? 30.27700  27.43800  -22.91500 1.000 100.13569 ? 47  VAL G CG2 1 
ATOM   3490 N N   . PRO D 4 48  ? 26.33600  25.72400  -20.72500 1.000 63.55236  ? 48  PRO G N   1 
ATOM   3491 C CA  . PRO D 4 48  ? 24.88800  25.57400  -20.56000 1.000 62.04165  ? 48  PRO G CA  1 
ATOM   3492 C C   . PRO D 4 48  ? 24.18900  26.90100  -20.79300 1.000 61.13365  ? 48  PRO G C   1 
ATOM   3493 O O   . PRO D 4 48  ? 24.73300  27.96900  -20.51500 1.000 64.02610  ? 48  PRO G O   1 
ATOM   3494 C CB  . PRO D 4 48  ? 24.73400  25.10900  -19.10300 1.000 63.21547  ? 48  PRO G CB  1 
ATOM   3495 C CG  . PRO D 4 48  ? 26.15000  24.89600  -18.57000 1.000 64.77882  ? 48  PRO G CG  1 
ATOM   3496 C CD  . PRO D 4 48  ? 27.05200  25.70100  -19.43900 1.000 66.76327  ? 48  PRO G CD  1 
ATOM   3497 N N   . ILE D 4 49  ? 22.96500  26.82500  -21.30200 1.000 68.09764  ? 49  ILE G N   1 
ATOM   3498 C CA  . ILE D 4 49  ? 22.21100  28.03700  -21.59000 1.000 68.10553  ? 49  ILE G CA  1 
ATOM   3499 C C   . ILE D 4 49  ? 21.70400  28.65700  -20.29000 1.000 69.62151  ? 49  ILE G C   1 
ATOM   3500 O O   . ILE D 4 49  ? 21.67800  28.01700  -19.23100 1.000 70.60057  ? 49  ILE G O   1 
ATOM   3501 C CB  . ILE D 4 49  ? 21.05600  27.74600  -22.56200 1.000 66.18688  ? 49  ILE G CB  1 
ATOM   3502 C CG1 . ILE D 4 49  ? 19.98000  26.89200  -21.87800 1.000 66.65273  ? 49  ILE G CG1 1 
ATOM   3503 C CG2 . ILE D 4 49  ? 21.59100  27.04500  -23.80200 1.000 65.45785  ? 49  ILE G CG2 1 
ATOM   3504 C CD1 . ILE D 4 49  ? 18.66200  26.85400  -22.62600 1.000 65.73683  ? 49  ILE G CD1 1 
ATOM   3505 N N   . PHE D 4 50  ? 21.29400  29.92900  -20.38100 1.000 77.00397  ? 50  PHE G N   1 
ATOM   3506 C CA  . PHE D 4 50  ? 20.80900  30.70400  -19.23100 1.000 79.38847  ? 50  PHE G CA  1 
ATOM   3507 C C   . PHE D 4 50  ? 21.84600  30.74600  -18.11400 1.000 82.46515  ? 50  PHE G C   1 
ATOM   3508 O O   . PHE D 4 50  ? 21.51000  30.63800  -16.93200 1.000 84.09166  ? 50  PHE G O   1 
ATOM   3509 C CB  . PHE D 4 50  ? 19.48600  30.15900  -18.68600 1.000 79.08580  ? 50  PHE G CB  1 
ATOM   3510 C CG  . PHE D 4 50  ? 18.29700  30.40800  -19.56900 1.000 78.63574  ? 50  PHE G CG  1 
ATOM   3511 C CD1 . PHE D 4 50  ? 18.24400  29.88600  -20.85700 1.000 76.47759  ? 50  PHE G CD1 1 
ATOM   3512 C CD2 . PHE D 4 50  ? 17.20800  31.12400  -19.09400 1.000 79.79378  ? 50  PHE G CD2 1 
ATOM   3513 C CE1 . PHE D 4 50  ? 17.14700  30.09800  -21.66300 1.000 75.85910  ? 50  PHE G CE1 1 
ATOM   3514 C CE2 . PHE D 4 50  ? 16.10100  31.33800  -19.89900 1.000 79.26213  ? 50  PHE G CE2 1 
ATOM   3515 C CZ  . PHE D 4 50  ? 16.07400  30.82300  -21.18600 1.000 77.45402  ? 50  PHE G CZ  1 
ATOM   3516 N N   . HIS D 4 51  ? 23.11700  30.89300  -18.49200 1.000 84.02586  ? 51  HIS G N   1 
ATOM   3517 C CA  . HIS D 4 51  ? 24.22600  30.90700  -17.53700 1.000 88.30796  ? 51  HIS G CA  1 
ATOM   3518 C C   . HIS D 4 51  ? 24.18100  29.68400  -16.62000 1.000 86.57617  ? 51  HIS G C   1 
ATOM   3519 O O   . HIS D 4 51  ? 24.43300  29.77000  -15.41700 1.000 89.62917  ? 51  HIS G O   1 
ATOM   3520 C CB  . HIS D 4 51  ? 24.23800  32.20300  -16.72000 1.000 94.20340  ? 51  HIS G CB  1 
ATOM   3521 C CG  . HIS D 4 51  ? 24.23000  33.44900  -17.55200 1.000 96.95636  ? 51  HIS G CG  1 
ATOM   3522 N ND1 . HIS D 4 51  ? 23.08600  34.18400  -17.78400 1.000 96.31418  ? 51  HIS G ND1 1 
ATOM   3523 C CD2 . HIS D 4 51  ? 25.22800  34.09400  -18.20200 1.000 101.22793 ? 51  HIS G CD2 1 
ATOM   3524 C CE1 . HIS D 4 51  ? 23.38000  35.22900  -18.53800 1.000 99.13031  ? 51  HIS G CE1 1 
ATOM   3525 N NE2 . HIS D 4 51  ? 24.67300  35.19700  -18.80700 1.000 102.44913 ? 51  HIS G NE2 1 
ATOM   3526 N N   . GLY D 4 52  ? 23.83200  28.53700  -17.19500 1.000 74.32207  ? 52  GLY G N   1 
ATOM   3527 C CA  . GLY D 4 52  ? 23.82700  27.29300  -16.44600 1.000 72.93769  ? 52  GLY G CA  1 
ATOM   3528 C C   . GLY D 4 52  ? 22.62200  27.07700  -15.55800 1.000 72.55870  ? 52  GLY G C   1 
ATOM   3529 O O   . GLY D 4 52  ? 22.76900  26.58300  -14.43100 1.000 74.97741  ? 52  GLY G O   1 
ATOM   3530 N N   . ARG D 4 53  ? 21.42800  27.43200  -16.03200 1.000 74.03256  ? 53  ARG G N   1 
ATOM   3531 C CA  . ARG D 4 53  ? 20.21800  27.21900  -15.24700 1.000 75.66434  ? 53  ARG G CA  1 
ATOM   3532 C C   . ARG D 4 53  ? 19.97700  25.72700  -15.02800 1.000 76.42495  ? 53  ARG G C   1 
ATOM   3533 O O   . ARG D 4 53  ? 19.94000  24.94200  -15.98100 1.000 74.64842  ? 53  ARG G O   1 
ATOM   3534 C CB  . ARG D 4 53  ? 19.00400  27.84600  -15.94100 1.000 74.79581  ? 53  ARG G CB  1 
ATOM   3535 C CG  . ARG D 4 53  ? 17.82200  28.06000  -15.00300 1.000 76.52496  ? 53  ARG G CG  1 
ATOM   3536 C CD  . ARG D 4 53  ? 16.47600  27.72400  -15.63200 1.000 76.80395  ? 53  ARG G CD  1 
ATOM   3537 N NE  . ARG D 4 53  ? 15.89300  28.84300  -16.36800 1.000 76.52233  ? 53  ARG G NE  1 
ATOM   3538 C CZ  . ARG D 4 53  ? 14.60300  28.95400  -16.66300 1.000 76.77499  ? 53  ARG G CZ  1 
ATOM   3539 N NH1 . ARG D 4 53  ? 13.72000  28.05300  -16.25900 1.000 77.25663  ? 53  ARG G NH1 1 
ATOM   3540 N NH2 . ARG D 4 53  ? 14.18700  29.99600  -17.38100 1.000 75.73276  ? 53  ARG G NH2 1 
ATOM   3541 N N   . LEU D 4 54  ? 19.82500  25.34500  -13.76000 1.000 77.27769  ? 54  LEU G N   1 
ATOM   3542 C CA  . LEU D 4 54  ? 19.44900  23.98800  -13.37300 1.000 78.29623  ? 54  LEU G CA  1 
ATOM   3543 C C   . LEU D 4 54  ? 17.93400  23.86800  -13.47300 1.000 78.50415  ? 54  LEU G C   1 
ATOM   3544 O O   . LEU D 4 54  ? 17.19900  24.38500  -12.63300 1.000 80.22804  ? 54  LEU G O   1 
ATOM   3545 C CB  . LEU D 4 54  ? 19.93200  23.68500  -11.96000 1.000 80.11750  ? 54  LEU G CB  1 
ATOM   3546 C CG  . LEU D 4 54  ? 20.93200  22.54400  -11.77200 1.000 80.43070  ? 54  LEU G CG  1 
ATOM   3547 C CD1 . LEU D 4 54  ? 20.33300  21.21000  -12.22200 1.000 80.45175  ? 54  LEU G CD1 1 
ATOM   3548 C CD2 . LEU D 4 54  ? 22.22300  22.85500  -12.51600 1.000 79.45426  ? 54  LEU G CD2 1 
ATOM   3549 N N   . PHE D 4 55  ? 17.45200  23.18700  -14.50400 1.000 62.78911  ? 55  PHE G N   1 
ATOM   3550 C CA  . PHE D 4 55  ? 16.01500  22.98100  -14.66900 1.000 64.01031  ? 55  PHE G CA  1 
ATOM   3551 C C   . PHE D 4 55  ? 15.55800  21.87200  -13.72700 1.000 65.32889  ? 55  PHE G C   1 
ATOM   3552 O O   . PHE D 4 55  ? 15.86300  20.69600  -13.94700 1.000 65.84737  ? 55  PHE G O   1 
ATOM   3553 C CB  . PHE D 4 55  ? 15.68600  22.64600  -16.12000 1.000 61.97059  ? 55  PHE G CB  1 
ATOM   3554 C CG  . PHE D 4 55  ? 15.94300  23.77200  -17.07400 1.000 60.11773  ? 55  PHE G CG  1 
ATOM   3555 C CD1 . PHE D 4 55  ? 17.18700  23.92600  -17.67100 1.000 59.23342  ? 55  PHE G CD1 1 
ATOM   3556 C CD2 . PHE D 4 55  ? 14.93900  24.67500  -17.38600 1.000 58.63335  ? 55  PHE G CD2 1 
ATOM   3557 C CE1 . PHE D 4 55  ? 17.42400  24.96100  -18.55300 1.000 57.66481  ? 55  PHE G CE1 1 
ATOM   3558 C CE2 . PHE D 4 55  ? 15.17300  25.70900  -18.26400 1.000 56.48309  ? 55  PHE G CE2 1 
ATOM   3559 C CZ  . PHE D 4 55  ? 16.41200  25.85200  -18.85200 1.000 56.42782  ? 55  PHE G CZ  1 
ATOM   3560 N N   . GLN D 4 56  ? 14.83900  22.24600  -12.67000 1.000 84.56540  ? 56  GLN G N   1 
ATOM   3561 C CA  . GLN D 4 56  ? 14.27500  21.29100  -11.72300 1.000 86.15507  ? 56  GLN G CA  1 
ATOM   3562 C C   . GLN D 4 56  ? 12.97200  20.67400  -12.22000 1.000 85.37603  ? 56  GLN G C   1 
ATOM   3563 O O   . GLN D 4 56  ? 12.26900  20.02600  -11.43700 1.000 85.92872  ? 56  GLN G O   1 
ATOM   3564 C CB  . GLN D 4 56  ? 14.05000  21.96800  -10.36600 1.000 87.04728  ? 56  GLN G CB  1 
ATOM   3565 N N   . GLU D 4 57  ? 12.65300  20.85600  -13.49900 1.000 79.32004  ? 57  GLU G N   1 
ATOM   3566 C CA  . GLU D 4 57  ? 11.39100  20.44300  -14.10100 1.000 78.43309  ? 57  GLU G CA  1 
ATOM   3567 C C   . GLU D 4 57  ? 11.51500  20.69100  -15.59500 1.000 77.22768  ? 57  GLU G C   1 
ATOM   3568 O O   . GLU D 4 57  ? 12.46700  21.33100  -16.05200 1.000 77.44876  ? 57  GLU G O   1 
ATOM   3569 C CB  . GLU D 4 57  ? 10.20400  21.21600  -13.51800 1.000 78.88577  ? 57  GLU G CB  1 
ATOM   3570 C CG  . GLU D 4 57  ? 10.43800  22.72600  -13.44400 1.000 78.81998  ? 57  GLU G CG  1 
ATOM   3571 C CD  . GLU D 4 57  ? 9.19300   23.54100  -13.76200 1.000 78.78839  ? 57  GLU G CD  1 
ATOM   3572 O OE1 . GLU D 4 57  ? 8.28000   23.60800  -12.90600 1.000 79.14370  ? 57  GLU G OE1 1 
ATOM   3573 O OE2 . GLU D 4 57  ? 9.12900   24.11100  -14.88000 1.000 78.04620  ? 57  GLU G OE2 1 
ATOM   3574 N N   . SER D 4 58  ? 10.54000  20.19100  -16.35600 1.000 56.04093  ? 58  SER G N   1 
ATOM   3575 C CA  . SER D 4 58  ? 10.51300  20.45300  -17.79300 1.000 54.88290  ? 58  SER G CA  1 
ATOM   3576 C C   . SER D 4 58  ? 10.61300  21.95300  -18.06700 1.000 55.31453  ? 58  SER G C   1 
ATOM   3577 O O   . SER D 4 58  ? 10.23500  22.78200  -17.23600 1.000 56.00145  ? 58  SER G O   1 
ATOM   3578 C CB  . SER D 4 58  ? 9.22700   19.90800  -18.39900 1.000 52.60894  ? 58  SER G CB  1 
ATOM   3579 O OG  . SER D 4 58  ? 8.12500   20.67500  -17.93000 1.000 54.38284  ? 58  SER G OG  1 
ATOM   3580 N N   . PHE D 4 59  ? 11.13200  22.30700  -19.24500 1.000 51.30878  ? 59  PHE G N   1 
ATOM   3581 C CA  . PHE D 4 59  ? 11.33200  23.70400  -19.62900 1.000 50.90347  ? 59  PHE G CA  1 
ATOM   3582 C C   . PHE D 4 59  ? 10.21200  24.12400  -20.57800 1.000 49.98494  ? 59  PHE G C   1 
ATOM   3583 O O   . PHE D 4 59  ? 10.18300  23.70600  -21.74000 1.000 47.71098  ? 59  PHE G O   1 
ATOM   3584 C CB  . PHE D 4 59  ? 12.70800  23.88900  -20.26300 1.000 49.62437  ? 59  PHE G CB  1 
ATOM   3585 C CG  . PHE D 4 59  ? 12.98200  25.29400  -20.77500 1.000 47.43727  ? 59  PHE G CG  1 
ATOM   3586 C CD1 . PHE D 4 59  ? 12.56700  26.41200  -20.06100 1.000 49.29538  ? 59  PHE G CD1 1 
ATOM   3587 C CD2 . PHE D 4 59  ? 13.67400  25.47900  -21.95700 1.000 44.09213  ? 59  PHE G CD2 1 
ATOM   3588 C CE1 . PHE D 4 59  ? 12.84700  27.70800  -20.52400 1.000 48.44265  ? 59  PHE G CE1 1 
ATOM   3589 C CE2 . PHE D 4 59  ? 13.95700  26.75200  -22.43400 1.000 43.56838  ? 59  PHE G CE2 1 
ATOM   3590 C CZ  . PHE D 4 59  ? 13.53800  27.87700  -21.72100 1.000 45.71864  ? 59  PHE G CZ  1 
ATOM   3591 N N   . ASN D 4 60  ? 9.29700   24.95500  -20.08300 1.000 55.13029  ? 60  ASN G N   1 
ATOM   3592 C CA  . ASN D 4 60  ? 8.13600   25.39100  -20.84700 1.000 54.18281  ? 60  ASN G CA  1 
ATOM   3593 C C   . ASN D 4 60  ? 8.46400   26.73900  -21.49000 1.000 53.32745  ? 60  ASN G C   1 
ATOM   3594 O O   . ASN D 4 60  ? 8.58100   27.75600  -20.80000 1.000 54.19597  ? 60  ASN G O   1 
ATOM   3595 C CB  . ASN D 4 60  ? 6.89300   25.47600  -19.96000 1.000 55.12766  ? 60  ASN G CB  1 
ATOM   3596 C CG  . ASN D 4 60  ? 5.58800   25.50400  -20.77100 1.000 55.62509  ? 60  ASN G CG  1 
ATOM   3597 O OD1 . ASN D 4 60  ? 5.60000   25.76700  -21.98100 1.000 54.44863  ? 60  ASN G OD1 1 
ATOM   3598 N ND2 . ASN D 4 60  ? 4.45700   25.22700  -20.10400 1.000 56.62521  ? 60  ASN G ND2 1 
ATOM   3599 N N   . MET D 4 61  ? 8.61300   26.74200  -22.80700 1.000 59.00707  ? 61  MET G N   1 
ATOM   3600 C CA  . MET D 4 61  ? 8.86300   27.96400  -23.56000 1.000 57.98853  ? 61  MET G CA  1 
ATOM   3601 C C   . MET D 4 61  ? 7.51800   28.52700  -24.00000 1.000 58.38858  ? 61  MET G C   1 
ATOM   3602 O O   . MET D 4 61  ? 6.83600   27.94300  -24.84700 1.000 58.35963  ? 61  MET G O   1 
ATOM   3603 C CB  . MET D 4 61  ? 9.76900   27.68300  -24.75600 1.000 55.24347  ? 61  MET G CB  1 
ATOM   3604 C CG  . MET D 4 61  ? 11.02900  26.90200  -24.41200 1.000 54.08543  ? 61  MET G CG  1 
ATOM   3605 S SD  . MET D 4 61  ? 12.08900  26.58800  -25.85200 1.000 50.26919  ? 61  MET G SD  1 
ATOM   3606 C CE  . MET D 4 61  ? 11.88200  24.85000  -26.11900 1.000 48.64267  ? 61  MET G CE  1 
ATOM   3607 N N   . SER D 4 62  ? 7.13800   29.65300  -23.43000 1.000 45.17647  ? 62  SER G N   1 
ATOM   3608 C CA  . SER D 4 62  ? 5.80600   30.19200  -23.66900 1.000 45.75285  ? 62  SER G CA  1 
ATOM   3609 C C   . SER D 4 62  ? 5.72000   31.63300  -23.19600 1.000 46.22396  ? 62  SER G C   1 
ATOM   3610 O O   . SER D 4 62  ? 6.05300   31.91700  -22.04100 1.000 46.95037  ? 62  SER G O   1 
ATOM   3611 C CB  . SER D 4 62  ? 4.74400   29.36300  -22.94300 1.000 47.33199  ? 62  SER G CB  1 
ATOM   3612 O OG  . SER D 4 62  ? 3.47200   29.95800  -23.09800 1.000 47.73730  ? 62  SER G OG  1 
ATOM   3613 N N   . PRO D 4 63  ? 5.28600   32.57000  -24.05400 1.000 47.08196  ? 63  PRO G N   1 
ATOM   3614 C CA  . PRO D 4 63  ? 5.05700   32.31100  -25.48100 1.000 46.06342  ? 63  PRO G CA  1 
ATOM   3615 C C   . PRO D 4 63  ? 6.36700   32.11300  -26.23100 1.000 44.81064  ? 63  PRO G C   1 
ATOM   3616 O O   . PRO D 4 63  ? 7.39200   32.69000  -25.85800 1.000 44.53955  ? 63  PRO G O   1 
ATOM   3617 C CB  . PRO D 4 63  ? 4.33700   33.57600  -25.96400 1.000 46.20028  ? 63  PRO G CB  1 
ATOM   3618 C CG  . PRO D 4 63  ? 4.69500   34.61400  -24.96200 1.000 47.05564  ? 63  PRO G CG  1 
ATOM   3619 C CD  . PRO D 4 63  ? 4.79700   33.89500  -23.65500 1.000 47.97680  ? 63  PRO G CD  1 
ATOM   3620 N N   . VAL D 4 64  ? 6.33700   31.28800  -27.27000 1.000 37.52292  ? 64  VAL G N   1 
ATOM   3621 C CA  . VAL D 4 64  ? 7.54100   31.02100  -28.03800 1.000 35.38582  ? 64  VAL G CA  1 
ATOM   3622 C C   . VAL D 4 64  ? 7.95400   32.29000  -28.77200 1.000 35.34898  ? 64  VAL G C   1 
ATOM   3623 O O   . VAL D 4 64  ? 7.11000   33.00100  -29.32500 1.000 36.17013  ? 64  VAL G O   1 
ATOM   3624 C CB  . VAL D 4 64  ? 7.30100   29.84400  -28.99300 1.000 34.38044  ? 64  VAL G CB  1 
ATOM   3625 C CG1 . VAL D 4 64  ? 8.40300   29.73600  -30.02800 1.000 32.31966  ? 64  VAL G CG1 1 
ATOM   3626 C CG2 . VAL D 4 64  ? 7.21500   28.54100  -28.19600 1.000 35.15948  ? 64  VAL G CG2 1 
ATOM   3627 N N   . THR D 4 65  ? 9.24600   32.60800  -28.73100 1.000 43.03674  ? 65  THR G N   1 
ATOM   3628 C CA  . THR D 4 65  ? 9.85200   33.66600  -29.52700 1.000 43.72893  ? 65  THR G CA  1 
ATOM   3629 C C   . THR D 4 65  ? 10.87400  33.05000  -30.47600 1.000 42.56563  ? 65  THR G C   1 
ATOM   3630 O O   . THR D 4 65  ? 11.23200  31.87500  -30.35500 1.000 40.84174  ? 65  THR G O   1 
ATOM   3631 C CB  . THR D 4 65  ? 10.55800  34.73200  -28.66300 1.000 46.20291  ? 65  THR G CB  1 
ATOM   3632 O OG1 . THR D 4 65  ? 11.79600  34.20600  -28.15400 1.000 44.96329  ? 65  THR G OG1 1 
ATOM   3633 C CG2 . THR D 4 65  ? 9.66700   35.22700  -27.51300 1.000 47.70046  ? 65  THR G CG2 1 
ATOM   3634 N N   . THR D 4 66  ? 11.38200  33.87600  -31.40400 1.000 40.26272  ? 66  THR G N   1 
ATOM   3635 C CA  . THR D 4 66  ? 12.43600  33.40500  -32.29700 1.000 39.75477  ? 66  THR G CA  1 
ATOM   3636 C C   . THR D 4 66  ? 13.70400  33.05400  -31.52600 1.000 39.31524  ? 66  THR G C   1 
ATOM   3637 O O   . THR D 4 66  ? 14.47400  32.19000  -31.96400 1.000 38.42040  ? 66  THR G O   1 
ATOM   3638 C CB  . THR D 4 66  ? 12.75600  34.45200  -33.38200 1.000 41.54972  ? 66  THR G CB  1 
ATOM   3639 O OG1 . THR D 4 66  ? 13.47500  35.56100  -32.81400 1.000 43.06832  ? 66  THR G OG1 1 
ATOM   3640 C CG2 . THR D 4 66  ? 11.47200  34.95000  -34.06800 1.000 42.38666  ? 66  THR G CG2 1 
ATOM   3641 N N   . ALA D 4 67  ? 13.94400  33.70200  -30.37700 1.000 41.39444  ? 67  ALA G N   1 
ATOM   3642 C CA  . ALA D 4 67  ? 15.12900  33.35000  -29.59500 1.000 40.63908  ? 67  ALA G CA  1 
ATOM   3643 C C   . ALA D 4 67  ? 15.05900  31.91200  -29.07500 1.000 39.33893  ? 67  ALA G C   1 
ATOM   3644 O O   . ALA D 4 67  ? 16.10100  31.32500  -28.77500 1.000 38.42829  ? 67  ALA G O   1 
ATOM   3645 C CB  . ALA D 4 67  ? 15.33600  34.35200  -28.44200 1.000 43.18413  ? 67  ALA G CB  1 
ATOM   3646 N N   . HIS D 4 68  ? 13.86500  31.30800  -29.02200 1.000 39.09153  ? 68  HIS G N   1 
ATOM   3647 C CA  . HIS D 4 68  ? 13.74800  29.91100  -28.60100 1.000 37.30710  ? 68  HIS G CA  1 
ATOM   3648 C C   . HIS D 4 68  ? 14.18900  28.93100  -29.68200 1.000 36.44911  ? 68  HIS G C   1 
ATOM   3649 O O   . HIS D 4 68  ? 14.48100  27.76900  -29.36700 1.000 35.40161  ? 68  HIS G O   1 
ATOM   3650 C CB  . HIS D 4 68  ? 12.30400  29.58800  -28.19000 1.000 37.51502  ? 68  HIS G CB  1 
ATOM   3651 C CG  . HIS D 4 68  ? 11.91000  30.19500  -26.87700 1.000 39.61528  ? 68  HIS G CG  1 
ATOM   3652 N ND1 . HIS D 4 68  ? 10.71900  30.85900  -26.69000 1.000 41.21284  ? 68  HIS G ND1 1 
ATOM   3653 C CD2 . HIS D 4 68  ? 12.56000  30.25400  -25.69200 1.000 40.77068  ? 68  HIS G CD2 1 
ATOM   3654 C CE1 . HIS D 4 68  ? 10.65500  31.30900  -25.44900 1.000 43.07885  ? 68  HIS G CE1 1 
ATOM   3655 N NE2 . HIS D 4 68  ? 11.76000  30.95500  -24.82300 1.000 42.91304  ? 68  HIS G NE2 1 
ATOM   3656 N N   . ALA D 4 69  ? 14.23200  29.35600  -30.94400 1.000 36.55175  ? 69  ALA G N   1 
ATOM   3657 C CA  . ALA D 4 69  ? 14.59700  28.43400  -32.01300 1.000 36.57017  ? 69  ALA G CA  1 
ATOM   3658 C C   . ALA D 4 69  ? 16.04900  28.01300  -31.84600 1.000 37.18341  ? 69  ALA G C   1 
ATOM   3659 O O   . ALA D 4 69  ? 16.91700  28.83100  -31.53500 1.000 37.52555  ? 69  ALA G O   1 
ATOM   3660 C CB  . ALA D 4 69  ? 14.38600  29.08100  -33.38500 1.000 38.52830  ? 69  ALA G CB  1 
ATOM   3661 N N   . GLY D 4 70  ? 16.31300  26.73000  -32.03700 1.000 37.76505  ? 70  GLY G N   1 
ATOM   3662 C CA  . GLY D 4 70  ? 17.67200  26.25100  -31.90200 1.000 38.49146  ? 70  GLY G CA  1 
ATOM   3663 C C   . GLY D 4 70  ? 17.71600  24.74100  -31.78800 1.000 39.38893  ? 70  GLY G C   1 
ATOM   3664 O O   . GLY D 4 70  ? 16.69600  24.04600  -31.83900 1.000 39.13890  ? 70  GLY G O   1 
ATOM   3665 N N   . ASN D 4 71  ? 18.93600  24.24900  -31.65200 1.000 36.39647  ? 71  ASN G N   1 
ATOM   3666 C CA  . ASN D 4 71  ? 19.24600  22.82500  -31.70000 1.000 38.74938  ? 71  ASN G CA  1 
ATOM   3667 C C   . ASN D 4 71  ? 19.77400  22.45700  -30.31900 1.000 37.44660  ? 71  ASN G C   1 
ATOM   3668 O O   . ASN D 4 71  ? 20.88800  22.85200  -29.94900 1.000 37.95981  ? 71  ASN G O   1 
ATOM   3669 C CB  . ASN D 4 71  ? 20.25100  22.55300  -32.82000 1.000 41.59183  ? 71  ASN G CB  1 
ATOM   3670 C CG  . ASN D 4 71  ? 20.65100  21.09500  -32.93800 1.000 44.32110  ? 71  ASN G CG  1 
ATOM   3671 O OD1 . ASN D 4 71  ? 20.29600  20.25900  -32.10700 1.000 45.25806  ? 71  ASN G OD1 1 
ATOM   3672 N ND2 . ASN D 4 71  ? 21.42000  20.78900  -33.98300 1.000 45.75812  ? 71  ASN G ND2 1 
ATOM   3673 N N   . TYR D 4 72  ? 18.96600  21.72300  -29.55800 1.000 44.97118  ? 72  TYR G N   1 
ATOM   3674 C CA  . TYR D 4 72  ? 19.16200  21.53800  -28.12800 1.000 43.28151  ? 72  TYR G CA  1 
ATOM   3675 C C   . TYR D 4 72  ? 19.65700  20.13700  -27.78500 1.000 45.37649  ? 72  TYR G C   1 
ATOM   3676 O O   . TYR D 4 72  ? 19.32400  19.16000  -28.45900 1.000 48.22683  ? 72  TYR G O   1 
ATOM   3677 C CB  . TYR D 4 72  ? 17.85100  21.77800  -27.36900 1.000 39.74687  ? 72  TYR G CB  1 
ATOM   3678 C CG  . TYR D 4 72  ? 17.36900  23.20900  -27.36200 1.000 38.37039  ? 72  TYR G CG  1 
ATOM   3679 C CD1 . TYR D 4 72  ? 16.62900  23.72000  -28.42300 1.000 38.63621  ? 72  TYR G CD1 1 
ATOM   3680 C CD2 . TYR D 4 72  ? 17.61700  24.02900  -26.27900 1.000 38.64148  ? 72  TYR G CD2 1 
ATOM   3681 C CE1 . TYR D 4 72  ? 16.17800  25.04600  -28.42200 1.000 38.28091  ? 72  TYR G CE1 1 
ATOM   3682 C CE2 . TYR D 4 72  ? 17.17500  25.35700  -26.26100 1.000 39.56527  ? 72  TYR G CE2 1 
ATOM   3683 C CZ  . TYR D 4 72  ? 16.45300  25.85400  -27.33500 1.000 38.84676  ? 72  TYR G CZ  1 
ATOM   3684 O OH  . TYR D 4 72  ? 16.00100  27.14900  -27.30500 1.000 39.21786  ? 72  TYR G OH  1 
ATOM   3685 N N   . THR D 4 73  ? 20.43800  20.05200  -26.70400 1.000 42.79724  ? 73  THR G N   1 
ATOM   3686 C CA  . THR D 4 73  ? 20.69600  18.79700  -26.00900 1.000 44.28163  ? 73  THR G CA  1 
ATOM   3687 C C   . THR D 4 73  ? 20.62000  19.05800  -24.51200 1.000 41.93134  ? 73  THR G C   1 
ATOM   3688 O O   . THR D 4 73  ? 20.82400  20.18600  -24.05100 1.000 41.28127  ? 73  THR G O   1 
ATOM   3689 C CB  . THR D 4 73  ? 22.06600  18.18400  -26.35900 1.000 48.56898  ? 73  THR G CB  1 
ATOM   3690 O OG1 . THR D 4 73  ? 23.09600  19.16200  -26.15700 1.000 48.42686  ? 73  THR G OG1 1 
ATOM   3691 C CG2 . THR D 4 73  ? 22.10600  17.69200  -27.79700 1.000 52.48524  ? 73  THR G CG2 1 
ATOM   3692 N N   . CYS D 4 74  ? 20.31600  18.00900  -23.74900 1.000 39.29682  ? 74  CYS G N   1 
ATOM   3693 C CA  . CYS D 4 74  ? 20.30900  18.10100  -22.29800 1.000 39.55737  ? 74  CYS G CA  1 
ATOM   3694 C C   . CYS D 4 74  ? 21.27300  17.09300  -21.68400 1.000 42.31297  ? 74  CYS G C   1 
ATOM   3695 O O   . CYS D 4 74  ? 21.64300  16.08700  -22.30100 1.000 43.84210  ? 74  CYS G O   1 
ATOM   3696 C CB  . CYS D 4 74  ? 18.90300  17.87800  -21.70100 1.000 39.79424  ? 74  CYS G CB  1 
ATOM   3697 S SG  . CYS D 4 74  ? 18.27300  16.17500  -21.70600 1.000 41.05492  ? 74  CYS G SG  1 
ATOM   3698 N N   . ARG D 4 75  ? 21.66600  17.39100  -20.44900 1.000 43.78157  ? 75  ARG G N   1 
ATOM   3699 C CA  . ARG D 4 75  ? 22.46300  16.51900  -19.60100 1.000 46.18185  ? 75  ARG G CA  1 
ATOM   3700 C C   . ARG D 4 75  ? 21.79700  16.48800  -18.23700 1.000 47.60044  ? 75  ARG G C   1 
ATOM   3701 O O   . ARG D 4 75  ? 21.43700  17.54100  -17.69600 1.000 47.71098  ? 75  ARG G O   1 
ATOM   3702 C CB  . ARG D 4 75  ? 23.91300  17.01200  -19.46600 1.000 46.87404  ? 75  ARG G CB  1 
ATOM   3703 C CG  . ARG D 4 75  ? 24.68900  17.01800  -20.76700 1.000 47.33199  ? 75  ARG G CG  1 
ATOM   3704 C CD  . ARG D 4 75  ? 26.11900  17.47100  -20.55200 1.000 48.84270  ? 75  ARG G CD  1 
ATOM   3705 N NE  . ARG D 4 75  ? 26.84600  17.51000  -21.81400 1.000 50.76398  ? 75  ARG G NE  1 
ATOM   3706 C CZ  . ARG D 4 75  ? 27.66600  16.55900  -22.24100 1.000 53.06426  ? 75  ARG G CZ  1 
ATOM   3707 N NH1 . ARG D 4 75  ? 27.92500  15.48500  -21.50900 1.000 53.46431  ? 75  ARG G NH1 1 
ATOM   3708 N NH2 . ARG D 4 75  ? 28.25100  16.69400  -23.42900 1.000 54.91185  ? 75  ARG G NH2 1 
ATOM   3709 N N   . GLY D 4 76  ? 21.60000  15.28700  -17.70300 1.000 46.44767  ? 76  GLY G N   1 
ATOM   3710 C CA  . GLY D 4 76  ? 21.01800  15.13900  -16.39100 1.000 48.81638  ? 76  GLY G CA  1 
ATOM   3711 C C   . GLY D 4 76  ? 22.09000  15.00100  -15.32600 1.000 49.99020  ? 76  GLY G C   1 
ATOM   3712 O O   . GLY D 4 76  ? 23.18300  14.51200  -15.58300 1.000 49.79018  ? 76  GLY G O   1 
ATOM   3713 N N   . SER D 4 77  ? 21.75500  15.43500  -14.11700 1.000 56.75417  ? 77  SER G N   1 
ATOM   3714 C CA  . SER D 4 77  ? 22.68500  15.35500  -13.00000 1.000 58.33068  ? 77  SER G CA  1 
ATOM   3715 C C   . SER D 4 77  ? 23.02500  13.90100  -12.68800 1.000 59.57556  ? 77  SER G C   1 
ATOM   3716 O O   . SER D 4 77  ? 22.13400  13.08000  -12.44300 1.000 60.95731  ? 77  SER G O   1 
ATOM   3717 C CB  . SER D 4 77  ? 22.07700  16.04200  -11.77900 1.000 59.80191  ? 77  SER G CB  1 
ATOM   3718 O OG  . SER D 4 77  ? 22.83700  15.78600  -10.61500 1.000 61.48369  ? 77  SER G OG  1 
ATOM   3719 N N   . HIS D 4 78  ? 24.31600  13.57800  -12.71600 1.000 73.31142  ? 78  HIS G N   1 
ATOM   3720 C CA  . HIS D 4 78  ? 24.80400  12.24200  -12.37700 1.000 74.55631  ? 78  HIS G CA  1 
ATOM   3721 C C   . HIS D 4 78  ? 25.86400  12.41100  -11.29600 1.000 76.17229  ? 78  HIS G C   1 
ATOM   3722 O O   . HIS D 4 78  ? 27.02800  12.72100  -11.60600 1.000 75.68276  ? 78  HIS G O   1 
ATOM   3723 C CB  . HIS D 4 78  ? 25.36300  11.51600  -13.59300 1.000 73.27194  ? 78  HIS G CB  1 
ATOM   3724 C CG  . HIS D 4 78  ? 25.67400  10.07500  -13.34000 1.000 74.92477  ? 78  HIS G CG  1 
ATOM   3725 N ND1 . HIS D 4 78  ? 26.48900  9.33200   -14.16600 1.000 74.85634  ? 78  HIS G ND1 1 
ATOM   3726 C CD2 . HIS D 4 78  ? 25.28100  9.23900   -12.34900 1.000 77.46981  ? 78  HIS G CD2 1 
ATOM   3727 C CE1 . HIS D 4 78  ? 26.58600  8.10100   -13.69400 1.000 76.89343  ? 78  HIS G CE1 1 
ATOM   3728 N NE2 . HIS D 4 78  ? 25.86100  8.01700   -12.59300 1.000 77.97777  ? 78  HIS G NE2 1 
ATOM   3729 N N   . PRO D 4 79  ? 25.50300  12.21100  -10.02600 1.000 83.44948  ? 79  PRO G N   1 
ATOM   3730 C CA  . PRO D 4 79  ? 26.34900  12.72100  -8.93600  1.000 84.83649  ? 79  PRO G CA  1 
ATOM   3731 C C   . PRO D 4 79  ? 27.69400  12.02800  -8.79600  1.000 85.96294  ? 79  PRO G C   1 
ATOM   3732 O O   . PRO D 4 79  ? 28.64100  12.64700  -8.29900  1.000 86.98411  ? 79  PRO G O   1 
ATOM   3733 C CB  . PRO D 4 79  ? 25.47300  12.50900  -7.69300  1.000 86.08927  ? 79  PRO G CB  1 
ATOM   3734 C CG  . PRO D 4 79  ? 24.06700  12.47700  -8.23000  1.000 85.87345  ? 79  PRO G CG  1 
ATOM   3735 C CD  . PRO D 4 79  ? 24.18300  11.77400  -9.54400  1.000 84.53645  ? 79  PRO G CD  1 
ATOM   3736 N N   . HIS D 4 80  ? 27.82900  10.77100  -9.19000  1.000 99.24874  ? 80  HIS G N   1 
ATOM   3737 C CA  . HIS D 4 80  ? 29.11200  10.08600  -9.04900  1.000 100.23044 ? 80  HIS G CA  1 
ATOM   3738 C C   . HIS D 4 80  ? 29.61900  9.74800   -10.44700 1.000 99.69880  ? 80  HIS G C   1 
ATOM   3739 O O   . HIS D 4 80  ? 29.22800  8.73500   -11.03500 1.000 99.13820  ? 80  HIS G O   1 
ATOM   3740 C CB  . HIS D 4 80  ? 28.97700  8.86600   -8.14100  1.000 102.35175 ? 80  HIS G CB  1 
ATOM   3741 C CG  . HIS D 4 80  ? 28.77200  9.22300   -6.70200  1.000 104.02037 ? 80  HIS G CG  1 
ATOM   3742 N ND1 . HIS D 4 80  ? 27.66300  9.91000   -6.25900  1.000 103.49662 ? 80  HIS G ND1 1 
ATOM   3743 C CD2 . HIS D 4 80  ? 29.54700  9.01600   -5.61200  1.000 106.94440 ? 80  HIS G CD2 1 
ATOM   3744 C CE1 . HIS D 4 80  ? 27.75600  10.09800  -4.95600  1.000 106.52330 ? 80  HIS G CE1 1 
ATOM   3745 N NE2 . HIS D 4 80  ? 28.88900  9.56400   -4.53800  1.000 108.62881 ? 80  HIS G NE2 1 
ATOM   3746 N N   . SER D 4 81  ? 30.48900  10.61200  -10.95900 1.000 91.79785  ? 81  SER G N   1 
ATOM   3747 C CA  . SER D 4 81  ? 30.88500  10.61700  -12.36000 1.000 91.48202  ? 81  SER G CA  1 
ATOM   3748 C C   . SER D 4 81  ? 31.99000  11.66100  -12.54100 1.000 91.36095  ? 81  SER G C   1 
ATOM   3749 O O   . SER D 4 81  ? 32.10900  12.58300  -11.72700 1.000 91.25568  ? 81  SER G O   1 
ATOM   3750 C CB  . SER D 4 81  ? 29.68800  10.92500  -13.27400 1.000 89.55021  ? 81  SER G CB  1 
ATOM   3751 O OG  . SER D 4 81  ? 29.14500  12.20300  -13.00000 1.000 88.84486  ? 81  SER G OG  1 
ATOM   3752 N N   . PRO D 4 82  ? 32.80200  11.53800  -13.60000 1.000 90.30556  ? 82  PRO G N   1 
ATOM   3753 C CA  . PRO D 4 82  ? 33.94700  12.45700  -13.75200 1.000 91.59519  ? 82  PRO G CA  1 
ATOM   3754 C C   . PRO D 4 82  ? 33.54700  13.88600  -14.06900 1.000 89.92657  ? 82  PRO G C   1 
ATOM   3755 O O   . PRO D 4 82  ? 34.32100  14.80700  -13.77900 1.000 89.96605  ? 82  PRO G O   1 
ATOM   3756 C CB  . PRO D 4 82  ? 34.74700  11.84200  -14.91200 1.000 92.76902  ? 82  PRO G CB  1 
ATOM   3757 C CG  . PRO D 4 82  ? 34.14800  10.47700  -15.14700 1.000 92.32423  ? 82  PRO G CG  1 
ATOM   3758 C CD  . PRO D 4 82  ? 32.73200  10.56700  -14.70300 1.000 90.89511  ? 82  PRO G CD  1 
ATOM   3759 N N   . THR D 4 83  ? 32.37900  14.10300  -14.67300 1.000 80.49123  ? 83  THR G N   1 
ATOM   3760 C CA  . THR D 4 83  ? 31.89400  15.45400  -14.89100 1.000 79.60165  ? 83  THR G CA  1 
ATOM   3761 C C   . THR D 4 83  ? 30.87200  15.88700  -13.85600 1.000 78.77523  ? 83  THR G C   1 
ATOM   3762 O O   . THR D 4 83  ? 30.68400  17.09400  -13.66600 1.000 76.94080  ? 83  THR G O   1 
ATOM   3763 C CB  . THR D 4 83  ? 31.27300  15.58700  -16.28700 1.000 78.30939  ? 83  THR G CB  1 
ATOM   3764 O OG1 . THR D 4 83  ? 30.31500  14.53600  -16.49300 1.000 77.76459  ? 83  THR G OG1 1 
ATOM   3765 C CG2 . THR D 4 83  ? 32.35000  15.53400  -17.36900 1.000 79.60428  ? 83  THR G CG2 1 
ATOM   3766 N N   . GLY D 4 84  ? 30.23600  14.93500  -13.16900 1.000 80.03065  ? 84  GLY G N   1 
ATOM   3767 C CA  . GLY D 4 84  ? 29.05100  15.20400  -12.38300 1.000 80.15435  ? 84  GLY G CA  1 
ATOM   3768 C C   . GLY D 4 84  ? 27.76300  15.19600  -13.17900 1.000 78.78576  ? 84  GLY G C   1 
ATOM   3769 O O   . GLY D 4 84  ? 26.69100  15.41700  -12.60100 1.000 78.53836  ? 84  GLY G O   1 
ATOM   3770 N N   . TRP D 4 85  ? 27.83400  14.94800  -14.48600 1.000 67.82919  ? 85  TRP G N   1 
ATOM   3771 C CA  . TRP D 4 85  ? 26.68400  15.05800  -15.36400 1.000 66.07371  ? 85  TRP G CA  1 
ATOM   3772 C C   . TRP D 4 85  ? 26.74300  13.95600  -16.41100 1.000 66.25005  ? 85  TRP G C   1 
ATOM   3773 O O   . TRP D 4 85  ? 27.79700  13.37600  -16.68100 1.000 67.03172  ? 85  TRP G O   1 
ATOM   3774 C CB  . TRP D 4 85  ? 26.61600  16.44600  -16.02000 1.000 64.77619  ? 85  TRP G CB  1 
ATOM   3775 C CG  . TRP D 4 85  ? 26.37600  17.52900  -15.00700 1.000 65.13149  ? 85  TRP G CG  1 
ATOM   3776 C CD1 . TRP D 4 85  ? 27.29800  18.10200  -14.18500 1.000 66.44744  ? 85  TRP G CD1 1 
ATOM   3777 C CD2 . TRP D 4 85  ? 25.12400  18.14100  -14.69200 1.000 64.75250  ? 85  TRP G CD2 1 
ATOM   3778 N NE1 . TRP D 4 85  ? 26.70000  19.03900  -13.37600 1.000 65.78157  ? 85  TRP G NE1 1 
ATOM   3779 C CE2 . TRP D 4 85  ? 25.36500  19.08500  -13.67300 1.000 65.58418  ? 85  TRP G CE2 1 
ATOM   3780 C CE3 . TRP D 4 85  ? 23.82300  17.98500  -15.17500 1.000 63.57078  ? 85  TRP G CE3 1 
ATOM   3781 C CZ2 . TRP D 4 85  ? 24.35600  19.86500  -13.12900 1.000 65.60787  ? 85  TRP G CZ2 1 
ATOM   3782 C CZ3 . TRP D 4 85  ? 22.82400  18.76700  -14.64100 1.000 64.13664  ? 85  TRP G CZ3 1 
ATOM   3783 C CH2 . TRP D 4 85  ? 23.09600  19.69400  -13.62500 1.000 65.58944  ? 85  TRP G CH2 1 
ATOM   3784 N N   . SER D 4 86  ? 25.58100  13.67200  -16.98900 1.000 45.38176  ? 86  SER G N   1 
ATOM   3785 C CA  . SER D 4 86  ? 25.41500  12.58700  -17.93200 1.000 45.01066  ? 86  SER G CA  1 
ATOM   3786 C C   . SER D 4 86  ? 26.00500  12.96000  -19.28300 1.000 44.78695  ? 86  SER G C   1 
ATOM   3787 O O   . SER D 4 86  ? 26.33400  14.11900  -19.55400 1.000 44.28163  ? 86  SER G O   1 
ATOM   3788 C CB  . SER D 4 86  ? 23.93600  12.25900  -18.10700 1.000 43.98159  ? 86  SER G CB  1 
ATOM   3789 O OG  . SER D 4 86  ? 23.31700  13.24000  -18.92400 1.000 42.42088  ? 86  SER G OG  1 
ATOM   3790 N N   . ALA D 4 87  ? 26.09400  11.96200  -20.15600 1.000 48.08998  ? 87  ALA G N   1 
ATOM   3791 C CA  . ALA D 4 87  ? 26.36100  12.24800  -21.55000 1.000 49.47698  ? 87  ALA G CA  1 
ATOM   3792 C C   . ALA D 4 87  ? 25.24200  13.11300  -22.12200 1.000 48.26368  ? 87  ALA G C   1 
ATOM   3793 O O   . ALA D 4 87  ? 24.15500  13.25000  -21.54100 1.000 45.38439  ? 87  ALA G O   1 
ATOM   3794 C CB  . ALA D 4 87  ? 26.49200  10.95400  -22.35500 1.000 51.05349  ? 87  ALA G CB  1 
ATOM   3795 N N   . ALA D 4 88  ? 25.53000  13.71100  -23.27300 1.000 48.52424  ? 88  ALA G N   1 
ATOM   3796 C CA  . ALA D 4 88  ? 24.54700  14.53000  -23.95900 1.000 47.18724  ? 88  ALA G CA  1 
ATOM   3797 C C   . ALA D 4 88  ? 23.41800  13.66900  -24.52000 1.000 47.18460  ? 88  ALA G C   1 
ATOM   3798 O O   . ALA D 4 88  ? 23.63900  12.55100  -24.99600 1.000 48.62425  ? 88  ALA G O   1 
ATOM   3799 C CB  . ALA D 4 88  ? 25.21400  15.32000  -25.08500 1.000 48.79796  ? 88  ALA G CB  1 
ATOM   3800 N N   . SER D 4 89  ? 22.20400  14.21100  -24.46200 1.000 43.32098  ? 89  SER G N   1 
ATOM   3801 C CA  . SER D 4 89  ? 21.00900  13.57100  -24.98000 1.000 42.34455  ? 89  SER G CA  1 
ATOM   3802 C C   . SER D 4 89  ? 20.97000  13.61800  -26.50700 1.000 44.42638  ? 89  SER G C   1 
ATOM   3803 O O   . SER D 4 89  ? 21.75300  14.31400  -27.16700 1.000 47.29251  ? 89  SER G O   1 
ATOM   3804 C CB  . SER D 4 89  ? 19.76100  14.26100  -24.43700 1.000 37.95455  ? 89  SER G CB  1 
ATOM   3805 O OG  . SER D 4 89  ? 19.65300  15.57700  -24.95000 1.000 36.25171  ? 89  SER G OG  1 
ATOM   3806 N N   . ASN D 4 90  ? 20.02800  12.86600  -27.06100 1.000 42.26559  ? 90  ASN G N   1 
ATOM   3807 C CA  . ASN D 4 90  ? 19.65600  13.05500  -28.45200 1.000 42.59721  ? 90  ASN G CA  1 
ATOM   3808 C C   . ASN D 4 90  ? 19.34000  14.52900  -28.69900 1.000 42.24191  ? 90  ASN G C   1 
ATOM   3809 O O   . ASN D 4 90  ? 18.78200  15.19600  -27.82000 1.000 39.13101  ? 90  ASN G O   1 
ATOM   3810 C CB  . ASN D 4 90  ? 18.42700  12.21700  -28.78800 1.000 39.71266  ? 90  ASN G CB  1 
ATOM   3811 C CG  . ASN D 4 90  ? 17.30300  12.49800  -27.84700 1.000 36.56228  ? 90  ASN G CG  1 
ATOM   3812 O OD1 . ASN D 4 90  ? 17.51100  12.52000  -26.63100 1.000 36.00432  ? 90  ASN G OD1 1 
ATOM   3813 N ND2 . ASN D 4 90  ? 16.11900  12.76600  -28.38000 1.000 33.88038  ? 90  ASN G ND2 1 
ATOM   3814 N N   . PRO D 4 91  ? 19.64700  15.05600  -29.87900 1.000 44.13161  ? 91  PRO G N   1 
ATOM   3815 C CA  . PRO D 4 91  ? 19.36600  16.47200  -30.15900 1.000 43.66576  ? 91  PRO G CA  1 
ATOM   3816 C C   . PRO D 4 91  ? 17.93400  16.70500  -30.61900 1.000 40.51012  ? 91  PRO G C   1 
ATOM   3817 O O   . PRO D 4 91  ? 17.38800  15.95400  -31.42700 1.000 39.30208  ? 91  PRO G O   1 
ATOM   3818 C CB  . PRO D 4 91  ? 20.35800  16.79500  -31.27600 1.000 44.96855  ? 91  PRO G CB  1 
ATOM   3819 C CG  . PRO D 4 91  ? 20.50600  15.48100  -32.01100 1.000 44.72378  ? 91  PRO G CG  1 
ATOM   3820 C CD  . PRO D 4 91  ? 20.42300  14.40600  -30.95300 1.000 44.83959  ? 91  PRO G CD  1 
ATOM   3821 N N   . VAL D 4 92  ? 17.32700  17.77700  -30.11600 1.000 37.50450  ? 92  VAL G N   1 
ATOM   3822 C CA  . VAL D 4 92  ? 15.99200  18.19300  -30.53600 1.000 35.30423  ? 92  VAL G CA  1 
ATOM   3823 C C   . VAL D 4 92  ? 16.07100  19.61600  -31.07800 1.000 34.26463  ? 92  VAL G C   1 
ATOM   3824 O O   . VAL D 4 92  ? 16.60500  20.51300  -30.41000 1.000 35.14369  ? 92  VAL G O   1 
ATOM   3825 C CB  . VAL D 4 92  ? 14.97000  18.10700  -29.38700 1.000 35.47531  ? 92  VAL G CB  1 
ATOM   3826 C CG1 . VAL D 4 92  ? 13.64600  18.69600  -29.81600 1.000 33.49612  ? 92  VAL G CG1 1 
ATOM   3827 C CG2 . VAL D 4 92  ? 14.77400  16.64100  -28.93100 1.000 37.14393  ? 92  VAL G CG2 1 
ATOM   3828 N N   . VAL D 4 93  ? 15.51700  19.82400  -32.27100 1.000 38.42303  ? 93  VAL G N   1 
ATOM   3829 C CA  . VAL D 4 93  ? 15.61300  21.08900  -33.00300 1.000 37.80453  ? 93  VAL G CA  1 
ATOM   3830 C C   . VAL D 4 93  ? 14.26500  21.79400  -32.91000 1.000 36.85179  ? 93  VAL G C   1 
ATOM   3831 O O   . VAL D 4 93  ? 13.26100  21.32600  -33.46400 1.000 35.98063  ? 93  VAL G O   1 
ATOM   3832 C CB  . VAL D 4 93  ? 16.02500  20.86200  -34.46400 1.000 36.76493  ? 93  VAL G CB  1 
ATOM   3833 C CG1 . VAL D 4 93  ? 16.01000  22.15400  -35.25200 1.000 36.03853  ? 93  VAL G CG1 1 
ATOM   3834 C CG2 . VAL D 4 93  ? 17.41700  20.19000  -34.53900 1.000 37.40975  ? 93  VAL G CG2 1 
ATOM   3835 N N   . ILE D 4 94  ? 14.21600  22.90600  -32.18900 1.000 34.18831  ? 94  ILE G N   1 
ATOM   3836 C CA  . ILE D 4 94  ? 12.99700  23.69800  -32.11100 1.000 33.41453  ? 94  ILE G CA  1 
ATOM   3837 C C   . ILE D 4 94  ? 12.99800  24.65000  -33.30400 1.000 32.53548  ? 94  ILE G C   1 
ATOM   3838 O O   . ILE D 4 94  ? 13.90800  25.47500  -33.45300 1.000 32.70918  ? 94  ILE G O   1 
ATOM   3839 C CB  . ILE D 4 94  ? 12.90100  24.46700  -30.78700 1.000 34.14620  ? 94  ILE G CB  1 
ATOM   3840 C CG1 . ILE D 4 94  ? 12.98200  23.51300  -29.58600 1.000 35.19369  ? 94  ILE G CG1 1 
ATOM   3841 C CG2 . ILE D 4 94  ? 11.60700  25.27100  -30.73400 1.000 34.64889  ? 94  ILE G CG2 1 
ATOM   3842 C CD1 . ILE D 4 94  ? 11.81600  22.55700  -29.51300 1.000 35.17001  ? 94  ILE G CD1 1 
ATOM   3843 N N   . MET D 4 95  ? 11.98900  24.52600  -34.15800 1.000 42.44193  ? 95  MET G N   1 
ATOM   3844 C CA  . MET D 4 95  ? 11.84400  25.37200  -35.33200 1.000 41.68921  ? 95  MET G CA  1 
ATOM   3845 C C   . MET D 4 95  ? 10.65800  26.29000  -35.09800 1.000 42.06820  ? 95  MET G C   1 
ATOM   3846 O O   . MET D 4 95  ? 9.54300   25.82000  -34.85800 1.000 42.20506  ? 95  MET G O   1 
ATOM   3847 C CB  . MET D 4 95  ? 11.64800  24.53400  -36.59000 1.000 40.13376  ? 95  MET G CB  1 
ATOM   3848 C CG  . MET D 4 95  ? 12.70200  23.47200  -36.78600 1.000 40.93122  ? 95  MET G CG  1 
ATOM   3849 S SD  . MET D 4 95  ? 12.43800  22.64200  -38.36500 1.000 39.84951  ? 95  MET G SD  1 
ATOM   3850 C CE  . MET D 4 95  ? 13.72900  21.38700  -38.33700 1.000 40.62856  ? 95  MET G CE  1 
ATOM   3851 N N   . VAL D 4 96  ? 10.90300  27.59400  -35.14700 1.000 32.69076  ? 96  VAL G N   1 
ATOM   3852 C CA  . VAL D 4 96  ? 9.87900   28.58600  -34.84800 1.000 33.49875  ? 96  VAL G CA  1 
ATOM   3853 C C   . VAL D 4 96  ? 9.36600   29.13800  -36.17000 1.000 32.45915  ? 96  VAL G C   1 
ATOM   3854 O O   . VAL D 4 96  ? 10.15400  29.62100  -36.99500 1.000 31.67748  ? 96  VAL G O   1 
ATOM   3855 C CB  . VAL D 4 96  ? 10.43800  29.69100  -33.94000 1.000 35.00157  ? 96  VAL G CB  1 
ATOM   3856 C CG1 . VAL D 4 96  ? 9.42300   30.82100  -33.77100 1.000 35.33318  ? 96  VAL G CG1 1 
ATOM   3857 C CG2 . VAL D 4 96  ? 10.82500  29.09100  -32.59000 1.000 36.06222  ? 96  VAL G CG2 1 
ATOM   3858 N N   . THR D 4 97  ? 8.05900   29.06300  -36.38500 1.000 32.41441  ? 97  THR G N   1 
ATOM   3859 C CA  . THR D 4 97  ? 7.46400   29.44600  -37.65900 1.000 30.58525  ? 97  THR G CA  1 
ATOM   3860 C C   . THR D 4 97  ? 6.81300   30.81800  -37.55200 1.000 30.66420  ? 97  THR G C   1 
ATOM   3861 O O   . THR D 4 97  ? 6.60500   31.35200  -36.46100 1.000 31.60116  ? 97  THR G O   1 
ATOM   3862 C CB  . THR D 4 97  ? 6.41500   28.42400  -38.12000 1.000 29.20350  ? 97  THR G CB  1 
ATOM   3863 O OG1 . THR D 4 97  ? 5.22800   28.56200  -37.32600 1.000 28.92715  ? 97  THR G OG1 1 
ATOM   3864 C CG2 . THR D 4 97  ? 6.96000   26.97400  -38.01400 1.000 29.33246  ? 97  THR G CG2 1 
ATOM   3865 N N   . GLY D 4 98  ? 6.44500   31.35400  -38.70600 1.000 35.43583  ? 98  GLY G N   1 
ATOM   3866 C CA  . GLY D 4 98  ? 5.79400   32.64100  -38.78900 1.000 35.26739  ? 98  GLY G CA  1 
ATOM   3867 C C   . GLY D 4 98  ? 6.71200   33.81800  -39.02800 1.000 36.15697  ? 98  GLY G C   1 
ATOM   3868 O O   . GLY D 4 98  ? 6.33900   34.94400  -38.67200 1.000 36.84126  ? 98  GLY G O   1 
ATOM   3869 N N   . ASN D 4 99  ? 7.89100   33.61700  -39.62700 1.000 34.68574  ? 99  ASN G N   1 
ATOM   3870 C CA  . ASN D 4 99  ? 8.84500   34.72400  -39.74200 1.000 35.62006  ? 99  ASN G CA  1 
ATOM   3871 C C   . ASN D 4 99  ? 9.08200   35.20400  -41.17500 1.000 34.98314  ? 99  ASN G C   1 
ATOM   3872 O O   . ASN D 4 99  ? 9.87900   36.12400  -41.37500 1.000 35.42793  ? 99  ASN G O   1 
ATOM   3873 C CB  . ASN D 4 99  ? 10.17600  34.33700  -39.08900 1.000 36.40700  ? 99  ASN G CB  1 
ATOM   3874 C CG  . ASN D 4 99  ? 9.98100   33.73800  -37.70000 1.000 37.13866  ? 99  ASN G CG  1 
ATOM   3875 O OD1 . ASN D 4 99  ? 9.62300   34.44500  -36.76100 1.000 37.82032  ? 99  ASN G OD1 1 
ATOM   3876 N ND2 . ASN D 4 99  ? 10.19600  32.42600  -37.57300 1.000 37.18867  ? 99  ASN G ND2 1 
ATOM   3877 N N   . HIS D 4 100 ? 8.42300   34.62000  -42.17000 1.000 35.40951  ? 100 HIS G N   1 
ATOM   3878 C CA  . HIS D 4 100 ? 8.48000   35.13600  -43.53600 1.000 35.41214  ? 100 HIS G CA  1 
ATOM   3879 C C   . HIS D 4 100 ? 7.11900   34.88700  -44.17000 1.000 34.76206  ? 100 HIS G C   1 
ATOM   3880 O O   . HIS D 4 100 ? 6.28300   34.17300  -43.61100 1.000 34.20410  ? 100 HIS G O   1 
ATOM   3881 C CB  . HIS D 4 100 ? 9.58800   34.46300  -44.37800 1.000 35.60690  ? 100 HIS G CB  1 
ATOM   3882 C CG  . HIS D 4 100 ? 10.88900  34.28600  -43.65400 1.000 36.32804  ? 100 HIS G CG  1 
ATOM   3883 N ND1 . HIS D 4 100 ? 11.80600  35.30300  -43.51100 1.000 36.70703  ? 100 HIS G ND1 1 
ATOM   3884 C CD2 . HIS D 4 100 ? 11.42300  33.20900  -43.02600 1.000 36.04116  ? 100 HIS G CD2 1 
ATOM   3885 C CE1 . HIS D 4 100 ? 12.84700  34.86600  -42.82000 1.000 36.87547  ? 100 HIS G CE1 1 
ATOM   3886 N NE2 . HIS D 4 100 ? 12.63900  33.59900  -42.51300 1.000 36.94127  ? 100 HIS G NE2 1 
ATOM   3887 N N   . ARG D 4 101 ? 6.90300   35.46000  -45.34800 1.000 42.23664  ? 101 ARG G N   1 
ATOM   3888 C CA  . ARG D 4 101 ? 5.68900   35.15800  -46.09300 1.000 41.95240  ? 101 ARG G CA  1 
ATOM   3889 C C   . ARG D 4 101 ? 5.63100   33.66300  -46.41900 1.000 41.44181  ? 101 ARG G C   1 
ATOM   3890 O O   . ARG D 4 101 ? 6.65500   32.99700  -46.59000 1.000 41.61815  ? 101 ARG G O   1 
ATOM   3891 C CB  . ARG D 4 101 ? 5.61600   35.99200  -47.37700 1.000 42.65511  ? 101 ARG G CB  1 
ATOM   3892 C CG  . ARG D 4 101 ? 5.66000   37.47200  -47.14100 1.000 44.13161  ? 101 ARG G CG  1 
ATOM   3893 C CD  . ARG D 4 101 ? 4.28500   38.12000  -46.83100 1.000 44.41585  ? 101 ARG G CD  1 
ATOM   3894 N NE  . ARG D 4 101 ? 3.50800   38.44900  -48.02700 1.000 45.76338  ? 101 ARG G NE  1 
ATOM   3895 C CZ  . ARG D 4 101 ? 3.61900   39.57500  -48.72600 1.000 47.21092  ? 101 ARG G CZ  1 
ATOM   3896 N NH1 . ARG D 4 101 ? 4.47000   40.53200  -48.38100 1.000 48.34264  ? 101 ARG G NH1 1 
ATOM   3897 N NH2 . ARG D 4 101 ? 2.84500   39.75700  -49.79800 1.000 47.75836  ? 101 ARG G NH2 1 
ATOM   3898 N N   . LYS D 4 102 ? 4.41900   33.13800  -46.49900 1.000 33.84353  ? 102 LYS G N   1 
ATOM   3899 C CA  . LYS D 4 102 ? 4.31900   31.69400  -46.65400 1.000 33.13555  ? 102 LYS G CA  1 
ATOM   3900 C C   . LYS D 4 102 ? 4.66000   31.28500  -48.07600 1.000 33.94354  ? 102 LYS G C   1 
ATOM   3901 O O   . LYS D 4 102 ? 4.43800   32.04700  -49.01400 1.000 34.53835  ? 102 LYS G O   1 
ATOM   3902 C CB  . LYS D 4 102 ? 2.91600   31.19000  -46.31800 1.000 32.35914  ? 102 LYS G CB  1 
ATOM   3903 C CG  . LYS D 4 102 ? 1.79900   31.73300  -47.20600 1.000 33.27767  ? 102 LYS G CG  1 
ATOM   3904 C CD  . LYS D 4 102 ? 0.50500   31.01200  -46.85600 1.000 32.29598  ? 102 LYS G CD  1 
ATOM   3905 C CE  . LYS D 4 102 ? -0.65200  31.94200  -46.86400 1.000 33.21714  ? 102 LYS G CE  1 
ATOM   3906 N NZ  . LYS D 4 102 ? -1.11300  32.26100  -48.23500 1.000 34.16462  ? 102 LYS G NZ  1 
ATOM   3907 N N   . PRO D 4 103 ? 5.18500   30.08500  -48.25000 1.000 31.80908  ? 103 PRO G N   1 
ATOM   3908 C CA  . PRO D 4 103 ? 5.33200   29.51000  -49.58700 1.000 32.75393  ? 103 PRO G CA  1 
ATOM   3909 C C   . PRO D 4 103 ? 4.01500   28.86200  -50.00300 1.000 32.58285  ? 103 PRO G C   1 
ATOM   3910 O O   . PRO D 4 103 ? 3.02300   28.90600  -49.28600 1.000 31.50904  ? 103 PRO G O   1 
ATOM   3911 C CB  . PRO D 4 103 ? 6.45100   28.49100  -49.40100 1.000 32.58549  ? 103 PRO G CB  1 
ATOM   3912 C CG  . PRO D 4 103 ? 6.30700   28.04500  -47.96900 1.000 31.51430  ? 103 PRO G CG  1 
ATOM   3913 C CD  . PRO D 4 103 ? 5.72500   29.20900  -47.19600 1.000 31.34850  ? 103 PRO G CD  1 
ATOM   3914 N N   . SER D 4 104 ? 4.01100   28.26600  -51.18800 1.000 34.17515  ? 104 SER G N   1 
ATOM   3915 C CA  . SER D 4 104 ? 2.84700   27.55500  -51.68900 1.000 34.80944  ? 104 SER G CA  1 
ATOM   3916 C C   . SER D 4 104 ? 3.16100   26.07200  -51.78800 1.000 35.10158  ? 104 SER G C   1 
ATOM   3917 O O   . SER D 4 104 ? 4.31100   25.68400  -52.01300 1.000 34.92524  ? 104 SER G O   1 
ATOM   3918 C CB  . SER D 4 104 ? 2.41400   28.09700  -53.05200 1.000 36.07275  ? 104 SER G CB  1 
ATOM   3919 O OG  . SER D 4 104 ? 1.98700   29.44100  -52.91700 1.000 35.98326  ? 104 SER G OG  1 
ATOM   3920 N N   . LEU D 4 105 ? 2.12300   25.24300  -51.62200 1.000 32.82236  ? 105 LEU G N   1 
ATOM   3921 C CA  . LEU D 4 105 ? 2.27100   23.79400  -51.60200 1.000 32.68287  ? 105 LEU G CA  1 
ATOM   3922 C C   . LEU D 4 105 ? 1.22100   23.17400  -52.51500 1.000 33.84353  ? 105 LEU G C   1 
ATOM   3923 O O   . LEU D 4 105 ? 0.02800   23.44800  -52.36900 1.000 34.05935  ? 105 LEU G O   1 
ATOM   3924 C CB  . LEU D 4 105 ? 2.12400   23.25200  -50.16800 1.000 29.56144  ? 105 LEU G CB  1 
ATOM   3925 C CG  . LEU D 4 105 ? 2.11300   21.73300  -49.95600 1.000 27.57436  ? 105 LEU G CG  1 
ATOM   3926 C CD1 . LEU D 4 105 ? 3.41000   21.12000  -50.39200 1.000 27.44540  ? 105 LEU G CD1 1 
ATOM   3927 C CD2 . LEU D 4 105 ? 1.84900   21.42800  -48.47300 1.000 24.97668  ? 105 LEU G CD2 1 
ATOM   3928 N N   . LEU D 4 106 ? 1.65300   22.34000  -53.45300 1.000 40.13902  ? 106 LEU G N   1 
ATOM   3929 C CA  . LEU D 4 106 ? 0.70100   21.68400  -54.33400 1.000 41.50234  ? 106 LEU G CA  1 
ATOM   3930 C C   . LEU D 4 106 ? 1.16500   20.25900  -54.59200 1.000 39.87320  ? 106 LEU G C   1 
ATOM   3931 O O   . LEU D 4 106 ? 2.35600   19.94800  -54.50000 1.000 38.10983  ? 106 LEU G O   1 
ATOM   3932 C CB  . LEU D 4 106 ? 0.50900   22.43300  -55.65600 1.000 43.78683  ? 106 LEU G CB  1 
ATOM   3933 C CG  . LEU D 4 106 ? 1.71200   22.53400  -56.58200 1.000 43.93158  ? 106 LEU G CG  1 
ATOM   3934 C CD1 . LEU D 4 106 ? 1.26500   22.97200  -57.98100 1.000 45.31070  ? 106 LEU G CD1 1 
ATOM   3935 C CD2 . LEU D 4 106 ? 2.70100   23.53900  -56.03300 1.000 43.82631  ? 106 LEU G CD2 1 
ATOM   3936 N N   . ALA D 4 107 ? 0.19600   19.39100  -54.87600 1.000 34.42781  ? 107 ALA G N   1 
ATOM   3937 C CA  . ALA D 4 107 ? 0.42300   17.96800  -55.04400 1.000 33.41190  ? 107 ALA G CA  1 
ATOM   3938 C C   . ALA D 4 107 ? 0.40600   17.63800  -56.53100 1.000 35.03578  ? 107 ALA G C   1 
ATOM   3939 O O   . ALA D 4 107 ? -0.43100  18.14900  -57.27400 1.000 36.76757  ? 107 ALA G O   1 
ATOM   3940 C CB  . ALA D 4 107 ? -0.65800  17.16200  -54.30700 1.000 33.61456  ? 107 ALA G CB  1 
ATOM   3941 N N   . HIS D 4 108 ? 1.33400   16.79000  -56.96400 1.000 40.88911  ? 108 HIS G N   1 
ATOM   3942 C CA  . HIS D 4 108 ? 1.39600   16.32800  -58.35000 1.000 41.82607  ? 108 HIS G CA  1 
ATOM   3943 C C   . HIS D 4 108 ? 1.29700   14.80900  -58.37100 1.000 42.18137  ? 108 HIS G C   1 
ATOM   3944 O O   . HIS D 4 108 ? 2.16000   14.13300  -57.78400 1.000 41.23652  ? 108 HIS G O   1 
ATOM   3945 C CB  . HIS D 4 108 ? 2.68500   16.76500  -59.03100 1.000 41.27337  ? 108 HIS G CB  1 
ATOM   3946 C CG  . HIS D 4 108 ? 2.86100   18.24900  -59.10600 1.000 42.11558  ? 108 HIS G CG  1 
ATOM   3947 N ND1 . HIS D 4 108 ? 2.25300   19.02500  -60.07100 1.000 44.08686  ? 108 HIS G ND1 1 
ATOM   3948 C CD2 . HIS D 4 108 ? 3.60100   19.09600  -58.35000 1.000 41.48392  ? 108 HIS G CD2 1 
ATOM   3949 C CE1 . HIS D 4 108 ? 2.60100   20.28800  -59.89800 1.000 43.62628  ? 108 HIS G CE1 1 
ATOM   3950 N NE2 . HIS D 4 108 ? 3.41800   20.35800  -58.86000 1.000 43.49995  ? 108 HIS G NE2 1 
ATOM   3951 N N   . PRO D 4 109 ? 0.30900   14.22200  -59.05400 1.000 42.19190  ? 109 PRO G N   1 
ATOM   3952 C CA  . PRO D 4 109 ? -0.68700  14.93000  -59.86300 1.000 43.41573  ? 109 PRO G CA  1 
ATOM   3953 C C   . PRO D 4 109 ? -1.88000  15.48000  -59.09100 1.000 44.19214  ? 109 PRO G C   1 
ATOM   3954 O O   . PRO D 4 109 ? -2.64600  16.23100  -59.67600 1.000 44.95013  ? 109 PRO G O   1 
ATOM   3955 C CB  . PRO D 4 109 ? -1.15500  13.84800  -60.83700 1.000 45.11330  ? 109 PRO G CB  1 
ATOM   3956 C CG  . PRO D 4 109 ? -1.02700  12.60200  -60.05800 1.000 44.45796  ? 109 PRO G CG  1 
ATOM   3957 C CD  . PRO D 4 109 ? 0.22800   12.76400  -59.25400 1.000 43.07359  ? 109 PRO G CD  1 
ATOM   3958 N N   . GLY D 4 110 ? -2.04800  15.11300  -57.81700 1.000 36.49648  ? 110 GLY G N   1 
ATOM   3959 C CA  . GLY D 4 110 ? -3.20100  15.54100  -57.05500 1.000 37.00180  ? 110 GLY G CA  1 
ATOM   3960 C C   . GLY D 4 110 ? -3.16700  15.01300  -55.63800 1.000 35.80429  ? 110 GLY G C   1 
ATOM   3961 O O   . GLY D 4 110 ? -2.34000  14.16400  -55.29600 1.000 35.63322  ? 110 GLY G O   1 
ATOM   3962 N N   . PRO D 4 111 ? -4.05200  15.51700  -54.77400 1.000 36.17802  ? 111 PRO G N   1 
ATOM   3963 C CA  . PRO D 4 111 ? -4.00100  15.13600  -53.35400 1.000 34.93577  ? 111 PRO G CA  1 
ATOM   3964 C C   . PRO D 4 111 ? -4.68200  13.81300  -53.00600 1.000 36.23329  ? 111 PRO G C   1 
ATOM   3965 O O   . PRO D 4 111 ? -4.55500  13.36500  -51.85600 1.000 36.07538  ? 111 PRO G O   1 
ATOM   3966 C CB  . PRO D 4 111 ? -4.71700  16.30500  -52.66400 1.000 34.14883  ? 111 PRO G CB  1 
ATOM   3967 C CG  . PRO D 4 111 ? -5.73100  16.72600  -53.67500 1.000 35.87535  ? 111 PRO G CG  1 
ATOM   3968 C CD  . PRO D 4 111 ? -5.07500  16.54500  -55.03500 1.000 37.21236  ? 111 PRO G CD  1 
ATOM   3969 N N   . LEU D 4 112 ? -5.39700  13.18000  -53.93700 1.000 43.39468  ? 112 LEU G N   1 
ATOM   3970 C CA  . LEU D 4 112 ? -6.00500  11.86600  -53.72000 1.000 44.65009  ? 112 LEU G CA  1 
ATOM   3971 C C   . LEU D 4 112 ? -5.04700  10.82500  -54.27200 1.000 45.59231  ? 112 LEU G C   1 
ATOM   3972 O O   . LEU D 4 112 ? -4.84700  10.75000  -55.48400 1.000 46.01341  ? 112 LEU G O   1 
ATOM   3973 C CB  . LEU D 4 112 ? -7.36000  11.74200  -54.41500 1.000 45.12646  ? 112 LEU G CB  1 
ATOM   3974 C CG  . LEU D 4 112 ? -8.50100  12.65100  -53.98800 1.000 44.43691  ? 112 LEU G CG  1 
ATOM   3975 C CD1 . LEU D 4 112 ? -9.79500  12.15500  -54.61100 1.000 45.24753  ? 112 LEU G CD1 1 
ATOM   3976 C CD2 . LEU D 4 112 ? -8.60300  12.67500  -52.48100 1.000 43.62365  ? 112 LEU G CD2 1 
ATOM   3977 N N   . VAL D 4 113 ? -4.47400  10.00700  -53.40000 1.000 36.62018  ? 113 VAL G N   1 
ATOM   3978 C CA  . VAL D 4 113 ? -3.34800  9.16100   -53.77100 1.000 35.90957  ? 113 VAL G CA  1 
ATOM   3979 C C   . VAL D 4 113 ? -3.74900  7.70300   -53.59000 1.000 37.02023  ? 113 VAL G C   1 
ATOM   3980 O O   . VAL D 4 113 ? -4.06200  7.28300   -52.47000 1.000 37.12287  ? 113 VAL G O   1 
ATOM   3981 C CB  . VAL D 4 113 ? -2.10500  9.51200   -52.94300 1.000 34.24358  ? 113 VAL G CB  1 
ATOM   3982 C CG1 . VAL D 4 113 ? -0.91100  8.74000   -53.43900 1.000 33.57771  ? 113 VAL G CG1 1 
ATOM   3983 C CG2 . VAL D 4 113 ? -1.85800  11.04300  -52.99400 1.000 32.95658  ? 113 VAL G CG2 1 
ATOM   3984 N N   . LYS D 4 114 ? -3.73900  6.94000   -54.68400 1.000 49.15063  ? 114 LYS G N   1 
ATOM   3985 C CA  . LYS D 4 114 ? -4.03700  5.51900   -54.59100 1.000 50.27708  ? 114 LYS G CA  1 
ATOM   3986 C C   . LYS D 4 114 ? -3.08200  4.84200   -53.61700 1.000 50.29287  ? 114 LYS G C   1 
ATOM   3987 O O   . LYS D 4 114 ? -1.87900  5.12300   -53.59600 1.000 49.27959  ? 114 LYS G O   1 
ATOM   3988 C CB  . LYS D 4 114 ? -3.95300  4.84100   -55.97000 1.000 51.62461  ? 114 LYS G CB  1 
ATOM   3989 C CG  . LYS D 4 114 ? -5.09400  5.19100   -56.92400 1.000 52.70369  ? 114 LYS G CG  1 
ATOM   3990 C CD  . LYS D 4 114 ? -5.10000  4.30400   -58.18300 1.000 54.46706  ? 114 LYS G CD  1 
ATOM   3991 C CE  . LYS D 4 114 ? -4.24000  4.89300   -59.32600 1.000 54.45653  ? 114 LYS G CE  1 
ATOM   3992 N NZ  . LYS D 4 114 ? -4.21200  4.01500   -60.55900 1.000 54.56181  ? 114 LYS G NZ  1 
ATOM   3993 N N   . SER D 4 115 ? -3.63800  3.95300   -52.79900 1.000 46.16606  ? 115 SER G N   1 
ATOM   3994 C CA  . SER D 4 115 ? -2.83600  3.12200   -51.91300 1.000 46.66875  ? 115 SER G CA  1 
ATOM   3995 C C   . SER D 4 115 ? -1.68600  2.47800   -52.67500 1.000 46.87930  ? 115 SER G C   1 
ATOM   3996 O O   . SER D 4 115 ? -1.87300  1.94600   -53.77100 1.000 47.81889  ? 115 SER G O   1 
ATOM   3997 C CB  . SER D 4 115 ? -3.72600  2.05100   -51.28000 1.000 47.66098  ? 115 SER G CB  1 
ATOM   3998 O OG  . SER D 4 115 ? -2.96400  1.12700   -50.53800 1.000 48.26368  ? 115 SER G OG  1 
ATOM   3999 N N   . GLY D 4 116 ? -0.48700  2.54700   -52.09300 1.000 46.90299  ? 116 GLY G N   1 
ATOM   4000 C CA  . GLY D 4 116 ? 0.69600   1.96700   -52.69500 1.000 46.66086  ? 116 GLY G CA  1 
ATOM   4001 C C   . GLY D 4 116 ? 1.42300   2.84000   -53.70000 1.000 45.68179  ? 116 GLY G C   1 
ATOM   4002 O O   . GLY D 4 116 ? 2.54200   2.49500   -54.09400 1.000 45.50809  ? 116 GLY G O   1 
ATOM   4003 N N   . GLU D 4 117 ? 0.84500   3.96000   -54.12600 1.000 48.37685  ? 117 GLU G N   1 
ATOM   4004 C CA  . GLU D 4 117 ? 1.44700   4.77500   -55.16300 1.000 47.03195  ? 117 GLU G CA  1 
ATOM   4005 C C   . GLU D 4 117 ? 2.21500   5.94100   -54.53200 1.000 44.67378  ? 117 GLU G C   1 
ATOM   4006 O O   . GLU D 4 117 ? 2.31000   6.07400   -53.31000 1.000 44.33689  ? 117 GLU G O   1 
ATOM   4007 C CB  . GLU D 4 117 ? 0.37400   5.24700   -56.14900 1.000 47.70572  ? 117 GLU G CB  1 
ATOM   4008 C CG  . GLU D 4 117 ? -0.40500  4.09000   -56.79000 1.000 50.03495  ? 117 GLU G CG  1 
ATOM   4009 C CD  . GLU D 4 117 ? -0.93400  4.40600   -58.19500 1.000 50.26129  ? 117 GLU G CD  1 
ATOM   4010 O OE1 . GLU D 4 117 ? -1.06300  5.59800   -58.54500 1.000 50.19549  ? 117 GLU G OE1 1 
ATOM   4011 O OE2 . GLU D 4 117 ? -1.22400  3.45300   -58.95900 1.000 52.61157  ? 117 GLU G OE2 1 
ATOM   4012 N N   . ARG D 4 118 ? 2.77800   6.79300   -55.37700 1.000 55.43559  ? 118 ARG G N   1 
ATOM   4013 C CA  . ARG D 4 118 ? 3.57700   7.91100   -54.90300 1.000 53.51694  ? 118 ARG G CA  1 
ATOM   4014 C C   . ARG D 4 118 ? 2.96200   9.23500   -55.32700 1.000 52.55630  ? 118 ARG G C   1 
ATOM   4015 O O   . ARG D 4 118 ? 2.21500   9.31800   -56.30000 1.000 53.95910  ? 118 ARG G O   1 
ATOM   4016 C CB  . ARG D 4 118 ? 5.00900   7.81600   -55.41700 1.000 53.03004  ? 118 ARG G CB  1 
ATOM   4017 C CG  . ARG D 4 118 ? 5.82300   6.84700   -54.61700 1.000 54.06701  ? 118 ARG G CG  1 
ATOM   4018 C CD  . ARG D 4 118 ? 7.18700   6.61900   -55.22700 1.000 54.49074  ? 118 ARG G CD  1 
ATOM   4019 N NE  . ARG D 4 118 ? 8.18300   6.46700   -54.17800 1.000 53.86962  ? 118 ARG G NE  1 
ATOM   4020 C CZ  . ARG D 4 118 ? 8.63800   5.30100   -53.74200 1.000 56.03303  ? 118 ARG G CZ  1 
ATOM   4021 N NH1 . ARG D 4 118 ? 8.24200   4.15300   -54.28500 1.000 57.82535  ? 118 ARG G NH1 1 
ATOM   4022 N NH2 . ARG D 4 118 ? 9.51600   5.28500   -52.74100 1.000 56.21990  ? 118 ARG G NH2 1 
ATOM   4023 N N   . VAL D 4 119 ? 3.29000   10.27500  -54.56500 1.000 37.15445  ? 119 VAL G N   1 
ATOM   4024 C CA  . VAL D 4 119 ? 2.83600   11.62300  -54.84800 1.000 36.32804  ? 119 VAL G CA  1 
ATOM   4025 C C   . VAL D 4 119 ? 4.01500   12.55800  -54.59600 1.000 34.63047  ? 119 VAL G C   1 
ATOM   4026 O O   . VAL D 4 119 ? 4.85100   12.31400  -53.71900 1.000 33.93828  ? 119 VAL G O   1 
ATOM   4027 C CB  . VAL D 4 119 ? 1.58900   11.99800  -54.00000 1.000 37.07550  ? 119 VAL G CB  1 
ATOM   4028 C CG1 . VAL D 4 119 ? 1.90700   12.02100  -52.51200 1.000 35.60690  ? 119 VAL G CG1 1 
ATOM   4029 C CG2 . VAL D 4 119 ? 0.99500   13.34600  -54.44700 1.000 37.24920  ? 119 VAL G CG2 1 
ATOM   4030 N N   . ILE D 4 120 ? 4.10400   13.61100  -55.39500 1.000 34.42255  ? 120 ILE G N   1 
ATOM   4031 C CA  . ILE D 4 120 ? 5.09100   14.67100  -55.19400 1.000 33.15134  ? 120 ILE G CA  1 
ATOM   4032 C C   . ILE D 4 120 ? 4.38700   15.85300  -54.56400 1.000 33.02501  ? 120 ILE G C   1 
ATOM   4033 O O   . ILE D 4 120 ? 3.35500   16.30600  -55.07200 1.000 34.22516  ? 120 ILE G O   1 
ATOM   4034 C CB  . ILE D 4 120 ? 5.74400   15.08700  -56.51700 1.000 33.84616  ? 120 ILE G CB  1 
ATOM   4035 C CG1 . ILE D 4 120 ? 6.53000   13.91400  -57.07400 1.000 35.14632  ? 120 ILE G CG1 1 
ATOM   4036 C CG2 . ILE D 4 120 ? 6.66000   16.31100  -56.29900 1.000 33.67772  ? 120 ILE G CG2 1 
ATOM   4037 C CD1 . ILE D 4 120 ? 7.58700   13.46800  -56.11200 1.000 34.68837  ? 120 ILE G CD1 1 
ATOM   4038 N N   . LEU D 4 121 ? 4.92400   16.34700  -53.45700 1.000 33.15661  ? 121 LEU G N   1 
ATOM   4039 C CA  . LEU D 4 121 ? 4.42700   17.57900  -52.85500 1.000 32.83815  ? 121 LEU G CA  1 
ATOM   4040 C C   . LEU D 4 121 ? 5.46400   18.65900  -53.14300 1.000 33.38558  ? 121 LEU G C   1 
ATOM   4041 O O   . LEU D 4 121 ? 6.60300   18.57800  -52.67500 1.000 32.67760  ? 121 LEU G O   1 
ATOM   4042 C CB  . LEU D 4 121 ? 4.17900   17.42100  -51.36000 1.000 31.26427  ? 121 LEU G CB  1 
ATOM   4043 C CG  . LEU D 4 121 ? 2.85500   16.79000  -50.91500 1.000 32.27492  ? 121 LEU G CG  1 
ATOM   4044 C CD1 . LEU D 4 121 ? 2.28300   15.82800  -51.89400 1.000 34.01724  ? 121 LEU G CD1 1 
ATOM   4045 C CD2 . LEU D 4 121 ? 3.03300   16.11500  -49.55600 1.000 30.90634  ? 121 LEU G CD2 1 
ATOM   4046 N N   . GLN D 4 122 ? 5.08300   19.64400  -53.94200 1.000 31.43272  ? 122 GLN G N   1 
ATOM   4047 C CA  . GLN D 4 122 ? 6.01400   20.67300  -54.38700 1.000 32.52758  ? 122 GLN G CA  1 
ATOM   4048 C C   . GLN D 4 122 ? 5.78800   21.94200  -53.56900 1.000 33.41980  ? 122 GLN G C   1 
ATOM   4049 O O   . GLN D 4 122 ? 4.67300   22.47300  -53.53500 1.000 34.47255  ? 122 GLN G O   1 
ATOM   4050 C CB  . GLN D 4 122 ? 5.85700   20.95500  -55.88100 1.000 33.52244  ? 122 GLN G CB  1 
ATOM   4051 C CG  . GLN D 4 122 ? 6.83000   22.03900  -56.38900 1.000 34.46992  ? 122 GLN G CG  1 
ATOM   4052 C CD  . GLN D 4 122 ? 6.69200   22.27900  -57.87200 1.000 35.90167  ? 122 GLN G CD  1 
ATOM   4053 O OE1 . GLN D 4 122 ? 5.58100   22.35400  -58.39600 1.000 37.16235  ? 122 GLN G OE1 1 
ATOM   4054 N NE2 . GLN D 4 122 ? 7.81000   22.38300  -58.55900 1.000 35.59374  ? 122 GLN G NE2 1 
ATOM   4055 N N   . CYS D 4 123 ? 6.82900   22.39100  -52.88100 1.000 39.43631  ? 123 CYS G N   1 
ATOM   4056 C CA  . CYS D 4 123 ? 6.81900   23.66500  -52.17700 1.000 40.42853  ? 123 CYS G CA  1 
ATOM   4057 C C   . CYS D 4 123 ? 7.57700   24.66700  -53.03200 1.000 41.26284  ? 123 CYS G C   1 
ATOM   4058 O O   . CYS D 4 123 ? 8.62000   24.33200  -53.59100 1.000 40.82595  ? 123 CYS G O   1 
ATOM   4059 C CB  . CYS D 4 123 ? 7.47500   23.53700  -50.80100 1.000 39.99953  ? 123 CYS G CB  1 
ATOM   4060 S SG  . CYS D 4 123 ? 7.07500   24.88100  -49.63500 1.000 40.96017  ? 123 CYS G SG  1 
ATOM   4061 N N   . TRP D 4 124 ? 7.04700   25.88400  -53.15000 1.000 35.05683  ? 124 TRP G N   1 
ATOM   4062 C CA  . TRP D 4 124 ? 7.68000   26.88800  -53.99800 1.000 35.20685  ? 124 TRP G CA  1 
ATOM   4063 C C   . TRP D 4 124 ? 7.30500   28.28100  -53.50700 1.000 35.00683  ? 124 TRP G C   1 
ATOM   4064 O O   . TRP D 4 124 ? 6.28100   28.47300  -52.84800 1.000 35.08579  ? 124 TRP G O   1 
ATOM   4065 C CB  . TRP D 4 124 ? 7.29600   26.70900  -55.47500 1.000 35.83061  ? 124 TRP G CB  1 
ATOM   4066 C CG  . TRP D 4 124 ? 5.87800   27.04700  -55.74800 1.000 36.50964  ? 124 TRP G CG  1 
ATOM   4067 C CD1 . TRP D 4 124 ? 4.80300   26.20600  -55.68400 1.000 37.51502  ? 124 TRP G CD1 1 
ATOM   4068 C CD2 . TRP D 4 124 ? 5.36600   28.32800  -56.11500 1.000 36.96233  ? 124 TRP G CD2 1 
ATOM   4069 N NE1 . TRP D 4 124 ? 3.65300   26.88700  -55.99500 1.000 37.95192  ? 124 TRP G NE1 1 
ATOM   4070 C CE2 . TRP D 4 124 ? 3.97500   28.19200  -56.26700 1.000 37.69399  ? 124 TRP G CE2 1 
ATOM   4071 C CE3 . TRP D 4 124 ? 5.95200   29.57700  -56.33100 1.000 36.85442  ? 124 TRP G CE3 1 
ATOM   4072 C CZ2 . TRP D 4 124 ? 3.15900   29.26000  -56.60800 1.000 38.05193  ? 124 TRP G CZ2 1 
ATOM   4073 C CZ3 . TRP D 4 124 ? 5.14600   30.63200  -56.67500 1.000 37.99666  ? 124 TRP G CZ3 1 
ATOM   4074 C CH2 . TRP D 4 124 ? 3.75600   30.46300  -56.81200 1.000 38.11246  ? 124 TRP G CH2 1 
ATOM   4075 N N   . SER D 4 125 ? 8.15300   29.25300  -53.84800 1.000 38.37565  ? 125 SER G N   1 
ATOM   4076 C CA  . SER D 4 125 ? 7.94900   30.63500  -53.43000 1.000 38.63884  ? 125 SER G CA  1 
ATOM   4077 C C   . SER D 4 125 ? 8.69900   31.57200  -54.37000 1.000 38.78360  ? 125 SER G C   1 
ATOM   4078 O O   . SER D 4 125 ? 9.71500   31.19200  -54.96100 1.000 38.44145  ? 125 SER G O   1 
ATOM   4079 C CB  . SER D 4 125 ? 8.41900   30.85200  -51.99000 1.000 37.95192  ? 125 SER G CB  1 
ATOM   4080 O OG  . SER D 4 125 ? 8.30000   32.21300  -51.60600 1.000 37.67820  ? 125 SER G OG  1 
ATOM   4081 N N   . ASP D 4 126 ? 8.18200   32.79900  -54.50700 1.000 61.15996  ? 126 ASP G N   1 
ATOM   4082 C CA  . ASP D 4 126 ? 8.96400   33.85400  -55.14300 1.000 63.93661  ? 126 ASP G CA  1 
ATOM   4083 C C   . ASP D 4 126 ? 10.07500  34.36100  -54.23200 1.000 64.60775  ? 126 ASP G C   1 
ATOM   4084 O O   . ASP D 4 126 ? 10.99400  35.02600  -54.71600 1.000 66.32374  ? 126 ASP G O   1 
ATOM   4085 C CB  . ASP D 4 126 ? 8.07400   35.02500  -55.58100 1.000 66.67378  ? 126 ASP G CB  1 
ATOM   4086 C CG  . ASP D 4 126 ? 6.82600   35.18900  -54.71600 1.000 66.26058  ? 126 ASP G CG  1 
ATOM   4087 O OD1 . ASP D 4 126 ? 6.64400   34.43500  -53.73000 1.000 63.32338  ? 126 ASP G OD1 1 
ATOM   4088 O OD2 . ASP D 4 126 ? 6.01200   36.07900  -55.04800 1.000 69.87680  ? 126 ASP G OD2 1 
ATOM   4089 N N   . ILE D 4 127 ? 10.01100  34.05400  -52.92800 1.000 53.88804  ? 127 ILE G N   1 
ATOM   4090 C CA  . ILE D 4 127 ? 11.11400  34.30800  -52.00500 1.000 54.37494  ? 127 ILE G CA  1 
ATOM   4091 C C   . ILE D 4 127 ? 12.17800  33.23700  -52.20200 1.000 53.88541  ? 127 ILE G C   1 
ATOM   4092 O O   . ILE D 4 127 ? 11.86600  32.04600  -52.34100 1.000 52.12204  ? 127 ILE G O   1 
ATOM   4093 C CB  . ILE D 4 127 ? 10.60100  34.32500  -50.55100 1.000 53.42219  ? 127 ILE G CB  1 
ATOM   4094 C CG1 . ILE D 4 127 ? 9.68500   35.52400  -50.30700 1.000 54.69866  ? 127 ILE G CG1 1 
ATOM   4095 C CG2 . ILE D 4 127 ? 11.75200  34.27800  -49.53900 1.000 53.48273  ? 127 ILE G CG2 1 
ATOM   4096 C CD1 . ILE D 4 127 ? 8.88200   35.40900  -49.02700 1.000 53.05899  ? 127 ILE G CD1 1 
ATOM   4097 N N   . MET D 4 128 ? 13.44600  33.65500  -52.20600 1.000 57.78851  ? 128 MET G N   1 
ATOM   4098 C CA  . MET D 4 128 ? 14.57600  32.74000  -52.36400 1.000 57.56480  ? 128 MET G CA  1 
ATOM   4099 C C   . MET D 4 128 ? 14.84800  32.05400  -51.02300 1.000 56.94630  ? 128 MET G C   1 
ATOM   4100 O O   . MET D 4 128 ? 15.67700  32.48100  -50.21700 1.000 58.56755  ? 128 MET G O   1 
ATOM   4101 C CB  . MET D 4 128 ? 15.80400  33.48700  -52.87700 1.000 59.90455  ? 128 MET G CB  1 
ATOM   4102 C CG  . MET D 4 128 ? 15.62000  34.10500  -54.26400 1.000 60.95731  ? 128 MET G CG  1 
ATOM   4103 S SD  . MET D 4 128 ? 15.11600  32.87300  -55.50500 1.000 61.06785  ? 128 MET G SD  1 
ATOM   4104 C CE  . MET D 4 128 ? 13.46300  33.44000  -55.90400 1.000 61.06522  ? 128 MET G CE  1 
ATOM   4105 N N   . PHE D 4 129 ? 14.12500  30.96400  -50.77000 1.000 42.60774  ? 129 PHE G N   1 
ATOM   4106 C CA  . PHE D 4 129 ? 14.35300  30.19600  -49.55600 1.000 41.88660  ? 129 PHE G CA  1 
ATOM   4107 C C   . PHE D 4 129 ? 15.52500  29.25000  -49.76200 1.000 42.43404  ? 129 PHE G C   1 
ATOM   4108 O O   . PHE D 4 129 ? 15.63900  28.60900  -50.80700 1.000 42.14979  ? 129 PHE G O   1 
ATOM   4109 C CB  . PHE D 4 129 ? 13.09900  29.40900  -49.16800 1.000 40.12060  ? 129 PHE G CB  1 
ATOM   4110 C CG  . PHE D 4 129 ? 12.00000  30.25800  -48.62100 1.000 39.89163  ? 129 PHE G CG  1 
ATOM   4111 C CD1 . PHE D 4 129 ? 12.19900  31.01100  -47.48100 1.000 41.00492  ? 129 PHE G CD1 1 
ATOM   4112 C CD2 . PHE D 4 129 ? 10.75800  30.27900  -49.22800 1.000 38.40987  ? 129 PHE G CD2 1 
ATOM   4113 C CE1 . PHE D 4 129 ? 11.17700  31.80000  -46.95400 1.000 40.97597  ? 129 PHE G CE1 1 
ATOM   4114 C CE2 . PHE D 4 129 ? 9.73500   31.05400  -48.71300 1.000 37.94666  ? 129 PHE G CE2 1 
ATOM   4115 C CZ  . PHE D 4 129 ? 9.93700   31.81700  -47.57900 1.000 39.85478  ? 129 PHE G CZ  1 
ATOM   4116 N N   . GLU D 4 130 ? 16.41000  29.17700  -48.76900 1.000 57.80693  ? 130 GLU G N   1 
ATOM   4117 C CA  . GLU D 4 130 ? 17.54800  28.27300  -48.87800 1.000 57.81483  ? 130 GLU G CA  1 
ATOM   4118 C C   . GLU D 4 130 ? 17.13000  26.82900  -48.63900 1.000 56.62521  ? 130 GLU G C   1 
ATOM   4119 O O   . GLU D 4 130 ? 17.61000  25.92100  -49.32400 1.000 55.64351  ? 130 GLU G O   1 
ATOM   4120 C CB  . GLU D 4 130 ? 18.65100  28.68300  -47.89900 1.000 59.45713  ? 130 GLU G CB  1 
ATOM   4121 C CG  . GLU D 4 130 ? 19.83500  27.72400  -47.86600 1.000 60.15458  ? 130 GLU G CG  1 
ATOM   4122 C CD  . GLU D 4 130 ? 21.17900  28.42700  -47.95700 1.000 62.56013  ? 130 GLU G CD  1 
ATOM   4123 O OE1 . GLU D 4 130 ? 21.25500  29.65000  -47.68900 1.000 64.78672  ? 130 GLU G OE1 1 
ATOM   4124 O OE2 . GLU D 4 130 ? 22.18200  27.76400  -48.32500 1.000 62.49960  ? 130 GLU G OE2 1 
ATOM   4125 N N   . HIS D 4 131 ? 16.23600  26.60000  -47.67600 1.000 42.99463  ? 131 HIS G N   1 
ATOM   4126 C CA  . HIS D 4 131 ? 15.69000  25.27900  -47.42400 1.000 42.01293  ? 131 HIS G CA  1 
ATOM   4127 C C   . HIS D 4 131 ? 14.17200  25.35700  -47.37000 1.000 41.59972  ? 131 HIS G C   1 
ATOM   4128 O O   . HIS D 4 131 ? 13.58100  26.41100  -47.11000 1.000 41.27863  ? 131 HIS G O   1 
ATOM   4129 C CB  . HIS D 4 131 ? 16.23700  24.67000  -46.12700 1.000 42.42088  ? 131 HIS G CB  1 
ATOM   4130 C CG  . HIS D 4 131 ? 17.72000  24.47600  -46.14000 1.000 43.86842  ? 131 HIS G CG  1 
ATOM   4131 N ND1 . HIS D 4 131 ? 18.59100  25.32800  -45.49100 1.000 45.68442  ? 131 HIS G ND1 1 
ATOM   4132 C CD2 . HIS D 4 131 ? 18.49000  23.55000  -46.75700 1.000 42.49983  ? 131 HIS G CD2 1 
ATOM   4133 C CE1 . HIS D 4 131 ? 19.83300  24.92300  -45.69100 1.000 46.18975  ? 131 HIS G CE1 1 
ATOM   4134 N NE2 . HIS D 4 131 ? 19.80000  23.84900  -46.46200 1.000 44.38690  ? 131 HIS G NE2 1 
ATOM   4135 N N   . PHE D 4 132 ? 13.55500  24.21800  -47.65400 1.000 35.91483  ? 132 PHE G N   1 
ATOM   4136 C CA  . PHE D 4 132 ? 12.12000  24.02600  -47.53800 1.000 34.78838  ? 132 PHE G CA  1 
ATOM   4137 C C   . PHE D 4 132 ? 11.87700  22.88000  -46.56600 1.000 34.27253  ? 132 PHE G C   1 
ATOM   4138 O O   . PHE D 4 132 ? 12.63600  21.90100  -46.55000 1.000 33.11450  ? 132 PHE G O   1 
ATOM   4139 C CB  . PHE D 4 132 ? 11.48200  23.69500  -48.89700 1.000 32.64339  ? 132 PHE G CB  1 
ATOM   4140 C CG  . PHE D 4 132 ? 11.33400  24.87600  -49.80000 1.000 33.31452  ? 132 PHE G CG  1 
ATOM   4141 C CD1 . PHE D 4 132 ? 10.31000  25.77200  -49.60700 1.000 32.15912  ? 132 PHE G CD1 1 
ATOM   4142 C CD2 . PHE D 4 132 ? 12.21500  25.08300  -50.85100 1.000 35.00420  ? 132 PHE G CD2 1 
ATOM   4143 C CE1 . PHE D 4 132 ? 10.15500  26.86400  -50.43600 1.000 32.90395  ? 132 PHE G CE1 1 
ATOM   4144 C CE2 . PHE D 4 132 ? 12.07400  26.17600  -51.67700 1.000 35.72270  ? 132 PHE G CE2 1 
ATOM   4145 C CZ  . PHE D 4 132 ? 11.04400  27.06700  -51.47400 1.000 34.92524  ? 132 PHE G CZ  1 
ATOM   4146 N N   . PHE D 4 133 ? 10.81500  22.99600  -45.77400 1.000 35.74113  ? 133 PHE G N   1 
ATOM   4147 C CA  . PHE D 4 133 ? 10.44600  21.98000  -44.80100 1.000 35.75692  ? 133 PHE G CA  1 
ATOM   4148 C C   . PHE D 4 133 ? 9.01900   21.53000  -45.07300 1.000 33.21714  ? 133 PHE G C   1 
ATOM   4149 O O   . PHE D 4 133 ? 8.12800   22.36500  -45.25700 1.000 32.13543  ? 133 PHE G O   1 
ATOM   4150 C CB  . PHE D 4 133 ? 10.56200  22.51500  -43.37500 1.000 38.69148  ? 133 PHE G CB  1 
ATOM   4151 C CG  . PHE D 4 133 ? 11.96200  22.85800  -42.96900 1.000 39.82583  ? 133 PHE G CG  1 
ATOM   4152 C CD1 . PHE D 4 133 ? 12.52800  24.06900  -43.33700 1.000 40.47327  ? 133 PHE G CD1 1 
ATOM   4153 C CD2 . PHE D 4 133 ? 12.71400  21.96700  -42.22000 1.000 39.71529  ? 133 PHE G CD2 1 
ATOM   4154 C CE1 . PHE D 4 133 ? 13.82200  24.38500  -42.96400 1.000 41.74448  ? 133 PHE G CE1 1 
ATOM   4155 C CE2 . PHE D 4 133 ? 14.01300  22.27900  -41.83200 1.000 40.84963  ? 133 PHE G CE2 1 
ATOM   4156 C CZ  . PHE D 4 133 ? 14.56900  23.49500  -42.20200 1.000 41.74974  ? 133 PHE G CZ  1 
ATOM   4157 N N   . LEU D 4 134 ? 8.80200   20.21900  -45.11200 1.000 36.12802  ? 134 LEU G N   1 
ATOM   4158 C CA  . LEU D 4 134 ? 7.46100   19.65800  -45.23100 1.000 33.86985  ? 134 LEU G CA  1 
ATOM   4159 C C   . LEU D 4 134 ? 7.08800   19.01000  -43.90400 1.000 36.57807  ? 134 LEU G C   1 
ATOM   4160 O O   . LEU D 4 134 ? 7.84300   18.18400  -43.38800 1.000 36.80704  ? 134 LEU G O   1 
ATOM   4161 C CB  . LEU D 4 134 ? 7.38900   18.64300  -46.37300 1.000 30.13782  ? 134 LEU G CB  1 
ATOM   4162 C CG  . LEU D 4 134 ? 5.99700   18.03300  -46.64100 1.000 28.84556  ? 134 LEU G CG  1 
ATOM   4163 C CD1 . LEU D 4 134 ? 5.05400   19.03800  -47.28200 1.000 27.34275  ? 134 LEU G CD1 1 
ATOM   4164 C CD2 . LEU D 4 134 ? 6.13200   16.76500  -47.50300 1.000 26.94270  ? 134 LEU G CD2 1 
ATOM   4165 N N   . HIS D 4 135 ? 5.94500   19.40600  -43.34100 1.000 33.98039  ? 135 HIS G N   1 
ATOM   4166 C CA  . HIS D 4 135 ? 5.52100   18.93500  -42.02500 1.000 36.24908  ? 135 HIS G CA  1 
ATOM   4167 C C   . HIS D 4 135 ? 4.10000   18.40300  -42.07500 1.000 36.34120  ? 135 HIS G C   1 
ATOM   4168 O O   . HIS D 4 135 ? 3.17800   19.12300  -42.47100 1.000 34.88313  ? 135 HIS G O   1 
ATOM   4169 C CB  . HIS D 4 135 ? 5.60200   20.04900  -40.97900 1.000 38.03877  ? 135 HIS G CB  1 
ATOM   4170 C CG  . HIS D 4 135 ? 5.35800   19.58500  -39.57500 1.000 38.86255  ? 135 HIS G CG  1 
ATOM   4171 N ND1 . HIS D 4 135 ? 4.42400   20.17400  -38.74900 1.000 39.51000  ? 135 HIS G ND1 1 
ATOM   4172 C CD2 . HIS D 4 135 ? 5.93300   18.59900  -38.84700 1.000 39.54158  ? 135 HIS G CD2 1 
ATOM   4173 C CE1 . HIS D 4 135 ? 4.42900   19.56700  -37.57500 1.000 40.54697  ? 135 HIS G CE1 1 
ATOM   4174 N NE2 . HIS D 4 135 ? 5.33100   18.60300  -37.61100 1.000 41.07071  ? 135 HIS G NE2 1 
ATOM   4175 N N   . LYS D 4 136 ? 3.91000   17.16200  -41.62000 1.000 39.83636  ? 136 LYS G N   1 
ATOM   4176 C CA  . LYS D 4 136 ? 2.57600   16.59400  -41.51200 1.000 40.51012  ? 136 LYS G CA  1 
ATOM   4177 C C   . LYS D 4 136 ? 2.01600   16.91300  -40.13100 1.000 41.83133  ? 136 LYS G C   1 
ATOM   4178 O O   . LYS D 4 136 ? 2.67800   16.67500  -39.10900 1.000 42.90514  ? 136 LYS G O   1 
ATOM   4179 C CB  . LYS D 4 136 ? 2.59900   15.07900  -41.76000 1.000 40.22588  ? 136 LYS G CB  1 
ATOM   4180 C CG  . LYS D 4 136 ? 1.30500   14.38000  -41.43500 1.000 41.39444  ? 136 LYS G CG  1 
ATOM   4181 C CD  . LYS D 4 136 ? 1.36400   12.90400  -41.84200 1.000 41.71026  ? 136 LYS G CD  1 
ATOM   4182 C CE  . LYS D 4 136 ? 0.58300   12.03600  -40.89600 1.000 43.16833  ? 136 LYS G CE  1 
ATOM   4183 N NZ  . LYS D 4 136 ? -0.85600  12.39400  -40.82000 1.000 43.20518  ? 136 LYS G NZ  1 
ATOM   4184 N N   . GLU D 4 137 ? 0.78900   17.42000  -40.13000 1.000 52.17204  ? 137 GLU G N   1 
ATOM   4185 C CA  . GLU D 4 137 ? 0.13400   17.81600  -38.86200 1.000 53.28797  ? 137 GLU G CA  1 
ATOM   4186 C C   . GLU D 4 137 ? 0.03400   16.62700  -37.91300 1.000 54.86447  ? 137 GLU G C   1 
ATOM   4187 O O   . GLU D 4 137 ? -0.23000  15.51600  -38.37200 1.000 55.28031  ? 137 GLU G O   1 
ATOM   4188 C CB  . GLU D 4 137 ? -1.25400  18.39000  -39.13000 1.000 51.97465  ? 137 GLU G CB  1 
ATOM   4189 C CG  . GLU D 4 137 ? -1.32500  19.89300  -38.96500 1.000 51.86938  ? 137 GLU G CG  1 
ATOM   4190 C CD  . GLU D 4 137 ? -2.35700  20.56000  -39.85400 1.000 49.81124  ? 137 GLU G CD  1 
ATOM   4191 O OE1 . GLU D 4 137 ? -3.55000  20.23200  -39.71300 1.000 49.40592  ? 137 GLU G OE1 1 
ATOM   4192 O OE2 . GLU D 4 137 ? -1.96200  21.40200  -40.68400 1.000 47.95312  ? 137 GLU G OE2 1 
ATOM   4193 N N   . GLY D 4 138 ? 0.21300   16.89100  -36.62900 1.000 63.24179  ? 138 GLY G N   1 
ATOM   4194 C CA  . GLY D 4 138 ? 0.13400   15.85800  -35.61400 1.000 64.89199  ? 138 GLY G CA  1 
ATOM   4195 C C   . GLY D 4 138 ? 1.04500   16.19500  -34.45500 1.000 66.78432  ? 138 GLY G C   1 
ATOM   4196 O O   . GLY D 4 138 ? 1.92800   17.04200  -34.55200 1.000 65.92106  ? 138 GLY G O   1 
ATOM   4197 N N   . ILE D 4 139 ? 0.79500   15.52400  -33.32800 1.000 76.39600  ? 139 ILE G N   1 
ATOM   4198 C CA  . ILE D 4 139 ? 1.70900   15.62100  -32.20000 1.000 77.61457  ? 139 ILE G CA  1 
ATOM   4199 C C   . ILE D 4 139 ? 2.99700   14.88200  -32.54200 1.000 78.21727  ? 139 ILE G C   1 
ATOM   4200 O O   . ILE D 4 139 ? 2.97700   13.85600  -33.23700 1.000 77.68300  ? 139 ILE G O   1 
ATOM   4201 C CB  . ILE D 4 139 ? 1.05300   15.05600  -30.92500 1.000 80.52018  ? 139 ILE G CB  1 
ATOM   4202 C CG1 . ILE D 4 139 ? -0.36200  15.62400  -30.73600 1.000 81.09920  ? 139 ILE G CG1 1 
ATOM   4203 C CG2 . ILE D 4 139 ? 1.89500   15.35900  -29.69100 1.000 82.99416  ? 139 ILE G CG2 1 
ATOM   4204 C CD1 . ILE D 4 139 ? -0.41700  17.13400  -30.58900 1.000 79.75430  ? 139 ILE G CD1 1 
ATOM   4205 N N   . SER D 4 140 ? 4.13000   15.42200  -32.08300 1.000 79.82536  ? 140 SER G N   1 
ATOM   4206 C CA  . SER D 4 140 ? 5.44600   14.77200  -32.17000 1.000 80.42806  ? 140 SER G CA  1 
ATOM   4207 C C   . SER D 4 140 ? 5.73200   14.25700  -33.58300 1.000 78.74365  ? 140 SER G C   1 
ATOM   4208 O O   . SER D 4 140 ? 6.00000   13.07800  -33.81000 1.000 78.63838  ? 140 SER G O   1 
ATOM   4209 C CB  . SER D 4 140 ? 5.56700   13.63600  -31.14500 1.000 83.02838  ? 140 SER G CB  1 
ATOM   4210 O OG  . SER D 4 140 ? 5.57400   14.11400  -29.80800 1.000 87.94739  ? 140 SER G OG  1 
ATOM   4211 N N   . LYS D 4 141 ? 5.67000   15.16700  -34.54300 1.000 74.73001  ? 141 LYS G N   1 
ATOM   4212 C CA  . LYS D 4 141 ? 5.90800   14.83300  -35.93900 1.000 72.86663  ? 141 LYS G CA  1 
ATOM   4213 C C   . LYS D 4 141 ? 7.09600   15.63300  -36.45500 1.000 72.20339  ? 141 LYS G C   1 
ATOM   4214 O O   . LYS D 4 141 ? 7.20800   16.83400  -36.18800 1.000 72.88242  ? 141 LYS G O   1 
ATOM   4215 C CB  . LYS D 4 141 ? 4.66400   15.10600  -36.78200 1.000 71.28486  ? 141 LYS G CB  1 
ATOM   4216 C CG  . LYS D 4 141 ? 3.49300   14.23400  -36.40400 1.000 72.33499  ? 141 LYS G CG  1 
ATOM   4217 C CD  . LYS D 4 141 ? 2.72600   13.78100  -37.62400 1.000 71.64280  ? 141 LYS G CD  1 
ATOM   4218 C CE  . LYS D 4 141 ? 3.67200   13.33800  -38.73900 1.000 70.80059  ? 141 LYS G CE  1 
ATOM   4219 N NZ  . LYS D 4 141 ? 4.54800   12.20300  -38.31800 1.000 71.96652  ? 141 LYS G NZ  1 
ATOM   4220 N N   . ASP D 4 142 ? 8.00600   14.94500  -37.21000 1.000 64.33929  ? 142 ASP G N   1 
ATOM   4221 C CA  . ASP D 4 142 ? 9.24800   15.57900  -37.62800 1.000 63.77080  ? 142 ASP G CA  1 
ATOM   4222 C C   . ASP D 4 142 ? 9.15800   16.04600  -39.07900 1.000 62.85227  ? 142 ASP G C   1 
ATOM   4223 O O   . ASP D 4 142 ? 8.53500   15.38200  -39.91600 1.000 60.97310  ? 142 ASP G O   1 
ATOM   4224 C CB  . ASP D 4 142 ? 10.42700  14.61900  -37.48000 1.000 64.13927  ? 142 ASP G CB  1 
ATOM   4225 C CG  . ASP D 4 142 ? 11.74400  15.27400  -37.81300 1.000 67.08436  ? 142 ASP G CG  1 
ATOM   4226 O OD1 . ASP D 4 142 ? 11.72500  16.48500  -38.14000 1.000 67.29754  ? 142 ASP G OD1 1 
ATOM   4227 O OD2 . ASP D 4 142 ? 12.78900  14.59000  -37.75000 1.000 68.32661  ? 142 ASP G OD2 1 
ATOM   4228 N N   . PRO D 4 143 ? 9.77000   17.18500  -39.40100 1.000 51.42459  ? 143 PRO G N   1 
ATOM   4229 C CA  . PRO D 4 143 ? 9.72900   17.69900  -40.77000 1.000 49.13484  ? 143 PRO G CA  1 
ATOM   4230 C C   . PRO D 4 143 ? 10.81500  17.08800  -41.64200 1.000 47.35568  ? 143 PRO G C   1 
ATOM   4231 O O   . PRO D 4 143 ? 11.86600  16.66000  -41.16800 1.000 48.94271  ? 143 PRO G O   1 
ATOM   4232 C CB  . PRO D 4 143 ? 9.96600   19.20400  -40.57100 1.000 51.12718  ? 143 PRO G CB  1 
ATOM   4233 C CG  . PRO D 4 143 ? 10.85800  19.27900  -39.36600 1.000 52.71685  ? 143 PRO G CG  1 
ATOM   4234 C CD  . PRO D 4 143 ? 10.48800  18.09400  -38.48400 1.000 53.33534  ? 143 PRO G CD  1 
ATOM   4235 N N   . SER D 4 144 ? 10.53100  17.02700  -42.93700 1.000 42.82882  ? 144 SER G N   1 
ATOM   4236 C CA  . SER D 4 144 ? 11.53300  16.67400  -43.93600 1.000 41.12598  ? 144 SER G CA  1 
ATOM   4237 C C   . SER D 4 144 ? 12.14000  17.96300  -44.48800 1.000 41.90239  ? 144 SER G C   1 
ATOM   4238 O O   . SER D 4 144 ? 11.43500  18.95500  -44.66800 1.000 42.62353  ? 144 SER G O   1 
ATOM   4239 C CB  . SER D 4 144 ? 10.90800  15.85900  -45.07500 1.000 38.19932  ? 144 SER G CB  1 
ATOM   4240 O OG  . SER D 4 144 ? 10.31300  14.65300  -44.59200 1.000 39.36261  ? 144 SER G OG  1 
ATOM   4241 N N   . ARG D 4 145 ? 13.44100  17.94700  -44.76000 1.000 47.48727  ? 145 ARG G N   1 
ATOM   4242 C CA  . ARG D 4 145 ? 14.12000  19.12900  -45.28100 1.000 49.24275  ? 145 ARG G CA  1 
ATOM   4243 C C   . ARG D 4 145 ? 14.71200  18.83900  -46.65000 1.000 47.65835  ? 145 ARG G C   1 
ATOM   4244 O O   . ARG D 4 145 ? 15.22100  17.74200  -46.89800 1.000 46.60559  ? 145 ARG G O   1 
ATOM   4245 C CB  . ARG D 4 145 ? 15.23400  19.62200  -44.34800 1.000 51.57724  ? 145 ARG G CB  1 
ATOM   4246 C CG  . ARG D 4 145 ? 15.73500  21.02100  -44.72800 1.000 53.23270  ? 145 ARG G CG  1 
ATOM   4247 C CD  . ARG D 4 145 ? 17.04100  21.39200  -44.05900 1.000 55.81459  ? 145 ARG G CD  1 
ATOM   4248 N NE  . ARG D 4 145 ? 18.09700  20.46400  -44.43700 1.000 55.65667  ? 145 ARG G NE  1 
ATOM   4249 C CZ  . ARG D 4 145 ? 19.36700  20.58400  -44.08200 1.000 57.71745  ? 145 ARG G CZ  1 
ATOM   4250 N NH1 . ARG D 4 145 ? 19.79300  21.62200  -43.37800 1.000 60.04404  ? 145 ARG G NH1 1 
ATOM   4251 N NH2 . ARG D 4 145 ? 20.23000  19.63200  -44.43000 1.000 56.83576  ? 145 ARG G NH2 1 
ATOM   4252 N N   . LEU D 4 146 ? 14.65400  19.84100  -47.52400 1.000 41.74185  ? 146 LEU G N   1 
ATOM   4253 C CA  . LEU D 4 146 ? 15.27500  19.82000  -48.84200 1.000 41.23389  ? 146 LEU G CA  1 
ATOM   4254 C C   . LEU D 4 146 ? 15.88900  21.18400  -49.14200 1.000 43.84210  ? 146 LEU G C   1 
ATOM   4255 O O   . LEU D 4 146 ? 15.38900  22.21700  -48.68800 1.000 45.52651  ? 146 LEU G O   1 
ATOM   4256 C CB  . LEU D 4 146 ? 14.25300  19.47000  -49.92700 1.000 39.36525  ? 146 LEU G CB  1 
ATOM   4257 C CG  . LEU D 4 146 ? 13.82700  17.99900  -49.95900 1.000 36.45174  ? 146 LEU G CG  1 
ATOM   4258 C CD1 . LEU D 4 146 ? 12.73200  17.78600  -50.97000 1.000 35.53321  ? 146 LEU G CD1 1 
ATOM   4259 C CD2 . LEU D 4 146 ? 15.03500  17.12700  -50.26000 1.000 36.33330  ? 146 LEU G CD2 1 
ATOM   4260 N N   . VAL D 4 147 ? 16.97300  21.18900  -49.92300 1.000 41.04439  ? 147 VAL G N   1 
ATOM   4261 C CA  . VAL D 4 147 ? 17.52800  22.46400  -50.37200 1.000 43.44468  ? 147 VAL G CA  1 
ATOM   4262 C C   . VAL D 4 147 ? 16.59800  23.07700  -51.41400 1.000 43.75261  ? 147 VAL G C   1 
ATOM   4263 O O   . VAL D 4 147 ? 15.97400  22.36900  -52.21400 1.000 42.42877  ? 147 VAL G O   1 
ATOM   4264 C CB  . VAL D 4 147 ? 18.95700  22.28100  -50.91600 1.000 44.00528  ? 147 VAL G CB  1 
ATOM   4265 C CG1 . VAL D 4 147 ? 18.96400  21.37100  -52.12500 1.000 42.66564  ? 147 VAL G CG1 1 
ATOM   4266 C CG2 . VAL D 4 147 ? 19.57900  23.62200  -51.25700 1.000 46.61612  ? 147 VAL G CG2 1 
ATOM   4267 N N   . GLY D 4 148 ? 16.47000  24.40000  -51.39000 1.000 44.32110  ? 148 GLY G N   1 
ATOM   4268 C CA  . GLY D 4 148 ? 15.64300  25.05800  -52.38200 1.000 45.16331  ? 148 GLY G CA  1 
ATOM   4269 C C   . GLY D 4 148 ? 16.35200  25.17800  -53.71600 1.000 46.32924  ? 148 GLY G C   1 
ATOM   4270 O O   . GLY D 4 148 ? 17.45900  25.71800  -53.77300 1.000 46.92405  ? 148 GLY G O   1 
ATOM   4271 N N   . GLN D 4 149 ? 15.74800  24.68800  -54.79300 1.000 49.93230  ? 149 GLN G N   1 
ATOM   4272 C CA  . GLN D 4 149 ? 16.32900  24.87600  -56.11500 1.000 51.26404  ? 149 GLN G CA  1 
ATOM   4273 C C   . GLN D 4 149 ? 15.86900  26.21500  -56.67400 1.000 52.73527  ? 149 GLN G C   1 
ATOM   4274 O O   . GLN D 4 149 ? 14.74600  26.65100  -56.42300 1.000 52.80633  ? 149 GLN G O   1 
ATOM   4275 C CB  . GLN D 4 149 ? 15.92900  23.73500  -57.04700 1.000 50.03495  ? 149 GLN G CB  1 
ATOM   4276 C CG  . GLN D 4 149 ? 16.18700  22.35900  -56.48000 1.000 47.91364  ? 149 GLN G CG  1 
ATOM   4277 C CD  . GLN D 4 149 ? 17.65900  22.02200  -56.35800 1.000 48.23999  ? 149 GLN G CD  1 
ATOM   4278 O OE1 . GLN D 4 149 ? 18.49100  22.47800  -57.15000 1.000 50.53764  ? 149 GLN G OE1 1 
ATOM   4279 N NE2 . GLN D 4 149 ? 17.99200  21.21500  -55.36700 1.000 46.63191  ? 149 GLN G NE2 1 
ATOM   4280 N N   . ILE D 4 150 ? 16.73900  26.88700  -57.41100 1.000 57.32003  ? 150 ILE G N   1 
ATOM   4281 C CA  . ILE D 4 150 ? 16.46000  28.24400  -57.87000 1.000 58.68335  ? 150 ILE G CA  1 
ATOM   4282 C C   . ILE D 4 150 ? 16.33100  28.23100  -59.38500 1.000 60.84940  ? 150 ILE G C   1 
ATOM   4283 O O   . ILE D 4 150 ? 17.29500  27.91400  -60.09400 1.000 61.00205  ? 150 ILE G O   1 
ATOM   4284 C CB  . ILE D 4 150 ? 17.54000  29.22800  -57.40900 1.000 60.13353  ? 150 ILE G CB  1 
ATOM   4285 C CG1 . ILE D 4 150 ? 17.53700  29.31000  -55.88200 1.000 59.49398  ? 150 ILE G CG1 1 
ATOM   4286 C CG2 . ILE D 4 150 ? 17.31800  30.60200  -58.05100 1.000 62.50486  ? 150 ILE G CG2 1 
ATOM   4287 C CD1 . ILE D 4 150 ? 18.63900  30.18100  -55.30000 1.000 60.79413  ? 150 ILE G CD1 1 
ATOM   4288 N N   . HIS D 4 151 ? 15.14600  28.58000  -59.88600 1.000 74.45630  ? 151 HIS G N   1 
ATOM   4289 C CA  . HIS D 4 151 ? 14.98400  28.71300  -61.32600 1.000 77.21715  ? 151 HIS G CA  1 
ATOM   4290 C C   . HIS D 4 151 ? 13.86600  29.68300  -61.67200 1.000 78.42256  ? 151 HIS G C   1 
ATOM   4291 O O   . HIS D 4 151 ? 12.73000  29.51400  -61.21900 1.000 77.50929  ? 151 HIS G O   1 
ATOM   4292 C CB  . HIS D 4 151 ? 14.70900  27.36500  -61.98600 1.000 76.67235  ? 151 HIS G CB  1 
ATOM   4293 C CG  . HIS D 4 151 ? 15.08500  27.34300  -63.43100 1.000 78.96736  ? 151 HIS G CG  1 
ATOM   4294 N ND1 . HIS D 4 151 ? 16.31300  27.78000  -63.87700 1.000 79.67008  ? 151 HIS G ND1 1 
ATOM   4295 C CD2 . HIS D 4 151 ? 14.39300  26.96800  -64.53200 1.000 80.28594  ? 151 HIS G CD2 1 
ATOM   4296 C CE1 . HIS D 4 151 ? 16.36600  27.66500  -65.19200 1.000 83.31525  ? 151 HIS G CE1 1 
ATOM   4297 N NE2 . HIS D 4 151 ? 15.21600  27.17000  -65.61400 1.000 83.40211  ? 151 HIS G NE2 1 
ATOM   4298 N N   . ASP D 4 152 ? 14.20000  30.68000  -62.50100 1.000 84.36011  ? 152 ASP G N   1 
ATOM   4299 C CA  . ASP D 4 152 ? 13.22600  31.62000  -63.06600 1.000 86.29982  ? 152 ASP G CA  1 
ATOM   4300 C C   . ASP D 4 152 ? 12.57900  32.47700  -61.98200 1.000 84.55224  ? 152 ASP G C   1 
ATOM   4301 O O   . ASP D 4 152 ? 11.37400  32.73900  -62.01000 1.000 84.59172  ? 152 ASP G O   1 
ATOM   4302 C CB  . ASP D 4 152 ? 12.15900  30.88800  -63.88300 1.000 87.08149  ? 152 ASP G CB  1 
ATOM   4303 C CG  . ASP D 4 152 ? 12.42500  30.93700  -65.37500 1.000 91.72679  ? 152 ASP G CG  1 
ATOM   4304 O OD1 . ASP D 4 152 ? 13.32500  31.69500  -65.80900 1.000 96.16679  ? 152 ASP G OD1 1 
ATOM   4305 O OD2 . ASP D 4 152 ? 11.72300  30.21100  -66.11700 1.000 92.35581  ? 152 ASP G OD2 1 
ATOM   4306 N N   . GLY D 4 153 ? 13.38200  32.91600  -61.01700 1.000 66.98961  ? 153 GLY G N   1 
ATOM   4307 C CA  . GLY D 4 153 ? 12.85300  33.74500  -59.95200 1.000 65.86053  ? 153 GLY G CA  1 
ATOM   4308 C C   . GLY D 4 153 ? 11.92400  33.05700  -58.96700 1.000 62.84964  ? 153 GLY G C   1 
ATOM   4309 O O   . GLY D 4 153 ? 11.14400  33.73600  -58.29500 1.000 62.46275  ? 153 GLY G O   1 
ATOM   4310 N N   . VAL D 4 154 ? 11.95500  31.73200  -58.86700 1.000 57.47268  ? 154 VAL G N   1 
ATOM   4311 C CA  . VAL D 4 154 ? 11.32600  31.06400  -57.73600 1.000 54.72498  ? 154 VAL G CA  1 
ATOM   4312 C C   . VAL D 4 154 ? 12.31300  30.05500  -57.17500 1.000 53.94068  ? 154 VAL G C   1 
ATOM   4313 O O   . VAL D 4 154 ? 13.17900  29.54200  -57.88700 1.000 54.55128  ? 154 VAL G O   1 
ATOM   4314 C CB  . VAL D 4 154 ? 9.97800   30.36600  -58.08300 1.000 54.40389  ? 154 VAL G CB  1 
ATOM   4315 C CG1 . VAL D 4 154 ? 9.06600   31.27400  -58.90300 1.000 56.69627  ? 154 VAL G CG1 1 
ATOM   4316 C CG2 . VAL D 4 154 ? 10.20100  29.00800  -58.76100 1.000 54.56707  ? 154 VAL G CG2 1 
ATOM   4317 N N   . SER D 4 155 ? 12.19400  29.78200  -55.88100 1.000 45.50282  ? 155 SER G N   1 
ATOM   4318 C CA  . SER D 4 155 ? 12.82700  28.60500  -55.31100 1.000 44.07897  ? 155 SER G CA  1 
ATOM   4319 C C   . SER D 4 155 ? 11.75600  27.56100  -55.01400 1.000 42.93146  ? 155 SER G C   1 
ATOM   4320 O O   . SER D 4 155 ? 10.62000  27.89400  -54.66700 1.000 41.40496  ? 155 SER G O   1 
ATOM   4321 C CB  . SER D 4 155 ? 13.62900  28.93300  -54.05400 1.000 44.02370  ? 155 SER G CB  1 
ATOM   4322 O OG  . SER D 4 155 ? 12.82500  29.56600  -53.08700 1.000 43.82631  ? 155 SER G OG  1 
ATOM   4323 N N   . LYS D 4 156 ? 12.12400  26.29400  -55.18000 1.000 40.96544  ? 156 LYS G N   1 
ATOM   4324 C CA  . LYS D 4 156 ? 11.15500  25.21100  -55.09300 1.000 39.95479  ? 156 LYS G CA  1 
ATOM   4325 C C   . LYS D 4 156 ? 11.85000  23.92700  -54.66500 1.000 38.83360  ? 156 LYS G C   1 
ATOM   4326 O O   . LYS D 4 156 ? 13.07100  23.79000  -54.77300 1.000 38.80202  ? 156 LYS G O   1 
ATOM   4327 C CB  . LYS D 4 156 ? 10.43300  25.00700  -56.42900 1.000 40.59697  ? 156 LYS G CB  1 
ATOM   4328 C CG  . LYS D 4 156 ? 11.35800  24.90200  -57.60600 1.000 42.38403  ? 156 LYS G CG  1 
ATOM   4329 C CD  . LYS D 4 156 ? 10.57000  24.77100  -58.89800 1.000 44.43691  ? 156 LYS G CD  1 
ATOM   4330 C CE  . LYS D 4 156 ? 11.48100  24.89600  -60.11200 1.000 46.97142  ? 156 LYS G CE  1 
ATOM   4331 N NZ  . LYS D 4 156 ? 10.74600  24.63900  -61.39800 1.000 48.53213  ? 156 LYS G NZ  1 
ATOM   4332 N N   . ALA D 4 157 ? 11.04600  22.97600  -54.18900 1.000 36.34120  ? 157 ALA G N   1 
ATOM   4333 C CA  . ALA D 4 157 ? 11.55400  21.67100  -53.79700 1.000 33.64351  ? 157 ALA G CA  1 
ATOM   4334 C C   . ALA D 4 157 ? 10.43500  20.64500  -53.93600 1.000 31.44061  ? 157 ALA G C   1 
ATOM   4335 O O   . ALA D 4 157 ? 9.27400   20.92100  -53.59700 1.000 30.97740  ? 157 ALA G O   1 
ATOM   4336 C CB  . ALA D 4 157 ? 12.08500  21.68800  -52.36300 1.000 32.46442  ? 157 ALA G CB  1 
ATOM   4337 N N   . ASN D 4 158 ? 10.79700  19.46200  -54.40800 1.000 36.59386  ? 158 ASN G N   1 
ATOM   4338 C CA  . ASN D 4 158 ? 9.85400   18.37700  -54.66900 1.000 34.56467  ? 158 ASN G CA  1 
ATOM   4339 C C   . ASN D 4 158 ? 10.02700  17.33100  -53.57600 1.000 31.46167  ? 158 ASN G C   1 
ATOM   4340 O O   . ASN D 4 158 ? 11.08000  16.69100  -53.48900 1.000 30.94582  ? 158 ASN G O   1 
ATOM   4341 C CB  . ASN D 4 158 ? 10.09800  17.77600  -56.05100 1.000 35.93852  ? 158 ASN G CB  1 
ATOM   4342 C CG  . ASN D 4 158 ? 9.38000   18.53300  -57.14800 1.000 39.67318  ? 158 ASN G CG  1 
ATOM   4343 O OD1 . ASN D 4 158 ? 8.78800   19.58600  -56.89900 1.000 40.66277  ? 158 ASN G OD1 1 
ATOM   4344 N ND2 . ASN D 4 158 ? 9.42500   17.99700  -58.38000 1.000 41.05229  ? 158 ASN G ND2 1 
ATOM   4345 N N   . PHE D 4 159 ? 9.02300   17.18400  -52.72400 1.000 35.27528  ? 159 PHE G N   1 
ATOM   4346 C CA  . PHE D 4 159 ? 9.03600   16.16600  -51.67600 1.000 33.40927  ? 159 PHE G CA  1 
ATOM   4347 C C   . PHE D 4 159 ? 8.27800   14.94600  -52.18400 1.000 32.94079  ? 159 PHE G C   1 
ATOM   4348 O O   . PHE D 4 159 ? 7.10800   15.06200  -52.56200 1.000 33.34610  ? 159 PHE G O   1 
ATOM   4349 C CB  . PHE D 4 159 ? 8.38900   16.67700  -50.38700 1.000 32.59601  ? 159 PHE G CB  1 
ATOM   4350 C CG  . PHE D 4 159 ? 9.16300   17.76000  -49.69000 1.000 34.29622  ? 159 PHE G CG  1 
ATOM   4351 C CD1 . PHE D 4 159 ? 8.92600   19.09600  -49.97900 1.000 35.75429  ? 159 PHE G CD1 1 
ATOM   4352 C CD2 . PHE D 4 159 ? 10.10200  17.44300  -48.71700 1.000 35.59374  ? 159 PHE G CD2 1 
ATOM   4353 C CE1 . PHE D 4 159 ? 9.63700   20.10300  -49.32600 1.000 38.10457  ? 159 PHE G CE1 1 
ATOM   4354 C CE2 . PHE D 4 159 ? 10.81200  18.42400  -48.07400 1.000 37.67031  ? 159 PHE G CE2 1 
ATOM   4355 C CZ  . PHE D 4 159 ? 10.58200  19.76600  -48.38200 1.000 39.37841  ? 159 PHE G CZ  1 
ATOM   4356 N N   . SER D 4 160 ? 8.92500   13.78700  -52.17200 1.000 40.29167  ? 160 SER G N   1 
ATOM   4357 C CA  . SER D 4 160 ? 8.30300   12.54400  -52.61000 1.000 40.79700  ? 160 SER G CA  1 
ATOM   4358 C C   . SER D 4 160 ? 7.72000   11.80700  -51.40300 1.000 40.66803  ? 160 SER G C   1 
ATOM   4359 O O   . SER D 4 160 ? 8.43500   11.53800  -50.43400 1.000 40.83911  ? 160 SER G O   1 
ATOM   4360 C CB  . SER D 4 160 ? 9.32300   11.66200  -53.32900 1.000 41.54182  ? 160 SER G CB  1 
ATOM   4361 O OG  . SER D 4 160 ? 8.73200   10.42200  -53.65500 1.000 42.66827  ? 160 SER G OG  1 
ATOM   4362 N N   . ILE D 4 161 ? 6.43100   11.48500  -51.45800 1.000 38.59147  ? 161 ILE G N   1 
ATOM   4363 C CA  . ILE D 4 161 ? 5.74100   10.78600  -50.37600 1.000 39.64160  ? 161 ILE G CA  1 
ATOM   4364 C C   . ILE D 4 161 ? 5.22100   9.46600   -50.91200 1.000 41.44971  ? 161 ILE G C   1 
ATOM   4365 O O   . ILE D 4 161 ? 4.53700   9.44700   -51.94100 1.000 41.55498  ? 161 ILE G O   1 
ATOM   4366 C CB  . ILE D 4 161 ? 4.57900   11.61800  -49.80300 1.000 39.68371  ? 161 ILE G CB  1 
ATOM   4367 C CG1 . ILE D 4 161 ? 5.10900   12.88100  -49.11800 1.000 39.52579  ? 161 ILE G CG1 1 
ATOM   4368 C CG2 . ILE D 4 161 ? 3.75500   10.78100  -48.84100 1.000 42.36561  ? 161 ILE G CG2 1 
ATOM   4369 C CD1 . ILE D 4 161 ? 6.21400   12.57100  -48.15100 1.000 40.29957  ? 161 ILE G CD1 1 
ATOM   4370 N N   . GLY D 4 162 ? 5.52300   8.36900   -50.21500 1.000 44.95802  ? 162 GLY G N   1 
ATOM   4371 C CA  . GLY D 4 162 ? 5.01700   7.07500   -50.61700 1.000 47.13460  ? 162 GLY G CA  1 
ATOM   4372 C C   . GLY D 4 162 ? 6.04900   5.97000   -50.50900 1.000 49.59279  ? 162 GLY G C   1 
ATOM   4373 O O   . GLY D 4 162 ? 7.20500   6.22300   -50.17100 1.000 48.12156  ? 162 GLY G O   1 
ATOM   4374 N N   . PRO D 4 163 ? 5.65400   4.70900   -50.78400 1.000 59.27816  ? 163 PRO G N   1 
ATOM   4375 C CA  . PRO D 4 163 ? 4.33300   4.22800   -51.21100 1.000 60.78887  ? 163 PRO G CA  1 
ATOM   4376 C C   . PRO D 4 163 ? 3.23200   4.56600   -50.21800 1.000 59.76506  ? 163 PRO G C   1 
ATOM   4377 O O   . PRO D 4 163 ? 3.38400   4.31600   -49.02700 1.000 60.67570  ? 163 PRO G O   1 
ATOM   4378 C CB  . PRO D 4 163 ? 4.52200   2.70700   -51.31600 1.000 64.21823  ? 163 PRO G CB  1 
ATOM   4379 C CG  . PRO D 4 163 ? 5.74500   2.41100   -50.51400 1.000 65.81579  ? 163 PRO G CG  1 
ATOM   4380 C CD  . PRO D 4 163 ? 6.62200   3.60300   -50.69500 1.000 62.25483  ? 163 PRO G CD  1 
ATOM   4381 N N   . MET D 4 164 ? 2.15800   5.16600   -50.72800 1.000 43.81052  ? 164 MET G N   1 
ATOM   4382 C CA  . MET D 4 164 ? 1.12300   5.72700   -49.88100 1.000 44.58166  ? 164 MET G CA  1 
ATOM   4383 C C   . MET D 4 164 ? 0.45800   4.65700   -49.02000 1.000 47.35041  ? 164 MET G C   1 
ATOM   4384 O O   . MET D 4 164 ? 0.05000   3.60300   -49.51200 1.000 48.26105  ? 164 MET G O   1 
ATOM   4385 C CB  . MET D 4 164 ? 0.07800   6.42700   -50.74600 1.000 44.51850  ? 164 MET G CB  1 
ATOM   4386 C CG  . MET D 4 164 ? -0.88300  7.27100   -49.95500 1.000 45.24490  ? 164 MET G CG  1 
ATOM   4387 S SD  . MET D 4 164 ? 0.02300   8.61100   -49.15700 1.000 43.49732  ? 164 MET G SD  1 
ATOM   4388 C CE  . MET D 4 164 ? -1.29400  9.35500   -48.24200 1.000 43.99738  ? 164 MET G CE  1 
ATOM   4389 N N   . MET D 4 165 ? 0.34800   4.94100   -47.72700 1.000 44.46323  ? 165 MET G N   1 
ATOM   4390 C CA  . MET D 4 165 ? -0.53800  4.19900   -46.83900 1.000 46.35819  ? 165 MET G CA  1 
ATOM   4391 C C   . MET D 4 165 ? -1.02500  5.16300   -45.75800 1.000 46.84772  ? 165 MET G C   1 
ATOM   4392 O O   . MET D 4 165 ? -0.62900  6.33100   -45.72100 1.000 45.44492  ? 165 MET G O   1 
ATOM   4393 C CB  . MET D 4 165 ? 0.16100   2.95700   -46.28000 1.000 49.62174  ? 165 MET G CB  1 
ATOM   4394 C CG  . MET D 4 165 ? 1.60300   3.15000   -45.89500 1.000 48.79269  ? 165 MET G CG  1 
ATOM   4395 S SD  . MET D 4 165 ? 1.80000   4.06100   -44.35100 1.000 47.95575  ? 165 MET G SD  1 
ATOM   4396 C CE  . MET D 4 165 ? 1.48900   2.73700   -43.14700 1.000 53.76697  ? 165 MET G CE  1 
ATOM   4397 N N   . PHE D 4 166 ? -1.88100  4.66400   -44.86600 1.000 46.89773  ? 166 PHE G N   1 
ATOM   4398 C CA  . PHE D 4 166 ? -2.63600  5.56100   -43.99300 1.000 46.02920  ? 166 PHE G CA  1 
ATOM   4399 C C   . PHE D 4 166 ? -1.75000  6.39300   -43.06900 1.000 44.14740  ? 166 PHE G C   1 
ATOM   4400 O O   . PHE D 4 166 ? -2.16500  7.47200   -42.64100 1.000 42.42614  ? 166 PHE G O   1 
ATOM   4401 C CB  . PHE D 4 166 ? -3.64600  4.76300   -43.16700 1.000 50.56659  ? 166 PHE G CB  1 
ATOM   4402 C CG  . PHE D 4 166 ? -3.03400  3.88600   -42.11100 1.000 54.26440  ? 166 PHE G CG  1 
ATOM   4403 C CD1 . PHE D 4 166 ? -2.44900  2.67100   -42.44800 1.000 57.20423  ? 166 PHE G CD1 1 
ATOM   4404 C CD2 . PHE D 4 166 ? -3.10500  4.23800   -40.76900 1.000 55.73826  ? 166 PHE G CD2 1 
ATOM   4405 C CE1 . PHE D 4 166 ? -1.91900  1.82700   -41.46400 1.000 61.59949  ? 166 PHE G CE1 1 
ATOM   4406 C CE2 . PHE D 4 166 ? -2.57900  3.39800   -39.77600 1.000 60.14669  ? 166 PHE G CE2 1 
ATOM   4407 C CZ  . PHE D 4 166 ? -1.98000  2.19800   -40.12700 1.000 63.10230  ? 166 PHE G CZ  1 
ATOM   4408 N N   . ALA D 4 167 ? -0.55600  5.91200   -42.72000 1.000 45.10804  ? 167 ALA G N   1 
ATOM   4409 C CA  . ALA D 4 167 ? 0.33000   6.71500   -41.87600 1.000 44.41059  ? 167 ALA G CA  1 
ATOM   4410 C C   . ALA D 4 167 ? 0.85100   7.96400   -42.57800 1.000 42.26559  ? 167 ALA G C   1 
ATOM   4411 O O   . ALA D 4 167 ? 1.29500   8.90000   -41.89900 1.000 42.04715  ? 167 ALA G O   1 
ATOM   4412 C CB  . ALA D 4 167 ? 1.51700   5.88700   -41.39300 1.000 46.69507  ? 167 ALA G CB  1 
ATOM   4413 N N   . LEU D 4 168 ? 0.81000   8.00700   -43.91000 1.000 42.54457  ? 168 LEU G N   1 
ATOM   4414 C CA  . LEU D 4 168 ? 1.26100   9.17200   -44.66400 1.000 40.53907  ? 168 LEU G CA  1 
ATOM   4415 C C   . LEU D 4 168 ? 0.12800   10.11500  -45.04200 1.000 41.28916  ? 168 LEU G C   1 
ATOM   4416 O O   . LEU D 4 168 ? 0.39400   11.21800  -45.53300 1.000 39.72055  ? 168 LEU G O   1 
ATOM   4417 C CB  . LEU D 4 168 ? 1.99500   8.72900   -45.93200 1.000 38.62042  ? 168 LEU G CB  1 
ATOM   4418 C CG  . LEU D 4 168 ? 3.09800   7.70200   -45.65900 1.000 39.01784  ? 168 LEU G CG  1 
ATOM   4419 C CD1 . LEU D 4 168 ? 3.67300   7.17000   -46.96900 1.000 37.30710  ? 168 LEU G CD1 1 
ATOM   4420 C CD2 . LEU D 4 168 ? 4.20300   8.30400   -44.81900 1.000 38.82308  ? 168 LEU G CD2 1 
ATOM   4421 N N   . ALA D 4 169 ? -1.11500  9.71300   -44.82800 1.000 40.47591  ? 169 ALA G N   1 
ATOM   4422 C CA  . ALA D 4 169 ? -2.26400  10.54300  -45.14600 1.000 39.88899  ? 169 ALA G CA  1 
ATOM   4423 C C   . ALA D 4 169 ? -2.49600  11.55400  -44.03700 1.000 39.67055  ? 169 ALA G C   1 
ATOM   4424 O O   . ALA D 4 169 ? -2.22500  11.28700  -42.86900 1.000 41.53393  ? 169 ALA G O   1 
ATOM   4425 C CB  . ALA D 4 169 ? -3.50700  9.66700   -45.34100 1.000 40.67067  ? 169 ALA G CB  1 
ATOM   4426 N N   . GLY D 4 170 ? -3.00600  12.71900  -44.40300 1.000 32.43020  ? 170 GLY G N   1 
ATOM   4427 C CA  . GLY D 4 170 ? -3.24500  13.75000  -43.42200 1.000 31.79855  ? 170 GLY G CA  1 
ATOM   4428 C C   . GLY D 4 170 ? -2.97900  15.11700  -44.01100 1.000 31.91698  ? 170 GLY G C   1 
ATOM   4429 O O   . GLY D 4 170 ? -2.81700  15.28000  -45.21800 1.000 31.60116  ? 170 GLY G O   1 
ATOM   4430 N N   . THR D 4 171 ? -2.97900  16.11700  -43.14300 1.000 32.78025  ? 171 THR G N   1 
ATOM   4431 C CA  . THR D 4 171 ? -2.84200  17.50400  -43.57100 1.000 33.15134  ? 171 THR G CA  1 
ATOM   4432 C C   . THR D 4 171 ? -1.37000  17.90100  -43.53700 1.000 32.75919  ? 171 THR G C   1 
ATOM   4433 O O   . THR D 4 171 ? -0.71200  17.77100  -42.50200 1.000 32.90131  ? 171 THR G O   1 
ATOM   4434 C CB  . THR D 4 171 ? -3.66200  18.43100  -42.67700 1.000 34.09093  ? 171 THR G CB  1 
ATOM   4435 O OG1 . THR D 4 171 ? -5.03200  18.01000  -42.67800 1.000 34.29622  ? 171 THR G OG1 1 
ATOM   4436 C CG2 . THR D 4 171 ? -3.58600  19.88200  -43.20600 1.000 34.57783  ? 171 THR G CG2 1 
ATOM   4437 N N   . TYR D 4 172 ? -0.85900  18.40300  -44.65800 1.000 31.60116  ? 172 TYR G N   1 
ATOM   4438 C CA  . TYR D 4 172 ? 0.53000   18.81800  -44.75500 1.000 31.29323  ? 172 TYR G CA  1 
ATOM   4439 C C   . TYR D 4 172 ? 0.62100   20.33400  -44.88400 1.000 31.70907  ? 172 TYR G C   1 
ATOM   4440 O O   . TYR D 4 172 ? -0.28400  20.98400  -45.42200 1.000 32.19070  ? 172 TYR G O   1 
ATOM   4441 C CB  . TYR D 4 172 ? 1.21100   18.16800  -45.96100 1.000 31.46693  ? 172 TYR G CB  1 
ATOM   4442 C CG  . TYR D 4 172 ? 1.55200   16.70400  -45.79600 1.000 32.05648  ? 172 TYR G CG  1 
ATOM   4443 C CD1 . TYR D 4 172 ? 0.58500   15.71500  -45.98800 1.000 31.65906  ? 172 TYR G CD1 1 
ATOM   4444 C CD2 . TYR D 4 172 ? 2.84400   16.30500  -45.47400 1.000 32.52232  ? 172 TYR G CD2 1 
ATOM   4445 C CE1 . TYR D 4 172 ? 0.90800   14.36900  -45.87300 1.000 32.02752  ? 172 TYR G CE1 1 
ATOM   4446 C CE2 . TYR D 4 172 ? 3.17000   14.96600  -45.34600 1.000 33.16450  ? 172 TYR G CE2 1 
ATOM   4447 C CZ  . TYR D 4 172 ? 2.19500   14.00500  -45.56000 1.000 33.14871  ? 172 TYR G CZ  1 
ATOM   4448 O OH  . TYR D 4 172 ? 2.50400   12.67600  -45.43100 1.000 34.68574  ? 172 TYR G OH  1 
ATOM   4449 N N   . ARG D 4 173 ? 1.73500   20.89000  -44.40800 1.000 36.00958  ? 173 ARG G N   1 
ATOM   4450 C CA  . ARG D 4 173 ? 2.08200   22.28600  -44.65500 1.000 36.43068  ? 173 ARG G CA  1 
ATOM   4451 C C   . ARG D 4 173 ? 3.57200   22.35600  -44.98200 1.000 36.52806  ? 173 ARG G C   1 
ATOM   4452 O O   . ARG D 4 173 ? 4.35500   21.50900  -44.55100 1.000 36.93338  ? 173 ARG G O   1 
ATOM   4453 C CB  . ARG D 4 173 ? 1.71700   23.18500  -43.44200 1.000 36.64124  ? 173 ARG G CB  1 
ATOM   4454 C CG  . ARG D 4 173 ? 0.35200   22.85200  -42.84800 1.000 36.99128  ? 173 ARG G CG  1 
ATOM   4455 C CD  . ARG D 4 173 ? -0.21500  23.82900  -41.86400 1.000 37.69399  ? 173 ARG G CD  1 
ATOM   4456 N NE  . ARG D 4 173 ? -0.66300  24.99700  -42.58500 1.000 39.98374  ? 173 ARG G NE  1 
ATOM   4457 C CZ  . ARG D 4 173 ? -1.37600  25.99200  -42.07800 1.000 40.75225  ? 173 ARG G CZ  1 
ATOM   4458 N NH1 . ARG D 4 173 ? -1.86400  25.93500  -40.84700 1.000 41.18125  ? 173 ARG G NH1 1 
ATOM   4459 N NH2 . ARG D 4 173 ? -1.60800  27.06800  -42.83500 1.000 40.77331  ? 173 ARG G NH2 1 
ATOM   4460 N N   . CYS D 4 174 ? 3.96900   23.33400  -45.77800 1.000 36.17276  ? 174 CYS G N   1 
ATOM   4461 C CA  . CYS D 4 174 ? 5.40400   23.49000  -45.97900 1.000 36.61755  ? 174 CYS G CA  1 
ATOM   4462 C C   . CYS D 4 174 ? 5.83900   24.90600  -45.62000 1.000 36.98601  ? 174 CYS G C   1 
ATOM   4463 O O   . CYS D 4 174 ? 5.02400   25.82100  -45.46100 1.000 36.68861  ? 174 CYS G O   1 
ATOM   4464 C CB  . CYS D 4 174 ? 5.84100   23.11500  -47.39700 1.000 36.81494  ? 174 CYS G CB  1 
ATOM   4465 S SG  . CYS D 4 174 ? 5.35100   24.24600  -48.71500 1.000 37.07287  ? 174 CYS G SG  1 
ATOM   4466 N N   . TYR D 4 175 ? 7.15900   25.05200  -45.50100 1.000 34.56993  ? 175 TYR G N   1 
ATOM   4467 C CA  . TYR D 4 175 ? 7.80100   26.17000  -44.82800 1.000 34.66731  ? 175 TYR G CA  1 
ATOM   4468 C C   . TYR D 4 175 ? 9.10600   26.45800  -45.54800 1.000 35.72797  ? 175 TYR G C   1 
ATOM   4469 O O   . TYR D 4 175 ? 9.75000   25.54400  -46.06300 1.000 36.18065  ? 175 TYR G O   1 
ATOM   4470 C CB  . TYR D 4 175 ? 8.11300   25.86400  -43.34600 1.000 35.04631  ? 175 TYR G CB  1 
ATOM   4471 C CG  . TYR D 4 175 ? 6.93700   25.53700  -42.44700 1.000 34.44887  ? 175 TYR G CG  1 
ATOM   4472 C CD1 . TYR D 4 175 ? 6.50600   24.21200  -42.27000 1.000 34.53309  ? 175 TYR G CD1 1 
ATOM   4473 C CD2 . TYR D 4 175 ? 6.27800   26.54000  -41.73900 1.000 33.78037  ? 175 TYR G CD2 1 
ATOM   4474 C CE1 . TYR D 4 175 ? 5.43100   23.90800  -41.43700 1.000 33.77773  ? 175 TYR G CE1 1 
ATOM   4475 C CE2 . TYR D 4 175 ? 5.22400   26.24800  -40.90100 1.000 33.34874  ? 175 TYR G CE2 1 
ATOM   4476 C CZ  . TYR D 4 175 ? 4.78800   24.93000  -40.76700 1.000 33.46717  ? 175 TYR G CZ  1 
ATOM   4477 O OH  . TYR D 4 175 ? 3.72400   24.65800  -39.93200 1.000 33.55665  ? 175 TYR G OH  1 
ATOM   4478 N N   . GLY D 4 176 ? 9.50100   27.72900  -45.57400 1.000 33.13292  ? 176 GLY G N   1 
ATOM   4479 C CA  . GLY D 4 176 ? 10.80600  28.12500  -46.08000 1.000 33.90933  ? 176 GLY G CA  1 
ATOM   4480 C C   . GLY D 4 176 ? 11.65200  28.68400  -44.94800 1.000 34.71732  ? 176 GLY G C   1 
ATOM   4481 O O   . GLY D 4 176 ? 11.12600  29.22300  -43.96600 1.000 34.30674  ? 176 GLY G O   1 
ATOM   4482 N N   . SER D 4 177 ? 12.97100  28.52800  -45.07000 1.000 37.35185  ? 177 SER G N   1 
ATOM   4483 C CA  . SER D 4 177 ? 13.90800  29.22000  -44.19500 1.000 38.90466  ? 177 SER G CA  1 
ATOM   4484 C C   . SER D 4 177 ? 14.96500  29.91000  -45.05000 1.000 38.65200  ? 177 SER G C   1 
ATOM   4485 O O   . SER D 4 177 ? 15.25000  29.48200  -46.17600 1.000 38.64148  ? 177 SER G O   1 
ATOM   4486 C CB  . SER D 4 177 ? 14.57000  28.26600  -43.15800 1.000 40.88911  ? 177 SER G CB  1 
ATOM   4487 O OG  . SER D 4 177 ? 15.45600  27.33900  -43.76000 1.000 41.73921  ? 177 SER G OG  1 
ATOM   4488 N N   . VAL D 4 178 ? 15.52500  30.99100  -44.51500 1.000 40.97333  ? 178 VAL G N   1 
ATOM   4489 C CA  . VAL D 4 178 ? 16.54900  31.76800  -45.20600 1.000 41.44707  ? 178 VAL G CA  1 
ATOM   4490 C C   . VAL D 4 178 ? 17.90200  31.50500  -44.54600 1.000 43.19465  ? 178 VAL G C   1 
ATOM   4491 O O   . VAL D 4 178 ? 17.99300  31.10900  -43.38200 1.000 44.35269  ? 178 VAL G O   1 
ATOM   4492 C CB  . VAL D 4 178 ? 16.23300  33.28500  -45.23600 1.000 40.75489  ? 178 VAL G CB  1 
ATOM   4493 C CG1 . VAL D 4 178 ? 14.80800  33.55100  -45.73500 1.000 38.86255  ? 178 VAL G CG1 1 
ATOM   4494 C CG2 . VAL D 4 178 ? 16.43500  33.90400  -43.86500 1.000 41.45760  ? 178 VAL G CG2 1 
ATOM   4495 N N   . THR D 4 179 ? 18.96200  31.75700  -45.32000 1.000 48.30053  ? 179 THR G N   1 
ATOM   4496 C CA  . THR D 4 179 ? 20.33400  31.31800  -45.04400 1.000 50.29024  ? 179 THR G CA  1 
ATOM   4497 C C   . THR D 4 179 ? 20.79600  31.37000  -43.58200 1.000 51.98781  ? 179 THR G C   1 
ATOM   4498 O O   . THR D 4 179 ? 21.30700  30.38100  -43.03700 1.000 52.91161  ? 179 THR G O   1 
ATOM   4499 C CB  . THR D 4 179 ? 21.28300  32.17400  -45.88900 1.000 49.91388  ? 179 THR G CB  1 
ATOM   4500 O OG1 . THR D 4 179 ? 21.05400  31.89600  -47.27900 1.000 48.38475  ? 179 THR G OG1 1 
ATOM   4501 C CG2 . THR D 4 179 ? 22.72400  31.87500  -45.52000 1.000 50.94032  ? 179 THR G CG2 1 
ATOM   4502 N N   . HIS D 4 180 ? 20.66100  32.51700  -42.94300 1.000 37.55977  ? 180 HIS G N   1 
ATOM   4503 C CA  . HIS D 4 180 ? 21.33100  32.74600  -41.66400 1.000 38.66516  ? 180 HIS G CA  1 
ATOM   4504 C C   . HIS D 4 180 ? 20.43500  32.52200  -40.45500 1.000 38.40987  ? 180 HIS G C   1 
ATOM   4505 O O   . HIS D 4 180 ? 20.89800  32.67100  -39.31800 1.000 39.15469  ? 180 HIS G O   1 
ATOM   4506 C CB  . HIS D 4 180 ? 21.90300  34.16000  -41.62600 1.000 38.80202  ? 180 HIS G CB  1 
ATOM   4507 C CG  . HIS D 4 180 ? 22.93500  34.40500  -42.67800 1.000 40.23904  ? 180 HIS G CG  1 
ATOM   4508 N ND1 . HIS D 4 180 ? 22.75600  35.31500  -43.69400 1.000 40.95491  ? 180 HIS G ND1 1 
ATOM   4509 C CD2 . HIS D 4 180 ? 24.14400  33.83700  -42.89000 1.000 41.44444  ? 180 HIS G CD2 1 
ATOM   4510 C CE1 . HIS D 4 180 ? 23.81400  35.30400  -44.48400 1.000 42.53142  ? 180 HIS G CE1 1 
ATOM   4511 N NE2 . HIS D 4 180 ? 24.66800  34.40900  -44.02400 1.000 42.86303  ? 180 HIS G NE2 1 
ATOM   4512 N N   . THR D 4 181 ? 19.17000  32.16600  -40.66000 1.000 39.97585  ? 181 THR G N   1 
ATOM   4513 C CA  . THR D 4 181 ? 18.27500  31.82000  -39.55700 1.000 39.34945  ? 181 THR G CA  1 
ATOM   4514 C C   . THR D 4 181 ? 17.64000  30.47500  -39.86600 1.000 39.52842  ? 181 THR G C   1 
ATOM   4515 O O   . THR D 4 181 ? 16.42000  30.37000  -40.03700 1.000 37.83612  ? 181 THR G O   1 
ATOM   4516 C CB  . THR D 4 181 ? 17.23600  32.91700  -39.33100 1.000 37.58609  ? 181 THR G CB  1 
ATOM   4517 O OG1 . THR D 4 181 ? 16.65900  33.28500  -40.58900 1.000 36.65703  ? 181 THR G OG1 1 
ATOM   4518 C CG2 . THR D 4 181 ? 17.90400  34.16200  -38.69300 1.000 37.88612  ? 181 THR G CG2 1 
ATOM   4519 N N   . PRO D 4 182 ? 18.45800  29.41400  -39.93000 1.000 39.77845  ? 182 PRO G N   1 
ATOM   4520 C CA  . PRO D 4 182 ? 17.96200  28.11700  -40.40900 1.000 39.53106  ? 182 PRO G CA  1 
ATOM   4521 C C   . PRO D 4 182 ? 16.87500  27.50400  -39.54900 1.000 39.85215  ? 182 PRO G C   1 
ATOM   4522 O O   . PRO D 4 182 ? 16.09100  26.69600  -40.06900 1.000 39.04416  ? 182 PRO G O   1 
ATOM   4523 C CB  . PRO D 4 182 ? 19.22400  27.24500  -40.40600 1.000 41.55235  ? 182 PRO G CB  1 
ATOM   4524 C CG  . PRO D 4 182 ? 20.12600  27.88900  -39.38500 1.000 42.25507  ? 182 PRO G CG  1 
ATOM   4525 C CD  . PRO D 4 182 ? 19.88500  29.35600  -39.56100 1.000 41.58657  ? 182 PRO G CD  1 
ATOM   4526 N N   . TYR D 4 183 ? 16.81400  27.84300  -38.26000 1.000 44.03423  ? 183 TYR G N   1 
ATOM   4527 C CA  . TYR D 4 183 ? 15.78800  27.32900  -37.35700 1.000 43.18413  ? 183 TYR G CA  1 
ATOM   4528 C C   . TYR D 4 183 ? 14.56400  28.22700  -37.28800 1.000 40.17324  ? 183 TYR G C   1 
ATOM   4529 O O   . TYR D 4 183 ? 13.61400  27.90200  -36.57000 1.000 38.68885  ? 183 TYR G O   1 
ATOM   4530 C CB  . TYR D 4 183 ? 16.35600  27.14500  -35.95100 1.000 43.73945  ? 183 TYR G CB  1 
ATOM   4531 C CG  . TYR D 4 183 ? 17.59400  26.29000  -35.89700 1.000 46.33713  ? 183 TYR G CG  1 
ATOM   4532 C CD1 . TYR D 4 183 ? 17.61700  25.04100  -36.49900 1.000 47.11618  ? 183 TYR G CD1 1 
ATOM   4533 C CD2 . TYR D 4 183 ? 18.75500  26.75000  -35.27400 1.000 47.62939  ? 183 TYR G CD2 1 
ATOM   4534 C CE1 . TYR D 4 183 ? 18.75200  24.24200  -36.45200 1.000 49.20064  ? 183 TYR G CE1 1 
ATOM   4535 C CE2 . TYR D 4 183 ? 19.89600  25.96400  -35.22100 1.000 50.14549  ? 183 TYR G CE2 1 
ATOM   4536 C CZ  . TYR D 4 183 ? 19.88600  24.70400  -35.81700 1.000 50.17707  ? 183 TYR G CZ  1 
ATOM   4537 O OH  . TYR D 4 183 ? 21.00900  23.89600  -35.78000 1.000 51.58513  ? 183 TYR G OH  1 
ATOM   4538 N N   . GLN D 4 184 ? 14.56400  29.33600  -38.01600 1.000 42.88409  ? 184 GLN G N   1 
ATOM   4539 C CA  . GLN D 4 184 ? 13.39100  30.18300  -38.16700 1.000 40.96544  ? 184 GLN G CA  1 
ATOM   4540 C C   . GLN D 4 184 ? 12.71200  29.85000  -39.49200 1.000 40.32062  ? 184 GLN G C   1 
ATOM   4541 O O   . GLN D 4 184 ? 13.34100  29.90900  -40.55300 1.000 41.22336  ? 184 GLN G O   1 
ATOM   4542 C CB  . GLN D 4 184 ? 13.77800  31.66000  -38.10600 1.000 40.43643  ? 184 GLN G CB  1 
ATOM   4543 C CG  . GLN D 4 184 ? 14.38700  32.03000  -36.77100 1.000 41.00755  ? 184 GLN G CG  1 
ATOM   4544 C CD  . GLN D 4 184 ? 14.62100  33.50100  -36.61000 1.000 40.85227  ? 184 GLN G CD  1 
ATOM   4545 O OE1 . GLN D 4 184 ? 13.89400  34.32400  -37.16600 1.000 39.56264  ? 184 GLN G OE1 1 
ATOM   4546 N NE2 . GLN D 4 184 ? 15.64000  33.85400  -35.83200 1.000 41.97872  ? 184 GLN G NE2 1 
ATOM   4547 N N   . LEU D 4 185 ? 11.44000  29.48100  -39.42700 1.000 32.24071  ? 185 LEU G N   1 
ATOM   4548 C CA  . LEU D 4 185 ? 10.67900  29.10900  -40.61100 1.000 31.68801  ? 185 LEU G CA  1 
ATOM   4549 C C   . LEU D 4 185 ? 9.66800   30.19200  -40.96900 1.000 30.77474  ? 185 LEU G C   1 
ATOM   4550 O O   . LEU D 4 185 ? 9.23100   30.97100  -40.11800 1.000 30.50629  ? 185 LEU G O   1 
ATOM   4551 C CB  . LEU D 4 185 ? 9.94600   27.77800  -40.38800 1.000 31.30902  ? 185 LEU G CB  1 
ATOM   4552 C CG  . LEU D 4 185 ? 10.74800  26.50400  -40.68600 1.000 32.54338  ? 185 LEU G CG  1 
ATOM   4553 C CD1 . LEU D 4 185 ? 12.09900  26.48900  -39.99000 1.000 34.36728  ? 185 LEU G CD1 1 
ATOM   4554 C CD2 . LEU D 4 185 ? 9.93600   25.25800  -40.30500 1.000 31.99857  ? 185 LEU G CD2 1 
ATOM   4555 N N   . SER D 4 186 ? 9.27200   30.18500  -42.24300 1.000 28.78503  ? 186 SER G N   1 
ATOM   4556 C CA  . SER D 4 186 ? 8.21500   31.04800  -42.74400 1.000 29.01664  ? 186 SER G CA  1 
ATOM   4557 C C   . SER D 4 186 ? 6.90100   30.79400  -42.00900 1.000 28.80082  ? 186 SER G C   1 
ATOM   4558 O O   . SER D 4 186 ? 6.75800   29.84300  -41.23300 1.000 28.22970  ? 186 SER G O   1 
ATOM   4559 C CB  . SER D 4 186 ? 8.00100   30.79700  -44.24100 1.000 28.89820  ? 186 SER G CB  1 
ATOM   4560 O OG  . SER D 4 186 ? 7.70100   29.41900  -44.44800 1.000 28.07705  ? 186 SER G OG  1 
ATOM   4561 N N   . ALA D 4 187 ? 5.92100   31.66200  -42.26500 1.000 31.00109  ? 187 ALA G N   1 
ATOM   4562 C CA  . ALA D 4 187 ? 4.53500   31.27000  -42.01000 1.000 31.16426  ? 187 ALA G CA  1 
ATOM   4563 C C   . ALA D 4 187 ? 4.22200   29.98800  -42.79500 1.000 30.73263  ? 187 ALA G C   1 
ATOM   4564 O O   . ALA D 4 187 ? 4.83200   29.73200  -43.83800 1.000 30.55103  ? 187 ALA G O   1 
ATOM   4565 C CB  . ALA D 4 187 ? 3.58200   32.39300  -42.42100 1.000 31.92225  ? 187 ALA G CB  1 
ATOM   4566 N N   . PRO D 4 188 ? 3.29900   29.14900  -42.31300 1.000 29.53249  ? 188 PRO G N   1 
ATOM   4567 C CA  . PRO D 4 188 ? 3.02700   27.89200  -43.02700 1.000 29.55618  ? 188 PRO G CA  1 
ATOM   4568 C C   . PRO D 4 188 ? 2.26900   28.13200  -44.32300 1.000 29.54828  ? 188 PRO G C   1 
ATOM   4569 O O   . PRO D 4 188 ? 1.44500   29.04500  -44.42800 1.000 30.13519  ? 188 PRO G O   1 
ATOM   4570 C CB  . PRO D 4 188 ? 2.17800   27.08900  -42.03200 1.000 29.49564  ? 188 PRO G CB  1 
ATOM   4571 C CG  . PRO D 4 188 ? 1.50400   28.12300  -41.19300 1.000 30.48523  ? 188 PRO G CG  1 
ATOM   4572 C CD  . PRO D 4 188 ? 2.52300   29.25000  -41.06000 1.000 30.14046  ? 188 PRO G CD  1 
ATOM   4573 N N   . SER D 4 189 ? 2.55800   27.29500  -45.32300 1.000 29.81147  ? 189 SER G N   1 
ATOM   4574 C CA  . SER D 4 189 ? 1.74600   27.30000  -46.53200 1.000 30.37469  ? 189 SER G CA  1 
ATOM   4575 C C   . SER D 4 189 ? 0.29100   26.98500  -46.18700 1.000 30.93002  ? 189 SER G C   1 
ATOM   4576 O O   . SER D 4 189 ? -0.00800  26.39800  -45.14200 1.000 30.55893  ? 189 SER G O   1 
ATOM   4577 C CB  . SER D 4 189 ? 2.24900   26.26300  -47.53200 1.000 30.02992  ? 189 SER G CB  1 
ATOM   4578 O OG  . SER D 4 189 ? 1.99600   24.96500  -47.03400 1.000 29.79305  ? 189 SER G OG  1 
ATOM   4579 N N   . ASP D 4 190 ? -0.62200  27.38500  -47.08200 1.000 35.53058  ? 190 ASP G N   1 
ATOM   4580 C CA  . ASP D 4 190 ? -1.99400  26.90200  -46.97500 1.000 36.09117  ? 190 ASP G CA  1 
ATOM   4581 C C   . ASP D 4 190 ? -1.98100  25.37600  -46.84700 1.000 35.61480  ? 190 ASP G C   1 
ATOM   4582 O O   . ASP D 4 190 ? -1.17700  24.70500  -47.51000 1.000 35.04368  ? 190 ASP G O   1 
ATOM   4583 C CB  . ASP D 4 190 ? -2.81700  27.31100  -48.20100 1.000 37.30184  ? 190 ASP G CB  1 
ATOM   4584 C CG  . ASP D 4 190 ? -3.04700  28.81200  -48.29900 1.000 38.13878  ? 190 ASP G CG  1 
ATOM   4585 O OD1 . ASP D 4 190 ? -2.66500  29.56000  -47.37800 1.000 37.91507  ? 190 ASP G OD1 1 
ATOM   4586 O OD2 . ASP D 4 190 ? -3.62300  29.24500  -49.31300 1.000 38.85466  ? 190 ASP G OD2 1 
ATOM   4587 N N   . PRO D 4 191 ? -2.83200  24.79000  -46.00900 1.000 34.54625  ? 191 PRO G N   1 
ATOM   4588 C CA  . PRO D 4 191 ? -2.75500  23.34000  -45.79000 1.000 33.93038  ? 191 PRO G CA  1 
ATOM   4589 C C   . PRO D 4 191 ? -3.22900  22.54900  -46.99800 1.000 34.22252  ? 191 PRO G C   1 
ATOM   4590 O O   . PRO D 4 191 ? -4.06600  22.99900  -47.78300 1.000 35.23054  ? 191 PRO G O   1 
ATOM   4591 C CB  . PRO D 4 191 ? -3.67000  23.11000  -44.57900 1.000 34.41465  ? 191 PRO G CB  1 
ATOM   4592 C CG  . PRO D 4 191 ? -4.66900  24.22700  -44.67300 1.000 35.68849  ? 191 PRO G CG  1 
ATOM   4593 C CD  . PRO D 4 191 ? -3.93500  25.41000  -45.25300 1.000 35.53847  ? 191 PRO G CD  1 
ATOM   4594 N N   . LEU D 4 192 ? -2.65600  21.35800  -47.14900 1.000 37.67031  ? 192 LEU G N   1 
ATOM   4595 C CA  . LEU D 4 192 ? -3.03400  20.41800  -48.19400 1.000 37.95718  ? 192 LEU G CA  1 
ATOM   4596 C C   . LEU D 4 192 ? -3.38700  19.08500  -47.54500 1.000 37.27289  ? 192 LEU G C   1 
ATOM   4597 O O   . LEU D 4 192 ? -2.54100  18.47200  -46.88200 1.000 36.12275  ? 192 LEU G O   1 
ATOM   4598 C CB  . LEU D 4 192 ? -1.89000  20.23900  -49.19000 1.000 37.56766  ? 192 LEU G CB  1 
ATOM   4599 C CG  . LEU D 4 192 ? -2.19500  19.70800  -50.58100 1.000 38.38355  ? 192 LEU G CG  1 
ATOM   4600 C CD1 . LEU D 4 192 ? -3.29200  20.53900  -51.23200 1.000 39.91005  ? 192 LEU G CD1 1 
ATOM   4601 C CD2 . LEU D 4 192 ? -0.92600  19.74100  -51.43400 1.000 37.50713  ? 192 LEU G CD2 1 
ATOM   4602 N N   . ASP D 4 193 ? -4.62900  18.63300  -47.73300 1.000 41.61288  ? 193 ASP G N   1 
ATOM   4603 C CA  . ASP D 4 193 ? -5.02500  17.32000  -47.22600 1.000 40.84437  ? 193 ASP G CA  1 
ATOM   4604 C C   . ASP D 4 193 ? -4.61300  16.26400  -48.24100 1.000 40.14955  ? 193 ASP G C   1 
ATOM   4605 O O   . ASP D 4 193 ? -5.05200  16.30200  -49.39600 1.000 40.79700  ? 193 ASP G O   1 
ATOM   4606 C CB  . ASP D 4 193 ? -6.52800  17.25400  -46.97600 1.000 41.76817  ? 193 ASP G CB  1 
ATOM   4607 C CG  . ASP D 4 193 ? -6.95900  18.09900  -45.79200 1.000 43.40784  ? 193 ASP G CG  1 
ATOM   4608 O OD1 . ASP D 4 193 ? -6.09500  18.49900  -44.98700 1.000 41.89713  ? 193 ASP G OD1 1 
ATOM   4609 O OD2 . ASP D 4 193 ? -8.17300  18.35200  -45.65900 1.000 44.39743  ? 193 ASP G OD2 1 
ATOM   4610 N N   . ILE D 4 194 ? -3.75100  15.34500  -47.83000 1.000 34.41202  ? 194 ILE G N   1 
ATOM   4611 C CA  . ILE D 4 194 ? -3.37400  14.22400  -48.67200 1.000 34.56993  ? 194 ILE G CA  1 
ATOM   4612 C C   . ILE D 4 194 ? -4.16200  13.00900  -48.18600 1.000 34.40676  ? 194 ILE G C   1 
ATOM   4613 O O   . ILE D 4 194 ? -4.05100  12.60800  -47.01700 1.000 34.23568  ? 194 ILE G O   1 
ATOM   4614 C CB  . ILE D 4 194 ? -1.85900  13.98000  -48.64300 1.000 34.58836  ? 194 ILE G CB  1 
ATOM   4615 C CG1 . ILE D 4 194 ? -1.09400  15.25000  -49.06200 1.000 34.45939  ? 194 ILE G CG1 1 
ATOM   4616 C CG2 . ILE D 4 194 ? -1.49900  12.79800  -49.52900 1.000 34.74890  ? 194 ILE G CG2 1 
ATOM   4617 C CD1 . ILE D 4 194 ? -1.30900  15.73800  -50.51400 1.000 34.70416  ? 194 ILE G CD1 1 
ATOM   4618 N N   . VAL D 4 195 ? -4.98200  12.45500  -49.07700 1.000 38.07825  ? 195 VAL G N   1 
ATOM   4619 C CA  . VAL D 4 195 ? -5.90100  11.35700  -48.78200 1.000 38.11246  ? 195 VAL G CA  1 
ATOM   4620 C C   . VAL D 4 195 ? -5.39400  10.10700  -49.49200 1.000 38.77307  ? 195 VAL G C   1 
ATOM   4621 O O   . VAL D 4 195 ? -4.91800  10.18900  -50.63200 1.000 39.70739  ? 195 VAL G O   1 
ATOM   4622 C CB  . VAL D 4 195 ? -7.32600  11.72100  -49.25300 1.000 38.92835  ? 195 VAL G CB  1 
ATOM   4623 C CG1 . VAL D 4 195 ? -8.27600  10.54600  -49.11000 1.000 40.47591  ? 195 VAL G CG1 1 
ATOM   4624 C CG2 . VAL D 4 195 ? -7.85300  12.93300  -48.50600 1.000 39.90742  ? 195 VAL G CG2 1 
ATOM   4625 N N   . VAL D 4 196 ? -5.46500  8.95900   -48.82200 1.000 37.07287  ? 196 VAL G N   1 
ATOM   4626 C CA  . VAL D 4 196 ? -5.17900  7.67100   -49.45100 1.000 38.13615  ? 196 VAL G CA  1 
ATOM   4627 C C   . VAL D 4 196 ? -6.50600  7.01300   -49.79800 1.000 38.60463  ? 196 VAL G C   1 
ATOM   4628 O O   . VAL D 4 196 ? -7.40800  6.93600   -48.95600 1.000 37.95718  ? 196 VAL G O   1 
ATOM   4629 C CB  . VAL D 4 196 ? -4.30300  6.77200   -48.55300 1.000 39.34419  ? 196 VAL G CB  1 
ATOM   4630 C CG1 . VAL D 4 196 ? -4.93900  6.52600   -47.16100 1.000 39.09679  ? 196 VAL G CG1 1 
ATOM   4631 C CG2 . VAL D 4 196 ? -4.00100  5.45000   -49.24900 1.000 41.07071  ? 196 VAL G CG2 1 
ATOM   4632 N N   . THR D 4 197 ? -6.65800  6.61300   -51.05900 1.000 40.11007  ? 197 THR G N   1 
ATOM   4633 C CA  . THR D 4 197 ? -7.84100  5.89300   -51.52100 1.000 40.38642  ? 197 THR G CA  1 
ATOM   4634 C C   . THR D 4 197 ? -7.52100  4.40500   -51.61100 1.000 42.16558  ? 197 THR G C   1 
ATOM   4635 O O   . THR D 4 197 ? -6.46700  4.02300   -52.13100 1.000 42.61037  ? 197 THR G O   1 
ATOM   4636 C CB  . THR D 4 197 ? -8.32300  6.39300   -52.88400 1.000 40.52854  ? 197 THR G CB  1 
ATOM   4637 O OG1 . THR D 4 197 ? -7.29000  6.19800   -53.85800 1.000 41.78133  ? 197 THR G OG1 1 
ATOM   4638 C CG2 . THR D 4 197 ? -8.70500  7.87000   -52.82800 1.000 40.41537  ? 197 THR G CG2 1 
ATOM   4639 N N   . GLY D 4 198 ? -8.43000  3.57200   -51.10800 1.000 36.38331  ? 198 GLY G N   1 
ATOM   4640 C CA  . GLY D 4 198 ? -8.22000  2.14300   -51.11300 1.000 37.73610  ? 198 GLY G CA  1 
ATOM   4641 C C   . GLY D 4 198 ? -7.44600  1.68200   -49.89600 1.000 38.69674  ? 198 GLY G C   1 
ATOM   4642 O O   . GLY D 4 198 ? -6.76900  2.47000   -49.22900 1.000 38.46777  ? 198 GLY G O   1 
ATOM   4643 N N   . PRO D 4 199 ? -7.50900  0.37900   -49.59300 1.000 42.23664  ? 199 PRO G N   1 
ATOM   4644 C CA  . PRO D 4 199 ? -8.09200  -0.66200  -50.44900 1.000 42.92357  ? 199 PRO G CA  1 
ATOM   4645 C C   . PRO D 4 199 ? -9.56300  -0.99000  -50.17100 1.000 42.28402  ? 199 PRO G C   1 
ATOM   4646 O O   . PRO D 4 199 ? -10.08000 -1.92000  -50.78400 1.000 42.55773  ? 199 PRO G O   1 
ATOM   4647 C CB  . PRO D 4 199 ? -7.20700  -1.87400  -50.14400 1.000 44.49481  ? 199 PRO G CB  1 
ATOM   4648 C CG  . PRO D 4 199 ? -6.85200  -1.69100  -48.68500 1.000 44.13950  ? 199 PRO G CG  1 
ATOM   4649 C CD  . PRO D 4 199 ? -6.85300  -0.19500  -48.40400 1.000 43.17360  ? 199 PRO G CD  1 
ATOM   4650 N N   . TYR D 4 200 ? -10.21600 -0.23400  -49.28500 1.000 40.54433  ? 200 TYR G N   1 
ATOM   4651 C CA  . TYR D 4 200 ? -11.63400 -0.44400  -49.00500 1.000 40.21272  ? 200 TYR G CA  1 
ATOM   4652 C C   . TYR D 4 200 ? -12.45400 -0.39800  -50.29800 1.000 40.10481  ? 200 TYR G C   1 
ATOM   4653 O O   . TYR D 4 200 ? -12.21400 0.43700   -51.17300 1.000 39.48895  ? 200 TYR G O   1 
ATOM   4654 C CB  . TYR D 4 200 ? -12.11900 0.62400   -48.02300 1.000 39.16259  ? 200 TYR G CB  1 
ATOM   4655 C CG  . TYR D 4 200 ? -11.21100 0.78200   -46.81900 1.000 39.48368  ? 200 TYR G CG  1 
ATOM   4656 C CD1 . TYR D 4 200 ? -11.20000 -0.17600  -45.80600 1.000 40.73910  ? 200 TYR G CD1 1 
ATOM   4657 C CD2 . TYR D 4 200 ? -10.36100 1.87600   -46.69600 1.000 39.11785  ? 200 TYR G CD2 1 
ATOM   4658 C CE1 . TYR D 4 200 ? -10.36500 -0.05000  -44.69500 1.000 40.45222  ? 200 TYR G CE1 1 
ATOM   4659 C CE2 . TYR D 4 200 ? -9.53100  2.01600   -45.58900 1.000 39.18365  ? 200 TYR G CE2 1 
ATOM   4660 C CZ  . TYR D 4 200 ? -9.54500  1.03900   -44.59000 1.000 40.41537  ? 200 TYR G CZ  1 
ATOM   4661 O OH  . TYR D 4 200 ? -8.71600  1.14300   -43.49300 1.000 40.64961  ? 200 TYR G OH  1 
ATOM   4662 N N   . GLU D 4 201 ? -13.42300 -1.30800  -50.41700 1.000 43.92895  ? 201 GLU G N   1 
ATOM   4663 C CA  . GLU D 4 201 ? -14.09600 -1.53000  -51.69700 1.000 44.32637  ? 201 GLU G CA  1 
ATOM   4664 C C   . GLU D 4 201 ? -14.88500 -0.30100  -52.14900 1.000 43.89474  ? 201 GLU G C   1 
ATOM   4665 O O   . GLU D 4 201 ? -15.47900 0.41500   -51.34200 1.000 43.07095  ? 201 GLU G O   1 
ATOM   4666 C CB  . GLU D 4 201 ? -15.02300 -2.73900  -51.60500 1.000 45.31859  ? 201 GLU G CB  1 
ATOM   4667 C CG  . GLU D 4 201 ? -16.11600 -2.60200  -50.56200 1.000 45.16068  ? 201 GLU G CG  1 
ATOM   4668 C CD  . GLU D 4 201 ? -17.22400 -3.60700  -50.76100 1.000 46.03447  ? 201 GLU G CD  1 
ATOM   4669 O OE1 . GLU D 4 201 ? -17.16300 -4.35000  -51.77400 1.000 46.12658  ? 201 GLU G OE1 1 
ATOM   4670 O OE2 . GLU D 4 201 ? -18.15000 -3.65600  -49.90700 1.000 45.34491  ? 201 GLU G OE2 1 
ATOM   4671 N N   . LYS D 4 202 ? -14.89200 -0.06100  -53.45700 1.000 36.97285  ? 202 LYS G N   1 
ATOM   4672 C CA  . LYS D 4 202 ? -15.54800 1.13500   -53.97000 1.000 37.00444  ? 202 LYS G CA  1 
ATOM   4673 C C   . LYS D 4 202 ? -17.05500 1.05700   -53.73700 1.000 37.85717  ? 202 LYS G C   1 
ATOM   4674 O O   . LYS D 4 202 ? -17.64800 -0.02600  -53.79700 1.000 37.99929  ? 202 LYS G O   1 
ATOM   4675 C CB  . LYS D 4 202 ? -15.27000 1.32100   -55.45900 1.000 37.63609  ? 202 LYS G CB  1 
ATOM   4676 C CG  . LYS D 4 202 ? -15.95100 0.26800   -56.32000 1.000 38.29670  ? 202 LYS G CG  1 
ATOM   4677 C CD  . LYS D 4 202 ? -15.54400 0.41600   -57.75600 1.000 39.04942  ? 202 LYS G CD  1 
ATOM   4678 C CE  . LYS D 4 202 ? -16.20300 -0.62300  -58.60000 1.000 40.11797  ? 202 LYS G CE  1 
ATOM   4679 N NZ  . LYS D 4 202 ? -15.73500 -0.46900  -59.99500 1.000 41.53130  ? 202 LYS G NZ  1 
ATOM   4680 N N   . PRO D 4 203 ? -17.69400 2.17500   -53.44100 1.000 38.48093  ? 203 PRO G N   1 
ATOM   4681 C CA  . PRO D 4 203 ? -19.15600 2.21400   -53.36900 1.000 39.56001  ? 203 PRO G CA  1 
ATOM   4682 C C   . PRO D 4 203 ? -19.76300 2.39700   -54.76100 1.000 41.05755  ? 203 PRO G C   1 
ATOM   4683 O O   . PRO D 4 203 ? -19.05600 2.52100   -55.77000 1.000 40.98649  ? 203 PRO G O   1 
ATOM   4684 C CB  . PRO D 4 203 ? -19.42100 3.42700   -52.47000 1.000 39.77056  ? 203 PRO G CB  1 
ATOM   4685 C CG  . PRO D 4 203 ? -18.23800 4.31300   -52.66000 1.000 39.23102  ? 203 PRO G CG  1 
ATOM   4686 C CD  . PRO D 4 203 ? -17.06800 3.45300   -53.04000 1.000 38.12826  ? 203 PRO G CD  1 
ATOM   4687 N N   . SER D 4 204 ? -21.09500 2.43100   -54.79300 1.000 48.60320  ? 204 SER G N   1 
ATOM   4688 C CA  . SER D 4 204 ? -21.88400 2.70100   -55.99100 1.000 50.20865  ? 204 SER G CA  1 
ATOM   4689 C C   . SER D 4 204 ? -22.42600 4.12500   -55.95900 1.000 52.47208  ? 204 SER G C   1 
ATOM   4690 O O   . SER D 4 204 ? -22.92900 4.58600   -54.93300 1.000 52.14836  ? 204 SER G O   1 
ATOM   4691 C CB  . SER D 4 204 ? -23.06300 1.73200   -56.10300 1.000 50.95348  ? 204 SER G CB  1 
ATOM   4692 O OG  . SER D 4 204 ? -22.67800 0.48400   -56.64700 1.000 50.96401  ? 204 SER G OG  1 
ATOM   4693 N N   . LEU D 4 205 ? -22.36300 4.81000   -57.09300 1.000 50.46658  ? 205 LEU G N   1 
ATOM   4694 C CA  . LEU D 4 205 ? -22.90200 6.15500   -57.19500 1.000 52.46945  ? 205 LEU G CA  1 
ATOM   4695 C C   . LEU D 4 205 ? -24.10900 6.13900   -58.12100 1.000 53.65380  ? 205 LEU G C   1 
ATOM   4696 O O   . LEU D 4 205 ? -24.14500 5.37100   -59.08800 1.000 54.05648  ? 205 LEU G O   1 
ATOM   4697 C CB  . LEU D 4 205 ? -21.84200 7.13400   -57.70600 1.000 53.27218  ? 205 LEU G CB  1 
ATOM   4698 C CG  . LEU D 4 205 ? -22.23000 8.61400   -57.72400 1.000 54.13017  ? 205 LEU G CG  1 
ATOM   4699 C CD1 . LEU D 4 205 ? -22.68000 9.06300   -56.34400 1.000 52.90634  ? 205 LEU G CD1 1 
ATOM   4700 C CD2 . LEU D 4 205 ? -21.06600 9.46400   -58.21400 1.000 54.65655  ? 205 LEU G CD2 1 
ATOM   4701 N N   . SER D 4 206 ? -25.11200 6.95600   -57.80000 1.000 57.64112  ? 206 SER G N   1 
ATOM   4702 C CA  . SER D 4 206 ? -26.26600 7.12000   -58.68200 1.000 59.02023  ? 206 SER G CA  1 
ATOM   4703 C C   . SER D 4 206 ? -27.05100 8.35100   -58.26100 1.000 59.57820  ? 206 SER G C   1 
ATOM   4704 O O   . SER D 4 206 ? -26.88500 8.87200   -57.15500 1.000 58.97812  ? 206 SER G O   1 
ATOM   4705 C CB  . SER D 4 206 ? -27.17600 5.89100   -58.67600 1.000 59.19131  ? 206 SER G CB  1 
ATOM   4706 O OG  . SER D 4 206 ? -27.84900 5.77100   -57.43600 1.000 59.43344  ? 206 SER G OG  1 
ATOM   4707 N N   . ALA D 4 207 ? -27.92300 8.79700   -59.15600 1.000 58.17013  ? 207 ALA G N   1 
ATOM   4708 C CA  . ALA D 4 207 ? -28.67800 10.02600  -58.97300 1.000 58.77547  ? 207 ALA G CA  1 
ATOM   4709 C C   . ALA D 4 207 ? -30.17100 9.73700   -58.93400 1.000 59.65978  ? 207 ALA G C   1 
ATOM   4710 O O   . ALA D 4 207 ? -30.65400 8.76300   -59.52700 1.000 59.65978  ? 207 ALA G O   1 
ATOM   4711 C CB  . ALA D 4 207 ? -28.38200 11.03000  -60.09200 1.000 59.52029  ? 207 ALA G CB  1 
ATOM   4712 N N   . GLN D 4 208 ? -30.89900 10.60500  -58.23300 1.000 80.73600  ? 208 GLN G N   1 
ATOM   4713 C CA  . GLN D 4 208 ? -32.34200 10.50400  -58.10000 1.000 81.78875  ? 208 GLN G CA  1 
ATOM   4714 C C   . GLN D 4 208 ? -32.96000 11.84900  -58.46600 1.000 82.87573  ? 208 GLN G C   1 
ATOM   4715 O O   . GLN D 4 208 ? -32.53600 12.88900  -57.93200 1.000 82.48094  ? 208 GLN G O   1 
ATOM   4716 C CB  . GLN D 4 208 ? -32.72700 10.09100  -56.67300 1.000 81.47819  ? 208 GLN G CB  1 
ATOM   4717 C CG  . GLN D 4 208 ? -33.96700 9.21700   -56.59800 1.000 82.85467  ? 208 GLN G CG  1 
ATOM   4718 C CD  . GLN D 4 208 ? -33.78700 7.87400   -57.29500 1.000 82.69413  ? 208 GLN G CD  1 
ATOM   4719 O OE1 . GLN D 4 208 ? -32.66700 7.36900   -57.42400 1.000 81.30975  ? 208 GLN G OE1 1 
ATOM   4720 N NE2 . GLN D 4 208 ? -34.89400 7.29300   -57.75100 1.000 83.29946  ? 208 GLN G NE2 1 
ATOM   4721 N N   . PRO D 4 209 ? -33.94600 11.88700  -59.38400 1.000 71.59016  ? 209 PRO G N   1 
ATOM   4722 C CA  . PRO D 4 209 ? -34.51600 10.73500  -60.10100 1.000 71.60069  ? 209 PRO G CA  1 
ATOM   4723 C C   . PRO D 4 209 ? -33.54300 10.13900  -61.12200 1.000 70.92956  ? 209 PRO G C   1 
ATOM   4724 O O   . PRO D 4 209 ? -33.71600 9.00300   -61.55700 1.000 71.16116  ? 209 PRO G O   1 
ATOM   4725 C CB  . PRO D 4 209 ? -35.74400 11.33300  -60.80400 1.000 72.67450  ? 209 PRO G CB  1 
ATOM   4726 C CG  . PRO D 4 209 ? -35.35900 12.77300  -61.01700 1.000 72.91401  ? 209 PRO G CG  1 
ATOM   4727 C CD  . PRO D 4 209 ? -34.57700 13.15500  -59.79300 1.000 71.52173  ? 209 PRO G CD  1 
ATOM   4728 N N   . GLY D 4 210 ? -32.52700 10.91100  -61.48900 1.000 73.44565  ? 210 GLY G N   1 
ATOM   4729 C CA  . GLY D 4 210 ? -31.53000 10.46700  -62.43000 1.000 73.00086  ? 210 GLY G CA  1 
ATOM   4730 C C   . GLY D 4 210 ? -30.52500 11.55700  -62.74200 1.000 72.92453  ? 210 GLY G C   1 
ATOM   4731 O O   . GLY D 4 210 ? -30.56500 12.65000  -62.16500 1.000 73.11929  ? 210 GLY G O   1 
ATOM   4732 N N   . PRO D 4 211 ? -29.60900 11.28600  -63.67900 1.000 68.26871  ? 211 PRO G N   1 
ATOM   4733 C CA  . PRO D 4 211 ? -28.51700 12.23100  -63.94300 1.000 67.86866  ? 211 PRO G CA  1 
ATOM   4734 C C   . PRO D 4 211 ? -28.85300 13.35300  -64.91800 1.000 68.25029  ? 211 PRO G C   1 
ATOM   4735 O O   . PRO D 4 211 ? -28.01800 14.25400  -65.09500 1.000 67.42914  ? 211 PRO G O   1 
ATOM   4736 C CB  . PRO D 4 211 ? -27.40400 11.33000  -64.51800 1.000 67.43703  ? 211 PRO G CB  1 
ATOM   4737 C CG  . PRO D 4 211 ? -28.06100 9.97100   -64.80300 1.000 68.03974  ? 211 PRO G CG  1 
ATOM   4738 C CD  . PRO D 4 211 ? -29.52700 10.09800  -64.54300 1.000 67.88972  ? 211 PRO G CD  1 
ATOM   4739 N N   . LYS D 4 212 ? -30.01900 13.33900  -65.56000 1.000 69.20303  ? 212 LYS G N   1 
ATOM   4740 C CA  . LYS D 4 212 ? -30.39600 14.39200  -66.50200 1.000 69.77942  ? 212 LYS G CA  1 
ATOM   4741 C C   . LYS D 4 212 ? -31.34700 15.36000  -65.79900 1.000 70.44529  ? 212 LYS G C   1 
ATOM   4742 O O   . LYS D 4 212 ? -32.51300 15.03400  -65.55300 1.000 70.67690  ? 212 LYS G O   1 
ATOM   4743 C CB  . LYS D 4 212 ? -31.02800 13.79600  -67.75900 1.000 70.72690  ? 212 LYS G CB  1 
ATOM   4744 N N   . VAL D 4 213 ? -30.85000 16.55200  -65.48900 1.000 80.77021  ? 213 VAL G N   1 
ATOM   4745 C CA  . VAL D 4 213 ? -31.55600 17.51900  -64.65500 1.000 81.75717  ? 213 VAL G CA  1 
ATOM   4746 C C   . VAL D 4 213 ? -31.96700 18.70000  -65.52100 1.000 82.91257  ? 213 VAL G C   1 
ATOM   4747 O O   . VAL D 4 213 ? -31.11600 19.33600  -66.15500 1.000 82.00983  ? 213 VAL G O   1 
ATOM   4748 C CB  . VAL D 4 213 ? -30.67500 17.98600  -63.48500 1.000 81.03340  ? 213 VAL G CB  1 
ATOM   4749 C CG1 . VAL D 4 213 ? -31.40600 19.00500  -62.61600 1.000 81.15184  ? 213 VAL G CG1 1 
ATOM   4750 C CG2 . VAL D 4 213 ? -30.22400 16.79300  -62.67500 1.000 80.00696  ? 213 VAL G CG2 1 
ATOM   4751 N N   . GLN D 4 214 ? -33.26200 19.00100  -65.54300 1.000 105.16261 ? 214 GLN G N   1 
ATOM   4752 C CA  . GLN D 4 214 ? -33.69500 20.24900  -66.14900 1.000 108.06032 ? 214 GLN G CA  1 
ATOM   4753 C C   . GLN D 4 214 ? -33.48300 21.40000  -65.16700 1.000 108.14981 ? 214 GLN G C   1 
ATOM   4754 O O   . GLN D 4 214 ? -33.24300 21.20200  -63.97300 1.000 106.37065 ? 214 GLN G O   1 
ATOM   4755 C CB  . GLN D 4 214 ? -35.16100 20.17100  -66.58300 1.000 111.62128 ? 214 GLN G CB  1 
ATOM   4756 C CG  . GLN D 4 214 ? -36.16100 20.09200  -65.43700 1.000 113.35043 ? 214 GLN G CG  1 
ATOM   4757 C CD  . GLN D 4 214 ? -37.60500 20.01300  -65.91600 1.000 118.53000 ? 214 GLN G CD  1 
ATOM   4758 O OE1 . GLN D 4 214 ? -38.29000 19.01000  -65.70300 1.000 119.40116 ? 214 GLN G OE1 1 
ATOM   4759 N NE2 . GLN D 4 214 ? -38.07400 21.07600  -66.56000 1.000 121.46456 ? 214 GLN G NE2 1 
ATOM   4760 N N   . ALA D 4 215 ? -33.56200 22.62200  -65.68600 1.000 91.89260  ? 215 ALA G N   1 
ATOM   4761 C CA  . ALA D 4 215 ? -33.41600 23.79200  -64.83300 1.000 92.55320  ? 215 ALA G CA  1 
ATOM   4762 C C   . ALA D 4 215 ? -34.59900 23.89400  -63.87400 1.000 94.89822  ? 215 ALA G C   1 
ATOM   4763 O O   . ALA D 4 215 ? -35.76000 23.83200  -64.29300 1.000 97.12480  ? 215 ALA G O   1 
ATOM   4764 C CB  . ALA D 4 215 ? -33.29900 25.05600  -65.68200 1.000 94.63240  ? 215 ALA G CB  1 
ATOM   4765 N N   . GLY D 4 216 ? -34.30100 24.02900  -62.58100 1.000 99.75407  ? 216 GLY G N   1 
ATOM   4766 C CA  . GLY D 4 216 ? -35.32000 24.13000  -61.55900 1.000 101.00948 ? 216 GLY G CA  1 
ATOM   4767 C C   . GLY D 4 216 ? -35.77600 22.81700  -60.95800 1.000 100.05147 ? 216 GLY G C   1 
ATOM   4768 O O   . GLY D 4 216 ? -36.68300 22.82700  -60.11600 1.000 102.12014 ? 216 GLY G O   1 
ATOM   4769 N N   . GLU D 4 217 ? -35.18200 21.69400  -61.35700 1.000 115.53491 ? 217 GLU G N   1 
ATOM   4770 C CA  . GLU D 4 217 ? -35.53500 20.37700  -60.84900 1.000 114.79534 ? 217 GLU G CA  1 
ATOM   4771 C C   . GLU D 4 217 ? -34.45900 19.88100  -59.89000 1.000 111.71076 ? 217 GLU G C   1 
ATOM   4772 O O   . GLU D 4 217 ? -33.28900 20.26100  -59.99400 1.000 109.84475 ? 217 GLU G O   1 
ATOM   4773 C CB  . GLU D 4 217 ? -35.72100 19.37500  -62.00000 1.000 115.20855 ? 217 GLU G CB  1 
ATOM   4774 C CG  . GLU D 4 217 ? -36.31200 18.02400  -61.59300 1.000 116.01654 ? 217 GLU G CG  1 
ATOM   4775 C CD  . GLU D 4 217 ? -36.25800 16.99300  -62.71100 1.000 115.42173 ? 217 GLU G CD  1 
ATOM   4776 O OE1 . GLU D 4 217 ? -35.83200 17.34500  -63.83200 1.000 115.61123 ? 217 GLU G OE1 1 
ATOM   4777 O OE2 . GLU D 4 217 ? -36.64000 15.82900  -62.46700 1.000 115.02958 ? 217 GLU G OE2 1 
ATOM   4778 N N   . SER D 4 218 ? -34.86800 19.02100  -58.95600 1.000 91.37411  ? 218 SER G N   1 
ATOM   4779 C CA  . SER D 4 218 ? -33.99300 18.53900  -57.89500 1.000 89.75023  ? 218 SER G CA  1 
ATOM   4780 C C   . SER D 4 218 ? -33.23500 17.29100  -58.32500 1.000 88.43166  ? 218 SER G C   1 
ATOM   4781 O O   . SER D 4 218 ? -33.78200 16.41100  -58.99900 1.000 89.30544  ? 218 SER G O   1 
ATOM   4782 C CB  . SER D 4 218 ? -34.80100 18.23900  -56.63200 1.000 90.07659  ? 218 SER G CB  1 
ATOM   4783 O OG  . SER D 4 218 ? -35.86200 17.34600  -56.91800 1.000 92.32686  ? 218 SER G OG  1 
ATOM   4784 N N   . VAL D 4 219 ? -31.97300 17.21900  -57.91700 1.000 68.94248  ? 219 VAL G N   1 
ATOM   4785 C CA  . VAL D 4 219 ? -31.11400 16.06700  -58.16800 1.000 68.92669  ? 219 VAL G CA  1 
ATOM   4786 C C   . VAL D 4 219 ? -30.39100 15.72200  -56.87200 1.000 67.21332  ? 219 VAL G C   1 
ATOM   4787 O O   . VAL D 4 219 ? -29.70000 16.56900  -56.29500 1.000 66.01318  ? 219 VAL G O   1 
ATOM   4788 C CB  . VAL D 4 219 ? -30.10200 16.33500  -59.29400 1.000 68.08974  ? 219 VAL G CB  1 
ATOM   4789 C CG1 . VAL D 4 219 ? -29.52700 17.74500  -59.17700 1.000 68.19502  ? 219 VAL G CG1 1 
ATOM   4790 C CG2 . VAL D 4 219 ? -28.98300 15.29600  -59.27200 1.000 67.25280  ? 219 VAL G CG2 1 
ATOM   4791 N N   . THR D 4 220 ? -30.54500 14.48100  -56.42100 1.000 75.06690  ? 220 THR G N   1 
ATOM   4792 C CA  . THR D 4 220 ? -29.83900 13.97300  -55.25400 1.000 73.74305  ? 220 THR G CA  1 
ATOM   4793 C C   . THR D 4 220 ? -28.91500 12.84200  -55.69400 1.000 72.64292  ? 220 THR G C   1 
ATOM   4794 O O   . THR D 4 220 ? -29.31800 11.97300  -56.47300 1.000 73.01402  ? 220 THR G O   1 
ATOM   4795 C CB  . THR D 4 220 ? -30.83600 13.49900  -54.18700 1.000 74.68527  ? 220 THR G CB  1 
ATOM   4796 O OG1 . THR D 4 220 ? -31.45100 12.27800  -54.61300 1.000 75.86962  ? 220 THR G OG1 1 
ATOM   4797 C CG2 . THR D 4 220 ? -31.93300 14.54400  -53.96100 1.000 74.84582  ? 220 THR G CG2 1 
ATOM   4798 N N   . LEU D 4 221 ? -27.67700 12.86100  -55.21100 1.000 59.71242  ? 221 LEU G N   1 
ATOM   4799 C CA  . LEU D 4 221 ? -26.68000 11.85000  -55.55700 1.000 58.95970  ? 221 LEU G CA  1 
ATOM   4800 C C   . LEU D 4 221 ? -26.54500 10.85900  -54.40800 1.000 58.06486  ? 221 LEU G C   1 
ATOM   4801 O O   . LEU D 4 221 ? -26.25900 11.25900  -53.27300 1.000 57.58059  ? 221 LEU G O   1 
ATOM   4802 C CB  . LEU D 4 221 ? -25.32600 12.48900  -55.85700 1.000 58.11223  ? 221 LEU G CB  1 
ATOM   4803 C CG  . LEU D 4 221 ? -25.28800 13.47100  -57.02600 1.000 59.63347  ? 221 LEU G CG  1 
ATOM   4804 C CD1 . LEU D 4 221 ? -23.84400 13.76900  -57.38500 1.000 59.14130  ? 221 LEU G CD1 1 
ATOM   4805 C CD2 . LEU D 4 221 ? -26.04200 12.90600  -58.21600 1.000 60.14669  ? 221 LEU G CD2 1 
ATOM   4806 N N   . SER D 4 222 ? -26.73000 9.57100   -54.70500 1.000 61.99954  ? 222 SER G N   1 
ATOM   4807 C CA  . SER D 4 222 ? -26.73800 8.50900   -53.70000 1.000 61.39947  ? 222 SER G CA  1 
ATOM   4808 C C   . SER D 4 222 ? -25.47700 7.65200   -53.80800 1.000 59.77032  ? 222 SER G C   1 
ATOM   4809 O O   . SER D 4 222 ? -25.27100 6.95700   -54.80800 1.000 59.79138  ? 222 SER G O   1 
ATOM   4810 C CB  . SER D 4 222 ? -27.98300 7.65000   -53.86400 1.000 61.68371  ? 222 SER G CB  1 
ATOM   4811 O OG  . SER D 4 222 ? -29.13800 8.41200   -53.59300 1.000 62.26536  ? 222 SER G OG  1 
ATOM   4812 N N   . CYS D 4 223 ? -24.66000 7.67100   -52.75900 1.000 61.07838  ? 223 CYS G N   1 
ATOM   4813 C CA  . CYS D 4 223 ? -23.52100 6.76900   -52.62100 1.000 59.35185  ? 223 CYS G CA  1 
ATOM   4814 C C   . CYS D 4 223 ? -23.91000 5.57600   -51.74400 1.000 58.81758  ? 223 CYS G C   1 
ATOM   4815 O O   . CYS D 4 223 ? -24.45200 5.76100   -50.65200 1.000 58.69388  ? 223 CYS G O   1 
ATOM   4816 C CB  . CYS D 4 223 ? -22.33500 7.51600   -52.02100 1.000 58.53070  ? 223 CYS G CB  1 
ATOM   4817 S SG  . CYS D 4 223 ? -20.75400 6.71200   -52.29400 1.000 58.53860  ? 223 CYS G SG  1 
ATOM   4818 N N   . SER D 4 224 ? -23.63000 4.35500   -52.21900 1.000 50.19286  ? 224 SER G N   1 
ATOM   4819 C CA  . SER D 4 224 ? -24.16100 3.13900   -51.60100 1.000 49.65332  ? 224 SER G CA  1 
ATOM   4820 C C   . SER D 4 224 ? -23.11400 2.02800   -51.56300 1.000 48.61899  ? 224 SER G C   1 
ATOM   4821 O O   . SER D 4 224 ? -22.27400 1.91800   -52.45900 1.000 47.88469  ? 224 SER G O   1 
ATOM   4822 C CB  . SER D 4 224 ? -25.39400 2.64100   -52.34900 1.000 50.74293  ? 224 SER G CB  1 
ATOM   4823 O OG  . SER D 4 224 ? -25.88900 1.45000   -51.77200 1.000 51.31668  ? 224 SER G OG  1 
ATOM   4824 N N   . SER D 4 225 ? -23.19300 1.17900   -50.53200 1.000 42.36561  ? 225 SER G N   1 
ATOM   4825 C CA  . SER D 4 225 ? -22.25200 0.07700   -50.38200 1.000 41.62604  ? 225 SER G CA  1 
ATOM   4826 C C   . SER D 4 225 ? -22.79800 -0.95900  -49.40200 1.000 43.22360  ? 225 SER G C   1 
ATOM   4827 O O   . SER D 4 225 ? -23.55300 -0.62900  -48.49000 1.000 44.50534  ? 225 SER G O   1 
ATOM   4828 C CB  . SER D 4 225 ? -20.89300 0.56500   -49.88700 1.000 39.88373  ? 225 SER G CB  1 
ATOM   4829 O OG  . SER D 4 225 ? -19.96600 -0.49600  -49.86200 1.000 39.38893  ? 225 SER G OG  1 
ATOM   4830 N N   . ARG D 4 226 ? -22.37500 -2.20900  -49.59100 1.000 57.52269  ? 226 ARG G N   1 
ATOM   4831 C CA  . ARG D 4 226 ? -22.56300 -3.21100  -48.55300 1.000 56.96736  ? 226 ARG G CA  1 
ATOM   4832 C C   . ARG D 4 226 ? -21.54700 -3.07500  -47.42500 1.000 55.29084  ? 226 ARG G C   1 
ATOM   4833 O O   . ARG D 4 226 ? -21.76600 -3.63000  -46.34300 1.000 55.07502  ? 226 ARG G O   1 
ATOM   4834 C CB  . ARG D 4 226 ? -22.50000 -4.61900  -49.15500 1.000 58.12013  ? 226 ARG G CB  1 
ATOM   4835 N N   . SER D 4 227 ? -20.45000 -2.35200  -47.64000 1.000 39.07574  ? 227 SER G N   1 
ATOM   4836 C CA  . SER D 4 227 ? -19.53300 -2.08300  -46.54400 1.000 37.69399  ? 227 SER G CA  1 
ATOM   4837 C C   . SER D 4 227 ? -20.09000 -0.97400  -45.66600 1.000 37.78085  ? 227 SER G C   1 
ATOM   4838 O O   . SER D 4 227 ? -20.77200 -0.05600  -46.13800 1.000 38.75465  ? 227 SER G O   1 
ATOM   4839 C CB  . SER D 4 227 ? -18.14600 -1.71300  -47.04500 1.000 37.45449  ? 227 SER G CB  1 
ATOM   4840 O OG  . SER D 4 227 ? -17.51700 -2.84200  -47.62300 1.000 38.25722  ? 227 SER G OG  1 
ATOM   4841 N N   . SER D 4 228 ? -19.80100 -1.09300  -44.37100 1.000 49.56121  ? 228 SER G N   1 
ATOM   4842 C CA  . SER D 4 228 ? -20.34600 -0.15000  -43.36300 1.000 50.95874  ? 228 SER G CA  1 
ATOM   4843 C C   . SER D 4 228 ? -19.52200 1.12900   -43.25500 1.000 50.87189  ? 228 SER G C   1 
ATOM   4844 O O   . SER D 4 228 ? -19.00400 1.39900   -42.16600 1.000 51.83253  ? 228 SER G O   1 
ATOM   4845 C CB  . SER D 4 228 ? -20.43900 -0.82800  -42.02200 1.000 51.84569  ? 228 SER G CB  1 
ATOM   4846 O OG  . SER D 4 228 ? -20.95600 0.05800   -41.04400 1.000 54.87500  ? 228 SER G OG  1 
ATOM   4847 N N   . TYR D 4 229 ? -19.42100 1.88300   -44.34200 1.000 39.38367  ? 229 TYR G N   1 
ATOM   4848 C CA  . TYR D 4 229 ? -18.76400 3.20400   -44.26700 1.000 39.53369  ? 229 TYR G CA  1 
ATOM   4849 C C   . TYR D 4 229 ? -19.60700 4.06200   -43.32800 1.000 43.16307  ? 229 TYR G C   1 
ATOM   4850 O O   . TYR D 4 229 ? -20.83600 4.01900   -43.42800 1.000 44.79221  ? 229 TYR G O   1 
ATOM   4851 C CB  . TYR D 4 229 ? -18.64000 3.78300   -45.67200 1.000 38.93362  ? 229 TYR G CB  1 
ATOM   4852 C CG  . TYR D 4 229 ? -17.72600 2.98500   -46.56300 1.000 37.11234  ? 229 TYR G CG  1 
ATOM   4853 C CD1 . TYR D 4 229 ? -16.37800 2.88000   -46.27400 1.000 36.48069  ? 229 TYR G CD1 1 
ATOM   4854 C CD2 . TYR D 4 229 ? -18.20900 2.31100   -47.67000 1.000 37.17288  ? 229 TYR G CD2 1 
ATOM   4855 C CE1 . TYR D 4 229 ? -15.52700 2.14100   -47.07400 1.000 36.17802  ? 229 TYR G CE1 1 
ATOM   4856 C CE2 . TYR D 4 229 ? -17.37100 1.56800   -48.48100 1.000 36.77020  ? 229 TYR G CE2 1 
ATOM   4857 C CZ  . TYR D 4 229 ? -16.02500 1.48400   -48.18100 1.000 36.44648  ? 229 TYR G CZ  1 
ATOM   4858 O OH  . TYR D 4 229 ? -15.18600 0.75300   -48.96300 1.000 37.99403  ? 229 TYR G OH  1 
ATOM   4859 N N   . ASP D 4 230 ? -18.97100 4.80800   -42.44000 1.000 50.93505  ? 230 ASP G N   1 
ATOM   4860 C CA  . ASP D 4 230 ? -19.77900 5.70100   -41.57900 1.000 55.03028  ? 230 ASP G CA  1 
ATOM   4861 C C   . ASP D 4 230 ? -19.89500 7.09000   -42.20800 1.000 57.46742  ? 230 ASP G C   1 
ATOM   4862 O O   . ASP D 4 230 ? -20.48500 7.96100   -41.56600 1.000 62.25220  ? 230 ASP G O   1 
ATOM   4863 C CB  . ASP D 4 230 ? -19.27800 5.72200   -40.13700 1.000 55.64615  ? 230 ASP G CB  1 
ATOM   4864 C CG  . ASP D 4 230 ? -17.78300 5.80800   -40.00900 1.000 55.99619  ? 230 ASP G CG  1 
ATOM   4865 O OD1 . ASP D 4 230 ? -17.23700 6.82600   -40.45900 1.000 56.09883  ? 230 ASP G OD1 1 
ATOM   4866 O OD2 . ASP D 4 230 ? -17.19500 4.86800   -39.44200 1.000 55.95934  ? 230 ASP G OD2 1 
ATOM   4867 N N   . MET D 4 231 ? -19.39000 7.26500   -43.43100 1.000 67.22648  ? 231 MET G N   1 
ATOM   4868 C CA  . MET D 4 231 ? -19.46400 8.57500   -44.05400 1.000 70.23474  ? 231 MET G CA  1 
ATOM   4869 C C   . MET D 4 231 ? -19.09900 8.43900   -45.52200 1.000 66.71853  ? 231 MET G C   1 
ATOM   4870 O O   . MET D 4 231 ? -18.24800 7.62400   -45.88700 1.000 62.13903  ? 231 MET G O   1 
ATOM   4871 C CB  . MET D 4 231 ? -18.51500 9.55400   -43.35900 1.000 72.44026  ? 231 MET G CB  1 
ATOM   4872 C CG  . MET D 4 231 ? -18.82800 11.00300  -43.58500 1.000 77.76459  ? 231 MET G CG  1 
ATOM   4873 S SD  . MET D 4 231 ? -17.97100 12.00000  -42.36400 1.000 80.10434  ? 231 MET G SD  1 
ATOM   4874 C CE  . MET D 4 231 ? -16.29100 11.94200  -42.99600 1.000 73.26668  ? 231 MET G CE  1 
ATOM   4875 N N   . TYR D 4 232 ? -19.74000 9.25100   -46.35300 1.000 48.57161  ? 232 TYR G N   1 
ATOM   4876 C CA  . TYR D 4 232 ? -19.45000 9.30100   -47.77700 1.000 45.53967  ? 232 TYR G CA  1 
ATOM   4877 C C   . TYR D 4 232 ? -18.96500 10.69200  -48.15900 1.000 47.22935  ? 232 TYR G C   1 
ATOM   4878 O O   . TYR D 4 232 ? -19.46500 11.70200  -47.64800 1.000 50.04547  ? 232 TYR G O   1 
ATOM   4879 C CB  . TYR D 4 232 ? -20.67100 8.92600   -48.60400 1.000 47.14776  ? 232 TYR G CB  1 
ATOM   4880 C CG  . TYR D 4 232 ? -20.97200 7.44700   -48.54500 1.000 45.95814  ? 232 TYR G CG  1 
ATOM   4881 C CD1 . TYR D 4 232 ? -20.12000 6.53300   -49.14700 1.000 41.29442  ? 232 TYR G CD1 1 
ATOM   4882 C CD2 . TYR D 4 232 ? -22.08700 6.96100   -47.88000 1.000 48.36369  ? 232 TYR G CD2 1 
ATOM   4883 C CE1 . TYR D 4 232 ? -20.37600 5.19300   -49.11600 1.000 39.98374  ? 232 TYR G CE1 1 
ATOM   4884 C CE2 . TYR D 4 232 ? -22.34800 5.60500   -47.83500 1.000 45.40281  ? 232 TYR G CE2 1 
ATOM   4885 C CZ  . TYR D 4 232 ? -21.48200 4.72600   -48.44900 1.000 41.77080  ? 232 TYR G CZ  1 
ATOM   4886 O OH  . TYR D 4 232 ? -21.71800 3.38200   -48.41500 1.000 40.36537  ? 232 TYR G OH  1 
ATOM   4887 N N   . HIS D 4 233 ? -17.99300 10.73800  -49.05800 1.000 52.39576  ? 233 HIS G N   1 
ATOM   4888 C CA  . HIS D 4 233 ? -17.46200 11.98500  -49.58800 1.000 53.44325  ? 233 HIS G CA  1 
ATOM   4889 C C   . HIS D 4 233 ? -17.80800 12.06400  -51.06400 1.000 53.09847  ? 233 HIS G C   1 
ATOM   4890 O O   . HIS D 4 233 ? -17.38300 11.20700  -51.84300 1.000 51.53249  ? 233 HIS G O   1 
ATOM   4891 C CB  . HIS D 4 233 ? -15.95200 12.06000  -49.40400 1.000 50.89031  ? 233 HIS G CB  1 
ATOM   4892 C CG  . HIS D 4 233 ? -15.50300 11.77600  -48.00900 1.000 51.19824  ? 233 HIS G CG  1 
ATOM   4893 N ND1 . HIS D 4 233 ? -15.08300 12.76500  -47.14800 1.000 53.12742  ? 233 HIS G ND1 1 
ATOM   4894 C CD2 . HIS D 4 233 ? -15.40400 10.61300  -47.32600 1.000 49.02693  ? 233 HIS G CD2 1 
ATOM   4895 C CE1 . HIS D 4 233 ? -14.74500 12.22200  -45.99200 1.000 53.41430  ? 233 HIS G CE1 1 
ATOM   4896 N NE2 . HIS D 4 233 ? -14.93000 10.91800  -46.07300 1.000 50.79030  ? 233 HIS G NE2 1 
ATOM   4897 N N   . LEU D 4 234 ? -18.56500 13.08800  -51.44700 1.000 54.60392  ? 234 LEU G N   1 
ATOM   4898 C CA  . LEU D 4 234 ? -18.93100 13.30800  -52.83900 1.000 54.54601  ? 234 LEU G CA  1 
ATOM   4899 C C   . LEU D 4 234 ? -17.98100 14.34700  -53.42200 1.000 55.96724  ? 234 LEU G C   1 
ATOM   4900 O O   . LEU D 4 234 ? -17.87600 15.46400  -52.89800 1.000 58.09118  ? 234 LEU G O   1 
ATOM   4901 C CB  . LEU D 4 234 ? -20.38700 13.75700  -52.95100 1.000 57.62533  ? 234 LEU G CB  1 
ATOM   4902 C CG  . LEU D 4 234 ? -20.94400 14.03800  -54.34600 1.000 58.69651  ? 234 LEU G CG  1 
ATOM   4903 C CD1 . LEU D 4 234 ? -21.10200 12.75700  -55.14200 1.000 57.12001  ? 234 LEU G CD1 1 
ATOM   4904 C CD2 . LEU D 4 234 ? -22.25800 14.77500  -54.22500 1.000 61.82583  ? 234 LEU G CD2 1 
ATOM   4905 N N   . SER D 4 235 ? -17.31100 13.98500  -54.51400 1.000 61.48369  ? 235 SER G N   1 
ATOM   4906 C CA  . SER D 4 235 ? -16.17800 14.73000  -55.05000 1.000 62.29431  ? 235 SER G CA  1 
ATOM   4907 C C   . SER D 4 235 ? -16.42200 14.97900  -56.52800 1.000 63.58394  ? 235 SER G C   1 
ATOM   4908 O O   . SER D 4 235 ? -16.63800 14.03200  -57.28800 1.000 62.89438  ? 235 SER G O   1 
ATOM   4909 C CB  . SER D 4 235 ? -14.87600 13.94200  -54.83000 1.000 59.76769  ? 235 SER G CB  1 
ATOM   4910 O OG  . SER D 4 235 ? -13.74900 14.61300  -55.35400 1.000 62.16535  ? 235 SER G OG  1 
ATOM   4911 N N   . ARG D 4 236 ? -16.38600 16.24900  -56.93300 1.000 71.78229  ? 236 ARG G N   1 
ATOM   4912 C CA  . ARG D 4 236 ? -16.72300 16.65300  -58.29200 1.000 74.78265  ? 236 ARG G CA  1 
ATOM   4913 C C   . ARG D 4 236 ? -15.45800 17.00800  -59.06600 1.000 77.09872  ? 236 ARG G C   1 
ATOM   4914 O O   . ARG D 4 236 ? -14.56400 17.67700  -58.53900 1.000 78.84630  ? 236 ARG G O   1 
ATOM   4915 C CB  . ARG D 4 236 ? -17.68100 17.84700  -58.28100 1.000 79.00947  ? 236 ARG G CB  1 
ATOM   4916 C CG  . ARG D 4 236 ? -18.49100 18.02500  -59.55300 1.000 81.80718  ? 236 ARG G CG  1 
ATOM   4917 C CD  . ARG D 4 236 ? -19.17500 19.38900  -59.57400 1.000 87.59471  ? 236 ARG G CD  1 
ATOM   4918 N NE  . ARG D 4 236 ? -18.19500 20.46400  -59.60200 1.000 92.35055  ? 236 ARG G NE  1 
ATOM   4919 C CZ  . ARG D 4 236 ? -17.74600 21.03400  -60.71200 1.000 97.01426  ? 236 ARG G CZ  1 
ATOM   4920 N NH1 . ARG D 4 236 ? -18.19600 20.67500  -61.90400 1.000 97.82489  ? 236 ARG G NH1 1 
ATOM   4921 N NH2 . ARG D 4 236 ? -16.82400 21.98500  -60.62600 1.000 100.93052 ? 236 ARG G NH2 1 
ATOM   4922 N N   . GLU D 4 237 ? -15.38600 16.55200  -60.31700 1.000 77.73564  ? 237 GLU G N   1 
ATOM   4923 C CA  . GLU D 4 237 ? -14.20500 16.79200  -61.13600 1.000 81.59926  ? 237 GLU G CA  1 
ATOM   4924 C C   . GLU D 4 237 ? -14.00400 18.28700  -61.35000 1.000 87.27362  ? 237 GLU G C   1 
ATOM   4925 O O   . GLU D 4 237 ? -14.79700 18.93000  -62.04400 1.000 90.82668  ? 237 GLU G O   1 
ATOM   4926 C CB  . GLU D 4 237 ? -14.31700 16.08200  -62.49000 1.000 81.68348  ? 237 GLU G CB  1 
ATOM   4927 C CG  . GLU D 4 237 ? -14.07600 14.57400  -62.46300 1.000 76.83290  ? 237 GLU G CG  1 
ATOM   4928 C CD  . GLU D 4 237 ? -13.67400 14.03400  -63.83200 1.000 79.07790  ? 237 GLU G CD  1 
ATOM   4929 O OE1 . GLU D 4 237 ? -13.96100 14.71200  -64.84300 1.000 83.53896  ? 237 GLU G OE1 1 
ATOM   4930 O OE2 . GLU D 4 237 ? -13.05200 12.95200  -63.90500 1.000 76.61708  ? 237 GLU G OE2 1 
ATOM   4931 N N   . GLY D 4 238 ? -12.96600 18.85300  -60.73800 1.000 79.39636  ? 238 GLY G N   1 
ATOM   4932 C CA  . GLY D 4 238 ? -12.61400 20.24300  -60.93200 1.000 86.17875  ? 238 GLY G CA  1 
ATOM   4933 C C   . GLY D 4 238 ? -13.04600 21.17100  -59.81400 1.000 88.05003  ? 238 GLY G C   1 
ATOM   4934 O O   . GLY D 4 238 ? -12.52700 22.29200  -59.72500 1.000 92.90851  ? 238 GLY G O   1 
ATOM   4935 N N   . GLY D 4 239 ? -13.97500 20.73900  -58.96200 1.000 88.46061  ? 239 GLY G N   1 
ATOM   4936 C CA  . GLY D 4 239 ? -14.44100 21.55900  -57.85600 1.000 89.93184  ? 239 GLY G CA  1 
ATOM   4937 C C   . GLY D 4 239 ? -13.49900 21.52800  -56.66900 1.000 88.71853  ? 239 GLY G C   1 
ATOM   4938 O O   . GLY D 4 239 ? -13.19900 20.45300  -56.14600 1.000 83.48369  ? 239 GLY G O   1 
ATOM   4939 N N   . HIS D 4 241 ? -15.86100 22.00800  -54.59700 1.000 115.10854 ? 241 HIS G N   1 
ATOM   4940 C CA  . HIS D 4 241 ? -17.03300 21.28400  -54.12200 1.000 111.28703 ? 241 HIS G CA  1 
ATOM   4941 C C   . HIS D 4 241 ? -16.64100 19.91900  -53.53300 1.000 104.73624 ? 241 HIS G C   1 
ATOM   4942 O O   . HIS D 4 241 ? -16.32400 18.97900  -54.26700 1.000 101.51217 ? 241 HIS G O   1 
ATOM   4943 C CB  . HIS D 4 241 ? -18.04600 21.11400  -55.25800 1.000 111.85815 ? 241 HIS G CB  1 
ATOM   4944 N N   . GLU D 4 242 ? -16.66500 19.82300  -52.20100 1.000 113.86102 ? 242 GLU G N   1 
ATOM   4945 C CA  . GLU D 4 242 ? -16.25900 18.60900  -51.48500 1.000 109.43944 ? 242 GLU G CA  1 
ATOM   4946 C C   . GLU D 4 242 ? -17.20600 18.38800  -50.30600 1.000 109.74474 ? 242 GLU G C   1 
ATOM   4947 O O   . GLU D 4 242 ? -17.01300 18.96200  -49.23000 1.000 111.26334 ? 242 GLU G O   1 
ATOM   4948 C CB  . GLU D 4 242 ? -14.80900 18.71300  -51.02300 1.000 108.59723 ? 242 GLU G CB  1 
ATOM   4949 C CG  . GLU D 4 242 ? -13.79800 18.05800  -51.95700 1.000 106.67332 ? 242 GLU G CG  1 
ATOM   4950 C CD  . GLU D 4 242 ? -13.68800 16.55600  -51.74900 1.000 103.01761 ? 242 GLU G CD  1 
ATOM   4951 O OE1 . GLU D 4 242 ? -14.49900 15.99400  -50.98000 1.000 101.85958 ? 242 GLU G OE1 1 
ATOM   4952 O OE2 . GLU D 4 242 ? -12.78600 15.93700  -52.35300 1.000 100.82261 ? 242 GLU G OE2 1 
ATOM   4953 N N   . ARG D 4 243 ? -18.20700 17.53400  -50.50800 1.000 77.14609  ? 243 ARG G N   1 
ATOM   4954 C CA  . ARG D 4 243 ? -19.29500 17.33200  -49.56200 1.000 78.84630  ? 243 ARG G CA  1 
ATOM   4955 C C   . ARG D 4 243 ? -19.08200 16.04900  -48.75900 1.000 76.20124  ? 243 ARG G C   1 
ATOM   4956 O O   . ARG D 4 243 ? -18.54300 15.06300  -49.26500 1.000 73.71410  ? 243 ARG G O   1 
ATOM   4957 C CB  . ARG D 4 243 ? -20.64400 17.26900  -50.29300 1.000 79.60691  ? 243 ARG G CB  1 
ATOM   4958 C CG  . ARG D 4 243 ? -20.96600 18.47400  -51.19400 1.000 82.90731  ? 243 ARG G CG  1 
ATOM   4959 C CD  . ARG D 4 243 ? -20.42600 18.31700  -52.63000 1.000 81.31764  ? 243 ARG G CD  1 
ATOM   4960 N NE  . ARG D 4 243 ? -20.48800 19.56400  -53.39500 1.000 85.26022  ? 243 ARG G NE  1 
ATOM   4961 C CZ  . ARG D 4 243 ? -21.48600 19.91100  -54.20100 1.000 87.53681  ? 243 ARG G CZ  1 
ATOM   4962 N NH1 . ARG D 4 243 ? -22.53200 19.12100  -54.38500 1.000 85.38129  ? 243 ARG G NH1 1 
ATOM   4963 N NH2 . ARG D 4 243 ? -21.43500 21.08400  -54.83500 1.000 92.07157  ? 243 ARG G NH2 1 
ATOM   4964 N N   . ARG D 4 244 ? -19.51000 16.07800  -47.49400 1.000 73.07455  ? 244 ARG G N   1 
ATOM   4965 C CA  . ARG D 4 244 ? -19.44300 14.94400  -46.58400 1.000 72.58239  ? 244 ARG G CA  1 
ATOM   4966 C C   . ARG D 4 244 ? -20.81000 14.74800  -45.94600 1.000 75.96437  ? 244 ARG G C   1 
ATOM   4967 O O   . ARG D 4 244 ? -21.50300 15.72200  -45.63300 1.000 79.23318  ? 244 ARG G O   1 
ATOM   4968 C CB  . ARG D 4 244 ? -18.38800 15.15400  -45.48200 1.000 72.63239  ? 244 ARG G CB  1 
ATOM   4969 C CG  . ARG D 4 244 ? -17.00400 15.53500  -45.98100 1.000 70.71637  ? 244 ARG G CG  1 
ATOM   4970 C CD  . ARG D 4 244 ? -16.17200 16.25300  -44.89500 1.000 71.80861  ? 244 ARG G CD  1 
ATOM   4971 N NE  . ARG D 4 244 ? -16.10800 15.49100  -43.65000 1.000 72.66924  ? 244 ARG G NE  1 
ATOM   4972 C CZ  . ARG D 4 244 ? -16.67000 15.86600  -42.50600 1.000 75.86699  ? 244 ARG G CZ  1 
ATOM   4973 N NH1 . ARG D 4 244 ? -17.30500 17.02100  -42.39500 1.000 78.48309  ? 244 ARG G NH1 1 
ATOM   4974 N NH2 . ARG D 4 244 ? -16.58800 15.06500  -41.44700 1.000 75.42746  ? 244 ARG G NH2 1 
ATOM   4975 N N   . LEU D 4 245 ? -21.19200 13.48800  -45.74900 1.000 66.42902  ? 245 LEU G N   1 
ATOM   4976 C CA  . LEU D 4 245 ? -22.48600 13.13300  -45.18700 1.000 68.73193  ? 245 LEU G CA  1 
ATOM   4977 C C   . LEU D 4 245 ? -22.36300 11.79400  -44.48800 1.000 68.40294  ? 245 LEU G C   1 
ATOM   4978 O O   . LEU D 4 245 ? -21.61200 10.92700  -44.94700 1.000 66.32111  ? 245 LEU G O   1 
ATOM   4979 C CB  . LEU D 4 245 ? -23.57300 13.04500  -46.26400 1.000 68.90300  ? 245 LEU G CB  1 
ATOM   4980 C CG  . LEU D 4 245 ? -24.38000 14.30600  -46.56800 1.000 71.21117  ? 245 LEU G CG  1 
ATOM   4981 C CD1 . LEU D 4 245 ? -25.49600 13.95600  -47.52900 1.000 70.86639  ? 245 LEU G CD1 1 
ATOM   4982 C CD2 . LEU D 4 245 ? -24.94600 14.91800  -45.29800 1.000 73.51934  ? 245 LEU G CD2 1 
ATOM   4983 N N   . PRO D 4 246 ? -23.08900 11.58600  -43.39700 1.000 62.78121  ? 246 PRO G N   1 
ATOM   4984 C CA  . PRO D 4 246 ? -23.05700 10.28300  -42.73500 1.000 60.58884  ? 246 PRO G CA  1 
ATOM   4985 C C   . PRO D 4 246 ? -23.86400 9.25600   -43.50700 1.000 58.68335  ? 246 PRO G C   1 
ATOM   4986 O O   . PRO D 4 246 ? -24.89100 9.55800   -44.11900 1.000 59.99404  ? 246 PRO G O   1 
ATOM   4987 C CB  . PRO D 4 246 ? -23.69500 10.56900  -41.37100 1.000 62.31010  ? 246 PRO G CB  1 
ATOM   4988 C CG  . PRO D 4 246 ? -24.63400 11.69400  -41.65000 1.000 65.62892  ? 246 PRO G CG  1 
ATOM   4989 C CD  . PRO D 4 246 ? -23.97100 12.54100  -42.70100 1.000 65.13939  ? 246 PRO G CD  1 
ATOM   4990 N N   . ALA D 4 247 ? -23.38100 8.02300   -43.47100 1.000 57.91484  ? 247 ALA G N   1 
ATOM   4991 C CA  . ALA D 4 247 ? -24.11800 6.93400   -44.08500 1.000 56.40150  ? 247 ALA G CA  1 
ATOM   4992 C C   . ALA D 4 247 ? -25.19400 6.42100   -43.12900 1.000 56.58836  ? 247 ALA G C   1 
ATOM   4993 O O   . ALA D 4 247 ? -25.03900 6.46900   -41.90500 1.000 56.81207  ? 247 ALA G O   1 
ATOM   4994 C CB  . ALA D 4 247 ? -23.16100 5.81300   -44.47800 1.000 51.52723  ? 247 ALA G CB  1 
ATOM   4995 N N   . VAL D 4 248 ? -26.31100 5.95900   -43.69800 1.000 61.81267  ? 248 VAL G N   1 
ATOM   4996 C CA  . VAL D 4 248 ? -27.39700 5.36500   -42.92700 1.000 62.63909  ? 248 VAL G CA  1 
ATOM   4997 C C   . VAL D 4 248 ? -27.70700 3.99000   -43.50800 1.000 60.84151  ? 248 VAL G C   1 
ATOM   4998 O O   . VAL D 4 248 ? -27.61700 3.78300   -44.72500 1.000 59.78612  ? 248 VAL G O   1 
ATOM   4999 C CB  . VAL D 4 248 ? -28.65700 6.26800   -42.89800 1.000 66.21057  ? 248 VAL G CB  1 
ATOM   5000 C CG1 . VAL D 4 248 ? -28.36500 7.59300   -42.17600 1.000 68.76088  ? 248 VAL G CG1 1 
ATOM   5001 C CG2 . VAL D 4 248 ? -29.22200 6.51200   -44.29700 1.000 67.10015  ? 248 VAL G CG2 1 
ATOM   5002 N N   . ARG D 4 249 ? -28.03800 3.04000   -42.62900 1.000 74.16942  ? 249 ARG G N   1 
ATOM   5003 C CA  . ARG D 4 249 ? -28.28200 1.66400   -43.04400 1.000 71.83230  ? 249 ARG G CA  1 
ATOM   5004 C C   . ARG D 4 249 ? -29.70800 1.51700   -43.56400 1.000 73.72989  ? 249 ARG G C   1 
ATOM   5005 O O   . ARG D 4 249 ? -30.66100 2.00200   -42.94700 1.000 76.39600  ? 249 ARG G O   1 
ATOM   5006 C CB  . ARG D 4 249 ? -28.03000 0.69700   -41.88200 1.000 71.29276  ? 249 ARG G CB  1 
ATOM   5007 C CG  . ARG D 4 249 ? -28.26000 -0.78000  -42.23000 1.000 70.77164  ? 249 ARG G CG  1 
ATOM   5008 C CD  . ARG D 4 249 ? -27.56000 -1.75100  -41.26600 1.000 70.08472  ? 249 ARG G CD  1 
ATOM   5009 N NE  . ARG D 4 249 ? -26.73700 -2.71700  -41.99200 1.000 68.38451  ? 249 ARG G NE  1 
ATOM   5010 C CZ  . ARG D 4 249 ? -25.78300 -3.47000  -41.45100 1.000 67.84498  ? 249 ARG G CZ  1 
ATOM   5011 N NH1 . ARG D 4 249 ? -25.53100 -3.44200  -40.15000 1.000 68.91353  ? 249 ARG G NH1 1 
ATOM   5012 N NH2 . ARG D 4 249 ? -25.05000 -4.25600  -42.23900 1.000 65.02622  ? 249 ARG G NH2 1 
ATOM   5013 N N   . LYS D 4 250 ? -29.84400 0.85000   -44.70400 1.000 59.71242  ? 250 LYS G N   1 
ATOM   5014 C CA  . LYS D 4 250 ? -31.11900 0.63700   -45.37000 1.000 61.20997  ? 250 LYS G CA  1 
ATOM   5015 C C   . LYS D 4 250 ? -31.62300 -0.77700  -45.10200 1.000 61.57580  ? 250 LYS G C   1 
ATOM   5016 O O   . LYS D 4 250 ? -30.90900 -1.62500  -44.57000 1.000 60.59674  ? 250 LYS G O   1 
ATOM   5017 C CB  . LYS D 4 250 ? -30.97200 0.89000   -46.87300 1.000 61.08890  ? 250 LYS G CB  1 
ATOM   5018 C CG  . LYS D 4 250 ? -30.52200 2.31000   -47.19900 1.000 61.94164  ? 250 LYS G CG  1 
ATOM   5019 C CD  . LYS D 4 250 ? -31.31500 3.31700   -46.37100 1.000 64.80777  ? 250 LYS G CD  1 
ATOM   5020 C CE  . LYS D 4 250 ? -31.40900 4.67200   -47.04300 1.000 66.25531  ? 250 LYS G CE  1 
ATOM   5021 N NZ  . LYS D 4 250 ? -32.66100 4.80800   -47.84300 1.000 67.80023  ? 250 LYS G NZ  1 
ATOM   5022 N N   . VAL D 4 251 ? -32.87000 -1.02900  -45.49200 1.000 62.18377  ? 251 VAL G N   1 
ATOM   5023 C CA  . VAL D 4 251 ? -33.49400 -2.31100  -45.17400 1.000 65.28678  ? 251 VAL G CA  1 
ATOM   5024 C C   . VAL D 4 251 ? -32.72700 -3.46500  -45.81800 1.000 63.27074  ? 251 VAL G C   1 
ATOM   5025 O O   . VAL D 4 251 ? -32.55400 -4.52900  -45.20900 1.000 64.80777  ? 251 VAL G O   1 
ATOM   5026 C CB  . VAL D 4 251 ? -34.97900 -2.30100  -45.58200 1.000 69.20303  ? 251 VAL G CB  1 
ATOM   5027 C CG1 . VAL D 4 251 ? -35.55800 -3.69400  -45.49700 1.000 72.47711  ? 251 VAL G CG1 1 
ATOM   5028 C CG2 . VAL D 4 251 ? -35.76400 -1.35000  -44.68800 1.000 72.27972  ? 251 VAL G CG2 1 
ATOM   5029 N N   . ASN D 4 252 ? -32.21800 -3.26800  -47.03400 1.000 60.19932  ? 252 ASN G N   1 
ATOM   5030 C CA  . ASN D 4 252 ? -31.49200 -4.32600  -47.72400 1.000 58.61755  ? 252 ASN G CA  1 
ATOM   5031 C C   . ASN D 4 252 ? -30.04700 -4.46700  -47.25300 1.000 55.61719  ? 252 ASN G C   1 
ATOM   5032 O O   . ASN D 4 252 ? -29.26300 -5.14100  -47.92900 1.000 53.88541  ? 252 ASN G O   1 
ATOM   5033 C CB  . ASN D 4 252 ? -31.53300 -4.08400  -49.23300 1.000 57.42004  ? 252 ASN G CB  1 
ATOM   5034 C CG  . ASN D 4 252 ? -31.04300 -2.70100  -49.61500 1.000 55.73826  ? 252 ASN G CG  1 
ATOM   5035 O OD1 . ASN D 4 252 ? -30.27800 -2.07300  -48.88700 1.000 55.08818  ? 252 ASN G OD1 1 
ATOM   5036 N ND2 . ASN D 4 252 ? -31.48100 -2.22100  -50.77000 1.000 56.85155  ? 252 ASN G ND2 1 
ATOM   5037 N N   . ARG D 4 253 ? -29.68800 -3.83300  -46.13400 1.000 63.03124  ? 253 ARG G N   1 
ATOM   5038 C CA  . ARG D 4 253 ? -28.37500 -3.87200  -45.48700 1.000 60.68096  ? 253 ARG G CA  1 
ATOM   5039 C C   . ARG D 4 253 ? -27.32000 -3.03100  -46.19800 1.000 58.90443  ? 253 ARG G C   1 
ATOM   5040 O O   . ARG D 4 253 ? -26.13700 -3.11700  -45.85100 1.000 57.10948  ? 253 ARG G O   1 
ATOM   5041 C CB  . ARG D 4 253 ? -27.84700 -5.30500  -45.32100 1.000 60.86256  ? 253 ARG G CB  1 
ATOM   5042 C CG  . ARG D 4 253 ? -28.62100 -6.15000  -44.32300 1.000 63.68132  ? 253 ARG G CG  1 
ATOM   5043 C CD  . ARG D 4 253 ? -28.64900 -7.61600  -44.73000 1.000 65.35784  ? 253 ARG G CD  1 
ATOM   5044 N NE  . ARG D 4 253 ? -29.36200 -7.80900  -45.99100 1.000 66.96066  ? 253 ARG G NE  1 
ATOM   5045 C CZ  . ARG D 4 253 ? -28.78600 -8.06300  -47.16100 1.000 64.70513  ? 253 ARG G CZ  1 
ATOM   5046 N NH1 . ARG D 4 253 ? -27.47400 -8.21000  -47.27000 1.000 62.77332  ? 253 ARG G NH1 1 
ATOM   5047 N NH2 . ARG D 4 253 ? -29.54800 -8.18900  -48.24500 1.000 66.11582  ? 253 ARG G NH2 1 
ATOM   5048 N N   . THR D 4 254 ? -27.70300 -2.21400  -47.17200 1.000 49.31381  ? 254 THR G N   1 
ATOM   5049 C CA  . THR D 4 254 ? -26.73500 -1.29200  -47.75600 1.000 48.90323  ? 254 THR G CA  1 
ATOM   5050 C C   . THR D 4 254 ? -26.54600 -0.07200  -46.85000 1.000 48.86902  ? 254 THR G C   1 
ATOM   5051 O O   . THR D 4 254 ? -27.42200 0.28800   -46.05300 1.000 50.48763  ? 254 THR G O   1 
ATOM   5052 C CB  . THR D 4 254 ? -27.17800 -0.83800  -49.15700 1.000 49.41908  ? 254 THR G CB  1 
ATOM   5053 O OG1 . THR D 4 254 ? -28.45100 -0.19800  -49.07000 1.000 51.61145  ? 254 THR G OG1 1 
ATOM   5054 C CG2 . THR D 4 254 ? -27.28700 -2.02000  -50.11300 1.000 49.45330  ? 254 THR G CG2 1 
ATOM   5055 N N   . PHE D 4 255 ? -25.37700 0.55200   -46.97100 1.000 44.10266  ? 255 PHE G N   1 
ATOM   5056 C CA  . PHE D 4 255 ? -25.04600 1.79500   -46.28000 1.000 44.35532  ? 255 PHE G CA  1 
ATOM   5057 C C   . PHE D 4 255 ? -24.98000 2.91300   -47.30700 1.000 46.75561  ? 255 PHE G C   1 
ATOM   5058 O O   . PHE D 4 255 ? -24.34700 2.76400   -48.36000 1.000 45.27911  ? 255 PHE G O   1 
ATOM   5059 C CB  . PHE D 4 255 ? -23.72600 1.67600   -45.51100 1.000 42.31560  ? 255 PHE G CB  1 
ATOM   5060 C CG  . PHE D 4 255 ? -23.83800 0.82400   -44.26700 1.000 42.26033  ? 255 PHE G CG  1 
ATOM   5061 C CD1 . PHE D 4 255 ? -23.77900 -0.55500  -44.35400 1.000 42.39719  ? 255 PHE G CD1 1 
ATOM   5062 C CD2 . PHE D 4 255 ? -24.03900 1.40900   -43.02600 1.000 43.82368  ? 255 PHE G CD2 1 
ATOM   5063 C CE1 . PHE D 4 255 ? -23.90200 -1.34600  -43.21300 1.000 44.31321  ? 255 PHE G CE1 1 
ATOM   5064 C CE2 . PHE D 4 255 ? -24.17200 0.62600   -41.87400 1.000 45.65811  ? 255 PHE G CE2 1 
ATOM   5065 C CZ  . PHE D 4 255 ? -24.09300 -0.74200  -41.97000 1.000 45.93445  ? 255 PHE G CZ  1 
ATOM   5066 N N   . GLN D 4 256 ? -25.62200 4.03100   -46.99300 1.000 55.76984  ? 256 GLN G N   1 
ATOM   5067 C CA  . GLN D 4 256 ? -25.99700 4.97300   -48.02600 1.000 57.77535  ? 256 GLN G CA  1 
ATOM   5068 C C   . GLN D 4 256 ? -26.09800 6.37100   -47.43500 1.000 61.08364  ? 256 GLN G C   1 
ATOM   5069 O O   . GLN D 4 256 ? -26.45600 6.54700   -46.26700 1.000 61.78899  ? 256 GLN G O   1 
ATOM   5070 C CB  . GLN D 4 256 ? -27.32400 4.54400   -48.66700 1.000 58.75968  ? 256 GLN G CB  1 
ATOM   5071 C CG  . GLN D 4 256 ? -27.77300 5.38200   -49.84200 1.000 60.05194  ? 256 GLN G CG  1 
ATOM   5072 C CD  . GLN D 4 256 ? -29.08200 4.88800   -50.42100 1.000 59.83612  ? 256 GLN G CD  1 
ATOM   5073 O OE1 . GLN D 4 256 ? -29.10500 3.95900   -51.22600 1.000 58.63861  ? 256 GLN G OE1 1 
ATOM   5074 N NE2 . GLN D 4 256 ? -30.17900 5.50200   -50.00900 1.000 62.05218  ? 256 GLN G NE2 1 
ATOM   5075 N N   . ALA D 4 257 ? -25.74900 7.36000   -48.25700 1.000 58.80442  ? 257 ALA G N   1 
ATOM   5076 C CA  . ALA D 4 257 ? -25.94200 8.77200   -47.95700 1.000 61.15207  ? 257 ALA G CA  1 
ATOM   5077 C C   . ALA D 4 257 ? -26.48200 9.44400   -49.20600 1.000 60.88625  ? 257 ALA G C   1 
ATOM   5078 O O   . ALA D 4 257 ? -26.06700 9.11800   -50.32200 1.000 59.31237  ? 257 ALA G O   1 
ATOM   5079 C CB  . ALA D 4 257 ? -24.64300 9.46300   -47.51500 1.000 61.01258  ? 257 ALA G CB  1 
ATOM   5080 N N   . ASP D 4 258 ? -27.40700 10.37400  -49.01400 1.000 85.12863  ? 258 ASP G N   1 
ATOM   5081 C CA  . ASP D 4 258 ? -28.08300 11.05100  -50.11200 1.000 86.01031  ? 258 ASP G CA  1 
ATOM   5082 C C   . ASP D 4 258 ? -27.68600 12.52300  -50.11000 1.000 87.26046  ? 258 ASP G C   1 
ATOM   5083 O O   . ASP D 4 258 ? -28.00000 13.25700  -49.16900 1.000 89.94763  ? 258 ASP G O   1 
ATOM   5084 C CB  . ASP D 4 258 ? -29.59600 10.87400  -50.00100 1.000 86.74461  ? 258 ASP G CB  1 
ATOM   5085 C CG  . ASP D 4 258 ? -30.04800 9.49300   -50.43100 1.000 85.56289  ? 258 ASP G CG  1 
ATOM   5086 O OD1 . ASP D 4 258 ? -29.75600 9.10700   -51.58200 1.000 83.70214  ? 258 ASP G OD1 1 
ATOM   5087 O OD2 . ASP D 4 258 ? -30.67900 8.78600   -49.61600 1.000 86.38667  ? 258 ASP G OD2 1 
ATOM   5088 N N   . PHE D 4 259 ? -26.99800 12.94600  -51.17000 1.000 61.02311  ? 259 PHE G N   1 
ATOM   5089 C CA  . PHE D 4 259 ? -26.49500 14.30100  -51.34300 1.000 61.19418  ? 259 PHE G CA  1 
ATOM   5090 C C   . PHE D 4 259 ? -27.47000 15.09600  -52.21400 1.000 65.19203  ? 259 PHE G C   1 
ATOM   5091 O O   . PHE D 4 259 ? -27.45100 14.95300  -53.44500 1.000 65.30257  ? 259 PHE G O   1 
ATOM   5092 C CB  . PHE D 4 259 ? -25.10100 14.28400  -51.98300 1.000 59.02023  ? 259 PHE G CB  1 
ATOM   5093 C CG  . PHE D 4 259 ? -24.00100 13.74000  -51.09100 1.000 58.05170  ? 259 PHE G CG  1 
ATOM   5094 C CD1 . PHE D 4 259 ? -23.34300 14.56800  -50.18800 1.000 58.58071  ? 259 PHE G CD1 1 
ATOM   5095 C CD2 . PHE D 4 259 ? -23.59600 12.41200  -51.18400 1.000 55.25926  ? 259 PHE G CD2 1 
ATOM   5096 C CE1 . PHE D 4 259 ? -22.32100 14.07700  -49.37600 1.000 56.99368  ? 259 PHE G CE1 1 
ATOM   5097 C CE2 . PHE D 4 259 ? -22.57300 11.92300  -50.38200 1.000 54.36704  ? 259 PHE G CE2 1 
ATOM   5098 C CZ  . PHE D 4 259 ? -21.93600 12.75800  -49.47800 1.000 55.32769  ? 259 PHE G CZ  1 
ATOM   5099 N N   . PRO D 4 260 ? -28.34000 15.92700  -51.64400 1.000 76.44864  ? 260 PRO G N   1 
ATOM   5100 C CA  . PRO D 4 260 ? -29.21300 16.75300  -52.48900 1.000 78.69628  ? 260 PRO G CA  1 
ATOM   5101 C C   . PRO D 4 260 ? -28.41200 17.86700  -53.14800 1.000 78.93052  ? 260 PRO G C   1 
ATOM   5102 O O   . PRO D 4 260 ? -27.65200 18.57700  -52.48900 1.000 79.70429  ? 260 PRO G O   1 
ATOM   5103 C CB  . PRO D 4 260 ? -30.25300 17.30400  -51.50400 1.000 81.89666  ? 260 PRO G CB  1 
ATOM   5104 C CG  . PRO D 4 260 ? -29.55400 17.27800  -50.17400 1.000 82.29934  ? 260 PRO G CG  1 
ATOM   5105 C CD  . PRO D 4 260 ? -28.58600 16.13300  -50.20500 1.000 78.09094  ? 260 PRO G CD  1 
ATOM   5106 N N   . LEU D 4 261 ? -28.55800 17.99500  -54.46000 1.000 81.10446  ? 261 LEU G N   1 
ATOM   5107 C CA  . LEU D 4 261 ? -27.92700 19.08500  -55.18200 1.000 84.21010  ? 261 LEU G CA  1 
ATOM   5108 C C   . LEU D 4 261 ? -28.95200 20.19600  -55.41300 1.000 89.71339  ? 261 LEU G C   1 
ATOM   5109 O O   . LEU D 4 261 ? -30.13400 20.07300  -55.07200 1.000 90.48190  ? 261 LEU G O   1 
ATOM   5110 C CB  . LEU D 4 261 ? -27.31200 18.57800  -56.49200 1.000 81.98088  ? 261 LEU G CB  1 
ATOM   5111 C CG  . LEU D 4 261 ? -25.85600 18.08800  -56.44600 1.000 78.37519  ? 261 LEU G CG  1 
ATOM   5112 C CD1 . LEU D 4 261 ? -25.53700 17.34400  -55.16300 1.000 75.73803  ? 261 LEU G CD1 1 
ATOM   5113 C CD2 . LEU D 4 261 ? -25.55800 17.21300  -57.65100 1.000 76.01175  ? 261 LEU G CD2 1 
ATOM   5114 N N   . GLY D 4 262 ? -28.48500 21.30000  -55.99000 1.000 107.11021 ? 262 GLY G N   1 
ATOM   5115 C CA  . GLY D 4 262 ? -29.31400 22.46400  -56.18900 1.000 113.60046 ? 262 GLY G CA  1 
ATOM   5116 C C   . GLY D 4 262 ? -28.95600 23.57200  -55.21900 1.000 117.33775 ? 262 GLY G C   1 
ATOM   5117 O O   . GLY D 4 262 ? -27.92600 23.51900  -54.54100 1.000 115.12959 ? 262 GLY G O   1 
ATOM   5118 N N   . PRO D 4 263 ? -29.79600 24.61600  -55.13900 1.000 122.31993 ? 263 PRO G N   1 
ATOM   5119 C CA  . PRO D 4 263 ? -30.99100 24.86100  -55.95700 1.000 126.65992 ? 263 PRO G CA  1 
ATOM   5120 C C   . PRO D 4 263 ? -30.68800 25.27300  -57.39800 1.000 129.94716 ? 263 PRO G C   1 
ATOM   5121 O O   . PRO D 4 263 ? -31.61300 25.62900  -58.13400 1.000 134.11345 ? 263 PRO G O   1 
ATOM   5122 C CB  . PRO D 4 263 ? -31.68800 26.00800  -55.22000 1.000 131.94740 ? 263 PRO G CB  1 
ATOM   5123 C CG  . PRO D 4 263 ? -30.61500 26.68100  -54.44900 1.000 133.48443 ? 263 PRO G CG  1 
ATOM   5124 C CD  . PRO D 4 263 ? -29.67300 25.59200  -54.04200 1.000 125.80193 ? 263 PRO G CD  1 
ATOM   5125 N N   . ALA D 4 264 ? -29.41200 25.23000  -57.78700 1.000 113.17410 ? 264 ALA G N   1 
ATOM   5126 C CA  . ALA D 4 264 ? -29.01000 25.57900  -59.14300 1.000 116.26394 ? 264 ALA G CA  1 
ATOM   5127 C C   . ALA D 4 264 ? -27.60100 25.08800  -59.44900 1.000 112.18450 ? 264 ALA G C   1 
ATOM   5128 O O   . ALA D 4 264 ? -26.83000 25.79400  -60.10900 1.000 115.90074 ? 264 ALA G O   1 
ATOM   5129 C CB  . ALA D 4 264 ? -29.09600 27.09200  -59.35700 1.000 124.67811 ? 264 ALA G CB  1 
ATOM   5130 N N   . THR D 4 265 ? -27.25100 23.89300  -58.97300 1.000 132.90015 ? 265 THR G N   1 
ATOM   5131 C CA  . THR D 4 265 ? -25.95400 23.31600  -59.30600 1.000 129.55501 ? 265 THR G CA  1 
ATOM   5132 C C   . THR D 4 265 ? -25.83600 23.12600  -60.81200 1.000 131.07624 ? 265 THR G C   1 
ATOM   5133 O O   . THR D 4 265 ? -26.79500 22.73300  -61.48100 1.000 131.32101 ? 265 THR G O   1 
ATOM   5134 C CB  . THR D 4 265 ? -25.75800 21.97300  -58.60000 1.000 121.96726 ? 265 THR G CB  1 
ATOM   5135 O OG1 . THR D 4 265 ? -26.95100 21.18700  -58.72000 1.000 120.23810 ? 265 THR G OG1 1 
ATOM   5136 C CG2 . THR D 4 265 ? -25.41300 22.17200  -57.12700 1.000 119.96175 ? 265 THR G CG2 1 
ATOM   5137 N N   . HIS D 4 266 ? -24.65000 23.41500  -61.34600 1.000 120.06966 ? 266 HIS G N   1 
ATOM   5138 C CA  . HIS D 4 266 ? -24.41500 23.33000  -62.78200 1.000 122.20676 ? 266 HIS G CA  1 
ATOM   5139 C C   . HIS D 4 266 ? -23.90600 21.96300  -63.22200 1.000 116.22973 ? 266 HIS G C   1 
ATOM   5140 O O   . HIS D 4 266 ? -23.90900 21.67500  -64.42300 1.000 117.15878 ? 266 HIS G O   1 
ATOM   5141 C CB  . HIS D 4 266 ? -23.42900 24.41900  -63.22700 1.000 127.66267 ? 266 HIS G CB  1 
ATOM   5142 N N   . GLY D 4 267 ? -23.46600 21.12300  -62.29100 1.000 102.59651 ? 267 GLY G N   1 
ATOM   5143 C CA  . GLY D 4 267 ? -23.17800 19.74000  -62.60800 1.000 96.47473  ? 267 GLY G CA  1 
ATOM   5144 C C   . GLY D 4 267 ? -21.79600 19.50500  -63.18700 1.000 95.44565  ? 267 GLY G C   1 
ATOM   5145 O O   . GLY D 4 267 ? -20.97800 20.40800  -63.36800 1.000 99.31191  ? 267 GLY G O   1 
ATOM   5146 N N   . GLY D 4 268 ? -21.55700 18.24400  -63.49800 1.000 90.72140  ? 268 GLY G N   1 
ATOM   5147 C CA  . GLY D 4 268 ? -20.24700 17.76000  -63.87700 1.000 89.47389  ? 268 GLY G CA  1 
ATOM   5148 C C   . GLY D 4 268 ? -20.15300 16.28400  -63.54300 1.000 82.90468  ? 268 GLY G C   1 
ATOM   5149 O O   . GLY D 4 268 ? -21.14800 15.64400  -63.21900 1.000 80.39122  ? 268 GLY G O   1 
ATOM   5150 N N   . THR D 4 269 ? -18.93500 15.75200  -63.62000 1.000 73.85096  ? 269 THR G N   1 
ATOM   5151 C CA  . THR D 4 269 ? -18.70100 14.33600  -63.34900 1.000 68.56875  ? 269 THR G CA  1 
ATOM   5152 C C   . THR D 4 269 ? -18.41600 14.14000  -61.86700 1.000 64.80514  ? 269 THR G C   1 
ATOM   5153 O O   . THR D 4 269 ? -17.61100 14.87400  -61.28200 1.000 65.72630  ? 269 THR G O   1 
ATOM   5154 C CB  . THR D 4 269 ? -17.54000 13.80400  -64.19100 1.000 68.67929  ? 269 THR G CB  1 
ATOM   5155 O OG1 . THR D 4 269 ? -17.83300 14.00200  -65.57700 1.000 72.67977  ? 269 THR G OG1 1 
ATOM   5156 C CG2 . THR D 4 269 ? -17.34300 12.31500  -63.93300 1.000 64.90252  ? 269 THR G CG2 1 
ATOM   5157 N N   . TYR D 4 270 ? -19.07000 13.14900  -61.26200 1.000 62.11008  ? 270 TYR G N   1 
ATOM   5158 C CA  . TYR D 4 270 ? -19.01500 12.94600  -59.82800 1.000 59.73348  ? 270 TYR G CA  1 
ATOM   5159 C C   . TYR D 4 270 ? -18.51600 11.54700  -59.50700 1.000 57.79904  ? 270 TYR G C   1 
ATOM   5160 O O   . TYR D 4 270 ? -18.80900 10.58100  -60.22200 1.000 57.46742  ? 270 TYR G O   1 
ATOM   5161 C CB  . TYR D 4 270 ? -20.39300 13.14600  -59.18200 1.000 60.30986  ? 270 TYR G CB  1 
ATOM   5162 C CG  . TYR D 4 270 ? -20.92200 14.57400  -59.16400 1.000 62.53381  ? 270 TYR G CG  1 
ATOM   5163 C CD1 . TYR D 4 270 ? -21.61100 15.09700  -60.25300 1.000 66.27110  ? 270 TYR G CD1 1 
ATOM   5164 C CD2 . TYR D 4 270 ? -20.77300 15.37900  -58.03700 1.000 63.59447  ? 270 TYR G CD2 1 
ATOM   5165 C CE1 . TYR D 4 270 ? -22.11100 16.39100  -60.23200 1.000 70.83218  ? 270 TYR G CE1 1 
ATOM   5166 C CE2 . TYR D 4 270 ? -21.28400 16.67800  -58.00400 1.000 67.67127  ? 270 TYR G CE2 1 
ATOM   5167 C CZ  . TYR D 4 270 ? -21.94400 17.18000  -59.10700 1.000 71.57700  ? 270 TYR G CZ  1 
ATOM   5168 O OH  . TYR D 4 270 ? -22.44700 18.46900  -59.08700 1.000 76.63814  ? 270 TYR G OH  1 
ATOM   5169 N N   . ARG D 4 271 ? -17.76800 11.45400  -58.41700 1.000 54.74867  ? 271 ARG G N   1 
ATOM   5170 C CA  . ARG D 4 271 ? -17.41800 10.19100  -57.80300 1.000 52.90108  ? 271 ARG G CA  1 
ATOM   5171 C C   . ARG D 4 271 ? -17.70800 10.30200  -56.31800 1.000 51.97202  ? 271 ARG G C   1 
ATOM   5172 O O   . ARG D 4 271 ? -17.79300 11.40200  -55.76300 1.000 52.17994  ? 271 ARG G O   1 
ATOM   5173 C CB  . ARG D 4 271 ? -15.94300 9.83600   -58.03400 1.000 52.74317  ? 271 ARG G CB  1 
ATOM   5174 C CG  . ARG D 4 271 ? -15.63300 9.39300   -59.44100 1.000 54.69077  ? 271 ARG G CG  1 
ATOM   5175 C CD  . ARG D 4 271 ? -14.13500 9.34200   -59.65100 1.000 55.26189  ? 271 ARG G CD  1 
ATOM   5176 N NE  . ARG D 4 271 ? -13.78500 9.19200   -61.05800 1.000 58.00695  ? 271 ARG G NE  1 
ATOM   5177 C CZ  . ARG D 4 271 ? -13.50900 8.03300   -61.64300 1.000 59.69926  ? 271 ARG G CZ  1 
ATOM   5178 N NH1 . ARG D 4 271 ? -13.56200 6.88500   -60.97100 1.000 58.27278  ? 271 ARG G NH1 1 
ATOM   5179 N NH2 . ARG D 4 271 ? -13.16100 8.02400   -62.93100 1.000 60.60463  ? 271 ARG G NH2 1 
ATOM   5180 N N   . CYS D 4 272 ? -17.86500 9.16000   -55.66700 1.000 49.27696  ? 272 CYS G N   1 
ATOM   5181 C CA  . CYS D 4 272 ? -18.02000 9.17400   -54.22500 1.000 48.30053  ? 272 CYS G CA  1 
ATOM   5182 C C   . CYS D 4 272 ? -17.09900 8.13400   -53.61100 1.000 45.63179  ? 272 CYS G C   1 
ATOM   5183 O O   . CYS D 4 272 ? -16.68100 7.17300   -54.26200 1.000 46.04236  ? 272 CYS G O   1 
ATOM   5184 C CB  . CYS D 4 272 ? -19.48100 8.96100   -53.81600 1.000 50.50606  ? 272 CYS G CB  1 
ATOM   5185 S SG  . CYS D 4 272 ? -20.12500 7.32600   -54.13100 1.000 50.44815  ? 272 CYS G SG  1 
ATOM   5186 N N   . PHE D 4 273 ? -16.76900 8.37500   -52.34700 1.000 42.23401  ? 273 PHE G N   1 
ATOM   5187 C CA  . PHE D 4 273 ? -15.83900 7.58200   -51.55600 1.000 40.53907  ? 273 PHE G CA  1 
ATOM   5188 C C   . PHE D 4 273 ? -16.44500 7.36500   -50.17900 1.000 40.32589  ? 273 PHE G C   1 
ATOM   5189 O O   . PHE D 4 273 ? -17.06200 8.27900   -49.62200 1.000 42.10242  ? 273 PHE G O   1 
ATOM   5190 C CB  . PHE D 4 273 ? -14.48100 8.29000   -51.36000 1.000 40.47854  ? 273 PHE G CB  1 
ATOM   5191 C CG  . PHE D 4 273 ? -13.85000 8.80500   -52.62700 1.000 41.65763  ? 273 PHE G CG  1 
ATOM   5192 C CD1 . PHE D 4 273 ? -14.38200 9.88400   -53.29900 1.000 43.50258  ? 273 PHE G CD1 1 
ATOM   5193 C CD2 . PHE D 4 273 ? -12.68800 8.22700   -53.10800 1.000 42.56300  ? 273 PHE G CD2 1 
ATOM   5194 C CE1 . PHE D 4 273 ? -13.78100 10.36900  -54.46800 1.000 45.29754  ? 273 PHE G CE1 1 
ATOM   5195 C CE2 . PHE D 4 273 ? -12.08400 8.69600   -54.26800 1.000 44.27636  ? 273 PHE G CE2 1 
ATOM   5196 C CZ  . PHE D 4 273 ? -12.62800 9.77300   -54.94400 1.000 45.14752  ? 273 PHE G CZ  1 
ATOM   5197 N N   . GLY D 4 274 ? -16.24600 6.17600   -49.61900 1.000 40.21272  ? 274 GLY G N   1 
ATOM   5198 C CA  . GLY D 4 274 ? -16.59500 5.93100   -48.23600 1.000 39.92847  ? 274 GLY G CA  1 
ATOM   5199 C C   . GLY D 4 274 ? -15.40000 6.12800   -47.31900 1.000 39.75213  ? 274 GLY G C   1 
ATOM   5200 O O   . GLY D 4 274 ? -14.24600 6.02500   -47.74300 1.000 39.24155  ? 274 GLY G O   1 
ATOM   5201 N N   . SER D 4 275 ? -15.69000 6.46300   -46.05900 1.000 39.09942  ? 275 SER G N   1 
ATOM   5202 C CA  . SER D 4 275 ? -14.66600 6.56200   -45.02700 1.000 39.68897  ? 275 SER G CA  1 
ATOM   5203 C C   . SER D 4 275 ? -15.28000 6.18100   -43.68500 1.000 40.58908  ? 275 SER G C   1 
ATOM   5204 O O   . SER D 4 275 ? -16.48100 5.94200   -43.57200 1.000 41.89186  ? 275 SER G O   1 
ATOM   5205 C CB  . SER D 4 275 ? -14.01800 7.96100   -44.98100 1.000 40.92596  ? 275 SER G CB  1 
ATOM   5206 O OG  . SER D 4 275 ? -14.94400 8.97600   -44.60800 1.000 44.01317  ? 275 SER G OG  1 
ATOM   5207 N N   . PHE D 4 276 ? -14.42600 6.12700   -42.66400 1.000 39.23628  ? 276 PHE G N   1 
ATOM   5208 C CA  . PHE D 4 276 ? -14.73000 5.54700   -41.36800 1.000 40.89438  ? 276 PHE G CA  1 
ATOM   5209 C C   . PHE D 4 276 ? -14.47300 6.54100   -40.24100 1.000 45.30017  ? 276 PHE G C   1 
ATOM   5210 O O   . PHE D 4 276 ? -13.65500 7.46500   -40.36400 1.000 45.51862  ? 276 PHE G O   1 
ATOM   5211 C CB  . PHE D 4 276 ? -13.88200 4.29800   -41.12200 1.000 40.61540  ? 276 PHE G CB  1 
ATOM   5212 C CG  . PHE D 4 276 ? -14.19200 3.14600   -42.04200 1.000 38.70201  ? 276 PHE G CG  1 
ATOM   5213 C CD1 . PHE D 4 276 ? -15.28900 2.33900   -41.81200 1.000 38.62305  ? 276 PHE G CD1 1 
ATOM   5214 C CD2 . PHE D 4 276 ? -13.35400 2.85300   -43.11300 1.000 37.39133  ? 276 PHE G CD2 1 
ATOM   5215 C CE1 . PHE D 4 276 ? -15.56500 1.25300   -42.65100 1.000 38.07562  ? 276 PHE G CE1 1 
ATOM   5216 C CE2 . PHE D 4 276 ? -13.62200 1.78900   -43.94800 1.000 36.92811  ? 276 PHE G CE2 1 
ATOM   5217 C CZ  . PHE D 4 276 ? -14.74200 0.98700   -43.72100 1.000 36.80178  ? 276 PHE G CZ  1 
ATOM   5218 N N   . ARG D 4 277 ? -15.15200 6.29500   -39.11700 1.000 69.15303  ? 277 ARG G N   1 
ATOM   5219 C CA  . ARG D 4 277 ? -15.02100 7.13800   -37.93300 1.000 72.24550  ? 277 ARG G CA  1 
ATOM   5220 C C   . ARG D 4 277 ? -13.57300 7.22500   -37.47600 1.000 72.36657  ? 277 ARG G C   1 
ATOM   5221 O O   . ARG D 4 277 ? -12.87500 6.20900   -37.38500 1.000 70.83218  ? 277 ARG G O   1 
ATOM   5222 C CB  . ARG D 4 277 ? -15.87700 6.58900   -36.79200 1.000 73.61409  ? 277 ARG G CB  1 
ATOM   5223 C CG  . ARG D 4 277 ? -17.25600 7.19700   -36.66200 1.000 76.64340  ? 277 ARG G CG  1 
ATOM   5224 C CD  . ARG D 4 277 ? -18.02800 6.52600   -35.52400 1.000 78.22780  ? 277 ARG G CD  1 
ATOM   5225 N NE  . ARG D 4 277 ? -17.55900 6.95100   -34.20800 1.000 80.73336  ? 277 ARG G NE  1 
ATOM   5226 C CZ  . ARG D 4 277 ? -17.98600 6.44500   -33.05700 1.000 82.27039  ? 277 ARG G CZ  1 
ATOM   5227 N NH1 . ARG D 4 277 ? -18.86000 5.45000   -33.01900 1.000 81.71506  ? 277 ARG G NH1 1 
ATOM   5228 N NH2 . ARG D 4 277 ? -17.52600 6.95200   -31.91500 1.000 83.07312  ? 277 ARG G NH2 1 
ATOM   5229 N N   . HIS D 4 278 ? -13.13800 8.44600   -37.17000 1.000 53.39061  ? 278 HIS G N   1 
ATOM   5230 C CA  . HIS D 4 278 ? -11.82800 8.76600   -36.60900 1.000 52.03782  ? 278 HIS G CA  1 
ATOM   5231 C C   . HIS D 4 278 ? -10.67700 8.55700   -37.58300 1.000 49.13747  ? 278 HIS G C   1 
ATOM   5232 O O   . HIS D 4 278 ? -9.51800  8.75400   -37.19000 1.000 47.22408  ? 278 HIS G O   1 
ATOM   5233 C CB  . HIS D 4 278 ? -11.52900 7.97400   -35.32500 1.000 52.30627  ? 278 HIS G CB  1 
ATOM   5234 C CG  . HIS D 4 278 ? -12.54300 8.16000   -34.24200 1.000 54.51443  ? 278 HIS G CG  1 
ATOM   5235 N ND1 . HIS D 4 278 ? -13.54700 7.24700   -34.00100 1.000 57.07790  ? 278 HIS G ND1 1 
ATOM   5236 C CD2 . HIS D 4 278 ? -12.69800 9.14000   -33.32500 1.000 55.26978  ? 278 HIS G CD2 1 
ATOM   5237 C CE1 . HIS D 4 278 ? -14.28100 7.65800   -32.98200 1.000 57.86220  ? 278 HIS G CE1 1 
ATOM   5238 N NE2 . HIS D 4 278 ? -13.78900 8.80600   -32.55600 1.000 57.88062  ? 278 HIS G NE2 1 
ATOM   5239 N N   . SER D 4 279 ? -10.94500 8.18500   -38.83800 1.000 46.55558  ? 279 SER G N   1 
ATOM   5240 C CA  . SER D 4 279 ? -9.91900  8.15200   -39.88600 1.000 44.28163  ? 279 SER G CA  1 
ATOM   5241 C C   . SER D 4 279 ? -10.34300 8.98800   -41.09700 1.000 44.20793  ? 279 SER G C   1 
ATOM   5242 O O   . SER D 4 279 ? -10.68200 8.44800   -42.15300 1.000 41.95503  ? 279 SER G O   1 
ATOM   5243 C CB  . SER D 4 279 ? -9.61200  6.71200   -40.29400 1.000 43.66576  ? 279 SER G CB  1 
ATOM   5244 O OG  . SER D 4 279 ? -8.95000  6.02700   -39.24100 1.000 43.03937  ? 279 SER G OG  1 
ATOM   5245 N N   . PRO D 4 280 ? -10.29300 10.32000  -40.98900 1.000 48.52161  ? 280 PRO G N   1 
ATOM   5246 C CA  . PRO D 4 280 ? -10.82700 11.16400  -42.07600 1.000 47.72677  ? 280 PRO G CA  1 
ATOM   5247 C C   . PRO D 4 280 ? -9.96700  11.23400  -43.34600 1.000 45.71601  ? 280 PRO G C   1 
ATOM   5248 O O   . PRO D 4 280 ? -10.42800 11.82400  -44.33000 1.000 45.67390  ? 280 PRO G O   1 
ATOM   5249 C CB  . PRO D 4 280 ? -10.96100 12.55000  -41.42100 1.000 50.80872  ? 280 PRO G CB  1 
ATOM   5250 C CG  . PRO D 4 280 ? -10.05600 12.52500  -40.23700 1.000 50.96664  ? 280 PRO G CG  1 
ATOM   5251 C CD  . PRO D 4 280 ? -9.98400  11.09100  -39.77000 1.000 49.94020  ? 280 PRO G CD  1 
ATOM   5252 N N   . TYR D 4 281 ? -8.76300  10.66200  -43.39200 1.000 44.67378  ? 281 TYR G N   1 
ATOM   5253 C CA  . TYR D 4 281 ? -7.94800  10.73400  -44.60400 1.000 43.63681  ? 281 TYR G CA  1 
ATOM   5254 C C   . TYR D 4 281 ? -7.71300  9.36900   -45.25200 1.000 42.99463  ? 281 TYR G C   1 
ATOM   5255 O O   . TYR D 4 281 ? -6.90700  9.27200   -46.18800 1.000 42.59721  ? 281 TYR G O   1 
ATOM   5256 C CB  . TYR D 4 281 ? -6.61100  11.43100  -44.30500 1.000 44.96065  ? 281 TYR G CB  1 
ATOM   5257 C CG  . TYR D 4 281 ? -6.77000  12.75000  -43.58700 1.000 46.58980  ? 281 TYR G CG  1 
ATOM   5258 C CD1 . TYR D 4 281 ? -7.10400  13.90300  -44.28400 1.000 47.46622  ? 281 TYR G CD1 1 
ATOM   5259 C CD2 . TYR D 4 281 ? -6.61100  12.84100  -42.20400 1.000 47.20040  ? 281 TYR G CD2 1 
ATOM   5260 C CE1 . TYR D 4 281 ? -7.25200  15.13300  -43.63400 1.000 50.54290  ? 281 TYR G CE1 1 
ATOM   5261 C CE2 . TYR D 4 281 ? -6.75400  14.06400  -41.53900 1.000 49.25064  ? 281 TYR G CE2 1 
ATOM   5262 C CZ  . TYR D 4 281 ? -7.08100  15.20800  -42.26400 1.000 51.27194  ? 281 TYR G CZ  1 
ATOM   5263 O OH  . TYR D 4 281 ? -7.24200  16.41800  -41.64100 1.000 53.47483  ? 281 TYR G OH  1 
ATOM   5264 N N   . GLU D 4 282 ? -8.38700  8.31100   -44.76400 1.000 43.36836  ? 282 GLU G N   1 
ATOM   5265 C CA  . GLU D 4 282 ? -8.43600  7.00300   -45.41800 1.000 42.49983  ? 282 GLU G CA  1 
ATOM   5266 C C   . GLU D 4 282 ? -9.77100  6.89200   -46.14100 1.000 41.49182  ? 282 GLU G C   1 
ATOM   5267 O O   . GLU D 4 282 ? -10.81200 6.72100   -45.50000 1.000 41.04439  ? 282 GLU G O   1 
ATOM   5268 C CB  . GLU D 4 282 ? -8.32300  5.85200   -44.41700 1.000 43.15517  ? 282 GLU G CB  1 
ATOM   5269 C CG  . GLU D 4 282 ? -6.98900  5.61600   -43.78100 1.000 44.52639  ? 282 GLU G CG  1 
ATOM   5270 C CD  . GLU D 4 282 ? -7.02200  4.42300   -42.80400 1.000 44.26057  ? 282 GLU G CD  1 
ATOM   5271 O OE1 . GLU D 4 282 ? -7.14500  3.26700   -43.27300 1.000 43.37099  ? 282 GLU G OE1 1 
ATOM   5272 O OE2 . GLU D 4 282 ? -6.92000  4.66300   -41.57600 1.000 43.06832  ? 282 GLU G OE2 1 
ATOM   5273 N N   . TRP D 4 283 ? -9.75100  6.98000   -47.46500 1.000 38.46251  ? 283 TRP G N   1 
ATOM   5274 C CA  . TRP D 4 283 ? -10.96400 6.79800   -48.24000 1.000 37.54924  ? 283 TRP G CA  1 
ATOM   5275 C C   . TRP D 4 283 ? -10.92600 5.47100   -48.98200 1.000 38.60463  ? 283 TRP G C   1 
ATOM   5276 O O   . TRP D 4 283 ? -9.85900  4.92400   -49.27800 1.000 40.20482  ? 283 TRP G O   1 
ATOM   5277 C CB  . TRP D 4 283 ? -11.17100 7.93400   -49.24100 1.000 38.23090  ? 283 TRP G CB  1 
ATOM   5278 C CG  . TRP D 4 283 ? -11.43900 9.27100   -48.61300 1.000 38.78886  ? 283 TRP G CG  1 
ATOM   5279 C CD1 . TRP D 4 283 ? -11.45300 9.56800   -47.27500 1.000 39.45999  ? 283 TRP G CD1 1 
ATOM   5280 C CD2 . TRP D 4 283 ? -11.74900 10.48000  -49.29900 1.000 39.72318  ? 283 TRP G CD2 1 
ATOM   5281 N NE1 . TRP D 4 283 ? -11.73500 10.90200  -47.09200 1.000 41.23916  ? 283 TRP G NE1 1 
ATOM   5282 C CE2 . TRP D 4 283 ? -11.91800 11.48600  -48.31900 1.000 41.55498  ? 283 TRP G CE2 1 
ATOM   5283 C CE3 . TRP D 4 283 ? -11.89700 10.81700  -50.64600 1.000 40.70488  ? 283 TRP G CE3 1 
ATOM   5284 C CZ2 . TRP D 4 283 ? -12.22600 12.80600  -48.64600 1.000 44.06844  ? 283 TRP G CZ2 1 
ATOM   5285 C CZ3 . TRP D 4 283 ? -12.18400 12.13400  -50.97200 1.000 43.84210  ? 283 TRP G CZ3 1 
ATOM   5286 C CH2 . TRP D 4 283 ? -12.34900 13.11200  -49.97300 1.000 45.53177  ? 283 TRP G CH2 1 
ATOM   5287 N N   . SER D 4 284 ? -12.12100 4.97700   -49.29500 1.000 32.36177  ? 284 SER G N   1 
ATOM   5288 C CA  . SER D 4 284 ? -12.26200 3.83200   -50.17900 1.000 33.64614  ? 284 SER G CA  1 
ATOM   5289 C C   . SER D 4 284 ? -11.74400 4.17500   -51.57200 1.000 35.84377  ? 284 SER G C   1 
ATOM   5290 O O   . SER D 4 284 ? -11.48500 5.33200   -51.90400 1.000 35.09631  ? 284 SER G O   1 
ATOM   5291 C CB  . SER D 4 284 ? -13.72400 3.41200   -50.28300 1.000 32.52495  ? 284 SER G CB  1 
ATOM   5292 O OG  . SER D 4 284 ? -14.47000 4.36900   -51.02400 1.000 32.58549  ? 284 SER G OG  1 
ATOM   5293 N N   . ASP D 4 285 ? -11.60500 3.13400   -52.39500 1.000 40.68909  ? 285 ASP G N   1 
ATOM   5294 C CA  . ASP D 4 285 ? -11.51700 3.28500   -53.84200 1.000 42.36561  ? 285 ASP G CA  1 
ATOM   5295 C C   . ASP D 4 285 ? -12.63600 4.19100   -54.35000 1.000 41.37338  ? 285 ASP G C   1 
ATOM   5296 O O   . ASP D 4 285 ? -13.74200 4.17100   -53.80100 1.000 39.64160  ? 285 ASP G O   1 
ATOM   5297 C CB  . ASP D 4 285 ? -11.62300 1.93300   -54.54300 1.000 43.29730  ? 285 ASP G CB  1 
ATOM   5298 C CG  . ASP D 4 285 ? -10.39600 1.07200   -54.36300 1.000 41.29969  ? 285 ASP G CG  1 
ATOM   5299 O OD1 . ASP D 4 285 ? -9.31200  1.61100   -54.08300 1.000 43.25519  ? 285 ASP G OD1 1 
ATOM   5300 O OD2 . ASP D 4 285 ? -10.52000 -0.16100  -54.55000 1.000 38.17300  ? 285 ASP G OD2 1 
ATOM   5301 N N   . PRO D 4 286 ? -12.39500 5.00200   -55.38200 1.000 37.79401  ? 286 PRO G N   1 
ATOM   5302 C CA  . PRO D 4 286 ? -13.49100 5.78900   -55.96000 1.000 37.50976  ? 286 PRO G CA  1 
ATOM   5303 C C   . PRO D 4 286 ? -14.55000 4.89500   -56.59700 1.000 38.94677  ? 286 PRO G C   1 
ATOM   5304 O O   . PRO D 4 286 ? -14.24100 3.90200   -57.26000 1.000 40.44959  ? 286 PRO G O   1 
ATOM   5305 C CB  . PRO D 4 286 ? -12.79700 6.64800   -57.02100 1.000 39.56264  ? 286 PRO G CB  1 
ATOM   5306 C CG  . PRO D 4 286 ? -11.57700 5.87800   -57.39900 1.000 40.53644  ? 286 PRO G CG  1 
ATOM   5307 C CD  . PRO D 4 286 ? -11.14900 5.11700   -56.15000 1.000 39.56790  ? 286 PRO G CD  1 
ATOM   5308 N N   . SER D 4 287 ? -15.80800 5.27300   -56.40400 1.000 38.49935  ? 287 SER G N   1 
ATOM   5309 C CA  . SER D 4 287 ? -16.88300 4.74500   -57.22900 1.000 39.85741  ? 287 SER G CA  1 
ATOM   5310 C C   . SER D 4 287 ? -16.59900 5.00100   -58.70900 1.000 42.58405  ? 287 SER G C   1 
ATOM   5311 O O   . SER D 4 287 ? -15.78200 5.86200   -59.07900 1.000 42.73933  ? 287 SER G O   1 
ATOM   5312 C CB  . SER D 4 287 ? -18.21500 5.40300   -56.86400 1.000 39.36261  ? 287 SER G CB  1 
ATOM   5313 O OG  . SER D 4 287 ? -18.26300 6.72000   -57.38700 1.000 40.90490  ? 287 SER G OG  1 
ATOM   5314 N N   . ASP D 4 288 ? -17.28500 4.23500   -59.56600 1.000 56.62258  ? 288 ASP G N   1 
ATOM   5315 C CA  . ASP D 4 288 ? -17.33200 4.56300   -60.98700 1.000 58.24646  ? 288 ASP G CA  1 
ATOM   5316 C C   . ASP D 4 288 ? -17.84400 5.98800   -61.12200 1.000 60.42567  ? 288 ASP G C   1 
ATOM   5317 O O   . ASP D 4 288 ? -18.65700 6.43200   -60.30300 1.000 58.81758  ? 288 ASP G O   1 
ATOM   5318 C CB  . ASP D 4 288 ? -18.23100 3.59400   -61.76300 1.000 54.82763  ? 288 ASP G CB  1 
ATOM   5319 C CG  . ASP D 4 288 ? -17.69500 2.16600   -61.76200 1.000 51.62987  ? 288 ASP G CG  1 
ATOM   5320 O OD1 . ASP D 4 288 ? -16.50500 1.97300   -61.47100 1.000 52.24047  ? 288 ASP G OD1 1 
ATOM   5321 O OD2 . ASP D 4 288 ? -18.46500 1.22800   -62.05600 1.000 48.46107  ? 288 ASP G OD2 1 
ATOM   5322 N N   . PRO D 4 289 ? -17.39100 6.74100   -62.12400 1.000 57.85694  ? 289 PRO G N   1 
ATOM   5323 C CA  . PRO D 4 289 ? -17.83500 8.13200   -62.25200 1.000 58.01485  ? 289 PRO G CA  1 
ATOM   5324 C C   . PRO D 4 289 ? -19.28200 8.21100   -62.70700 1.000 58.60439  ? 289 PRO G C   1 
ATOM   5325 O O   . PRO D 4 289 ? -19.80200 7.30800   -63.36600 1.000 56.62258  ? 289 PRO G O   1 
ATOM   5326 C CB  . PRO D 4 289 ? -16.88900 8.70900   -63.31100 1.000 60.13353  ? 289 PRO G CB  1 
ATOM   5327 C CG  . PRO D 4 289 ? -16.53500 7.52700   -64.16400 1.000 60.79413  ? 289 PRO G CG  1 
ATOM   5328 C CD  . PRO D 4 289 ? -16.48300 6.34300   -63.21600 1.000 59.43344  ? 289 PRO G CD  1 
ATOM   5329 N N   . LEU D 4 290 ? -19.93300 9.31500   -62.35100 1.000 61.13628  ? 290 LEU G N   1 
ATOM   5330 C CA  . LEU D 4 290 ? -21.28100 9.60400   -62.82300 1.000 62.01270  ? 290 LEU G CA  1 
ATOM   5331 C C   . LEU D 4 290 ? -21.31600 11.04600  -63.30200 1.000 64.20770  ? 290 LEU G C   1 
ATOM   5332 O O   . LEU D 4 290 ? -20.91500 11.95100  -62.56400 1.000 64.21823  ? 290 LEU G O   1 
ATOM   5333 C CB  . LEU D 4 290 ? -22.32900 9.37900   -61.72300 1.000 60.45988  ? 290 LEU G CB  1 
ATOM   5334 C CG  . LEU D 4 290 ? -23.80400 9.52500   -62.11800 1.000 61.30472  ? 290 LEU G CG  1 
ATOM   5335 C CD1 . LEU D 4 290 ? -24.32400 8.24800   -62.78600 1.000 58.67546  ? 290 LEU G CD1 1 
ATOM   5336 C CD2 . LEU D 4 290 ? -24.66700 9.90300   -60.91200 1.000 61.48895  ? 290 LEU G CD2 1 
ATOM   5337 N N   . LEU D 4 291 ? -21.78800 11.25400  -64.53100 1.000 63.62079  ? 291 LEU G N   1 
ATOM   5338 C CA  . LEU D 4 291 ? -21.84900 12.57900  -65.14300 1.000 68.54769  ? 291 LEU G CA  1 
ATOM   5339 C C   . LEU D 4 291 ? -23.26300 13.12800  -65.01400 1.000 70.72953  ? 291 LEU G C   1 
ATOM   5340 O O   . LEU D 4 291 ? -24.22100 12.52100  -65.50700 1.000 70.82691  ? 291 LEU G O   1 
ATOM   5341 C CB  . LEU D 4 291 ? -21.41800 12.53600  -66.61100 1.000 71.68228  ? 291 LEU G CB  1 
ATOM   5342 C CG  . LEU D 4 291 ? -21.55300 13.76700  -67.54200 1.000 77.79354  ? 291 LEU G CG  1 
ATOM   5343 C CD1 . LEU D 4 291 ? -22.92800 13.85000  -68.21000 1.000 80.46754  ? 291 LEU G CD1 1 
ATOM   5344 C CD2 . LEU D 4 291 ? -21.21900 15.10700  -66.86600 1.000 80.24910  ? 291 LEU G CD2 1 
ATOM   5345 N N   . VAL D 4 292 ? -23.38200 14.28100  -64.36600 1.000 72.88242  ? 292 VAL G N   1 
ATOM   5346 C CA  . VAL D 4 292 ? -24.64400 14.99000  -64.20500 1.000 75.84330  ? 292 VAL G CA  1 
ATOM   5347 C C   . VAL D 4 292 ? -24.61700 16.21100  -65.11800 1.000 81.91245  ? 292 VAL G C   1 
ATOM   5348 O O   . VAL D 4 292 ? -23.63700 16.96700  -65.12800 1.000 83.85479  ? 292 VAL G O   1 
ATOM   5349 C CB  . VAL D 4 292 ? -24.87100 15.39200  -62.73800 1.000 74.44050  ? 292 VAL G CB  1 
ATOM   5350 C CG1 . VAL D 4 292 ? -26.20800 16.07300  -62.57800 1.000 77.84354  ? 292 VAL G CG1 1 
ATOM   5351 C CG2 . VAL D 4 292 ? -24.76400 14.16200  -61.81700 1.000 68.81088  ? 292 VAL G CG2 1 
ATOM   5352 N N   . SER D 4 293 ? -25.68400 16.39200  -65.89300 1.000 107.02336 ? 293 SER G N   1 
ATOM   5353 C CA  . SER D 4 293 ? -25.79800 17.48800  -66.84800 1.000 114.18474 ? 293 SER G CA  1 
ATOM   5354 C C   . SER D 4 293 ? -27.07200 18.26600  -66.55100 1.000 118.40893 ? 293 SER G C   1 
ATOM   5355 O O   . SER D 4 293 ? -28.16600 17.69100  -66.54000 1.000 117.15878 ? 293 SER G O   1 
ATOM   5356 C CB  . SER D 4 293 ? -25.80400 16.96400  -68.28600 1.000 115.91916 ? 293 SER G CB  1 
ATOM   5357 O OG  . SER D 4 293 ? -26.82300 15.99600  -68.47500 1.000 113.47413 ? 293 SER G OG  1 
ATOM   5358 N N   . VAL D 4 294 ? -26.92700 19.56500  -66.30000 1.000 98.86975  ? 294 VAL G N   1 
ATOM   5359 C CA  . VAL D 4 294 ? -28.05000 20.45300  -66.02500 1.000 93.66649  ? 294 VAL G CA  1 
ATOM   5360 C C   . VAL D 4 294 ? -28.38200 21.19100  -67.31300 1.000 97.07480  ? 294 VAL G C   1 
ATOM   5361 O O   . VAL D 4 294 ? -27.51400 21.85200  -67.89600 1.000 103.17026 ? 294 VAL G O   1 
ATOM   5362 C CB  . VAL D 4 294 ? -27.72800 21.43200  -64.88500 1.000 92.07683  ? 294 VAL G CB  1 
ATOM   5363 N N   . THR D 4 295 ? -29.63400 21.07100  -67.75300 1.000 66.93000  ? 295 THR G N   1 
ATOM   5364 C CA  . THR D 4 295 ? -30.10500 21.60000  -69.04300 1.000 66.93000  ? 295 THR G CA  1 
ATOM   5365 C C   . THR D 4 295 ? -29.63700 23.02600  -69.33900 1.000 66.93000  ? 295 THR G C   1 
ATOM   5366 O O   . THR D 4 295 ? -28.67600 23.22900  -70.08500 1.000 66.93000  ? 295 THR G O   1 
ATOM   5367 C CB  . THR D 4 295 ? -31.64900 21.57500  -69.11900 1.000 66.93000  ? 295 THR G CB  1 
HETATM 5368 C C1  . NAG E 5 .   ? -31.11600 -0.91700  -51.26600 1.000 75.35377  ? 401 NAG G C1  1 
HETATM 5369 C C2  . NAG E 5 .   ? -30.89900 -0.98100  -52.77500 1.000 79.07527  ? 401 NAG G C2  1 
HETATM 5370 C C3  . NAG E 5 .   ? -30.63000 0.41400   -53.33700 1.000 82.17301  ? 401 NAG G C3  1 
HETATM 5371 C C4  . NAG E 5 .   ? -31.72600 1.38700   -52.91800 1.000 84.94966  ? 401 NAG G C4  1 
HETATM 5372 C C5  . NAG E 5 .   ? -31.88600 1.36300   -51.40100 1.000 79.52796  ? 401 NAG G C5  1 
HETATM 5373 C C6  . NAG E 5 .   ? -33.02000 2.23000   -50.89600 1.000 77.85934  ? 401 NAG G C6  1 
HETATM 5374 C C7  . NAG E 5 .   ? -29.98600 -3.14300  -53.49700 1.000 83.66793  ? 401 NAG G C7  1 
HETATM 5375 C C8  . NAG E 5 .   ? -28.74200 -3.92500  -53.78900 1.000 78.22254  ? 401 NAG G C8  1 
HETATM 5376 N N2  . NAG E 5 .   ? -29.80400 -1.88000  -53.10100 1.000 77.91460  ? 401 NAG G N2  1 
HETATM 5377 O O3  . NAG E 5 .   ? -30.57200 0.32500   -54.75500 1.000 91.95050  ? 401 NAG G O3  1 
HETATM 5378 O O4  . NAG E 5 .   ? -31.40500 2.70900   -53.34000 1.000 74.17731  ? 401 NAG G O4  1 
HETATM 5379 O O5  . NAG E 5 .   ? -32.15700 0.02300   -50.96700 1.000 74.29838  ? 401 NAG G O5  1 
HETATM 5380 O O6  . NAG E 5 .   ? -34.23400 2.00100   -51.59800 1.000 76.47233  ? 401 NAG G O6  1 
HETATM 5381 O O7  . NAG E 5 .   ? -31.10400 -3.63400  -53.61000 1.000 86.67355  ? 401 NAG G O7  1 
HETATM 5382 C C1  . NAG F 5 .   ? 8.74200   18.60000  -59.50800 1.000 68.27398  ? 402 NAG G C1  1 
HETATM 5383 C C2  . NAG F 5 .   ? 9.66200   18.88300  -60.69600 1.000 82.97311  ? 402 NAG G C2  1 
HETATM 5384 C C3  . NAG F 5 .   ? 8.85300   19.36500  -61.90300 1.000 80.81232  ? 402 NAG G C3  1 
HETATM 5385 C C4  . NAG F 5 .   ? 7.70000   18.41900  -62.20400 1.000 80.94918  ? 402 NAG G C4  1 
HETATM 5386 C C5  . NAG F 5 .   ? 6.86200   18.21000  -60.95200 1.000 64.58932  ? 402 NAG G C5  1 
HETATM 5387 C C6  . NAG F 5 .   ? 5.77200   17.18100  -61.14200 1.000 76.79342  ? 402 NAG G C6  1 
HETATM 5388 C C7  . NAG F 5 .   ? 11.96300  19.62100  -60.26800 1.000 88.81591  ? 402 NAG G C7  1 
HETATM 5389 C C8  . NAG F 5 .   ? 12.83100  20.76800  -59.85500 1.000 91.53729  ? 402 NAG G C8  1 
HETATM 5390 N N2  . NAG F 5 .   ? 10.65400  19.87700  -60.32800 1.000 85.19706  ? 402 NAG G N2  1 
HETATM 5391 O O3  . NAG F 5 .   ? 9.71000   19.44500  -63.03700 1.000 87.11308  ? 402 NAG G O3  1 
HETATM 5392 O O4  . NAG F 5 .   ? 6.88200   18.96800  -63.23000 1.000 92.18211  ? 402 NAG G O4  1 
HETATM 5393 O O5  . NAG F 5 .   ? 7.70400   17.71800  -59.90400 1.000 63.08651  ? 402 NAG G O5  1 
HETATM 5394 O O6  . NAG F 5 .   ? 6.24800   15.86900  -60.87200 1.000 79.28582  ? 402 NAG G O6  1 
HETATM 5395 O O7  . NAG F 5 .   ? 12.42400  18.51400  -60.53200 1.000 87.80263  ? 402 NAG G O7  1 
HETATM 5396 C C1  . NAG G 5 .   ? 3.15600   25.22500  -20.75400 1.000 101.21214 ? 403 NAG G C1  1 
HETATM 5397 C C2  . NAG G 5 .   ? 2.07600   24.43400  -20.00200 1.000 106.86808 ? 403 NAG G C2  1 
HETATM 5398 C C3  . NAG G 5 .   ? 0.74900   24.47700  -20.76800 1.000 105.58898 ? 403 NAG G C3  1 
HETATM 5399 C C4  . NAG G 5 .   ? 0.36300   25.91000  -21.11300 1.000 91.54519  ? 403 NAG G C4  1 
HETATM 5400 C C5  . NAG G 5 .   ? 1.51900   26.66000  -21.76900 1.000 99.17242  ? 403 NAG G C5  1 
HETATM 5401 C C6  . NAG G 5 .   ? 1.22700   28.13300  -21.93200 1.000 90.51085  ? 403 NAG G C6  1 
HETATM 5402 C C7  . NAG G 5 .   ? 2.66100   22.12700  -20.69100 1.000 95.49829  ? 403 NAG G C7  1 
HETATM 5403 C C8  . NAG G 5 .   ? 3.08000   20.77200  -20.20200 1.000 91.20567  ? 403 NAG G C8  1 
HETATM 5404 N N2  . NAG G 5 .   ? 2.48700   23.06000  -19.74400 1.000 102.22015 ? 403 NAG G N2  1 
HETATM 5405 O O3  . NAG G 5 .   ? -0.28100  23.88900  -19.98000 1.000 97.91437  ? 403 NAG G O3  1 
HETATM 5406 O O4  . NAG G 5 .   ? -0.72900  25.90700  -22.02400 1.000 80.17803  ? 403 NAG G O4  1 
HETATM 5407 O O5  . NAG G 5 .   ? 2.70500   26.56500  -20.96500 1.000 105.07839 ? 403 NAG G O5  1 
HETATM 5408 O O6  . NAG G 5 .   ? 0.82100   28.72000  -20.70300 1.000 88.08425  ? 403 NAG G O6  1 
HETATM 5409 O O7  . NAG G 5 .   ? 2.49500   22.36200  -21.88700 1.000 91.28200  ? 403 NAG G O7  1 
HETATM 5410 C C1  . NAG H 5 .   ? 21.89300  19.44700  -34.19700 1.000 52.49314  ? 404 NAG G C1  1 
HETATM 5411 C C2  . NAG H 5 .   ? 22.07200  19.10900  -35.67900 1.000 45.64495  ? 404 NAG G C2  1 
HETATM 5412 C C3  . NAG H 5 .   ? 22.64600  17.70900  -35.83300 1.000 58.07538  ? 404 NAG G C3  1 
HETATM 5413 C C4  . NAG H 5 .   ? 23.94000  17.58300  -35.04300 1.000 64.28402  ? 404 NAG G C4  1 
HETATM 5414 C C5  . NAG H 5 .   ? 23.67000  17.93400  -33.58400 1.000 56.93314  ? 404 NAG G C5  1 
HETATM 5415 C C6  . NAG H 5 .   ? 24.90600  17.89600  -32.71500 1.000 55.56192  ? 404 NAG G C6  1 
HETATM 5416 C C7  . NAG H 5 .   ? 20.53500  20.23800  -37.21400 1.000 48.41107  ? 404 NAG G C7  1 
HETATM 5417 C C8  . NAG H 5 .   ? 19.19000  20.19400  -37.88200 1.000 48.22683  ? 404 NAG G C8  1 
HETATM 5418 N N2  . NAG H 5 .   ? 20.81600  19.21800  -36.39800 1.000 44.88170  ? 404 NAG G N2  1 
HETATM 5419 O O3  . NAG H 5 .   ? 22.86700  17.45000  -37.21200 1.000 50.94821  ? 404 NAG G O3  1 
HETATM 5420 O O4  . NAG H 5 .   ? 24.44400  16.25600  -35.13900 1.000 74.42208  ? 404 NAG G O4  1 
HETATM 5421 O O5  . NAG H 5 .   ? 23.14500  19.26900  -33.50400 1.000 55.27768  ? 404 NAG G O5  1 
HETATM 5422 O O6  . NAG H 5 .   ? 24.56600  17.99800  -31.33800 1.000 58.68598  ? 404 NAG G O6  1 
HETATM 5423 O O7  . NAG H 5 .   ? 21.33100  21.15500  -37.40600 1.000 54.64866  ? 404 NAG G O7  1 
HETATM 5424 O O   . HOH I 6 .   ? 2.44400   7.58400   -36.86700 1.000 48.68000  ? 301 HOH A O   1 
HETATM 5425 O O   . HOH I 6 .   ? 6.10400   -40.27500 -22.52600 1.000 59.65000  ? 302 HOH A O   1 
HETATM 5426 O O   . HOH I 6 .   ? 8.00100   -39.95900 -1.79600  1.000 48.81000  ? 303 HOH A O   1 
HETATM 5427 O O   . HOH I 6 .   ? 5.06800   -26.39900 -18.80500 1.000 36.52000  ? 304 HOH A O   1 
HETATM 5428 O O   . HOH I 6 .   ? 3.63700   -28.54500 10.84900  1.000 53.90000  ? 305 HOH A O   1 
HETATM 5429 O O   . HOH I 6 .   ? 5.30100   -32.28300 -25.98000 1.000 48.81000  ? 306 HOH A O   1 
HETATM 5430 O O   . HOH I 6 .   ? -8.85500  -26.15500 -35.99100 1.000 46.40000  ? 307 HOH A O   1 
HETATM 5431 O O   . HOH I 6 .   ? -6.13100  -27.52100 -42.05200 1.000 46.98000  ? 308 HOH A O   1 
HETATM 5432 O O   . HOH I 6 .   ? -0.40600  8.31900   -25.53300 1.000 37.64000  ? 309 HOH A O   1 
HETATM 5433 O O   . HOH I 6 .   ? 14.73500  10.53400  -30.68900 1.000 48.56000  ? 310 HOH A O   1 
HETATM 5434 O O   . HOH I 6 .   ? 3.15800   -31.57400 -45.49000 1.000 48.56000  ? 311 HOH A O   1 
HETATM 5435 O O   . HOH I 6 .   ? 21.74200  -17.56000 -32.65700 1.000 45.35000  ? 312 HOH A O   1 
HETATM 5436 O O   . HOH I 6 .   ? 15.59600  -13.62800 -26.47500 1.000 33.92000  ? 313 HOH A O   1 
HETATM 5437 O O   . HOH I 6 .   ? 10.38300  -27.87400 -31.06300 1.000 38.55000  ? 314 HOH A O   1 
HETATM 5438 O O   . HOH I 6 .   ? -12.37800 -2.30000  -23.86100 1.000 46.66000  ? 315 HOH A O   1 
HETATM 5439 O O   . HOH I 6 .   ? 2.10300   -33.01300 -20.44100 1.000 50.41000  ? 316 HOH A O   1 
HETATM 5440 O O   . HOH I 6 .   ? -1.26400  -12.63700 -47.37500 1.000 35.25000  ? 317 HOH A O   1 
HETATM 5441 O O   . HOH I 6 .   ? 11.70700  2.98800   -31.22000 1.000 38.33000  ? 318 HOH A O   1 
HETATM 5442 O O   . HOH I 6 .   ? 8.56500   10.42300  -26.49700 1.000 42.03000  ? 319 HOH A O   1 
HETATM 5443 O O   . HOH I 6 .   ? -16.20500 -10.59600 -39.91300 1.000 38.64000  ? 320 HOH A O   1 
HETATM 5444 O O   . HOH I 6 .   ? 20.599    -23.741   -26.846   1.000 43.94000  ? 321 HOH A O   1 
HETATM 5445 O O   . HOH I 6 .   ? -6.18800  -18.29000 -31.84800 1.000 41.83000  ? 322 HOH A O   1 
HETATM 5446 O O   . HOH I 6 .   ? 20.00900  -21.84300 -41.48900 1.000 43.02000  ? 323 HOH A O   1 
HETATM 5447 O O   . HOH I 6 .   ? 14.45900  -38.45100 -14.96000 1.000 44.81000  ? 324 HOH A O   1 
HETATM 5448 O O   . HOH I 6 .   ? 10.00800  -1.44300  -44.98900 1.000 39.39000  ? 325 HOH A O   1 
HETATM 5449 O O   . HOH I 6 .   ? 9.89500   -20.64900 -24.85900 1.000 48.56000  ? 326 HOH A O   1 
HETATM 5450 O O   . HOH I 6 .   ? 20.30900  -2.94100  -41.53700 1.000 48.56000  ? 327 HOH A O   1 
HETATM 5451 O O   . HOH I 6 .   ? 9.30200   -6.90200  -47.39400 1.000 48.56000  ? 328 HOH A O   1 
HETATM 5452 O O   . HOH I 6 .   ? 6.79300   -43.24600 5.42300   1.000 58.89000  ? 329 HOH A O   1 
HETATM 5453 O O   . HOH I 6 .   ? -1.67900  -32.11700 -40.05200 1.000 48.84000  ? 330 HOH A O   1 
HETATM 5454 O O   . HOH I 6 .   ? 19.29900  -27.12300 -34.31900 1.000 35.96000  ? 331 HOH A O   1 
HETATM 5455 O O   . HOH I 6 .   ? 13.38900  6.00500   -28.08900 1.000 48.81000  ? 332 HOH A O   1 
HETATM 5456 O O   . HOH I 6 .   ? 21.67100  -3.17400  -35.72800 1.000 48.56000  ? 333 HOH A O   1 
HETATM 5457 O O   . HOH I 6 .   ? 14.31000  -10.54400 -50.05500 1.000 48.81000  ? 334 HOH A O   1 
HETATM 5458 O O   . HOH I 6 .   ? -6.61100  -9.13600  -20.16900 1.000 46.59000  ? 335 HOH A O   1 
HETATM 5459 O O   . HOH I 6 .   ? -4.08900  -26.66900 -33.31400 1.000 47.14000  ? 336 HOH A O   1 
HETATM 5460 O O   . HOH I 6 .   ? -3.57900  8.17000   -22.26500 1.000 45.58000  ? 337 HOH A O   1 
HETATM 5461 O O   . HOH I 6 .   ? 16.62600  -25.01900 -31.33000 1.000 32.52000  ? 338 HOH A O   1 
HETATM 5462 O O   . HOH I 6 .   ? 12.19900  -12.74800 -45.81100 1.000 33.01000  ? 339 HOH A O   1 
HETATM 5463 O O   . HOH I 6 .   ? 16.34300  -19.34900 -28.65900 1.000 31.00000  ? 340 HOH A O   1 
HETATM 5464 O O   . HOH I 6 .   ? 15.38700  -25.56600 -29.35900 1.000 38.20000  ? 341 HOH A O   1 
HETATM 5465 O O   . HOH I 6 .   ? 16.73400  -33.15900 -11.31100 1.000 42.48000  ? 342 HOH A O   1 
HETATM 5466 O O   . HOH I 6 .   ? 3.38500   1.31600   -20.32300 1.000 51.57000  ? 343 HOH A O   1 
HETATM 5467 O O   . HOH I 6 .   ? 11.77300  13.63300  -22.75000 1.000 33.67000  ? 344 HOH A O   1 
HETATM 5468 O O   . HOH I 6 .   ? -11.68800 -9.05900  -43.34500 1.000 30.95000  ? 345 HOH A O   1 
HETATM 5469 O O   . HOH I 6 .   ? 4.09100   -5.43600  -42.77600 1.000 44.34000  ? 346 HOH A O   1 
HETATM 5470 O O   . HOH I 6 .   ? -18.40800 0.67800   -33.11500 1.000 46.84000  ? 347 HOH A O   1 
HETATM 5471 O O   . HOH I 6 .   ? 10.75700  -43.49800 -19.27500 1.000 46.80000  ? 348 HOH A O   1 
HETATM 5472 O O   . HOH I 6 .   ? -7.08400  1.14300   -22.57700 1.000 37.85000  ? 349 HOH A O   1 
HETATM 5473 O O   . HOH I 6 .   ? -14.52600 -25.72900 -34.85200 1.000 37.90000  ? 350 HOH A O   1 
HETATM 5474 O O   . HOH I 6 .   ? -13.25500 -19.10700 -34.06000 1.000 37.27000  ? 351 HOH A O   1 
HETATM 5475 O O   . HOH I 6 .   ? -17.44300 -8.97400  -33.68800 1.000 43.76000  ? 352 HOH A O   1 
HETATM 5476 O O   . HOH I 6 .   ? 4.01000   5.59100   -38.43900 1.000 41.88000  ? 353 HOH A O   1 
HETATM 5477 O O   . HOH I 6 .   ? -8.03900  -18.63300 -35.68000 1.000 45.54000  ? 354 HOH A O   1 
HETATM 5478 O O   . HOH I 6 .   ? -7.73300  -10.73100 -29.08000 1.000 36.40000  ? 355 HOH A O   1 
HETATM 5479 O O   . HOH I 6 .   ? 6.48400   7.18000   -27.20200 1.000 36.32000  ? 356 HOH A O   1 
HETATM 5480 O O   . HOH I 6 .   ? 20.15800  -9.69800  -39.69100 1.000 49.31000  ? 357 HOH A O   1 
HETATM 5481 O O   . HOH I 6 .   ? -1.92200  -4.83700  -25.28700 1.000 34.52000  ? 358 HOH A O   1 
HETATM 5482 O O   . HOH I 6 .   ? -1.89700  -19.34000 -49.76100 1.000 36.63000  ? 359 HOH A O   1 
HETATM 5483 O O   . HOH I 6 .   ? -7.13900  -15.90100 -49.21500 1.000 44.95000  ? 360 HOH A O   1 
HETATM 5484 O O   . HOH I 6 .   ? 6.10900   -33.26300 -23.35000 1.000 37.74000  ? 361 HOH A O   1 
HETATM 5485 O O   . HOH I 6 .   ? -6.51500  9.43700   -21.05700 1.000 54.73000  ? 362 HOH A O   1 
HETATM 5486 O O   . HOH I 6 .   ? 7.02300   -17.75400 -12.45400 1.000 36.82000  ? 363 HOH A O   1 
HETATM 5487 O O   . HOH I 6 .   ? -8.46100  -2.71200  -24.34300 1.000 38.78000  ? 364 HOH A O   1 
HETATM 5488 O O   . HOH I 6 .   ? 7.02600   -21.12100 -49.65000 1.000 48.81000  ? 365 HOH A O   1 
HETATM 5489 O O   . HOH I 6 .   ? 11.46000  -14.27600 -39.65000 1.000 29.80000  ? 366 HOH A O   1 
HETATM 5490 O O   . HOH I 6 .   ? -6.95300  -16.25500 -34.05500 1.000 39.14000  ? 367 HOH A O   1 
HETATM 5491 O O   . HOH I 6 .   ? 20.52100  -27.90400 -36.93500 1.000 34.64000  ? 368 HOH A O   1 
HETATM 5492 O O   . HOH I 6 .   ? -0.48800  6.15000   -27.14500 1.000 35.16000  ? 369 HOH A O   1 
HETATM 5493 O O   . HOH I 6 .   ? 1.26600   -17.54600 -48.50800 1.000 34.82000  ? 370 HOH A O   1 
HETATM 5494 O O   . HOH I 6 .   ? -2.52900  4.28000   -27.78500 1.000 32.72000  ? 371 HOH A O   1 
HETATM 5495 O O   . HOH I 6 .   ? 14.11500  -19.64800 -27.10400 1.000 39.01000  ? 372 HOH A O   1 
HETATM 5496 O O   . HOH I 6 .   ? 9.38100   -30.00500 -41.76200 1.000 41.17000  ? 373 HOH A O   1 
HETATM 5497 O O   . HOH I 6 .   ? 5.43800   -27.32600 -25.19000 1.000 42.75000  ? 374 HOH A O   1 
HETATM 5498 O O   . HOH I 6 .   ? 16.07200  -30.27700 -28.04400 1.000 50.50000  ? 375 HOH A O   1 
HETATM 5499 O O   . HOH I 6 .   ? -10.00100 -16.71800 -32.59800 1.000 46.76000  ? 376 HOH A O   1 
HETATM 5500 O O   . HOH I 6 .   ? -10.14400 -4.00800  -25.87400 1.000 42.54000  ? 377 HOH A O   1 
HETATM 5501 O O   . HOH I 6 .   ? 7.05000   -8.66200  -28.46300 1.000 34.97000  ? 378 HOH A O   1 
HETATM 5502 O O   . HOH I 6 .   ? 2.73000   8.27000   -19.78400 1.000 48.56000  ? 379 HOH A O   1 
HETATM 5503 O O   . HOH I 6 .   ? 1.03300   1.11600   -20.79400 1.000 44.70000  ? 380 HOH A O   1 
HETATM 5504 O O   . HOH I 6 .   ? -4.32800  -6.69000  -39.32800 1.000 35.62000  ? 381 HOH A O   1 
HETATM 5505 O O   . HOH I 6 .   ? -4.30200  10.31000  -31.66900 1.000 50.36000  ? 382 HOH A O   1 
HETATM 5506 O O   . HOH I 6 .   ? 15.94400  -21.59600 -21.83200 1.000 44.54000  ? 383 HOH A O   1 
HETATM 5507 O O   . HOH I 6 .   ? 19.55500  -16.07900 -28.63300 1.000 47.52000  ? 384 HOH A O   1 
HETATM 5508 O O   . HOH I 6 .   ? 5.39000   8.30900   -20.42800 1.000 44.19000  ? 385 HOH A O   1 
HETATM 5509 O O   . HOH I 6 .   ? 28.16000  -18.53500 -43.66800 1.000 46.59000  ? 386 HOH A O   1 
HETATM 5510 O O   . HOH I 6 .   ? -7.82200  -22.17800 -38.56800 1.000 36.73000  ? 387 HOH A O   1 
HETATM 5511 O O   . HOH I 6 .   ? 8.69600   -21.21400 -19.44400 1.000 34.82000  ? 388 HOH A O   1 
HETATM 5512 O O   . HOH I 6 .   ? -1.79000  4.75200   -19.74000 1.000 52.78000  ? 389 HOH A O   1 
HETATM 5513 O O   . HOH I 6 .   ? 9.84200   1.85200   -39.22100 1.000 42.53000  ? 390 HOH A O   1 
HETATM 5514 O O   . HOH I 6 .   ? 15.51800  -17.38300 -48.05600 1.000 49.76000  ? 391 HOH A O   1 
HETATM 5515 O O   . HOH I 6 .   ? -12.74500 -20.83400 -44.46300 1.000 45.11000  ? 392 HOH A O   1 
HETATM 5516 O O   . HOH I 6 .   ? 13.62300  -22.29700 -25.81500 1.000 42.39000  ? 393 HOH A O   1 
HETATM 5517 O O   . HOH I 6 .   ? 9.35600   -44.84900 -13.16300 1.000 50.09000  ? 394 HOH A O   1 
HETATM 5518 O O   . HOH I 6 .   ? 5.32600   -21.39400 -31.40600 1.000 40.52000  ? 395 HOH A O   1 
HETATM 5519 O O   . HOH I 6 .   ? 13.71100  -34.80600 -41.70500 1.000 49.28000  ? 396 HOH A O   1 
HETATM 5520 O O   . HOH I 6 .   ? 14.89800  -26.46800 -44.79600 1.000 48.81000  ? 397 HOH A O   1 
HETATM 5521 O O   . HOH I 6 .   ? 0.75800   -24.71100 -48.16400 1.000 47.31000  ? 398 HOH A O   1 
HETATM 5522 O O   . HOH I 6 .   ? 21.33800  -9.05000  -32.74100 1.000 48.81000  ? 399 HOH A O   1 
HETATM 5523 O O   . HOH I 6 .   ? 22.73700  -14.77400 -39.79800 1.000 38.64000  ? 400 HOH A O   1 
HETATM 5524 O O   . HOH I 6 .   ? -2.46500  -24.22000 -30.60200 1.000 48.56000  ? 401 HOH A O   1 
HETATM 5525 O O   . HOH I 6 .   ? 1.11400   -26.93200 -47.52000 1.000 48.81000  ? 402 HOH A O   1 
HETATM 5526 O O   . HOH I 6 .   ? -0.67900  -0.86600  -21.31300 1.000 33.66000  ? 403 HOH A O   1 
HETATM 5527 O O   . HOH I 6 .   ? 5.52000   -31.49400 -38.73100 1.000 41.72000  ? 404 HOH A O   1 
HETATM 5528 O O   . HOH I 6 .   ? 19.96500  -25.66800 -40.73200 1.000 37.37000  ? 405 HOH A O   1 
HETATM 5529 O O   . HOH I 6 .   ? 11.86000  -30.02900 -0.28900  1.000 48.28000  ? 406 HOH A O   1 
HETATM 5530 O O   . HOH I 6 .   ? -17.56700 -2.99400  -43.65100 1.000 35.50000  ? 407 HOH A O   1 
HETATM 5531 O O   . HOH I 6 .   ? 8.97600   -15.69400 -47.89100 1.000 37.79000  ? 408 HOH A O   1 
HETATM 5532 O O   . HOH I 6 .   ? 5.02600   -19.72200 -10.46000 1.000 48.81000  ? 409 HOH A O   1 
HETATM 5533 O O   . HOH I 6 .   ? 22.862    -22.520   -39.259   1.000 49.27000  ? 410 HOH A O   1 
HETATM 5534 O O   . HOH I 6 .   ? 1.60800   -42.84300 -3.95200  1.000 50.75000  ? 411 HOH A O   1 
HETATM 5535 O O   . HOH I 6 .   ? 3.76900   0.46600   -43.30700 1.000 48.81000  ? 412 HOH A O   1 
HETATM 5536 O O   . HOH I 6 .   ? 3.71700   -23.43100 -16.27000 1.000 39.16000  ? 413 HOH A O   1 
HETATM 5537 O O   . HOH I 6 .   ? 19.92300  -27.07500 -18.06200 1.000 48.56000  ? 414 HOH A O   1 
HETATM 5538 O O   . HOH I 6 .   ? 13.97400  -38.41300 -27.17600 1.000 51.43000  ? 415 HOH A O   1 
HETATM 5539 O O   . HOH I 6 .   ? 16.33800  -38.25700 -17.77800 1.000 51.15000  ? 416 HOH A O   1 
HETATM 5540 O O   . HOH I 6 .   ? 11.21100  -32.58000 -43.85100 1.000 48.56000  ? 417 HOH A O   1 
HETATM 5541 O O   . HOH I 6 .   ? -7.76200  -29.25400 -38.38800 1.000 48.11000  ? 418 HOH A O   1 
HETATM 5542 O O   . HOH I 6 .   ? 17.48000  -26.91500 -16.92600 1.000 48.81000  ? 419 HOH A O   1 
HETATM 5543 O O   . HOH I 6 .   ? -19.20100 -5.38200  -38.78100 1.000 48.56000  ? 420 HOH A O   1 
HETATM 5544 O O   . HOH I 6 .   ? -11.88500 -10.21200 -29.62800 1.000 43.84000  ? 421 HOH A O   1 
HETATM 5545 O O   . HOH I 6 .   ? 1.58700   -25.32000 -14.03700 1.000 28.78000  ? 422 HOH A O   1 
HETATM 5546 O O   . HOH I 6 .   ? -8.41600  -10.09600 -22.32300 1.000 43.11000  ? 423 HOH A O   1 
HETATM 5547 O O   . HOH I 6 .   ? 11.21400  -32.15600 -40.72800 1.000 43.52000  ? 424 HOH A O   1 
HETATM 5548 O O   . HOH I 6 .   ? -7.87400  -9.34100  -49.89400 1.000 49.98000  ? 425 HOH A O   1 
HETATM 5549 O O   . HOH I 6 .   ? 23.26300  -20.97700 -28.68800 1.000 44.77000  ? 426 HOH A O   1 
HETATM 5550 O O   . HOH I 6 .   ? 17.806    -23.404   -45.089   1.000 53.79000  ? 427 HOH A O   1 
HETATM 5551 O O   . HOH I 6 .   ? 15.96400  -27.00900 -27.21000 1.000 41.24000  ? 428 HOH A O   1 
HETATM 5552 O O   . HOH I 6 .   ? 16.68200  -4.64200  -34.18600 1.000 47.35000  ? 429 HOH A O   1 
HETATM 5553 O O   . HOH I 6 .   ? 11.26900  -25.84100 -48.96800 1.000 45.85000  ? 430 HOH A O   1 
HETATM 5554 O O   . HOH I 6 .   ? -2.62400  -25.29700 -46.31300 1.000 46.69000  ? 431 HOH A O   1 
HETATM 5555 O O   . HOH I 6 .   ? 2.36800   6.52800   -31.34900 1.000 39.99000  ? 432 HOH A O   1 
HETATM 5556 O O   . HOH I 6 .   ? -18.46200 -4.28600  -36.58200 1.000 41.52000  ? 433 HOH A O   1 
HETATM 5557 O O   . HOH I 6 .   ? 13.40000  -22.71800 -7.14100  1.000 48.56000  ? 434 HOH A O   1 
HETATM 5558 O O   . HOH I 6 .   ? 5.73400   -39.54800 -20.38200 1.000 43.10000  ? 435 HOH A O   1 
HETATM 5559 O O   . HOH I 6 .   ? -15.03500 -19.54200 -37.36900 1.000 46.24000  ? 436 HOH A O   1 
HETATM 5560 O O   . HOH I 6 .   ? 3.12600   -26.88200 -16.94300 1.000 51.93000  ? 437 HOH A O   1 
HETATM 5561 O O   . HOH I 6 .   ? 5.73700   -29.40900 -49.31400 1.000 48.81000  ? 438 HOH A O   1 
HETATM 5562 O O   . HOH I 6 .   ? 17.67900  -6.79800  -33.41900 1.000 50.59000  ? 439 HOH A O   1 
HETATM 5563 O O   . HOH I 6 .   ? -1.69400  -27.50500 -45.43400 1.000 39.64000  ? 440 HOH A O   1 
HETATM 5564 O O   . HOH I 6 .   ? 10.50800  -27.99400 -46.61400 1.000 53.16000  ? 441 HOH A O   1 
HETATM 5565 O O   . HOH I 6 .   ? -5.52900  -4.42900  -46.55300 1.000 51.25000  ? 442 HOH A O   1 
HETATM 5566 O O   . HOH I 6 .   ? -6.22500  -18.24000 -49.46700 1.000 46.77000  ? 443 HOH A O   1 
HETATM 5567 O O   . HOH I 6 .   ? -7.17100  -25.41100 -40.76200 1.000 48.81000  ? 444 HOH A O   1 
HETATM 5568 O O   . HOH I 6 .   ? 13.23600  2.69600   -35.86000 1.000 54.36000  ? 445 HOH A O   1 
HETATM 5569 O O   . HOH I 6 .   ? 17.80600  -17.42000 -27.58600 1.000 48.81000  ? 446 HOH A O   1 
HETATM 5570 O O   . HOH I 6 .   ? -12.556   -24.845   -31.739   1.000 48.81000  ? 447 HOH A O   1 
HETATM 5571 O O   . HOH I 6 .   ? -0.547    -28.785   12.353    1.000 48.81000  ? 448 HOH A O   1 
HETATM 5572 O O   . HOH I 6 .   ? 2.67000   -16.00400 -16.93600 1.000 45.78000  ? 449 HOH A O   1 
HETATM 5573 O O   . HOH I 6 .   ? -4.67600  7.75400   -39.00800 1.000 48.81000  ? 450 HOH A O   1 
HETATM 5574 O O   . HOH I 6 .   ? 4.75900   -20.28200 -29.03200 1.000 45.71000  ? 451 HOH A O   1 
HETATM 5575 O O   . HOH I 6 .   ? 20.24300  -16.97800 -21.22700 1.000 45.52000  ? 452 HOH A O   1 
HETATM 5576 O O   . HOH I 6 .   ? 22.70300  -18.43000 -30.02200 1.000 51.98000  ? 453 HOH A O   1 
HETATM 5577 O O   . HOH I 6 .   ? 9.01500   0.44300   -44.35400 1.000 48.52000  ? 454 HOH A O   1 
HETATM 5578 O O   . HOH I 6 .   ? -11.01100 -28.21700 -35.93300 1.000 42.33000  ? 455 HOH A O   1 
HETATM 5579 O O   . HOH I 6 .   ? -7.29800  -12.96700 -22.71800 1.000 49.63000  ? 456 HOH A O   1 
HETATM 5580 O O   . HOH I 6 .   ? 16.575    0.906     -47.567   1.000 54.70000  ? 457 HOH A O   1 
HETATM 5581 O O   . HOH I 6 .   ? 1.04700   -14.31600 -47.49000 1.000 46.16000  ? 458 HOH A O   1 
HETATM 5582 O O   . HOH I 6 .   ? -5.97100  6.33000   -20.66000 1.000 48.81000  ? 459 HOH A O   1 
HETATM 5583 O O   . HOH I 6 .   ? 20.210    -23.666   -43.486   1.000 41.34000  ? 460 HOH A O   1 
HETATM 5584 O O   . HOH I 6 .   ? 0.47900   7.24700   -29.65400 1.000 42.75000  ? 461 HOH A O   1 
HETATM 5585 O O   . HOH I 6 .   ? 21.67900  -11.86800 -39.82400 1.000 48.81000  ? 462 HOH A O   1 
HETATM 5586 O O   . HOH I 6 .   ? -10.21500 -12.00800 -28.99700 1.000 48.81000  ? 463 HOH A O   1 
HETATM 5587 O O   . HOH I 6 .   ? 0.74900   -6.44900  -39.45200 1.000 48.81000  ? 464 HOH A O   1 
HETATM 5588 O O   . HOH I 6 .   ? -0.91200  -31.09300 -9.71200  1.000 61.53000  ? 465 HOH A O   1 
HETATM 5589 O O   . HOH I 6 .   ? -13.24600 -10.51300 -44.97200 1.000 48.81000  ? 466 HOH A O   1 
HETATM 5590 O O   . HOH I 6 .   ? -5.47500  9.33800   -35.51500 1.000 48.81000  ? 467 HOH A O   1 
HETATM 5591 O O   . HOH I 6 .   ? 12.25700  0.95200   -37.69500 1.000 50.88000  ? 468 HOH A O   1 
HETATM 5592 O O   . HOH I 6 .   ? 17.74400  -16.68300 -22.59700 1.000 51.07000  ? 469 HOH A O   1 
HETATM 5593 O O   . HOH I 6 .   ? -8.83900  0.33100   -23.99800 1.000 48.56000  ? 470 HOH A O   1 
HETATM 5594 O O   . HOH I 6 .   ? 4.85000   -29.82300 -26.68000 1.000 48.56000  ? 471 HOH A O   1 
HETATM 5595 O O   . HOH I 6 .   ? 6.62100   -30.17500 -41.00300 1.000 48.81000  ? 472 HOH A O   1 
HETATM 5596 O O   . HOH I 6 .   ? 4.71900   -24.14000 -20.49900 1.000 48.56000  ? 473 HOH A O   1 
HETATM 5597 O O   . HOH I 6 .   ? -5.948    -27.420   -44.814   1.000 48.75000  ? 474 HOH A O   1 
HETATM 5598 O O   . HOH I 6 .   ? -13.67000 -11.41000 -28.02300 1.000 47.46000  ? 475 HOH A O   1 
HETATM 5599 O O   . HOH I 6 .   ? -5.93100  -25.69000 -31.07800 1.000 48.56000  ? 476 HOH A O   1 
HETATM 5600 O O   . HOH I 6 .   ? 13.64400  -16.03400 -48.75800 1.000 47.92000  ? 477 HOH A O   1 
HETATM 5601 O O   . HOH I 6 .   ? 0.67000   -19.54400 -51.07100 1.000 51.80000  ? 478 HOH A O   1 
HETATM 5602 O O   . HOH I 6 .   ? -5.77900  11.68100  -30.33000 1.000 53.32000  ? 479 HOH A O   1 
HETATM 5603 O O   . HOH I 6 .   ? 6.84100   -22.37700 -20.87300 1.000 48.78000  ? 480 HOH A O   1 
HETATM 5604 O O   . HOH I 6 .   ? 8.94500   -16.50700 -50.32400 1.000 50.29000  ? 481 HOH A O   1 
HETATM 5605 O O   . HOH I 6 .   ? 11.47600  -14.52800 -47.58600 1.000 39.78000  ? 482 HOH A O   1 
HETATM 5606 O O   . HOH I 6 .   ? -2.89400  -26.03900 -49.15100 1.000 50.95000  ? 483 HOH A O   1 
HETATM 5607 O O   . HOH I 6 .   ? 3.48600   8.96300   -31.68100 1.000 53.87000  ? 484 HOH A O   1 
HETATM 5608 O O   . HOH J 6 .   ? 29.59700  -16.67200 -5.77600  1.000 63.33000  ? 101 HOH B O   1 
HETATM 5609 O O   . HOH J 6 .   ? 6.31800   -0.78900  -15.03800 1.000 38.04000  ? 102 HOH B O   1 
HETATM 5610 O O   . HOH J 6 .   ? 29.80200  -13.88000 -8.62400  1.000 48.81000  ? 103 HOH B O   1 
HETATM 5611 O O   . HOH J 6 .   ? 25.09000  -23.78200 -19.85600 1.000 53.20000  ? 104 HOH B O   1 
HETATM 5612 O O   . HOH J 6 .   ? 3.88700   -18.17600 -21.02100 1.000 48.81000  ? 105 HOH B O   1 
HETATM 5613 O O   . HOH J 6 .   ? 20.65200  -18.46700 -18.22600 1.000 41.43000  ? 106 HOH B O   1 
HETATM 5614 O O   . HOH J 6 .   ? 8.89600   -2.26000  -22.03900 1.000 45.02000  ? 107 HOH B O   1 
HETATM 5615 O O   . HOH J 6 .   ? 9.85700   -17.12100 -6.27800  1.000 47.38000  ? 108 HOH B O   1 
HETATM 5616 O O   . HOH J 6 .   ? -5.99300  -14.74700 -23.95600 1.000 47.66000  ? 109 HOH B O   1 
HETATM 5617 O O   . HOH J 6 .   ? 11.29400  -13.07000 -22.98700 1.000 38.03000  ? 110 HOH B O   1 
HETATM 5618 O O   . HOH J 6 .   ? 8.85200   -18.61700 -20.76700 1.000 38.18000  ? 111 HOH B O   1 
HETATM 5619 O O   . HOH J 6 .   ? 26.06400  -25.10900 -0.58700  1.000 48.56000  ? 112 HOH B O   1 
HETATM 5620 O O   . HOH J 6 .   ? 17.10200  -8.64700  -25.47700 1.000 48.81000  ? 113 HOH B O   1 
HETATM 5621 O O   . HOH J 6 .   ? 15.81000  -19.49200 -5.23500  1.000 48.81000  ? 114 HOH B O   1 
HETATM 5622 O O   . HOH J 6 .   ? 3.60700   -14.27800 -18.64500 1.000 35.39000  ? 115 HOH B O   1 
HETATM 5623 O O   . HOH J 6 .   ? 29.02100  -7.58100  -4.60900  1.000 59.19000  ? 116 HOH B O   1 
HETATM 5624 O O   . HOH J 6 .   ? 10.61700  -4.31800  -20.62700 1.000 41.15000  ? 117 HOH B O   1 
HETATM 5625 O O   . HOH J 6 .   ? 1.68100   -16.16900 -26.08900 1.000 35.71000  ? 118 HOH B O   1 
HETATM 5626 O O   . HOH J 6 .   ? 6.55800   0.82100   -22.59300 1.000 48.56000  ? 119 HOH B O   1 
HETATM 5627 O O   . HOH J 6 .   ? 8.28700   -15.54900 -12.99100 1.000 35.57000  ? 120 HOH B O   1 
HETATM 5628 O O   . HOH J 6 .   ? 22.36600  -9.98900  -2.68300  1.000 47.39000  ? 121 HOH B O   1 
HETATM 5629 O O   . HOH J 6 .   ? 27.65500  -12.94000 -17.43300 1.000 48.56000  ? 122 HOH B O   1 
HETATM 5630 O O   . HOH J 6 .   ? 21.94600  -16.66800 -2.33800  1.000 42.73000  ? 123 HOH B O   1 
HETATM 5631 O O   . HOH J 6 .   ? 13.16800  -6.83300  -25.37000 1.000 44.07000  ? 124 HOH B O   1 
HETATM 5632 O O   . HOH J 6 .   ? -1.25500  -2.27200  -18.79600 1.000 53.75000  ? 125 HOH B O   1 
HETATM 5633 O O   . HOH J 6 .   ? 7.07400   -14.65800 -7.38300  1.000 49.40000  ? 126 HOH B O   1 
HETATM 5634 O O   . HOH J 6 .   ? 5.31200   -0.49600  -20.43900 1.000 51.10000  ? 127 HOH B O   1 
HETATM 5635 O O   . HOH J 6 .   ? 28.52900  -6.30000  -0.68200  1.000 48.56000  ? 128 HOH B O   1 
HETATM 5636 O O   . HOH J 6 .   ? 27.67900  -24.32000 -9.96600  1.000 57.83000  ? 129 HOH B O   1 
HETATM 5637 O O   . HOH J 6 .   ? 15.65900  -3.26600  -9.87100  1.000 49.35000  ? 130 HOH B O   1 
HETATM 5638 O O   . HOH J 6 .   ? 3.22300   -2.59700  -3.86900  1.000 48.56000  ? 131 HOH B O   1 
HETATM 5639 O O   . HOH J 6 .   ? 12.45000  -17.87300 -6.59800  1.000 37.93000  ? 132 HOH B O   1 
HETATM 5640 O O   . HOH J 6 .   ? 23.61800  -17.72100 -22.04600 1.000 54.72000  ? 133 HOH B O   1 
HETATM 5641 O O   . HOH J 6 .   ? 13.31000  -4.89000  -20.09100 1.000 48.56000  ? 134 HOH B O   1 
HETATM 5642 O O   . HOH J 6 .   ? 2.18600   -19.56100 -27.74100 1.000 47.19000  ? 135 HOH B O   1 
HETATM 5643 O O   . HOH J 6 .   ? 1.06900   -18.85000 -22.78500 1.000 39.99000  ? 136 HOH B O   1 
HETATM 5644 O O   . HOH J 6 .   ? -1.31400  -17.14900 -20.47800 1.000 38.83000  ? 137 HOH B O   1 
HETATM 5645 O O   . HOH J 6 .   ? 21.66000  -6.02500  -12.70800 1.000 53.55000  ? 138 HOH B O   1 
HETATM 5646 O O   . HOH J 6 .   ? -1.71900  -8.59700  -10.43100 1.000 48.56000  ? 139 HOH B O   1 
HETATM 5647 O O   . HOH J 6 .   ? 29.62100  -19.50000 -21.11400 1.000 61.71000  ? 140 HOH B O   1 
HETATM 5648 O O   . HOH J 6 .   ? -2.01700  -14.27600 -27.28700 1.000 48.81000  ? 141 HOH B O   1 
HETATM 5649 O O   . HOH J 6 .   ? 18.22700  -14.45500 -24.29600 1.000 48.81000  ? 142 HOH B O   1 
HETATM 5650 O O   . HOH J 6 .   ? 17.59700  -23.25600 -8.09600  1.000 48.56000  ? 143 HOH B O   1 
HETATM 5651 O O   . HOH J 6 .   ? 7.77700   -14.81800 -5.14000  1.000 59.44000  ? 144 HOH B O   1 
HETATM 5652 O O   . HOH J 6 .   ? 5.85500   -18.68600 -27.34800 1.000 48.69000  ? 145 HOH B O   1 
HETATM 5653 O O   . HOH J 6 .   ? 5.51100   1.19100   -16.24100 1.000 47.89000  ? 146 HOH B O   1 
HETATM 5654 O O   . HOH J 6 .   ? 18.07000  -25.77300 -8.84200  1.000 48.56000  ? 147 HOH B O   1 
HETATM 5655 O O   . HOH J 6 .   ? 11.34600  -18.25400 -22.02400 1.000 42.20000  ? 148 HOH B O   1 
HETATM 5656 O O   . HOH K 6 .   ? 6.86100   -4.82400  -46.07300 1.000 48.81000  ? 101 HOH C O   1 
HETATM 5657 O O   . HOH K 6 .   ? 2.77400   -3.01900  -44.86600 1.000 48.81000  ? 102 HOH C O   1 
HETATM 5658 O O   . HOH K 6 .   ? 2.77400   -8.01000  -40.08500 1.000 43.39000  ? 103 HOH C O   1 
HETATM 5659 O O   . HOH K 6 .   ? 5.19900   -14.22100 -45.26000 1.000 44.39000  ? 104 HOH C O   1 
HETATM 5660 O O   . HOH K 6 .   ? 8.08200   -12.50700 -44.80400 1.000 39.68000  ? 105 HOH C O   1 
HETATM 5661 O O   . HOH K 6 .   ? -3.45200  2.38100   -45.87300 1.000 37.54000  ? 106 HOH C O   1 
HETATM 5662 O O   . HOH K 6 .   ? 1.79800   -0.66600  -44.46100 1.000 48.56000  ? 107 HOH C O   1 
HETATM 5663 O O   . HOH K 6 .   ? 3.03400   -12.45800 -46.09600 1.000 44.13000  ? 108 HOH C O   1 
HETATM 5664 O O   . HOH K 6 .   ? -6.41000  -2.34800  -44.74800 1.000 44.99000  ? 109 HOH C O   1 
HETATM 5665 O O   . HOH L 6 .   ? 19.62500  34.15700  -44.07100 1.000 48.81000  ? 501 HOH G O   1 
HETATM 5666 O O   . HOH L 6 .   ? -31.44900 21.55400  -59.53000 1.000 48.81000  ? 502 HOH G O   1 
HETATM 5667 O O   . HOH L 6 .   ? -6.30600  6.35300   -40.09800 1.000 48.56000  ? 503 HOH G O   1 
HETATM 5668 O O   . HOH L 6 .   ? 9.23400   25.69700  -16.63100 1.000 48.81000  ? 504 HOH G O   1 
HETATM 5669 O O   . HOH L 6 .   ? 19.39000  29.17500  -31.40500 1.000 47.97000  ? 505 HOH G O   1 
HETATM 5670 O O   . HOH L 6 .   ? 16.61200  16.28300  -33.79800 1.000 53.73000  ? 506 HOH G O   1 
HETATM 5671 O O   . HOH L 6 .   ? 23.28000  32.70200  -38.48200 1.000 38.80000  ? 507 HOH G O   1 
HETATM 5672 O O   . HOH L 6 .   ? 14.76200  31.63000  -41.74200 1.000 36.94000  ? 508 HOH G O   1 
HETATM 5673 O O   . HOH L 6 .   ? 16.86800  31.39000  -32.20400 1.000 40.48000  ? 509 HOH G O   1 
HETATM 5674 O O   . HOH L 6 .   ? -7.59300  4.26600   -47.61200 1.000 39.09000  ? 510 HOH G O   1 
HETATM 5675 O O   . HOH L 6 .   ? -9.62300  -2.51500  -53.22500 1.000 48.24000  ? 511 HOH G O   1 
HETATM 5676 O O   . HOH L 6 .   ? 4.63000   34.97100  -36.49000 1.000 48.81000  ? 512 HOH G O   1 
HETATM 5677 O O   . HOH L 6 .   ? -16.98500 18.11600  -63.09000 1.000 48.56000  ? 513 HOH G O   1 
HETATM 5678 O O   . HOH L 6 .   ? 3.91100   31.04600  -53.45300 1.000 45.96000  ? 514 HOH G O   1 
HETATM 5679 O O   . HOH L 6 .   ? 4.35900   17.77200  -34.90400 1.000 51.22000  ? 515 HOH G O   1 
HETATM 5680 O O   . HOH L 6 .   ? -28.78700 11.66500  -52.98000 1.000 48.81000  ? 516 HOH G O   1 
HETATM 5681 O O   . HOH L 6 .   ? 8.38400   10.10700  -56.19600 1.000 58.24000  ? 517 HOH G O   1 
HETATM 5682 O O   . HOH L 6 .   ? 9.10300   8.34800   -52.15800 1.000 48.56000  ? 518 HOH G O   1 
HETATM 5683 O O   . HOH L 6 .   ? 13.38600  16.35000  -54.61200 1.000 48.56000  ? 519 HOH G O   1 
HETATM 5684 O O   . HOH L 6 .   ? -0.15200  9.48000   -57.36600 1.000 40.23000  ? 520 HOH G O   1 
HETATM 5685 O O   . HOH L 6 .   ? -24.12400 -4.75100  -45.63400 1.000 52.51000  ? 521 HOH G O   1 
HETATM 5686 O O   . HOH L 6 .   ? 15.77200  20.21900  -53.69600 1.000 39.36000  ? 522 HOH G O   1 
HETATM 5687 O O   . HOH L 6 .   ? 4.29600   22.83500  -24.53000 1.000 51.17000  ? 523 HOH G O   1 
HETATM 5688 O O   . HOH L 6 .   ? -0.15100  26.41200  -51.02400 1.000 47.68000  ? 524 HOH G O   1 
HETATM 5689 O O   . HOH L 6 .   ? 8.69400   13.42500  -46.26000 1.000 48.81000  ? 525 HOH G O   1 
HETATM 5690 O O   . HOH L 6 .   ? 3.30300   26.76500  -37.47800 1.000 46.01000  ? 526 HOH G O   1 
HETATM 5691 O O   . HOH L 6 .   ? -11.59200 6.10500   -42.97600 1.000 41.20000  ? 527 HOH G O   1 
HETATM 5692 O O   . HOH L 6 .   ? 7.41000   15.20600  -24.86000 1.000 48.81000  ? 528 HOH G O   1 
HETATM 5693 O O   . HOH L 6 .   ? -12.17400 2.56100   -58.23300 1.000 48.87000  ? 529 HOH G O   1 
HETATM 5694 O O   . HOH L 6 .   ? 4.41100   36.98400  -50.04100 1.000 48.81000  ? 530 HOH G O   1 
HETATM 5695 O O   . HOH L 6 .   ? -12.89100 -1.29700  -54.92000 1.000 44.19000  ? 531 HOH G O   1 
HETATM 5696 O O   . HOH L 6 .   ? 22.95400  20.86700  -28.19200 1.000 48.74000  ? 532 HOH G O   1 
HETATM 5697 O O   . HOH L 6 .   ? -19.71300 -1.19400  -52.42900 1.000 42.08000  ? 533 HOH G O   1 
HETATM 5698 O O   . HOH L 6 .   ? 19.08600  7.28800   -23.97300 1.000 58.08000  ? 534 HOH G O   1 
HETATM 5699 O O   . HOH L 6 .   ? 16.02600  35.31500  -32.05500 1.000 53.24000  ? 535 HOH G O   1 
HETATM 5700 O O   . HOH L 6 .   ? -17.45600 -5.04400  -46.10800 1.000 43.59000  ? 536 HOH G O   1 
HETATM 5701 O O   . HOH L 6 .   ? 10.57600  15.58000  -58.45200 1.000 57.04000  ? 537 HOH G O   1 
HETATM 5702 O O   . HOH L 6 .   ? 23.55500  22.78900  -37.44800 1.000 51.90000  ? 538 HOH G O   1 
HETATM 5703 O O   . HOH L 6 .   ? 12.04700  31.48700  -22.20900 1.000 50.74000  ? 539 HOH G O   1 
HETATM 5704 O O   . HOH L 6 .   ? 12.80400  34.24800  -25.65700 1.000 54.54000  ? 540 HOH G O   1 
HETATM 5705 O O   . HOH L 6 .   ? 3.12300   34.17100  -50.02500 1.000 48.56000  ? 541 HOH G O   1 
HETATM 5706 O O   . HOH L 6 .   ? -33.63400 -1.10800  -49.01000 1.000 48.81000  ? 542 HOH G O   1 
HETATM 5707 O O   . HOH L 6 .   ? 9.54100   13.44300  -48.86200 1.000 48.81000  ? 543 HOH G O   1 
HETATM 5708 O O   . HOH L 6 .   ? 4.63800   22.90700  -29.67100 1.000 37.23000  ? 544 HOH G O   1 
HETATM 5709 O O   . HOH L 6 .   ? 8.49700   33.89000  -23.68200 1.000 48.56000  ? 545 HOH G O   1 
HETATM 5710 O O   . HOH L 6 .   ? -18.92600 1.96600   -58.43400 1.000 44.57000  ? 546 HOH G O   1 
HETATM 5711 O O   . HOH L 6 .   ? 0.85300   32.36300  -32.71900 1.000 42.98000  ? 547 HOH G O   1 
HETATM 5712 O O   . HOH L 6 .   ? -24.81100 9.98500   -66.35000 1.000 49.29000  ? 548 HOH G O   1 
HETATM 5713 O O   . HOH L 6 .   ? 3.63900   32.75800  -35.40900 1.000 41.10000  ? 549 HOH G O   1 
HETATM 5714 O O   . HOH L 6 .   ? 16.97700  35.83900  -34.48700 1.000 54.39000  ? 550 HOH G O   1 
HETATM 5715 O O   . HOH L 6 .   ? -22.23900 9.07500   -66.14800 1.000 48.89000  ? 551 HOH G O   1 
HETATM 5716 O O   . HOH L 6 .   ? -1.72400  11.77300  -56.51100 1.000 39.31000  ? 552 HOH G O   1 
HETATM 5717 O O   . HOH L 6 .   ? 6.07600   15.28000  -41.16200 1.000 40.79000  ? 553 HOH G O   1 
HETATM 5718 O O   . HOH L 6 .   ? 16.41400  13.37300  -31.47300 1.000 46.81000  ? 554 HOH G O   1 
HETATM 5719 O O   . HOH L 6 .   ? -7.83300  3.72800   -55.06300 1.000 43.36000  ? 555 HOH G O   1 
HETATM 5720 O O   . HOH L 6 .   ? 17.18800  25.58300  -42.34900 1.000 41.82000  ? 556 HOH G O   1 
HETATM 5721 O O   . HOH L 6 .   ? 20.63700  10.50700  -30.61200 1.000 48.56000  ? 557 HOH G O   1 
HETATM 5722 O O   . HOH L 6 .   ? -5.67500  25.11000  -48.58100 1.000 51.13000  ? 558 HOH G O   1 
HETATM 5723 O O   . HOH L 6 .   ? 0.25400   28.89900  -49.41300 1.000 31.14000  ? 559 HOH G O   1 
HETATM 5724 O O   . HOH L 6 .   ? 12.56300  19.67500  -35.58800 1.000 42.74000  ? 560 HOH G O   1 
HETATM 5725 O O   . HOH L 6 .   ? 14.47500  34.83500  -39.84100 1.000 47.26000  ? 561 HOH G O   1 
HETATM 5726 O O   . HOH L 6 .   ? 12.53000  13.50500  -29.20900 1.000 41.24000  ? 562 HOH G O   1 
HETATM 5727 O O   . HOH L 6 .   ? -5.93500  2.81700   -45.74200 1.000 43.42000  ? 563 HOH G O   1 
HETATM 5728 O O   . HOH L 6 .   ? 26.84500  18.26600  -29.75000 1.000 65.23000  ? 564 HOH G O   1 
HETATM 5729 O O   . HOH L 6 .   ? 22.68400  19.83500  -30.39000 1.000 54.17000  ? 565 HOH G O   1 
HETATM 5730 O O   . HOH L 6 .   ? 3.84600   12.15600  -58.82100 1.000 48.81000  ? 566 HOH G O   1 
HETATM 5731 O O   . HOH L 6 .   ? 0.07400   31.10100  -43.09700 1.000 37.16000  ? 567 HOH G O   1 
HETATM 5732 O O   . HOH L 6 .   ? -1.65200  24.02300  -50.19300 1.000 42.94000  ? 568 HOH G O   1 
HETATM 5733 O O   . HOH L 6 .   ? -30.822   2.870     -40.274   1.000 48.56000  ? 569 HOH G O   1 
HETATM 5734 O O   . HOH L 6 .   ? -21.29200 -4.39700  -43.67200 1.000 43.30000  ? 570 HOH G O   1 
HETATM 5735 O O   . HOH L 6 .   ? -6.64500  19.96100  -49.20900 1.000 43.70000  ? 571 HOH G O   1 
HETATM 5736 O O   . HOH L 6 .   ? 3.77500   28.18600  -18.90000 1.000 48.81000  ? 572 HOH G O   1 
HETATM 5737 O O   . HOH L 6 .   ? 3.12400   6.38200   -58.16100 1.000 48.56000  ? 573 HOH G O   1 
HETATM 5738 O O   . HOH L 6 .   ? 5.57600   35.72100  -51.41200 1.000 48.56000  ? 574 HOH G O   1 
HETATM 5739 O O   . HOH L 6 .   ? -6.51300  9.52300   -57.45700 1.000 44.95000  ? 575 HOH G O   1 
HETATM 5740 O O   . HOH L 6 .   ? -7.61700  -1.31600  -42.52900 1.000 41.03000  ? 576 HOH G O   1 
HETATM 5741 O O   . HOH L 6 .   ? 29.11600  15.82100  -18.76100 1.000 48.56000  ? 577 HOH G O   1 
HETATM 5742 O O   . HOH L 6 .   ? 18.30300  9.40900   -25.94800 1.000 46.25000  ? 578 HOH G O   1 
HETATM 5743 O O   . HOH L 6 .   ? -7.27800  9.39500   -41.27100 1.000 42.59000  ? 579 HOH G O   1 
HETATM 5744 O O   . HOH L 6 .   ? -26.03000 13.33500  -67.60500 1.000 64.21000  ? 580 HOH G O   1 
HETATM 5745 O O   . HOH L 6 .   ? -11.51500 -4.40700  -51.09200 1.000 49.69000  ? 581 HOH G O   1 
HETATM 5746 O O   . HOH L 6 .   ? 11.24700  37.46100  -45.35000 1.000 54.82000  ? 582 HOH G O   1 
HETATM 5747 O O   . HOH L 6 .   ? 7.82800   17.30700  -32.83700 1.000 48.56000  ? 583 HOH G O   1 
HETATM 5748 O O   . HOH L 6 .   ? 7.21100   8.59400   -47.87900 1.000 43.06000  ? 584 HOH G O   1 
HETATM 5749 O O   . HOH L 6 .   ? -6.64400  8.55100   -37.49800 1.000 48.81000  ? 585 HOH G O   1 
HETATM 5750 O O   . HOH L 6 .   ? 14.12100  17.65100  -33.60200 1.000 55.26000  ? 586 HOH G O   1 
HETATM 5751 O O   . HOH L 6 .   ? -2.33700  15.12500  -40.34000 1.000 39.71000  ? 587 HOH G O   1 
HETATM 5752 O O   . HOH L 6 .   ? 17.81100  32.42200  -48.23900 1.000 51.74000  ? 588 HOH G O   1 
HETATM 5753 O O   . HOH L 6 .   ? 18.23900  28.21200  -43.89300 1.000 46.88000  ? 589 HOH G O   1 
HETATM 5754 O O   . HOH L 6 .   ? -7.68300  16.80900  -50.57600 1.000 48.81000  ? 590 HOH G O   1 
HETATM 5755 O O   . HOH L 6 .   ? -2.49300  7.85000   -57.18000 1.000 41.37000  ? 591 HOH G O   1 
HETATM 5756 O O   . HOH L 6 .   ? 2.13400   34.73900  -45.58600 1.000 32.85000  ? 592 HOH G O   1 
HETATM 5757 O O   . HOH L 6 .   ? 14.13100  15.04500  -47.32000 1.000 42.25000  ? 593 HOH G O   1 
HETATM 5758 O O   . HOH L 6 .   ? 14.37800  36.42900  -51.91400 1.000 48.42000  ? 594 HOH G O   1 
HETATM 5759 O O   . HOH L 6 .   ? 21.00200  25.19000  -18.76300 1.000 53.70000  ? 595 HOH G O   1 
HETATM 5760 O O   . HOH L 6 .   ? 13.67100  19.27800  -55.04900 1.000 42.78000  ? 596 HOH G O   1 
HETATM 5761 O O   . HOH L 6 .   ? -20.72700 -3.48200  -51.68200 1.000 47.77000  ? 597 HOH G O   1 
HETATM 5762 O O   . HOH L 6 .   ? 15.32900  15.85900  -43.85600 1.000 46.88000  ? 598 HOH G O   1 
HETATM 5763 O O   . HOH L 6 .   ? 18.21100  30.07000  -36.89900 1.000 36.26000  ? 599 HOH G O   1 
HETATM 5764 O O   . HOH L 6 .   ? -28.20100 10.78100  -46.18900 1.000 51.80000  ? 600 HOH G O   1 
HETATM 5765 O O   . HOH L 6 .   ? 5.18300   11.93800  -44.38700 1.000 43.45000  ? 601 HOH G O   1 
HETATM 5766 O O   . HOH L 6 .   ? 14.78800  24.24400  -39.00700 1.000 48.81000  ? 602 HOH G O   1 
HETATM 5767 O O   . HOH L 6 .   ? 9.70600   37.42300  -36.85000 1.000 51.98000  ? 603 HOH G O   1 
HETATM 5768 O O   . HOH L 6 .   ? 7.39000   14.80500  -44.00000 1.000 48.81000  ? 604 HOH G O   1 
HETATM 5769 O O   . HOH L 6 .   ? 25.98300  18.43300  -26.50800 1.000 55.69000  ? 605 HOH G O   1 
HETATM 5770 O O   . HOH L 6 .   ? 1.74800   26.12600  -29.84200 1.000 44.41000  ? 606 HOH G O   1 
HETATM 5771 O O   . HOH L 6 .   ? -17.11300 -2.57300  -55.30200 1.000 48.02000  ? 607 HOH G O   1 
HETATM 5772 O O   . HOH L 6 .   ? 10.28700  36.67900  -31.33800 1.000 48.48000  ? 608 HOH G O   1 
HETATM 5773 O O   . HOH L 6 .   ? 8.98800   37.60400  -45.86300 1.000 40.89000  ? 609 HOH G O   1 
HETATM 5774 O O   . HOH L 6 .   ? 11.83500  13.73900  -51.24200 1.000 48.04000  ? 610 HOH G O   1 
HETATM 5775 O O   . HOH L 6 .   ? 10.93000  15.77800  -29.80200 1.000 43.15000  ? 611 HOH G O   1 
HETATM 5776 O O   . HOH L 6 .   ? 8.010     33.930    -20.786   1.000 49.13000  ? 612 HOH G O   1 
HETATM 5777 O O   . HOH L 6 .   ? -22.11600 -1.15900  -54.10100 1.000 50.91000  ? 613 HOH G O   1 
HETATM 5778 O O   . HOH L 6 .   ? 22.89600  33.00400  -20.73700 1.000 48.56000  ? 614 HOH G O   1 
HETATM 5779 O O   . HOH L 6 .   ? 3.07300   30.75100  -37.69900 1.000 35.49000  ? 615 HOH G O   1 
HETATM 5780 O O   . HOH L 6 .   ? 7.49600   23.07600  -61.60900 1.000 48.56000  ? 616 HOH G O   1 
HETATM 5781 O O   . HOH L 6 .   ? -30.91400 -6.44700  -52.19200 1.000 48.81000  ? 617 HOH G O   1 
HETATM 5782 O O   . HOH L 6 .   ? -5.71000  13.41400  -57.10000 1.000 48.56000  ? 618 HOH G O   1 
HETATM 5783 O O   . HOH L 6 .   ? -14.53700 13.17600  -59.52800 1.000 48.81000  ? 619 HOH G O   1 
HETATM 5784 O O   . HOH L 6 .   ? 21.08700  26.60100  -31.93700 1.000 53.19000  ? 620 HOH G O   1 
HETATM 5785 O O   . HOH L 6 .   ? 26.84200  32.57100  -45.54600 1.000 46.85000  ? 621 HOH G O   1 
HETATM 5786 O O   . HOH L 6 .   ? 7.37400   6.17200   -46.93300 1.000 56.65000  ? 622 HOH G O   1 
HETATM 5787 O O   . HOH L 6 .   ? -24.61400 -1.36400  -52.80700 1.000 54.67000  ? 623 HOH G O   1 
HETATM 5788 O O   . HOH L 6 .   ? -0.956    30.557    -28.258   1.000 45.78000  ? 624 HOH G O   1 
HETATM 5789 O O   . HOH L 6 .   ? -7.60800  9.72000   -34.69900 1.000 48.81000  ? 625 HOH G O   1 
HETATM 5790 O O   . HOH L 6 .   ? 21.73100  24.92600  -38.82100 1.000 43.05000  ? 626 HOH G O   1 
HETATM 5791 O O   . HOH L 6 .   ? 19.01700  31.27400  -49.91100 1.000 56.93000  ? 627 HOH G O   1 
HETATM 5792 O O   . HOH L 6 .   ? 12.21900  37.21800  -30.08600 1.000 48.56000  ? 628 HOH G O   1 
HETATM 5793 O O   . HOH L 6 .   ? -8.24500  7.53000   -56.94900 1.000 48.56000  ? 629 HOH G O   1 
HETATM 5794 O O   . HOH L 6 .   ? 22.68300  26.78300  -36.94600 1.000 57.88000  ? 630 HOH G O   1 
HETATM 5795 O O   . HOH L 6 .   ? 9.72700   38.50000  -34.76800 1.000 49.84000  ? 631 HOH G O   1 
HETATM 5796 O O   . HOH L 6 .   ? -0.54900  33.08900  -30.79600 1.000 46.22000  ? 632 HOH G O   1 
HETATM 5797 O O   . HOH L 6 .   ? -9.05800  16.34700  -53.30500 1.000 48.56000  ? 633 HOH G O   1 
HETATM 5798 O O   . HOH L 6 .   ? 0.06000   9.06900   -59.92100 1.000 48.56000  ? 634 HOH G O   1 
HETATM 5799 O O   . HOH L 6 .   ? 2.48500   23.73900  -31.20600 1.000 41.38000  ? 635 HOH G O   1 
HETATM 5800 O O   . HOH L 6 .   ? 17.72700  18.17000  -52.76300 1.000 49.40000  ? 636 HOH G O   1 
HETATM 5801 O O   . HOH L 6 .   ? 17.76900  16.46800  -43.79600 1.000 48.81000  ? 637 HOH G O   1 
HETATM 5802 O O   . HOH L 6 .   ? 17.24000  22.71200  -39.60200 1.000 50.53000  ? 638 HOH G O   1 
HETATM 5803 O O   . HOH L 6 .   ? 2.48100   32.63000  -39.39000 1.000 37.99000  ? 639 HOH G O   1 
HETATM 5804 O O   . HOH L 6 .   ? 12.26900  14.11300  -48.43900 1.000 48.56000  ? 640 HOH G O   1 
HETATM 5805 O O   . HOH L 6 .   ? -7.89700  11.73500  -58.43700 1.000 48.56000  ? 641 HOH G O   1 
HETATM 5806 O O   . HOH L 6 .   ? 12.68400  38.39000  -50.63300 1.000 50.11000  ? 642 HOH G O   1 
HETATM 5807 O O   . HOH L 6 .   ? 7.09400   10.26600  -45.72500 1.000 49.70000  ? 643 HOH G O   1 
HETATM 5808 O O   . HOH L 6 .   ? 12.04800  16.00000  -32.18700 1.000 53.10000  ? 644 HOH G 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   . GLY A 1   ? 0.81020 0.55100 0.77360 0.01940  0.05030  0.01840  1   GLY A N   
2    C CA  . GLY A 1   ? 0.79420 0.54380 0.79010 0.00900  0.06710  0.02260  1   GLY A CA  
3    C C   . GLY A 1   ? 0.76070 0.55380 0.79500 -0.00100 0.04250  0.01180  1   GLY A C   
4    O O   . GLY A 1   ? 0.75930 0.57320 0.78580 0.00190  0.01250  0.00200  1   GLY A O   
5    N N   . SER A 2   ? 0.65260 0.45360 0.72460 -0.01090 0.05780  0.01380  2   SER A N   
6    C CA  . SER A 2   ? 0.63770 0.47550 0.74260 -0.01800 0.03700  0.00500  2   SER A CA  
7    C C   . SER A 2   ? 0.63180 0.49030 0.68710 -0.00760 0.02990  0.01360  2   SER A C   
8    O O   . SER A 2   ? 0.64340 0.48870 0.65040 0.00400  0.04440  0.02590  2   SER A O   
9    C CB  . SER A 2   ? 0.60110 0.43970 0.77270 -0.03210 0.05770  0.00240  2   SER A CB  
10   O OG  . SER A 2   ? 0.59970 0.42790 0.83700 -0.04430 0.05770  -0.01200 2   SER A OG  
11   N N   . HIS A 3   ? 0.44710 0.33500 0.51470 -0.01060 0.00580  0.00550  3   HIS A N   
12   C CA  . HIS A 3   ? 0.45210 0.35960 0.47980 -0.00290 -0.00100 0.01150  3   HIS A CA  
13   C C   . HIS A 3   ? 0.42190 0.35160 0.47770 -0.01000 -0.01170 0.00640  3   HIS A C   
14   O O   . HIS A 3   ? 0.40420 0.33740 0.50610 -0.01780 -0.02330 -0.00480 3   HIS A O   
15   C CB  . HIS A 3   ? 0.46010 0.37390 0.44830 0.00650  -0.01950 0.00820  3   HIS A CB  
16   C CG  . HIS A 3   ? 0.47910 0.37330 0.43680 0.01660  -0.01110 0.01270  3   HIS A CG  
17   N ND1 . HIS A 3   ? 0.47970 0.36840 0.40250 0.02820  0.00090  0.02190  3   HIS A ND1 
18   C CD2 . HIS A 3   ? 0.49450 0.37030 0.44910 0.01910  -0.01550 0.00780  3   HIS A CD2 
19   C CE1 . HIS A 3   ? 0.49660 0.36460 0.39580 0.03820  0.00360  0.02300  3   HIS A CE1 
20   N NE2 . HIS A 3   ? 0.50400 0.36420 0.42210 0.03190  -0.00440 0.01540  3   HIS A NE2 
21   N N   . SER A 4   ? 0.47160 0.41560 0.50040 -0.00580 -0.01050 0.01290  4   SER A N   
22   C CA  . SER A 4   ? 0.45300 0.41420 0.50220 -0.01110 -0.01790 0.00990  4   SER A CA  
23   C C   . SER A 4   ? 0.44950 0.42560 0.46100 -0.00580 -0.02780 0.01190  4   SER A C   
24   O O   . SER A 4   ? 0.45100 0.42780 0.42960 0.00140  -0.02330 0.01660  4   SER A O   
25   C CB  . SER A 4   ? 0.44130 0.39860 0.51170 -0.01480 0.00620  0.01690  4   SER A CB  
26   O OG  . SER A 4   ? 0.45150 0.40430 0.47630 -0.00580 0.01820  0.02750  4   SER A OG  
27   N N   . MET A 5   ? 0.47590 0.46190 0.49580 -0.00880 -0.04160 0.00680  5   MET A N   
28   C CA  . MET A 5   ? 0.45470 0.45140 0.44700 -0.00650 -0.04510 0.00910  5   MET A CA  
29   C C   . MET A 5   ? 0.43770 0.44210 0.44950 -0.01090 -0.04340 0.01000  5   MET A C   
30   O O   . MET A 5   ? 0.43460 0.43750 0.48040 -0.01410 -0.05100 0.00390  5   MET A O   
31   C CB  . MET A 5   ? 0.44050 0.43020 0.40930 -0.00290 -0.06150 0.00280  5   MET A CB  
32   C CG  . MET A 5   ? 0.41730 0.41250 0.36050 -0.00220 -0.05870 0.00540  5   MET A CG  
33   S SD  . MET A 5   ? 0.43060 0.40610 0.33210 0.00480  -0.06390 0.00170  5   MET A SD  
34   C CE  . MET A 5   ? 0.44270 0.39230 0.33720 0.01030  -0.08820 -0.00650 5   MET A CE  
35   N N   . ARG A 6   ? 0.37100 0.38390 0.36580 -0.01010 -0.03490 0.01560  6   ARG A N   
36   C CA  . ARG A 6   ? 0.36070 0.37910 0.36760 -0.01310 -0.03310 0.01670  6   ARG A CA  
37   C C   . ARG A 6   ? 0.33370 0.35860 0.31490 -0.01280 -0.03610 0.01730  6   ARG A C   
38   O O   . ARG A 6   ? 0.32060 0.35050 0.28290 -0.01040 -0.03210 0.01830  6   ARG A O   
39   C CB  . ARG A 6   ? 0.36640 0.38140 0.38180 -0.01230 -0.01390 0.02310  6   ARG A CB  
40   C CG  . ARG A 6   ? 0.37490 0.37910 0.42250 -0.01450 -0.00110 0.02360  6   ARG A CG  
41   C CD  . ARG A 6   ? 0.36240 0.37280 0.45980 -0.02050 -0.00680 0.01610  6   ARG A CD  
42   N NE  . ARG A 6   ? 0.36110 0.36190 0.50080 -0.02460 0.01230  0.01560  6   ARG A NE  
43   C CZ  . ARG A 6   ? 0.36220 0.35680 0.52450 -0.02760 0.00870  0.00980  6   ARG A CZ  
44   N NH1 . ARG A 6   ? 0.36750 0.36420 0.51230 -0.02540 -0.01610 0.00330  6   ARG A NH1 
45   N NH2 . ARG A 6   ? 0.35690 0.33880 0.55840 -0.03260 0.03360  0.01070  6   ARG A NH2 
46   N N   . TYR A 7   ? 0.39060 0.41470 0.37580 -0.01480 -0.04270 0.01550  7   TYR A N   
47   C CA  . TYR A 7   ? 0.37580 0.40290 0.34370 -0.01630 -0.04010 0.01690  7   TYR A CA  
48   C C   . TYR A 7   ? 0.37850 0.40890 0.36060 -0.01720 -0.03430 0.01930  7   TYR A C   
49   O O   . TYR A 7   ? 0.39080 0.41930 0.39820 -0.01710 -0.03650 0.01790  7   TYR A O   
50   C CB  . TYR A 7   ? 0.37670 0.39010 0.32530 -0.01560 -0.04950 0.01420  7   TYR A CB  
51   C CG  . TYR A 7   ? 0.38380 0.38890 0.30880 -0.01380 -0.04820 0.01310  7   TYR A CG  
52   C CD1 . TYR A 7   ? 0.40030 0.39400 0.32120 -0.00880 -0.05830 0.00970  7   TYR A CD1 
53   C CD2 . TYR A 7   ? 0.38390 0.39250 0.29590 -0.01680 -0.03560 0.01380  7   TYR A CD2 
54   C CE1 . TYR A 7   ? 0.41150 0.39420 0.30670 -0.00540 -0.05440 0.00890  7   TYR A CE1 
55   C CE2 . TYR A 7   ? 0.40130 0.40230 0.29680 -0.01480 -0.02910 0.01240  7   TYR A CE2 
56   C CZ  . TYR A 7   ? 0.41310 0.39950 0.29590 -0.00840 -0.03780 0.01090  7   TYR A CZ  
57   O OH  . TYR A 7   ? 0.43690 0.41230 0.29940 -0.00480 -0.02910 0.00970  7   TYR A OH  
58   N N   . PHE A 8   ? 0.36310 0.39790 0.33200 -0.01720 -0.02750 0.02090  8   PHE A N   
59   C CA  . PHE A 8   ? 0.37000 0.40330 0.34240 -0.01600 -0.02120 0.02290  8   PHE A CA  
60   C C   . PHE A 8   ? 0.36320 0.39680 0.32310 -0.01920 -0.02450 0.02050  8   PHE A C   
61   O O   . PHE A 8   ? 0.35650 0.39510 0.30630 -0.02100 -0.02480 0.01710  8   PHE A O   
62   C CB  . PHE A 8   ? 0.37660 0.40540 0.33750 -0.00930 -0.01080 0.02570  8   PHE A CB  
63   C CG  . PHE A 8   ? 0.39460 0.41550 0.36190 -0.00570 -0.00200 0.02940  8   PHE A CG  
64   C CD1 . PHE A 8   ? 0.40550 0.41850 0.39770 -0.00660 0.01080  0.03260  8   PHE A CD1 
65   C CD2 . PHE A 8   ? 0.39400 0.41400 0.34640 -0.00140 -0.00430 0.02880  8   PHE A CD2 
66   C CE1 . PHE A 8   ? 0.41600 0.41750 0.41760 -0.00500 0.02380  0.03590  8   PHE A CE1 
67   C CE2 . PHE A 8   ? 0.40990 0.41690 0.36430 0.00220  0.00590  0.03280  8   PHE A CE2 
68   C CZ  . PHE A 8   ? 0.42200 0.41850 0.40100 -0.00050 0.02110  0.03670  8   PHE A CZ  
69   N N   . TYR A 9   ? 0.35900 0.38680 0.32430 -0.01980 -0.02620 0.02100  9   TYR A N   
70   C CA  . TYR A 9   ? 0.35920 0.38160 0.31180 -0.02280 -0.02700 0.01950  9   TYR A CA  
71   C C   . TYR A 9   ? 0.36710 0.38760 0.32020 -0.01960 -0.02140 0.02010  9   TYR A C   
72   O O   . TYR A 9   ? 0.38090 0.39930 0.34790 -0.01540 -0.01660 0.02270  9   TYR A O   
73   C CB  . TYR A 9   ? 0.37290 0.38150 0.32110 -0.02220 -0.03500 0.01930  9   TYR A CB  
74   C CG  . TYR A 9   ? 0.37790 0.37550 0.31230 -0.02110 -0.04200 0.01830  9   TYR A CG  
75   C CD1 . TYR A 9   ? 0.36960 0.37260 0.29800 -0.02360 -0.03750 0.01810  9   TYR A CD1 
76   C CD2 . TYR A 9   ? 0.39730 0.37450 0.31970 -0.01470 -0.05430 0.01670  9   TYR A CD2 
77   C CE1 . TYR A 9   ? 0.38310 0.36990 0.29190 -0.02060 -0.04190 0.01740  9   TYR A CE1 
78   C CE2 . TYR A 9   ? 0.41400 0.37120 0.31160 -0.00940 -0.06230 0.01530  9   TYR A CE2 
79   C CZ  . TYR A 9   ? 0.40580 0.36720 0.29550 -0.01300 -0.05420 0.01630  9   TYR A CZ  
80   O OH  . TYR A 9   ? 0.42790 0.36380 0.28630 -0.00600 -0.06000 0.01500  9   TYR A OH  
81   N N   . THR A 10  ? 0.36580 0.38510 0.30680 -0.02160 -0.02120 0.01630  10  THR A N   
82   C CA  . THR A 10  ? 0.37960 0.39080 0.31360 -0.01770 -0.01850 0.01540  10  THR A CA  
83   C C   . THR A 10  ? 0.38980 0.39340 0.31860 -0.02420 -0.02110 0.01210  10  THR A C   
84   O O   . THR A 10  ? 0.39700 0.40340 0.32590 -0.03120 -0.02200 0.00670  10  THR A O   
85   C CB  . THR A 10  ? 0.39310 0.40280 0.31290 -0.01040 -0.01910 0.01110  10  THR A CB  
86   O OG1 . THR A 10  ? 0.38860 0.39720 0.30570 -0.00320 -0.01340 0.01590  10  THR A OG1 
87   C CG2 . THR A 10  ? 0.41260 0.40640 0.31630 -0.00310 -0.01650 0.00980  10  THR A CG2 
88   N N   . ALA A 11  ? 0.41850 0.41110 0.34630 -0.02180 -0.02040 0.01480  11  ALA A N   
89   C CA  . ALA A 11  ? 0.43860 0.41640 0.35580 -0.02600 -0.02110 0.01290  11  ALA A CA  
90   C C   . ALA A 11  ? 0.45340 0.42390 0.36500 -0.02080 -0.01920 0.01080  11  ALA A C   
91   O O   . ALA A 11  ? 0.45600 0.42510 0.37280 -0.01240 -0.01560 0.01430  11  ALA A O   
92   C CB  . ALA A 11  ? 0.44260 0.40640 0.35530 -0.02340 -0.02550 0.01680  11  ALA A CB  
93   N N   . MET A 12  ? 0.57650 0.54100 0.48070 -0.02550 -0.02050 0.00370  12  MET A N   
94   C CA  . MET A 12  ? 0.60040 0.55430 0.49310 -0.01870 -0.02150 -0.00080 12  MET A CA  
95   C C   . MET A 12  ? 0.62500 0.56200 0.51240 -0.02510 -0.02190 -0.00520 12  MET A C   
96   O O   . MET A 12  ? 0.63660 0.57250 0.53190 -0.03690 -0.02080 -0.01020 12  MET A O   
97   C CB  . MET A 12  ? 0.60150 0.56040 0.48870 -0.01400 -0.02860 -0.01000 12  MET A CB  
98   C CG  . MET A 12  ? 0.58980 0.56460 0.48330 -0.01200 -0.02940 -0.00800 12  MET A CG  
99   S SD  . MET A 12  ? 0.61190 0.59090 0.50010 -0.00470 -0.04500 -0.02310 12  MET A SD  
100  C CE  . MET A 12  ? 0.60490 0.58210 0.51040 -0.01560 -0.05400 -0.03880 12  MET A CE  
101  N N   . SER A 13  ? 0.50070 0.42240 0.37630 -0.01740 -0.02010 -0.00340 13  SER A N   
102  C CA  . SER A 13  ? 0.52650 0.42780 0.39250 -0.02110 -0.02100 -0.00890 13  SER A CA  
103  C C   . SER A 13  ? 0.53870 0.43420 0.39430 -0.01490 -0.02790 -0.02000 13  SER A C   
104  O O   . SER A 13  ? 0.52900 0.42440 0.37130 -0.00160 -0.02790 -0.01870 13  SER A O   
105  C CB  . SER A 13  ? 0.54330 0.42790 0.40000 -0.01370 -0.01740 -0.00200 13  SER A CB  
106  O OG  . SER A 13  ? 0.54240 0.42940 0.39800 0.00010  -0.01370 0.00080  13  SER A OG  
107  N N   . ARG A 14  ? 0.60430 0.49000 0.46430 -0.02360 -0.03340 -0.03180 14  ARG A N   
108  C CA  . ARG A 14  ? 0.61460 0.49150 0.46540 -0.01650 -0.04700 -0.04720 14  ARG A CA  
109  C C   . ARG A 14  ? 0.62780 0.48460 0.48260 -0.02540 -0.04870 -0.05700 14  ARG A C   
110  O O   . ARG A 14  ? 0.62610 0.48680 0.50760 -0.03710 -0.05630 -0.07290 14  ARG A O   
111  C CB  . ARG A 14  ? 0.60210 0.49890 0.47160 -0.01830 -0.06000 -0.05970 14  ARG A CB  
112  C CG  . ARG A 14  ? 0.59110 0.50790 0.49590 -0.03650 -0.05150 -0.05790 14  ARG A CG  
113  C CD  . ARG A 14  ? 0.58370 0.52490 0.51060 -0.03630 -0.06170 -0.06730 14  ARG A CD  
114  N NE  . ARG A 14  ? 0.56920 0.52420 0.53770 -0.05560 -0.05260 -0.07290 14  ARG A NE  
115  C CZ  . ARG A 14  ? 0.54930 0.52680 0.55450 -0.05970 -0.06110 -0.08790 14  ARG A CZ  
116  N NH1 . ARG A 14  ? 0.55380 0.54110 0.55380 -0.04380 -0.08360 -0.09900 14  ARG A NH1 
117  N NH2 . ARG A 14  ? 0.53000 0.51660 0.57620 -0.07810 -0.04550 -0.09230 14  ARG A NH2 
118  N N   . PRO A 15  ? 0.57070 0.40550 0.40460 -0.02020 -0.04100 -0.04900 15  PRO A N   
119  C CA  . PRO A 15  ? 0.58700 0.39760 0.42200 -0.02960 -0.03890 -0.05550 15  PRO A CA  
120  C C   . PRO A 15  ? 0.59780 0.40030 0.44040 -0.03070 -0.05540 -0.07770 15  PRO A C   
121  O O   . PRO A 15  ? 0.60340 0.39760 0.42140 -0.01360 -0.06880 -0.08500 15  PRO A O   
122  C CB  . PRO A 15  ? 0.60950 0.39890 0.41510 -0.01590 -0.03240 -0.04460 15  PRO A CB  
123  C CG  . PRO A 15  ? 0.59120 0.39840 0.39480 -0.00540 -0.02650 -0.03090 15  PRO A CG  
124  C CD  . PRO A 15  ? 0.57360 0.40500 0.38770 -0.00550 -0.03220 -0.03430 15  PRO A CD  
125  N N   . GLY A 16  ? 0.55030 0.35100 0.42690 -0.05000 -0.05350 -0.08960 16  GLY A N   
126  C CA  . GLY A 16  ? 0.56110 0.35570 0.45960 -0.05390 -0.07170 -0.11530 16  GLY A CA  
127  C C   . GLY A 16  ? 0.54500 0.36740 0.47390 -0.05190 -0.09260 -0.13380 16  GLY A C   
128  O O   . GLY A 16  ? 0.56490 0.38670 0.52590 -0.05620 -0.11200 -0.16020 16  GLY A O   
129  N N   . ARG A 17  ? 0.68820 0.53400 0.61080 -0.04460 -0.09140 -0.12280 17  ARG A N   
130  C CA  . ARG A 17  ? 0.66890 0.53950 0.61610 -0.03970 -0.11190 -0.13910 17  ARG A CA  
131  C C   . ARG A 17  ? 0.64820 0.54930 0.64420 -0.05810 -0.09790 -0.13670 17  ARG A C   
132  O O   . ARG A 17  ? 0.62720 0.55080 0.66630 -0.06040 -0.11390 -0.15710 17  ARG A O   
133  C CB  . ARG A 17  ? 0.67230 0.53930 0.56830 -0.01350 -0.12180 -0.13030 17  ARG A CB  
134  C CG  . ARG A 17  ? 0.70460 0.53510 0.54570 0.00910  -0.13440 -0.13470 17  ARG A CG  
135  C CD  . ARG A 17  ? 0.71570 0.53250 0.50170 0.03650  -0.13880 -0.12680 17  ARG A CD  
136  N NE  . ARG A 17  ? 0.71790 0.53830 0.48560 0.03760  -0.10960 -0.09860 17  ARG A NE  
137  C CZ  . ARG A 17  ? 0.70750 0.55120 0.48690 0.03490  -0.10020 -0.08680 17  ARG A CZ  
138  N NH1 . ARG A 17  ? 0.68340 0.55020 0.49150 0.03030  -0.11510 -0.09830 17  ARG A NH1 
139  N NH2 . ARG A 17  ? 0.69590 0.54000 0.46260 0.03730  -0.07620 -0.06470 17  ARG A NH2 
140  N N   . GLY A 18  ? 0.50320 0.40300 0.49250 -0.06870 -0.06980 -0.11400 18  GLY A N   
141  C CA  . GLY A 18  ? 0.48190 0.40140 0.50810 -0.08480 -0.05210 -0.11020 18  GLY A CA  
142  C C   . GLY A 18  ? 0.48620 0.38680 0.48460 -0.09070 -0.02470 -0.08550 18  GLY A C   
143  O O   . GLY A 18  ? 0.50650 0.38490 0.46440 -0.08190 -0.02270 -0.07290 18  GLY A O   
144  N N   . GLU A 19  ? 0.62610 0.53230 0.64550 -0.10380 -0.00440 -0.08030 19  GLU A N   
145  C CA  . GLU A 19  ? 0.63560 0.51980 0.61880 -0.10380 0.01640  -0.05780 19  GLU A CA  
146  C C   . GLU A 19  ? 0.63010 0.52930 0.58410 -0.08730 0.00530  -0.04410 19  GLU A C   
147  O O   . GLU A 19  ? 0.61710 0.54430 0.58390 -0.08050 -0.00950 -0.05020 19  GLU A O   
148  C CB  . GLU A 19  ? 0.63920 0.51790 0.64470 -0.11940 0.04350  -0.05620 19  GLU A CB  
149  C CG  . GLU A 19  ? 0.63700 0.49890 0.68210 -0.13890 0.06300  -0.07000 19  GLU A CG  
150  C CD  . GLU A 19  ? 0.68340 0.49620 0.69050 -0.14080 0.07820  -0.06040 19  GLU A CD  
151  O OE1 . GLU A 19  ? 0.70050 0.49450 0.65210 -0.12530 0.07050  -0.04410 19  GLU A OE1 
152  O OE2 . GLU A 19  ? 0.69140 0.48340 0.72820 -0.15760 0.09840  -0.07030 19  GLU A OE2 
153  N N   . PRO A 20  ? 0.58070 0.45950 0.49730 -0.07970 0.01120  -0.02720 20  PRO A N   
154  C CA  . PRO A 20  ? 0.57700 0.47120 0.47900 -0.06700 0.00310  -0.01640 20  PRO A CA  
155  C C   . PRO A 20  ? 0.55920 0.47590 0.48070 -0.07200 0.00640  -0.01780 20  PRO A C   
156  O O   . PRO A 20  ? 0.55340 0.46110 0.48400 -0.08330 0.02270  -0.01850 20  PRO A O   
157  C CB  . PRO A 20  ? 0.58730 0.45140 0.45550 -0.06060 0.00890  -0.00300 20  PRO A CB  
158  C CG  . PRO A 20  ? 0.60500 0.43850 0.46100 -0.06430 0.01540  -0.00520 20  PRO A CG  
159  C CD  . PRO A 20  ? 0.60750 0.44550 0.49500 -0.08110 0.02460  -0.01850 20  PRO A CD  
160  N N   . ARG A 21  ? 0.59700 0.53930 0.52430 -0.06320 -0.00610 -0.01830 21  ARG A N   
161  C CA  . ARG A 21  ? 0.58110 0.54730 0.52990 -0.06610 -0.00670 -0.02280 21  ARG A CA  
162  C C   . ARG A 21  ? 0.57180 0.54560 0.50680 -0.05750 -0.00890 -0.01130 21  ARG A C   
163  O O   . ARG A 21  ? 0.56130 0.53550 0.48380 -0.04690 -0.01590 -0.00540 21  ARG A O   
164  C CB  . ARG A 21  ? 0.56970 0.55570 0.53800 -0.06170 -0.02260 -0.03790 21  ARG A CB  
165  C CG  . ARG A 21  ? 0.55400 0.56450 0.54350 -0.06090 -0.02690 -0.04370 21  ARG A CG  
166  C CD  . ARG A 21  ? 0.55030 0.57310 0.54930 -0.05030 -0.04840 -0.05980 21  ARG A CD  
167  N NE  . ARG A 21  ? 0.53560 0.58120 0.55760 -0.04820 -0.05420 -0.06730 21  ARG A NE  
168  C CZ  . ARG A 21  ? 0.52650 0.58070 0.54970 -0.03390 -0.07590 -0.08050 21  ARG A CZ  
169  N NH1 . ARG A 21  ? 0.55030 0.58840 0.54770 -0.01950 -0.09330 -0.08770 21  ARG A NH1 
170  N NH2 . ARG A 21  ? 0.51340 0.58790 0.55860 -0.03120 -0.08080 -0.08700 21  ARG A NH2 
171  N N   . PHE A 22  ? 0.46920 0.44800 0.41040 -0.06230 -0.00110 -0.00940 22  PHE A N   
172  C CA  . PHE A 22  ? 0.44730 0.43080 0.37750 -0.05520 -0.00400 -0.00060 22  PHE A CA  
173  C C   . PHE A 22  ? 0.44080 0.44810 0.39130 -0.05620 -0.00520 -0.00650 22  PHE A C   
174  O O   . PHE A 22  ? 0.44300 0.45440 0.41180 -0.06500 0.00490  -0.01320 22  PHE A O   
175  C CB  . PHE A 22  ? 0.45050 0.40580 0.35490 -0.05550 0.00490  0.00790  22  PHE A CB  
176  C CG  . PHE A 22  ? 0.42980 0.38630 0.32340 -0.04750 -0.00180 0.01370  22  PHE A CG  
177  C CD1 . PHE A 22  ? 0.41630 0.37130 0.30490 -0.03730 -0.01550 0.01760  22  PHE A CD1 
178  C CD2 . PHE A 22  ? 0.42520 0.38340 0.31810 -0.04990 0.00590  0.01350  22  PHE A CD2 
179  C CE1 . PHE A 22  ? 0.40920 0.36460 0.29490 -0.03040 -0.02440 0.01970  22  PHE A CE1 
180  C CE2 . PHE A 22  ? 0.41800 0.37340 0.29870 -0.04180 -0.00230 0.01730  22  PHE A CE2 
181  C CZ  . PHE A 22  ? 0.41090 0.36500 0.28910 -0.03240 -0.01900 0.01970  22  PHE A CZ  
182  N N   . ILE A 23  ? 0.46330 0.48410 0.41270 -0.04690 -0.01520 -0.00450 23  ILE A N   
183  C CA  . ILE A 23  ? 0.45220 0.49200 0.41450 -0.04380 -0.01930 -0.00950 23  ILE A CA  
184  C C   . ILE A 23  ? 0.42580 0.46420 0.37700 -0.03860 -0.01930 0.00020  23  ILE A C   
185  O O   . ILE A 23  ? 0.41500 0.44620 0.35720 -0.03320 -0.02190 0.00710  23  ILE A O   
186  C CB  . ILE A 23  ? 0.44970 0.49760 0.41270 -0.03370 -0.03200 -0.01710 23  ILE A CB  
187  C CG1 . ILE A 23  ? 0.46260 0.51250 0.44090 -0.03700 -0.03840 -0.03140 23  ILE A CG1 
188  C CG2 . ILE A 23  ? 0.43330 0.49490 0.40160 -0.02600 -0.03850 -0.02120 23  ILE A CG2 
189  C CD1 . ILE A 23  ? 0.47620 0.52110 0.43800 -0.02160 -0.05420 -0.03830 23  ILE A CD1 
190  N N   . ALA A 24  ? 0.33960 0.38470 0.29640 -0.04020 -0.01590 -0.00100 24  ALA A N   
191  C CA  . ALA A 24  ? 0.31790 0.36030 0.26550 -0.03530 -0.01780 0.00570  24  ALA A CA  
192  C C   . ALA A 24  ? 0.31630 0.37460 0.27400 -0.03120 -0.02000 0.00100  24  ALA A C   
193  O O   . ALA A 24  ? 0.33420 0.40410 0.30830 -0.03430 -0.01720 -0.00770 24  ALA A O   
194  C CB  . ALA A 24  ? 0.32890 0.35210 0.26020 -0.03800 -0.01190 0.00990  24  ALA A CB  
195  N N   . VAL A 25  ? 0.36850 0.42650 0.32060 -0.02380 -0.02440 0.00560  25  VAL A N   
196  C CA  . VAL A 25  ? 0.36550 0.43260 0.32060 -0.01790 -0.02670 0.00230  25  VAL A CA  
197  C C   . VAL A 25  ? 0.36010 0.41870 0.30850 -0.01610 -0.02610 0.00880  25  VAL A C   
198  O O   . VAL A 25  ? 0.35530 0.40390 0.30260 -0.01700 -0.02690 0.01420  25  VAL A O   
199  C CB  . VAL A 25  ? 0.36990 0.43850 0.31930 -0.00670 -0.03370 -0.00130 25  VAL A CB  
200  C CG1 . VAL A 25  ? 0.37980 0.45760 0.34030 -0.00690 -0.04070 -0.01320 25  VAL A CG1 
201  C CG2 . VAL A 25  ? 0.37220 0.42420 0.30640 -0.00160 -0.02990 0.00740  25  VAL A CG2 
202  N N   . GLY A 26  ? 0.38710 0.45010 0.33600 -0.01360 -0.02560 0.00620  26  GLY A N   
203  C CA  . GLY A 26  ? 0.38880 0.44230 0.33130 -0.01100 -0.02700 0.01010  26  GLY A CA  
204  C C   . GLY A 26  ? 0.39280 0.44860 0.33370 -0.00230 -0.02840 0.00960  26  GLY A C   
205  O O   . GLY A 26  ? 0.39940 0.46610 0.34290 0.00330  -0.03050 0.00340  26  GLY A O   
206  N N   . TYR A 27  ? 0.39680 0.44020 0.33590 -0.00020 -0.02780 0.01470  27  TYR A N   
207  C CA  . TYR A 27  ? 0.41160 0.44680 0.34260 0.00890  -0.02560 0.01650  27  TYR A CA  
208  C C   . TYR A 27  ? 0.42850 0.45450 0.36240 0.00760  -0.02650 0.01720  27  TYR A C   
209  O O   . TYR A 27  ? 0.43420 0.45490 0.37960 0.00110  -0.02960 0.01720  27  TYR A O   
210  C CB  . TYR A 27  ? 0.42510 0.44460 0.35090 0.01290  -0.01690 0.02290  27  TYR A CB  
211  C CG  . TYR A 27  ? 0.42690 0.44480 0.33500 0.02170  -0.01810 0.02140  27  TYR A CG  
212  C CD1 . TYR A 27  ? 0.41430 0.44150 0.32850 0.01650  -0.02060 0.01910  27  TYR A CD1 
213  C CD2 . TYR A 27  ? 0.44380 0.44540 0.32440 0.03770  -0.01890 0.02110  27  TYR A CD2 
214  C CE1 . TYR A 27  ? 0.42100 0.44370 0.31790 0.02600  -0.02510 0.01520  27  TYR A CE1 
215  C CE2 . TYR A 27  ? 0.44950 0.44340 0.30750 0.05010  -0.02530 0.01690  27  TYR A CE2 
216  C CZ  . TYR A 27  ? 0.44340 0.44900 0.31140 0.04370  -0.02900 0.01330  27  TYR A CZ  
217  O OH  . TYR A 27  ? 0.45910 0.45370 0.30280 0.05780  -0.03890 0.00680  27  TYR A OH  
218  N N   . VAL A 28  ? 0.37270 0.39540 0.29620 0.01560  -0.02690 0.01570  28  VAL A N   
219  C CA  . VAL A 28  ? 0.39590 0.40290 0.31900 0.01690  -0.02600 0.01700  28  VAL A CA  
220  C C   . VAL A 28  ? 0.41670 0.40550 0.32760 0.02570  -0.01660 0.02260  28  VAL A C   
221  O O   . VAL A 28  ? 0.41320 0.40140 0.30390 0.03800  -0.01850 0.02140  28  VAL A O   
222  C CB  . VAL A 28  ? 0.39940 0.40910 0.31370 0.02120  -0.03080 0.01180  28  VAL A CB  
223  C CG1 . VAL A 28  ? 0.42910 0.41890 0.34050 0.02410  -0.03070 0.01260  28  VAL A CG1 
224  C CG2 . VAL A 28  ? 0.38980 0.40370 0.30400 0.01500  -0.03480 0.00810  28  VAL A CG2 
225  N N   . ASP A 29  ? 0.46250 0.43330 0.38590 0.02090  -0.00610 0.02740  29  ASP A N   
226  C CA  . ASP A 29  ? 0.49100 0.43350 0.39760 0.02910  0.01140  0.03520  29  ASP A CA  
227  C C   . ASP A 29  ? 0.47600 0.41580 0.35570 0.03930  0.01330  0.03780  29  ASP A C   
228  O O   . ASP A 29  ? 0.45850 0.41100 0.35080 0.03270  0.01300  0.03750  29  ASP A O   
229  C CB  . ASP A 29  ? 0.50500 0.42760 0.38860 0.03990  0.01270  0.03610  29  ASP A CB  
230  C CG  . ASP A 29  ? 0.52120 0.44030 0.42990 0.03060  0.01100  0.03260  29  ASP A CG  
231  O OD1 . ASP A 29  ? 0.52280 0.44080 0.46760 0.01780  0.01630  0.03150  29  ASP A OD1 
232  O OD2 . ASP A 29  ? 0.53470 0.45250 0.43000 0.03690  0.00240  0.02890  29  ASP A OD2 
233  N N   . ASP A 30  ? 0.55160 0.47340 0.39220 0.05740  0.01140  0.03840  30  ASP A N   
234  C CA  . ASP A 30  ? 0.55060 0.46340 0.35970 0.07150  0.00770  0.03780  30  ASP A CA  
235  C C   . ASP A 30  ? 0.53280 0.47800 0.34710 0.07650  -0.01720 0.02480  30  ASP A C   
236  O O   . ASP A 30  ? 0.53490 0.47260 0.32430 0.09160  -0.02750 0.01970  30  ASP A O   
237  C CB  . ASP A 30  ? 0.59300 0.45540 0.34790 0.09380  0.01900  0.04470  30  ASP A CB  
238  C CG  . ASP A 30  ? 0.62130 0.44570 0.37420 0.08820  0.05250  0.05800  30  ASP A CG  
239  O OD1 . ASP A 30  ? 0.61240 0.44220 0.38950 0.07600  0.06600  0.06140  30  ASP A OD1 
240  O OD2 . ASP A 30  ? 0.64640 0.43550 0.37820 0.09560  0.06700  0.06420  30  ASP A OD2 
241  N N   . THR A 31  ? 0.43850 0.41620 0.28570 0.06460  -0.02580 0.01830  31  THR A N   
242  C CA  . THR A 31  ? 0.41900 0.42570 0.28020 0.06850  -0.04260 0.00510  31  THR A CA  
243  C C   . THR A 31  ? 0.39610 0.43040 0.28850 0.05100  -0.04270 0.00160  31  THR A C   
244  O O   . THR A 31  ? 0.38970 0.42930 0.29680 0.03720  -0.03600 0.00530  31  THR A O   
245  C CB  . THR A 31  ? 0.42280 0.43670 0.29090 0.07230  -0.04620 0.00060  31  THR A CB  
246  O OG1 . THR A 31  ? 0.45160 0.43600 0.28560 0.09180  -0.04790 0.00300  31  THR A OG1 
247  C CG2 . THR A 31  ? 0.40720 0.45450 0.30390 0.07370  -0.05760 -0.01430 31  THR A CG2 
248  N N   . GLN A 32  ? 0.40860 0.45480 0.30700 0.05340  -0.05130 -0.00640 32  GLN A N   
249  C CA  . GLN A 32  ? 0.39180 0.45930 0.31760 0.03730  -0.04910 -0.00990 32  GLN A CA  
250  C C   . GLN A 32  ? 0.39010 0.48010 0.34370 0.03160  -0.04800 -0.01850 32  GLN A C   
251  O O   . GLN A 32  ? 0.39600 0.49810 0.36180 0.04210  -0.05660 -0.02970 32  GLN A O   
252  C CB  . GLN A 32  ? 0.39330 0.46550 0.32110 0.04110  -0.05850 -0.01790 32  GLN A CB  
253  C CG  . GLN A 32  ? 0.38070 0.46520 0.32990 0.02350  -0.05180 -0.01780 32  GLN A CG  
254  C CD  . GLN A 32  ? 0.38850 0.48470 0.35350 0.02490  -0.06280 -0.03130 32  GLN A CD  
255  O OE1 . GLN A 32  ? 0.39060 0.47890 0.34060 0.04100  -0.07800 -0.03900 32  GLN A OE1 
256  N NE2 . GLN A 32  ? 0.38550 0.49530 0.37790 0.00930  -0.05550 -0.03510 32  GLN A NE2 
257  N N   . PHE A 33  ? 0.34210 0.43380 0.30380 0.01730  -0.03670 -0.01410 33  PHE A N   
258  C CA  . PHE A 33  ? 0.35690 0.46080 0.33750 0.01350  -0.02860 -0.02070 33  PHE A CA  
259  C C   . PHE A 33  ? 0.37010 0.48040 0.36890 0.00040  -0.01630 -0.02390 33  PHE A C   
260  O O   . PHE A 33  ? 0.39070 0.51120 0.41200 -0.00210 -0.00450 -0.03150 33  PHE A O   
261  C CB  . PHE A 33  ? 0.36910 0.45680 0.33050 0.01420  -0.02270 -0.01360 33  PHE A CB  
262  C CG  . PHE A 33  ? 0.36780 0.43560 0.31080 0.00580  -0.01880 -0.00450 33  PHE A CG  
263  C CD1 . PHE A 33  ? 0.35180 0.40780 0.28540 0.00520  -0.02560 0.00250  33  PHE A CD1 
264  C CD2 . PHE A 33  ? 0.38630 0.44300 0.32030 0.00080  -0.00800 -0.00420 33  PHE A CD2 
265  C CE1 . PHE A 33  ? 0.35420 0.39480 0.27910 -0.00020 -0.02720 0.00670  33  PHE A CE1 
266  C CE2 . PHE A 33  ? 0.38600 0.41900 0.29680 -0.00200 -0.01040 0.00170  33  PHE A CE2 
267  C CZ  . PHE A 33  ? 0.36620 0.39430 0.27660 -0.00250 -0.02290 0.00580  33  PHE A CZ  
268  N N   . VAL A 34  ? 0.32020 0.42230 0.31110 -0.00740 -0.01560 -0.01860 34  VAL A N   
269  C CA  . VAL A 34  ? 0.33720 0.43920 0.34140 -0.01900 -0.00230 -0.02120 34  VAL A CA  
270  C C   . VAL A 34  ? 0.32270 0.42620 0.32940 -0.02220 -0.01030 -0.02170 34  VAL A C   
271  O O   . VAL A 34  ? 0.30180 0.39980 0.29170 -0.01600 -0.02200 -0.01660 34  VAL A O   
272  C CB  . VAL A 34  ? 0.34790 0.42210 0.32310 -0.02420 0.01200  -0.01140 34  VAL A CB  
273  C CG1 . VAL A 34  ? 0.36160 0.42760 0.32910 -0.02040 0.02410  -0.01200 34  VAL A CG1 
274  C CG2 . VAL A 34  ? 0.32700 0.38320 0.27350 -0.02160 -0.00010 -0.00150 34  VAL A CG2 
275  N N   . ARG A 35  ? 0.40860 0.51580 0.43600 -0.03200 -0.00070 -0.02790 35  ARG A N   
276  C CA  . ARG A 35  ? 0.40180 0.50610 0.42910 -0.03590 -0.00660 -0.02850 35  ARG A CA  
277  C C   . ARG A 35  ? 0.41180 0.50350 0.44530 -0.04910 0.01300  -0.02810 35  ARG A C   
278  O O   . ARG A 35  ? 0.41170 0.50310 0.46290 -0.05530 0.03230  -0.03220 35  ARG A O   
279  C CB  . ARG A 35  ? 0.38290 0.50700 0.43620 -0.02970 -0.02380 -0.04370 35  ARG A CB  
280  C CG  . ARG A 35  ? 0.37980 0.52660 0.48580 -0.03520 -0.01890 -0.06200 35  ARG A CG  
281  C CD  . ARG A 35  ? 0.37590 0.53150 0.51260 -0.03960 -0.02820 -0.07720 35  ARG A CD  
282  N NE  . ARG A 35  ? 0.35310 0.53550 0.55560 -0.04390 -0.02710 -0.09970 35  ARG A NE  
283  C CZ  . ARG A 35  ? 0.34240 0.54640 0.57870 -0.03190 -0.05460 -0.12170 35  ARG A CZ  
284  N NH1 . ARG A 35  ? 0.33600 0.53120 0.53350 -0.01220 -0.08370 -0.12210 35  ARG A NH1 
285  N NH2 . ARG A 35  ? 0.31840 0.54960 0.62940 -0.03840 -0.05260 -0.14540 35  ARG A NH2 
286  N N   . PHE A 36  ? 0.35310 0.43050 0.37030 -0.05240 0.01060  -0.02280 36  PHE A N   
287  C CA  . PHE A 36  ? 0.36420 0.42500 0.38420 -0.06360 0.02760  -0.02300 36  PHE A CA  
288  C C   . PHE A 36  ? 0.36490 0.42940 0.39250 -0.06500 0.01530  -0.02800 36  PHE A C   
289  O O   . PHE A 36  ? 0.36080 0.42350 0.36740 -0.05660 -0.00020 -0.02250 36  PHE A O   
290  C CB  . PHE A 36  ? 0.37220 0.39610 0.34580 -0.06270 0.03850  -0.00830 36  PHE A CB  
291  C CG  . PHE A 36  ? 0.38740 0.38260 0.34970 -0.07100 0.05680  -0.00600 36  PHE A CG  
292  C CD1 . PHE A 36  ? 0.39230 0.37810 0.34340 -0.07120 0.04740  -0.00350 36  PHE A CD1 
293  C CD2 . PHE A 36  ? 0.40370 0.37600 0.36320 -0.07770 0.08650  -0.00550 36  PHE A CD2 
294  C CE1 . PHE A 36  ? 0.41010 0.36430 0.34640 -0.07780 0.06480  -0.00080 36  PHE A CE1 
295  C CE2 . PHE A 36  ? 0.41990 0.35610 0.36190 -0.08450 0.10790  -0.00170 36  PHE A CE2 
296  C CZ  . PHE A 36  ? 0.42780 0.35560 0.35810 -0.08450 0.09520  0.00050  36  PHE A CZ  
297  N N   . ASP A 37  ? 0.39370 0.46090 0.45300 -0.07550 0.02460  -0.03910 37  ASP A N   
298  C CA  . ASP A 37  ? 0.39720 0.46480 0.46350 -0.07660 0.01220  -0.04610 37  ASP A CA  
299  C C   . ASP A 37  ? 0.40840 0.45540 0.48460 -0.09120 0.03430  -0.04740 37  ASP A C   
300  O O   . ASP A 37  ? 0.39630 0.45080 0.51650 -0.10250 0.05120  -0.05910 37  ASP A O   
301  C CB  . ASP A 37  ? 0.37740 0.47350 0.48190 -0.07090 -0.00950 -0.06630 37  ASP A CB  
302  C CG  . ASP A 37  ? 0.38660 0.47780 0.49060 -0.06840 -0.02610 -0.07530 37  ASP A CG  
303  O OD1 . ASP A 37  ? 0.40540 0.47460 0.48840 -0.07410 -0.01760 -0.06700 37  ASP A OD1 
304  O OD2 . ASP A 37  ? 0.37970 0.48590 0.50080 -0.05790 -0.05040 -0.09220 37  ASP A OD2 
305  N N   . SER A 38  ? 0.43650 0.45560 0.47480 -0.09050 0.03620  -0.03590 38  SER A N   
306  C CA  . SER A 38  ? 0.44970 0.43850 0.48460 -0.10220 0.05920  -0.03410 38  SER A CA  
307  C C   . SER A 38  ? 0.44540 0.44650 0.53050 -0.11340 0.05860  -0.05300 38  SER A C   
308  O O   . SER A 38  ? 0.45290 0.43000 0.54840 -0.12640 0.08330  -0.05450 38  SER A O   
309  C CB  . SER A 38  ? 0.46760 0.42440 0.45000 -0.09500 0.05530  -0.01950 38  SER A CB  
310  O OG  . SER A 38  ? 0.47220 0.44180 0.45590 -0.08860 0.03230  -0.02360 38  SER A OG  
311  N N   . ASP A 39  ? 0.63060 0.66300 0.74420 -0.10710 0.03070  -0.06850 39  ASP A N   
312  C CA  . ASP A 39  ? 0.62200 0.66560 0.78490 -0.11470 0.02200  -0.09090 39  ASP A CA  
313  C C   . ASP A 39  ? 0.59920 0.66730 0.83520 -0.12670 0.03340  -0.11080 39  ASP A C   
314  O O   . ASP A 39  ? 0.59840 0.66920 0.88730 -0.13970 0.03850  -0.12950 39  ASP A O   
315  C CB  . ASP A 39  ? 0.62400 0.68240 0.77920 -0.09840 -0.01550 -0.10160 39  ASP A CB  
316  C CG  . ASP A 39  ? 0.64850 0.68250 0.77110 -0.09540 -0.02280 -0.09810 39  ASP A CG  
317  O OD1 . ASP A 39  ? 0.67340 0.68030 0.76730 -0.10200 -0.00240 -0.08200 39  ASP A OD1 
318  O OD2 . ASP A 39  ? 0.65980 0.69780 0.78130 -0.08410 -0.04960 -0.11190 39  ASP A OD2 
319  N N   . ALA A 40  ? 0.65740 0.74380 0.90400 -0.12290 0.03820  -0.10910 40  ALA A N   
320  C CA  . ALA A 40  ? 0.63570 0.74550 0.95840 -0.13450 0.05450  -0.12810 40  ALA A CA  
321  C C   . ALA A 40  ? 0.63830 0.71970 0.98220 -0.15590 0.10040  -0.12510 40  ALA A C   
322  O O   . ALA A 40  ? 0.66500 0.70350 0.95010 -0.15870 0.12040  -0.10430 40  ALA A O   
323  C CB  . ALA A 40  ? 0.63260 0.75830 0.95130 -0.12630 0.05870  -0.12210 40  ALA A CB  
324  N N   . ALA A 41  ? 0.85850 0.96150 1.29000 -0.17020 0.11740  -0.14780 41  ALA A N   
325  C CA  . ALA A 41  ? 0.86960 0.93920 1.31140 -0.18390 0.16830  -0.14080 41  ALA A CA  
326  C C   . ALA A 41  ? 0.88030 0.93560 1.29220 -0.18110 0.19990  -0.12380 41  ALA A C   
327  O O   . ALA A 41  ? 0.84120 0.93140 1.28100 -0.17330 0.18760  -0.13180 41  ALA A O   
328  C CB  . ALA A 41  ? 0.84850 0.93830 1.37410 -0.18690 0.17040  -0.16670 41  ALA A CB  
329  N N   . SER A 42  ? 0.71540 0.71360 1.06130 -0.18370 0.23810  -0.10010 42  SER A N   
330  C CA  . SER A 42  ? 0.73680 0.70510 1.02590 -0.17610 0.26480  -0.08010 42  SER A CA  
331  C C   . SER A 42  ? 0.73280 0.72400 0.97960 -0.16010 0.22630  -0.07170 42  SER A C   
332  O O   . SER A 42  ? 0.70890 0.73390 0.98400 -0.15390 0.21750  -0.07900 42  SER A O   
333  C CB  . SER A 42  ? 0.72930 0.70630 1.06870 -0.17540 0.29160  -0.09100 42  SER A CB  
334  O OG  . SER A 42  ? 0.77390 0.72970 1.14950 -0.18360 0.31990  -0.10050 42  SER A OG  
335  N N   . PRO A 43  ? 0.50040 0.47430 0.67980 -0.14900 0.19860  -0.05760 43  PRO A N   
336  C CA  . PRO A 43  ? 0.49010 0.48000 0.62660 -0.13090 0.16320  -0.04870 43  PRO A CA  
337  C C   . PRO A 43  ? 0.50940 0.47900 0.60640 -0.12260 0.18130  -0.03610 43  PRO A C   
338  O O   . PRO A 43  ? 0.53630 0.45550 0.59090 -0.12370 0.21630  -0.02390 43  PRO A O   
339  C CB  . PRO A 43  ? 0.51240 0.47390 0.58620 -0.12340 0.14550  -0.03460 43  PRO A CB  
340  C CG  . PRO A 43  ? 0.52300 0.47830 0.62790 -0.13650 0.15320  -0.04410 43  PRO A CG  
341  C CD  . PRO A 43  ? 0.51670 0.45750 0.66390 -0.15280 0.19860  -0.05100 43  PRO A CD  
342  N N   . ARG A 44  ? 0.55930 0.56240 0.66460 -0.11230 0.15770  -0.03930 44  ARG A N   
343  C CA  . ARG A 44  ? 0.57490 0.55740 0.63530 -0.10190 0.16780  -0.02730 44  ARG A CA  
344  C C   . ARG A 44  ? 0.56820 0.58430 0.62620 -0.08910 0.13120  -0.02850 44  ARG A C   
345  O O   . ARG A 44  ? 0.53450 0.59220 0.63720 -0.08850 0.10690  -0.04170 44  ARG A O   
346  C CB  . ARG A 44  ? 0.57630 0.55490 0.67150 -0.10910 0.20830  -0.03350 44  ARG A CB  
347  C CG  . ARG A 44  ? 0.54360 0.58000 0.72810 -0.11410 0.20010  -0.05570 44  ARG A CG  
348  C CD  . ARG A 44  ? 0.55670 0.58780 0.76830 -0.11700 0.24040  -0.05940 44  ARG A CD  
349  N NE  . ARG A 44  ? 0.60530 0.57570 0.77820 -0.12400 0.29100  -0.04660 44  ARG A NE  
350  C CZ  . ARG A 44  ? 0.64780 0.56830 0.75510 -0.11470 0.32040  -0.03120 44  ARG A CZ  
351  N NH1 . ARG A 44  ? 0.65510 0.58260 0.73350 -0.09970 0.30420  -0.02730 44  ARG A NH1 
352  N NH2 . ARG A 44  ? 0.67390 0.53030 0.73500 -0.11250 0.35180  -0.02130 44  ARG A NH2 
353  N N   . MET A 45  ? 0.46040 0.45240 0.46220 -0.07720 0.12730  -0.01540 45  MET A N   
354  C CA  . MET A 45  ? 0.44600 0.46440 0.44790 -0.06630 0.10030  -0.01640 45  MET A CA  
355  C C   . MET A 45  ? 0.43790 0.48930 0.49380 -0.06780 0.10850  -0.03000 45  MET A C   
356  O O   . MET A 45  ? 0.44110 0.48030 0.51020 -0.07280 0.14120  -0.03230 45  MET A O   
357  C CB  . MET A 45  ? 0.46880 0.45260 0.40800 -0.05440 0.09670  -0.00330 45  MET A CB  
358  C CG  . MET A 45  ? 0.45210 0.45880 0.39040 -0.04450 0.06710  -0.00310 45  MET A CG  
359  S SD  . MET A 45  ? 0.43590 0.45570 0.37430 -0.04300 0.03750  -0.00060 45  MET A SD  
360  C CE  . MET A 45  ? 0.44130 0.42470 0.32670 -0.03290 0.02500  0.01000  45  MET A CE  
361  N N   . ALA A 46  ? 0.34400 0.43380 0.43120 -0.06190 0.08060  -0.03990 46  ALA A N   
362  C CA  . ALA A 46  ? 0.32750 0.45190 0.47280 -0.06050 0.08160  -0.05690 46  ALA A CA  
363  C C   . ALA A 46  ? 0.32710 0.46580 0.45820 -0.04510 0.05600  -0.05630 46  ALA A C   
364  O O   . ALA A 46  ? 0.33050 0.46190 0.42480 -0.03800 0.03390  -0.04740 46  ALA A O   
365  C CB  . ALA A 46  ? 0.29680 0.45260 0.50630 -0.06670 0.07060  -0.07710 46  ALA A CB  
366  N N   . PRO A 47  ? 0.31850 0.47470 0.47900 -0.03950 0.06120  -0.06560 47  PRO A N   
367  C CA  . PRO A 47  ? 0.32500 0.48860 0.46680 -0.02370 0.03870  -0.06430 47  PRO A CA  
368  C C   . PRO A 47  ? 0.30450 0.49040 0.46310 -0.01330 0.00530  -0.07560 47  PRO A C   
369  O O   . PRO A 47  ? 0.27830 0.48730 0.48660 -0.01510 -0.00270 -0.09370 47  PRO A O   
370  C CB  . PRO A 47  ? 0.32260 0.49860 0.49750 -0.02050 0.05650  -0.07350 47  PRO A CB  
371  C CG  . PRO A 47  ? 0.30670 0.49860 0.54400 -0.03330 0.07950  -0.08790 47  PRO A CG  
372  C CD  . PRO A 47  ? 0.30850 0.47520 0.52130 -0.04700 0.09190  -0.07740 47  PRO A CD  
373  N N   . ARG A 48  ? 0.43510 0.60880 0.55010 -0.00100 -0.01360 -0.06600 48  ARG A N   
374  C CA  . ARG A 48  ? 0.41670 0.59790 0.52960 0.01430  -0.04270 -0.07460 48  ARG A CA  
375  C C   . ARG A 48  ? 0.42550 0.60270 0.51860 0.03270  -0.05560 -0.07430 48  ARG A C   
376  O O   . ARG A 48  ? 0.41300 0.58590 0.49140 0.04990  -0.07890 -0.08040 48  ARG A O   
377  C CB  . ARG A 48  ? 0.41800 0.57860 0.49160 0.01340  -0.05030 -0.06290 48  ARG A CB  
378  C CG  . ARG A 48  ? 0.41590 0.58130 0.51140 -0.00060 -0.04460 -0.06760 48  ARG A CG  
379  C CD  . ARG A 48  ? 0.40150 0.59310 0.55080 0.00250  -0.05900 -0.09250 48  ARG A CD  
380  N NE  . ARG A 48  ? 0.39560 0.57980 0.52540 0.01670  -0.08640 -0.09930 48  ARG A NE  
381  C CZ  . ARG A 48  ? 0.38740 0.58690 0.54940 0.02850  -0.11220 -0.12330 48  ARG A CZ  
382  N NH1 . ARG A 48  ? 0.36540 0.59620 0.59530 0.02620  -0.11460 -0.14520 48  ARG A NH1 
383  N NH2 . ARG A 48  ? 0.39910 0.57980 0.52530 0.04480  -0.13660 -0.12710 48  ARG A NH2 
384  N N   . ALA A 49  ? 0.34010 0.51290 0.42710 0.03160  -0.04090 -0.06790 49  ALA A N   
385  C CA  . ALA A 49  ? 0.34440 0.51310 0.41730 0.04790  -0.04960 -0.06870 49  ALA A CA  
386  C C   . ALA A 49  ? 0.35250 0.53670 0.45960 0.04530  -0.03230 -0.07650 49  ALA A C   
387  O O   . ALA A 49  ? 0.36720 0.54510 0.47650 0.03060  -0.00740 -0.07020 49  ALA A O   
388  C CB  . ALA A 49  ? 0.35800 0.49480 0.37650 0.04950  -0.04710 -0.04930 49  ALA A CB  
389  N N   . PRO A 50  ? 0.32660 0.52600 0.45660 0.06130  -0.04350 -0.09010 50  PRO A N   
390  C CA  . PRO A 50  ? 0.32020 0.53700 0.49220 0.05910  -0.02330 -0.09970 50  PRO A CA  
391  C C   . PRO A 50  ? 0.35540 0.54550 0.48840 0.05270  0.00160  -0.08300 50  PRO A C   
392  O O   . PRO A 50  ? 0.35620 0.54900 0.51230 0.04470  0.02990  -0.08580 50  PRO A O   
393  C CB  . PRO A 50  ? 0.31410 0.54740 0.50760 0.08250  -0.04710 -0.11640 50  PRO A CB  
394  C CG  . PRO A 50  ? 0.29900 0.53340 0.48540 0.09440  -0.08010 -0.12450 50  PRO A CG  
395  C CD  . PRO A 50  ? 0.31460 0.51690 0.44020 0.08380  -0.07540 -0.10140 50  PRO A CD  
396  N N   . TRP A 51  ? 0.39030 0.55060 0.46480 0.05660  -0.00660 -0.06690 51  TRP A N   
397  C CA  . TRP A 51  ? 0.41600 0.54960 0.45530 0.05460  0.01030  -0.05590 51  TRP A CA  
398  C C   . TRP A 51  ? 0.42360 0.53650 0.44230 0.03930  0.03030  -0.04590 51  TRP A C   
399  O O   . TRP A 51  ? 0.44710 0.53280 0.43330 0.04010  0.04440  -0.03940 51  TRP A O   
400  C CB  . TRP A 51  ? 0.42750 0.53550 0.42020 0.06320  -0.00540 -0.04510 51  TRP A CB  
401  C CG  . TRP A 51  ? 0.41570 0.51420 0.38870 0.05980  -0.02000 -0.03670 51  TRP A CG  
402  C CD1 . TRP A 51  ? 0.39770 0.49720 0.36600 0.07090  -0.03740 -0.03850 51  TRP A CD1 
403  C CD2 . TRP A 51  ? 0.40850 0.49000 0.36070 0.04680  -0.01680 -0.02550 51  TRP A CD2 
404  N NE1 . TRP A 51  ? 0.38400 0.46830 0.33150 0.06410  -0.04050 -0.02810 51  TRP A NE1 
405  C CE2 . TRP A 51  ? 0.38650 0.46370 0.32990 0.04860  -0.02930 -0.02100 51  TRP A CE2 
406  C CE3 . TRP A 51  ? 0.41440 0.48020 0.35200 0.03630  -0.00510 -0.01990 51  TRP A CE3 
407  C CZ2 . TRP A 51  ? 0.37200 0.43650 0.30320 0.03840  -0.02900 -0.01170 51  TRP A CZ2 
408  C CZ3 . TRP A 51  ? 0.39970 0.45190 0.32210 0.02800  -0.01050 -0.01190 51  TRP A CZ3 
409  C CH2 . TRP A 51  ? 0.37580 0.43090 0.30070 0.02810  -0.02170 -0.00820 51  TRP A CH2 
410  N N   . ILE A 52  ? 0.41240 0.53180 0.44290 0.02800  0.03060  -0.04510 52  ILE A N   
411  C CA  . ILE A 52  ? 0.42230 0.51740 0.43050 0.01630  0.05090  -0.03680 52  ILE A CA  
412  C C   . ILE A 52  ? 0.41830 0.52230 0.46480 0.00890  0.08180  -0.04530 52  ILE A C   
413  O O   . ILE A 52  ? 0.43690 0.50940 0.45540 0.00280  0.10670  -0.03770 52  ILE A O   
414  C CB  . ILE A 52  ? 0.41890 0.50900 0.41360 0.00830  0.03750  -0.02960 52  ILE A CB  
415  C CG1 . ILE A 52  ? 0.43290 0.48720 0.38760 0.00170  0.05090  -0.01920 52  ILE A CG1 
416  C CG2 . ILE A 52  ? 0.39500 0.51490 0.43610 0.00230  0.03420  -0.04000 52  ILE A CG2 
417  C CD1 . ILE A 52  ? 0.44750 0.46920 0.35360 0.00940  0.04330  -0.01150 52  ILE A CD1 
418  N N   . GLU A 53  ? 0.44850 0.59020 0.55830 0.01100  0.08220  -0.06210 53  GLU A N   
419  C CA  . GLU A 53  ? 0.43200 0.58820 0.59760 0.00040  0.11220  -0.07340 53  GLU A CA  
420  C C   . GLU A 53  ? 0.45980 0.58800 0.61100 0.00000  0.15380  -0.06910 53  GLU A C   
421  O O   . GLU A 53  ? 0.44780 0.56760 0.62360 -0.01160 0.18960  -0.07140 53  GLU A O   
422  C CB  . GLU A 53  ? 0.39320 0.59940 0.64060 0.00500  0.09740  -0.09720 53  GLU A CB  
423  C CG  . GLU A 53  ? 0.37330 0.59770 0.62650 0.00820  0.05840  -0.10260 53  GLU A CG  
424  C CD  . GLU A 53  ? 0.34660 0.61470 0.67720 0.01570  0.03790  -0.12980 53  GLU A CD  
425  O OE1 . GLU A 53  ? 0.33380 0.62500 0.72410 0.01800  0.05260  -0.14580 53  GLU A OE1 
426  O OE2 . GLU A 53  ? 0.33290 0.61060 0.66510 0.02110  0.00550  -0.13670 53  GLU A OE2 
427  N N   . GLN A 54  ? 0.48500 0.59290 0.59380 0.01280  0.15290  -0.06280 54  GLN A N   
428  C CA  . GLN A 54  ? 0.50990 0.58350 0.59450 0.01590  0.19330  -0.05860 54  GLN A CA  
429  C C   . GLN A 54  ? 0.55500 0.56560 0.54630 0.01810  0.20120  -0.03980 54  GLN A C   
430  O O   . GLN A 54  ? 0.58910 0.55810 0.53460 0.02720  0.22650  -0.03440 54  GLN A O   
431  C CB  . GLN A 54  ? 0.51500 0.59950 0.60900 0.03120  0.19040  -0.06550 54  GLN A CB  
432  C CG  . GLN A 54  ? 0.47370 0.61700 0.66060 0.03380  0.18130  -0.08730 54  GLN A CG  
433  C CD  . GLN A 54  ? 0.45190 0.61720 0.71870 0.02160  0.21930  -0.10180 54  GLN A CD  
434  O OE1 . GLN A 54  ? 0.46670 0.59760 0.71750 0.01530  0.26660  -0.09500 54  GLN A OE1 
435  N NE2 . GLN A 54  ? 0.40170 0.62090 0.75550 0.01970  0.19940  -0.12330 54  GLN A NE2 
436  N N   . GLU A 55  ? 0.63000 0.62980 0.59040 0.01250  0.17850  -0.03120 55  GLU A N   
437  C CA  . GLU A 55  ? 0.66610 0.60630 0.55020 0.01430  0.18940  -0.01750 55  GLU A CA  
438  C C   . GLU A 55  ? 0.67300 0.58950 0.56450 0.00570  0.23710  -0.01650 55  GLU A C   
439  O O   . GLU A 55  ? 0.64050 0.59410 0.60310 -0.00830 0.24950  -0.02570 55  GLU A O   
440  C CB  . GLU A 55  ? 0.66000 0.59850 0.52150 0.01030  0.15540  -0.01100 55  GLU A CB  
441  C CG  . GLU A 55  ? 0.65740 0.61110 0.51110 0.01680  0.11450  -0.01050 55  GLU A CG  
442  C CD  . GLU A 55  ? 0.68590 0.59900 0.47940 0.03110  0.10530  -0.00630 55  GLU A CD  
443  O OE1 . GLU A 55  ? 0.70770 0.56730 0.44190 0.03910  0.12210  -0.00120 55  GLU A OE1 
444  O OE2 . GLU A 55  ? 0.66510 0.59500 0.46720 0.03580  0.08030  -0.00880 55  GLU A OE2 
445  N N   . GLY A 56  ? 0.75800 0.60660 0.57210 0.01520  0.26350  -0.00590 56  GLY A N   
446  C CA  . GLY A 56  ? 0.76640 0.57800 0.57550 0.00980  0.31850  -0.00290 56  GLY A CA  
447  C C   . GLY A 56  ? 0.76380 0.56290 0.57010 -0.00250 0.32290  0.00220  56  GLY A C   
448  O O   . GLY A 56  ? 0.74560 0.56450 0.55030 -0.00570 0.28140  0.00360  56  GLY A O   
449  N N   . PRO A 57  ? 0.57010 0.70220 0.54950 -0.11710 0.13620  -0.04230 57  PRO A N   
450  C CA  . PRO A 57  ? 0.57120 0.68420 0.53880 -0.12580 0.14420  -0.03070 57  PRO A CA  
451  C C   . PRO A 57  ? 0.60960 0.68780 0.50980 -0.11440 0.13180  -0.01680 57  PRO A C   
452  O O   . PRO A 57  ? 0.60070 0.66710 0.49570 -0.11920 0.12660  -0.00690 57  PRO A O   
453  C CB  . PRO A 57  ? 0.57990 0.68000 0.56100 -0.13440 0.19120  -0.02960 57  PRO A CB  
454  C CG  . PRO A 57  ? 0.60100 0.70380 0.57090 -0.12520 0.20520  -0.03630 57  PRO A CG  
455  C CD  . PRO A 57  ? 0.58370 0.72080 0.58110 -0.11990 0.16950  -0.04980 57  PRO A CD  
456  N N   . GLU A 58  ? 0.69450 0.76020 0.54680 -0.09720 0.12440  -0.02070 58  GLU A N   
457  C CA  . GLU A 58  ? 0.72430 0.76840 0.52000 -0.08120 0.10420  -0.01600 58  GLU A CA  
458  C C   . GLU A 58  ? 0.68860 0.74740 0.51630 -0.08690 0.06930  -0.02010 58  GLU A C   
459  O O   . GLU A 58  ? 0.68840 0.73290 0.49040 -0.08160 0.05530  -0.01240 58  GLU A O   
460  C CB  . GLU A 58  ? 0.77180 0.81050 0.51730 -0.05700 0.09780  -0.03150 58  GLU A CB  
461  C CG  . GLU A 58  ? 0.76470 0.82960 0.55260 -0.05740 0.07240  -0.05860 58  GLU A CG  
462  C CD  . GLU A 58  ? 0.74920 0.83380 0.59330 -0.07110 0.08920  -0.06260 58  GLU A CD  
463  O OE1 . GLU A 58  ? 0.75860 0.83870 0.59180 -0.07190 0.12010  -0.05760 58  GLU A OE1 
464  O OE2 . GLU A 58  ? 0.71540 0.81850 0.61540 -0.07780 0.07490  -0.06900 58  GLU A OE2 
465  N N   . TYR A 59  ? 0.51610 0.60090 0.39900 -0.09420 0.05940  -0.02900 59  TYR A N   
466  C CA  . TYR A 59  ? 0.48800 0.58160 0.40110 -0.09570 0.03680  -0.02720 59  TYR A CA  
467  C C   . TYR A 59  ? 0.46290 0.55670 0.38180 -0.10490 0.03610  -0.01320 59  TYR A C   
468  O O   . TYR A 59  ? 0.45790 0.54010 0.36400 -0.10330 0.02170  -0.00700 59  TYR A O   
469  C CB  . TYR A 59  ? 0.48140 0.59640 0.44470 -0.09350 0.03660  -0.03240 59  TYR A CB  
470  C CG  . TYR A 59  ? 0.45200 0.56930 0.44350 -0.08900 0.02400  -0.02480 59  TYR A CG  
471  C CD1 . TYR A 59  ? 0.45620 0.56200 0.46280 -0.08420 0.01520  -0.03390 59  TYR A CD1 
472  C CD2 . TYR A 59  ? 0.40530 0.53830 0.41250 -0.08640 0.02300  -0.01190 59  TYR A CD2 
473  C CE1 . TYR A 59  ? 0.42500 0.52720 0.46320 -0.07950 0.01360  -0.02410 59  TYR A CE1 
474  C CE2 . TYR A 59  ? 0.38380 0.51440 0.40720 -0.07600 0.01770  -0.00030 59  TYR A CE2 
475  C CZ  . TYR A 59  ? 0.39880 0.51030 0.43880 -0.07380 0.01710  -0.00320 59  TYR A CZ  
476  O OH  . TYR A 59  ? 0.38350 0.48680 0.44610 -0.06320 0.02140  0.01080  59  TYR A OH  
477  N N   . TRP A 60  ? 0.48090 0.59120 0.42650 -0.11400 0.05110  -0.01350 60  TRP A N   
478  C CA  . TRP A 60  ? 0.44860 0.56890 0.41530 -0.12180 0.04760  -0.01110 60  TRP A CA  
479  C C   . TRP A 60  ? 0.47210 0.56060 0.40900 -0.12860 0.05890  -0.00090 60  TRP A C   
480  O O   . TRP A 60  ? 0.45300 0.53870 0.39370 -0.13130 0.04810  0.00310  60  TRP A O   
481  C CB  . TRP A 60  ? 0.41820 0.57370 0.43490 -0.12750 0.05780  -0.02630 60  TRP A CB  
482  C CG  . TRP A 60  ? 0.40100 0.58600 0.43960 -0.11290 0.04610  -0.03160 60  TRP A CG  
483  C CD1 . TRP A 60  ? 0.40610 0.60330 0.46000 -0.10930 0.05740  -0.03890 60  TRP A CD1 
484  C CD2 . TRP A 60  ? 0.38190 0.58170 0.42500 -0.09490 0.02610  -0.02530 60  TRP A CD2 
485  N NE1 . TRP A 60  ? 0.39060 0.60900 0.46020 -0.08960 0.04500  -0.03710 60  TRP A NE1 
486  C CE2 . TRP A 60  ? 0.38330 0.60170 0.44410 -0.07880 0.02820  -0.02670 60  TRP A CE2 
487  C CE3 . TRP A 60  ? 0.36990 0.56650 0.40250 -0.08780 0.01110  -0.01650 60  TRP A CE3 
488  C CZ2 . TRP A 60  ? 0.38120 0.61050 0.44590 -0.05230 0.01980  -0.01530 60  TRP A CZ2 
489  C CZ3 . TRP A 60  ? 0.36610 0.57490 0.40140 -0.06250 0.00270  -0.00640 60  TRP A CZ3 
490  C CH2 . TRP A 60  ? 0.38090 0.60400 0.43050 -0.04340 0.00900  -0.00400 60  TRP A CH2 
491  N N   . ASP A 61  ? 0.58720 0.64900 0.49130 -0.12710 0.08420  0.00560  61  ASP A N   
492  C CA  . ASP A 61  ? 0.61750 0.64070 0.48370 -0.12500 0.10210  0.02240  61  ASP A CA  
493  C C   . ASP A 61  ? 0.62890 0.63690 0.45070 -0.11010 0.07370  0.03050  61  ASP A C   
494  O O   . ASP A 61  ? 0.63030 0.62110 0.44480 -0.11130 0.07290  0.04110  61  ASP A O   
495  C CB  . ASP A 61  ? 0.66820 0.66190 0.49550 -0.11590 0.14060  0.03300  61  ASP A CB  
496  C CG  . ASP A 61  ? 0.66900 0.67480 0.55550 -0.13380 0.17790  0.02380  61  ASP A CG  
497  O OD1 . ASP A 61  ? 0.62000 0.66530 0.57800 -0.15070 0.16620  0.00340  61  ASP A OD1 
498  O OD2 . ASP A 61  ? 0.70590 0.68350 0.56770 -0.12710 0.21990  0.03520  61  ASP A OD2 
499  N N   . GLY A 62  ? 0.58540 0.60140 0.38640 -0.09600 0.05090  0.02110  62  GLY A N   
500  C CA  . GLY A 62  ? 0.58160 0.59360 0.36220 -0.08290 0.02080  0.01850  62  GLY A CA  
501  C C   . GLY A 62  ? 0.53200 0.55840 0.35710 -0.09430 0.00280  0.01840  62  GLY A C   
502  O O   . GLY A 62  ? 0.52970 0.54480 0.34260 -0.08940 -0.01020 0.02410  62  GLY A O   
503  N N   . GLU A 63  ? 0.47630 0.52740 0.34860 -0.10440 0.00280  0.01290  63  GLU A N   
504  C CA  . GLU A 63  ? 0.44420 0.50720 0.34740 -0.10710 -0.00950 0.01610  63  GLU A CA  
505  C C   . GLU A 63  ? 0.44470 0.50240 0.34810 -0.11590 -0.00330 0.02290  63  GLU A C   
506  O O   . GLU A 63  ? 0.42950 0.48030 0.33180 -0.11430 -0.01420 0.02830  63  GLU A O   
507  C CB  . GLU A 63  ? 0.41980 0.50950 0.36060 -0.10470 -0.00800 0.01210  63  GLU A CB  
508  C CG  . GLU A 63  ? 0.42280 0.51300 0.37950 -0.09620 -0.01050 0.00620  63  GLU A CG  
509  C CD  . GLU A 63  ? 0.41700 0.49280 0.37690 -0.09220 -0.02350 0.00220  63  GLU A CD  
510  O OE1 . GLU A 63  ? 0.38930 0.46410 0.37140 -0.08880 -0.02550 0.01050  63  GLU A OE1 
511  O OE2 . GLU A 63  ? 0.43390 0.50220 0.37550 -0.08900 -0.03170 -0.01180 63  GLU A OE2 
512  N N   . THR A 64  ? 0.44220 0.50310 0.35620 -0.12600 0.01710  0.01920  64  THR A N   
513  C CA  . THR A 64  ? 0.43060 0.48790 0.36300 -0.13680 0.02690  0.01760  64  THR A CA  
514  C C   . THR A 64  ? 0.46150 0.47850 0.35620 -0.13370 0.03280  0.03440  64  THR A C   
515  O O   . THR A 64  ? 0.45130 0.46400 0.35510 -0.13630 0.02580  0.03580  64  THR A O   
516  C CB  . THR A 64  ? 0.43140 0.50060 0.40140 -0.14980 0.05320  0.00410  64  THR A CB  
517  O OG1 . THR A 64  ? 0.39180 0.50750 0.40040 -0.14680 0.03950  -0.01500 64  THR A OG1 
518  C CG2 . THR A 64  ? 0.43380 0.49400 0.43890 -0.16430 0.07180  -0.00380 64  THR A CG2 
519  N N   . ARG A 65  ? 0.60880 0.59740 0.45580 -0.12230 0.04410  0.04690  65  ARG A N   
520  C CA  . ARG A 65  ? 0.64280 0.59430 0.44220 -0.10800 0.04720  0.06500  65  ARG A CA  
521  C C   . ARG A 65  ? 0.62160 0.58100 0.41840 -0.10010 0.01250  0.06280  65  ARG A C   
522  O O   . ARG A 65  ? 0.62970 0.57100 0.42060 -0.09810 0.01210  0.07230  65  ARG A O   
523  C CB  . ARG A 65  ? 0.69480 0.62320 0.43120 -0.08480 0.05850  0.07540  65  ARG A CB  
524  C CG  . ARG A 65  ? 0.74930 0.63450 0.45820 -0.07910 0.10640  0.09830  65  ARG A CG  
525  C CD  . ARG A 65  ? 0.79400 0.65490 0.42620 -0.04680 0.12290  0.11180  65  ARG A CD  
526  N NE  . ARG A 65  ? 0.80430 0.66450 0.45290 -0.05680 0.15930  0.11030  65  ARG A NE  
527  C CZ  . ARG A 65  ? 0.81380 0.65100 0.50030 -0.07370 0.21070  0.12100  65  ARG A CZ  
528  N NH1 . ARG A 65  ? 0.80850 0.62140 0.52560 -0.08510 0.23240  0.13180  65  ARG A NH1 
529  N NH2 . ARG A 65  ? 0.81430 0.65290 0.51770 -0.08000 0.24410  0.11750  65  ARG A NH2 
530  N N   . ASN A 66  ? 0.51320 0.49700 0.32170 -0.09550 -0.01230 0.04950  66  ASN A N   
531  C CA  A ASN A 66  ? 0.48970 0.48130 0.31280 -0.08990 -0.03810 0.04490  66  ASN A CA  
532  C CA  B ASN A 66  ? 0.48860 0.48100 0.31310 -0.09030 -0.03830 0.04450  66  ASN A CA  
533  C C   . ASN A 66  ? 0.46190 0.46010 0.31810 -0.10190 -0.03740 0.04860  66  ASN A C   
534  O O   . ASN A 66  ? 0.45970 0.44790 0.31430 -0.09780 -0.04670 0.05340  66  ASN A O   
535  C CB  A ASN A 66  ? 0.46770 0.48160 0.31800 -0.08640 -0.05280 0.02820  66  ASN A CB  
536  C CB  B ASN A 66  ? 0.46420 0.47990 0.31940 -0.08820 -0.05180 0.02840  66  ASN A CB  
537  C CG  A ASN A 66  ? 0.44520 0.46390 0.31860 -0.07850 -0.07400 0.01850  66  ASN A CG  
538  C CG  B ASN A 66  ? 0.48970 0.50620 0.32260 -0.07200 -0.06450 0.01300  66  ASN A CG  
539  O OD1 A ASN A 66  ? 0.46740 0.47510 0.31810 -0.06730 -0.08610 0.01950  66  ASN A OD1 
540  O OD1 B ASN A 66  ? 0.52840 0.52910 0.30910 -0.05550 -0.06600 0.01680  66  ASN A OD1 
541  N ND2 A ASN A 66  ? 0.41860 0.45220 0.34190 -0.08190 -0.07490 0.00910  66  ASN A ND2 
542  N ND2 B ASN A 66  ? 0.47240 0.50750 0.34510 -0.07220 -0.07230 -0.00630 66  ASN A ND2 
543  N N   . MET A 67  ? 0.47810 0.49670 0.36310 -0.11240 -0.02870 0.04320  67  MET A N   
544  C CA  . MET A 67  ? 0.45590 0.48750 0.36540 -0.11570 -0.03210 0.04080  67  MET A CA  
545  C C   . MET A 67  ? 0.47480 0.48710 0.38180 -0.12390 -0.02160 0.04280  67  MET A C   
546  O O   . MET A 67  ? 0.46170 0.47050 0.37410 -0.12200 -0.02900 0.04410  67  MET A O   
547  C CB  . MET A 67  ? 0.42460 0.49010 0.36070 -0.11580 -0.02990 0.02890  67  MET A CB  
548  C CG  . MET A 67  ? 0.40620 0.48660 0.34910 -0.10310 -0.03510 0.03170  67  MET A CG  
549  S SD  . MET A 67  ? 0.38760 0.46020 0.33630 -0.08850 -0.04160 0.04390  67  MET A SD  
550  C CE  . MET A 67  ? 0.39510 0.44430 0.34290 -0.09240 -0.04720 0.04310  67  MET A CE  
551  N N   . LYS A 68  ? 0.52920 0.52500 0.43210 -0.13210 0.00130  0.04400  68  LYS A N   
552  C CA  . LYS A 68  ? 0.54740 0.51510 0.45530 -0.13910 0.02120  0.04880  68  LYS A CA  
553  C C   . LYS A 68  ? 0.56800 0.50470 0.43740 -0.12490 0.01280  0.06790  68  LYS A C   
554  O O   . LYS A 68  ? 0.57020 0.49490 0.45150 -0.12740 0.01480  0.06910  68  LYS A O   
555  C CB  . LYS A 68  ? 0.57200 0.51640 0.48300 -0.14670 0.05880  0.05340  68  LYS A CB  
556  C CG  . LYS A 68  ? 0.55070 0.52760 0.52550 -0.16510 0.07150  0.02560  68  LYS A CG  
557  C CD  . LYS A 68  ? 0.57860 0.52430 0.58080 -0.17740 0.12050  0.02800  68  LYS A CD  
558  C CE  . LYS A 68  ? 0.54780 0.53460 0.62570 -0.19520 0.13160  -0.00710 68  LYS A CE  
559  N NZ  . LYS A 68  ? 0.51510 0.52830 0.67450 -0.21160 0.13350  -0.04500 68  LYS A NZ  
560  N N   . ALA A 69  ? 0.54810 0.47640 0.37510 -0.10730 0.00060  0.07790  69  ALA A N   
561  C CA  . ALA A 69  ? 0.56550 0.47520 0.36030 -0.08780 -0.01480 0.08890  69  ALA A CA  
562  C C   . ALA A 69  ? 0.52920 0.45790 0.35570 -0.09090 -0.03820 0.08020  69  ALA A C   
563  O O   . ALA A 69  ? 0.53580 0.44810 0.35960 -0.08560 -0.04030 0.08740  69  ALA A O   
564  C CB  . ALA A 69  ? 0.58290 0.49450 0.33570 -0.06470 -0.03070 0.08780  69  ALA A CB  
565  N N   . SER A 70  ? 0.52840 0.48790 0.38520 -0.09690 -0.05030 0.06760  70  SER A N   
566  C CA  . SER A 70  ? 0.49770 0.46970 0.38250 -0.09530 -0.06310 0.06410  70  SER A CA  
567  C C   . SER A 70  ? 0.50080 0.47340 0.40040 -0.10330 -0.05470 0.06330  70  SER A C   
568  O O   . SER A 70  ? 0.49900 0.46770 0.40770 -0.09870 -0.06060 0.06540  70  SER A O   
569  C CB  . SER A 70  ? 0.46240 0.45890 0.37410 -0.09410 -0.06710 0.05690  70  SER A CB  
570  O OG  . SER A 70  ? 0.46470 0.46340 0.37500 -0.08770 -0.07600 0.04940  70  SER A OG  
571  N N   . ALA A 71  ? 0.41880 0.40050 0.32820 -0.11420 -0.04170 0.05470  71  ALA A N   
572  C CA  . ALA A 71  ? 0.41010 0.39760 0.34160 -0.12070 -0.03610 0.04280  71  ALA A CA  
573  C C   . ALA A 71  ? 0.43820 0.39010 0.36330 -0.12270 -0.02670 0.05210  71  ALA A C   
574  O O   . ALA A 71  ? 0.43390 0.38570 0.37210 -0.12150 -0.03010 0.04670  71  ALA A O   
575  C CB  . ALA A 71  ? 0.40100 0.40910 0.35960 -0.13260 -0.02420 0.02220  71  ALA A CB  
576  N N   . GLN A 72  ? 0.53310 0.45260 0.43380 -0.12090 -0.01220 0.06790  72  GLN A N   
577  C CA  . GLN A 72  ? 0.56100 0.44100 0.44740 -0.11430 0.00010  0.08350  72  GLN A CA  
578  C C   . GLN A 72  ? 0.55500 0.43450 0.42600 -0.09780 -0.02470 0.09110  72  GLN A C   
579  O O   . GLN A 72  ? 0.56250 0.42780 0.44310 -0.09580 -0.02310 0.09350  72  GLN A O   
580  C CB  . GLN A 72  ? 0.60810 0.45040 0.45730 -0.10440 0.02500  0.10500  72  GLN A CB  
581  C CG  . GLN A 72  ? 0.65930 0.45570 0.47720 -0.08480 0.03860  0.12950  72  GLN A CG  
582  C CD  . GLN A 72  ? 0.71530 0.46640 0.48740 -0.06670 0.07470  0.15710  72  GLN A CD  
583  O OE1 . GLN A 72  ? 0.73260 0.48940 0.46500 -0.05320 0.07050  0.16230  72  GLN A OE1 
584  N NE2 . GLN A 72  ? 0.73690 0.43990 0.51350 -0.06310 0.11440  0.17590  72  GLN A NE2 
585  N N   . THR A 73  ? 0.49670 0.39350 0.35420 -0.08670 -0.04630 0.09070  73  THR A N   
586  C CA  . THR A 73  ? 0.48520 0.38930 0.34960 -0.07330 -0.06890 0.08930  73  THR A CA  
587  C C   . THR A 73  ? 0.46190 0.37890 0.36180 -0.08130 -0.06960 0.08230  73  THR A C   
588  O O   . THR A 73  ? 0.46600 0.37130 0.37270 -0.07510 -0.07230 0.08570  73  THR A O   
589  C CB  . THR A 73  ? 0.47180 0.39910 0.34040 -0.06550 -0.08770 0.07910  73  THR A CB  
590  O OG1 . THR A 73  ? 0.50350 0.41950 0.32950 -0.04640 -0.09430 0.08270  73  THR A OG1 
591  C CG2 . THR A 73  ? 0.45550 0.39900 0.36360 -0.05980 -0.10390 0.06890  73  THR A CG2 
592  N N   . TYR A 74  ? 0.48410 0.42490 0.40150 -0.09000 -0.06580 0.07320  74  TYR A N   
593  C CA  . TYR A 74  ? 0.47170 0.42630 0.41010 -0.08680 -0.06560 0.06900  74  TYR A CA  
594  C C   . TYR A 74  ? 0.48500 0.43500 0.42750 -0.09160 -0.05760 0.06080  74  TYR A C   
595  O O   . TYR A 74  ? 0.48820 0.43990 0.43990 -0.08430 -0.05790 0.05950  74  TYR A O   
596  C CB  . TYR A 74  ? 0.45070 0.43090 0.39660 -0.08280 -0.06300 0.06590  74  TYR A CB  
597  C CG  . TYR A 74  ? 0.43820 0.41850 0.40330 -0.07610 -0.06630 0.07100  74  TYR A CG  
598  C CD1 . TYR A 74  ? 0.44660 0.42360 0.43850 -0.06760 -0.06190 0.07480  74  TYR A CD1 
599  C CD2 . TYR A 74  ? 0.42830 0.41200 0.39350 -0.07870 -0.07220 0.06750  74  TYR A CD2 
600  C CE1 . TYR A 74  ? 0.44410 0.42300 0.47550 -0.06420 -0.06170 0.07150  74  TYR A CE1 
601  C CE2 . TYR A 74  ? 0.42680 0.41460 0.42570 -0.07370 -0.07620 0.06160  74  TYR A CE2 
602  C CZ  . TYR A 74  ? 0.42700 0.41290 0.46480 -0.06780 -0.07040 0.06210  74  TYR A CZ  
603  O OH  . TYR A 74  ? 0.42460 0.41700 0.51700 -0.06530 -0.07080 0.04900  74  TYR A OH  
604  N N   . ARG A 75  ? 0.57570 0.51790 0.51860 -0.10360 -0.04710 0.05320  75  ARG A N   
605  C CA  . ARG A 75  ? 0.59060 0.52300 0.55230 -0.11050 -0.03660 0.04020  75  ARG A CA  
606  C C   . ARG A 75  ? 0.60350 0.50410 0.56020 -0.10360 -0.03540 0.05510  75  ARG A C   
607  O O   . ARG A 75  ? 0.61210 0.51300 0.58420 -0.10180 -0.03430 0.04540  75  ARG A O   
608  C CB  . ARG A 75  ? 0.60460 0.52580 0.58340 -0.12650 -0.01640 0.03060  75  ARG A CB  
609  C CG  . ARG A 75  ? 0.62420 0.53760 0.64390 -0.13790 0.00020  0.00770  75  ARG A CG  
610  C CD  . ARG A 75  ? 0.62630 0.53560 0.68490 -0.15660 0.02630  -0.00900 75  ARG A CD  
611  N NE  . ARG A 75  ? 0.62290 0.55350 0.66790 -0.15740 0.02120  -0.00620 75  ARG A NE  
612  C CZ  . ARG A 75  ? 0.64440 0.54750 0.67790 -0.16210 0.04390  0.01290  75  ARG A CZ  
613  N NH1 . ARG A 75  ? 0.67210 0.52230 0.70250 -0.16320 0.07760  0.03460  75  ARG A NH1 
614  N NH2 . ARG A 75  ? 0.61290 0.53960 0.63420 -0.16160 0.03640  0.01260  75  ARG A NH2 
615  N N   . GLU A 76  ? 0.51740 0.39420 0.45040 -0.09490 -0.03770 0.07640  76  GLU A N   
616  C CA  . GLU A 76  ? 0.53650 0.38750 0.46290 -0.08170 -0.04020 0.08980  76  GLU A CA  
617  C C   . GLU A 76  ? 0.51200 0.38270 0.45300 -0.07170 -0.05900 0.08710  76  GLU A C   
618  O O   . GLU A 76  ? 0.51870 0.37860 0.47180 -0.06540 -0.05890 0.08850  76  GLU A O   
619  C CB  . GLU A 76  ? 0.56390 0.38870 0.45280 -0.06520 -0.03970 0.11030  76  GLU A CB  
620  C CG  . GLU A 76  ? 0.59840 0.39530 0.47550 -0.04450 -0.04090 0.12500  76  GLU A CG  
621  C CD  . GLU A 76  ? 0.63080 0.39180 0.52330 -0.05270 -0.01010 0.12980  76  GLU A CD  
622  O OE1 . GLU A 76  ? 0.62400 0.37770 0.53530 -0.07290 0.01510  0.12160  76  GLU A OE1 
623  O OE2 . GLU A 76  ? 0.65090 0.39220 0.54580 -0.03880 -0.01000 0.13830  76  GLU A OE2 
624  N N   . ASN A 77  ? 0.46330 0.35950 0.41000 -0.06990 -0.07030 0.08340  77  ASN A N   
625  C CA  . ASN A 77  ? 0.45030 0.36160 0.42610 -0.06230 -0.07680 0.08050  77  ASN A CA  
626  C C   . ASN A 77  ? 0.44640 0.36210 0.43380 -0.06270 -0.06430 0.07620  77  ASN A C   
627  O O   . ASN A 77  ? 0.44680 0.36150 0.45670 -0.05430 -0.06220 0.07770  77  ASN A O   
628  C CB  . ASN A 77  ? 0.43250 0.36540 0.42230 -0.06220 -0.08020 0.07680  77  ASN A CB  
629  C CG  . ASN A 77  ? 0.44420 0.37930 0.43050 -0.05570 -0.09800 0.07270  77  ASN A CG  
630  O OD1 . ASN A 77  ? 0.45890 0.38610 0.44140 -0.04300 -0.11190 0.07190  77  ASN A OD1 
631  N ND2 . ASN A 77  ? 0.43370 0.38200 0.41790 -0.05980 -0.09900 0.06800  77  ASN A ND2 
632  N N   . LEU A 78  ? 0.43410 0.35770 0.40890 -0.06940 -0.05650 0.06680  78  LEU A N   
633  C CA  . LEU A 78  ? 0.46690 0.39960 0.44490 -0.06300 -0.04910 0.05550  78  LEU A CA  
634  C C   . LEU A 78  ? 0.47730 0.38700 0.46630 -0.06440 -0.04580 0.05320  78  LEU A C   
635  O O   . LEU A 78  ? 0.49550 0.40580 0.49270 -0.05390 -0.04110 0.05170  78  LEU A O   
636  C CB  . LEU A 78  ? 0.48140 0.43740 0.45100 -0.06630 -0.04850 0.03430  78  LEU A CB  
637  C CG  . LEU A 78  ? 0.48170 0.46680 0.43640 -0.05430 -0.05010 0.03470  78  LEU A CG  
638  C CD1 . LEU A 78  ? 0.46970 0.48320 0.42370 -0.05770 -0.05560 0.00750  78  LEU A CD1 
639  C CD2 . LEU A 78  ? 0.51440 0.50920 0.45700 -0.02770 -0.04120 0.04240  78  LEU A CD2 
640  N N   . ARG A 79  ? 0.47110 0.35610 0.45920 -0.07430 -0.04330 0.05600  79  ARG A N   
641  C CA  . ARG A 79  ? 0.48870 0.34500 0.48770 -0.07250 -0.03600 0.05860  79  ARG A CA  
642  C C   . ARG A 79  ? 0.47550 0.32450 0.47960 -0.05760 -0.04570 0.07400  79  ARG A C   
643  O O   . ARG A 79  ? 0.48340 0.32350 0.50340 -0.05130 -0.04150 0.07190  79  ARG A O   
644  C CB  . ARG A 79  ? 0.50670 0.33000 0.50070 -0.08020 -0.02210 0.06640  79  ARG A CB  
645  N N   . ILE A 80  ? 0.49780 0.35360 0.49540 -0.05100 -0.05960 0.08410  80  ILE A N   
646  C CA  . ILE A 80  ? 0.49260 0.35350 0.51190 -0.03610 -0.07300 0.08760  80  ILE A CA  
647  C C   . ILE A 80  ? 0.48110 0.35880 0.53360 -0.03490 -0.06450 0.08100  80  ILE A C   
648  O O   . ILE A 80  ? 0.48040 0.35330 0.55900 -0.02630 -0.06270 0.08040  80  ILE A O   
649  C CB  . ILE A 80  ? 0.49030 0.36580 0.50610 -0.02900 -0.09180 0.08730  80  ILE A CB  
650  C CG1 . ILE A 80  ? 0.52300 0.37650 0.49330 -0.01960 -0.09640 0.09890  80  ILE A CG1 
651  C CG2 . ILE A 80  ? 0.49320 0.38480 0.55100 -0.01410 -0.10820 0.07820  80  ILE A CG2 
652  C CD1 . ILE A 80  ? 0.52620 0.39740 0.48030 -0.00910 -0.11610 0.09430  80  ILE A CD1 
653  N N   . ALA A 81  ? 0.49470 0.38990 0.54470 -0.03940 -0.05510 0.07850  81  ALA A N   
654  C CA  . ALA A 81  ? 0.49710 0.40130 0.56810 -0.03070 -0.03720 0.07930  81  ALA A CA  
655  C C   . ALA A 81  ? 0.52880 0.42350 0.59280 -0.02510 -0.02660 0.07470  81  ALA A C   
656  O O   . ALA A 81  ? 0.53840 0.43160 0.62630 -0.01410 -0.01210 0.07770  81  ALA A O   
657  C CB  . ALA A 81  ? 0.50190 0.42150 0.55480 -0.02790 -0.02540 0.08210  81  ALA A CB  
658  N N   . LEU A 82  ? 0.51060 0.39820 0.55040 -0.03260 -0.03040 0.06450  82  LEU A N   
659  C CA  . LEU A 82  ? 0.55030 0.42990 0.59130 -0.02810 -0.02160 0.05260  82  LEU A CA  
660  C C   . LEU A 82  ? 0.52810 0.38790 0.59740 -0.02320 -0.02110 0.06040  82  LEU A C   
661  O O   . LEU A 82  ? 0.55310 0.41140 0.63460 -0.01290 -0.00910 0.05670  82  LEU A O   
662  C CB  . LEU A 82  ? 0.57170 0.44500 0.60440 -0.04120 -0.02310 0.03420  82  LEU A CB  
663  C CG  . LEU A 82  ? 0.61420 0.51650 0.63070 -0.04160 -0.02430 0.01000  82  LEU A CG  
664  C CD1 . LEU A 82  ? 0.60900 0.50440 0.64590 -0.05750 -0.02100 -0.01790 82  LEU A CD1 
665  C CD2 . LEU A 82  ? 0.67130 0.59820 0.66870 -0.01690 -0.01900 0.00070  82  LEU A CD2 
666  N N   . ARG A 83  ? 0.53530 0.38150 0.61200 -0.02550 -0.03440 0.07060  83  ARG A N   
667  C CA  . ARG A 83  ? 0.53470 0.36660 0.63710 -0.01450 -0.03840 0.07590  83  ARG A CA  
668  C C   . ARG A 83  ? 0.51640 0.36760 0.66110 -0.00520 -0.03850 0.07560  83  ARG A C   
669  O O   . ARG A 83  ? 0.51190 0.35920 0.68810 0.00370  -0.03130 0.07370  83  ARG A O   
670  C CB  . ARG A 83  ? 0.54440 0.35840 0.63190 -0.00820 -0.05360 0.08710  83  ARG A CB  
671  N N   . TYR A 84  ? 0.52430 0.39520 0.67980 -0.00800 -0.04230 0.07570  84  TYR A N   
672  C CA  . TYR A 84  ? 0.50820 0.39530 0.72360 -0.00200 -0.03430 0.07160  84  TYR A CA  
673  C C   . TYR A 84  ? 0.51450 0.39660 0.74210 0.00430  -0.00100 0.07580  84  TYR A C   
674  O O   . TYR A 84  ? 0.50450 0.38840 0.78770 0.01170  0.01150  0.07280  84  TYR A O   
675  C CB  . TYR A 84  ? 0.48950 0.39410 0.71890 -0.00770 -0.03540 0.06950  84  TYR A CB  
676  C CG  . TYR A 84  ? 0.49390 0.41100 0.72670 -0.00720 -0.06820 0.05930  84  TYR A CG  
677  C CD1 . TYR A 84  ? 0.51760 0.43100 0.74070 0.00510  -0.09460 0.05550  84  TYR A CD1 
678  C CD2 . TYR A 84  ? 0.49240 0.42480 0.73440 -0.01340 -0.07150 0.05360  84  TYR A CD2 
679  C CE1 . TYR A 84  ? 0.53160 0.45900 0.74480 0.01590  -0.12540 0.04570  84  TYR A CE1 
680  C CE2 . TYR A 84  ? 0.50820 0.45560 0.74900 -0.00840 -0.10260 0.03990  84  TYR A CE2 
681  C CZ  . TYR A 84  ? 0.52650 0.47270 0.74850 0.00840  -0.13040 0.03570  84  TYR A CZ  
682  O OH  . TYR A 84  ? 0.53040 0.49390 0.73820 0.02240  -0.16170 0.02170  84  TYR A OH  
683  N N   . TYR A 85  ? 0.40190 0.51140 0.69980 0.02270  0.00550  -0.01060 85  TYR A N   
684  C CA  . TYR A 85  ? 0.40060 0.51080 0.71010 0.00910  0.04640  -0.02660 85  TYR A CA  
685  C C   . TYR A 85  ? 0.42660 0.52180 0.74130 0.01620  0.05410  -0.03190 85  TYR A C   
686  O O   . TYR A 85  ? 0.42970 0.51590 0.74080 0.00560  0.08920  -0.04530 85  TYR A O   
687  C CB  . TYR A 85  ? 0.41950 0.50840 0.65990 -0.00930 0.06800  -0.01460 85  TYR A CB  
688  C CG  . TYR A 85  ? 0.39850 0.49980 0.63840 -0.01930 0.06970  -0.01410 85  TYR A CG  
689  C CD1 . TYR A 85  ? 0.37770 0.49070 0.65570 -0.03210 0.10020  -0.03470 85  TYR A CD1 
690  C CD2 . TYR A 85  ? 0.40190 0.50010 0.60500 -0.01750 0.04520  0.00490  85  TYR A CD2 
691  C CE1 . TYR A 85  ? 0.35750 0.47870 0.63680 -0.04250 0.10280  -0.03520 85  TYR A CE1 
692  C CE2 . TYR A 85  ? 0.38070 0.48830 0.58310 -0.02600 0.04600  0.00420  85  TYR A CE2 
693  C CZ  . TYR A 85  ? 0.35900 0.47770 0.59880 -0.03820 0.07300  -0.01500 85  TYR A CZ  
694  O OH  . TYR A 85  ? 0.34170 0.46660 0.58130 -0.04760 0.07380  -0.01590 85  TYR A OH  
695  N N   . ASN A 86  ? 0.50950 0.59400 0.82530 0.03370  0.02400  -0.02190 86  ASN A N   
696  C CA  . ASN A 86  ? 0.52450 0.59400 0.85310 0.04230  0.02860  -0.02870 86  ASN A CA  
697  C C   . ASN A 86  ? 0.55150 0.59590 0.82450 0.02770  0.05530  -0.02430 86  ASN A C   
698  O O   . ASN A 86  ? 0.55950 0.59750 0.84350 0.02430  0.08120  -0.04170 86  ASN A O   
699  C CB  . ASN A 86  ? 0.49550 0.59090 0.91010 0.05000  0.04020  -0.06040 86  ASN A CB  
700  C CG  . ASN A 86  ? 0.51100 0.59660 0.96150 0.07290  0.01630  -0.06570 86  ASN A CG  
701  O OD1 . ASN A 86  ? 0.54140 0.59470 0.94540 0.08190  -0.00720 -0.04330 86  ASN A OD1 
702  N ND2 . ASN A 86  ? 0.49160 0.60190 1.02810 0.08210  0.02440  -0.09720 86  ASN A ND2 
703  N N   . GLN A 87  ? 0.48420 0.51250 0.69780 0.01990  0.04740  -0.00380 87  GLN A N   
704  C CA  . GLN A 87  ? 0.51200 0.51600 0.67330 0.00890  0.06100  -0.00120 87  GLN A CA  
705  C C   . GLN A 87  ? 0.52820 0.51140 0.67330 0.01370  0.04520  0.01000  87  GLN A C   
706  O O   . GLN A 87  ? 0.52240 0.50270 0.67300 0.02110  0.02610  0.02390  87  GLN A O   
707  C CB  . GLN A 87  ? 0.50760 0.50990 0.62540 -0.00300 0.06230  0.00800  87  GLN A CB  
708  C CG  . GLN A 87  ? 0.48980 0.50260 0.61500 -0.01160 0.08370  -0.00260 87  GLN A CG  
709  C CD  . GLN A 87  ? 0.47930 0.48880 0.56540 -0.02060 0.07990  0.00840  87  GLN A CD  
710  O OE1 . GLN A 87  ? 0.47080 0.48490 0.54470 -0.01820 0.05780  0.02330  87  GLN A OE1 
711  N NE2 . GLN A 87  ? 0.48010 0.47720 0.54610 -0.03170 0.10510  -0.00000 87  GLN A NE2 
712  N N   . SER A 88  ? 0.62480 0.58710 0.74450 0.00860  0.05440  0.00270  88  SER A N   
713  C CA  A SER A 88  ? 0.63910 0.58150 0.75350 0.01030  0.04430  0.00740  88  SER A CA  
714  C CA  B SER A 88  ? 0.63920 0.58160 0.75350 0.01020  0.04430  0.00740  88  SER A CA  
715  C C   . SER A 88  ? 0.61640 0.55690 0.71110 0.00330  0.03210  0.02250  88  SER A C   
716  O O   . SER A 88  ? 0.60670 0.55770 0.68230 -0.00300 0.03050  0.02610  88  SER A O   
717  C CB  A SER A 88  ? 0.66770 0.58850 0.76200 0.00660  0.05410  -0.00930 88  SER A CB  
718  C CB  B SER A 88  ? 0.66790 0.58860 0.76150 0.00650  0.05370  -0.00910 88  SER A CB  
719  O OG  A SER A 88  ? 0.67350 0.57700 0.77300 0.00680  0.04500  -0.00860 88  SER A OG  
720  O OG  B SER A 88  ? 0.67290 0.57920 0.75770 0.00230  0.04170  -0.00640 88  SER A OG  
721  N N   . GLU A 89  ? 0.59580 0.51910 0.69680 0.00370  0.02690  0.02970  89  GLU A N   
722  C CA  . GLU A 89  ? 0.57750 0.49640 0.66780 -0.00590 0.02400  0.03920  89  GLU A CA  
723  C C   . GLU A 89  ? 0.58980 0.50700 0.67840 -0.01490 0.02290  0.02430  89  GLU A C   
724  O O   . GLU A 89  ? 0.58230 0.50120 0.67690 -0.02370 0.02200  0.02540  89  GLU A O   
725  C CB  . GLU A 89  ? 0.59460 0.48550 0.68690 -0.00480 0.02550  0.05240  89  GLU A CB  
726  N N   . ALA A 90  ? 0.52940 0.44100 0.60950 -0.01220 0.02210  0.00760  90  ALA A N   
727  C CA  . ALA A 90  ? 0.54620 0.44860 0.61820 -0.01630 0.01170  -0.01020 90  ALA A CA  
728  C C   . ALA A 90  ? 0.57430 0.47920 0.61180 -0.01590 0.00160  -0.01460 90  ALA A C   
729  O O   . ALA A 90  ? 0.57050 0.46820 0.60350 -0.01660 -0.01630 -0.02850 90  ALA A O   
730  C CB  . ALA A 90  ? 0.57540 0.45580 0.64140 -0.01190 0.01330  -0.02740 90  ALA A CB  
731  N N   . GLY A 91  ? 0.52420 0.43570 0.53940 -0.01400 0.01070  -0.00520 91  GLY A N   
732  C CA  . GLY A 91  ? 0.53480 0.43710 0.50810 -0.01400 0.00420  -0.00790 91  GLY A CA  
733  C C   . GLY A 91  ? 0.50330 0.42560 0.48760 -0.01720 -0.00590 0.00180  91  GLY A C   
734  O O   . GLY A 91  ? 0.46040 0.40360 0.47900 -0.02060 -0.00190 0.01270  91  GLY A O   
735  N N   . SER A 92  ? 0.54990 0.45720 0.49670 -0.01510 -0.01880 -0.00300 92  SER A N   
736  C CA  A SER A 92  ? 0.51150 0.43380 0.46660 -0.01630 -0.03060 0.00180  92  SER A CA  
737  C CA  B SER A 92  ? 0.51170 0.43400 0.46670 -0.01630 -0.03060 0.00180  92  SER A CA  
738  C C   . SER A 92  ? 0.48740 0.41110 0.41550 -0.01830 -0.01820 0.01460  92  SER A C   
739  O O   . SER A 92  ? 0.50880 0.40390 0.38950 -0.01760 -0.00990 0.01260  92  SER A O   
740  C CB  A SER A 92  ? 0.51230 0.41360 0.44970 -0.00940 -0.06070 -0.01520 92  SER A CB  
741  C CB  B SER A 92  ? 0.51260 0.41390 0.45000 -0.00940 -0.06070 -0.01520 92  SER A CB  
742  O OG  A SER A 92  ? 0.48460 0.39280 0.41870 -0.00790 -0.07150 -0.01150 92  SER A OG  
743  O OG  B SER A 92  ? 0.50810 0.41380 0.48590 -0.00890 -0.07360 -0.03190 92  SER A OG  
744  N N   . HIS A 93  ? 0.48090 0.43270 0.43630 -0.02220 -0.01430 0.02600  93  HIS A N   
745  C CA  . HIS A 93  ? 0.44990 0.40810 0.39150 -0.02500 -0.00380 0.03590  93  HIS A CA  
746  C C   . HIS A 93  ? 0.41890 0.38910 0.36580 -0.02600 -0.01450 0.03970  93  HIS A C   
747  O O   . HIS A 93  ? 0.41220 0.39280 0.38510 -0.02580 -0.02460 0.03520  93  HIS A O   
748  C CB  . HIS A 93  ? 0.42950 0.40930 0.40070 -0.02650 0.01090  0.04400  93  HIS A CB  
749  C CG  . HIS A 93  ? 0.46980 0.44070 0.44550 -0.02430 0.02250  0.03720  93  HIS A CG  
750  N ND1 . HIS A 93  ? 0.48660 0.44710 0.44850 -0.02670 0.04100  0.03080  93  HIS A ND1 
751  C CD2 . HIS A 93  ? 0.49100 0.45830 0.48410 -0.02090 0.02160  0.03330  93  HIS A CD2 
752  C CE1 . HIS A 93  ? 0.52260 0.47680 0.49620 -0.02390 0.05080  0.02240  93  HIS A CE1 
753  N NE2 . HIS A 93  ? 0.52450 0.48240 0.51600 -0.01950 0.03700  0.02460  93  HIS A NE2 
754  N N   . ILE A 94  ? 0.47530 0.44370 0.40290 -0.02850 -0.00880 0.04550  94  ILE A N   
755  C CA  . ILE A 94  ? 0.45380 0.42900 0.38200 -0.02870 -0.01850 0.04760  94  ILE A CA  
756  C C   . ILE A 94  ? 0.42400 0.41610 0.35890 -0.03400 -0.00670 0.05660  94  ILE A C   
757  O O   . ILE A 94  ? 0.43520 0.41860 0.35610 -0.03780 0.00630  0.05710  94  ILE A O   
758  C CB  . ILE A 94  ? 0.48320 0.42290 0.36800 -0.02320 -0.03390 0.04100  94  ILE A CB  
759  C CG1 . ILE A 94  ? 0.50730 0.43190 0.39250 -0.01470 -0.05630 0.02700  94  ILE A CG1 
760  C CG2 . ILE A 94  ? 0.46140 0.40730 0.34880 -0.02280 -0.04200 0.04300  94  ILE A CG2 
761  C CD1 . ILE A 94  ? 0.54090 0.41850 0.37320 -0.00380 -0.08190 0.01840  94  ILE A CD1 
762  N N   . ILE A 95  ? 0.36760 0.38070 0.32430 -0.03510 -0.00950 0.06090  95  ILE A N   
763  C CA  . ILE A 95  ? 0.34380 0.36820 0.30130 -0.03830 -0.00640 0.06590  95  ILE A CA  
764  C C   . ILE A 95  ? 0.34070 0.35830 0.28590 -0.03830 -0.01420 0.06290  95  ILE A C   
765  O O   . ILE A 95  ? 0.34830 0.36740 0.30420 -0.03550 -0.02230 0.05730  95  ILE A O   
766  C CB  . ILE A 95  ? 0.33210 0.37170 0.30580 -0.03780 -0.00580 0.07220  95  ILE A CB  
767  C CG1 . ILE A 95  ? 0.34940 0.39220 0.33570 -0.03440 -0.00360 0.07430  95  ILE A CG1 
768  C CG2 . ILE A 95  ? 0.31950 0.36680 0.28880 -0.03960 -0.00870 0.07410  95  ILE A CG2 
769  C CD1 . ILE A 95  ? 0.35840 0.39910 0.34490 -0.02980 -0.00880 0.08200  95  ILE A CD1 
770  N N   . GLN A 96  ? 0.37900 0.39000 0.30950 -0.04180 -0.01070 0.06400  96  GLN A N   
771  C CA  . GLN A 96  ? 0.37900 0.38120 0.29820 -0.04080 -0.01870 0.06160  96  GLN A CA  
772  C C   . GLN A 96  ? 0.36590 0.38400 0.29500 -0.04600 -0.01400 0.06370  96  GLN A C   
773  O O   . GLN A 96  ? 0.36900 0.39650 0.30780 -0.05060 -0.00620 0.06480  96  GLN A O   
774  C CB  . GLN A 96  ? 0.41510 0.37730 0.29330 -0.03930 -0.02150 0.06000  96  GLN A CB  
775  C CG  . GLN A 96  ? 0.44240 0.38070 0.30280 -0.02940 -0.03830 0.05400  96  GLN A CG  
776  C CD  . GLN A 96  ? 0.48680 0.37050 0.28560 -0.02790 -0.03720 0.05490  96  GLN A CD  
777  O OE1 . GLN A 96  ? 0.49930 0.37080 0.28140 -0.03240 -0.02130 0.05620  96  GLN A OE1 
778  N NE2 . GLN A 96  ? 0.51530 0.35830 0.27380 -0.02100 -0.05280 0.05370  96  GLN A NE2 
779  N N   . VAL A 97  ? 0.34420 0.36600 0.27620 -0.04450 -0.02030 0.06080  97  VAL A N   
780  C CA  . VAL A 97  ? 0.34430 0.37790 0.28090 -0.04830 -0.01860 0.06050  97  VAL A CA  
781  C C   . VAL A 97  ? 0.36090 0.38100 0.28820 -0.04730 -0.02370 0.05530  97  VAL A C   
782  O O   . VAL A 97  ? 0.37340 0.38680 0.30420 -0.04100 -0.03150 0.04970  97  VAL A O   
783  C CB  . VAL A 97  ? 0.33790 0.38480 0.28120 -0.04730 -0.01700 0.06160  97  VAL A CB  
784  C CG1 . VAL A 97  ? 0.34780 0.39800 0.28330 -0.04950 -0.01980 0.05990  97  VAL A CG1 
785  C CG2 . VAL A 97  ? 0.32950 0.38010 0.27680 -0.04570 -0.01460 0.06790  97  VAL A CG2 
786  N N   . MET A 98  ? 0.38220 0.39860 0.30450 -0.05300 -0.02110 0.05420  98  MET A N   
787  C CA  . MET A 98  ? 0.40770 0.40950 0.32130 -0.05240 -0.02550 0.04910  98  MET A CA  
788  C C   . MET A 98  ? 0.41230 0.42980 0.33510 -0.05730 -0.02430 0.04480  98  MET A C   
789  O O   . MET A 98  ? 0.41360 0.44340 0.34650 -0.06250 -0.02240 0.04470  98  MET A O   
790  C CB  . MET A 98  ? 0.44020 0.40460 0.32640 -0.05550 -0.02230 0.05130  98  MET A CB  
791  C CG  . MET A 98  ? 0.47880 0.42060 0.35260 -0.05560 -0.02640 0.04690  98  MET A CG  
792  S SD  . MET A 98  ? 0.49820 0.45240 0.38920 -0.06990 -0.01470 0.04150  98  MET A SD  
793  C CE  . MET A 98  ? 0.52420 0.43320 0.38820 -0.08250 0.00610  0.04530  98  MET A CE  
794  N N   . TYR A 99  ? 0.35510 0.37190 0.27760 -0.05440 -0.02760 0.03810  99  TYR A N   
795  C CA  . TYR A 99  ? 0.37380 0.39490 0.29530 -0.05880 -0.02860 0.03150  99  TYR A CA  
796  C C   . TYR A 99  ? 0.39800 0.40580 0.31730 -0.05580 -0.03050 0.02280  99  TYR A C   
797  O O   . TYR A 99  ? 0.39900 0.39970 0.32420 -0.04820 -0.03310 0.01980  99  TYR A O   
798  C CB  . TYR A 99  ? 0.36210 0.39630 0.27700 -0.05760 -0.02940 0.03100  99  TYR A CB  
799  C CG  . TYR A 99  ? 0.35840 0.39170 0.26800 -0.05380 -0.02000 0.03010  99  TYR A CG  
800  C CD1 . TYR A 99  ? 0.38980 0.41690 0.29420 -0.05360 -0.01250 0.01950  99  TYR A CD1 
801  C CD2 . TYR A 99  ? 0.33980 0.37720 0.25380 -0.05220 -0.01440 0.03700  99  TYR A CD2 
802  C CE1 . TYR A 99  ? 0.40210 0.42820 0.31040 -0.05350 0.00440  0.01430  99  TYR A CE1 
803  C CE2 . TYR A 99  ? 0.35560 0.39110 0.27260 -0.05230 0.00030  0.03300  99  TYR A CE2 
804  C CZ  . TYR A 99  ? 0.38440 0.41480 0.30090 -0.05380 0.01180  0.02090  99  TYR A CZ  
805  O OH  . TYR A 99  ? 0.40480 0.43340 0.33360 -0.05690 0.03400  0.01290  99  TYR A OH  
806  N N   . GLY A 100 ? 0.37280 0.37800 0.28930 -0.06040 -0.03190 0.01550  100 GLY A N   
807  C CA  . GLY A 100 ? 0.39920 0.39210 0.31520 -0.05720 -0.03300 0.00500  100 GLY A CA  
808  C C   . GLY A 100 ? 0.42570 0.40760 0.33930 -0.06480 -0.03540 -0.00150 100 GLY A C   
809  O O   . GLY A 100 ? 0.42330 0.41310 0.34300 -0.07310 -0.03630 -0.00130 100 GLY A O   
810  N N   . CYS A 101 ? 0.46540 0.43050 0.37810 -0.06140 -0.03710 -0.01080 101 CYS A N   
811  C CA  . CYS A 101 ? 0.48670 0.44020 0.39880 -0.06850 -0.03860 -0.02080 101 CYS A CA  
812  C C   . CYS A 101 ? 0.52930 0.44570 0.43570 -0.06570 -0.04030 -0.02160 101 CYS A C   
813  O O   . CYS A 101 ? 0.54260 0.44520 0.44670 -0.05340 -0.04620 -0.01970 101 CYS A O   
814  C CB  . CYS A 101 ? 0.48790 0.45140 0.39450 -0.06640 -0.03910 -0.03520 101 CYS A CB  
815  S SG  . CYS A 101 ? 0.49600 0.46340 0.40600 -0.05480 -0.02920 -0.04280 101 CYS A SG  
816  N N   . ASP A 102 ? 0.52730 0.42410 0.43270 -0.07660 -0.03710 -0.02610 102 ASP A N   
817  C CA  . ASP A 102 ? 0.57690 0.42700 0.46810 -0.07530 -0.03780 -0.02750 102 ASP A CA  
818  C C   . ASP A 102 ? 0.57970 0.43100 0.48190 -0.07760 -0.04020 -0.04540 102 ASP A C   
819  O O   . ASP A 102 ? 0.55920 0.43220 0.47540 -0.08870 -0.03870 -0.05510 102 ASP A O   
820  C CB  . ASP A 102 ? 0.59780 0.41000 0.47350 -0.09020 -0.02390 -0.01860 102 ASP A CB  
821  C CG  . ASP A 102 ? 0.59250 0.39940 0.45180 -0.09110 -0.01670 -0.00280 102 ASP A CG  
822  O OD1 . ASP A 102 ? 0.58990 0.40640 0.44140 -0.07630 -0.02810 0.00370  102 ASP A OD1 
823  O OD2 . ASP A 102 ? 0.59000 0.38050 0.44700 -0.10800 0.00330  0.00040  102 ASP A OD2 
824  N N   . VAL A 103 ? 0.55030 0.37580 0.44800 -0.06570 -0.04710 -0.05230 103 VAL A N   
825  C CA  . VAL A 103 ? 0.56750 0.38820 0.47370 -0.06780 -0.04790 -0.07080 103 VAL A CA  
826  C C   . VAL A 103 ? 0.61570 0.37880 0.50770 -0.06660 -0.05030 -0.07050 103 VAL A C   
827  O O   . VAL A 103 ? 0.64160 0.36530 0.51150 -0.05620 -0.05710 -0.05810 103 VAL A O   
828  C CB  . VAL A 103 ? 0.55630 0.40140 0.47500 -0.05490 -0.04950 -0.08630 103 VAL A CB  
829  C CG1 . VAL A 103 ? 0.52620 0.41260 0.44350 -0.05770 -0.04340 -0.08460 103 VAL A CG1 
830  C CG2 . VAL A 103 ? 0.56400 0.39360 0.49380 -0.03570 -0.05800 -0.08740 103 VAL A CG2 
831  N N   . GLY A 104 ? 0.76430 0.51540 0.66300 -0.07660 -0.04680 -0.08480 104 GLY A N   
832  C CA  . GLY A 104 ? 0.80410 0.49450 0.68700 -0.07660 -0.04720 -0.08580 104 GLY A CA  
833  C C   . GLY A 104 ? 0.83100 0.50830 0.72020 -0.05540 -0.06120 -0.09930 104 GLY A C   
834  O O   . GLY A 104 ? 0.79220 0.50880 0.70190 -0.04190 -0.06610 -0.10830 104 GLY A O   
835  N N   . PRO A 105 ? 0.93640 0.55490 0.81110 -0.05270 -0.06510 -0.10270 105 PRO A N   
836  C CA  . PRO A 105 ? 0.94150 0.54460 0.83010 -0.02990 -0.08080 -0.11910 105 PRO A CA  
837  C C   . PRO A 105 ? 0.91740 0.56970 0.84080 -0.03010 -0.07460 -0.14540 105 PRO A C   
838  O O   . PRO A 105 ? 0.90520 0.56940 0.85440 -0.01100 -0.08120 -0.16190 105 PRO A O   
839  C CB  . PRO A 105 ? 0.99740 0.52060 0.85650 -0.03200 -0.08320 -0.11620 105 PRO A CB  
840  C CG  . PRO A 105 ? 1.02270 0.50660 0.83980 -0.04970 -0.06970 -0.09150 105 PRO A CG  
841  C CD  . PRO A 105 ? 0.98060 0.53510 0.82330 -0.06900 -0.05370 -0.09090 105 PRO A CD  
842  N N   . ASP A 106 ? 0.95180 0.62910 0.87650 -0.05060 -0.06250 -0.15280 106 ASP A N   
843  C CA  . ASP A 106 ? 0.92720 0.64130 0.86500 -0.05090 -0.05690 -0.17660 106 ASP A CA  
844  C C   . ASP A 106 ? 0.89700 0.66080 0.83590 -0.04760 -0.05040 -0.17400 106 ASP A C   
845  O O   . ASP A 106 ? 0.88930 0.67390 0.82360 -0.04800 -0.04160 -0.19200 106 ASP A O   
846  C CB  . ASP A 106 ? 0.93580 0.65060 0.86910 -0.07130 -0.05440 -0.18800 106 ASP A CB  
847  C CG  . ASP A 106 ? 0.92610 0.65730 0.85820 -0.08860 -0.05300 -0.17240 106 ASP A CG  
848  O OD1 . ASP A 106 ? 0.90150 0.64370 0.82860 -0.08520 -0.05120 -0.15110 106 ASP A OD1 
849  O OD2 . ASP A 106 ? 0.92000 0.65400 0.86240 -0.10530 -0.05420 -0.18480 106 ASP A OD2 
850  N N   . GLY A 107 ? 0.75720 0.53290 0.69480 -0.04500 -0.05260 -0.15260 107 GLY A N   
851  C CA  . GLY A 107 ? 0.72880 0.54590 0.66700 -0.04310 -0.04470 -0.14910 107 GLY A CA  
852  C C   . GLY A 107 ? 0.71320 0.55380 0.63110 -0.05800 -0.04230 -0.14370 107 GLY A C   
853  O O   . GLY A 107 ? 0.69200 0.55860 0.60030 -0.05670 -0.03550 -0.13980 107 GLY A O   
854  N N   . ARG A 108 ? 0.68910 0.51890 0.60360 -0.07160 -0.04870 -0.14500 108 ARG A N   
855  C CA  . ARG A 108 ? 0.67470 0.52770 0.58100 -0.08250 -0.05430 -0.14490 108 ARG A CA  
856  C C   . ARG A 108 ? 0.64920 0.51460 0.56560 -0.08840 -0.05420 -0.12310 108 ARG A C   
857  O O   . ARG A 108 ? 0.66220 0.50650 0.58500 -0.08950 -0.04910 -0.10970 108 ARG A O   
858  C CB  . ARG A 108 ? 0.68410 0.52570 0.59780 -0.09440 -0.06340 -0.16410 108 ARG A CB  
859  C CG  . ARG A 108 ? 0.71540 0.54420 0.61050 -0.08930 -0.06490 -0.18910 108 ARG A CG  
860  C CD  . ARG A 108 ? 0.73370 0.54620 0.64470 -0.10150 -0.07520 -0.20940 108 ARG A CD  
861  N NE  . ARG A 108 ? 0.76920 0.57030 0.65550 -0.09810 -0.08160 -0.23630 108 ARG A NE  
862  C CZ  . ARG A 108 ? 0.77560 0.57960 0.65280 -0.10380 -0.10210 -0.25630 108 ARG A CZ  
863  N NH1 . ARG A 108 ? 0.76040 0.58540 0.66320 -0.11270 -0.11890 -0.25480 108 ARG A NH1 
864  N NH2 . ARG A 108 ? 0.82360 0.60770 0.66780 -0.09960 -0.10750 -0.28150 108 ARG A NH2 
865  N N   . LEU A 109 ? 0.57940 0.47230 0.49080 -0.09090 -0.06050 -0.12060 109 LEU A N   
866  C CA  . LEU A 109 ? 0.56150 0.47040 0.48520 -0.09510 -0.05910 -0.10280 109 LEU A CA  
867  C C   . LEU A 109 ? 0.56460 0.46220 0.51760 -0.11100 -0.05450 -0.10350 109 LEU A C   
868  O O   . LEU A 109 ? 0.56510 0.46270 0.53920 -0.12140 -0.06080 -0.12230 109 LEU A O   
869  C CB  . LEU A 109 ? 0.53520 0.47090 0.44850 -0.09260 -0.07120 -0.10410 109 LEU A CB  
870  C CG  . LEU A 109 ? 0.50980 0.46490 0.44370 -0.09670 -0.07100 -0.08980 109 LEU A CG  
871  C CD1 . LEU A 109 ? 0.50470 0.45910 0.42710 -0.08940 -0.05800 -0.06930 109 LEU A CD1 
872  C CD2 . LEU A 109 ? 0.50960 0.48490 0.43900 -0.09300 -0.09090 -0.09570 109 LEU A CD2 
873  N N   . LEU A 110 ? 0.55510 0.43880 0.50820 -0.11390 -0.04130 -0.08520 110 LEU A N   
874  C CA  . LEU A 110 ? 0.56290 0.42880 0.53680 -0.13200 -0.02600 -0.08410 110 LEU A CA  
875  C C   . LEU A 110 ? 0.53220 0.42940 0.53050 -0.13850 -0.02200 -0.07950 110 LEU A C   
876  O O   . LEU A 110 ? 0.53270 0.44220 0.57450 -0.15450 -0.01620 -0.09400 110 LEU A O   
877  C CB  . LEU A 110 ? 0.60050 0.41060 0.54180 -0.13140 -0.01110 -0.06750 110 LEU A CB  
878  C CG  . LEU A 110 ? 0.64040 0.40570 0.56320 -0.12690 -0.01360 -0.07320 110 LEU A CG  
879  C CD1 . LEU A 110 ? 0.68260 0.38530 0.56000 -0.12010 -0.00720 -0.05350 110 LEU A CD1 
880  C CD2 . LEU A 110 ? 0.65510 0.40810 0.60510 -0.14610 -0.00550 -0.09270 110 LEU A CD2 
881  N N   . ARG A 111 ? 0.64320 0.55370 0.62200 -0.12670 -0.02410 -0.06240 111 ARG A N   
882  C CA  . ARG A 111 ? 0.61240 0.55840 0.61470 -0.12810 -0.02640 -0.06060 111 ARG A CA  
883  C C   . ARG A 111 ? 0.59670 0.55610 0.57100 -0.11180 -0.03350 -0.04450 111 ARG A C   
884  O O   . ARG A 111 ? 0.61430 0.55550 0.55940 -0.10160 -0.03230 -0.03460 111 ARG A O   
885  C CB  . ARG A 111 ? 0.61180 0.54640 0.63650 -0.14450 -0.00170 -0.05740 111 ARG A CB  
886  C CG  . ARG A 111 ? 0.64370 0.52660 0.62470 -0.14640 0.01980  -0.03840 111 ARG A CG  
887  C CD  . ARG A 111 ? 0.63310 0.50450 0.63270 -0.16500 0.05030  -0.03820 111 ARG A CD  
888  N NE  . ARG A 111 ? 0.59950 0.52060 0.63130 -0.16000 0.04260  -0.03960 111 ARG A NE  
889  C CZ  . ARG A 111 ? 0.57350 0.50220 0.63480 -0.17210 0.06510  -0.04320 111 ARG A CZ  
890  N NH1 . ARG A 111 ? 0.58130 0.46940 0.64330 -0.19360 0.10370  -0.04650 111 ARG A NH1 
891  N NH2 . ARG A 111 ? 0.54420 0.51730 0.63300 -0.16280 0.05170  -0.04430 111 ARG A NH2 
892  N N   . GLY A 112 ? 0.43540 0.42630 0.42540 -0.10900 -0.04250 -0.04480 112 GLY A N   
893  C CA  . GLY A 112 ? 0.41820 0.42120 0.38670 -0.09650 -0.04640 -0.03050 112 GLY A CA  
894  C C   . GLY A 112 ? 0.40520 0.41370 0.38760 -0.10040 -0.03470 -0.01970 112 GLY A C   
895  O O   . GLY A 112 ? 0.40340 0.41450 0.41900 -0.11300 -0.02440 -0.02740 112 GLY A O   
896  N N   . HIS A 113 ? 0.40870 0.41830 0.37040 -0.09100 -0.03310 -0.00510 113 HIS A N   
897  C CA  . HIS A 113 ? 0.40060 0.41100 0.36870 -0.09340 -0.02180 0.00460  113 HIS A CA  
898  C C   . HIS A 113 ? 0.37890 0.40910 0.34120 -0.08260 -0.03060 0.01250  113 HIS A C   
899  O O   . HIS A 113 ? 0.37100 0.40110 0.31230 -0.07390 -0.03680 0.01550  113 HIS A O   
900  C CB  . HIS A 113 ? 0.42020 0.39310 0.35830 -0.09360 -0.00910 0.01560  113 HIS A CB  
901  C CG  . HIS A 113 ? 0.45740 0.39370 0.38450 -0.10280 0.00070  0.01140  113 HIS A CG  
902  N ND1 . HIS A 113 ? 0.46990 0.37690 0.39450 -0.11790 0.02390  0.01150  113 HIS A ND1 
903  C CD2 . HIS A 113 ? 0.48470 0.40260 0.39960 -0.09980 -0.00640 0.00660  113 HIS A CD2 
904  C CE1 . HIS A 113 ? 0.50450 0.37230 0.41130 -0.12430 0.03050  0.00870  113 HIS A CE1 
905  N NE2 . HIS A 113 ? 0.52280 0.39860 0.42580 -0.11230 0.00980  0.00550  113 HIS A NE2 
906  N N   . ASN A 114 ? 0.41430 0.45860 0.39740 -0.08420 -0.02750 0.01410  114 ASN A N   
907  C CA  . ASN A 114 ? 0.39490 0.44990 0.37000 -0.07470 -0.03270 0.02360  114 ASN A CA  
908  C C   . ASN A 114 ? 0.38750 0.44960 0.38770 -0.07910 -0.02200 0.02410  114 ASN A C   
909  O O   . ASN A 114 ? 0.37930 0.45910 0.41980 -0.08340 -0.02420 0.01150  114 ASN A O   
910  C CB  . ASN A 114 ? 0.38840 0.45470 0.35780 -0.06620 -0.05240 0.01990  114 ASN A CB  
911  C CG  . ASN A 114 ? 0.37580 0.44180 0.32780 -0.05720 -0.05440 0.03150  114 ASN A CG  
912  O OD1 . ASN A 114 ? 0.36750 0.42750 0.30930 -0.05670 -0.04200 0.04090  114 ASN A OD1 
913  N ND2 . ASN A 114 ? 0.37960 0.44770 0.32790 -0.04930 -0.07240 0.02930  114 ASN A ND2 
914  N N   . GLN A 115 ? 0.42910 0.47680 0.40980 -0.07760 -0.01080 0.03480  115 GLN A N   
915  C CA  . GLN A 115 ? 0.41690 0.46320 0.41140 -0.08230 0.00450  0.03480  115 GLN A CA  
916  C C   . GLN A 115 ? 0.40070 0.44760 0.37990 -0.07270 0.00050  0.04510  115 GLN A C   
917  O O   . GLN A 115 ? 0.39050 0.42950 0.34540 -0.06580 -0.00730 0.05200  115 GLN A O   
918  C CB  . GLN A 115 ? 0.43320 0.44240 0.40480 -0.09350 0.02750  0.03550  115 GLN A CB  
919  C CG  . GLN A 115 ? 0.46030 0.46040 0.44400 -0.10550 0.03600  0.02560  115 GLN A CG  
920  C CD  . GLN A 115 ? 0.49340 0.44200 0.44220 -0.11820 0.06450  0.02800  115 GLN A CD  
921  O OE1 . GLN A 115 ? 0.51970 0.44210 0.45780 -0.12730 0.07330  0.02460  115 GLN A OE1 
922  N NE2 . GLN A 115 ? 0.49080 0.41630 0.41370 -0.11890 0.08040  0.03390  115 GLN A NE2 
923  N N   . TYR A 116 ? 0.36590 0.42350 0.36740 -0.07290 0.00720  0.04280  116 TYR A N   
924  C CA  . TYR A 116 ? 0.35810 0.41590 0.35050 -0.06470 0.00440  0.05060  116 TYR A CA  
925  C C   . TYR A 116 ? 0.35980 0.40240 0.35020 -0.07020 0.02490  0.04840  116 TYR A C   
926  O O   . TYR A 116 ? 0.37130 0.41490 0.38560 -0.08000 0.04310  0.03800  116 TYR A O   
927  C CB  . TYR A 116 ? 0.36090 0.44130 0.37670 -0.05560 -0.01150 0.05010  116 TYR A CB  
928  C CG  . TYR A 116 ? 0.36740 0.45070 0.37050 -0.05050 -0.02930 0.05150  116 TYR A CG  
929  C CD1 . TYR A 116 ? 0.36790 0.46000 0.38710 -0.05310 -0.03840 0.04090  116 TYR A CD1 
930  C CD2 . TYR A 116 ? 0.35430 0.42710 0.32780 -0.04450 -0.03400 0.06110  116 TYR A CD2 
931  C CE1 . TYR A 116 ? 0.37270 0.45950 0.36880 -0.04780 -0.05480 0.04100  116 TYR A CE1 
932  C CE2 . TYR A 116 ? 0.35280 0.41780 0.30250 -0.04130 -0.04400 0.06170  116 TYR A CE2 
933  C CZ  . TYR A 116 ? 0.36910 0.43940 0.32530 -0.04210 -0.05570 0.05210  116 TYR A CZ  
934  O OH  . TYR A 116 ? 0.38180 0.43720 0.30410 -0.03820 -0.06610 0.05140  116 TYR A OH  
935  N N   . ALA A 117 ? 0.34970 0.37710 0.31390 -0.06440 0.02380  0.05520  117 ALA A N   
936  C CA  . ALA A 117 ? 0.37250 0.37750 0.32160 -0.06780 0.04200  0.05290  117 ALA A CA  
937  C C   . ALA A 117 ? 0.36690 0.38290 0.32580 -0.05900 0.03450  0.05520  117 ALA A C   
938  O O   . ALA A 117 ? 0.34120 0.36710 0.30050 -0.05140 0.01710  0.06110  117 ALA A O   
939  C CB  . ALA A 117 ? 0.39010 0.34730 0.27990 -0.06860 0.04500  0.05700  117 ALA A CB  
940  N N   . TYR A 118 ? 0.36550 0.37560 0.33250 -0.06170 0.05190  0.04880  118 TYR A N   
941  C CA  . TYR A 118 ? 0.37200 0.38300 0.34140 -0.05410 0.04740  0.04970  118 TYR A CA  
942  C C   . TYR A 118 ? 0.40220 0.37260 0.32810 -0.05780 0.06520  0.04550  118 TYR A C   
943  O O   . TYR A 118 ? 0.41810 0.37190 0.33930 -0.06780 0.09330  0.03740  118 TYR A O   
944  C CB  . TYR A 118 ? 0.37460 0.41640 0.39790 -0.04960 0.04660  0.04380  118 TYR A CB  
945  C CG  . TYR A 118 ? 0.38510 0.42430 0.41060 -0.04120 0.04120  0.04570  118 TYR A CG  
946  C CD1 . TYR A 118 ? 0.37260 0.40730 0.38130 -0.03560 0.02450  0.05540  118 TYR A CD1 
947  C CD2 . TYR A 118 ? 0.40490 0.44560 0.45540 -0.04030 0.05590  0.03500  118 TYR A CD2 
948  C CE1 . TYR A 118 ? 0.38950 0.41880 0.40330 -0.03000 0.02180  0.05580  118 TYR A CE1 
949  C CE2 . TYR A 118 ? 0.42280 0.45860 0.47600 -0.03260 0.05060  0.03590  118 TYR A CE2 
950  C CZ  . TYR A 118 ? 0.41940 0.44840 0.45300 -0.02780 0.03310  0.04700  118 TYR A CZ  
951  O OH  . TYR A 118 ? 0.44020 0.46130 0.47910 -0.02220 0.03030  0.04660  118 TYR A OH  
952  N N   . ASP A 119 ? 0.51970 0.42130 0.39400 -0.01970 0.00770  -0.00900 119 ASP A N   
953  C CA  . ASP A 119 ? 0.55450 0.44020 0.39130 -0.01310 0.00760  -0.02110 119 ASP A CA  
954  C C   . ASP A 119 ? 0.55460 0.43150 0.35280 -0.00980 0.01520  -0.01360 119 ASP A C   
955  O O   . ASP A 119 ? 0.57960 0.44370 0.34520 -0.00460 0.02690  -0.01840 119 ASP A O   
956  C CB  . ASP A 119 ? 0.57220 0.45120 0.41350 -0.00930 0.01900  -0.03310 119 ASP A CB  
957  C CG  . ASP A 119 ? 0.56290 0.44120 0.43110 -0.01110 0.00640  -0.04430 119 ASP A CG  
958  O OD1 . ASP A 119 ? 0.54590 0.42680 0.41950 -0.01490 -0.01110 -0.04590 119 ASP A OD1 
959  O OD2 . ASP A 119 ? 0.56820 0.44300 0.45450 -0.00890 0.01460  -0.05150 119 ASP A OD2 
960  N N   . GLY A 120 ? 0.57140 0.45370 0.37180 -0.01270 0.00880  -0.00170 120 GLY A N   
961  C CA  . GLY A 120 ? 0.57290 0.44370 0.33850 -0.00990 0.01250  0.00730  120 GLY A CA  
962  C C   . GLY A 120 ? 0.56220 0.43230 0.32890 -0.01280 0.03480  0.01850  120 GLY A C   
963  O O   . GLY A 120 ? 0.56860 0.42530 0.30380 -0.01110 0.04110  0.02710  120 GLY A O   
964  N N   . LYS A 121 ? 0.58700 0.47060 0.39040 -0.01710 0.04630  0.01920  121 LYS A N   
965  C CA  . LYS A 121 ? 0.57310 0.46040 0.38770 -0.02080 0.06690  0.02820  121 LYS A CA  
966  C C   . LYS A 121 ? 0.53160 0.43620 0.38860 -0.02760 0.06220  0.03570  121 LYS A C   
967  O O   . LYS A 121 ? 0.51640 0.43170 0.39780 -0.02880 0.04930  0.03220  121 LYS A O   
968  C CB  . LYS A 121 ? 0.59580 0.48540 0.41900 -0.01830 0.08560  0.02010  121 LYS A CB  
969  C CG  . LYS A 121 ? 0.65430 0.52640 0.43250 -0.01080 0.09150  0.00930  121 LYS A CG  
970  C CD  . LYS A 121 ? 0.68070 0.55630 0.47190 -0.00710 0.11060  -0.00190 121 LYS A CD  
971  C CE  . LYS A 121 ? 0.64930 0.54600 0.49990 -0.01100 0.11530  0.00070  121 LYS A CE  
972  N NZ  . LYS A 121 ? 0.62580 0.53150 0.49230 -0.01600 0.13620  0.01170  121 LYS A NZ  
973  N N   . ASP A 122 ? 0.54620 0.45220 0.41040 -0.03260 0.07290  0.04600  122 ASP A N   
974  C CA  . ASP A 122 ? 0.51040 0.43250 0.41340 -0.03900 0.06830  0.05120  122 ASP A CA  
975  C C   . ASP A 122 ? 0.50040 0.43880 0.43940 -0.03880 0.06730  0.04570  122 ASP A C   
976  O O   . ASP A 122 ? 0.51520 0.45530 0.46170 -0.03590 0.08020  0.04050  122 ASP A O   
977  C CB  . ASP A 122 ? 0.50270 0.42480 0.41530 -0.04500 0.08300  0.06020  122 ASP A CB  
978  C CG  . ASP A 122 ? 0.51110 0.41740 0.39850 -0.04650 0.07860  0.06850  122 ASP A CG  
979  O OD1 . ASP A 122 ? 0.50500 0.40810 0.38160 -0.04370 0.06080  0.06710  122 ASP A OD1 
980  O OD2 . ASP A 122 ? 0.51950 0.41650 0.40070 -0.05050 0.09360  0.07650  122 ASP A OD2 
981  N N   . TYR A 123 ? 0.38130 0.33070 0.34130 -0.04140 0.05220  0.04700  123 TYR A N   
982  C CA  . TYR A 123 ? 0.37390 0.33660 0.36670 -0.04120 0.04850  0.04520  123 TYR A CA  
983  C C   . TYR A 123 ? 0.34130 0.31860 0.36350 -0.04640 0.04520  0.05130  123 TYR A C   
984  O O   . TYR A 123 ? 0.34290 0.33010 0.39220 -0.04680 0.05350  0.05150  123 TYR A O   
985  C CB  . TYR A 123 ? 0.37490 0.33650 0.36530 -0.03960 0.03360  0.04190  123 TYR A CB  
986  C CG  . TYR A 123 ? 0.36620 0.33640 0.38620 -0.03880 0.02890  0.04220  123 TYR A CG  
987  C CD1 . TYR A 123 ? 0.39630 0.36310 0.42700 -0.03370 0.03590  0.03590  123 TYR A CD1 
988  C CD2 . TYR A 123 ? 0.34030 0.32010 0.37510 -0.04250 0.01720  0.04890  123 TYR A CD2 
989  C CE1 . TYR A 123 ? 0.39660 0.36800 0.45540 -0.03170 0.02990  0.03730  123 TYR A CE1 
990  C CE2 . TYR A 123 ? 0.33870 0.32330 0.39700 -0.04100 0.01130  0.05180  123 TYR A CE2 
991  C CZ  . TYR A 123 ? 0.36780 0.34750 0.43950 -0.03540 0.01730  0.04660  123 TYR A CZ  
992  O OH  . TYR A 123 ? 0.37060 0.35180 0.46630 -0.03270 0.01070  0.05030  123 TYR A OH  
993  N N   . ILE A 124 ? 0.37510 0.35470 0.39350 -0.05020 0.03340  0.05510  124 ILE A N   
994  C CA  . ILE A 124 ? 0.35470 0.34660 0.39650 -0.05520 0.02830  0.05870  124 ILE A CA  
995  C C   . ILE A 124 ? 0.34940 0.33580 0.37460 -0.05860 0.02200  0.06030  124 ILE A C   
996  O O   . ILE A 124 ? 0.35410 0.33210 0.35600 -0.05620 0.01710  0.05900  124 ILE A O   
997  C CB  . ILE A 124 ? 0.34620 0.35000 0.40790 -0.05420 0.01590  0.05980  124 ILE A CB  
998  C CG1 . ILE A 124 ? 0.33220 0.34990 0.41970 -0.05810 0.00940  0.06210  124 ILE A CG1 
999  C CG2 . ILE A 124 ? 0.33940 0.34000 0.38270 -0.05420 0.00450  0.06050  124 ILE A CG2 
1000 C CD1 . ILE A 124 ? 0.33890 0.36600 0.44150 -0.05580 -0.00400 0.06510  124 ILE A CD1 
1001 N N   . ALA A 125 ? 0.36870 0.36000 0.40910 -0.06390 0.02170  0.06190  125 ALA A N   
1002 C CA  . ALA A 125 ? 0.37040 0.35450 0.39880 -0.06680 0.01660  0.06210  125 ALA A CA  
1003 C C   . ALA A 125 ? 0.35930 0.35500 0.40960 -0.07190 0.00720  0.06030  125 ALA A C   
1004 O O   . ALA A 125 ? 0.35570 0.36220 0.43370 -0.07520 0.00910  0.06030  125 ALA A O   
1005 C CB  . ALA A 125 ? 0.38350 0.35140 0.39970 -0.06850 0.02910  0.06570  125 ALA A CB  
1006 N N   . LEU A 126 ? 0.38130 0.37530 0.42010 -0.07210 -0.00320 0.05730  126 LEU A N   
1007 C CA  . LEU A 126 ? 0.38370 0.38480 0.43640 -0.07680 -0.01270 0.05300  126 LEU A CA  
1008 C C   . LEU A 126 ? 0.39380 0.38510 0.45730 -0.08260 -0.00640 0.05260  126 LEU A C   
1009 O O   . LEU A 126 ? 0.40140 0.37570 0.44830 -0.08160 0.00010  0.05500  126 LEU A O   
1010 C CB  . LEU A 126 ? 0.39370 0.39480 0.42780 -0.07440 -0.02300 0.04830  126 LEU A CB  
1011 C CG  . LEU A 126 ? 0.40350 0.41130 0.44310 -0.07770 -0.03470 0.04110  126 LEU A CG  
1012 C CD1 . LEU A 126 ? 0.40170 0.42530 0.45410 -0.07860 -0.04350 0.04240  126 LEU A CD1 
1013 C CD2 . LEU A 126 ? 0.42180 0.42770 0.43910 -0.07420 -0.03940 0.03560  126 LEU A CD2 
1014 N N   . ASN A 127 ? 0.38420 0.38540 0.47680 -0.08890 -0.00940 0.05000  127 ASN A N   
1015 C CA  . ASN A 127 ? 0.38630 0.37790 0.49480 -0.09650 -0.00230 0.04990  127 ASN A CA  
1016 C C   . ASN A 127 ? 0.40160 0.38110 0.49930 -0.09790 -0.01150 0.04350  127 ASN A C   
1017 O O   . ASN A 127 ? 0.40740 0.39050 0.48880 -0.09330 -0.02340 0.03750  127 ASN A O   
1018 C CB  . ASN A 127 ? 0.37480 0.38310 0.52480 -0.10360 -0.00330 0.04740  127 ASN A CB  
1019 C CG  . ASN A 127 ? 0.36990 0.39000 0.53540 -0.10110 0.00810  0.05260  127 ASN A CG  
1020 O OD1 . ASN A 127 ? 0.36980 0.37950 0.51660 -0.09750 0.02310  0.05870  127 ASN A OD1 
1021 N ND2 . ASN A 127 ? 0.35460 0.39600 0.55390 -0.10220 -0.00010 0.04930  127 ASN A ND2 
1022 N N   . GLU A 128 ? 0.43640 0.39990 0.54300 -0.10410 -0.00420 0.04500  128 GLU A N   
1023 C CA  . GLU A 128 ? 0.45210 0.40000 0.55240 -0.10520 -0.01200 0.03820  128 GLU A CA  
1024 C C   . GLU A 128 ? 0.45570 0.41720 0.56740 -0.10720 -0.02980 0.02420  128 GLU A C   
1025 O O   . GLU A 128 ? 0.46860 0.42280 0.56440 -0.10350 -0.03870 0.01550  128 GLU A O   
1026 C CB  . GLU A 128 ? 0.46520 0.39320 0.58120 -0.11390 -0.00100 0.04330  128 GLU A CB  
1027 C CG  . GLU A 128 ? 0.49240 0.39520 0.59640 -0.11260 -0.00570 0.03970  128 GLU A CG  
1028 C CD  . GLU A 128 ? 0.50170 0.37960 0.61860 -0.12140 0.00680  0.04840  128 GLU A CD  
1029 O OE1 . GLU A 128 ? 0.48400 0.36820 0.62730 -0.13150 0.01880  0.05420  128 GLU A OE1 
1030 O OE2 . GLU A 128 ? 0.52610 0.37770 0.62950 -0.11840 0.00490  0.04940  128 GLU A OE2 
1031 N N   . ASP A 129 ? 0.41540 0.39670 0.55390 -0.11230 -0.03580 0.02120  129 ASP A N   
1032 C CA  . ASP A 129 ? 0.41820 0.41190 0.56310 -0.11360 -0.05520 0.00790  129 ASP A CA  
1033 C C   . ASP A 129 ? 0.42790 0.43010 0.54050 -0.10440 -0.06440 0.00540  129 ASP A C   
1034 O O   . ASP A 129 ? 0.43920 0.44850 0.54590 -0.10410 -0.07970 -0.00550 129 ASP A O   
1035 C CB  . ASP A 129 ? 0.40690 0.42090 0.59060 -0.12030 -0.06190 0.00580  129 ASP A CB  
1036 C CG  . ASP A 129 ? 0.39560 0.42630 0.58360 -0.11530 -0.05740 0.01560  129 ASP A CG  
1037 O OD1 . ASP A 129 ? 0.39960 0.42890 0.55780 -0.10680 -0.05430 0.02170  129 ASP A OD1 
1038 O OD2 . ASP A 129 ? 0.38260 0.42840 0.60820 -0.11990 -0.05690 0.01640  129 ASP A OD2 
1039 N N   . LEU A 130 ? 0.36670 0.36750 0.45780 -0.09740 -0.05520 0.01500  130 LEU A N   
1040 C CA  . LEU A 130 ? 0.37410 0.38240 0.43760 -0.09000 -0.06010 0.01510  130 LEU A CA  
1041 C C   . LEU A 130 ? 0.37610 0.40270 0.44410 -0.08970 -0.07220 0.01540  130 LEU A C   
1042 O O   . LEU A 130 ? 0.38430 0.41650 0.42870 -0.08560 -0.07930 0.01360  130 LEU A O   
1043 C CB  . LEU A 130 ? 0.39200 0.39280 0.43340 -0.08660 -0.06470 0.00460  130 LEU A CB  
1044 C CG  . LEU A 130 ? 0.40060 0.38140 0.43860 -0.08510 -0.05660 0.00330  130 LEU A CG  
1045 C CD1 . LEU A 130 ? 0.42150 0.39840 0.44000 -0.07940 -0.06080 -0.00840 130 LEU A CD1 
1046 C CD2 . LEU A 130 ? 0.39590 0.36980 0.42790 -0.08150 -0.04410 0.01620  130 LEU A CD2 
1047 N N   . SER A 131 ? 0.41590 0.45230 0.51420 -0.09370 -0.07460 0.01810  131 SER A N   
1048 C CA  . SER A 131 ? 0.42070 0.47350 0.52430 -0.09170 -0.08910 0.01910  131 SER A CA  
1049 C C   . SER A 131 ? 0.40820 0.47120 0.54090 -0.09110 -0.08440 0.02780  131 SER A C   
1050 O O   . SER A 131 ? 0.40730 0.48380 0.55110 -0.08860 -0.09780 0.02940  131 SER A O   
1051 C CB  . SER A 131 ? 0.43240 0.49170 0.54650 -0.09610 -0.10770 0.00650  131 SER A CB  
1052 O OG  . SER A 131 ? 0.41950 0.47880 0.57140 -0.10410 -0.10520 0.00180  131 SER A OG  
1053 N N   . SER A 132 ? 0.38840 0.44490 0.53220 -0.09210 -0.06600 0.03340  132 SER A N   
1054 C CA  . SER A 132 ? 0.37750 0.44300 0.54650 -0.09010 -0.05800 0.04020  132 SER A CA  
1055 C C   . SER A 132 ? 0.37380 0.42640 0.52470 -0.08670 -0.03890 0.04700  132 SER A C   
1056 O O   . SER A 132 ? 0.37830 0.41600 0.50330 -0.08690 -0.03270 0.04670  132 SER A O   
1057 C CB  . SER A 132 ? 0.36340 0.43900 0.57780 -0.09730 -0.05520 0.03650  132 SER A CB  
1058 O OG  . SER A 132 ? 0.36360 0.42550 0.57940 -0.10470 -0.04240 0.03460  132 SER A OG  
1059 N N   . TRP A 133 ? 0.30250 0.36090 0.46810 -0.08290 -0.03070 0.05190  133 TRP A N   
1060 C CA  . TRP A 133 ? 0.30290 0.34980 0.45040 -0.07880 -0.01460 0.05640  133 TRP A CA  
1061 C C   . TRP A 133 ? 0.29620 0.34510 0.46810 -0.08080 0.00350  0.05730  133 TRP A C   
1062 O O   . TRP A 133 ? 0.29120 0.35550 0.50170 -0.08340 0.00320  0.05540  133 TRP A O   
1063 C CB  . TRP A 133 ? 0.31070 0.35920 0.44760 -0.07130 -0.01950 0.06010  133 TRP A CB  
1064 C CG  . TRP A 133 ? 0.31820 0.36690 0.43370 -0.07010 -0.03500 0.06080  133 TRP A CG  
1065 C CD1 . TRP A 133 ? 0.32840 0.38760 0.45130 -0.06950 -0.05150 0.06140  133 TRP A CD1 
1066 C CD2 . TRP A 133 ? 0.32060 0.35890 0.40310 -0.06950 -0.03470 0.06070  133 TRP A CD2 
1067 N NE1 . TRP A 133 ? 0.34160 0.39670 0.43420 -0.06890 -0.05930 0.06240  133 TRP A NE1 
1068 C CE2 . TRP A 133 ? 0.33450 0.37830 0.40540 -0.06910 -0.04840 0.06150  133 TRP A CE2 
1069 C CE3 . TRP A 133 ? 0.31200 0.33790 0.37440 -0.06860 -0.02470 0.05990  133 TRP A CE3 
1070 C CZ2 . TRP A 133 ? 0.34330 0.38210 0.38630 -0.06860 -0.04930 0.06110  133 TRP A CZ2 
1071 C CZ3 . TRP A 133 ? 0.31700 0.33910 0.35540 -0.06750 -0.02860 0.05890  133 TRP A CZ3 
1072 C CH2 . TRP A 133 ? 0.33230 0.36170 0.36300 -0.06790 -0.03920 0.05930  133 TRP A CH2 
1073 N N   . THR A 134 ? 0.37920 0.41310 0.52820 -0.07940 0.01970  0.05990  134 THR A N   
1074 C CA  . THR A 134 ? 0.38380 0.41780 0.54550 -0.07910 0.04020  0.06130  134 THR A CA  
1075 C C   . THR A 134 ? 0.39030 0.41720 0.52950 -0.07050 0.04510  0.06130  134 THR A C   
1076 O O   . THR A 134 ? 0.39570 0.40790 0.49890 -0.06780 0.04250  0.06220  134 THR A O   
1077 C CB  . THR A 134 ? 0.39230 0.41140 0.54240 -0.08540 0.05630  0.06460  134 THR A CB  
1078 O OG1 . THR A 134 ? 0.38010 0.40450 0.55550 -0.09430 0.05050  0.06330  134 THR A OG1 
1079 C CG2 . THR A 134 ? 0.39390 0.41450 0.55590 -0.08550 0.08040  0.06620  134 THR A CG2 
1080 N N   . ALA A 135 ? 0.38010 0.41770 0.54380 -0.06600 0.05110  0.05920  135 ALA A N   
1081 C CA  . ALA A 135 ? 0.39700 0.42790 0.54580 -0.05770 0.05520  0.05700  135 ALA A CA  
1082 C C   . ALA A 135 ? 0.41480 0.43920 0.55750 -0.05620 0.07950  0.05450  135 ALA A C   
1083 O O   . ALA A 135 ? 0.40250 0.43780 0.57460 -0.05940 0.09370  0.05410  135 ALA A O   
1084 C CB  . ALA A 135 ? 0.39700 0.44120 0.57640 -0.05180 0.04490  0.05560  135 ALA A CB  
1085 N N   . ALA A 136 ? 0.46200 0.46970 0.56740 -0.05130 0.08410  0.05220  136 ALA A N   
1086 C CA  . ALA A 136 ? 0.48230 0.47940 0.56760 -0.04930 0.10660  0.04980  136 ALA A CA  
1087 C C   . ALA A 136 ? 0.50650 0.51030 0.61110 -0.04200 0.11910  0.04150  136 ALA A C   
1088 O O   . ALA A 136 ? 0.51610 0.51630 0.61290 -0.04090 0.14210  0.03870  136 ALA A O   
1089 C CB  . ALA A 136 ? 0.50640 0.48180 0.53990 -0.04640 0.10300  0.04940  136 ALA A CB  
1090 N N   . ASP A 137 ? 0.45820 0.46940 0.58540 -0.03640 0.10580  0.03760  137 ASP A N   
1091 C CA  . ASP A 137 ? 0.47840 0.49440 0.62760 -0.02790 0.11670  0.02860  137 ASP A CA  
1092 C C   . ASP A 137 ? 0.47060 0.49950 0.66030 -0.02400 0.09870  0.02950  137 ASP A C   
1093 O O   . ASP A 137 ? 0.45250 0.48760 0.65000 -0.02850 0.08000  0.03730  137 ASP A O   
1094 C CB  . ASP A 137 ? 0.51380 0.50970 0.62350 -0.02140 0.12190  0.01980  137 ASP A CB  
1095 C CG  . ASP A 137 ? 0.53010 0.51350 0.61560 -0.02140 0.09940  0.02100  137 ASP A CG  
1096 O OD1 . ASP A 137 ? 0.50760 0.49840 0.61340 -0.02330 0.08140  0.02710  137 ASP A OD1 
1097 O OD2 . ASP A 137 ? 0.55410 0.52060 0.60010 -0.01950 0.09970  0.01570  137 ASP A OD2 
1098 N N   . THR A 138 ? 0.49050 0.52200 0.70420 -0.01460 0.10410  0.02140  138 THR A N   
1099 C CA  . THR A 138 ? 0.48120 0.52350 0.73570 -0.00930 0.08710  0.02380  138 THR A CA  
1100 C C   . THR A 138 ? 0.50080 0.52870 0.73540 -0.00860 0.06500  0.02900  138 THR A C   
1101 O O   . THR A 138 ? 0.48970 0.52410 0.74590 -0.00740 0.04640  0.03680  138 THR A O   
1102 C CB  . THR A 138 ? 0.49060 0.53930 0.78160 0.00170  0.09980  0.01340  138 THR A CB  
1103 O OG1 . THR A 138 ? 0.53620 0.56580 0.79600 0.00680  0.11300  0.00240  138 THR A OG1 
1104 C CG2 . THR A 138 ? 0.46590 0.53730 0.79430 0.00030  0.11960  0.01020  138 THR A CG2 
1105 N N   . ALA A 139 ? 0.47000 0.47840 0.66420 -0.00930 0.06630  0.02520  139 ALA A N   
1106 C CA  . ALA A 139 ? 0.47420 0.47080 0.65160 -0.01130 0.04730  0.03100  139 ALA A CA  
1107 C C   . ALA A 139 ? 0.43900 0.44280 0.60580 -0.01980 0.03450  0.04220  139 ALA A C   
1108 O O   . ALA A 139 ? 0.42540 0.43120 0.60000 -0.02070 0.01800  0.05090  139 ALA A O   
1109 C CB  . ALA A 139 ? 0.49080 0.46800 0.63130 -0.01130 0.05080  0.02270  139 ALA A CB  
1110 N N   . ALA A 140 ? 0.38800 0.39410 0.53520 -0.02570 0.04250  0.04220  140 ALA A N   
1111 C CA  . ALA A 140 ? 0.35500 0.36670 0.49240 -0.03330 0.03180  0.05010  140 ALA A CA  
1112 C C   . ALA A 140 ? 0.34170 0.37090 0.51280 -0.03430 0.02290  0.05550  140 ALA A C   
1113 O O   . ALA A 140 ? 0.32470 0.35790 0.48990 -0.03880 0.00860  0.06150  140 ALA A O   
1114 C CB  . ALA A 140 ? 0.34010 0.34730 0.45280 -0.03820 0.04310  0.04870  140 ALA A CB  
1115 N N   . GLN A 141 ? 0.38380 0.42460 0.59120 -0.02990 0.03050  0.05210  141 GLN A N   
1116 C CA  . GLN A 141 ? 0.37370 0.43280 0.61800 -0.02970 0.01800  0.05610  141 GLN A CA  
1117 C C   . GLN A 141 ? 0.38480 0.44100 0.63160 -0.02510 -0.00310 0.06330  141 GLN A C   
1118 O O   . GLN A 141 ? 0.37850 0.44470 0.63510 -0.02670 -0.02000 0.06920  141 GLN A O   
1119 C CB  . GLN A 141 ? 0.36990 0.44440 0.65870 -0.02510 0.03120  0.04990  141 GLN A CB  
1120 C CG  . GLN A 141 ? 0.35430 0.43350 0.64270 -0.03220 0.05230  0.04590  141 GLN A CG  
1121 C CD  . GLN A 141 ? 0.35570 0.45380 0.69260 -0.02940 0.06850  0.03980  141 GLN A CD  
1122 O OE1 . GLN A 141 ? 0.36950 0.47470 0.73740 -0.01970 0.06790  0.03570  141 GLN A OE1 
1123 N NE2 . GLN A 141 ? 0.35300 0.45950 0.69980 -0.03830 0.08380  0.03930  141 GLN A NE2 
1124 N N   . ILE A 142 ? 0.38380 0.42480 0.62010 -0.01970 -0.00280 0.06330  142 ILE A N   
1125 C CA  . ILE A 142 ? 0.39170 0.42530 0.62430 -0.01710 -0.02120 0.07310  142 ILE A CA  
1126 C C   . ILE A 142 ? 0.38140 0.41140 0.57890 -0.02550 -0.03060 0.08000  142 ILE A C   
1127 O O   . ILE A 142 ? 0.38250 0.41740 0.57880 -0.02630 -0.04670 0.08880  142 ILE A O   
1128 C CB  . ILE A 142 ? 0.40500 0.42000 0.63460 -0.01140 -0.01730 0.07100  142 ILE A CB  
1129 C CG1 . ILE A 142 ? 0.41680 0.43490 0.68050 -0.00190 -0.00550 0.06090  142 ILE A CG1 
1130 C CG2 . ILE A 142 ? 0.39800 0.40310 0.62530 -0.00970 -0.03530 0.08410  142 ILE A CG2 
1131 C CD1 . ILE A 142 ? 0.43230 0.42990 0.69160 0.00360  -0.00020 0.05470  142 ILE A CD1 
1132 N N   . THR A 143 ? 0.38460 0.40630 0.55260 -0.03100 -0.02070 0.07550  143 THR A N   
1133 C CA  . THR A 143 ? 0.36290 0.38280 0.50090 -0.03810 -0.02710 0.07980  143 THR A CA  
1134 C C   . THR A 143 ? 0.35990 0.39370 0.50160 -0.04190 -0.03500 0.08130  143 THR A C   
1135 O O   . THR A 143 ? 0.36640 0.40200 0.49410 -0.04440 -0.04730 0.08750  143 THR A O   
1136 C CB  . THR A 143 ? 0.35220 0.36340 0.46550 -0.04140 -0.01560 0.07280  143 THR A CB  
1137 O OG1 . THR A 143 ? 0.36510 0.36320 0.47520 -0.03830 -0.01190 0.06990  143 THR A OG1 
1138 C CG2 . THR A 143 ? 0.33290 0.34410 0.42040 -0.04750 -0.02090 0.07530  143 THR A CG2 
1139 N N   . GLN A 144 ? 0.38400 0.42760 0.54560 -0.04260 -0.02770 0.07540  144 GLN A N   
1140 C CA  . GLN A 144 ? 0.37300 0.42960 0.54450 -0.04700 -0.03600 0.07480  144 GLN A CA  
1141 C C   . GLN A 144 ? 0.38590 0.45190 0.57330 -0.04350 -0.05570 0.08070  144 GLN A C   
1142 O O   . GLN A 144 ? 0.38870 0.45880 0.56300 -0.04700 -0.06920 0.08230  144 GLN A O   
1143 C CB  . GLN A 144 ? 0.35550 0.42100 0.55360 -0.04910 -0.02280 0.06830  144 GLN A CB  
1144 C CG  . GLN A 144 ? 0.34660 0.42670 0.56560 -0.05470 -0.03180 0.06590  144 GLN A CG  
1145 C CD  . GLN A 144 ? 0.33330 0.41990 0.57780 -0.05910 -0.01450 0.06060  144 GLN A CD  
1146 O OE1 . GLN A 144 ? 0.33780 0.41710 0.57770 -0.05750 0.00490  0.05930  144 GLN A OE1 
1147 N NE2 . GLN A 144 ? 0.32160 0.42130 0.59200 -0.06540 -0.02090 0.05740  144 GLN A NE2 
1148 N N   . ARG A 145 ? 0.40260 0.47140 0.61750 -0.03580 -0.05850 0.08330  145 ARG A N   
1149 C CA  . ARG A 145 ? 0.40980 0.48530 0.63840 -0.03060 -0.07990 0.09060  145 ARG A CA  
1150 C C   . ARG A 145 ? 0.42240 0.48560 0.61170 -0.03190 -0.09150 0.10090  145 ARG A C   
1151 O O   . ARG A 145 ? 0.42040 0.48910 0.59940 -0.03270 -0.10890 0.10510  145 ARG A O   
1152 C CB  . ARG A 145 ? 0.40880 0.48580 0.67360 -0.02030 -0.08020 0.09210  145 ARG A CB  
1153 C CG  . ARG A 145 ? 0.39680 0.49030 0.70450 -0.01910 -0.06780 0.08160  145 ARG A CG  
1154 C CD  . ARG A 145 ? 0.41390 0.51330 0.76560 -0.00720 -0.06930 0.08090  145 ARG A CD  
1155 N NE  . ARG A 145 ? 0.42200 0.50460 0.76740 -0.00190 -0.05370 0.07850  145 ARG A NE  
1156 C CZ  . ARG A 145 ? 0.43300 0.50360 0.78630 0.00760  -0.06200 0.08430  145 ARG A CZ  
1157 N NH1 . ARG A 145 ? 0.42000 0.49220 0.78390 0.01340  -0.08580 0.09520  145 ARG A NH1 
1158 N NH2 . ARG A 145 ? 0.45210 0.50700 0.80140 0.01160  -0.04710 0.07890  145 ARG A NH2 
1159 N N   . LYS A 146 ? 0.40150 0.44850 0.56770 -0.03290 -0.08140 0.10410  146 LYS A N   
1160 C CA  . LYS A 146 ? 0.40170 0.43780 0.53300 -0.03560 -0.08810 0.11430  146 LYS A CA  
1161 C C   . LYS A 146 ? 0.40240 0.44380 0.50510 -0.04300 -0.08940 0.11060  146 LYS A C   
1162 O O   . LYS A 146 ? 0.40410 0.44550 0.48440 -0.04400 -0.10130 0.11750  146 LYS A O   
1163 C CB  . LYS A 146 ? 0.39370 0.41330 0.51370 -0.03670 -0.07560 0.11600  146 LYS A CB  
1164 C CG  . LYS A 146 ? 0.40070 0.41060 0.54590 -0.02900 -0.07580 0.11950  146 LYS A CG  
1165 C CD  . LYS A 146 ? 0.39630 0.38980 0.53250 -0.03130 -0.06370 0.11740  146 LYS A CD  
1166 C CE  . LYS A 146 ? 0.39430 0.37440 0.50970 -0.03530 -0.06870 0.13110  146 LYS A CE  
1167 N NZ  . LYS A 146 ? 0.38730 0.35120 0.50180 -0.03830 -0.05900 0.12850  146 LYS A NZ  
1168 N N   . TRP A 147 ? 0.41470 0.45890 0.51580 -0.04760 -0.07710 0.09980  147 TRP A N   
1169 C CA  . TRP A 147 ? 0.41230 0.45940 0.48870 -0.05350 -0.07780 0.09490  147 TRP A CA  
1170 C C   . TRP A 147 ? 0.40590 0.46500 0.48990 -0.05420 -0.09230 0.09130  147 TRP A C   
1171 O O   . TRP A 147 ? 0.40960 0.47000 0.46910 -0.05740 -0.09870 0.08900  147 TRP A O   
1172 C CB  . TRP A 147 ? 0.38150 0.42560 0.45540 -0.05700 -0.06250 0.08560  147 TRP A CB  
1173 C CG  . TRP A 147 ? 0.37030 0.40350 0.43150 -0.05680 -0.05180 0.08680  147 TRP A CG  
1174 C CD1 . TRP A 147 ? 0.37200 0.39770 0.42740 -0.05550 -0.05300 0.09490  147 TRP A CD1 
1175 C CD2 . TRP A 147 ? 0.34420 0.37170 0.39740 -0.05840 -0.04000 0.07980  147 TRP A CD2 
1176 N NE1 . TRP A 147 ? 0.35060 0.36840 0.39870 -0.05680 -0.04280 0.09130  147 TRP A NE1 
1177 C CE2 . TRP A 147 ? 0.33650 0.35560 0.38140 -0.05780 -0.03590 0.08210  147 TRP A CE2 
1178 C CE3 . TRP A 147 ? 0.33640 0.36350 0.38830 -0.06020 -0.03350 0.07260  147 TRP A CE3 
1179 C CZ2 . TRP A 147 ? 0.32470 0.33710 0.36060 -0.05810 -0.02750 0.07580  147 TRP A CZ2 
1180 C CZ3 . TRP A 147 ? 0.32460 0.34290 0.36390 -0.05980 -0.02450 0.06860  147 TRP A CZ3 
1181 C CH2 . TRP A 147 ? 0.32320 0.33520 0.35440 -0.05840 -0.02270 0.06950  147 TRP A CH2 
1182 N N   . GLU A 148 ? 0.38660 0.45540 0.50610 -0.05130 -0.09760 0.08920  148 GLU A N   
1183 C CA  . GLU A 148 ? 0.38480 0.46660 0.51670 -0.05190 -0.11540 0.08540  148 GLU A CA  
1184 C C   . GLU A 148 ? 0.39900 0.47950 0.51170 -0.04720 -0.13520 0.09550  148 GLU A C   
1185 O O   . GLU A 148 ? 0.40570 0.48990 0.49790 -0.04910 -0.14930 0.09270  148 GLU A O   
1186 C CB  . GLU A 148 ? 0.36770 0.46330 0.54950 -0.05010 -0.11540 0.08040  148 GLU A CB  
1187 C CG  . GLU A 148 ? 0.34920 0.44520 0.54480 -0.05640 -0.09540 0.07120  148 GLU A CG  
1188 C CD  . GLU A 148 ? 0.33630 0.44590 0.58200 -0.05570 -0.08840 0.06690  148 GLU A CD  
1189 O OE1 . GLU A 148 ? 0.34320 0.46160 0.61750 -0.04830 -0.09560 0.07020  148 GLU A OE1 
1190 O OE2 . GLU A 148 ? 0.31830 0.42930 0.57590 -0.06220 -0.07390 0.06060  148 GLU A OE2 
1191 N N   . ALA A 149 ? 0.34810 0.42110 0.46430 -0.04080 -0.13650 0.10740  149 ALA A N   
1192 C CA  . ALA A 149 ? 0.36440 0.43280 0.46060 -0.03570 -0.15570 0.12020  149 ALA A CA  
1193 C C   . ALA A 149 ? 0.37750 0.43530 0.42170 -0.04040 -0.15280 0.12560  149 ALA A C   
1194 O O   . ALA A 149 ? 0.40340 0.45960 0.41990 -0.03840 -0.16910 0.13290  149 ALA A O   
1195 C CB  . ALA A 149 ? 0.36810 0.42750 0.48310 -0.02760 -0.15680 0.13240  149 ALA A CB  
1196 N N   . ALA A 150 ? 0.45470 0.50630 0.48510 -0.04620 -0.13260 0.12160  150 ALA A N   
1197 C CA  . ALA A 150 ? 0.46070 0.50540 0.44880 -0.05100 -0.12570 0.12460  150 ALA A CA  
1198 C C   . ALA A 150 ? 0.46340 0.51580 0.43650 -0.05580 -0.12400 0.10980  150 ALA A C   
1199 O O   . ALA A 150 ? 0.46710 0.51630 0.40790 -0.05920 -0.11650 0.10930  150 ALA A O   
1200 C CB  . ALA A 150 ? 0.45400 0.48860 0.44040 -0.05400 -0.10610 0.12790  150 ALA A CB  
1201 N N   . ARG A 151 ? 0.53190 0.59400 0.53090 -0.05640 -0.12890 0.09730  151 ARG A N   
1202 C CA  . ARG A 151 ? 0.53090 0.59750 0.52160 -0.06100 -0.12790 0.08220  151 ARG A CA  
1203 C C   . ARG A 151 ? 0.52670 0.58680 0.50330 -0.06450 -0.10820 0.07770  151 ARG A C   
1204 O O   . ARG A 151 ? 0.53180 0.59120 0.48240 -0.06660 -0.10570 0.07090  151 ARG A O   
1205 C CB  . ARG A 151 ? 0.54820 0.61770 0.50780 -0.06060 -0.14470 0.07930  151 ARG A CB  
1206 C CG  . ARG A 151 ? 0.56280 0.64160 0.54050 -0.05760 -0.16880 0.07770  151 ARG A CG  
1207 C CD  . ARG A 151 ? 0.57400 0.65040 0.54940 -0.05080 -0.18140 0.09510  151 ARG A CD  
1208 N NE  . ARG A 151 ? 0.58960 0.67500 0.57000 -0.04660 -0.20940 0.09310  151 ARG A NE  
1209 C CZ  . ARG A 151 ? 0.56370 0.66120 0.59140 -0.04360 -0.22240 0.09020  151 ARG A CZ  
1210 N NH1 . ARG A 151 ? 0.53940 0.64100 0.61190 -0.04410 -0.20800 0.08930  151 ARG A NH1 
1211 N NH2 . ARG A 151 ? 0.57630 0.68290 0.60700 -0.03980 -0.25050 0.08720  151 ARG A NH2 
1212 N N   . VAL A 152 ? 0.43630 0.49200 0.43140 -0.06440 -0.09470 0.08030  152 VAL A N   
1213 C CA  . VAL A 152 ? 0.43610 0.48630 0.42030 -0.06650 -0.07910 0.07640  152 VAL A CA  
1214 C C   . VAL A 152 ? 0.42860 0.47930 0.41560 -0.06890 -0.07610 0.06280  152 VAL A C   
1215 O O   . VAL A 152 ? 0.42610 0.47390 0.39730 -0.06970 -0.06870 0.05720  152 VAL A O   
1216 C CB  . VAL A 152 ? 0.42440 0.46850 0.42460 -0.06520 -0.06820 0.08150  152 VAL A CB  
1217 C CG1 . VAL A 152 ? 0.40140 0.44090 0.39330 -0.06670 -0.05540 0.07590  152 VAL A CG1 
1218 C CG2 . VAL A 152 ? 0.42310 0.46300 0.41930 -0.06340 -0.07030 0.09450  152 VAL A CG2 
1219 N N   . ALA A 153 ? 0.41380 0.46780 0.42350 -0.07020 -0.08180 0.05740  153 ALA A N   
1220 C CA  . ALA A 153 ? 0.40950 0.46020 0.42340 -0.07330 -0.07860 0.04600  153 ALA A CA  
1221 C C   . ALA A 153 ? 0.42320 0.47410 0.41240 -0.07400 -0.08500 0.03670  153 ALA A C   
1222 O O   . ALA A 153 ? 0.42520 0.46980 0.40690 -0.07430 -0.07800 0.02880  153 ALA A O   
1223 C CB  . ALA A 153 ? 0.39720 0.45210 0.44330 -0.07650 -0.08330 0.04220  153 ALA A CB  
1224 N N   . GLU A 154 ? 0.54000 0.59740 0.51520 -0.07320 -0.09850 0.03720  154 GLU A N   
1225 C CA  . GLU A 154 ? 0.55550 0.61320 0.50220 -0.07320 -0.10420 0.02690  154 GLU A CA  
1226 C C   . GLU A 154 ? 0.55830 0.61240 0.48170 -0.07150 -0.08950 0.02630  154 GLU A C   
1227 O O   . GLU A 154 ? 0.56900 0.62090 0.48040 -0.07110 -0.08680 0.01340  154 GLU A O   
1228 C CB  . GLU A 154 ? 0.57080 0.63450 0.49750 -0.07150 -0.12040 0.03110  154 GLU A CB  
1229 C CG  . GLU A 154 ? 0.57710 0.64760 0.52860 -0.07210 -0.13930 0.02940  154 GLU A CG  
1230 C CD  . GLU A 154 ? 0.61180 0.68680 0.53790 -0.06890 -0.15910 0.03320  154 GLU A CD  
1231 O OE1 . GLU A 154 ? 0.62000 0.69140 0.50920 -0.06620 -0.15550 0.04290  154 GLU A OE1 
1232 O OE2 . GLU A 154 ? 0.62150 0.70380 0.56510 -0.06920 -0.17890 0.02670  154 GLU A OE2 
1233 N N   . GLN A 155 ? 0.57820 0.63230 0.49860 -0.07050 -0.08010 0.03920  155 GLN A N   
1234 C CA  . GLN A 155 ? 0.58000 0.63390 0.48580 -0.06970 -0.06590 0.03880  155 GLN A CA  
1235 C C   . GLN A 155 ? 0.56800 0.61700 0.49000 -0.06870 -0.05720 0.03080  155 GLN A C   
1236 O O   . GLN A 155 ? 0.57370 0.62360 0.48690 -0.06690 -0.05030 0.02180  155 GLN A O   
1237 C CB  . GLN A 155 ? 0.57420 0.62840 0.47810 -0.07020 -0.05950 0.05440  155 GLN A CB  
1238 C CG  . GLN A 155 ? 0.59020 0.64580 0.47280 -0.07050 -0.06700 0.06530  155 GLN A CG  
1239 C CD  . GLN A 155 ? 0.58250 0.63380 0.47350 -0.07110 -0.06380 0.08180  155 GLN A CD  
1240 O OE1 . GLN A 155 ? 0.57550 0.62560 0.46940 -0.07310 -0.05090 0.08550  155 GLN A OE1 
1241 N NE2 . GLN A 155 ? 0.58450 0.63330 0.48340 -0.06910 -0.07640 0.09080  155 GLN A NE2 
1242 N N   . LEU A 156 ? 0.42400 0.46770 0.36900 -0.06910 -0.05690 0.03430  156 LEU A N   
1243 C CA  . LEU A 156 ? 0.41650 0.45230 0.37210 -0.06770 -0.05060 0.02840  156 LEU A CA  
1244 C C   . LEU A 156 ? 0.42910 0.46030 0.38360 -0.06770 -0.05500 0.01510  156 LEU A C   
1245 O O   . LEU A 156 ? 0.43070 0.45660 0.38310 -0.06460 -0.05020 0.00760  156 LEU A O   
1246 C CB  . LEU A 156 ? 0.39990 0.42960 0.37510 -0.06860 -0.04860 0.03480  156 LEU A CB  
1247 C CG  . LEU A 156 ? 0.38710 0.41380 0.36430 -0.06650 -0.04050 0.04180  156 LEU A CG  
1248 C CD1 . LEU A 156 ? 0.39210 0.41340 0.36400 -0.06310 -0.03560 0.03630  156 LEU A CD1 
1249 C CD2 . LEU A 156 ? 0.38600 0.41980 0.35700 -0.06680 -0.04010 0.04940  156 LEU A CD2 
1250 N N   A ARG A 157 ? 0.40510 0.43790 0.36380 -0.07090 -0.06540 0.01120  157 ARG A N   
1251 N N   B ARG A 157 ? 0.40520 0.43810 0.36370 -0.07090 -0.06540 0.01130  157 ARG A N   
1252 C CA  A ARG A 157 ? 0.41630 0.44270 0.37770 -0.07210 -0.07100 -0.00300 157 ARG A CA  
1253 C CA  B ARG A 157 ? 0.41610 0.44250 0.37730 -0.07210 -0.07100 -0.00290 157 ARG A CA  
1254 C C   A ARG A 157 ? 0.43350 0.46210 0.37130 -0.06840 -0.07010 -0.01480 157 ARG A C   
1255 C C   B ARG A 157 ? 0.43340 0.46200 0.37120 -0.06850 -0.07010 -0.01470 157 ARG A C   
1256 O O   A ARG A 157 ? 0.44030 0.46020 0.37990 -0.06600 -0.06770 -0.02640 157 ARG A O   
1257 O O   B ARG A 157 ? 0.44030 0.46020 0.38010 -0.06610 -0.06770 -0.02630 157 ARG A O   
1258 C CB  A ARG A 157 ? 0.41420 0.44430 0.38830 -0.07690 -0.08450 -0.00600 157 ARG A CB  
1259 C CB  B ARG A 157 ? 0.41420 0.44470 0.38770 -0.07680 -0.08450 -0.00560 157 ARG A CB  
1260 C CG  A ARG A 157 ? 0.42430 0.44690 0.40480 -0.07970 -0.09230 -0.02240 157 ARG A CG  
1261 C CG  B ARG A 157 ? 0.42060 0.44260 0.40580 -0.08020 -0.09110 -0.02020 157 ARG A CG  
1262 C CD  A ARG A 157 ? 0.42150 0.44950 0.42330 -0.08570 -0.10700 -0.02620 157 ARG A CD  
1263 C CD  B ARG A 157 ? 0.41300 0.44080 0.42250 -0.08630 -0.10370 -0.02130 157 ARG A CD  
1264 N NE  A ARG A 157 ? 0.43610 0.45560 0.44450 -0.08920 -0.11550 -0.04410 157 ARG A NE  
1265 N NE  B ARG A 157 ? 0.42400 0.46370 0.41800 -0.08550 -0.11960 -0.02540 157 ARG A NE  
1266 C CZ  A ARG A 157 ? 0.43410 0.45630 0.46630 -0.09580 -0.12930 -0.05230 157 ARG A CZ  
1267 C CZ  B ARG A 157 ? 0.42140 0.47260 0.41620 -0.08420 -0.12600 -0.01400 157 ARG A CZ  
1268 N NH1 A ARG A 157 ? 0.41100 0.44600 0.46670 -0.09920 -0.13610 -0.04410 157 ARG A NH1 
1269 N NH1 B ARG A 157 ? 0.40180 0.45510 0.41270 -0.08350 -0.11650 0.00080  157 ARG A NH1 
1270 N NH2 A ARG A 157 ? 0.43480 0.44680 0.47060 -0.09880 -0.13690 -0.07050 157 ARG A NH2 
1271 N NH2 B ARG A 157 ? 0.43600 0.49520 0.41310 -0.08290 -0.14300 -0.01770 157 ARG A NH2 
1272 N N   . ALA A 158 ? 0.39970 0.43870 0.31480 -0.06760 -0.07060 -0.01150 158 ALA A N   
1273 C CA  . ALA A 158 ? 0.41980 0.46270 0.31000 -0.06420 -0.06620 -0.02270 158 ALA A CA  
1274 C C   . ALA A 158 ? 0.41780 0.45970 0.31370 -0.05980 -0.05230 -0.02540 158 ALA A C   
1275 O O   . ALA A 158 ? 0.43700 0.47710 0.32790 -0.05570 -0.04890 -0.04040 158 ALA A O   
1276 C CB  . ALA A 158 ? 0.42930 0.48210 0.29190 -0.06480 -0.06620 -0.01420 158 ALA A CB  
1277 N N   . TYR A 159 ? 0.38560 0.42870 0.29420 -0.05990 -0.04550 -0.01240 159 TYR A N   
1278 C CA  . TYR A 159 ? 0.38570 0.42940 0.30360 -0.05530 -0.03560 -0.01490 159 TYR A CA  
1279 C C   . TYR A 159 ? 0.38950 0.41880 0.32310 -0.05170 -0.03870 -0.02280 159 TYR A C   
1280 O O   . TYR A 159 ? 0.40070 0.42830 0.33700 -0.04580 -0.03510 -0.03410 159 TYR A O   
1281 C CB  . TYR A 159 ? 0.37220 0.41940 0.29920 -0.05670 -0.03060 -0.00040 159 TYR A CB  
1282 C CG  . TYR A 159 ? 0.37480 0.42090 0.31600 -0.05190 -0.02530 -0.00270 159 TYR A CG  
1283 C CD1 . TYR A 159 ? 0.38740 0.44560 0.32980 -0.04880 -0.01680 -0.00880 159 TYR A CD1 
1284 C CD2 . TYR A 159 ? 0.36270 0.39650 0.31630 -0.05020 -0.02900 0.00120  159 TYR A CD2 
1285 C CE1 . TYR A 159 ? 0.38820 0.44750 0.34740 -0.04350 -0.01480 -0.01160 159 TYR A CE1 
1286 C CE2 . TYR A 159 ? 0.36640 0.39830 0.32980 -0.04460 -0.02740 -0.00050 159 TYR A CE2 
1287 C CZ  . TYR A 159 ? 0.37870 0.42390 0.34690 -0.04090 -0.02180 -0.00740 159 TYR A CZ  
1288 O OH  . TYR A 159 ? 0.38010 0.42510 0.36210 -0.03450 -0.02320 -0.01000 159 TYR A OH  
1289 N N   . LEU A 160 ? 0.41050 0.42890 0.35590 -0.05510 -0.04430 -0.01630 160 LEU A N   
1290 C CA  . LEU A 160 ? 0.41690 0.41810 0.37540 -0.05270 -0.04580 -0.01970 160 LEU A CA  
1291 C C   . LEU A 160 ? 0.43730 0.43050 0.39500 -0.05110 -0.05030 -0.03630 160 LEU A C   
1292 O O   . LEU A 160 ? 0.45260 0.43440 0.41670 -0.04510 -0.04900 -0.04320 160 LEU A O   
1293 C CB  . LEU A 160 ? 0.40230 0.39460 0.37250 -0.05830 -0.04780 -0.00890 160 LEU A CB  
1294 C CG  . LEU A 160 ? 0.38970 0.38660 0.36060 -0.05820 -0.04260 0.00500  160 LEU A CG  
1295 C CD1 . LEU A 160 ? 0.37590 0.36810 0.35800 -0.06360 -0.04250 0.01390  160 LEU A CD1 
1296 C CD2 . LEU A 160 ? 0.39220 0.38200 0.36240 -0.05170 -0.03850 0.00690  160 LEU A CD2 
1297 N N   . GLU A 161 ? 0.49750 0.49590 0.44690 -0.05540 -0.05690 -0.04390 161 GLU A N   
1298 C CA  . GLU A 161 ? 0.51720 0.50760 0.46420 -0.05390 -0.06230 -0.06280 161 GLU A CA  
1299 C C   . GLU A 161 ? 0.53370 0.53190 0.46580 -0.04610 -0.05540 -0.07590 161 GLU A C   
1300 O O   . GLU A 161 ? 0.54660 0.53490 0.48080 -0.04160 -0.05690 -0.09290 161 GLU A O   
1301 C CB  . GLU A 161 ? 0.51780 0.51260 0.45820 -0.06040 -0.07380 -0.06900 161 GLU A CB  
1302 C CG  . GLU A 161 ? 0.51340 0.50460 0.47410 -0.06870 -0.08140 -0.05990 161 GLU A CG  
1303 C CD  . GLU A 161 ? 0.51420 0.51410 0.46900 -0.07370 -0.09590 -0.06750 161 GLU A CD  
1304 O OE1 . GLU A 161 ? 0.52700 0.53540 0.45390 -0.07060 -0.09960 -0.07660 161 GLU A OE1 
1305 O OE2 . GLU A 161 ? 0.50530 0.50410 0.48280 -0.08060 -0.10400 -0.06460 161 GLU A OE2 
1306 N N   . GLY A 162 ? 0.47840 0.49400 0.39750 -0.04470 -0.04700 -0.06900 162 GLY A N   
1307 C CA  . GLY A 162 ? 0.49770 0.52480 0.40230 -0.03890 -0.03760 -0.08120 162 GLY A CA  
1308 C C   . GLY A 162 ? 0.49500 0.52920 0.41390 -0.03230 -0.02640 -0.07880 162 GLY A C   
1309 O O   . GLY A 162 ? 0.49450 0.51930 0.42990 -0.02500 -0.02660 -0.08790 162 GLY A O   
1310 N N   . LEU A 163 ? 0.44710 0.50960 0.37130 -0.10070 -0.08320 0.05350  163 LEU A N   
1311 C CA  . LEU A 163 ? 0.45280 0.49060 0.37290 -0.08710 -0.06160 0.03600  163 LEU A CA  
1312 C C   . LEU A 163 ? 0.42720 0.44870 0.36840 -0.08730 -0.05650 0.02710  163 LEU A C   
1313 O O   . LEU A 163 ? 0.42690 0.42590 0.35630 -0.08280 -0.04940 0.00760  163 LEU A O   
1314 C CB  . LEU A 163 ? 0.45790 0.50770 0.39000 -0.07370 -0.04050 0.05090  163 LEU A CB  
1315 C CG  . LEU A 163 ? 0.49470 0.55600 0.40080 -0.07040 -0.04090 0.05590  163 LEU A CG  
1316 C CD1 . LEU A 163 ? 0.47410 0.54310 0.39150 -0.05910 -0.02030 0.07450  163 LEU A CD1 
1317 C CD2 . LEU A 163 ? 0.51690 0.55840 0.38820 -0.06780 -0.03930 0.03240  163 LEU A CD2 
1318 N N   . CYS A 164 ? 0.51690 0.55290 0.48970 -0.09010 -0.05840 0.04400  164 CYS A N   
1319 C CA  . CYS A 164 ? 0.48670 0.50660 0.47740 -0.08890 -0.05210 0.03700  164 CYS A CA  
1320 C C   . CYS A 164 ? 0.47930 0.47430 0.45030 -0.09890 -0.06590 0.01480  164 CYS A C   
1321 O O   . CYS A 164 ? 0.47280 0.44610 0.43820 -0.09230 -0.05640 -0.00190 164 CYS A O   
1322 C CB  . CYS A 164 ? 0.45820 0.49990 0.48240 -0.08790 -0.05130 0.06170  164 CYS A CB  
1323 S SG  . CYS A 164 ? 0.42720 0.44500 0.46910 -0.08130 -0.03670 0.05550  164 CYS A SG  
1324 N N   . VAL A 165 ? 0.49440 0.48970 0.45000 -0.11560 -0.08870 0.01550  165 VAL A N   
1325 C CA  A VAL A 165 ? 0.49720 0.45430 0.42390 -0.12490 -0.10060 -0.00580 165 VAL A CA  
1326 C CA  B VAL A 165 ? 0.49860 0.45590 0.42390 -0.12590 -0.10190 -0.00550 165 VAL A CA  
1327 C C   . VAL A 165 ? 0.53910 0.46510 0.42040 -0.11330 -0.09400 -0.02840 165 VAL A C   
1328 O O   . VAL A 165 ? 0.54010 0.43300 0.40270 -0.10590 -0.08890 -0.04630 165 VAL A O   
1329 C CB  A VAL A 165 ? 0.49940 0.45640 0.41480 -0.15220 -0.12950 0.00200  165 VAL A CB  
1330 C CB  B VAL A 165 ? 0.50590 0.46480 0.41660 -0.15320 -0.13120 0.00270  165 VAL A CB  
1331 C CG1 A VAL A 165 ? 0.45910 0.45520 0.42600 -0.15980 -0.13230 0.02880  165 VAL A CG1 
1332 C CG1 B VAL A 165 ? 0.53190 0.43460 0.39640 -0.16510 -0.14460 -0.02060 165 VAL A CG1 
1333 C CG2 A VAL A 165 ? 0.52860 0.49740 0.41560 -0.16360 -0.14560 0.00840  165 VAL A CG2 
1334 C CG2 B VAL A 165 ? 0.46630 0.46740 0.42740 -0.16330 -0.13700 0.03120  165 VAL A CG2 
1335 N N   . GLU A 166 ? 0.54550 0.48360 0.40870 -0.10810 -0.09130 -0.02530 166 GLU A N   
1336 C CA  . GLU A 166 ? 0.59190 0.50440 0.41080 -0.09330 -0.08190 -0.04330 166 GLU A CA  
1337 C C   . GLU A 166 ? 0.57960 0.49760 0.41840 -0.07330 -0.05760 -0.04820 166 GLU A C   
1338 O O   . GLU A 166 ? 0.59740 0.48980 0.41030 -0.06010 -0.05010 -0.06320 166 GLU A O   
1339 C CB  . GLU A 166 ? 0.61810 0.54700 0.41570 -0.09200 -0.08340 -0.03560 166 GLU A CB  
1340 C CG  . GLU A 166 ? 0.64950 0.56700 0.41200 -0.11510 -0.11230 -0.03340 166 GLU A CG  
1341 C CD  . GLU A 166 ? 0.66700 0.62290 0.43380 -0.12020 -0.11880 -0.01320 166 GLU A CD  
1342 O OE1 . GLU A 166 ? 0.65270 0.63810 0.44540 -0.10410 -0.09930 -0.00160 166 GLU A OE1 
1343 O OE2 . GLU A 166 ? 0.67960 0.63500 0.42100 -0.14260 -0.14520 -0.00730 166 GLU A OE2 
1344 N N   . TRP A 167 ? 0.43830 0.38730 0.32000 -0.07140 -0.04560 -0.03380 167 TRP A N   
1345 C CA  . TRP A 167 ? 0.42910 0.38590 0.32840 -0.06010 -0.02700 -0.03570 167 TRP A CA  
1346 C C   . TRP A 167 ? 0.40060 0.34170 0.31220 -0.06020 -0.02790 -0.04410 167 TRP A C   
1347 O O   . TRP A 167 ? 0.40530 0.34620 0.31570 -0.04890 -0.01740 -0.05040 167 TRP A O   
1348 C CB  . TRP A 167 ? 0.42070 0.40040 0.34950 -0.06300 -0.01600 -0.01900 167 TRP A CB  
1349 C CG  . TRP A 167 ? 0.45680 0.45260 0.37330 -0.05800 -0.00730 -0.01200 167 TRP A CG  
1350 C CD1 . TRP A 167 ? 0.47300 0.47960 0.38600 -0.06030 -0.00920 0.00110  167 TRP A CD1 
1351 C CD2 . TRP A 167 ? 0.46750 0.47500 0.37400 -0.04830 0.00550  -0.01460 167 TRP A CD2 
1352 N NE1 . TRP A 167 ? 0.48220 0.50180 0.38160 -0.05390 0.00180  0.00520  167 TRP A NE1 
1353 C CE2 . TRP A 167 ? 0.47900 0.50190 0.37570 -0.04680 0.01130  -0.00340 167 TRP A CE2 
1354 C CE3 . TRP A 167 ? 0.46220 0.47480 0.37010 -0.03940 0.01380  -0.02130 167 TRP A CE3 
1355 C CZ2 . TRP A 167 ? 0.47810 0.52130 0.36670 -0.03820 0.02520  0.00110  167 TRP A CZ2 
1356 C CZ3 . TRP A 167 ? 0.46730 0.50560 0.37010 -0.02940 0.02780  -0.01460 167 TRP A CZ3 
1357 C CH2 . TRP A 167 ? 0.47000 0.52330 0.36300 -0.02950 0.03350  -0.00360 167 TRP A CH2 
1358 N N   . LEU A 168 ? 0.48490 0.41870 0.41140 -0.07200 -0.03960 -0.04040 168 LEU A N   
1359 C CA  . LEU A 168 ? 0.45700 0.37420 0.39310 -0.07210 -0.04060 -0.04750 168 LEU A CA  
1360 C C   . LEU A 168 ? 0.48690 0.37160 0.38550 -0.06400 -0.04390 -0.06470 168 LEU A C   
1361 O O   . LEU A 168 ? 0.48860 0.36620 0.38890 -0.05220 -0.03480 -0.07090 168 LEU A O   
1362 C CB  . LEU A 168 ? 0.42040 0.33860 0.37750 -0.08610 -0.05230 -0.03730 168 LEU A CB  
1363 C CG  . LEU A 168 ? 0.39860 0.29660 0.36170 -0.08800 -0.05540 -0.04360 168 LEU A CG  
1364 C CD1 . LEU A 168 ? 0.37710 0.27940 0.35630 -0.07710 -0.03990 -0.04590 168 LEU A CD1 
1365 C CD2 . LEU A 168 ? 0.37440 0.28230 0.36240 -0.10190 -0.06560 -0.02800 168 LEU A CD2 
1366 N N   . ARG A 169 ? 0.62780 0.48910 0.48660 -0.06890 -0.05590 -0.07140 169 ARG A N   
1367 C CA  . ARG A 169 ? 0.66760 0.48320 0.47490 -0.05720 -0.05550 -0.08870 169 ARG A CA  
1368 C C   . ARG A 169 ? 0.69230 0.52010 0.49110 -0.02920 -0.03280 -0.09120 169 ARG A C   
1369 O O   . ARG A 169 ? 0.70650 0.51270 0.48720 -0.01020 -0.02270 -0.09890 169 ARG A O   
1370 C CB  . ARG A 169 ? 0.70680 0.48710 0.46050 -0.07020 -0.07340 -0.09580 169 ARG A CB  
1371 C CG  . ARG A 169 ? 0.69610 0.46430 0.45220 -0.10240 -0.10000 -0.09050 169 ARG A CG  
1372 C CD  . ARG A 169 ? 0.76280 0.48570 0.45300 -0.11750 -0.11930 -0.09940 169 ARG A CD  
1373 N NE  . ARG A 169 ? 0.79280 0.52580 0.45540 -0.10980 -0.11590 -0.10030 169 ARG A NE  
1374 C CZ  . ARG A 169 ? 0.79610 0.55760 0.46250 -0.12940 -0.13250 -0.08730 169 ARG A CZ  
1375 N NH1 . ARG A 169 ? 0.77600 0.56140 0.47200 -0.15850 -0.15460 -0.07070 169 ARG A NH1 
1376 N NH2 . ARG A 169 ? 0.81600 0.58900 0.46010 -0.11710 -0.12480 -0.08680 169 ARG A NH2 
1377 N N   . ARG A 170 ? 0.54730 0.41350 0.36070 -0.02550 -0.02370 -0.08130 170 ARG A N   
1378 C CA  . ARG A 170 ? 0.57150 0.46250 0.38530 -0.00200 -0.00230 -0.07750 170 ARG A CA  
1379 C C   . ARG A 170 ? 0.54500 0.46480 0.40150 0.00190  0.00740  -0.07000 170 ARG A C   
1380 O O   . ARG A 170 ? 0.55390 0.48120 0.40410 0.02390  0.02120  -0.06910 170 ARG A O   
1381 C CB  . ARG A 170 ? 0.57660 0.50290 0.39870 -0.00400 0.00400  -0.06580 170 ARG A CB  
1382 C CG  . ARG A 170 ? 0.61230 0.51520 0.38030 0.00400  0.00220  -0.07240 170 ARG A CG  
1383 C CD  . ARG A 170 ? 0.62600 0.56870 0.40310 0.00730  0.01330  -0.05840 170 ARG A CD  
1384 N NE  . ARG A 170 ? 0.61700 0.57550 0.41970 -0.01510 0.00130  -0.04830 170 ARG A NE  
1385 C CZ  . ARG A 170 ? 0.63250 0.57590 0.40990 -0.02580 -0.01430 -0.04960 170 ARG A CZ  
1386 N NH1 . ARG A 170 ? 0.65980 0.56570 0.37910 -0.02040 -0.02160 -0.06300 170 ARG A NH1 
1387 N NH2 . ARG A 170 ? 0.60830 0.57200 0.41510 -0.04200 -0.02290 -0.03570 170 ARG A NH2 
1388 N N   . TYR A 171 ? 0.44920 0.38500 0.34550 -0.01750 0.00100  -0.06280 171 TYR A N   
1389 C CA  . TYR A 171 ? 0.43120 0.38960 0.36040 -0.01770 0.00740  -0.05620 171 TYR A CA  
1390 C C   . TYR A 171 ? 0.43310 0.36600 0.35280 -0.00660 0.00600  -0.06510 171 TYR A C   
1391 O O   . TYR A 171 ? 0.44160 0.39560 0.37400 0.00560  0.01530  -0.05970 171 TYR A O   
1392 C CB  . TYR A 171 ? 0.38310 0.34870 0.34260 -0.03900 0.00200  -0.04840 171 TYR A CB  
1393 C CG  . TYR A 171 ? 0.38940 0.37290 0.35530 -0.04880 0.00560  -0.03750 171 TYR A CG  
1394 C CD1 . TYR A 171 ? 0.42350 0.43430 0.38540 -0.04310 0.01560  -0.03030 171 TYR A CD1 
1395 C CD2 . TYR A 171 ? 0.35020 0.32350 0.32520 -0.06130 0.00090  -0.03160 171 TYR A CD2 
1396 C CE1 . TYR A 171 ? 0.41600 0.43820 0.38110 -0.05330 0.01920  -0.01910 171 TYR A CE1 
1397 C CE2 . TYR A 171 ? 0.35230 0.33460 0.32850 -0.06720 0.00610  -0.02040 171 TYR A CE2 
1398 C CZ  . TYR A 171 ? 0.38110 0.38500 0.35120 -0.06490 0.01430  -0.01510 171 TYR A CZ  
1399 O OH  . TYR A 171 ? 0.37370 0.38120 0.34210 -0.07180 0.01960  -0.00290 171 TYR A OH  
1400 N N   . LEU A 172 ? 0.54470 0.43400 0.44180 -0.01220 -0.00640 -0.07620 172 LEU A N   
1401 C CA  . LEU A 172 ? 0.54470 0.40060 0.42670 -0.00270 -0.00760 -0.08440 172 LEU A CA  
1402 C C   . LEU A 172 ? 0.58950 0.43050 0.43410 0.02810  0.00690  -0.08900 172 LEU A C   
1403 O O   . LEU A 172 ? 0.59850 0.43580 0.44350 0.04580  0.01540  -0.08770 172 LEU A O   
1404 C CB  . LEU A 172 ? 0.53160 0.34210 0.39280 -0.02050 -0.02580 -0.09280 172 LEU A CB  
1405 C CG  . LEU A 172 ? 0.47880 0.30830 0.38150 -0.04360 -0.03580 -0.08320 172 LEU A CG  
1406 C CD1 . LEU A 172 ? 0.47480 0.27990 0.36400 -0.06510 -0.05510 -0.08360 172 LEU A CD1 
1407 C CD2 . LEU A 172 ? 0.45370 0.28650 0.38100 -0.04060 -0.03160 -0.08040 172 LEU A CD2 
1408 N N   . GLU A 173 ? 0.64270 0.47530 0.45230 0.03810  0.01190  -0.09250 173 GLU A N   
1409 C CA  . GLU A 173 ? 0.67370 0.49750 0.44660 0.07410  0.03170  -0.09270 173 GLU A CA  
1410 C C   . GLU A 173 ? 0.65860 0.55360 0.47630 0.08960  0.04920  -0.07290 173 GLU A C   
1411 O O   . GLU A 173 ? 0.67070 0.57250 0.48370 0.11820  0.06420  -0.06630 173 GLU A O   
1412 C CB  . GLU A 173 ? 0.71430 0.51550 0.43740 0.08160  0.03460  -0.09910 173 GLU A CB  
1413 C CG  . GLU A 173 ? 0.75520 0.47850 0.41450 0.07020  0.01830  -0.11810 173 GLU A CG  
1414 C CD  . GLU A 173 ? 0.80780 0.50980 0.41140 0.07960  0.02230  -0.12350 173 GLU A CD  
1415 O OE1 . GLU A 173 ? 0.78240 0.53920 0.41580 0.07640  0.02700  -0.11180 173 GLU A OE1 
1416 O OE2 . GLU A 173 ? 0.87120 0.49590 0.39520 0.08970  0.02100  -0.13950 173 GLU A OE2 
1417 N N   . ASN A 174 ? 0.54960 0.49850 0.40870 0.07020  0.04720  -0.06050 174 ASN A N   
1418 C CA  . ASN A 174 ? 0.52760 0.54650 0.42660 0.07690  0.06010  -0.03870 174 ASN A CA  
1419 C C   . ASN A 174 ? 0.51070 0.54840 0.43960 0.07760  0.05910  -0.03150 174 ASN A C   
1420 O O   . ASN A 174 ? 0.49900 0.58210 0.44300 0.09860  0.07280  -0.01400 174 ASN A O   
1421 C CB  . ASN A 174 ? 0.50770 0.56580 0.44080 0.04740  0.05410  -0.02800 174 ASN A CB  
1422 C CG  . ASN A 174 ? 0.52240 0.58000 0.43260 0.05010  0.05880  -0.02790 174 ASN A CG  
1423 O OD1 . ASN A 174 ? 0.54250 0.58600 0.41460 0.07740  0.07070  -0.03120 174 ASN A OD1 
1424 N ND2 . ASN A 174 ? 0.52210 0.59050 0.45030 0.02380  0.05090  -0.02340 174 ASN A ND2 
1425 N N   . GLY A 175 ? 0.46610 0.47560 0.40580 0.05530  0.04340  -0.04120 175 GLY A N   
1426 C CA  . GLY A 175 ? 0.45330 0.47940 0.41970 0.05280  0.04080  -0.03440 175 GLY A CA  
1427 C C   . GLY A 175 ? 0.46430 0.43620 0.40500 0.06670  0.03850  -0.04740 175 GLY A C   
1428 O O   . GLY A 175 ? 0.45170 0.41760 0.41010 0.05490  0.03010  -0.04780 175 GLY A O   
1429 N N   . LYS A 176 ? 0.59840 0.52530 0.49160 0.09160  0.04660  -0.05760 176 LYS A N   
1430 C CA  . LYS A 176 ? 0.61130 0.47120 0.46940 0.09960  0.04240  -0.07150 176 LYS A CA  
1431 C C   . LYS A 176 ? 0.60280 0.47920 0.48180 0.11360  0.04780  -0.06110 176 LYS A C   
1432 O O   . LYS A 176 ? 0.58520 0.43360 0.46970 0.09920  0.03650  -0.06690 176 LYS A O   
1433 C CB  . LYS A 176 ? 0.65430 0.45550 0.44520 0.12780  0.05330  -0.08260 176 LYS A CB  
1434 C CG  . LYS A 176 ? 0.67290 0.39160 0.41760 0.13050  0.04700  -0.09750 176 LYS A CG  
1435 C CD  . LYS A 176 ? 0.74230 0.38310 0.40500 0.15060  0.05400  -0.11210 176 LYS A CD  
1436 C CE  . LYS A 176 ? 0.77870 0.35840 0.41590 0.13650  0.04170  -0.11710 176 LYS A CE  
1437 N NZ  . LYS A 176 ? 0.85410 0.37380 0.42530 0.14540  0.04460  -0.12180 176 LYS A NZ  
1438 N N   . GLU A 177 ? 0.75410 0.68340 0.64810 0.14130  0.06490  -0.04220 177 GLU A N   
1439 C CA  . GLU A 177 ? 0.74810 0.69930 0.65890 0.16040  0.07170  -0.02810 177 GLU A CA  
1440 C C   . GLU A 177 ? 0.73020 0.71910 0.68990 0.12800  0.05550  -0.02130 177 GLU A C   
1441 O O   . GLU A 177 ? 0.72130 0.72060 0.69250 0.13850  0.05680  -0.01180 177 GLU A O   
1442 C CB  . GLU A 177 ? 0.74790 0.76240 0.66880 0.19790  0.09410  -0.00290 177 GLU A CB  
1443 C CG  . GLU A 177 ? 0.78630 0.76450 0.65210 0.23620  0.11530  -0.00730 177 GLU A CG  
1444 C CD  . GLU A 177 ? 0.80510 0.79810 0.66900 0.21890  0.11290  -0.01210 177 GLU A CD  
1445 O OE1 . GLU A 177 ? 0.76350 0.80400 0.67350 0.18040  0.09760  -0.00770 177 GLU A OE1 
1446 O OE2 . GLU A 177 ? 0.82520 0.77570 0.63500 0.24500  0.12710  -0.02030 177 GLU A OE2 
1447 N N   . THR A 178 ? 0.49030 0.49460 0.47290 0.09100  0.04160  -0.02520 178 THR A N   
1448 C CA  . THR A 178 ? 0.48280 0.49910 0.49460 0.06130  0.02740  -0.02300 178 THR A CA  
1449 C C   . THR A 178 ? 0.47460 0.43890 0.47700 0.03680  0.01470  -0.04030 178 THR A C   
1450 O O   . THR A 178 ? 0.45280 0.40380 0.46480 0.02400  0.00690  -0.04140 178 THR A O   
1451 C CB  . THR A 178 ? 0.46680 0.54670 0.51180 0.03790  0.02300  -0.00700 178 THR A CB  
1452 O OG1 . THR A 178 ? 0.46600 0.54530 0.50660 0.02440  0.02280  -0.01160 178 THR A OG1 
1453 C CG2 . THR A 178 ? 0.44120 0.59020 0.50660 0.05680  0.03240  0.01810  178 THR A CG2 
1454 N N   . LEU A 179 ? 0.55510 0.49560 0.54050 0.03040  0.01290  -0.05070 179 LEU A N   
1455 C CA  . LEU A 179 ? 0.51090 0.41650 0.49410 0.00740  0.00100  -0.06050 179 LEU A CA  
1456 C C   . LEU A 179 ? 0.50540 0.35580 0.46320 0.01150  -0.00440 -0.07100 179 LEU A C   
1457 O O   . LEU A 179 ? 0.46280 0.29500 0.42910 -0.00660 -0.01400 -0.07240 179 LEU A O   
1458 C CB  . LEU A 179 ? 0.50800 0.41500 0.48400 -0.00240 -0.00080 -0.06380 179 LEU A CB  
1459 C CG  . LEU A 179 ? 0.50380 0.45580 0.50200 -0.01380 0.00270  -0.05300 179 LEU A CG  
1460 C CD1 . LEU A 179 ? 0.50220 0.45060 0.48960 -0.02020 0.00180  -0.05560 179 LEU A CD1 
1461 C CD2 . LEU A 179 ? 0.45600 0.41290 0.47510 -0.03440 -0.00270 -0.04760 179 LEU A CD2 
1462 N N   . GLN A 180 ? 0.59920 0.41880 0.52150 0.03460  0.00240  -0.07700 180 GLN A N   
1463 C CA  . GLN A 180 ? 0.61150 0.36560 0.49810 0.03360  -0.00460 -0.08780 180 GLN A CA  
1464 C C   . GLN A 180 ? 0.62990 0.36140 0.50210 0.05760  0.00420  -0.08540 180 GLN A C   
1465 O O   . GLN A 180 ? 0.66190 0.32800 0.48780 0.06530  0.00350  -0.09470 180 GLN A O   
1466 C CB  . GLN A 180 ? 0.64720 0.35580 0.48270 0.03730  -0.00620 -0.10000 180 GLN A CB  
1467 C CG  . GLN A 180 ? 0.62660 0.36030 0.47280 0.01790  -0.01360 -0.10040 180 GLN A CG  
1468 C CD  . GLN A 180 ? 0.67050 0.35380 0.45980 0.01840  -0.01830 -0.11270 180 GLN A CD  
1469 O OE1 . GLN A 180 ? 0.68930 0.32950 0.45180 0.00850  -0.02740 -0.11700 180 GLN A OE1 
1470 N NE2 . GLN A 180 ? 0.68760 0.39250 0.46720 0.02830  -0.01050 -0.11250 180 GLN A NE2 
1471 N N   . ARG A 181 ? 0.92020 0.70110 0.82560 0.06930  0.01220  -0.07200 181 ARG A N   
1472 C CA  . ARG A 181 ? 0.93610 0.70300 0.83400 0.09190  0.01980  -0.06570 181 ARG A CA  
1473 C C   . ARG A 181 ? 0.90640 0.69860 0.84280 0.07160  0.01050  -0.05840 181 ARG A C   
1474 O O   . ARG A 181 ? 0.91260 0.76340 0.88410 0.06430  0.01010  -0.04730 181 ARG A O   
1475 C CB  . ARG A 181 ? 0.96160 0.77030 0.86140 0.12860  0.03830  -0.05110 181 ARG A CB  
1476 C CG  . ARG A 181 ? 1.00230 0.77870 0.85410 0.15870  0.05350  -0.05650 181 ARG A CG  
1477 C CD  . ARG A 181 ? 1.04980 0.73030 0.83630 0.17780  0.05860  -0.06920 181 ARG A CD  
1478 N NE  . ARG A 181 ? 1.06880 0.69510 0.82170 0.14800  0.04350  -0.08720 181 ARG A NE  
1479 C CZ  . ARG A 181 ? 1.10130 0.70540 0.81460 0.15460  0.04810  -0.09360 181 ARG A CZ  
1480 N NH1 . ARG A 181 ? 1.13480 0.76000 0.83290 0.19330  0.07020  -0.08480 181 ARG A NH1 
1481 N NH2 . ARG A 181 ? 1.11140 0.67910 0.80270 0.12190  0.03050  -0.10550 181 ARG A NH2 
1482 N N   . ALA A 182 ? 0.58870 0.33370 0.51390 0.06030  0.00260  -0.06370 182 ALA A N   
1483 C CA  . ALA A 182 ? 0.56040 0.32250 0.51560 0.04400  -0.00400 -0.05640 182 ALA A CA  
1484 C C   . ALA A 182 ? 0.58360 0.37380 0.54920 0.06570  0.00400  -0.04330 182 ALA A C   
1485 O O   . ALA A 182 ? 0.61460 0.37660 0.55530 0.09250  0.01290  -0.04130 182 ALA A O   
1486 C CB  . ALA A 182 ? 0.54610 0.25430 0.48690 0.02780  -0.01320 -0.06150 182 ALA A CB  
1487 N N   . ASP A 183 ? 0.52250 0.36640 0.52000 0.05470  0.00090  -0.03320 183 ASP A N   
1488 C CA  . ASP A 183 ? 0.54630 0.42480 0.55650 0.06870  0.00390  -0.01760 183 ASP A CA  
1489 C C   . ASP A 183 ? 0.52970 0.38420 0.54170 0.05810  -0.00190 -0.01640 183 ASP A C   
1490 O O   . ASP A 183 ? 0.50410 0.35940 0.52630 0.03300  -0.00920 -0.01930 183 ASP A O   
1491 C CB  . ASP A 183 ? 0.55400 0.50040 0.59040 0.05630  0.00010  -0.00580 183 ASP A CB  
1492 C CG  . ASP A 183 ? 0.58140 0.56540 0.62180 0.06910  0.00760  -0.00040 183 ASP A CG  
1493 O OD1 . ASP A 183 ? 0.59420 0.56040 0.61550 0.09980  0.02000  -0.00080 183 ASP A OD1 
1494 O OD2 . ASP A 183 ? 0.58380 0.61180 0.64210 0.04870  0.00200  0.00550  183 ASP A OD2 
1495 N N   . PRO A 184 ? 0.50600 0.33690 0.50550 0.07850  0.00310  -0.01040 184 PRO A N   
1496 C CA  . PRO A 184 ? 0.49170 0.29770 0.49170 0.06820  -0.00160 -0.00830 184 PRO A CA  
1497 C C   . PRO A 184 ? 0.49780 0.35130 0.51740 0.05810  -0.00690 0.00340  184 PRO A C   
1498 O O   . PRO A 184 ? 0.52220 0.42910 0.55400 0.06340  -0.00760 0.01410  184 PRO A O   
1499 C CB  . PRO A 184 ? 0.51710 0.28210 0.49300 0.09590  0.00670  -0.00380 184 PRO A CB  
1500 C CG  . PRO A 184 ? 0.53820 0.33020 0.50840 0.12720  0.01780  0.00360  184 PRO A CG  
1501 C CD  . PRO A 184 ? 0.53070 0.35240 0.51080 0.11560  0.01590  -0.00380 184 PRO A CD  
1502 N N   . PRO A 185 ? 0.51250 0.34910 0.53280 0.04200  -0.01130 0.00360  185 PRO A N   
1503 C CA  . PRO A 185 ? 0.52580 0.39510 0.55140 0.03230  -0.01680 0.01360  185 PRO A CA  
1504 C C   . PRO A 185 ? 0.56120 0.44870 0.58630 0.05330  -0.01540 0.02920  185 PRO A C   
1505 O O   . PRO A 185 ? 0.55890 0.41420 0.57510 0.07360  -0.00850 0.03170  185 PRO A O   
1506 C CB  . PRO A 185 ? 0.49110 0.32710 0.51050 0.01530  -0.01740 0.00950  185 PRO A CB  
1507 C CG  . PRO A 185 ? 0.47470 0.26680 0.49130 0.02150  -0.01290 0.00520  185 PRO A CG  
1508 C CD  . PRO A 185 ? 0.48000 0.26770 0.49360 0.03160  -0.01140 -0.00260 185 PRO A CD  
1509 N N   . LYS A 186 ? 0.49060 0.43000 0.52290 0.04710  -0.02300 0.04180  186 LYS A N   
1510 C CA  . LYS A 186 ? 0.50810 0.47210 0.54070 0.06110  -0.02500 0.06030  186 LYS A CA  
1511 C C   . LYS A 186 ? 0.51520 0.45280 0.53230 0.04340  -0.03020 0.05850  186 LYS A C   
1512 O O   . LYS A 186 ? 0.51190 0.44200 0.51880 0.01700  -0.03630 0.04990  186 LYS A O   
1513 C CB  . LYS A 186 ? 0.50560 0.54600 0.55380 0.05900  -0.03360 0.07920  186 LYS A CB  
1514 N N   . THR A 187 ? 0.54900 0.46610 0.55950 0.06010  -0.02560 0.06700  187 THR A N   
1515 C CA  . THR A 187 ? 0.54950 0.43180 0.54380 0.04870  -0.02570 0.06520  187 THR A CA  
1516 C C   . THR A 187 ? 0.57490 0.47720 0.56050 0.05690  -0.03010 0.08330  187 THR A C   
1517 O O   . THR A 187 ? 0.57710 0.50640 0.57170 0.08050  -0.02860 0.09880  187 THR A O   
1518 C CB  . THR A 187 ? 0.52870 0.35530 0.52160 0.05600  -0.01500 0.05820  187 THR A CB  
1519 O OG1 . THR A 187 ? 0.53540 0.34970 0.52890 0.08270  -0.00850 0.06540  187 THR A OG1 
1520 C CG2 . THR A 187 ? 0.49170 0.29980 0.49080 0.04240  -0.01330 0.04210  187 THR A CG2 
1521 N N   . HIS A 188 ? 0.53330 0.42020 0.49740 0.03980  -0.03410 0.08260  188 HIS A N   
1522 C CA  . HIS A 188 ? 0.55270 0.44780 0.50180 0.04600  -0.03790 0.09850  188 HIS A CA  
1523 C C   . HIS A 188 ? 0.56470 0.42020 0.48300 0.03010  -0.03560 0.09250  188 HIS A C   
1524 O O   . HIS A 188 ? 0.55910 0.38840 0.46750 0.01480  -0.03180 0.07820  188 HIS A O   
1525 C CB  . HIS A 188 ? 0.56290 0.52180 0.51280 0.03990  -0.05430 0.11440  188 HIS A CB  
1526 C CG  . HIS A 188 ? 0.57650 0.54510 0.50370 0.00430  -0.06920 0.10700  188 HIS A CG  
1527 N ND1 . HIS A 188 ? 0.56870 0.55040 0.50540 -0.01220 -0.07310 0.09660  188 HIS A ND1 
1528 C CD2 . HIS A 188 ? 0.59740 0.55620 0.48470 -0.01900 -0.08100 0.10840  188 HIS A CD2 
1529 C CE1 . HIS A 188 ? 0.57950 0.55640 0.48320 -0.04530 -0.08690 0.09220  188 HIS A CE1 
1530 N NE2 . HIS A 188 ? 0.60290 0.56270 0.47280 -0.05040 -0.09220 0.09830  188 HIS A NE2 
1531 N N   . VAL A 189 ? 0.62230 0.47420 0.52270 0.03710  -0.03610 0.10570  189 VAL A N   
1532 C CA  . VAL A 189 ? 0.64530 0.45810 0.51100 0.02910  -0.03030 0.10380  189 VAL A CA  
1533 C C   . VAL A 189 ? 0.68460 0.51610 0.51320 0.01600  -0.04580 0.11250  189 VAL A C   
1534 O O   . VAL A 189 ? 0.68930 0.56050 0.52610 0.02510  -0.05550 0.12950  189 VAL A O   
1535 C CB  . VAL A 189 ? 0.63280 0.41520 0.50610 0.04880  -0.01480 0.11320  189 VAL A CB  
1536 C CG1 . VAL A 189 ? 0.65430 0.40140 0.49190 0.04430  -0.00530 0.11490  189 VAL A CG1 
1537 C CG2 . VAL A 189 ? 0.59670 0.35980 0.50210 0.05470  -0.00440 0.10610  189 VAL A CG2 
1538 N N   . THR A 190 ? 0.69720 0.49740 0.48020 -0.00490 -0.04810 0.10220  190 THR A N   
1539 C CA  . THR A 190 ? 0.72820 0.52940 0.46010 -0.02240 -0.06390 0.10830  190 THR A CA  
1540 C C   . THR A 190 ? 0.75590 0.50180 0.44170 -0.01430 -0.04890 0.10860  190 THR A C   
1541 O O   . THR A 190 ? 0.74660 0.45620 0.43980 -0.00000 -0.02660 0.10370  190 THR A O   
1542 C CB  . THR A 190 ? 0.75150 0.54940 0.44850 -0.05700 -0.08080 0.09680  190 THR A CB  
1543 O OG1 . THR A 190 ? 0.76370 0.49970 0.43170 -0.06100 -0.06470 0.07860  190 THR A OG1 
1544 C CG2 . THR A 190 ? 0.70920 0.56800 0.45520 -0.06400 -0.09350 0.09990  190 THR A CG2 
1545 N N   . HIS A 191 ? 0.79550 0.53950 0.43270 -0.02460 -0.06210 0.11700  191 HIS A N   
1546 C CA  . HIS A 191 ? 0.82910 0.52750 0.41720 -0.01400 -0.04930 0.12190  191 HIS A CA  
1547 C C   . HIS A 191 ? 0.88360 0.54860 0.38760 -0.04280 -0.06590 0.11520  191 HIS A C   
1548 O O   . HIS A 191 ? 0.88670 0.59170 0.38130 -0.06750 -0.09460 0.12130  191 HIS A O   
1549 C CB  . HIS A 191 ? 0.81770 0.55000 0.43170 0.00760  -0.04980 0.14400  191 HIS A CB  
1550 C CG  . HIS A 191 ? 0.85170 0.54380 0.42000 0.02090  -0.03590 0.15270  191 HIS A CG  
1551 N ND1 . HIS A 191 ? 0.90570 0.57950 0.40240 0.00630  -0.04920 0.15560  191 HIS A ND1 
1552 C CD2 . HIS A 191 ? 0.84090 0.51020 0.42450 0.04640  -0.01080 0.16170  191 HIS A CD2 
1553 C CE1 . HIS A 191 ? 0.91890 0.55840 0.38680 0.02610  -0.03030 0.16480  191 HIS A CE1 
1554 N NE2 . HIS A 191 ? 0.88200 0.52170 0.40520 0.05050  -0.00660 0.17010  191 HIS A NE2 
1555 N N   . HIS A 192 ? 1.00860 0.59990 0.44790 -0.04040 -0.04790 0.10470  192 HIS A N   
1556 C CA  . HIS A 192 ? 1.07240 0.61440 0.41370 -0.06530 -0.06190 0.09870  192 HIS A CA  
1557 C C   . HIS A 192 ? 1.11680 0.58900 0.39410 -0.04230 -0.03490 0.09970  192 HIS A C   
1558 O O   . HIS A 192 ? 1.10680 0.54460 0.39330 -0.01800 -0.00330 0.09530  192 HIS A O   
1559 C CB  . HIS A 192 ? 1.10090 0.60630 0.39910 -0.09760 -0.07320 0.07920  192 HIS A CB  
1560 C CG  . HIS A 192 ? 1.07270 0.65030 0.42690 -0.12340 -0.10110 0.08170  192 HIS A CG  
1561 N ND1 . HIS A 192 ? 1.03460 0.64030 0.45640 -0.11700 -0.09300 0.07530  192 HIS A ND1 
1562 C CD2 . HIS A 192 ? 1.06120 0.69710 0.41860 -0.15300 -0.13590 0.09400  192 HIS A CD2 
1563 C CE1 . HIS A 192 ? 0.99550 0.66830 0.45540 -0.13990 -0.11950 0.08220  192 HIS A CE1 
1564 N NE2 . HIS A 192 ? 1.01580 0.71250 0.44120 -0.16200 -0.14570 0.09530  192 HIS A NE2 
1565 N N   . PRO A 193 ? 1.15340 0.62100 0.38810 -0.04720 -0.04460 0.10410  193 PRO A N   
1566 C CA  . PRO A 193 ? 1.19370 0.60840 0.38550 -0.02330 -0.01730 0.10130  193 PRO A CA  
1567 C C   . PRO A 193 ? 1.25360 0.59010 0.38260 -0.02980 -0.00440 0.07740  193 PRO A C   
1568 O O   . PRO A 193 ? 1.27420 0.59070 0.37140 -0.06360 -0.02570 0.06240  193 PRO A O   
1569 C CB  . PRO A 193 ? 1.23550 0.66770 0.39370 -0.03450 -0.03820 0.11090  193 PRO A CB  
1570 C CG  . PRO A 193 ? 1.20320 0.71230 0.40370 -0.05800 -0.07380 0.12410  193 PRO A CG  
1571 C CD  . PRO A 193 ? 1.17170 0.68720 0.39810 -0.07630 -0.08160 0.11220  193 PRO A CD  
1572 N N   . ILE A 194 ? 1.34750 0.64190 0.46380 0.00430  0.03170  0.07640  194 ILE A N   
1573 C CA  . ILE A 194 ? 1.41500 0.62490 0.46260 0.00860  0.04920  0.05780  194 ILE A CA  
1574 C C   . ILE A 194 ? 1.50450 0.66620 0.48890 0.02410  0.06190  0.05850  194 ILE A C   
1575 O O   . ILE A 194 ? 1.58870 0.66790 0.50300 0.02800  0.07470  0.04460  194 ILE A O   
1576 C CB  . ILE A 194 ? 1.39070 0.58920 0.47340 0.03930  0.08350  0.05630  194 ILE A CB  
1577 C CG1 . ILE A 194 ? 1.37700 0.59640 0.49520 0.08210  0.11730  0.07360  194 ILE A CG1 
1578 C CG2 . ILE A 194 ? 1.31120 0.56710 0.46670 0.02810  0.07280  0.05980  194 ILE A CG2 
1579 C CD1 . ILE A 194 ? 1.33520 0.57060 0.50720 0.11040  0.14830  0.07780  194 ILE A CD1 
1580 N N   . SER A 195 ? 1.36560 0.57140 0.37020 0.03440  0.05940  0.07590  195 SER A N   
1581 C CA  . SER A 195 ? 1.44360 0.61160 0.39070 0.04860  0.06980  0.07890  195 SER A CA  
1582 C C   . SER A 195 ? 1.40510 0.64210 0.38920 0.04860  0.05520  0.10030  195 SER A C   
1583 O O   . SER A 195 ? 1.33800 0.63970 0.37520 0.03150  0.03130  0.10990  195 SER A O   
1584 C CB  . SER A 195 ? 1.46310 0.59540 0.40820 0.09430  0.11480  0.08230  195 SER A CB  
1585 O OG  . SER A 195 ? 1.36900 0.57200 0.40590 0.11950  0.13310  0.10230  195 SER A OG  
1586 N N   . ASP A 196 ? 1.47860 0.70270 0.43650 0.07020  0.07050  0.11010  196 ASP A N   
1587 C CA  . ASP A 196 ? 1.44230 0.73010 0.43900 0.07480  0.06080  0.13330  196 ASP A CA  
1588 C C   . ASP A 196 ? 1.36380 0.69760 0.44470 0.10810  0.08840  0.15370  196 ASP A C   
1589 O O   . ASP A 196 ? 1.34050 0.71760 0.45430 0.11700  0.08650  0.17450  196 ASP A O   
1590 C CB  . ASP A 196 ? 1.53320 0.78850 0.45790 0.07580  0.05850  0.13520  196 ASP A CB  
1591 C CG  . ASP A 196 ? 1.56810 0.84830 0.46100 0.03690  0.01510  0.13570  196 ASP A CG  
1592 O OD1 . ASP A 196 ? 1.50060 0.84210 0.44350 0.01600  -0.01130 0.14240  196 ASP A OD1 
1593 O OD2 . ASP A 196 ? 1.66150 0.90370 0.48110 0.02800  0.00740  0.13150  196 ASP A OD2 
1594 N N   . HIS A 197 ? 1.29670 0.62360 0.41490 0.12500  0.11340  0.14930  197 HIS A N   
1595 C CA  . HIS A 197 ? 1.22160 0.59960 0.42760 0.14870  0.13520  0.16880  197 HIS A CA  
1596 C C   . HIS A 197 ? 1.15160 0.55060 0.41950 0.14810  0.14190  0.16450  197 HIS A C   
1597 O O   . HIS A 197 ? 1.09240 0.53440 0.43540 0.16270  0.15810  0.17930  197 HIS A O   
1598 C CB  . HIS A 197 ? 1.25990 0.62150 0.45610 0.18160  0.17010  0.17840  197 HIS A CB  
1599 C CG  . HIS A 197 ? 1.31820 0.62000 0.46400 0.19840  0.19450  0.16320  197 HIS A CG  
1600 N ND1 . HIS A 197 ? 1.42350 0.65040 0.47020 0.20000  0.19600  0.14860  197 HIS A ND1 
1601 C CD2 . HIS A 197 ? 1.29200 0.59590 0.47170 0.21570  0.21840  0.16180  197 HIS A CD2 
1602 C CE1 . HIS A 197 ? 1.46320 0.64100 0.48250 0.22050  0.22130  0.13860  197 HIS A CE1 
1603 N NE2 . HIS A 197 ? 1.38200 0.61000 0.48250 0.23130  0.23560  0.14710  197 HIS A NE2 
1604 N N   . GLU A 198 ? 1.08070 0.59620 0.35170 0.09020  0.15600  0.07080  198 GLU A N   
1605 C CA  . GLU A 198 ? 1.02330 0.58790 0.37610 0.08520  0.15360  0.06510  198 GLU A CA  
1606 C C   . GLU A 198 ? 0.99920 0.55520 0.37420 0.08840  0.11420  0.05550  198 GLU A C   
1607 O O   . GLU A 198 ? 1.01050 0.53660 0.34510 0.09700  0.09210  0.04670  198 GLU A O   
1608 C CB  . GLU A 198 ? 1.01100 0.61760 0.39080 0.09990  0.17820  0.05400  198 GLU A CB  
1609 C CG  . GLU A 198 ? 1.02960 0.67970 0.41840 0.09480  0.22050  0.06540  198 GLU A CG  
1610 C CD  . GLU A 198 ? 1.01580 0.72040 0.43940 0.11780  0.24340  0.05600  198 GLU A CD  
1611 O OE1 . GLU A 198 ? 1.03570 0.71100 0.41550 0.14650  0.24670  0.04270  198 GLU A OE1 
1612 O OE2 . GLU A 198 ? 0.98520 0.75970 0.47560 0.10800  0.25730  0.06220  198 GLU A OE2 
1613 N N   . ALA A 199 ? 0.90510 0.49040 0.34280 0.07850  0.10590  0.05720  199 ALA A N   
1614 C CA  . ALA A 199 ? 0.87050 0.46050 0.33920 0.08090  0.07330  0.04930  199 ALA A CA  
1615 C C   . ALA A 199 ? 0.82650 0.46210 0.36600 0.07620  0.07790  0.04320  199 ALA A C   
1616 O O   . ALA A 199 ? 0.82110 0.48570 0.38950 0.06640  0.10120  0.04890  199 ALA A O   
1617 C CB  . ALA A 199 ? 0.87210 0.43940 0.32970 0.07830  0.05230  0.06120  199 ALA A CB  
1618 N N   . THR A 200 ? 0.77960 0.42490 0.34530 0.08060  0.05480  0.03240  200 THR A N   
1619 C CA  . THR A 200 ? 0.74430 0.42820 0.37230 0.07710  0.05360  0.02720  200 THR A CA  
1620 C C   . THR A 200 ? 0.72060 0.40840 0.37650 0.06900  0.03630  0.03240  200 THR A C   
1621 O O   . THR A 200 ? 0.71700 0.39020 0.35830 0.07370  0.01330  0.03300  200 THR A O   
1622 C CB  . THR A 200 ? 0.73430 0.41980 0.36760 0.08590  0.04140  0.01330  200 THR A CB  
1623 O OG1 . THR A 200 ? 0.76830 0.43610 0.36280 0.09900  0.05880  0.00730  200 THR A OG1 
1624 C CG2 . THR A 200 ? 0.70440 0.42910 0.39790 0.08400  0.04160  0.00990  200 THR A CG2 
1625 N N   . LEU A 201 ? 0.66910 0.37890 0.36240 0.05750  0.04750  0.03610  201 LEU A N   
1626 C CA  . LEU A 201 ? 0.63810 0.35130 0.36020 0.05240  0.03330  0.03660  201 LEU A CA  
1627 C C   . LEU A 201 ? 0.60620 0.35850 0.37740 0.05310  0.02740  0.02610  201 LEU A C   
1628 O O   . LEU A 201 ? 0.61090 0.39360 0.40470 0.05060  0.04230  0.02330  201 LEU A O   
1629 C CB  . LEU A 201 ? 0.65520 0.35560 0.37580 0.03420  0.04780  0.04590  201 LEU A CB  
1630 C CG  . LEU A 201 ? 0.69880 0.34920 0.36240 0.03170  0.05550  0.05920  201 LEU A CG  
1631 C CD1 . LEU A 201 ? 0.72170 0.34940 0.37670 0.00610  0.07080  0.06830  201 LEU A CD1 
1632 C CD2 . LEU A 201 ? 0.70530 0.32210 0.33900 0.05270  0.03200  0.06250  201 LEU A CD2 
1633 N N   . ARG A 202 ? 0.67210 0.42810 0.45860 0.05840  0.00660  0.02170  202 ARG A N   
1634 C CA  . ARG A 202 ? 0.63520 0.42250 0.46170 0.05810  -0.00010 0.01310  202 ARG A CA  
1635 C C   . ARG A 202 ? 0.60320 0.39720 0.45350 0.05500  -0.00920 0.01330  202 ARG A C   
1636 O O   . ARG A 202 ? 0.59850 0.38020 0.43700 0.06340  -0.02230 0.01620  202 ARG A O   
1637 C CB  . ARG A 202 ? 0.63310 0.41880 0.44940 0.06460  -0.01480 0.00630  202 ARG A CB  
1638 C CG  . ARG A 202 ? 0.60000 0.40970 0.44970 0.06300  -0.02050 -0.00060 202 ARG A CG  
1639 C CD  . ARG A 202 ? 0.61350 0.40930 0.44200 0.06250  -0.03250 -0.00700 202 ARG A CD  
1640 N NE  . ARG A 202 ? 0.64640 0.41620 0.44200 0.07030  -0.01980 -0.01080 202 ARG A NE  
1641 C CZ  . ARG A 202 ? 0.69400 0.43120 0.44200 0.07160  -0.02060 -0.01230 202 ARG A CZ  
1642 N NH1 . ARG A 202 ? 0.69610 0.42800 0.42640 0.06430  -0.03660 -0.00950 202 ARG A NH1 
1643 N NH2 . ARG A 202 ? 0.71690 0.42750 0.43130 0.08350  -0.00490 -0.01660 202 ARG A NH2 
1644 N N   . CYS A 203 ? 0.60790 0.42350 0.48870 0.04530  -0.00220 0.01050  203 CYS A N   
1645 C CA  . CYS A 203 ? 0.58840 0.40470 0.48510 0.04150  -0.00840 0.00850  203 CYS A CA  
1646 C C   . CYS A 203 ? 0.54180 0.38720 0.46720 0.04660  -0.02000 0.00160  203 CYS A C   
1647 O O   . CYS A 203 ? 0.53480 0.40420 0.47890 0.04450  -0.01700 -0.00170 203 CYS A O   
1648 C CB  . CYS A 203 ? 0.61870 0.44060 0.52580 0.02150  0.00410  0.00910  203 CYS A CB  
1649 S SG  . CYS A 203 ? 0.62010 0.41990 0.52500 0.01460  -0.00170 0.00520  203 CYS A SG  
1650 N N   . TRP A 204 ? 0.56900 0.41350 0.49530 0.05540  -0.03200 0.00080  204 TRP A N   
1651 C CA  . TRP A 204 ? 0.53220 0.40540 0.48120 0.05760  -0.04240 -0.00380 204 TRP A CA  
1652 C C   . TRP A 204 ? 0.51500 0.39760 0.48120 0.05650  -0.04220 -0.00760 204 TRP A C   
1653 O O   . TRP A 204 ? 0.52930 0.39030 0.48170 0.06230  -0.04020 -0.00670 204 TRP A O   
1654 C CB  . TRP A 204 ? 0.52870 0.41060 0.46980 0.06670  -0.05600 -0.00100 204 TRP A CB  
1655 C CG  . TRP A 204 ? 0.54910 0.42450 0.47110 0.06280  -0.06070 -0.00040 204 TRP A CG  
1656 C CD1 . TRP A 204 ? 0.58310 0.43500 0.47450 0.06690  -0.06000 0.00400  204 TRP A CD1 
1657 C CD2 . TRP A 204 ? 0.55710 0.43990 0.47910 0.05300  -0.06690 -0.00470 204 TRP A CD2 
1658 N NE1 . TRP A 204 ? 0.61030 0.45610 0.48240 0.06020  -0.06570 0.00100  204 TRP A NE1 
1659 C CE2 . TRP A 204 ? 0.59130 0.45150 0.47960 0.05090  -0.06990 -0.00460 204 TRP A CE2 
1660 C CE3 . TRP A 204 ? 0.54320 0.44150 0.48280 0.04470  -0.06970 -0.00830 204 TRP A CE3 
1661 C CZ2 . TRP A 204 ? 0.61870 0.46470 0.48630 0.03990  -0.07580 -0.00960 204 TRP A CZ2 
1662 C CZ3 . TRP A 204 ? 0.57470 0.45800 0.49410 0.03370  -0.07520 -0.01140 204 TRP A CZ3 
1663 C CH2 . TRP A 204 ? 0.61120 0.46580 0.49350 0.03090  -0.07820 -0.01280 204 TRP A CH2 
1664 N N   . ALA A 205 ? 0.40850 0.31640 0.39670 0.05110  -0.04450 -0.01170 205 ALA A N   
1665 C CA  . ALA A 205 ? 0.39940 0.31830 0.39980 0.05050  -0.04570 -0.01600 205 ALA A CA  
1666 C C   . ALA A 205 ? 0.37030 0.31690 0.38500 0.05150  -0.05330 -0.01640 205 ALA A C   
1667 O O   . ALA A 205 ? 0.36020 0.31320 0.37900 0.04530  -0.05480 -0.01590 205 ALA A O   
1668 C CB  . ALA A 205 ? 0.41300 0.33610 0.42210 0.03740  -0.04000 -0.01950 205 ALA A CB  
1669 N N   . LEU A 206 ? 0.42590 0.38740 0.44400 0.06020  -0.05690 -0.01620 206 LEU A N   
1670 C CA  . LEU A 206 ? 0.40670 0.40120 0.43750 0.05630  -0.06330 -0.01430 206 LEU A CA  
1671 C C   . LEU A 206 ? 0.39840 0.41250 0.43830 0.06130  -0.06000 -0.01700 206 LEU A C   
1672 O O   . LEU A 206 ? 0.41290 0.41620 0.44460 0.07600  -0.05490 -0.01990 206 LEU A O   
1673 C CB  . LEU A 206 ? 0.40500 0.42040 0.43510 0.06080  -0.07160 -0.00890 206 LEU A CB  
1674 C CG  . LEU A 206 ? 0.42610 0.42050 0.43870 0.05690  -0.07630 -0.00650 206 LEU A CG  
1675 C CD1 . LEU A 206 ? 0.42430 0.44990 0.43680 0.06080  -0.08800 -0.00070 206 LEU A CD1 
1676 C CD2 . LEU A 206 ? 0.44020 0.41730 0.44400 0.04000  -0.07680 -0.00870 206 LEU A CD2 
1677 N N   . GLY A 207 ? 0.38660 0.42280 0.43590 0.04980  -0.06190 -0.01590 207 GLY A N   
1678 C CA  . GLY A 207 ? 0.38770 0.45000 0.44390 0.05410  -0.05780 -0.01700 207 GLY A CA  
1679 C C   . GLY A 207 ? 0.40160 0.44410 0.44870 0.05700  -0.05190 -0.02420 207 GLY A C   
1680 O O   . GLY A 207 ? 0.42300 0.47380 0.46510 0.06850  -0.04590 -0.02780 207 GLY A O   
1681 N N   . PHE A 208 ? 0.33080 0.35090 0.37380 0.04730  -0.05350 -0.02640 208 PHE A N   
1682 C CA  . PHE A 208 ? 0.35680 0.36350 0.39030 0.04460  -0.05130 -0.03340 208 PHE A CA  
1683 C C   . PHE A 208 ? 0.34650 0.36850 0.38270 0.03570  -0.05460 -0.03160 208 PHE A C   
1684 O O   . PHE A 208 ? 0.32230 0.35070 0.36380 0.03120  -0.05810 -0.02460 208 PHE A O   
1685 C CB  . PHE A 208 ? 0.38010 0.36330 0.40860 0.03760  -0.05120 -0.03600 208 PHE A CB  
1686 C CG  . PHE A 208 ? 0.35470 0.34560 0.39540 0.03210  -0.05380 -0.03010 208 PHE A CG  
1687 C CD1 . PHE A 208 ? 0.34580 0.32820 0.38610 0.03660  -0.05290 -0.02580 208 PHE A CD1 
1688 C CD2 . PHE A 208 ? 0.33860 0.34520 0.38700 0.02620  -0.05680 -0.02870 208 PHE A CD2 
1689 C CE1 . PHE A 208 ? 0.33520 0.31790 0.37840 0.03550  -0.05260 -0.02170 208 PHE A CE1 
1690 C CE2 . PHE A 208 ? 0.32790 0.34060 0.38330 0.02940  -0.05650 -0.02290 208 PHE A CE2 
1691 C CZ  . PHE A 208 ? 0.33120 0.32840 0.38190 0.03420  -0.05320 -0.02020 208 PHE A CZ  
1692 N N   . TYR A 209 ? 0.39500 0.41480 0.41940 0.03380  -0.05380 -0.03790 209 TYR A N   
1693 C CA  . TYR A 209 ? 0.38930 0.42130 0.40950 0.02700  -0.05840 -0.03640 209 TYR A CA  
1694 C C   . TYR A 209 ? 0.41800 0.43950 0.42340 0.01930  -0.06140 -0.04600 209 TYR A C   
1695 O O   . TYR A 209 ? 0.46270 0.46070 0.44920 0.02190  -0.05600 -0.05520 209 TYR A O   
1696 C CB  . TYR A 209 ? 0.40440 0.45140 0.41750 0.02950  -0.05400 -0.03340 209 TYR A CB  
1697 C CG  . TYR A 209 ? 0.40540 0.45880 0.40800 0.02320  -0.05940 -0.02910 209 TYR A CG  
1698 C CD1 . TYR A 209 ? 0.41150 0.46490 0.41530 0.02030  -0.06340 -0.01760 209 TYR A CD1 
1699 C CD2 . TYR A 209 ? 0.42950 0.48150 0.41300 0.02110  -0.06110 -0.03630 209 TYR A CD2 
1700 C CE1 . TYR A 209 ? 0.42680 0.48030 0.41450 0.01930  -0.06880 -0.01120 209 TYR A CE1 
1701 C CE2 . TYR A 209 ? 0.44240 0.50210 0.41310 0.01720  -0.06800 -0.03080 209 TYR A CE2 
1702 C CZ  . TYR A 209 ? 0.43730 0.49860 0.41120 0.01830  -0.07170 -0.01720 209 TYR A CZ  
1703 O OH  . TYR A 209 ? 0.45590 0.51950 0.41120 0.01910  -0.07880 -0.00950 209 TYR A OH  
1704 N N   . PRO A 210 ? 0.47230 0.50930 0.48140 0.01000  -0.07030 -0.04400 210 PRO A N   
1705 C CA  . PRO A 210 ? 0.44520 0.50330 0.46820 0.01410  -0.07620 -0.03260 210 PRO A CA  
1706 C C   . PRO A 210 ? 0.42320 0.48280 0.46490 0.01780  -0.07460 -0.02780 210 PRO A C   
1707 O O   . PRO A 210 ? 0.43080 0.47580 0.47490 0.01480  -0.06920 -0.03240 210 PRO A O   
1708 C CB  . PRO A 210 ? 0.45370 0.53420 0.47180 0.00670  -0.08700 -0.03350 210 PRO A CB  
1709 C CG  . PRO A 210 ? 0.47970 0.55020 0.48750 -0.01020 -0.08790 -0.04630 210 PRO A CG  
1710 C CD  . PRO A 210 ? 0.50550 0.53840 0.49800 -0.00480 -0.07610 -0.05370 210 PRO A CD  
1711 N N   . ALA A 211 ? 0.38560 0.45780 0.43400 0.02740  -0.07790 -0.01820 211 ALA A N   
1712 C CA  . ALA A 211 ? 0.38150 0.44860 0.43930 0.03600  -0.07320 -0.01370 211 ALA A CA  
1713 C C   . ALA A 211 ? 0.37810 0.46990 0.45390 0.03000  -0.07200 -0.01590 211 ALA A C   
1714 O O   . ALA A 211 ? 0.38080 0.46360 0.46120 0.03230  -0.06480 -0.01520 211 ALA A O   
1715 C CB  . ALA A 211 ? 0.38650 0.44790 0.43480 0.05350  -0.07480 -0.00310 211 ALA A CB  
1716 N N   . GLU A 212 ? 0.46060 0.58540 0.54410 0.01900  -0.07920 -0.01790 212 GLU A N   
1717 C CA  . GLU A 212 ? 0.46300 0.61970 0.56450 0.00460  -0.07830 -0.01900 212 GLU A CA  
1718 C C   . GLU A 212 ? 0.48810 0.60870 0.58020 -0.01070 -0.06960 -0.02610 212 GLU A C   
1719 O O   . GLU A 212 ? 0.50900 0.59140 0.57970 -0.01770 -0.06910 -0.03420 212 GLU A O   
1720 C CB  . GLU A 212 ? 0.46670 0.66140 0.57140 -0.01470 -0.09050 -0.02230 212 GLU A CB  
1721 C CG  . GLU A 212 ? 0.47040 0.69860 0.58990 -0.04300 -0.09070 -0.02470 212 GLU A CG  
1722 C CD  . GLU A 212 ? 0.45490 0.74390 0.60840 -0.03050 -0.08620 -0.01290 212 GLU A CD  
1723 O OE1 . GLU A 212 ? 0.43450 0.76280 0.60140 -0.00360 -0.09160 -0.00320 212 GLU A OE1 
1724 O OE2 . GLU A 212 ? 0.46470 0.76120 0.62810 -0.04500 -0.07610 -0.01220 212 GLU A OE2 
1725 N N   . ILE A 213 ? 0.31580 0.44720 0.42000 -0.01170 -0.06130 -0.02190 213 ILE A N   
1726 C CA  . ILE A 213 ? 0.34880 0.44250 0.43890 -0.02480 -0.05270 -0.02580 213 ILE A CA  
1727 C C   . ILE A 213 ? 0.35680 0.48410 0.46420 -0.03310 -0.04420 -0.01940 213 ILE A C   
1728 O O   . ILE A 213 ? 0.33270 0.50510 0.46220 -0.01650 -0.04210 -0.01170 213 ILE A O   
1729 C CB  . ILE A 213 ? 0.35750 0.40560 0.43150 -0.00610 -0.04820 -0.02580 213 ILE A CB  
1730 C CG1 . ILE A 213 ? 0.40630 0.41130 0.45870 -0.01520 -0.04160 -0.02880 213 ILE A CG1 
1731 C CG2 . ILE A 213 ? 0.33870 0.39590 0.42070 0.01490  -0.04430 -0.01830 213 ILE A CG2 
1732 C CD1 . ILE A 213 ? 0.40920 0.37790 0.44480 0.00180  -0.04150 -0.03000 213 ILE A CD1 
1733 N N   . THR A 214 ? 0.44570 0.55030 0.53900 -0.05830 -0.03800 -0.02180 214 THR A N   
1734 C CA  . THR A 214 ? 0.45300 0.58330 0.55740 -0.06910 -0.02600 -0.01460 214 THR A CA  
1735 C C   . THR A 214 ? 0.50080 0.56800 0.57490 -0.06690 -0.01600 -0.01420 214 THR A C   
1736 O O   . THR A 214 ? 0.53050 0.54180 0.57250 -0.08160 -0.01700 -0.01960 214 THR A O   
1737 C CB  . THR A 214 ? 0.44460 0.61230 0.55700 -0.11070 -0.02730 -0.01480 214 THR A CB  
1738 O OG1 . THR A 214 ? 0.40330 0.63630 0.54310 -0.11280 -0.04010 -0.01460 214 THR A OG1 
1739 C CG2 . THR A 214 ? 0.44840 0.65690 0.57710 -0.12250 -0.01190 -0.00490 214 THR A CG2 
1740 N N   . LEU A 215 ? 0.43230 0.50440 0.51020 -0.04590 -0.00660 -0.00780 215 LEU A N   
1741 C CA  . LEU A 215 ? 0.47950 0.50250 0.52870 -0.04380 0.00290  -0.00500 215 LEU A CA  
1742 C C   . LEU A 215 ? 0.48470 0.54160 0.54190 -0.05670 0.01860  0.00330  215 LEU A C   
1743 O O   . LEU A 215 ? 0.46310 0.57140 0.54450 -0.03950 0.02520  0.00790  215 LEU A O   
1744 C CB  . LEU A 215 ? 0.49210 0.49080 0.53130 -0.01200 0.00070  -0.00490 215 LEU A CB  
1745 C CG  . LEU A 215 ? 0.47030 0.44300 0.50230 0.00240  -0.01230 -0.01040 215 LEU A CG  
1746 C CD1 . LEU A 215 ? 0.43450 0.39140 0.45500 0.02370  -0.01350 -0.00870 215 LEU A CD1 
1747 C CD2 . LEU A 215 ? 0.47380 0.40160 0.48100 -0.00550 -0.01500 -0.01350 215 LEU A CD2 
1748 N N   . THR A 216 ? 0.54110 0.56560 0.57300 -0.08440 0.02660  0.00610  216 THR A N   
1749 C CA  . THR A 216 ? 0.54610 0.60220 0.58180 -0.10030 0.04450  0.01570  216 THR A CA  
1750 C C   . THR A 216 ? 0.59210 0.57730 0.58020 -0.10300 0.05390  0.02040  216 THR A C   
1751 O O   . THR A 216 ? 0.61050 0.52360 0.56130 -0.10500 0.04650  0.01720  216 THR A O   
1752 C CB  . THR A 216 ? 0.53280 0.63830 0.58650 -0.14630 0.04740  0.01830  216 THR A CB  
1753 O OG1 . THR A 216 ? 0.55850 0.59580 0.57390 -0.17760 0.03970  0.01230  216 THR A OG1 
1754 C CG2 . THR A 216 ? 0.47210 0.66370 0.57550 -0.14080 0.03770  0.01650  216 THR A CG2 
1755 N N   . TRP A 217 ? 0.53820 0.54480 0.52460 -0.09870 0.07100  0.02900  217 TRP A N   
1756 C CA  . TRP A 217 ? 0.57310 0.52210 0.51250 -0.10760 0.08280  0.03660  217 TRP A CA  
1757 C C   . TRP A 217 ? 0.58880 0.56440 0.52760 -0.15350 0.09940  0.04570  217 TRP A C   
1758 O O   . TRP A 217 ? 0.55820 0.62280 0.54060 -0.16330 0.10930  0.04950  217 TRP A O   
1759 C CB  . TRP A 217 ? 0.58760 0.53600 0.51530 -0.07460 0.09190  0.04000  217 TRP A CB  
1760 C CG  . TRP A 217 ? 0.59020 0.48630 0.49530 -0.04280 0.07560  0.03390  217 TRP A CG  
1761 C CD1 . TRP A 217 ? 0.57280 0.48490 0.49520 -0.01380 0.06490  0.02640  217 TRP A CD1 
1762 C CD2 . TRP A 217 ? 0.61050 0.43340 0.46960 -0.03850 0.06770  0.03610  217 TRP A CD2 
1763 N NE1 . TRP A 217 ? 0.57630 0.43820 0.47110 0.00250  0.05020  0.02340  217 TRP A NE1 
1764 C CE2 . TRP A 217 ? 0.59010 0.40220 0.44860 -0.00850 0.05140  0.02970  217 TRP A CE2 
1765 C CE3 . TRP A 217 ? 0.63500 0.39890 0.44920 -0.05640 0.07290  0.04420  217 TRP A CE3 
1766 C CZ2 . TRP A 217 ? 0.58830 0.34960 0.41240 0.00560  0.03890  0.03150  217 TRP A CZ2 
1767 C CZ3 . TRP A 217 ? 0.64770 0.34960 0.42180 -0.03620 0.06110  0.04620  217 TRP A CZ3 
1768 C CH2 . TRP A 217 ? 0.61690 0.32580 0.40030 -0.00450 0.04380  0.04010  217 TRP A CH2 
1769 N N   . GLN A 218 ? 0.79900 0.69880 0.68650 -0.18170 0.10240  0.05010  218 GLN A N   
1770 C CA  . GLN A 218 ? 0.81660 0.72310 0.68750 -0.23140 0.12050  0.06100  218 GLN A CA  
1771 C C   . GLN A 218 ? 0.86360 0.70540 0.67830 -0.22650 0.13560  0.07250  218 GLN A C   
1772 O O   . GLN A 218 ? 0.87930 0.64840 0.65540 -0.19290 0.12650  0.07110  218 GLN A O   
1773 C CB  . GLN A 218 ? 0.83770 0.69290 0.67910 -0.27950 0.11270  0.05740  218 GLN A CB  
1774 C CG  . GLN A 218 ? 0.80640 0.73450 0.69740 -0.30230 0.10040  0.04840  218 GLN A CG  
1775 C CD  . GLN A 218 ? 0.83770 0.69480 0.68350 -0.34930 0.09110  0.04190  218 GLN A CD  
1776 O OE1 . GLN A 218 ? 0.89740 0.66290 0.67660 -0.37850 0.09980  0.04760  218 GLN A OE1 
1777 N NE2 . GLN A 218 ? 0.80810 0.69780 0.68110 -0.35580 0.07350  0.02980  218 GLN A NE2 
1778 N N   . ARG A 219 ? 0.96620 0.84100 0.77640 -0.26140 0.15860  0.08520  219 ARG A N   
1779 C CA  . ARG A 219 ? 1.00850 0.81610 0.75560 -0.26880 0.17540  0.09880  219 ARG A CA  
1780 C C   . ARG A 219 ? 1.03650 0.83250 0.75760 -0.33720 0.19060  0.10970  219 ARG A C   
1781 O O   . ARG A 219 ? 1.00090 0.89820 0.77060 -0.37160 0.20370  0.11400  219 ARG A O   
1782 C CB  . ARG A 219 ? 0.99890 0.86120 0.75970 -0.23910 0.19360  0.10510  219 ARG A CB  
1783 C CG  . ARG A 219 ? 1.04880 0.85650 0.74570 -0.25500 0.21500  0.12130  219 ARG A CG  
1784 C CD  . ARG A 219 ? 1.03500 0.91400 0.75030 -0.23180 0.23740  0.12640  219 ARG A CD  
1785 N NE  . ARG A 219 ? 1.04250 1.00000 0.77900 -0.27670 0.26630  0.13940  219 ARG A NE  
1786 C CZ  . ARG A 219 ? 1.03430 1.06340 0.78470 -0.26310 0.29340  0.14680  219 ARG A CZ  
1787 N NH1 . ARG A 219 ? 1.03140 1.05370 0.77080 -0.20690 0.29460  0.14060  219 ARG A NH1 
1788 N NH2 . ARG A 219 ? 1.04590 1.15520 0.81820 -0.30840 0.32050  0.16060  219 ARG A NH2 
1789 N N   . ASP A 220 ? 1.15210 0.82570 0.79470 -0.35690 0.18850  0.11480  220 ASP A N   
1790 C CA  . ASP A 220 ? 1.22340 0.87680 0.84490 -0.40540 0.18770  0.11500  220 ASP A CA  
1791 C C   . ASP A 220 ? 1.19490 0.91720 0.86840 -0.43840 0.17510  0.10300  220 ASP A C   
1792 O O   . ASP A 220 ? 1.22830 0.99770 0.91580 -0.48370 0.17860  0.10460  220 ASP A O   
1793 C CB  . ASP A 220 ? 1.25610 0.95210 0.87570 -0.43030 0.21140  0.13000  220 ASP A CB  
1794 C CG  . ASP A 220 ? 1.29820 0.92230 0.85920 -0.39870 0.22190  0.14150  220 ASP A CG  
1795 O OD1 . ASP A 220 ? 1.30900 0.84120 0.82460 -0.36000 0.20750  0.13780  220 ASP A OD1 
1796 O OD2 . ASP A 220 ? 1.33080 0.99590 0.89250 -0.40970 0.24350  0.15430  220 ASP A OD2 
1797 N N   . GLY A 221 ? 1.15940 0.89070 0.86060 -0.41520 0.15910  0.09130  221 GLY A N   
1798 C CA  . GLY A 221 ? 1.12260 0.91720 0.87010 -0.43930 0.14370  0.07910  221 GLY A CA  
1799 C C   . GLY A 221 ? 1.04540 0.99580 0.88240 -0.44300 0.14970  0.08180  221 GLY A C   
1800 O O   . GLY A 221 ? 1.01230 1.02440 0.89250 -0.45410 0.13340  0.07190  221 GLY A O   
1801 N N   . GLU A 222 ? 1.29000 1.30720 1.15310 -0.42790 0.17200  0.09450  222 GLU A N   
1802 C CA  . GLU A 222 ? 1.22510 1.39520 1.17170 -0.41820 0.17940  0.09750  222 GLU A CA  
1803 C C   . GLU A 222 ? 1.17840 1.37650 1.16370 -0.35070 0.16640  0.08700  222 GLU A C   
1804 O O   . GLU A 222 ? 1.20360 1.32990 1.15770 -0.30320 0.16390  0.08340  222 GLU A O   
1805 C CB  . GLU A 222 ? 1.24610 1.47050 1.20000 -0.41510 0.20760  0.11260  222 GLU A CB  
1806 N N   . ASP A 223 ? 1.01760 1.31890 1.06820 -0.34510 0.15550  0.08220  223 ASP A N   
1807 C CA  . ASP A 223 ? 0.98650 1.30500 1.06780 -0.28220 0.14070  0.07220  223 ASP A CA  
1808 C C   . ASP A 223 ? 0.97240 1.33010 1.06770 -0.22990 0.15960  0.07800  223 ASP A C   
1809 O O   . ASP A 223 ? 0.93620 1.39970 1.07170 -0.22980 0.17880  0.08830  223 ASP A O   
1810 C CB  . ASP A 223 ? 0.93570 1.35100 1.07590 -0.28950 0.12420  0.06780  223 ASP A CB  
1811 C CG  . ASP A 223 ? 0.94280 1.30030 1.07460 -0.26470 0.09720  0.05280  223 ASP A CG  
1812 O OD1 . ASP A 223 ? 0.96620 1.24160 1.06690 -0.22400 0.09310  0.04670  223 ASP A OD1 
1813 O OD2 . ASP A 223 ? 0.91250 1.31160 1.06820 -0.28790 0.07990  0.04750  223 ASP A OD2 
1814 N N   . GLN A 224 ? 0.73470 1.00840 0.79380 -0.18550 0.15440  0.07140  224 GLN A N   
1815 C CA  . GLN A 224 ? 0.74110 1.02450 0.79580 -0.13500 0.16900  0.07330  224 GLN A CA  
1816 C C   . GLN A 224 ? 0.69850 1.03290 0.79200 -0.08660 0.16010  0.06660  224 GLN A C   
1817 O O   . GLN A 224 ? 0.72080 1.00590 0.78970 -0.04310 0.15710  0.06020  224 GLN A O   
1818 C CB  . GLN A 224 ? 0.78770 0.95570 0.77940 -0.11670 0.16430  0.06940  224 GLN A CB  
1819 C CG  . GLN A 224 ? 0.82960 0.93750 0.77130 -0.15410 0.17600  0.07900  224 GLN A CG  
1820 C CD  . GLN A 224 ? 0.83940 1.00560 0.78280 -0.16690 0.20760  0.09260  224 GLN A CD  
1821 O OE1 . GLN A 224 ? 0.81140 1.04260 0.78050 -0.21160 0.22000  0.10160  224 GLN A OE1 
1822 N NE2 . GLN A 224 ? 0.85900 1.00540 0.77320 -0.13030 0.22120  0.09420  224 GLN A NE2 
1823 N N   . THR A 225 ? 1.12730 1.55670 1.27580 -0.09370 0.15500  0.06850  225 THR A N   
1824 C CA  . THR A 225 ? 1.09100 1.55040 1.26690 -0.04810 0.14180  0.06260  225 THR A CA  
1825 C C   . THR A 225 ? 1.08180 1.55950 1.25220 0.00910  0.16040  0.06500  225 THR A C   
1826 O O   . THR A 225 ? 1.09040 1.52240 1.24350 0.05170  0.15050  0.05720  225 THR A O   
1827 C CB  . THR A 225 ? 1.03820 1.60250 1.27160 -0.06790 0.13180  0.06650  225 THR A CB  
1828 O OG1 . THR A 225 ? 1.04310 1.55840 1.26890 -0.09330 0.10510  0.05670  225 THR A OG1 
1829 C CG2 . THR A 225 ? 0.99810 1.63890 1.26710 -0.01210 0.13360  0.06980  225 THR A CG2 
1830 N N   . GLN A 226 ? 1.03060 1.56780 1.20810 0.00990  0.18880  0.07560  226 GLN A N   
1831 C CA  . GLN A 226 ? 1.03020 1.58330 1.19590 0.06880  0.20960  0.07720  226 GLN A CA  
1832 C C   . GLN A 226 ? 1.08860 1.52000 1.18390 0.09050  0.21090  0.06800  226 GLN A C   
1833 O O   . GLN A 226 ? 1.09070 1.48690 1.15880 0.14100  0.21330  0.06160  226 GLN A O   
1834 C CB  . GLN A 226 ? 1.00990 1.67130 1.20420 0.06490  0.24250  0.09180  226 GLN A CB  
1835 C CG  . GLN A 226 ? 0.97010 1.75010 1.23170 0.04930  0.23430  0.09890  226 GLN A CG  
1836 C CD  . GLN A 226 ? 0.97870 1.78940 1.25630 0.11090  0.22530  0.09690  226 GLN A CD  
1837 O OE1 . GLN A 226 ? 0.99300 1.73690 1.23200 0.16370  0.22730  0.09000  226 GLN A OE1 
1838 N NE2 . GLN A 226 ? 0.97060 1.87410 1.29640 0.10220  0.21440  0.10360  226 GLN A NE2 
1839 N N   . ASP A 227 ? 0.78290 1.14560 0.84240 0.05290  0.20830  0.06750  227 ASP A N   
1840 C CA  . ASP A 227 ? 0.83290 1.09050 0.82640 0.06950  0.20670  0.06030  227 ASP A CA  
1841 C C   . ASP A 227 ? 0.84170 1.01710 0.81560 0.07280  0.17490  0.04820  227 ASP A C   
1842 O O   . ASP A 227 ? 0.86750 0.96240 0.79000 0.08330  0.16850  0.04210  227 ASP A O   
1843 C CB  . ASP A 227 ? 0.87510 1.09970 0.83410 0.03320  0.21970  0.06840  227 ASP A CB  
1844 C CG  . ASP A 227 ? 0.88330 1.18110 0.84900 0.03260  0.25600  0.08090  227 ASP A CG  
1845 O OD1 . ASP A 227 ? 0.87480 1.20840 0.84060 0.07840  0.27380  0.07970  227 ASP A OD1 
1846 O OD2 . ASP A 227 ? 0.89480 1.21150 0.86100 -0.01310 0.26830  0.09240  227 ASP A OD2 
1847 N N   . THR A 228 ? 0.61670 0.81660 0.62980 0.06360  0.15510  0.04500  228 THR A N   
1848 C CA  . THR A 228 ? 0.62010 0.75450 0.61980 0.06350  0.12730  0.03510  228 THR A CA  
1849 C C   . THR A 228 ? 0.59410 0.71470 0.58680 0.10480  0.12060  0.02800  228 THR A C   
1850 O O   . THR A 228 ? 0.56300 0.74280 0.58440 0.12830  0.12790  0.03110  228 THR A O   
1851 C CB  . THR A 228 ? 0.59970 0.75850 0.63550 0.03080  0.11080  0.03480  228 THR A CB  
1852 O OG1 . THR A 228 ? 0.62750 0.77270 0.65260 -0.00990 0.11600  0.04030  228 THR A OG1 
1853 C CG2 . THR A 228 ? 0.59770 0.70040 0.62300 0.03580  0.08540  0.02520  228 THR A CG2 
1854 N N   . GLU A 229 ? 0.73100 0.77360 0.68190 0.11340  0.10680  0.01970  229 GLU A N   
1855 C CA  . GLU A 229 ? 0.71460 0.72430 0.64900 0.14100  0.09600  0.01230  229 GLU A CA  
1856 C C   . GLU A 229 ? 0.69630 0.69460 0.65050 0.12330  0.07090  0.00840  229 GLU A C   
1857 O O   . GLU A 229 ? 0.70950 0.67230 0.65260 0.10190  0.05780  0.00580  229 GLU A O   
1858 C CB  . GLU A 229 ? 0.75670 0.68980 0.62760 0.15470  0.09600  0.00520  229 GLU A CB  
1859 C CG  . GLU A 229 ? 0.75720 0.63670 0.60280 0.16380  0.07720  -0.00330 229 GLU A CG  
1860 C CD  . GLU A 229 ? 0.80460 0.60760 0.58080 0.17210  0.07620  -0.01140 229 GLU A CD  
1861 O OE1 . GLU A 229 ? 0.83020 0.61310 0.58250 0.15760  0.07600  -0.01150 229 GLU A OE1 
1862 O OE2 . GLU A 229 ? 0.82620 0.58440 0.56590 0.19230  0.07490  -0.01740 229 GLU A OE2 
1863 N N   . LEU A 230 ? 0.58640 0.61680 0.56770 0.13560  0.06530  0.00910  230 LEU A N   
1864 C CA  . LEU A 230 ? 0.56030 0.58530 0.55920 0.12120  0.04420  0.00610  230 LEU A CA  
1865 C C   . LEU A 230 ? 0.55910 0.54140 0.53070 0.14360  0.03590  0.00220  230 LEU A C   
1866 O O   . LEU A 230 ? 0.55640 0.54770 0.52070 0.17450  0.04500  0.00510  230 LEU A O   
1867 C CB  . LEU A 230 ? 0.53120 0.62840 0.57980 0.11070  0.04230  0.01100  230 LEU A CB  
1868 C CG  . LEU A 230 ? 0.54710 0.68850 0.62380 0.07770  0.04700  0.01480  230 LEU A CG  
1869 C CD1 . LEU A 230 ? 0.50970 0.73820 0.63110 0.07730  0.04900  0.02110  230 LEU A CD1 
1870 C CD2 . LEU A 230 ? 0.55690 0.66250 0.62910 0.04850  0.03160  0.00940  230 LEU A CD2 
1871 N N   . VAL A 231 ? 0.53620 0.47300 0.49020 0.12880  0.01950  -0.00310 231 VAL A N   
1872 C CA  . VAL A 231 ? 0.53710 0.43220 0.46320 0.14110  0.01120  -0.00540 231 VAL A CA  
1873 C C   . VAL A 231 ? 0.50220 0.43160 0.46020 0.14020  0.00210  -0.00170 231 VAL A C   
1874 O O   . VAL A 231 ? 0.47670 0.44900 0.47270 0.12160  -0.00320 -0.00080 231 VAL A O   
1875 C CB  . VAL A 231 ? 0.55510 0.39410 0.44700 0.12190  -0.00260 -0.01140 231 VAL A CB  
1876 C CG1 . VAL A 231 ? 0.61040 0.39510 0.44810 0.13060  0.00400  -0.01610 231 VAL A CG1 
1877 C CG2 . VAL A 231 ? 0.52590 0.38810 0.44550 0.09600  -0.01260 -0.01180 231 VAL A CG2 
1878 N N   . GLU A 232 ? 0.55400 0.45390 0.48660 0.16020  0.00010  0.00020  232 GLU A N   
1879 C CA  . GLU A 232 ? 0.53390 0.45270 0.48380 0.15980  -0.01030 0.00440  232 GLU A CA  
1880 C C   . GLU A 232 ? 0.51580 0.42930 0.47630 0.12640  -0.02440 0.00040  232 GLU A C   
1881 O O   . GLU A 232 ? 0.53550 0.40910 0.47220 0.11010  -0.02910 -0.00410 232 GLU A O   
1882 C CB  . GLU A 232 ? 0.56800 0.43220 0.47080 0.18660  -0.00950 0.00790  232 GLU A CB  
1883 C CG  . GLU A 232 ? 0.56890 0.44180 0.47840 0.18730  -0.02040 0.01410  232 GLU A CG  
1884 C CD  . GLU A 232 ? 0.61300 0.42160 0.46670 0.21690  -0.01810 0.01980  232 GLU A CD  
1885 O OE1 . GLU A 232 ? 0.65670 0.40050 0.45930 0.23130  -0.00920 0.01630  232 GLU A OE1 
1886 O OE2 . GLU A 232 ? 0.61510 0.43140 0.46870 0.22700  -0.02500 0.02800  232 GLU A OE2 
1887 N N   . THR A 233 ? 0.45780 0.41700 0.45350 0.11680  -0.03080 0.00220  233 THR A N   
1888 C CA  . THR A 233 ? 0.45070 0.40670 0.45310 0.09250  -0.04150 -0.00110 233 THR A CA  
1889 C C   . THR A 233 ? 0.47820 0.38740 0.44580 0.09010  -0.04730 0.00070  233 THR A C   
1890 O O   . THR A 233 ? 0.49610 0.38240 0.44000 0.10800  -0.04630 0.00620  233 THR A O   
1891 C CB  . THR A 233 ? 0.41700 0.42020 0.45030 0.08630  -0.04670 -0.00020 233 THR A CB  
1892 O OG1 . THR A 233 ? 0.40820 0.45030 0.46790 0.08030  -0.04170 -0.00170 233 THR A OG1 
1893 C CG2 . THR A 233 ? 0.40660 0.40490 0.44190 0.06650  -0.05420 -0.00430 233 THR A CG2 
1894 N N   . ARG A 234 ? 0.44100 0.33620 0.40270 0.06810  -0.05300 -0.00270 234 ARG A N   
1895 C CA  . ARG A 234 ? 0.48110 0.33160 0.40590 0.05670  -0.05780 -0.00080 234 ARG A CA  
1896 C C   . ARG A 234 ? 0.48430 0.35800 0.42380 0.03380  -0.06450 -0.00020 234 ARG A C   
1897 O O   . ARG A 234 ? 0.44790 0.36060 0.41860 0.02810  -0.06540 -0.00360 234 ARG A O   
1898 C CB  . ARG A 234 ? 0.51770 0.32790 0.41050 0.04910  -0.05790 -0.00500 234 ARG A CB  
1899 C CG  . ARG A 234 ? 0.50310 0.34130 0.41670 0.03170  -0.06300 -0.00890 234 ARG A CG  
1900 C CD  . ARG A 234 ? 0.52770 0.33510 0.41300 0.03190  -0.06230 -0.01300 234 ARG A CD  
1901 N NE  . ARG A 234 ? 0.52350 0.35720 0.42280 0.01640  -0.07040 -0.01440 234 ARG A NE  
1902 C CZ  . ARG A 234 ? 0.54430 0.36110 0.42180 0.01370  -0.07300 -0.01730 234 ARG A CZ  
1903 N NH1 . ARG A 234 ? 0.57160 0.34100 0.40930 0.02390  -0.06640 -0.02060 234 ARG A NH1 
1904 N NH2 . ARG A 234 ? 0.52860 0.37700 0.42100 0.00400  -0.08220 -0.01630 234 ARG A NH2 
1905 N N   . PRO A 235 ? 0.47050 0.31780 0.38320 0.02180  -0.06760 0.00500  235 PRO A N   
1906 C CA  . PRO A 235 ? 0.46960 0.34730 0.39690 0.00020  -0.07090 0.00700  235 PRO A CA  
1907 C C   . PRO A 235 ? 0.45880 0.34810 0.38750 -0.02450 -0.07550 0.00510  235 PRO A C   
1908 O O   . PRO A 235 ? 0.48920 0.33920 0.38500 -0.03790 -0.07920 0.00460  235 PRO A O   
1909 C CB  . PRO A 235 ? 0.51740 0.35720 0.40800 -0.00520 -0.07110 0.01550  235 PRO A CB  
1910 C CG  . PRO A 235 ? 0.54540 0.31520 0.38730 0.00330  -0.07010 0.01630  235 PRO A CG  
1911 C CD  . PRO A 235 ? 0.51240 0.29800 0.37570 0.03030  -0.06610 0.01040  235 PRO A CD  
1912 N N   . ALA A 236 ? 0.45030 0.39490 0.41420 -0.02890 -0.07580 0.00390  236 ALA A N   
1913 C CA  . ALA A 236 ? 0.43760 0.41320 0.41020 -0.04890 -0.08120 0.00470  236 ALA A CA  
1914 C C   . ALA A 236 ? 0.46110 0.44100 0.41740 -0.08140 -0.08360 0.01170  236 ALA A C   
1915 O O   . ALA A 236 ? 0.45640 0.45350 0.40900 -0.10710 -0.09080 0.01350  236 ALA A O   
1916 C CB  . ALA A 236 ? 0.38610 0.41950 0.39820 -0.03420 -0.07880 0.00230  236 ALA A CB  
1917 N N   . GLY A 237 ? 0.51420 0.47850 0.45690 -0.08390 -0.07830 0.01670  237 GLY A N   
1918 C CA  . GLY A 237 ? 0.54060 0.50720 0.46430 -0.11780 -0.07790 0.02530  237 GLY A CA  
1919 C C   . GLY A 237 ? 0.51600 0.55160 0.47250 -0.11990 -0.07060 0.02930  237 GLY A C   
1920 O O   . GLY A 237 ? 0.54190 0.58190 0.48200 -0.14730 -0.06690 0.03820  237 GLY A O   
1921 N N   . ASP A 238 ? 0.50100 0.58420 0.49650 -0.09180 -0.06690 0.02320  238 ASP A N   
1922 C CA  . ASP A 238 ? 0.48050 0.62360 0.50150 -0.08430 -0.05740 0.02450  238 ASP A CA  
1923 C C   . ASP A 238 ? 0.48640 0.61250 0.50520 -0.05680 -0.05160 0.01890  238 ASP A C   
1924 O O   . ASP A 238 ? 0.47230 0.63670 0.50850 -0.04030 -0.04370 0.01500  238 ASP A O   
1925 C CB  . ASP A 238 ? 0.43090 0.63860 0.48900 -0.07160 -0.05730 0.02180  238 ASP A CB  
1926 C CG  . ASP A 238 ? 0.42050 0.60370 0.48510 -0.04370 -0.06210 0.01290  238 ASP A CG  
1927 O OD1 . ASP A 238 ? 0.43050 0.55940 0.47850 -0.03340 -0.06320 0.00800  238 ASP A OD1 
1928 O OD2 . ASP A 238 ? 0.39540 0.61730 0.48080 -0.03190 -0.06460 0.01240  238 ASP A OD2 
1929 N N   . ARG A 239 ? 0.41140 0.48210 0.40630 -0.05050 -0.05570 0.01830  239 ARG A N   
1930 C CA  . ARG A 239 ? 0.41450 0.47350 0.40740 -0.02860 -0.05460 0.01320  239 ARG A CA  
1931 C C   . ARG A 239 ? 0.37890 0.44590 0.39360 -0.00770 -0.05550 0.00230  239 ARG A C   
1932 O O   . ARG A 239 ? 0.37700 0.44480 0.39190 0.00470  -0.05420 -0.00390 239 ARG A O   
1933 C CB  . ARG A 239 ? 0.43340 0.51620 0.42030 -0.02960 -0.04690 0.01530  239 ARG A CB  
1934 C CG  . ARG A 239 ? 0.48700 0.55400 0.44410 -0.05330 -0.04470 0.02850  239 ARG A CG  
1935 C CD  . ARG A 239 ? 0.51560 0.59920 0.45790 -0.05390 -0.03640 0.03210  239 ARG A CD  
1936 N NE  . ARG A 239 ? 0.56620 0.62950 0.47520 -0.08070 -0.03310 0.04690  239 ARG A NE  
1937 C CZ  . ARG A 239 ? 0.58130 0.67770 0.49390 -0.10930 -0.02480 0.05460  239 ARG A CZ  
1938 N NH1 . ARG A 239 ? 0.54150 0.70330 0.49390 -0.10900 -0.01920 0.04970  239 ARG A NH1 
1939 N NH2 . ARG A 239 ? 0.61240 0.67710 0.48560 -0.13910 -0.02220 0.06900  239 ARG A NH2 
1940 N N   . THR A 240 ? 0.42420 0.49230 0.45100 -0.00630 -0.05820 0.00000  240 THR A N   
1941 C CA  . THR A 240 ? 0.39720 0.45450 0.43340 0.00990  -0.05930 -0.00760 240 THR A CA  
1942 C C   . THR A 240 ? 0.40230 0.42700 0.42930 0.00900  -0.06420 -0.00600 240 THR A C   
1943 O O   . THR A 240 ? 0.43320 0.43580 0.44150 -0.00140 -0.06690 -0.00020 240 THR A O   
1944 C CB  . THR A 240 ? 0.37890 0.45920 0.42990 0.01950  -0.05690 -0.01100 240 THR A CB  
1945 O OG1 . THR A 240 ? 0.38050 0.47440 0.43590 0.00890  -0.06170 -0.00570 240 THR A OG1 
1946 C CG2 . THR A 240 ? 0.39290 0.50370 0.44820 0.02870  -0.04890 -0.01320 240 THR A CG2 
1947 N N   . PHE A 241 ? 0.37300 0.38990 0.40740 0.02000  -0.06360 -0.01110 241 PHE A N   
1948 C CA  . PHE A 241 ? 0.38360 0.37590 0.41000 0.02420  -0.06460 -0.01000 241 PHE A CA  
1949 C C   . PHE A 241 ? 0.37670 0.36540 0.40760 0.02790  -0.06340 -0.01300 241 PHE A C   
1950 O O   . PHE A 241 ? 0.36370 0.36580 0.40320 0.03070  -0.06260 -0.01550 241 PHE A O   
1951 C CB  . PHE A 241 ? 0.37540 0.36980 0.40550 0.03320  -0.06360 -0.01020 241 PHE A CB  
1952 C CG  . PHE A 241 ? 0.39500 0.38860 0.41390 0.03390  -0.06650 -0.00490 241 PHE A CG  
1953 C CD1 . PHE A 241 ? 0.39110 0.40300 0.41270 0.02920  -0.06750 -0.00650 241 PHE A CD1 
1954 C CD2 . PHE A 241 ? 0.42740 0.39520 0.42550 0.04210  -0.06740 0.00190  241 PHE A CD2 
1955 C CE1 . PHE A 241 ? 0.41670 0.42550 0.42250 0.03010  -0.07050 -0.00010 241 PHE A CE1 
1956 C CE2 . PHE A 241 ? 0.45220 0.41180 0.43250 0.04560  -0.07020 0.00900  241 PHE A CE2 
1957 C CZ  . PHE A 241 ? 0.44590 0.42870 0.43170 0.03850  -0.07240 0.00850  241 PHE A CZ  
1958 N N   . GLN A 242 ? 0.37580 0.34230 0.39500 0.03130  -0.06250 -0.01200 242 GLN A N   
1959 C CA  . GLN A 242 ? 0.38230 0.33860 0.39640 0.03390  -0.06140 -0.01320 242 GLN A CA  
1960 C C   . GLN A 242 ? 0.39300 0.33670 0.40220 0.04330  -0.05420 -0.01310 242 GLN A C   
1961 O O   . GLN A 242 ? 0.40150 0.33820 0.40370 0.05020  -0.05210 -0.01100 242 GLN A O   
1962 C CB  . GLN A 242 ? 0.41690 0.36000 0.41190 0.02420  -0.06820 -0.01170 242 GLN A CB  
1963 C CG  . GLN A 242 ? 0.40350 0.37490 0.40730 0.01140  -0.07530 -0.00950 242 GLN A CG  
1964 C CD  . GLN A 242 ? 0.42460 0.39110 0.40960 -0.00570 -0.08490 -0.00790 242 GLN A CD  
1965 O OE1 . GLN A 242 ? 0.46060 0.38970 0.41770 -0.00770 -0.08610 -0.00980 242 GLN A OE1 
1966 N NE2 . GLN A 242 ? 0.40510 0.41320 0.40400 -0.01880 -0.09140 -0.00440 242 GLN A NE2 
1967 N N   . LYS A 243 ? 0.35650 0.29880 0.36720 0.04550  -0.04920 -0.01400 243 LYS A N   
1968 C CA  . LYS A 243 ? 0.36920 0.30850 0.37620 0.05300  -0.03960 -0.01260 243 LYS A CA  
1969 C C   . LYS A 243 ? 0.39110 0.31630 0.38610 0.05140  -0.03560 -0.01210 243 LYS A C   
1970 O O   . LYS A 243 ? 0.39040 0.31190 0.38490 0.04730  -0.04010 -0.01240 243 LYS A O   
1971 C CB  . LYS A 243 ? 0.36700 0.33820 0.39800 0.05200  -0.03510 -0.01190 243 LYS A CB  
1972 C CG  . LYS A 243 ? 0.38500 0.37430 0.42060 0.06330  -0.02500 -0.00820 243 LYS A CG  
1973 C CD  . LYS A 243 ? 0.38330 0.41880 0.44750 0.05500  -0.02390 -0.00680 243 LYS A CD  
1974 C CE  . LYS A 243 ? 0.38000 0.45600 0.45810 0.06960  -0.01410 -0.00080 243 LYS A CE  
1975 N NZ  . LYS A 243 ? 0.36190 0.43290 0.42970 0.09700  -0.01550 0.00270  243 LYS A NZ  
1976 N N   . TRP A 244 ? 0.43190 0.34730 0.41270 0.05840  -0.02610 -0.01060 244 TRP A N   
1977 C CA  . TRP A 244 ? 0.46040 0.36350 0.42760 0.05600  -0.01960 -0.00830 244 TRP A CA  
1978 C C   . TRP A 244 ? 0.49680 0.41520 0.46680 0.06030  -0.00300 -0.00520 244 TRP A C   
1979 O O   . TRP A 244 ? 0.49060 0.42680 0.46830 0.07230  0.00270  -0.00490 244 TRP A O   
1980 C CB  . TRP A 244 ? 0.47900 0.35120 0.41350 0.05820  -0.02630 -0.00880 244 TRP A CB  
1981 C CG  . TRP A 244 ? 0.50290 0.35060 0.40850 0.06440  -0.02680 -0.01200 244 TRP A CG  
1982 C CD1 . TRP A 244 ? 0.50550 0.33730 0.39610 0.05790  -0.03990 -0.01530 244 TRP A CD1 
1983 C CD2 . TRP A 244 ? 0.53100 0.36060 0.41070 0.07710  -0.01280 -0.01260 244 TRP A CD2 
1984 N NE1 . TRP A 244 ? 0.54510 0.33800 0.39540 0.06380  -0.03610 -0.01890 244 TRP A NE1 
1985 C CE2 . TRP A 244 ? 0.56440 0.35500 0.40670 0.07960  -0.01880 -0.01770 244 TRP A CE2 
1986 C CE3 . TRP A 244 ? 0.55610 0.39850 0.43720 0.08540  0.00560  -0.00900 244 TRP A CE3 
1987 C CZ2 . TRP A 244 ? 0.59710 0.35250 0.39810 0.09570  -0.00660 -0.02090 244 TRP A CZ2 
1988 C CZ3 . TRP A 244 ? 0.59010 0.41260 0.43940 0.10290  0.01910  -0.01070 244 TRP A CZ3 
1989 C CH2 . TRP A 244 ? 0.60810 0.38270 0.41470 0.11070  0.01320  -0.01730 244 TRP A CH2 
1990 N N   . ALA A 245 ? 0.42370 0.33650 0.38530 0.05190  0.00560  -0.00140 245 ALA A N   
1991 C CA  . ALA A 245 ? 0.45920 0.39360 0.42300 0.05150  0.02400  0.00340  245 ALA A CA  
1992 C C   . ALA A 245 ? 0.49380 0.39400 0.42100 0.05080  0.03130  0.00710  245 ALA A C   
1993 O O   . ALA A 245 ? 0.49830 0.36880 0.40910 0.04240  0.02390  0.00880  245 ALA A O   
1994 C CB  . ALA A 245 ? 0.47720 0.44740 0.46970 0.03060  0.02880  0.00640  245 ALA A CB  
1995 N N   . ALA A 246 ? 0.50530 0.40740 0.41470 0.06350  0.04630  0.00870  246 ALA A N   
1996 C CA  . ALA A 246 ? 0.53470 0.40230 0.40190 0.06440  0.05390  0.01210  246 ALA A CA  
1997 C C   . ALA A 246 ? 0.54810 0.44420 0.41550 0.06170  0.07960  0.01950  246 ALA A C   
1998 O O   . ALA A 246 ? 0.53260 0.47610 0.42540 0.07220  0.09280  0.02010  246 ALA A O   
1999 C CB  . ALA A 246 ? 0.54030 0.36980 0.36740 0.08200  0.04770  0.00570  246 ALA A CB  
2000 N N   . VAL A 247 ? 0.56870 0.43800 0.40500 0.04960  0.08730  0.02650  247 VAL A N   
2001 C CA  . VAL A 247 ? 0.58190 0.47250 0.40750 0.04440  0.11390  0.03510  247 VAL A CA  
2002 C C   . VAL A 247 ? 0.61570 0.45310 0.38080 0.05280  0.11770  0.03730  247 VAL A C   
2003 O O   . VAL A 247 ? 0.62510 0.41340 0.36090 0.05290  0.09830  0.03610  247 VAL A O   
2004 C CB  . VAL A 247 ? 0.58730 0.49990 0.43180 0.00970  0.12290  0.04470  247 VAL A CB  
2005 C CG1 . VAL A 247 ? 0.56480 0.53810 0.46630 -0.00000 0.11890  0.04190  247 VAL A CG1 
2006 C CG2 . VAL A 247 ? 0.60260 0.45020 0.41560 -0.00570 0.10780  0.04760  247 VAL A CG2 
2007 N N   . VAL A 248 ? 0.67320 0.52650 0.41910 0.06230  0.14300  0.04100  248 VAL A N   
2008 C CA  . VAL A 248 ? 0.71320 0.51870 0.39600 0.06830  0.15040  0.04410  248 VAL A CA  
2009 C C   . VAL A 248 ? 0.73620 0.54210 0.40640 0.04110  0.16780  0.05940  248 VAL A C   
2010 O O   . VAL A 248 ? 0.72870 0.59120 0.43220 0.02480  0.18980  0.06700  248 VAL A O   
2011 C CB  . VAL A 248 ? 0.72910 0.54030 0.38530 0.09750  0.17000  0.03810  248 VAL A CB  
2012 C CG1 . VAL A 248 ? 0.79400 0.55020 0.37560 0.10250  0.17680  0.04010  248 VAL A CG1 
2013 C CG2 . VAL A 248 ? 0.71370 0.51030 0.37350 0.12000  0.15300  0.02370  248 VAL A CG2 
2014 N N   . VAL A 249 ? 0.78250 0.52690 0.40330 0.03450  0.15700  0.06540  249 VAL A N   
2015 C CA  . VAL A 249 ? 0.81090 0.53490 0.40860 0.00680  0.16990  0.08120  249 VAL A CA  
2016 C C   . VAL A 249 ? 0.87550 0.55010 0.40040 0.01440  0.17870  0.08920  249 VAL A C   
2017 O O   . VAL A 249 ? 0.88850 0.52860 0.37800 0.03750  0.16120  0.08180  249 VAL A O   
2018 C CB  . VAL A 249 ? 0.80570 0.49190 0.40780 -0.00730 0.14720  0.08380  249 VAL A CB  
2019 C CG1 . VAL A 249 ? 0.76070 0.49210 0.42880 -0.01160 0.13580  0.07360  249 VAL A CG1 
2020 C CG2 . VAL A 249 ? 0.81500 0.44590 0.37710 0.01490  0.12050  0.08180  249 VAL A CG2 
2021 N N   . PRO A 250 ? 0.92890 0.60030 0.42660 -0.00740 0.20530  0.10440  250 PRO A N   
2022 C CA  . PRO A 250 ? 1.00180 0.61580 0.42140 -0.00220 0.21170  0.11460  250 PRO A CA  
2023 C C   . PRO A 250 ? 1.02570 0.56770 0.40580 0.00330  0.18090  0.11920  250 PRO A C   
2024 O O   . PRO A 250 ? 1.01640 0.53940 0.41270 -0.01090 0.16940  0.12370  250 PRO A O   
2025 C CB  . PRO A 250 ? 1.05020 0.67780 0.45620 -0.03590 0.24670  0.13260  250 PRO A CB  
2026 C CG  . PRO A 250 ? 0.99360 0.71090 0.47830 -0.05190 0.26220  0.12840  250 PRO A CG  
2027 C CD  . PRO A 250 ? 0.92280 0.64760 0.45850 -0.04120 0.23060  0.11370  250 PRO A CD  
2028 N N   . SER A 251 ? 1.25540 0.75900 0.58100 0.02630  0.16690  0.11770  251 SER A N   
2029 C CA  A SER A 251 ? 1.28120 0.72810 0.56730 0.03730  0.13730  0.12480  251 SER A CA  
2030 C CA  B SER A 251 ? 1.28110 0.72770 0.56650 0.03740  0.13730  0.12480  251 SER A CA  
2031 C C   . SER A 251 ? 1.32820 0.72400 0.57400 0.01830  0.14890  0.14560  251 SER A C   
2032 O O   . SER A 251 ? 1.36070 0.75520 0.58440 0.00120  0.17440  0.15380  251 SER A O   
2033 C CB  A SER A 251 ? 1.30460 0.72710 0.53350 0.06000  0.12150  0.12120  251 SER A CB  
2034 C CB  B SER A 251 ? 1.30610 0.72740 0.53290 0.05980  0.12230  0.12170  251 SER A CB  
2035 O OG  A SER A 251 ? 1.27370 0.72860 0.53750 0.07380  0.10080  0.10110  251 SER A OG  
2036 O OG  B SER A 251 ? 1.27420 0.72940 0.53070 0.07300  0.10820  0.10110  251 SER A OG  
2037 N N   . GLY A 252 ? 1.21820 0.58350 0.47150 0.02160  0.12780  0.14890  252 GLY A N   
2038 C CA  . GLY A 252 ? 1.26430 0.58330 0.49440 0.00470  0.13400  0.16070  252 GLY A CA  
2039 C C   . GLY A 252 ? 1.25500 0.57870 0.51600 -0.03060 0.15140  0.16250  252 GLY A C   
2040 O O   . GLY A 252 ? 1.30330 0.57950 0.54320 -0.04500 0.15160  0.16870  252 GLY A O   
2041 N N   . GLU A 253 ? 1.14250 0.52340 0.45220 -0.04500 0.16500  0.15560  253 GLU A N   
2042 C CA  . GLU A 253 ? 1.12440 0.52790 0.47560 -0.08230 0.17750  0.15410  253 GLU A CA  
2043 C C   . GLU A 253 ? 1.05970 0.48540 0.46760 -0.07100 0.15340  0.13820  253 GLU A C   
2044 O O   . GLU A 253 ? 1.04180 0.50030 0.49270 -0.09980 0.16010  0.13300  253 GLU A O   
2045 C CB  . GLU A 253 ? 1.09560 0.58340 0.49030 -0.10700 0.20680  0.15220  253 GLU A CB  
2046 C CG  . GLU A 253 ? 1.17380 0.64790 0.52040 -0.13350 0.23700  0.16980  253 GLU A CG  
2047 C CD  . GLU A 253 ? 1.14820 0.71760 0.53680 -0.15240 0.27040  0.17050  253 GLU A CD  
2048 O OE1 . GLU A 253 ? 1.07820 0.72700 0.54270 -0.15240 0.26740  0.15760  253 GLU A OE1 
2049 O OE2 . GLU A 253 ? 1.19380 0.77840 0.56030 -0.15850 0.29070  0.17940  253 GLU A OE2 
2050 N N   . GLU A 254 ? 1.08430 0.49600 0.49100 -0.03190 0.12540  0.13140  254 GLU A N   
2051 C CA  . GLU A 254 ? 1.03890 0.47900 0.49980 -0.01900 0.10410  0.11660  254 GLU A CA  
2052 C C   . GLU A 254 ? 1.06430 0.46050 0.51830 -0.03960 0.10460  0.11870  254 GLU A C   
2053 O O   . GLU A 254 ? 1.02680 0.46190 0.53310 -0.05070 0.10060  0.10650  254 GLU A O   
2054 C CB  . GLU A 254 ? 1.02790 0.45900 0.47960 0.02230  0.07550  0.11330  254 GLU A CB  
2055 C CG  . GLU A 254 ? 1.00010 0.47760 0.46560 0.03870  0.06860  0.10470  254 GLU A CG  
2056 C CD  . GLU A 254 ? 1.05050 0.49430 0.45070 0.04520  0.07520  0.11620  254 GLU A CD  
2057 O OE1 . GLU A 254 ? 1.09130 0.48020 0.43830 0.03440  0.08900  0.13270  254 GLU A OE1 
2058 O OE2 . GLU A 254 ? 1.03960 0.50630 0.43540 0.05950  0.06640  0.10850  254 GLU A OE2 
2059 N N   . GLN A 255 ? 1.19430 0.50200 0.57600 -0.04530 0.10980  0.13400  255 GLN A N   
2060 C CA  . GLN A 255 ? 1.21930 0.48480 0.59230 -0.06300 0.10810  0.12920  255 GLN A CA  
2061 C C   . GLN A 255 ? 1.20500 0.49860 0.60610 -0.11700 0.12670  0.12680  255 GLN A C   
2062 O O   . GLN A 255 ? 1.22590 0.50020 0.63290 -0.13320 0.12120  0.11780  255 GLN A O   
2063 C CB  . GLN A 255 ? 1.31000 0.50480 0.61880 -0.05950 0.10970  0.13680  255 GLN A CB  
2064 C CG  . GLN A 255 ? 1.33700 0.50710 0.61830 -0.00600 0.08920  0.13890  255 GLN A CG  
2065 C CD  . GLN A 255 ? 1.43510 0.54060 0.64870 -0.00320 0.09500  0.15010  255 GLN A CD  
2066 O OE1 . GLN A 255 ? 1.44630 0.55630 0.63910 -0.00740 0.10320  0.15970  255 GLN A OE1 
2067 N NE2 . GLN A 255 ? 1.49510 0.53700 0.66900 0.00550  0.09150  0.14850  255 GLN A NE2 
2068 N N   . ARG A 256 ? 1.14510 0.49750 0.56890 -0.14360 0.14760  0.13230  256 ARG A N   
2069 C CA  . ARG A 256 ? 1.12930 0.53840 0.59460 -0.19440 0.16310  0.12910  256 ARG A CA  
2070 C C   . ARG A 256 ? 1.07660 0.56590 0.62210 -0.18730 0.14880  0.11060  256 ARG A C   
2071 O O   . ARG A 256 ? 1.06420 0.59720 0.64300 -0.22810 0.15510  0.10690  256 ARG A O   
2072 C CB  . ARG A 256 ? 1.12930 0.60430 0.60900 -0.21510 0.18940  0.13850  256 ARG A CB  
2073 C CG  . ARG A 256 ? 1.20950 0.62950 0.62750 -0.23370 0.20320  0.15310  256 ARG A CG  
2074 C CD  . ARG A 256 ? 1.20750 0.69340 0.63580 -0.24030 0.22960  0.16270  256 ARG A CD  
2075 N NE  . ARG A 256 ? 1.21050 0.77810 0.68310 -0.28980 0.25030  0.16600  256 ARG A NE  
2076 C CZ  . ARG A 256 ? 1.16080 0.83870 0.68960 -0.29260 0.27030  0.16610  256 ARG A CZ  
2077 N NH1 . ARG A 256 ? 1.10000 0.81680 0.65250 -0.24460 0.26840  0.15750  256 ARG A NH1 
2078 N NH2 . ARG A 256 ? 1.16520 0.92500 0.73580 -0.33470 0.28670  0.17150  256 ARG A NH2 
2079 N N   . TYR A 257 ? 0.93990 0.45080 0.51430 -0.14020 0.12930  0.09990  257 TYR A N   
2080 C CA  . TYR A 257 ? 0.88390 0.47560 0.53210 -0.13030 0.11820  0.08440  257 TYR A CA  
2081 C C   . TYR A 257 ? 0.86930 0.42510 0.51880 -0.11760 0.09720  0.07410  257 TYR A C   
2082 O O   . TYR A 257 ? 0.88970 0.38370 0.50080 -0.08740 0.08490  0.07580  257 TYR A O   
2083 C CB  . TYR A 257 ? 0.85320 0.49660 0.53070 -0.09160 0.11360  0.07930  257 TYR A CB  
2084 C CG  . TYR A 257 ? 0.85650 0.55080 0.54170 -0.09970 0.13710  0.08590  257 TYR A CG  
2085 C CD1 . TYR A 257 ? 0.89370 0.54670 0.52350 -0.10030 0.15130  0.09870  257 TYR A CD1 
2086 C CD2 . TYR A 257 ? 0.82320 0.60770 0.56780 -0.10320 0.14630  0.08030  257 TYR A CD2 
2087 C CE1 . TYR A 257 ? 0.90060 0.60140 0.53390 -0.10520 0.17590  0.10450  257 TYR A CE1 
2088 C CE2 . TYR A 257 ? 0.82850 0.66420 0.57910 -0.10390 0.17070  0.08680  257 TYR A CE2 
2089 C CZ  . TYR A 257 ? 0.86370 0.65740 0.55850 -0.10560 0.18650  0.09840  257 TYR A CZ  
2090 O OH  . TYR A 257 ? 0.86650 0.71160 0.56310 -0.10370 0.21390  0.10470  257 TYR A OH  
2091 N N   . THR A 258 ? 0.81760 0.41700 0.51020 -0.13860 0.09350  0.06400  258 THR A N   
2092 C CA  . THR A 258 ? 0.81130 0.38590 0.50790 -0.12660 0.07580  0.05250  258 THR A CA  
2093 C C   . THR A 258 ? 0.75630 0.41930 0.52380 -0.11670 0.06640  0.04080  258 THR A C   
2094 O O   . THR A 258 ? 0.74280 0.47850 0.55210 -0.13700 0.07490  0.04100  258 THR A O   
2095 C CB  . THR A 258 ? 0.84860 0.36290 0.50620 -0.16760 0.07900  0.05120  258 THR A CB  
2096 O OG1 . THR A 258 ? 0.83950 0.41630 0.52920 -0.21700 0.08980  0.05200  258 THR A OG1 
2097 C CG2 . THR A 258 ? 0.94220 0.34650 0.51510 -0.17250 0.08740  0.06350  258 THR A CG2 
2098 N N   . CYS A 259 ? 0.73850 0.39800 0.51800 -0.08360 0.04970  0.03230  259 CYS A N   
2099 C CA  . CYS A 259 ? 0.69740 0.42470 0.53310 -0.07470 0.03970  0.02190  259 CYS A CA  
2100 C C   . CYS A 259 ? 0.70290 0.41570 0.53790 -0.09310 0.03260  0.01280  259 CYS A C   
2101 O O   . CYS A 259 ? 0.72570 0.36700 0.51630 -0.08820 0.02910  0.01090  259 CYS A O   
2102 C CB  . CYS A 259 ? 0.66640 0.40340 0.51460 -0.03430 0.02660  0.01850  259 CYS A CB  
2103 S SG  . CYS A 259 ? 0.62830 0.43090 0.53260 -0.02560 0.01480  0.00730  259 CYS A SG  
2104 N N   . HIS A 260 ? 0.66590 0.44380 0.54430 -0.11200 0.03080  0.00760  260 HIS A N   
2105 C CA  . HIS A 260 ? 0.66790 0.43790 0.54390 -0.13360 0.02260  -0.00210 260 HIS A CA  
2106 C C   . HIS A 260 ? 0.62190 0.44420 0.54070 -0.11010 0.00980  -0.01000 260 HIS A C   
2107 O O   . HIS A 260 ? 0.59610 0.48390 0.55720 -0.09700 0.00980  -0.00720 260 HIS A O   
2108 C CB  . HIS A 260 ? 0.66710 0.46970 0.55060 -0.18490 0.02920  -0.00000 260 HIS A CB  
2109 C CG  . HIS A 260 ? 0.71350 0.45940 0.54870 -0.21530 0.04350  0.00910  260 HIS A CG  
2110 N ND1 . HIS A 260 ? 0.76930 0.43630 0.54700 -0.25270 0.04440  0.00610  260 HIS A ND1 
2111 C CD2 . HIS A 260 ? 0.72780 0.47360 0.55420 -0.21360 0.05820  0.02160  260 HIS A CD2 
2112 C CE1 . HIS A 260 ? 0.80660 0.42840 0.54330 -0.27570 0.05920  0.01780  260 HIS A CE1 
2113 N NE2 . HIS A 260 ? 0.78370 0.45480 0.55050 -0.25120 0.06800  0.02760  260 HIS A NE2 
2114 N N   . VAL A 261 ? 0.63620 0.42280 0.53710 -0.10230 0.00050  -0.01930 261 VAL A N   
2115 C CA  . VAL A 261 ? 0.59890 0.42410 0.53070 -0.08010 -0.01060 -0.02590 261 VAL A CA  
2116 C C   . VAL A 261 ? 0.60160 0.42350 0.52490 -0.10330 -0.01770 -0.03620 261 VAL A C   
2117 O O   . VAL A 261 ? 0.63790 0.39050 0.51220 -0.11450 -0.01660 -0.04250 261 VAL A O   
2118 C CB  . VAL A 261 ? 0.59200 0.38660 0.51080 -0.04190 -0.01440 -0.02650 261 VAL A CB  
2119 C CG1 . VAL A 261 ? 0.54490 0.38570 0.49700 -0.02460 -0.02360 -0.03100 261 VAL A CG1 
2120 C CG2 . VAL A 261 ? 0.58820 0.37570 0.50280 -0.02420 -0.00970 -0.01680 261 VAL A CG2 
2121 N N   . GLN A 262 ? 0.59160 0.48210 0.55510 -0.10900 -0.02520 -0.03770 262 GLN A N   
2122 C CA  . GLN A 262 ? 0.59640 0.49280 0.55300 -0.12870 -0.03520 -0.04760 262 GLN A CA  
2123 C C   . GLN A 262 ? 0.56000 0.48770 0.53940 -0.09940 -0.04360 -0.05010 262 GLN A C   
2124 O O   . GLN A 262 ? 0.52340 0.50230 0.54020 -0.08050 -0.04460 -0.04270 262 GLN A O   
2125 C CB  . GLN A 262 ? 0.57080 0.52870 0.55150 -0.16750 -0.03890 -0.04540 262 GLN A CB  
2126 C CG  . GLN A 262 ? 0.60890 0.53470 0.56150 -0.20790 -0.02990 -0.04290 262 GLN A CG  
2127 C CD  . GLN A 262 ? 0.58570 0.60210 0.58000 -0.24090 -0.03010 -0.03530 262 GLN A CD  
2128 O OE1 . GLN A 262 ? 0.58610 0.63170 0.58020 -0.28010 -0.04020 -0.04020 262 GLN A OE1 
2129 N NE2 . GLN A 262 ? 0.56310 0.63010 0.59290 -0.22420 -0.01900 -0.02310 262 GLN A NE2 
2130 N N   . HIS A 263 ? 0.54320 0.43360 0.49310 -0.09570 -0.04800 -0.06030 263 HIS A N   
2131 C CA  . HIS A 263 ? 0.52030 0.43680 0.48560 -0.07160 -0.05400 -0.06190 263 HIS A CA  
2132 C C   . HIS A 263 ? 0.54740 0.42990 0.47510 -0.08050 -0.05830 -0.07480 263 HIS A C   
2133 O O   . HIS A 263 ? 0.59460 0.40910 0.47420 -0.08800 -0.05320 -0.08310 263 HIS A O   
2134 C CB  . HIS A 263 ? 0.50490 0.41090 0.47590 -0.03620 -0.04870 -0.05710 263 HIS A CB  
2135 C CG  . HIS A 263 ? 0.47190 0.41160 0.46110 -0.01880 -0.05360 -0.05590 263 HIS A CG  
2136 N ND1 . HIS A 263 ? 0.49000 0.41390 0.45860 -0.00930 -0.05340 -0.06300 263 HIS A ND1 
2137 C CD2 . HIS A 263 ? 0.43010 0.41290 0.44950 -0.01020 -0.05740 -0.04780 263 HIS A CD2 
2138 C CE1 . HIS A 263 ? 0.45540 0.41560 0.44380 0.00090  -0.05690 -0.05820 263 HIS A CE1 
2139 N NE2 . HIS A 263 ? 0.41840 0.40910 0.43470 0.00010  -0.06000 -0.04910 263 HIS A NE2 
2140 N N   . GLU A 264 ? 0.65770 0.58070 0.60020 -0.07700 -0.06700 -0.07610 264 GLU A N   
2141 C CA  . GLU A 264 ? 0.68610 0.58240 0.59050 -0.08580 -0.07180 -0.08870 264 GLU A CA  
2142 C C   . GLU A 264 ? 0.73000 0.55950 0.59100 -0.06220 -0.06050 -0.09680 264 GLU A C   
2143 O O   . GLU A 264 ? 0.77800 0.55200 0.58620 -0.07270 -0.05950 -0.11020 264 GLU A O   
2144 C CB  . GLU A 264 ? 0.65740 0.60820 0.58460 -0.07700 -0.08110 -0.08520 264 GLU A CB  
2145 C CG  . GLU A 264 ? 0.69480 0.63500 0.58630 -0.09520 -0.09030 -0.09700 264 GLU A CG  
2146 C CD  . GLU A 264 ? 0.66900 0.66050 0.57860 -0.08390 -0.09940 -0.09070 264 GLU A CD  
2147 O OE1 . GLU A 264 ? 0.61590 0.65390 0.56730 -0.06880 -0.10090 -0.07650 264 GLU A OE1 
2148 O OE2 . GLU A 264 ? 0.69820 0.67570 0.57250 -0.08960 -0.10450 -0.10000 264 GLU A OE2 
2149 N N   . GLY A 265 ? 0.65330 0.48770 0.53240 -0.02950 -0.05200 -0.08900 265 GLY A N   
2150 C CA  . GLY A 265 ? 0.68460 0.47500 0.53140 0.00070  -0.04080 -0.09350 265 GLY A CA  
2151 C C   . GLY A 265 ? 0.72650 0.44460 0.53100 0.00450  -0.03290 -0.09640 265 GLY A C   
2152 O O   . GLY A 265 ? 0.75400 0.42910 0.52330 0.03520  -0.02300 -0.10030 265 GLY A O   
2153 N N   . LEU A 266 ? 0.73690 0.44140 0.54190 -0.02360 -0.03560 -0.09320 266 LEU A N   
2154 C CA  . LEU A 266 ? 0.78350 0.40760 0.53790 -0.02660 -0.02800 -0.09470 266 LEU A CA  
2155 C C   . LEU A 266 ? 0.84480 0.40550 0.54060 -0.06330 -0.03030 -0.10880 266 LEU A C   
2156 O O   . LEU A 266 ? 0.83220 0.43210 0.54720 -0.10460 -0.04060 -0.11080 266 LEU A O   
2157 C CB  . LEU A 266 ? 0.76430 0.40650 0.54580 -0.04060 -0.02760 -0.08210 266 LEU A CB  
2158 C CG  . LEU A 266 ? 0.71980 0.41080 0.54670 -0.00900 -0.02640 -0.06930 266 LEU A CG  
2159 C CD1 . LEU A 266 ? 0.70290 0.42310 0.55860 -0.02820 -0.02660 -0.05900 266 LEU A CD1 
2160 C CD2 . LEU A 266 ? 0.73830 0.38260 0.53360 0.03010  -0.01910 -0.06620 266 LEU A CD2 
2161 N N   . PRO A 267 ? 0.92690 0.39100 0.54790 -0.04960 -0.02160 -0.11900 267 PRO A N   
2162 C CA  . PRO A 267 ? 0.98190 0.39320 0.55010 -0.08870 -0.02370 -0.12850 267 PRO A CA  
2163 C C   . PRO A 267 ? 0.99890 0.39860 0.56380 -0.13340 -0.02480 -0.12030 267 PRO A C   
2164 O O   . PRO A 267 ? 1.02770 0.43170 0.58030 -0.17990 -0.03180 -0.12430 267 PRO A O   
2165 C CB  . PRO A 267 ? 1.05150 0.38960 0.55960 -0.04970 -0.01030 -0.13080 267 PRO A CB  
2166 C CG  . PRO A 267 ? 1.03430 0.37320 0.55800 -0.00210 -0.00120 -0.11790 267 PRO A CG  
2167 C CD  . PRO A 267 ? 0.94510 0.36250 0.53760 0.00330  -0.00870 -0.11460 267 PRO A CD  
2168 N N   . LYS A 268 ? 0.97970 0.37130 0.55590 -0.12100 -0.01800 -0.10780 268 LYS A N   
2169 C CA  . LYS A 268 ? 0.98710 0.37750 0.56470 -0.16220 -0.01670 -0.09820 268 LYS A CA  
2170 C C   . LYS A 268 ? 0.92940 0.37320 0.56240 -0.15450 -0.01690 -0.08780 268 LYS A C   
2171 O O   . LYS A 268 ? 0.89380 0.36040 0.55310 -0.10500 -0.01460 -0.08240 268 LYS A O   
2172 C CB  . LYS A 268 ? 1.06870 0.36850 0.57840 -0.15660 -0.00480 -0.09150 268 LYS A CB  
2173 C CG  . LYS A 268 ? 1.17090 0.40110 0.61130 -0.16740 -0.00310 -0.10080 268 LYS A CG  
2174 C CD  . LYS A 268 ? 1.27610 0.41260 0.64380 -0.15980 0.00850  -0.09290 268 LYS A CD  
2175 C CE  . LYS A 268 ? 1.38590 0.43940 0.67510 -0.15230 0.01250  -0.10190 268 LYS A CE  
2176 N NZ  . LYS A 268 ? 1.49720 0.45390 0.70850 -0.13960 0.02400  -0.09340 268 LYS A NZ  
2177 N N   . PRO A 269 ? 0.92070 0.41300 0.58580 -0.19640 -0.01830 -0.08000 269 PRO A N   
2178 C CA  . PRO A 269 ? 0.86960 0.43180 0.59470 -0.17750 -0.01440 -0.06450 269 PRO A CA  
2179 C C   . PRO A 269 ? 0.90330 0.39540 0.59020 -0.14690 -0.00360 -0.05560 269 PRO A C   
2180 O O   . PRO A 269 ? 0.96160 0.35920 0.57880 -0.15450 0.00330  -0.05630 269 PRO A O   
2181 C CB  . PRO A 269 ? 0.85570 0.47290 0.60780 -0.23030 -0.01400 -0.05820 269 PRO A CB  
2182 C CG  . PRO A 269 ? 0.88780 0.48760 0.60950 -0.27880 -0.02240 -0.07030 269 PRO A CG  
2183 C CD  . PRO A 269 ? 0.95100 0.45260 0.60400 -0.25360 -0.02020 -0.08000 269 PRO A CD  
2184 N N   . LEU A 270 ? 0.96080 0.50450 0.69260 -0.10970 -0.00320 -0.04600 270 LEU A N   
2185 C CA  . LEU A 270 ? 0.97810 0.47710 0.68420 -0.07570 0.00320  -0.03580 270 LEU A CA  
2186 C C   . LEU A 270 ? 0.98090 0.49580 0.69650 -0.09560 0.01070  -0.02270 270 LEU A C   
2187 O O   . LEU A 270 ? 0.94610 0.54200 0.71600 -0.11220 0.01020  -0.01970 270 LEU A O   
2188 C CB  . LEU A 270 ? 0.93370 0.48320 0.67980 -0.02660 -0.00280 -0.03350 270 LEU A CB  
2189 C CG  . LEU A 270 ? 0.93140 0.46920 0.66690 0.00610  -0.00640 -0.04240 270 LEU A CG  
2190 C CD1 . LEU A 270 ? 0.87790 0.47910 0.65830 0.04380  -0.01180 -0.03610 270 LEU A CD1 
2191 C CD2 . LEU A 270 ? 0.99810 0.42990 0.65490 0.02380  0.00100  -0.04420 270 LEU A CD2 
2192 N N   . THR A 271 ? 1.04930 0.48580 0.70850 -0.08830 0.01860  -0.01400 271 THR A N   
2193 C CA  . THR A 271 ? 1.05870 0.50220 0.71780 -0.09820 0.02730  0.00020  271 THR A CA  
2194 C C   . THR A 271 ? 1.06110 0.48650 0.70740 -0.04780 0.02500  0.00930  271 THR A C   
2195 O O   . THR A 271 ? 1.08160 0.43830 0.67960 -0.01630 0.02320  0.00990  271 THR A O   
2196 C CB  . THR A 271 ? 1.13110 0.49530 0.72650 -0.14280 0.03900  0.00540  271 THR A CB  
2197 O OG1 . THR A 271 ? 1.12500 0.51830 0.73540 -0.19560 0.03820  -0.00340 271 THR A OG1 
2198 C CG2 . THR A 271 ? 1.13510 0.50990 0.72840 -0.15300 0.05060  0.02140  271 THR A CG2 
2199 N N   . LEU A 272 ? 0.99040 0.47800 0.67650 -0.03870 0.02460  0.01640  272 LEU A N   
2200 C CA  . LEU A 272 ? 0.98380 0.46960 0.66310 0.00360  0.01870  0.02450  272 LEU A CA  
2201 C C   . LEU A 272 ? 0.99750 0.47220 0.65610 -0.00620 0.02790  0.03750  272 LEU A C   
2202 O O   . LEU A 272 ? 0.99990 0.51120 0.68010 -0.03830 0.03800  0.03880  272 LEU A O   
2203 C CB  . LEU A 272 ? 0.91700 0.48590 0.65730 0.02620  0.00660  0.01900  272 LEU A CB  
2204 C CG  . LEU A 272 ? 0.89040 0.48510 0.65710 0.03990  -0.00230 0.00790  272 LEU A CG  
2205 C CD1 . LEU A 272 ? 0.83870 0.49970 0.64890 0.06250  -0.01360 0.00770  272 LEU A CD1 
2206 C CD2 . LEU A 272 ? 0.93370 0.45860 0.64990 0.06420  -0.00210 0.00750  272 LEU A CD2 
2207 N N   . ARG A 273 ? 1.20570 0.63610 0.82250 0.02490  0.02450  0.04810  273 ARG A N   
2208 C CA  . ARG A 273 ? 1.22670 0.65120 0.82180 0.02390  0.03050  0.06070  273 ARG A CA  
2209 C C   . ARG A 273 ? 1.20020 0.64380 0.79600 0.06760  0.01470  0.06550  273 ARG A C   
2210 O O   . ARG A 273 ? 1.18730 0.63070 0.78490 0.10020  0.00200  0.06350  273 ARG A O   
2211 C CB  . ARG A 273 ? 1.30030 0.63090 0.82040 0.00610  0.04440  0.07330  273 ARG A CB  
2212 C CG  . ARG A 273 ? 1.34640 0.62620 0.83060 0.02410  0.03990  0.06860  273 ARG A CG  
2213 C CD  . ARG A 273 ? 1.42080 0.63380 0.83980 0.01520  0.05000  0.07790  273 ARG A CD  
2214 N NE  . ARG A 273 ? 1.45370 0.65730 0.86300 -0.03810 0.06690  0.08280  273 ARG A NE  
2215 C CZ  . ARG A 273 ? 1.48080 0.66600 0.88250 -0.08290 0.07560  0.07640  273 ARG A CZ  
2216 N NH1 . ARG A 273 ? 1.49010 0.65580 0.88790 -0.08080 0.06890  0.06370  273 ARG A NH1 
2217 N NH2 . ARG A 273 ? 1.49180 0.68470 0.88930 -0.13210 0.09130  0.08290  273 ARG A NH2 
2218 N N   . TRP A 274 ? 0.99950 0.46540 0.59340 0.06700  0.01580  0.07180  274 TRP A N   
2219 C CA  . TRP A 274 ? 0.98710 0.47240 0.57530 0.10060  -0.00110 0.07690  274 TRP A CA  
2220 C C   . TRP A 274 ? 1.03710 0.45420 0.55670 0.12290  -0.00240 0.09310  274 TRP A C   
2221 O O   . TRP A 274 ? 1.08380 0.45030 0.56200 0.10270  0.01370  0.09990  274 TRP A O   
2222 C CB  . TRP A 274 ? 0.96720 0.49950 0.57460 0.08960  -0.00010 0.07410  274 TRP A CB  
2223 C CG  . TRP A 274 ? 0.96330 0.51140 0.55650 0.11510  -0.01880 0.07870  274 TRP A CG  
2224 C CD1 . TRP A 274 ? 0.92820 0.52960 0.55560 0.13120  -0.03980 0.07220  274 TRP A CD1 
2225 C CD2 . TRP A 274 ? 1.00460 0.51870 0.54280 0.12410  -0.01960 0.09150  274 TRP A CD2 
2226 N NE1 . TRP A 274 ? 0.93850 0.54530 0.53700 0.14740  -0.05570 0.07980  274 TRP A NE1 
2227 C CE2 . TRP A 274 ? 0.98640 0.53830 0.52860 0.14560  -0.04420 0.09140  274 TRP A CE2 
2228 C CE3 . TRP A 274 ? 1.05180 0.50820 0.53480 0.11320  -0.00210 0.10390  274 TRP A CE3 
2229 C CZ2 . TRP A 274 ? 1.01090 0.54520 0.50350 0.15840  -0.05370 0.10250  274 TRP A CZ2 
2230 C CZ3 . TRP A 274 ? 1.08110 0.51530 0.51300 0.12820  -0.00930 0.11550  274 TRP A CZ3 
2231 C CH2 . TRP A 274 ? 1.06810 0.54180 0.50520 0.15150  -0.03590 0.11410  274 TRP A CH2 
2232 N N   . GLU A 275 ? 1.15710 0.60260 0.68250 0.15890  -0.02100 0.09410  275 GLU A N   
2233 C CA  . GLU A 275 ? 1.20980 0.62680 0.69220 0.18210  -0.02450 0.10350  275 GLU A CA  
2234 C C   . GLU A 275 ? 1.18450 0.66020 0.68190 0.20790  -0.04690 0.10750  275 GLU A C   
2235 O O   . GLU A 275 ? 1.13460 0.67330 0.67860 0.22020  -0.06200 0.10160  275 GLU A O   
2236 C CB  . GLU A 275 ? 1.25440 0.64150 0.72260 0.20260  -0.02210 0.10110  275 GLU A CB  
2237 C CG  . GLU A 275 ? 1.29280 0.61650 0.73650 0.17340  -0.00290 0.09600  275 GLU A CG  
2238 C CD  . GLU A 275 ? 1.33630 0.63260 0.76420 0.19550  -0.00190 0.09040  275 GLU A CD  
2239 O OE1 . GLU A 275 ? 1.39530 0.67120 0.78900 0.22990  -0.00580 0.09690  275 GLU A OE1 
2240 O OE2 . GLU A 275 ? 1.31350 0.60890 0.76050 0.18010  0.00300  0.07950  275 GLU A OE2 
2241 N N   . PRO A 276 ? 1.08850 0.54830 0.54690 0.21360  -0.05030 0.11740  276 PRO A N   
2242 C CA  . PRO A 276 ? 1.08350 0.59770 0.54900 0.23430  -0.07360 0.12190  276 PRO A CA  
2243 C C   . PRO A 276 ? 1.06720 0.63400 0.56490 0.26770  -0.08970 0.12240  276 PRO A C   
2244 O O   . PRO A 276 ? 1.01520 0.65550 0.55940 0.26790  -0.10650 0.11750  276 PRO A O   
2245 C CB  . PRO A 276 ? 1.15310 0.61860 0.55910 0.23830  -0.06910 0.13380  276 PRO A CB  
2246 C CG  . PRO A 276 ? 1.17590 0.57780 0.55180 0.20690  -0.04310 0.13370  276 PRO A CG  
2247 C CD  . PRO A 276 ? 1.14680 0.53660 0.54980 0.19600  -0.03140 0.12510  276 PRO A CD  
2248 N N   . MET B 1   ? 1.25770 1.06660 1.29320 0.34590  0.15310  0.08760  0   MET B N   
2249 C CA  . MET B 1   ? 1.20850 1.09490 1.24780 0.28350  0.09210  0.08000  0   MET B CA  
2250 C C   . MET B 1   ? 1.22720 1.13010 1.23560 0.26700  0.11610  0.05460  0   MET B C   
2251 O O   . MET B 1   ? 1.25710 1.08710 1.19940 0.29210  0.16770  0.02940  0   MET B O   
2252 C CB  . MET B 1   ? 1.33820 1.16550 1.27850 0.24380  0.04000  0.05140  0   MET B CB  
2253 C CG  . MET B 1   ? 1.32430 1.17840 1.31260 0.23390  -0.00990 0.08020  0   MET B CG  
2254 S SD  . MET B 1   ? 1.35820 1.10620 1.22030 0.21150  -0.04840 0.04680  0   MET B SD  
2255 C CE  . MET B 1   ? 1.34390 1.04890 1.09720 0.17650  -0.04140 0.00380  0   MET B CE  
2256 N N   . ILE B 2   ? 1.25160 1.24120 1.29860 0.22070  0.08000  0.06180  1   ILE B N   
2257 C CA  . ILE B 2   ? 1.24400 1.25050 1.25900 0.19860  0.09790  0.03770  1   ILE B CA  
2258 C C   . ILE B 2   ? 1.26260 1.18690 1.15430 0.17180  0.08550  -0.00230 1   ILE B C   
2259 O O   . ILE B 2   ? 1.24190 1.16160 1.10420 0.13410  0.04100  -0.00520 1   ILE B O   
2260 C CB  . ILE B 2   ? 1.20100 1.30810 1.28050 0.15330  0.06730  0.05870  1   ILE B CB  
2261 N N   . GLN B 3   ? 1.04000 0.89670 0.85930 0.18840  0.12470  -0.02750 2   GLN B N   
2262 C CA  . GLN B 3   ? 1.00910 0.79430 0.71860 0.15820  0.10990  -0.05330 2   GLN B CA  
2263 C C   . GLN B 3   ? 0.93360 0.74550 0.63050 0.14010  0.13260  -0.06440 2   GLN B C   
2264 O O   . GLN B 3   ? 0.93000 0.75030 0.64530 0.16660  0.17770  -0.06780 2   GLN B O   
2265 C CB  . GLN B 3   ? 1.06380 0.72620 0.67270 0.17910  0.12690  -0.06910 2   GLN B CB  
2266 C CG  . GLN B 3   ? 1.12210 0.75240 0.74580 0.20340  0.11330  -0.05700 2   GLN B CG  
2267 C CD  . GLN B 3   ? 1.16650 0.66970 0.66360 0.19520  0.10170  -0.07450 2   GLN B CD  
2268 O OE1 . GLN B 3   ? 1.19810 0.60890 0.58840 0.18910  0.12680  -0.09380 2   GLN B OE1 
2269 N NE2 . GLN B 3   ? 1.16490 0.65800 0.66570 0.18910  0.06050  -0.06580 2   GLN B NE2 
2270 N N   . ARG B 4   ? 0.94840 0.77270 0.61900 0.09730  0.10570  -0.06610 3   ARG B N   
2271 C CA  . ARG B 4   ? 0.85430 0.71260 0.52470 0.07690  0.12530  -0.06980 3   ARG B CA  
2272 C C   . ARG B 4   ? 0.80050 0.60250 0.39010 0.04620  0.10890  -0.07050 3   ARG B C   
2273 O O   . ARG B 4   ? 0.77020 0.55210 0.33990 0.02370  0.07290  -0.05990 3   ARG B O   
2274 C CB  . ARG B 4   ? 0.79720 0.73950 0.53730 0.05190  0.11780  -0.05750 3   ARG B CB  
2275 C CG  . ARG B 4   ? 0.83810 0.85010 0.65950 0.07050  0.13600  -0.04910 3   ARG B CG  
2276 C CD  . ARG B 4   ? 0.81870 0.89060 0.68360 0.03330  0.11740  -0.03470 3   ARG B CD  
2277 N NE  . ARG B 4   ? 0.89360 0.96620 0.77750 0.02560  0.07810  -0.01930 3   ARG B NE  
2278 C CZ  . ARG B 4   ? 0.87480 0.98340 0.78300 -0.01210 0.05420  -0.00310 3   ARG B CZ  
2279 N NH1 . ARG B 4   ? 0.80750 0.94740 0.71830 -0.04600 0.06890  -0.00190 3   ARG B NH1 
2280 N NH2 . ARG B 4   ? 0.88830 0.99290 0.80880 -0.02030 0.01510  0.01320  3   ARG B NH2 
2281 N N   . THR B 5   ? 0.89380 0.67310 0.44070 0.04250  0.13320  -0.07700 4   THR B N   
2282 C CA  . THR B 5   ? 0.86300 0.58960 0.33330 0.00750  0.11220  -0.06700 4   THR B CA  
2283 C C   . THR B 5   ? 0.76690 0.56040 0.28800 -0.02430 0.10620  -0.04270 4   THR B C   
2284 O O   . THR B 5   ? 0.72720 0.59080 0.31710 -0.01860 0.13170  -0.04390 4   THR B O   
2285 C CB  . THR B 5   ? 0.93340 0.59470 0.32260 0.00980  0.13910  -0.08040 4   THR B CB  
2286 O OG1 . THR B 5   ? 0.96760 0.56020 0.27330 -0.03030 0.10380  -0.06500 4   THR B OG1 
2287 C CG2 . THR B 5   ? 0.88060 0.61080 0.32360 0.00960  0.17110  -0.07970 4   THR B CG2 
2288 N N   . PRO B 6   ? 0.78870 0.56060 0.28210 -0.05830 0.07490  -0.01500 5   PRO B N   
2289 C CA  . PRO B 6   ? 0.71600 0.54770 0.27190 -0.08160 0.08030  0.01640  5   PRO B CA  
2290 C C   . PRO B 6   ? 0.69890 0.56460 0.26940 -0.09350 0.10810  0.02950  5   PRO B C   
2291 O O   . PRO B 6   ? 0.73610 0.56770 0.25570 -0.10130 0.10140  0.02850  5   PRO B O   
2292 C CB  . PRO B 6   ? 0.71340 0.51040 0.24390 -0.11060 0.03870  0.05180  5   PRO B CB  
2293 C CG  . PRO B 6   ? 0.80840 0.52390 0.24130 -0.11670 0.00970  0.04110  5   PRO B CG  
2294 C CD  . PRO B 6   ? 0.84080 0.53250 0.25330 -0.07650 0.03410  -0.00570 5   PRO B CD  
2295 N N   . LYS B 7   ? 0.81050 0.48790 0.42550 0.05810  0.08650  -0.01900 6   LYS B N   
2296 C CA  . LYS B 7   ? 0.79670 0.48970 0.41290 0.03170  0.07860  -0.01320 6   LYS B CA  
2297 C C   . LYS B 7   ? 0.76790 0.45050 0.37400 0.01060  0.05360  -0.00540 6   LYS B C   
2298 O O   . LYS B 7   ? 0.75470 0.43750 0.37680 0.01560  0.04620  -0.00200 6   LYS B O   
2299 C CB  . LYS B 7   ? 0.78640 0.53640 0.46430 0.03580  0.07880  -0.01100 6   LYS B CB  
2300 C CG  . LYS B 7   ? 0.82610 0.60310 0.54050 0.05290  0.10490  -0.02410 6   LYS B CG  
2301 C CD  . LYS B 7   ? 0.84600 0.68000 0.63330 0.04830  0.10600  -0.02850 6   LYS B CD  
2302 C CE  . LYS B 7   ? 0.81770 0.69770 0.65630 0.06880  0.07950  -0.03740 6   LYS B CE  
2303 N NZ  . LYS B 7   ? 0.82230 0.73910 0.70450 0.10050  0.08480  -0.05730 6   LYS B NZ  
2304 N N   . ILE B 8   ? 0.70030 0.37390 0.27970 -0.01000 0.04160  -0.00270 7   ILE B N   
2305 C CA  . ILE B 8   ? 0.69330 0.36440 0.27200 -0.02970 0.01460  -0.00130 7   ILE B CA  
2306 C C   . ILE B 8   ? 0.68310 0.38000 0.27140 -0.03620 -0.00420 0.01120  7   ILE B C   
2307 O O   . ILE B 8   ? 0.70360 0.38450 0.25030 -0.03530 0.00090  0.01510  7   ILE B O   
2308 C CB  . ILE B 8   ? 0.74810 0.37350 0.27320 -0.04540 0.00820  -0.01810 7   ILE B CB  
2309 C CG1 . ILE B 8   ? 0.77890 0.36210 0.28470 -0.03650 0.03360  -0.03000 7   ILE B CG1 
2310 C CG2 . ILE B 8   ? 0.74990 0.38800 0.29980 -0.06760 -0.02160 -0.02340 7   ILE B CG2 
2311 C CD1 . ILE B 8   ? 0.83850 0.36620 0.28130 -0.05060 0.03470  -0.05240 7   ILE B CD1 
2312 N N   . GLN B 9   ? 0.59650 0.32470 0.23210 -0.04050 -0.02220 0.01870  8   GLN B N   
2313 C CA  . GLN B 9   ? 0.58880 0.33660 0.23470 -0.04300 -0.04370 0.03100  8   GLN B CA  
2314 C C   . GLN B 9   ? 0.59640 0.36250 0.27170 -0.05550 -0.07230 0.02550  8   GLN B C   
2315 O O   . GLN B 9   ? 0.58580 0.36360 0.30320 -0.06090 -0.06510 0.02060  8   GLN B O   
2316 C CB  . GLN B 9   ? 0.55320 0.32900 0.24570 -0.03290 -0.03350 0.04310  8   GLN B CB  
2317 C CG  . GLN B 9   ? 0.57260 0.34050 0.25520 -0.02590 -0.00630 0.04510  8   GLN B CG  
2318 C CD  . GLN B 9   ? 0.56670 0.35380 0.29100 -0.02290 0.00010  0.05420  8   GLN B CD  
2319 O OE1 . GLN B 9   ? 0.57600 0.35120 0.28790 -0.02330 -0.00780 0.06940  8   GLN B OE1 
2320 N NE2 . GLN B 9   ? 0.56160 0.37490 0.33250 -0.01760 0.01270  0.04340  8   GLN B NE2 
2321 N N   . VAL B 10  ? 0.61340 0.38170 0.26680 -0.05830 -0.10340 0.02560  9   VAL B N   
2322 C CA  A VAL B 10  ? 0.62730 0.42880 0.32650 -0.06900 -0.13670 0.01580  9   VAL B CA  
2323 C CA  B VAL B 10  ? 0.62690 0.42840 0.32620 -0.06900 -0.13650 0.01590  9   VAL B CA  
2324 C C   . VAL B 10  ? 0.61710 0.44610 0.33660 -0.05250 -0.16000 0.03400  9   VAL B C   
2325 O O   . VAL B 10  ? 0.63940 0.44360 0.29860 -0.03720 -0.16790 0.04800  9   VAL B O   
2326 C CB  A VAL B 10  ? 0.68030 0.46580 0.33990 -0.08380 -0.16490 -0.00900 9   VAL B CB  
2327 C CB  B VAL B 10  ? 0.67880 0.46390 0.33910 -0.08410 -0.16380 -0.00910 9   VAL B CB  
2328 C CG1 A VAL B 10  ? 0.68180 0.51320 0.41910 -0.10250 -0.19370 -0.02900 9   VAL B CG1 
2329 C CG1 B VAL B 10  ? 0.69760 0.44530 0.33920 -0.09810 -0.13410 -0.02540 9   VAL B CG1 
2330 C CG2 A VAL B 10  ? 0.70590 0.44310 0.31950 -0.09350 -0.13580 -0.02370 9   VAL B CG2 
2331 C CG2 B VAL B 10  ? 0.71930 0.47220 0.28750 -0.06950 -0.18180 -0.00370 9   VAL B CG2 
2332 N N   . TYR B 11  ? 0.57060 0.44340 0.37000 -0.05320 -0.16610 0.03500  10  TYR B N   
2333 C CA  . TYR B 11  ? 0.55990 0.45510 0.38600 -0.03260 -0.18080 0.05380  10  TYR B CA  
2334 C C   . TYR B 11  ? 0.54580 0.49450 0.46880 -0.03660 -0.18710 0.04650  10  TYR B C   
2335 O O   . TYR B 11  ? 0.53960 0.50070 0.50490 -0.05690 -0.17000 0.03050  10  TYR B O   
2336 C CB  . TYR B 11  ? 0.53610 0.40630 0.34580 -0.02010 -0.14680 0.07330  10  TYR B CB  
2337 C CG  . TYR B 11  ? 0.49580 0.37090 0.33960 -0.02840 -0.11240 0.06620  10  TYR B CG  
2338 C CD1 . TYR B 11  ? 0.49300 0.34400 0.30300 -0.03660 -0.09170 0.05670  10  TYR B CD1 
2339 C CD2 . TYR B 11  ? 0.47200 0.37150 0.37360 -0.02240 -0.10140 0.06900  10  TYR B CD2 
2340 C CE1 . TYR B 11  ? 0.46800 0.32050 0.29800 -0.03550 -0.06650 0.05160  10  TYR B CE1 
2341 C CE2 . TYR B 11  ? 0.44960 0.34700 0.36390 -0.02400 -0.07390 0.06260  10  TYR B CE2 
2342 C CZ  . TYR B 11  ? 0.44710 0.32140 0.32360 -0.02870 -0.05930 0.05480  10  TYR B CZ  
2343 O OH  . TYR B 11  ? 0.43200 0.30170 0.31140 -0.02210 -0.03810 0.05000  10  TYR B OH  
2344 N N   . SER B 12  ? 0.53330 0.50770 0.49020 -0.01520 -0.20590 0.05960  11  SER B N   
2345 C CA  . SER B 12  ? 0.51370 0.54270 0.57040 -0.01500 -0.20720 0.05290  11  SER B CA  
2346 C C   . SER B 12  ? 0.49840 0.51850 0.57790 -0.00390 -0.16820 0.06690  11  SER B C   
2347 O O   . SER B 12  ? 0.49020 0.47130 0.51970 0.00820  -0.15360 0.08260  11  SER B O   
2348 C CB  . SER B 12  ? 0.51940 0.59220 0.61330 0.00640  -0.25740 0.05320  11  SER B CB  
2349 O OG  . SER B 12  ? 0.54420 0.58110 0.57370 0.03850  -0.27060 0.08000  11  SER B OG  
2350 N N   . ARG B 13  ? 0.54450 0.50250 0.60760 -0.01120 -0.24790 0.04110  12  ARG B N   
2351 C CA  . ARG B 13  ? 0.57130 0.53350 0.64620 0.00100  -0.23010 0.02370  12  ARG B CA  
2352 C C   . ARG B 13  ? 0.58810 0.55620 0.69020 0.04680  -0.20830 0.01680  12  ARG B C   
2353 O O   . ARG B 13  ? 0.58890 0.51700 0.69980 0.06670  -0.19290 0.00110  12  ARG B O   
2354 C CB  . ARG B 13  ? 0.56910 0.60350 0.64060 -0.02560 -0.23290 0.02290  12  ARG B CB  
2355 C CG  . ARG B 13  ? 0.60830 0.65780 0.69360 -0.01380 -0.21190 0.00150  12  ARG B CG  
2356 C CD  . ARG B 13  ? 0.62050 0.74990 0.69990 -0.04530 -0.21150 -0.00230 12  ARG B CD  
2357 N NE  . ARG B 13  ? 0.58130 0.69330 0.62170 -0.09710 -0.23700 0.01000  12  ARG B NE  
2358 C CZ  . ARG B 13  ? 0.57510 0.74830 0.59610 -0.13900 -0.24430 0.01380  12  ARG B CZ  
2359 N NH1 . ARG B 13  ? 0.59050 0.85450 0.63040 -0.13620 -0.22450 0.00130  12  ARG B NH1 
2360 N NH2 . ARG B 13  ? 0.55130 0.69440 0.53390 -0.18670 -0.27400 0.02870  12  ARG B NH2 
2361 N N   . HIS B 14  ? 0.57610 0.59120 0.69260 0.06410  -0.20970 0.02820  13  HIS B N   
2362 C CA  . HIS B 14  ? 0.58590 0.60630 0.73070 0.10790  -0.19740 0.02430  13  HIS B CA  
2363 C C   . HIS B 14  ? 0.57850 0.56480 0.71350 0.12000  -0.20710 0.04370  13  HIS B C   
2364 O O   . HIS B 14  ? 0.57320 0.55670 0.68580 0.09460  -0.22180 0.05840  13  HIS B O   
2365 C CB  . HIS B 14  ? 0.59400 0.70790 0.77180 0.11990  -0.19390 0.01690  13  HIS B CB  
2366 C CG  . HIS B 14  ? 0.60500 0.76270 0.79030 0.10380  -0.18180 -0.00450 13  HIS B CG  
2367 N ND1 . HIS B 14  ? 0.62260 0.85960 0.80530 0.07190  -0.18600 -0.00590 13  HIS B ND1 
2368 C CD2 . HIS B 14  ? 0.61880 0.75400 0.81130 0.11190  -0.16540 -0.02560 13  HIS B CD2 
2369 C CE1 . HIS B 14  ? 0.63670 0.89820 0.82160 0.05840  -0.17270 -0.02660 13  HIS B CE1 
2370 N NE2 . HIS B 14  ? 0.64070 0.84140 0.83260 0.08350  -0.16020 -0.03910 13  HIS B NE2 
2371 N N   . PRO B 15  ? 0.62640 0.58300 0.77510 0.15580  -0.20100 0.04410  14  PRO B N   
2372 C CA  . PRO B 15  ? 0.63560 0.56780 0.77160 0.16480  -0.21300 0.06540  14  PRO B CA  
2373 C C   . PRO B 15  ? 0.64290 0.64420 0.78450 0.15700  -0.22990 0.08120  14  PRO B C   
2374 O O   . PRO B 15  ? 0.63970 0.71130 0.81390 0.17120  -0.23130 0.07490  14  PRO B O   
2375 C CB  . PRO B 15  ? 0.64480 0.55130 0.80270 0.20640  -0.20800 0.06230  14  PRO B CB  
2376 C CG  . PRO B 15  ? 0.63740 0.51960 0.80660 0.21360  -0.18890 0.03840  14  PRO B CG  
2377 C CD  . PRO B 15  ? 0.61970 0.55490 0.79210 0.18680  -0.18480 0.02560  14  PRO B CD  
2378 N N   . ALA B 16  ? 0.75140 0.73560 0.86330 0.13370  -0.24230 0.09870  15  ALA B N   
2379 C CA  . ALA B 16  ? 0.74100 0.78810 0.85370 0.11990  -0.25880 0.11360  15  ALA B CA  
2380 C C   . ALA B 16  ? 0.75260 0.82890 0.88670 0.15160  -0.26980 0.12580  15  ALA B C   
2381 O O   . ALA B 16  ? 0.77350 0.79790 0.90060 0.17270  -0.27280 0.13480  15  ALA B O   
2382 C CB  . ALA B 16  ? 0.74440 0.76160 0.82130 0.08700  -0.26940 0.12610  15  ALA B CB  
2383 N N   . GLU B 17  ? 0.77370 0.93340 0.93420 0.15340  -0.27800 0.12530  16  GLU B N   
2384 C CA  . GLU B 17  ? 0.77510 0.97260 0.96220 0.18210  -0.29420 0.13510  16  GLU B CA  
2385 C C   . GLU B 17  ? 0.74260 1.01290 0.93020 0.15930  -0.30760 0.14480  16  GLU B C   
2386 O O   . GLU B 17  ? 0.71860 1.04880 0.91580 0.13780  -0.30070 0.13210  16  GLU B O   
2387 C CB  . GLU B 17  ? 0.77050 1.00700 1.01100 0.22040  -0.28850 0.11240  16  GLU B CB  
2388 C CG  . GLU B 17  ? 0.79540 1.07700 1.07480 0.25320  -0.31020 0.11700  16  GLU B CG  
2389 C CD  . GLU B 17  ? 0.81880 1.11760 1.15500 0.29800  -0.30840 0.09190  16  GLU B CD  
2390 O OE1 . GLU B 17  ? 0.80830 1.09340 1.15330 0.30130  -0.28690 0.06970  16  GLU B OE1 
2391 O OE2 . GLU B 17  ? 0.83380 1.15630 1.20440 0.32560  -0.32540 0.09380  16  GLU B OE2 
2392 N N   . ASN B 18  ? 0.75860 1.02230 0.93190 0.16040  -0.32720 0.16780  17  ASN B N   
2393 C CA  . ASN B 18  ? 0.73950 1.06330 0.90620 0.13770  -0.33500 0.17350  17  ASN B CA  
2394 C C   . ASN B 18  ? 0.71840 1.14220 0.93890 0.15170  -0.33970 0.15880  17  ASN B C   
2395 O O   . ASN B 18  ? 0.72780 1.17610 0.99230 0.19120  -0.34830 0.15240  17  ASN B O   
2396 C CB  . ASN B 18  ? 0.76430 1.05570 0.90050 0.14050  -0.34290 0.18910  17  ASN B CB  
2397 C CG  . ASN B 18  ? 0.77130 0.99320 0.85480 0.11010  -0.33390 0.19840  17  ASN B CG  
2398 O OD1 . ASN B 18  ? 0.75790 0.96600 0.82740 0.08250  -0.32400 0.19060  17  ASN B OD1 
2399 N ND2 . ASN B 18  ? 0.81020 0.99070 0.86710 0.11340  -0.33890 0.21310  17  ASN B ND2 
2400 N N   . GLY B 19  ? 0.70440 1.18270 0.92110 0.11750  -0.33200 0.14900  18  GLY B N   
2401 C CA  . GLY B 19  ? 0.69370 1.27180 0.95500 0.11990  -0.32930 0.12950  18  GLY B CA  
2402 C C   . GLY B 19  ? 0.68410 1.30440 0.97060 0.11990  -0.31060 0.10340  18  GLY B C   
2403 O O   . GLY B 19  ? 0.67540 1.38970 0.99660 0.11480  -0.30450 0.08180  18  GLY B O   
2404 N N   . LYS B 20  ? 0.65850 1.20490 0.92520 0.12190  -0.29700 0.09930  19  LYS B N   
2405 C CA  . LYS B 20  ? 0.66240 1.22900 0.94550 0.12020  -0.27550 0.07120  19  LYS B CA  
2406 C C   . LYS B 20  ? 0.65820 1.19910 0.89460 0.07090  -0.26930 0.07600  19  LYS B C   
2407 O O   . LYS B 20  ? 0.66450 1.12600 0.86120 0.05700  -0.27600 0.09430  19  LYS B O   
2408 C CB  . LYS B 20  ? 0.69880 1.20060 0.99800 0.16080  -0.26640 0.06060  19  LYS B CB  
2409 C CG  . LYS B 20  ? 0.70390 1.21750 1.05030 0.21150  -0.27860 0.05640  19  LYS B CG  
2410 C CD  . LYS B 20  ? 0.69700 1.32280 1.10550 0.22640  -0.27620 0.02550  19  LYS B CD  
2411 C CE  . LYS B 20  ? 0.71750 1.35980 1.17420 0.27340  -0.29980 0.02560  19  LYS B CE  
2412 N NZ  . LYS B 20  ? 0.75610 1.31560 1.22440 0.31610  -0.30590 0.02680  19  LYS B NZ  
2413 N N   . SER B 21  ? 0.67650 0.72890 0.74590 -0.02070 -0.16120 0.07490  20  SER B N   
2414 C CA  . SER B 21  ? 0.72650 0.77870 0.79190 -0.02330 -0.15220 0.06820  20  SER B CA  
2415 C C   . SER B 21  ? 0.75630 0.79820 0.80140 -0.02050 -0.13960 0.06220  20  SER B C   
2416 O O   . SER B 21  ? 0.64970 0.69030 0.69410 -0.01510 -0.13360 0.06350  20  SER B O   
2417 C CB  . SER B 21  ? 0.69180 0.76110 0.78670 -0.02120 -0.14560 0.07030  20  SER B CB  
2418 O OG  . SER B 21  ? 0.83970 0.91010 0.93430 -0.02620 -0.14420 0.06600  20  SER B OG  
2419 N N   . ASN B 22  ? 0.68520 0.71960 0.71440 -0.02420 -0.13560 0.05570  21  ASN B N   
2420 C CA  . ASN B 22  ? 0.62090 0.64520 0.63040 -0.02240 -0.12490 0.05040  21  ASN B CA  
2421 C C   . ASN B 22  ? 0.71740 0.74030 0.72140 -0.02580 -0.11900 0.04430  21  ASN B C   
2422 O O   . ASN B 22  ? 0.69040 0.72120 0.70790 -0.02880 -0.12180 0.04450  21  ASN B O   
2423 C CB  . ASN B 22  ? 0.59190 0.60070 0.57600 -0.02310 -0.13030 0.05050  21  ASN B CB  
2424 C CG  . ASN B 22  ? 0.72070 0.72170 0.69110 -0.01940 -0.11920 0.04790  21  ASN B CG  
2425 O OD1 . ASN B 22  ? 0.60990 0.61430 0.58420 -0.01780 -0.10790 0.04420  21  ASN B OD1 
2426 N ND2 . ASN B 22  ? 0.52750 0.51750 0.48110 -0.01830 -0.12280 0.05010  21  ASN B ND2 
2427 N N   . PHE B 23  ? 0.64940 0.66220 0.63430 -0.02540 -0.11080 0.03930  22  PHE B N   
2428 C CA  . PHE B 23  ? 0.51610 0.52580 0.49320 -0.02840 -0.10560 0.03370  22  PHE B CA  
2429 C C   . PHE B 23  ? 0.58430 0.57760 0.53340 -0.03020 -0.10550 0.03040  22  PHE B C   
2430 O O   . PHE B 23  ? 0.55340 0.54000 0.49120 -0.02730 -0.10100 0.03060  22  PHE B O   
2431 C CB  . PHE B 23  ? 0.52410 0.54070 0.51070 -0.02520 -0.09260 0.03110  22  PHE B CB  
2432 C CG  . PHE B 23  ? 0.55410 0.58520 0.56530 -0.02440 -0.09110 0.03300  22  PHE B CG  
2433 C CD1 . PHE B 23  ? 0.54740 0.58770 0.57640 -0.02000 -0.09020 0.03760  22  PHE B CD1 
2434 C CD2 . PHE B 23  ? 0.56970 0.60470 0.58630 -0.02770 -0.09000 0.03060  22  PHE B CD2 
2435 C CE1 . PHE B 23  ? 0.60780 0.66100 0.65930 -0.01880 -0.08770 0.03970  22  PHE B CE1 
2436 C CE2 . PHE B 23  ? 0.65960 0.70770 0.69880 -0.02680 -0.08760 0.03280  22  PHE B CE2 
2437 C CZ  . PHE B 23  ? 0.49940 0.55660 0.55590 -0.02220 -0.08620 0.03740  22  PHE B CZ  
2438 N N   . LEU B 24  ? 0.52210 0.50860 0.46030 -0.03480 -0.10950 0.02730  23  LEU B N   
2439 C CA  . LEU B 24  ? 0.57520 0.54550 0.48620 -0.03620 -0.10760 0.02360  23  LEU B CA  
2440 C C   . LEU B 24  ? 0.57000 0.54010 0.47850 -0.03570 -0.09580 0.01860  23  LEU B C   
2441 O O   . LEU B 24  ? 0.56230 0.53940 0.48230 -0.03760 -0.09450 0.01670  23  LEU B O   
2442 C CB  . LEU B 24  ? 0.54660 0.50690 0.44450 -0.04120 -0.11960 0.02310  23  LEU B CB  
2443 C CG  . LEU B 24  ? 0.61650 0.55800 0.48430 -0.04270 -0.11780 0.01900  23  LEU B CG  
2444 C CD1 . LEU B 24  ? 0.57350 0.50410 0.42270 -0.03950 -0.11660 0.02100  23  LEU B CD1 
2445 C CD2 . LEU B 24  ? 0.60120 0.53360 0.45860 -0.04820 -0.12940 0.01750  23  LEU B CD2 
2446 N N   . ASN B 25  ? 0.50690 0.46940 0.40150 -0.03320 -0.08720 0.01700  24  ASN B N   
2447 C CA  . ASN B 25  ? 0.44830 0.41150 0.34200 -0.03210 -0.07570 0.01320  24  ASN B CA  
2448 C C   . ASN B 25  ? 0.51360 0.46170 0.38340 -0.03330 -0.07290 0.01010  24  ASN B C   
2449 O O   . ASN B 25  ? 0.54650 0.48290 0.39830 -0.03300 -0.07540 0.01120  24  ASN B O   
2450 C CB  . ASN B 25  ? 0.47920 0.44730 0.37950 -0.02800 -0.06680 0.01430  24  ASN B CB  
2451 C CG  . ASN B 25  ? 0.57780 0.55970 0.50060 -0.02610 -0.06690 0.01650  24  ASN B CG  
2452 O OD1 . ASN B 25  ? 0.56790 0.55840 0.50480 -0.02760 -0.06980 0.01650  24  ASN B OD1 
2453 N ND2 . ASN B 25  ? 0.57860 0.56220 0.50530 -0.02270 -0.06320 0.01860  24  ASN B ND2 
2454 N N   . CYS B 26  ? 0.43470 0.38260 0.30390 -0.03430 -0.06710 0.00630  25  CYS B N   
2455 C CA  . CYS B 26  ? 0.51950 0.45420 0.36820 -0.03400 -0.06080 0.00350  25  CYS B CA  
2456 C C   . CYS B 26  ? 0.53620 0.47760 0.39370 -0.03190 -0.04910 0.00190  25  CYS B C   
2457 O O   . CYS B 26  ? 0.52570 0.47540 0.39610 -0.03280 -0.04720 -0.00000 25  CYS B O   
2458 C CB  . CYS B 26  ? 0.53990 0.46390 0.37500 -0.03750 -0.06620 0.00060  25  CYS B CB  
2459 S SG  . CYS B 26  ? 0.64920 0.55650 0.45940 -0.03620 -0.05680 -0.00280 25  CYS B SG  
2460 N N   . TYR B 27  ? 0.44890 0.38740 0.30080 -0.02910 -0.04170 0.00300  26  TYR B N   
2461 C CA  . TYR B 27  ? 0.38990 0.33510 0.25110 -0.02720 -0.03170 0.00210  26  TYR B CA  
2462 C C   . TYR B 27  ? 0.47520 0.41010 0.32140 -0.02680 -0.02460 0.00000  26  TYR B C   
2463 O O   . TYR B 27  ? 0.49560 0.41890 0.32460 -0.02570 -0.02270 0.00100  26  TYR B O   
2464 C CB  . TYR B 27  ? 0.42670 0.37610 0.29420 -0.02470 -0.02810 0.00500  26  TYR B CB  
2465 C CG  . TYR B 27  ? 0.45490 0.41090 0.33220 -0.02330 -0.01920 0.00440  26  TYR B CG  
2466 C CD1 . TYR B 27  ? 0.39030 0.35680 0.28310 -0.02380 -0.01790 0.00260  26  TYR B CD1 
2467 C CD2 . TYR B 27  ? 0.48540 0.43700 0.35700 -0.02160 -0.01220 0.00610  26  TYR B CD2 
2468 C CE1 . TYR B 27  ? 0.42020 0.39190 0.32120 -0.02270 -0.01060 0.00230  26  TYR B CE1 
2469 C CE2 . TYR B 27  ? 0.47620 0.43430 0.35850 -0.02080 -0.00510 0.00620  26  TYR B CE2 
2470 C CZ  . TYR B 27  ? 0.46200 0.42970 0.35800 -0.02140 -0.00480 0.00410  26  TYR B CZ  
2471 O OH  . TYR B 27  ? 0.48560 0.45860 0.39070 -0.02080 0.00120  0.00420  26  TYR B OH  
2472 N N   . VAL B 28  ? 0.44650 0.38510 0.29860 -0.02730 -0.02050 -0.00260 27  VAL B N   
2473 C CA  . VAL B 28  ? 0.49340 0.42350 0.33390 -0.02620 -0.01260 -0.00430 27  VAL B CA  
2474 C C   . VAL B 28  ? 0.48740 0.42670 0.34110 -0.02430 -0.00370 -0.00370 27  VAL B C   
2475 O O   . VAL B 28  ? 0.49990 0.45100 0.37060 -0.02490 -0.00450 -0.00400 27  VAL B O   
2476 C CB  . VAL B 28  ? 0.51540 0.44010 0.35010 -0.02840 -0.01530 -0.00780 27  VAL B CB  
2477 C CG1 . VAL B 28  ? 0.54200 0.45440 0.35990 -0.03050 -0.02390 -0.00840 27  VAL B CG1 
2478 C CG2 . VAL B 28  ? 0.56830 0.50580 0.42210 -0.03020 -0.01880 -0.00860 27  VAL B CG2 
2479 N N   . SER B 29  ? 0.47720 0.41060 0.32310 -0.02210 0.00460  -0.00250 28  SER B N   
2480 C CA  . SER B 29  ? 0.45510 0.39710 0.31400 -0.02060 0.01220  -0.00100 28  SER B CA  
2481 C C   . SER B 29  ? 0.51780 0.45240 0.36770 -0.01840 0.02170  -0.00020 28  SER B C   
2482 O O   . SER B 29  ? 0.54620 0.46760 0.37760 -0.01750 0.02320  -0.00070 28  SER B O   
2483 C CB  . SER B 29  ? 0.51740 0.46480 0.38400 -0.02010 0.01170  0.00210  28  SER B CB  
2484 O OG  . SER B 29  ? 0.52560 0.46300 0.37790 -0.01890 0.01320  0.00450  28  SER B OG  
2485 N N   . GLY B 30  ? 0.45900 0.40180 0.32210 -0.01740 0.02820  0.00120  29  GLY B N   
2486 C CA  . GLY B 30  ? 0.45710 0.39520 0.31590 -0.01490 0.03800  0.00300  29  GLY B CA  
2487 C C   . GLY B 30  ? 0.53840 0.46940 0.38870 -0.01380 0.04150  0.00050  29  GLY B C   
2488 O O   . GLY B 30  ? 0.53020 0.45500 0.37400 -0.01110 0.05020  0.00210  29  GLY B O   
2489 N N   . PHE B 31  ? 0.49360 0.42560 0.34480 -0.01570 0.03570  -0.00310 30  PHE B N   
2490 C CA  . PHE B 31  ? 0.52160 0.44490 0.36300 -0.01490 0.03860  -0.00570 30  PHE B CA  
2491 C C   . PHE B 31  ? 0.51420 0.44650 0.37040 -0.01450 0.04160  -0.00630 30  PHE B C   
2492 O O   . PHE B 31  ? 0.45330 0.39840 0.32630 -0.01590 0.03880  -0.00570 30  PHE B O   
2493 C CB  . PHE B 31  ? 0.45060 0.36510 0.27920 -0.01740 0.02990  -0.00920 30  PHE B CB  
2494 C CG  . PHE B 31  ? 0.54790 0.47320 0.39000 -0.02080 0.02040  -0.01050 30  PHE B CG  
2495 C CD1 . PHE B 31  ? 0.50910 0.44010 0.35640 -0.02210 0.01420  -0.00890 30  PHE B CD1 
2496 C CD2 . PHE B 31  ? 0.49350 0.42230 0.34250 -0.02240 0.01820  -0.01290 30  PHE B CD2 
2497 C CE1 . PHE B 31  ? 0.44880 0.38930 0.30860 -0.02460 0.00650  -0.00970 30  PHE B CE1 
2498 C CE2 . PHE B 31  ? 0.49140 0.42980 0.35280 -0.02520 0.01050  -0.01350 30  PHE B CE2 
2499 C CZ  . PHE B 31  ? 0.50930 0.45370 0.37620 -0.02620 0.00500  -0.01180 30  PHE B CZ  
2500 N N   . HIS B 32  ? 0.57610 0.41850 0.31080 0.07430  0.12340  -0.03480 31  HIS B N   
2501 C CA  . HIS B 32  ? 0.60270 0.41360 0.32300 0.07220  0.12140  -0.03760 31  HIS B CA  
2502 C C   . HIS B 32  ? 0.66190 0.40920 0.31860 0.09760  0.10340  -0.05200 31  HIS B C   
2503 O O   . HIS B 32  ? 0.67150 0.42660 0.31520 0.13040  0.10390  -0.05080 31  HIS B O   
2504 C CB  . HIS B 32  ? 0.57930 0.42800 0.34420 0.07880  0.13540  -0.02340 31  HIS B CB  
2505 C CG  . HIS B 32  ? 0.58800 0.42720 0.36330 0.06310  0.13570  -0.02350 31  HIS B CG  
2506 N ND1 . HIS B 32  ? 0.62050 0.41240 0.35840 0.06990  0.13060  -0.03100 31  HIS B ND1 
2507 C CD2 . HIS B 32  ? 0.56200 0.43050 0.37630 0.04530  0.13750  -0.01800 31  HIS B CD2 
2508 C CE1 . HIS B 32  ? 0.61620 0.41330 0.37290 0.05340  0.13430  -0.02750 31  HIS B CE1 
2509 N NE2 . HIS B 32  ? 0.58100 0.42690 0.38380 0.04070  0.13770  -0.02010 31  HIS B NE2 
2510 N N   . PRO B 33  ? 0.71530 0.39410 0.32810 0.08520  0.08030  -0.06450 32  PRO B N   
2511 C CA  . PRO B 33  ? 0.72550 0.39670 0.35320 0.04430  0.07530  -0.05780 32  PRO B CA  
2512 C C   . PRO B 33  ? 0.72080 0.42060 0.37250 0.01050  0.06700  -0.04800 32  PRO B C   
2513 O O   . PRO B 33  ? 0.70710 0.41310 0.34390 0.02150  0.07250  -0.05570 32  PRO B O   
2514 C CB  . PRO B 33  ? 0.79350 0.39130 0.39030 0.04020  0.03340  -0.06330 32  PRO B CB  
2515 C CG  . PRO B 33  ? 0.84730 0.38180 0.37950 0.07770  0.00770  -0.08650 32  PRO B CG  
2516 C CD  . PRO B 33  ? 0.77730 0.38840 0.33520 0.11240  0.04590  -0.07970 32  PRO B CD  
2517 N N   . SER B 34  ? 0.61350 0.33720 0.30150 -0.02640 0.05500  -0.02740 33  SER B N   
2518 C CA  . SER B 34  ? 0.59620 0.37360 0.31520 -0.05230 0.05650  -0.01090 33  SER B CA  
2519 C C   . SER B 34  ? 0.67360 0.41920 0.38450 -0.07650 0.01650  -0.00240 33  SER B C   
2520 O O   . SER B 34  ? 0.64930 0.43580 0.37690 -0.09010 0.01920  0.00690  33  SER B O   
2521 C CB  . SER B 34  ? 0.56920 0.40770 0.33080 -0.07010 0.06630  0.01420  33  SER B CB  
2522 O OG  . SER B 34  ? 0.65020 0.46380 0.41910 -0.09060 0.03940  0.03400  33  SER B OG  
2523 N N   . ASP B 35  ? 0.80900 0.48040 0.49740 -0.08270 -0.02630 -0.00380 34  ASP B N   
2524 C CA  . ASP B 35  ? 0.87180 0.49920 0.55540 -0.10620 -0.07730 0.00400  34  ASP B CA  
2525 C C   . ASP B 35  ? 0.85230 0.46460 0.49750 -0.08110 -0.07220 -0.02350 34  ASP B C   
2526 O O   . ASP B 35  ? 0.83030 0.40890 0.42430 -0.03590 -0.05720 -0.05510 34  ASP B O   
2527 C CB  . ASP B 35  ? 0.93110 0.45700 0.58430 -0.10640 -0.13560 -0.00260 34  ASP B CB  
2528 C CG  . ASP B 35  ? 0.94640 0.48660 0.64870 -0.14330 -0.15380 0.03660  34  ASP B CG  
2529 O OD1 . ASP B 35  ? 0.89270 0.52760 0.64670 -0.16160 -0.11620 0.06800  34  ASP B OD1 
2530 O OD2 . ASP B 35  ? 0.99310 0.44820 0.67890 -0.14980 -0.20910 0.03670  34  ASP B OD2 
2531 N N   . ILE B 36  ? 0.78190 0.42890 0.45380 -0.10750 -0.08210 -0.00680 35  ILE B N   
2532 C CA  . ILE B 36  ? 0.76910 0.40450 0.40750 -0.08700 -0.07970 -0.03010 35  ILE B CA  
2533 C C   . ILE B 36  ? 0.80120 0.44450 0.47110 -0.12680 -0.11950 -0.00550 35  ILE B C   
2534 O O   . ILE B 36  ? 0.79180 0.49520 0.52310 -0.16720 -0.12400 0.03720  35  ILE B O   
2535 C CB  . ILE B 36  ? 0.68110 0.38990 0.32700 -0.06530 -0.01790 -0.03780 35  ILE B CB  
2536 C CG1 . ILE B 36  ? 0.65180 0.34480 0.25750 -0.03700 -0.01270 -0.06130 35  ILE B CG1 
2537 C CG2 . ILE B 36  ? 0.63110 0.43070 0.33510 -0.09450 0.00400  -0.00830 35  ILE B CG2 
2538 C CD1 . ILE B 36  ? 0.57520 0.32390 0.18740 -0.01020 0.04200  -0.06640 35  ILE B CD1 
2539 N N   . GLU B 37  ? 0.92840 0.51360 0.55610 -0.11190 -0.15110 -0.02910 36  GLU B N   
2540 C CA  . GLU B 37  ? 0.94750 0.53290 0.60310 -0.14700 -0.19450 -0.00840 36  GLU B CA  
2541 C C   . GLU B 37  ? 0.90910 0.53700 0.54860 -0.12780 -0.15960 -0.02510 36  GLU B C   
2542 O O   . GLU B 37  ? 0.90010 0.49020 0.47740 -0.08060 -0.14460 -0.06360 36  GLU B O   
2543 C CB  . GLU B 37  ? 1.00720 0.47100 0.62500 -0.14600 -0.27800 -0.02360 36  GLU B CB  
2544 C CG  . GLU B 37  ? 1.04430 0.50990 0.72320 -0.20170 -0.33920 0.01880  36  GLU B CG  
2545 C CD  . GLU B 37  ? 1.14610 0.52160 0.81150 -0.18330 -0.41010 0.01720  36  GLU B CD  
2546 O OE1 . GLU B 37  ? 1.18610 0.50800 0.82130 -0.15730 -0.42380 0.00300  36  GLU B OE1 
2547 O OE2 . GLU B 37  ? 1.18880 0.54600 0.87060 -0.19280 -0.45450 0.03010  36  GLU B OE2 
2548 N N   . VAL B 38  ? 0.80310 0.51620 0.49820 -0.16010 -0.14570 0.00740  37  VAL B N   
2549 C CA  . VAL B 38  ? 0.76650 0.52680 0.45290 -0.14560 -0.11340 -0.00460 37  VAL B CA  
2550 C C   . VAL B 38  ? 0.78560 0.56940 0.51110 -0.18310 -0.15160 0.02480  37  VAL B C   
2551 O O   . VAL B 38  ? 0.76290 0.60960 0.55400 -0.22260 -0.16210 0.07400  37  VAL B O   
2552 C CB  . VAL B 38  ? 0.67970 0.53390 0.39120 -0.13630 -0.04990 0.00270  37  VAL B CB  
2553 C CG1 . VAL B 38  ? 0.62560 0.52250 0.33160 -0.12530 -0.02730 -0.00640 37  VAL B CG1 
2554 C CG2 . VAL B 38  ? 0.64430 0.47630 0.32700 -0.10250 -0.01700 -0.02140 37  VAL B CG2 
2555 N N   . ASP B 39  ? 0.85830 0.59930 0.54610 -0.16820 -0.17190 -0.00050 38  ASP B N   
2556 C CA  . ASP B 39  ? 0.86610 0.62850 0.58880 -0.20030 -0.20820 0.02420  38  ASP B CA  
2557 C C   . ASP B 39  ? 0.82420 0.62910 0.52390 -0.17610 -0.16890 0.00340  38  ASP B C   
2558 O O   . ASP B 39  ? 0.81340 0.57690 0.45040 -0.13200 -0.14690 -0.03880 38  ASP B O   
2559 C CB  . ASP B 39  ? 0.91620 0.56400 0.61330 -0.20750 -0.29190 0.01220  38  ASP B CB  
2560 C CG  . ASP B 39  ? 0.95480 0.56310 0.69280 -0.24410 -0.34630 0.04510  38  ASP B CG  
2561 O OD1 . ASP B 39  ? 0.91120 0.60940 0.73000 -0.28690 -0.33570 0.10280  38  ASP B OD1 
2562 O OD2 . ASP B 39  ? 1.03380 0.53950 0.72980 -0.21390 -0.38540 0.02020  38  ASP B OD2 
2563 N N   . LEU B 40  ? 0.79120 0.68380 0.54320 -0.20280 -0.16110 0.03780  39  LEU B N   
2564 C CA  . LEU B 40  ? 0.76110 0.68680 0.49550 -0.18620 -0.13870 0.02200  39  LEU B CA  
2565 C C   . LEU B 40  ? 0.80380 0.67600 0.53410 -0.20260 -0.20020 0.02180  39  LEU B C   
2566 O O   . LEU B 40  ? 0.81000 0.69220 0.59780 -0.24670 -0.25020 0.06470  39  LEU B O   
2567 C CB  . LEU B 40  ? 0.68350 0.73390 0.46750 -0.19590 -0.09810 0.05560  39  LEU B CB  
2568 C CG  . LEU B 40  ? 0.62340 0.71490 0.40380 -0.17270 -0.04590 0.04910  39  LEU B CG  
2569 C CD1 . LEU B 40  ? 0.50950 0.70850 0.31420 -0.16270 -0.00980 0.06720  39  LEU B CD1 
2570 C CD2 . LEU B 40  ? 0.59940 0.62720 0.32150 -0.13460 -0.02190 0.00120  39  LEU B CD2 
2571 N N   . LEU B 41  ? 0.79280 0.60870 0.45850 -0.16660 -0.20080 -0.02210 40  LEU B N   
2572 C CA  . LEU B 41  ? 0.83940 0.58390 0.48520 -0.17160 -0.26610 -0.03300 40  LEU B CA  
2573 C C   . LEU B 41  ? 0.81140 0.61230 0.46360 -0.17090 -0.24930 -0.03190 40  LEU B C   
2574 O O   . LEU B 41  ? 0.76390 0.60650 0.38830 -0.13940 -0.19040 -0.05180 40  LEU B O   
2575 C CB  . LEU B 41  ? 0.89930 0.54130 0.47430 -0.11300 -0.27580 -0.08120 40  LEU B CB  
2576 C CG  . LEU B 41  ? 0.95570 0.53180 0.50710 -0.09140 -0.28730 -0.09310 40  LEU B CG  
2577 C CD1 . LEU B 41  ? 1.02670 0.53080 0.52260 -0.02820 -0.29860 -0.12730 40  LEU B CD1 
2578 C CD2 . LEU B 41  ? 0.99590 0.54370 0.60040 -0.14110 -0.34710 -0.05650 40  LEU B CD2 
2579 N N   . LYS B 42  ? 0.81500 0.61570 0.50970 -0.20580 -0.30430 -0.00520 41  LYS B N   
2580 C CA  . LYS B 42  ? 0.80350 0.63850 0.50030 -0.20170 -0.30070 -0.00770 41  LYS B CA  
2581 C C   . LYS B 42  ? 0.90320 0.63550 0.57530 -0.17880 -0.35190 -0.03280 41  LYS B C   
2582 O O   . LYS B 42  ? 0.96890 0.65760 0.68400 -0.20680 -0.41170 -0.00500 41  LYS B O   
2583 C CB  . LYS B 42  ? 0.75160 0.70250 0.53750 -0.25280 -0.30590 0.05500  41  LYS B CB  
2584 C CG  . LYS B 42  ? 0.74180 0.72960 0.53040 -0.24730 -0.30280 0.05310  41  LYS B CG  
2585 C CD  . LYS B 42  ? 0.70010 0.80910 0.58340 -0.28820 -0.30450 0.12220  41  LYS B CD  
2586 C CE  . LYS B 42  ? 0.69030 0.83480 0.56970 -0.27810 -0.29840 0.11610  41  LYS B CE  
2587 N NZ  . LYS B 42  ? 0.66350 0.92340 0.63250 -0.30930 -0.29780 0.18630  41  LYS B NZ  
2588 N N   . ASN B 43  ? 0.59000 0.87110 0.59650 -0.10810 -0.31590 -0.00300 42  ASN B N   
2589 C CA  . ASN B 43  ? 0.62970 0.89340 0.60710 -0.10770 -0.33250 -0.01090 42  ASN B CA  
2590 C C   . ASN B 43  ? 0.67190 0.87330 0.59220 -0.13530 -0.33260 -0.00030 42  ASN B C   
2591 O O   . ASN B 43  ? 0.71470 0.90560 0.61980 -0.15830 -0.34520 -0.01490 42  ASN B O   
2592 C CB  . ASN B 43  ? 0.64230 0.96260 0.66420 -0.11700 -0.34860 -0.04540 42  ASN B CB  
2593 C CG  . ASN B 43  ? 0.61470 0.98850 0.68280 -0.07930 -0.35560 -0.06370 42  ASN B CG  
2594 O OD1 . ASN B 43  ? 0.60080 0.96750 0.64780 -0.04850 -0.34930 -0.04480 42  ASN B OD1 
2595 N ND2 . ASN B 43  ? 0.62160 1.02670 0.74830 -0.08710 -0.36700 -0.09130 42  ASN B ND2 
2596 N N   . GLY B 44  ? 0.69870 0.85430 0.58670 -0.13050 -0.31990 0.02160  43  GLY B N   
2597 C CA  . GLY B 44  ? 0.76230 0.84650 0.58880 -0.14760 -0.32210 0.02800  43  GLY B CA  
2598 C C   . GLY B 44  ? 0.82050 0.88290 0.63240 -0.19640 -0.31990 0.02520  43  GLY B C   
2599 O O   . GLY B 44  ? 0.87360 0.85850 0.62390 -0.20750 -0.32310 0.03040  43  GLY B O   
2600 N N   . GLU B 45  ? 0.77240 0.89720 0.63500 -0.22520 -0.31250 0.01480  44  GLU B N   
2601 C CA  . GLU B 45  ? 0.82390 0.93300 0.66990 -0.28140 -0.30350 0.01130  44  GLU B CA  
2602 C C   . GLU B 45  ? 0.82660 0.94540 0.67890 -0.28750 -0.28570 0.02470  44  GLU B C   
2603 O O   . GLU B 45  ? 0.75220 0.93880 0.66200 -0.26060 -0.27800 0.02390  44  GLU B O   
2604 C CB  . GLU B 45  ? 0.80680 0.98600 0.70590 -0.31420 -0.30030 -0.01440 44  GLU B CB  
2605 C CG  . GLU B 45  ? 0.84850 0.99880 0.72660 -0.32410 -0.31920 -0.02890 44  GLU B CG  
2606 C CD  . GLU B 45  ? 0.86100 1.08030 0.79560 -0.35780 -0.31600 -0.05750 44  GLU B CD  
2607 O OE1 . GLU B 45  ? 0.84200 1.12640 0.82480 -0.37970 -0.29470 -0.06570 44  GLU B OE1 
2608 O OE2 . GLU B 45  ? 0.89770 1.10830 0.82990 -0.35970 -0.33470 -0.07420 44  GLU B OE2 
2609 N N   . ARG B 46  ? 0.84160 0.88090 0.63280 -0.31210 -0.27410 0.03550  45  ARG B N   
2610 C CA  . ARG B 46  ? 0.85960 0.89080 0.64560 -0.31010 -0.25270 0.04830  45  ARG B CA  
2611 C C   . ARG B 46  ? 0.81350 0.94350 0.66190 -0.34080 -0.23400 0.03600  45  ARG B C   
2612 O O   . ARG B 46  ? 0.83160 0.99480 0.69080 -0.39290 -0.22870 0.02100  45  ARG B O   
2613 C CB  . ARG B 46  ? 0.94980 0.86540 0.64550 -0.33510 -0.24960 0.06000  45  ARG B CB  
2614 C CG  . ARG B 46  ? 0.98860 0.87890 0.66410 -0.32830 -0.23150 0.07350  45  ARG B CG  
2615 C CD  . ARG B 46  ? 1.08270 0.84030 0.65570 -0.34420 -0.23750 0.08460  45  ARG B CD  
2616 N NE  . ARG B 46  ? 1.16020 0.88050 0.68860 -0.41350 -0.23480 0.08260  45  ARG B NE  
2617 C CZ  . ARG B 46  ? 1.20910 0.93180 0.71750 -0.46580 -0.21150 0.08820  45  ARG B CZ  
2618 N NH1 . ARG B 46  ? 1.19050 0.95070 0.71800 -0.45240 -0.19040 0.09450  45  ARG B NH1 
2619 N NH2 . ARG B 46  ? 1.26650 0.95280 0.73230 -0.53530 -0.20910 0.08700  45  ARG B NH2 
2620 N N   . ILE B 47  ? 0.76610 0.94900 0.65930 -0.30800 -0.22540 0.03880  46  ILE B N   
2621 C CA  . ILE B 47  ? 0.72290 1.00130 0.67260 -0.32920 -0.20720 0.02390  46  ILE B CA  
2622 C C   . ILE B 47  ? 0.82150 1.05100 0.71530 -0.36940 -0.18110 0.03460  46  ILE B C   
2623 O O   . ILE B 47  ? 0.87550 1.00980 0.70530 -0.35190 -0.18040 0.05540  46  ILE B O   
2624 C CB  . ILE B 47  ? 0.63800 0.98050 0.65000 -0.27450 -0.21360 0.02200  46  ILE B CB  
2625 C CG1 . ILE B 47  ? 0.55580 0.92960 0.61280 -0.23340 -0.23380 0.01050  46  ILE B CG1 
2626 C CG2 . ILE B 47  ? 0.58940 1.02220 0.65080 -0.28830 -0.19430 0.00530  46  ILE B CG2 
2627 C CD1 . ILE B 47  ? 0.49910 0.86390 0.57720 -0.17100 -0.24120 0.02000  46  ILE B CD1 
2628 N N   . GLU B 48  ? 0.71350 1.00910 0.62870 -0.42410 -0.16010 0.01850  47  GLU B N   
2629 C CA  . GLU B 48  ? 0.79510 1.03530 0.64100 -0.47800 -0.13380 0.03020  47  GLU B CA  
2630 C C   . GLU B 48  ? 0.77450 1.02580 0.61670 -0.45540 -0.11520 0.03810  47  GLU B C   
2631 O O   . GLU B 48  ? 0.84460 0.98920 0.60540 -0.45170 -0.11190 0.06080  47  GLU B O   
2632 C CB  . GLU B 48  ? 0.83690 1.15110 0.70690 -0.55330 -0.11400 0.00900  47  GLU B CB  
2633 N N   . LYS B 49  ? 1.03490 1.41170 0.96220 -0.43690 -0.10690 0.01660  48  LYS B N   
2634 C CA  . LYS B 49  ? 1.05120 1.45400 0.97770 -0.42440 -0.08660 0.01800  48  LYS B CA  
2635 C C   . LYS B 49  ? 1.02120 1.38700 0.95610 -0.34830 -0.10680 0.03120  48  LYS B C   
2636 O O   . LYS B 49  ? 0.93110 1.37850 0.93560 -0.30630 -0.11310 0.01690  48  LYS B O   
2637 C CB  . LYS B 49  ? 0.95050 1.51010 0.96420 -0.43960 -0.06970 -0.01710 48  LYS B CB  
2638 C CG  . LYS B 49  ? 0.98500 1.59430 0.99270 -0.52340 -0.04150 -0.03280 48  LYS B CG  
2639 C CD  . LYS B 49  ? 1.10800 1.62150 1.00780 -0.57730 -0.01180 -0.00690 48  LYS B CD  
2640 C CE  . LYS B 49  ? 1.15670 1.72060 1.04570 -0.65000 0.02330  -0.02290 48  LYS B CE  
2641 N NZ  . LYS B 49  ? 1.26910 1.74630 1.04850 -0.70220 0.05240  0.00220  48  LYS B NZ  
2642 N N   . VAL B 50  ? 0.67030 0.90980 0.53190 -0.33140 -0.11880 0.05650  49  VAL B N   
2643 C CA  . VAL B 50  ? 0.62420 0.82240 0.48960 -0.26570 -0.13650 0.06840  49  VAL B CA  
2644 C C   . VAL B 50  ? 0.70060 0.83350 0.50400 -0.26060 -0.12440 0.08080  49  VAL B C   
2645 O O   . VAL B 50  ? 0.79390 0.83010 0.50630 -0.29440 -0.11740 0.09410  49  VAL B O   
2646 C CB  . VAL B 50  ? 0.63140 0.74670 0.46540 -0.24250 -0.15960 0.08110  49  VAL B CB  
2647 C CG1 . VAL B 50  ? 0.58950 0.67070 0.43010 -0.18170 -0.17340 0.09080  49  VAL B CG1 
2648 C CG2 . VAL B 50  ? 0.59150 0.76830 0.48140 -0.24230 -0.17390 0.06930  49  VAL B CG2 
2649 N N   . GLU B 51  ? 0.71140 0.88680 0.55780 -0.21600 -0.12670 0.07630  50  GLU B N   
2650 C CA  . GLU B 51  ? 0.75750 0.87150 0.55030 -0.19920 -0.12100 0.08580  50  GLU B CA  
2651 C C   . GLU B 51  ? 0.69320 0.75210 0.49220 -0.13710 -0.14600 0.09440  50  GLU B C   
2652 O O   . GLU B 51  ? 0.60030 0.68590 0.45370 -0.10820 -0.16330 0.09310  50  GLU B O   
2653 C CB  . GLU B 51  ? 0.75580 0.96410 0.59070 -0.19720 -0.10370 0.06970  50  GLU B CB  
2654 C CG  . GLU B 51  ? 0.77330 1.07550 0.63270 -0.25460 -0.07860 0.05200  50  GLU B CG  
2655 C CD  . GLU B 51  ? 0.74170 1.15000 0.64700 -0.24830 -0.06160 0.02960  50  GLU B CD  
2656 O OE1 . GLU B 51  ? 0.82680 1.19600 0.67210 -0.25290 -0.04540 0.03660  50  GLU B OE1 
2657 O OE2 . GLU B 51  ? 0.58890 1.11790 0.58710 -0.23530 -0.06730 0.00280  50  GLU B OE2 
2658 N N   . HIS B 52  ? 0.76860 0.74870 0.50780 -0.11840 -0.14790 0.10240  51  HIS B N   
2659 C CA  . HIS B 52  ? 0.69260 0.63150 0.44540 -0.06040 -0.17060 0.10530  51  HIS B CA  
2660 C C   . HIS B 52  ? 0.70770 0.62370 0.43920 -0.03250 -0.17070 0.10340  51  HIS B C   
2661 O O   . HIS B 52  ? 0.78710 0.68040 0.45880 -0.06060 -0.15400 0.10500  51  HIS B O   
2662 C CB  . HIS B 52  ? 0.69940 0.53450 0.39060 -0.05480 -0.18630 0.11320  51  HIS B CB  
2663 C CG  . HIS B 52  ? 0.79430 0.51710 0.37270 -0.08010 -0.18500 0.12060  51  HIS B CG  
2664 N ND1 . HIS B 52  ? 0.82720 0.48110 0.35190 -0.05400 -0.19250 0.12150  51  HIS B ND1 
2665 C CD2 . HIS B 52  ? 0.87930 0.53790 0.38200 -0.12980 -0.18060 0.12780  51  HIS B CD2 
2666 C CE1 . HIS B 52  ? 0.94110 0.49040 0.35980 -0.08560 -0.19220 0.12900  51  HIS B CE1 
2667 N NE2 . HIS B 52  ? 0.97200 0.51760 0.37070 -0.13410 -0.18630 0.13500  51  HIS B NE2 
2668 N N   . SER B 53  ? 0.53770 0.50910 0.45370 0.03830  -0.00460 -0.00610 52  SER B N   
2669 C CA  . SER B 53  ? 0.52200 0.50150 0.42310 0.03950  0.00390  -0.00510 52  SER B CA  
2670 C C   . SER B 53  ? 0.50840 0.49500 0.41660 0.02690  0.00880  0.00840  52  SER B C   
2671 O O   . SER B 53  ? 0.50980 0.48730 0.43290 0.01800  0.00350  0.01410  52  SER B O   
2672 C CB  . SER B 53  ? 0.51440 0.46290 0.38870 0.04490  -0.00090 -0.01490 52  SER B CB  
2673 O OG  . SER B 53  ? 0.50080 0.42560 0.36690 0.03630  -0.00340 -0.01040 52  SER B OG  
2674 N N   . ASP B 54  ? 0.54250 0.54570 0.44060 0.02820  0.01640  0.01170  53  ASP B N   
2675 C CA  . ASP B 54  ? 0.52990 0.53870 0.43220 0.01690  0.01980  0.02560  53  ASP B CA  
2676 C C   . ASP B 54  ? 0.51980 0.49260 0.40670 0.01220  0.01510  0.02040  53  ASP B C   
2677 O O   . ASP B 54  ? 0.51380 0.46560 0.37980 0.01850  0.01280  0.00900  53  ASP B O   
2678 C CB  . ASP B 54  ? 0.51500 0.55540 0.40560 0.02240  0.02850  0.02940  53  ASP B CB  
2679 C CG  . ASP B 54  ? 0.52410 0.61190 0.42870 0.02930  0.03600  0.03520  53  ASP B CG  
2680 O OD1 . ASP B 54  ? 0.53240 0.63690 0.46870 0.02030  0.03590  0.05080  53  ASP B OD1 
2681 O OD2 . ASP B 54  ? 0.52400 0.63460 0.41100 0.04500  0.04050  0.02300  53  ASP B OD2 
2682 N N   . LEU B 55  ? 0.45990 0.42850 0.36160 0.00100  0.01240  0.03040  54  LEU B N   
2683 C CA  . LEU B 55  ? 0.44800 0.39030 0.34020 -0.00300 0.00870  0.02580  54  LEU B CA  
2684 C C   . LEU B 55  ? 0.44170 0.37680 0.31130 -0.00100 0.01230  0.02290  54  LEU B C   
2685 O O   . LEU B 55  ? 0.44480 0.39740 0.31180 -0.00160 0.01600  0.02940  54  LEU B O   
2686 C CB  . LEU B 55  ? 0.44850 0.39190 0.36560 -0.01320 0.00270  0.03520  54  LEU B CB  
2687 C CG  . LEU B 55  ? 0.44340 0.36510 0.35380 -0.01440 -0.00130 0.02710  54  LEU B CG  
2688 C CD1 . LEU B 55  ? 0.45480 0.36690 0.36550 -0.00800 -0.00720 0.01440  54  LEU B CD1 
2689 C CD2 . LEU B 55  ? 0.44400 0.36690 0.37720 -0.02330 -0.00800 0.03570  54  LEU B CD2 
2690 N N   . SER B 56  ? 0.50810 0.42020 0.36290 0.00160  0.00990  0.01440  55  SER B N   
2691 C CA  . SER B 56  ? 0.50640 0.40660 0.34730 0.00230  0.00900  0.01140  55  SER B CA  
2692 C C   . SER B 56  ? 0.50170 0.38330 0.34170 -0.00280 0.00700  0.01210  55  SER B C   
2693 O O   . SER B 56  ? 0.49800 0.37990 0.34360 -0.00390 0.00710  0.01240  55  SER B O   
2694 C CB  . SER B 56  ? 0.52730 0.42440 0.35650 0.01340  0.00540  0.00130  55  SER B CB  
2695 O OG  . SER B 56  ? 0.54060 0.42860 0.36150 0.01550  0.00040  -0.00370 55  SER B OG  
2696 N N   . PHE B 57  ? 0.45920 0.32850 0.29360 -0.00460 0.00430  0.01180  56  PHE B N   
2697 C CA  . PHE B 57  ? 0.45880 0.31900 0.29620 -0.01030 0.00440  0.01640  56  PHE B CA  
2698 C C   . PHE B 57  ? 0.47170 0.31600 0.30800 -0.01140 -0.00200 0.01820  56  PHE B C   
2699 O O   . PHE B 57  ? 0.48120 0.31860 0.31480 -0.00680 -0.00910 0.01160  56  PHE B O   
2700 C CB  . PHE B 57  ? 0.44870 0.31550 0.29600 -0.01660 0.00660  0.01850  56  PHE B CB  
2701 C CG  . PHE B 57  ? 0.44930 0.31650 0.29730 -0.01900 0.00430  0.01920  56  PHE B CG  
2702 C CD1 . PHE B 57  ? 0.45680 0.31310 0.30350 -0.02090 -0.00020 0.01880  56  PHE B CD1 
2703 C CD2 . PHE B 57  ? 0.44480 0.32560 0.29740 -0.01960 0.00490  0.02250  56  PHE B CD2 
2704 C CE1 . PHE B 57  ? 0.46070 0.31890 0.30520 -0.02110 -0.00420 0.01780  56  PHE B CE1 
2705 C CE2 . PHE B 57  ? 0.44910 0.33570 0.29900 -0.02100 0.00280  0.02600  56  PHE B CE2 
2706 C CZ  . PHE B 57  ? 0.45740 0.33220 0.30070 -0.02060 -0.00190 0.02170  56  PHE B CZ  
2707 N N   . SER B 58  ? 0.52540 0.36730 0.36640 -0.01650 -0.00110 0.02750  57  SER B N   
2708 C CA  . SER B 58  ? 0.54380 0.37200 0.39320 -0.02100 -0.00900 0.03630  57  SER B CA  
2709 C C   . SER B 58  ? 0.54510 0.37190 0.40620 -0.02800 -0.01040 0.03870  57  SER B C   
2710 O O   . SER B 58  ? 0.53120 0.36850 0.39220 -0.02940 -0.00430 0.03470  57  SER B O   
2711 C CB  . SER B 58  ? 0.54190 0.37770 0.39270 -0.02420 -0.00570 0.05180  57  SER B CB  
2712 O OG  . SER B 58  ? 0.54590 0.38350 0.38530 -0.01700 -0.00540 0.04870  57  SER B OG  
2713 N N   . LYS B 59  ? 0.62530 0.43810 0.50140 -0.03310 -0.02110 0.04670  58  LYS B N   
2714 C CA  . LYS B 59  ? 0.62610 0.43600 0.51750 -0.03970 -0.02550 0.04840  58  LYS B CA  
2715 C C   . LYS B 59  ? 0.60410 0.43660 0.50210 -0.04620 -0.01230 0.05740  58  LYS B C   
2716 O O   . LYS B 59  ? 0.60490 0.43910 0.51170 -0.04930 -0.01320 0.05380  58  LYS B O   
2717 C CB  . LYS B 59  ? 0.64410 0.43420 0.55870 -0.04490 -0.04300 0.05720  58  LYS B CB  
2718 C CG  . LYS B 59  ? 0.67760 0.44400 0.58940 -0.03410 -0.06200 0.03960  58  LYS B CG  
2719 C CD  . LYS B 59  ? 0.69830 0.46700 0.59450 -0.02460 -0.06360 0.01800  58  LYS B CD  
2720 C CE  . LYS B 59  ? 0.72350 0.47290 0.62210 -0.01150 -0.08720 -0.00240 58  LYS B CE  
2721 N NZ  . LYS B 59  ? 0.71430 0.47810 0.58620 0.00420  -0.08540 -0.02410 58  LYS B NZ  
2722 N N   . ASP B 60  ? 0.56520 0.41760 0.45840 -0.04600 -0.00110 0.06640  59  ASP B N   
2723 C CA  . ASP B 60  ? 0.55860 0.43910 0.45640 -0.04690 0.01080  0.06890  59  ASP B CA  
2724 C C   . ASP B 60  ? 0.55010 0.43780 0.43700 -0.03900 0.01540  0.05120  59  ASP B C   
2725 O O   . ASP B 60  ? 0.54600 0.45690 0.43720 -0.03570 0.02210  0.04750  59  ASP B O   
2726 C CB  . ASP B 60  ? 0.55850 0.46550 0.45570 -0.04750 0.01960  0.08620  59  ASP B CB  
2727 C CG  . ASP B 60  ? 0.56090 0.47180 0.43570 -0.03820 0.02260  0.08120  59  ASP B CG  
2728 O OD1 . ASP B 60  ? 0.54990 0.44300 0.41360 -0.03250 0.01820  0.06540  59  ASP B OD1 
2729 O OD2 . ASP B 60  ? 0.55650 0.49220 0.42540 -0.03630 0.02920  0.09450  59  ASP B OD2 
2730 N N   . TRP B 61  ? 0.47210 0.34340 0.34870 -0.03540 0.01030  0.04090  60  TRP B N   
2731 C CA  . TRP B 61  ? 0.46350 0.33800 0.33740 -0.03100 0.01050  0.02940  60  TRP B CA  
2732 C C   . TRP B 61  ? 0.45980 0.34550 0.32670 -0.02380 0.01390  0.02440  60  TRP B C   
2733 O O   . TRP B 61  ? 0.45690 0.34410 0.32810 -0.02100 0.01090  0.01670  60  TRP B O   
2734 C CB  . TRP B 61  ? 0.46650 0.34850 0.35530 -0.03310 0.00950  0.02530  60  TRP B CB  
2735 C CG  . TRP B 61  ? 0.47150 0.34320 0.36840 -0.03960 0.00440  0.02930  60  TRP B CG  
2736 C CD1 . TRP B 61  ? 0.47960 0.35770 0.39130 -0.04440 0.00520  0.03500  60  TRP B CD1 
2737 C CD2 . TRP B 61  ? 0.47200 0.32910 0.36360 -0.04070 -0.00320 0.02760  60  TRP B CD2 
2738 N NE1 . TRP B 61  ? 0.48380 0.34670 0.40180 -0.04900 -0.00380 0.03560  60  TRP B NE1 
2739 C CE2 . TRP B 61  ? 0.48310 0.33360 0.38600 -0.04550 -0.00920 0.02990  60  TRP B CE2 
2740 C CE3 . TRP B 61  ? 0.46920 0.32330 0.34790 -0.03700 -0.00550 0.02490  60  TRP B CE3 
2741 C CZ2 . TRP B 61  ? 0.49670 0.33540 0.39510 -0.04490 -0.01930 0.02630  60  TRP B CZ2 
2742 C CZ3 . TRP B 61  ? 0.48190 0.33050 0.35430 -0.03610 -0.01270 0.02350  60  TRP B CZ3 
2743 C CH2 . TRP B 61  ? 0.49850 0.33790 0.37890 -0.03920 -0.02050 0.02260  60  TRP B CH2 
2744 N N   . SER B 62  ? 0.51740 0.41100 0.37580 -0.02090 0.01770  0.03010  61  SER B N   
2745 C CA  . SER B 62  ? 0.51620 0.41980 0.36630 -0.01220 0.01830  0.02300  61  SER B CA  
2746 C C   . SER B 62  ? 0.51420 0.40280 0.35790 -0.01050 0.01390  0.02070  61  SER B C   
2747 O O   . SER B 62  ? 0.51600 0.39010 0.35620 -0.01340 0.01160  0.02580  61  SER B O   
2748 C CB  . SER B 62  ? 0.52360 0.44620 0.36360 -0.00830 0.02370  0.03160  61  SER B CB  
2749 O OG  . SER B 62  ? 0.52930 0.43920 0.36520 -0.01400 0.02220  0.04740  61  SER B OG  
2750 N N   . PHE B 63  ? 0.54130 0.33490 0.32580 0.03690  -0.04330 0.02680  62  PHE B N   
2751 C CA  . PHE B 63  ? 0.51810 0.29540 0.28440 0.01840  -0.04880 0.02770  62  PHE B CA  
2752 C C   . PHE B 63  ? 0.49560 0.28960 0.25590 0.01010  -0.04210 0.02440  62  PHE B C   
2753 O O   . PHE B 63  ? 0.50210 0.31290 0.26140 0.01720  -0.03370 0.02090  62  PHE B O   
2754 C CB  . PHE B 63  ? 0.55740 0.29710 0.31010 0.01510  -0.05790 0.02400  62  PHE B CB  
2755 C CG  . PHE B 63  ? 0.58240 0.30110 0.34420 0.02020  -0.06970 0.03380  62  PHE B CG  
2756 C CD1 . PHE B 63  ? 0.55750 0.28130 0.31640 0.00730  -0.07660 0.05380  62  PHE B CD1 
2757 C CD2 . PHE B 63  ? 0.63430 0.33280 0.40660 0.04120  -0.07490 0.02340  62  PHE B CD2 
2758 C CE1 . PHE B 63  ? 0.57640 0.28390 0.34290 0.01090  -0.09000 0.06890  62  PHE B CE1 
2759 C CE2 . PHE B 63  ? 0.64540 0.32210 0.43180 0.04700  -0.08960 0.03540  62  PHE B CE2 
2760 C CZ  . PHE B 63  ? 0.61160 0.29170 0.39530 0.02950  -0.09820 0.06140  62  PHE B CZ  
2761 N N   . TYR B 64  ? 0.53610 0.33120 0.29110 -0.00310 -0.04580 0.02700  63  TYR B N   
2762 C CA  . TYR B 64  ? 0.52360 0.33020 0.27580 -0.01040 -0.04320 0.02440  63  TYR B CA  
2763 C C   . TYR B 64  ? 0.52500 0.32950 0.26900 -0.02230 -0.04620 0.02550  63  TYR B C   
2764 O O   . TYR B 64  ? 0.52190 0.32980 0.26350 -0.02500 -0.04810 0.03190  63  TYR B O   
2765 C CB  . TYR B 64  ? 0.50520 0.33240 0.27830 -0.00990 -0.04560 0.02910  63  TYR B CB  
2766 C CG  . TYR B 64  ? 0.50800 0.33680 0.28860 -0.00870 -0.05520 0.02580  63  TYR B CG  
2767 C CD1 . TYR B 64  ? 0.51160 0.34850 0.28570 -0.00970 -0.05730 0.01820  63  TYR B CD1 
2768 C CD2 . TYR B 64  ? 0.51730 0.34550 0.31130 -0.00320 -0.06340 0.02800  63  TYR B CD2 
2769 C CE1 . TYR B 64  ? 0.52460 0.36940 0.29720 -0.00080 -0.06650 0.00760  63  TYR B CE1 
2770 C CE2 . TYR B 64  ? 0.53190 0.36090 0.32540 0.00130  -0.07720 0.01860  63  TYR B CE2 
2771 C CZ  . TYR B 64  ? 0.53550 0.37310 0.31450 0.00460  -0.07810 0.00590  63  TYR B CZ  
2772 O OH  . TYR B 64  ? 0.55750 0.40170 0.32800 0.01620  -0.09200 -0.01040 63  TYR B OH  
2773 N N   . LEU B 65  ? 0.55110 0.35850 0.29160 -0.02960 -0.04680 0.02270  64  LEU B N   
2774 C CA  . LEU B 65  ? 0.56170 0.37800 0.30450 -0.04290 -0.04980 0.02780  64  LEU B CA  
2775 C C   . LEU B 65  ? 0.55390 0.38840 0.30360 -0.04540 -0.05110 0.02500  64  LEU B C   
2776 O O   . LEU B 65  ? 0.55080 0.38060 0.29330 -0.04220 -0.05290 0.02050  64  LEU B O   
2777 C CB  . LEU B 65  ? 0.60120 0.39010 0.33930 -0.05460 -0.06000 0.03050  64  LEU B CB  
2778 C CG  . LEU B 65  ? 0.62880 0.39520 0.36770 -0.05670 -0.06540 0.04070  64  LEU B CG  
2779 C CD1 . LEU B 65  ? 0.68920 0.41580 0.43170 -0.06760 -0.08480 0.03980  64  LEU B CD1 
2780 C CD2 . LEU B 65  ? 0.61410 0.41440 0.35950 -0.06490 -0.05940 0.06200  64  LEU B CD2 
2781 N N   . LEU B 66  ? 0.49550 0.35730 0.25900 -0.04920 -0.05010 0.02940  65  LEU B N   
2782 C CA  . LEU B 66  ? 0.50040 0.38090 0.27720 -0.05200 -0.05480 0.02930  65  LEU B CA  
2783 C C   . LEU B 66  ? 0.52450 0.41690 0.31030 -0.06940 -0.06000 0.03880  65  LEU B C   
2784 O O   . LEU B 66  ? 0.53220 0.44740 0.32800 -0.07530 -0.05430 0.05060  65  LEU B O   
2785 C CB  . LEU B 66  ? 0.50330 0.41050 0.29950 -0.03800 -0.05320 0.02450  65  LEU B CB  
2786 C CG  . LEU B 66  ? 0.51670 0.44460 0.33400 -0.03870 -0.06060 0.02640  65  LEU B CG  
2787 C CD1 . LEU B 66  ? 0.50650 0.41540 0.31920 -0.04110 -0.07000 0.03070  65  LEU B CD1 
2788 C CD2 . LEU B 66  ? 0.54180 0.49720 0.38300 -0.01910 -0.06120 0.01620  65  LEU B CD2 
2789 N N   . TYR B 67  ? 0.54010 0.42120 0.32300 -0.07880 -0.07270 0.03650  66  TYR B N   
2790 C CA  . TYR B 67  ? 0.56930 0.46050 0.36950 -0.09850 -0.08600 0.04590  66  TYR B CA  
2791 C C   . TYR B 67  ? 0.56830 0.49580 0.39020 -0.09670 -0.08990 0.04890  66  TYR B C   
2792 O O   . TYR B 67  ? 0.55040 0.47340 0.36220 -0.08550 -0.09250 0.04180  66  TYR B O   
2793 C CB  . TYR B 67  ? 0.59530 0.44250 0.37510 -0.10790 -0.10650 0.03460  66  TYR B CB  
2794 C CG  . TYR B 67  ? 0.62620 0.43400 0.39780 -0.11130 -0.11080 0.03330  66  TYR B CG  
2795 C CD1 . TYR B 67  ? 0.61250 0.40010 0.36150 -0.09250 -0.09870 0.02260  66  TYR B CD1 
2796 C CD2 . TYR B 67  ? 0.66980 0.46120 0.46410 -0.13470 -0.13070 0.04700  66  TYR B CD2 
2797 C CE1 . TYR B 67  ? 0.65020 0.40120 0.39680 -0.09290 -0.10530 0.02250  66  TYR B CE1 
2798 C CE2 . TYR B 67  ? 0.69840 0.44760 0.49170 -0.13780 -0.14020 0.04940  66  TYR B CE2 
2799 C CZ  . TYR B 67  ? 0.70030 0.42890 0.46810 -0.11480 -0.12690 0.03560  66  TYR B CZ  
2800 O OH  . TYR B 67  ? 0.72750 0.41310 0.49840 -0.11490 -0.13900 0.03830  66  TYR B OH  
2801 N N   . TYR B 68  ? 0.48360 0.45330 0.34060 -0.10730 -0.09050 0.06400  67  TYR B N   
2802 C CA  . TYR B 68  ? 0.48030 0.49070 0.36590 -0.10000 -0.09350 0.06640  67  TYR B CA  
2803 C C   . TYR B 68  ? 0.50500 0.55670 0.43100 -0.12090 -0.10370 0.08600  67  TYR B C   
2804 O O   . TYR B 68  ? 0.52370 0.59030 0.46540 -0.13870 -0.10110 0.10410  67  TYR B O   
2805 C CB  . TYR B 68  ? 0.48000 0.52260 0.37870 -0.07310 -0.07590 0.05970  67  TYR B CB  
2806 C CG  . TYR B 68  ? 0.50510 0.58500 0.40980 -0.06990 -0.05690 0.06700  67  TYR B CG  
2807 C CD1 . TYR B 68  ? 0.48740 0.54010 0.36160 -0.06750 -0.04790 0.06340  67  TYR B CD1 
2808 C CD2 . TYR B 68  ? 0.53350 0.68520 0.47490 -0.06830 -0.04770 0.08100  67  TYR B CD2 
2809 C CE1 . TYR B 68  ? 0.50570 0.59830 0.37950 -0.06500 -0.03190 0.07480  67  TYR B CE1 
2810 C CE2 . TYR B 68  ? 0.55120 0.75230 0.49330 -0.06430 -0.02750 0.09320  67  TYR B CE2 
2811 C CZ  . TYR B 68  ? 0.53370 0.70320 0.43860 -0.06330 -0.02050 0.09060  67  TYR B CZ  
2812 O OH  . TYR B 68  ? 0.52280 0.74560 0.42220 -0.05950 -0.00190 0.10650  67  TYR B OH  
2813 N N   . THR B 69  ? 0.57880 0.65240 0.52740 -0.12060 -0.11810 0.08760  68  THR B N   
2814 C CA  . THR B 69  ? 0.57950 0.70640 0.57930 -0.13820 -0.12830 0.10880  68  THR B CA  
2815 C C   . THR B 69  ? 0.57200 0.73880 0.60240 -0.11990 -0.13280 0.10740  68  THR B C   
2816 O O   . THR B 69  ? 0.56290 0.69840 0.57070 -0.10630 -0.14210 0.09450  68  THR B O   
2817 C CB  . THR B 69  ? 0.58520 0.67950 0.58490 -0.17110 -0.16080 0.11480  68  THR B CB  
2818 O OG1 . THR B 69  ? 0.57450 0.72690 0.63500 -0.19040 -0.17460 0.13950  68  THR B OG1 
2819 C CG2 . THR B 69  ? 0.57840 0.62550 0.53630 -0.16600 -0.18250 0.09330  68  THR B CG2 
2820 N N   . GLU B 70  ? 0.65470 0.89650 0.74130 -0.11870 -0.12620 0.12460  69  GLU B N   
2821 C CA  . GLU B 70  ? 0.64400 0.92930 0.77140 -0.09920 -0.13370 0.12430  69  GLU B CA  
2822 C C   . GLU B 70  ? 0.62300 0.89520 0.76110 -0.12340 -0.16970 0.13420  69  GLU B C   
2823 O O   . GLU B 70  ? 0.62820 0.89490 0.77330 -0.15690 -0.18730 0.14760  69  GLU B O   
2824 C CB  . GLU B 70  ? 0.64830 1.03140 0.83510 -0.08570 -0.11280 0.13850  69  GLU B CB  
2825 C CG  . GLU B 70  ? 0.64710 1.07750 0.87820 -0.05040 -0.11520 0.12940  69  GLU B CG  
2826 C CD  . GLU B 70  ? 0.66010 1.18940 0.93380 -0.02000 -0.08450 0.13020  69  GLU B CD  
2827 O OE1 . GLU B 70  ? 0.65580 1.23820 0.93860 -0.03780 -0.06420 0.15340  69  GLU B OE1 
2828 O OE2 . GLU B 70  ? 0.67200 1.22870 0.97050 0.02370  -0.08190 0.10820  69  GLU B OE2 
2829 N N   . PHE B 71  ? 0.56400 0.82760 0.70350 -0.10670 -0.18550 0.12790  70  PHE B N   
2830 C CA  . PHE B 71  ? 0.55740 0.80690 0.69370 -0.12580 -0.22220 0.13530  70  PHE B CA  
2831 C C   . PHE B 71  ? 0.55250 0.82560 0.71990 -0.10230 -0.23570 0.14010  70  PHE B C   
2832 O O   . PHE B 71  ? 0.55590 0.82760 0.73110 -0.07100 -0.22100 0.13130  70  PHE B O   
2833 C CB  . PHE B 71  ? 0.56240 0.73740 0.62250 -0.13780 -0.23480 0.12100  70  PHE B CB  
2834 C CG  . PHE B 71  ? 0.56620 0.70980 0.58820 -0.11600 -0.23220 0.11460  70  PHE B CG  
2835 C CD1 . PHE B 71  ? 0.56550 0.70520 0.59400 -0.09050 -0.20790 0.10920  70  PHE B CD1 
2836 C CD2 . PHE B 71  ? 0.56930 0.69070 0.55000 -0.12190 -0.25750 0.11640  70  PHE B CD2 
2837 C CE1 . PHE B 71  ? 0.56580 0.67650 0.57120 -0.07630 -0.21120 0.11120  70  PHE B CE1 
2838 C CE2 . PHE B 71  ? 0.56910 0.67230 0.52080 -0.10620 -0.25520 0.12190  70  PHE B CE2 
2839 C CZ  . PHE B 71  ? 0.56890 0.66500 0.53830 -0.08590 -0.23340 0.12220  70  PHE B CZ  
2840 N N   . THR B 72  ? 0.60550 0.89580 0.79280 -0.11790 -0.26960 0.15390  71  THR B N   
2841 C CA  . THR B 72  ? 0.59190 0.90190 0.81010 -0.09960 -0.29130 0.16450  71  THR B CA  
2842 C C   . THR B 72  ? 0.60480 0.86980 0.76340 -0.11320 -0.32210 0.16830  71  THR B C   
2843 O O   . THR B 72  ? 0.60900 0.87670 0.75590 -0.13890 -0.35160 0.17190  71  THR B O   
2844 C CB  . THR B 72  ? 0.57850 0.96580 0.87950 -0.10270 -0.30630 0.18260  71  THR B CB  
2845 O OG1 . THR B 72  ? 0.57070 1.01600 0.92220 -0.08620 -0.27190 0.18070  71  THR B OG1 
2846 C CG2 . THR B 72  ? 0.56150 0.96740 0.90010 -0.08080 -0.33230 0.19470  71  THR B CG2 
2847 N N   . PRO B 73  ? 0.70470 0.65030 0.76330 -0.22030 -0.16970 0.10700  72  PRO B N   
2848 C CA  . PRO B 73  ? 0.85140 0.80620 0.81470 -0.20490 -0.17750 0.10950  72  PRO B CA  
2849 C C   . PRO B 73  ? 0.91300 0.89130 0.87180 -0.21990 -0.21200 0.16270  72  PRO B C   
2850 O O   . PRO B 73  ? 0.85440 0.86450 0.91160 -0.23410 -0.20820 0.20950  72  PRO B O   
2851 C CB  . PRO B 73  ? 0.88590 0.87650 0.88100 -0.18340 -0.11500 0.10920  72  PRO B CB  
2852 C CG  . PRO B 73  ? 0.73260 0.75170 0.86070 -0.19400 -0.08130 0.13330  72  PRO B CG  
2853 C CD  . PRO B 73  ? 0.62810 0.60890 0.78060 -0.21240 -0.11040 0.11390  72  PRO B CD  
2854 N N   . THR B 74  ? 0.96980 0.93110 0.81360 -0.21690 -0.24780 0.15340  73  THR B N   
2855 C CA  . THR B 74  ? 1.01720 0.99930 0.83010 -0.22680 -0.28410 0.20080  73  THR B CA  
2856 C C   . THR B 74  ? 1.11050 1.09480 0.81190 -0.20980 -0.26900 0.19660  73  THR B C   
2857 O O   . THR B 74  ? 1.13810 1.10310 0.78340 -0.19280 -0.23940 0.14860  73  THR B O   
2858 C CB  . THR B 74  ? 0.97080 0.92640 0.74430 -0.24730 -0.35300 0.19230  73  THR B CB  
2859 O OG1 . THR B 74  ? 1.00470 0.91990 0.65130 -0.24010 -0.37210 0.14060  73  THR B OG1 
2860 C CG2 . THR B 74  ? 0.86660 0.80520 0.73450 -0.26520 -0.36110 0.18000  73  THR B CG2 
2861 N N   . GLU B 75  ? 1.10390 1.10960 0.77160 -0.21470 -0.28970 0.24660  74  GLU B N   
2862 C CA  . GLU B 75  ? 1.18920 1.18970 0.73650 -0.20270 -0.27480 0.24230  74  GLU B CA  
2863 C C   . GLU B 75  ? 1.21990 1.18090 0.63650 -0.20700 -0.31820 0.19480  74  GLU B C   
2864 O O   . GLU B 75  ? 1.28290 1.22740 0.59900 -0.19580 -0.29500 0.16290  74  GLU B O   
2865 C CB  . GLU B 75  ? 1.23310 1.26190 0.77180 -0.20600 -0.28230 0.31300  74  GLU B CB  
2866 C CG  . GLU B 75  ? 1.32520 1.35070 0.76570 -0.19220 -0.23820 0.31430  74  GLU B CG  
2867 C CD  . GLU B 75  ? 1.33330 1.36190 0.81480 -0.17410 -0.16210 0.27400  74  GLU B CD  
2868 O OE1 . GLU B 75  ? 1.29230 1.35100 0.88340 -0.16850 -0.11550 0.30310  74  GLU B OE1 
2869 O OE2 . GLU B 75  ? 1.35970 1.36170 0.77020 -0.16550 -0.14980 0.21110  74  GLU B OE2 
2870 N N   . LYS B 76  ? 1.31530 1.26000 0.73600 -0.22440 -0.37740 0.18600  75  LYS B N   
2871 C CA  . LYS B 76  ? 1.31870 1.23010 0.65070 -0.22110 -0.40250 0.13410  75  LYS B CA  
2872 C C   . LYS B 76  ? 1.28970 1.16540 0.60260 -0.20720 -0.37690 0.06480  75  LYS B C   
2873 O O   . LYS B 76  ? 1.31490 1.17360 0.56490 -0.19390 -0.37450 0.02000  75  LYS B O   
2874 C CB  . LYS B 76  ? 1.29300 1.20470 0.67870 -0.23270 -0.44600 0.13870  75  LYS B CB  
2875 N N   . ASP B 77  ? 1.20070 1.06910 0.57400 -0.20820 -0.35730 0.05560  76  ASP B N   
2876 C CA  . ASP B 77  ? 1.13970 0.97290 0.51940 -0.19090 -0.33630 -0.00770 76  ASP B CA  
2877 C C   . ASP B 77  ? 1.17190 1.00290 0.51690 -0.17080 -0.28820 -0.03840 76  ASP B C   
2878 O O   . ASP B 77  ? 1.20270 1.07130 0.60780 -0.16150 -0.24230 -0.01020 76  ASP B O   
2879 C CB  . ASP B 77  ? 1.04550 0.86660 0.52540 -0.20000 -0.34020 -0.00670 76  ASP B CB  
2880 C CG  . ASP B 77  ? 1.02500 0.84210 0.55020 -0.21420 -0.37180 0.00860  76  ASP B CG  
2881 O OD1 . ASP B 77  ? 1.08760 0.89540 0.56770 -0.20780 -0.38510 -0.01260 76  ASP B OD1 
2882 O OD2 . ASP B 77  ? 0.96400 0.79070 0.57560 -0.23330 -0.38080 0.04020  76  ASP B OD2 
2883 N N   . GLU B 78  ? 1.16490 0.97260 0.47230 -0.14940 -0.27570 -0.09630 77  GLU B N   
2884 C CA  . GLU B 78  ? 1.18090 0.98370 0.45870 -0.12730 -0.23220 -0.13840 77  GLU B CA  
2885 C C   . GLU B 78  ? 1.08990 0.88050 0.44410 -0.10680 -0.21800 -0.17960 77  GLU B C   
2886 O O   . GLU B 78  ? 1.06260 0.84930 0.44820 -0.10250 -0.23160 -0.19520 77  GLU B O   
2887 C CB  . GLU B 78  ? 1.24150 1.05060 0.44650 -0.11530 -0.22410 -0.16660 77  GLU B CB  
2888 C CG  . GLU B 78  ? 1.33120 1.15340 0.45920 -0.13310 -0.24070 -0.12390 77  GLU B CG  
2889 C CD  . GLU B 78  ? 1.39110 1.21680 0.49320 -0.13510 -0.27490 -0.13320 77  GLU B CD  
2890 O OE1 . GLU B 78  ? 1.36520 1.18500 0.50780 -0.12730 -0.28340 -0.16890 77  GLU B OE1 
2891 O OE2 . GLU B 78  ? 1.46470 1.30130 0.50510 -0.14570 -0.29090 -0.10310 77  GLU B OE2 
2892 N N   . TYR B 79  ? 0.79500 0.58920 0.44920 -0.26650 -0.26110 0.08940  78  TYR B N   
2893 C CA  . TYR B 79  ? 0.76070 0.56890 0.43200 -0.26220 -0.25010 0.08950  78  TYR B CA  
2894 C C   . TYR B 79  ? 0.78130 0.55380 0.41540 -0.25030 -0.23790 0.07810  78  TYR B C   
2895 O O   . TYR B 79  ? 0.77370 0.53820 0.39140 -0.23790 -0.23100 0.07020  78  TYR B O   
2896 C CB  . TYR B 79  ? 0.68050 0.56410 0.42300 -0.24730 -0.23680 0.09220  78  TYR B CB  
2897 C CG  . TYR B 79  ? 0.67520 0.59530 0.45220 -0.25570 -0.24600 0.10100  78  TYR B CG  
2898 C CD1 . TYR B 79  ? 0.68400 0.61150 0.46910 -0.26880 -0.25010 0.10940  78  TYR B CD1 
2899 C CD2 . TYR B 79  ? 0.67600 0.61830 0.47080 -0.25470 -0.25320 0.10380  78  TYR B CD2 
2900 C CE1 . TYR B 79  ? 0.68660 0.64540 0.49590 -0.28170 -0.26070 0.12160  78  TYR B CE1 
2901 C CE2 . TYR B 79  ? 0.68300 0.65470 0.50180 -0.26740 -0.26490 0.11540  78  TYR B CE2 
2902 C CZ  . TYR B 79  ? 0.68990 0.67150 0.51590 -0.28080 -0.26790 0.12430  78  TYR B CZ  
2903 O OH  . TYR B 79  ? 0.69890 0.71380 0.54770 -0.29370 -0.27880 0.13640  78  TYR B OH  
2904 N N   . ALA B 80  ? 0.79110 0.54280 0.41060 -0.25320 -0.23490 0.07730  79  ALA B N   
2905 C CA  . ALA B 80  ? 0.80730 0.52730 0.39160 -0.23840 -0.22120 0.06530  79  ALA B CA  
2906 C C   . ALA B 80  ? 0.78480 0.51650 0.38680 -0.23850 -0.21450 0.06820  79  ALA B C   
2907 O O   . ALA B 80  ? 0.76800 0.52520 0.40230 -0.25230 -0.22200 0.07990  79  ALA B O   
2908 C CB  . ALA B 80  ? 0.90240 0.53990 0.40680 -0.24070 -0.22830 0.05530  79  ALA B CB  
2909 N N   . CYS B 81  ? 0.90160 0.61690 0.48110 -0.22130 -0.19880 0.05790  80  CYS B N   
2910 C CA  . CYS B 81  ? 0.90080 0.61090 0.48100 -0.22050 -0.19290 0.05850  80  CYS B CA  
2911 C C   . CYS B 81  ? 0.99440 0.61870 0.49450 -0.21300 -0.19230 0.04570  80  CYS B C   
2912 O O   . CYS B 81  ? 1.02190 0.61700 0.48080 -0.19410 -0.18130 0.03350  80  CYS B O   
2913 C CB  . CYS B 81  ? 0.83720 0.60870 0.46450 -0.20140 -0.17110 0.05820  80  CYS B CB  
2914 S SG  . CYS B 81  ? 0.85000 0.62060 0.47950 -0.19830 -0.16150 0.05970  80  CYS B SG  
2915 N N   . ARG B 82  ? 0.95680 0.54160 0.43530 -0.22560 -0.20320 0.04920  81  ARG B N   
2916 C CA  . ARG B 82  ? 1.04320 0.53870 0.44400 -0.21630 -0.20430 0.03700  81  ARG B CA  
2917 C C   . ARG B 82  ? 1.04550 0.53870 0.44720 -0.20510 -0.19210 0.03510  81  ARG B C   
2918 O O   . ARG B 82  ? 1.01560 0.53650 0.45530 -0.22440 -0.20190 0.04830  81  ARG B O   
2919 C CB  . ARG B 82  ? 1.11390 0.54990 0.47700 -0.24040 -0.23160 0.04370  81  ARG B CB  
2920 C CG  . ARG B 82  ? 1.21480 0.55360 0.49660 -0.22860 -0.23500 0.03130  81  ARG B CG  
2921 C CD  . ARG B 82  ? 1.29750 0.57910 0.54000 -0.25210 -0.26370 0.03950  81  ARG B CD  
2922 N NE  . ARG B 82  ? 1.28110 0.59680 0.56610 -0.28080 -0.28100 0.06110  81  ARG B NE  
2923 C CZ  . ARG B 82  ? 1.31400 0.62040 0.59460 -0.30680 -0.30470 0.07600  81  ARG B CZ  
2924 N NH1 . ARG B 82  ? 1.37770 0.63650 0.61230 -0.31080 -0.31660 0.07170  81  ARG B NH1 
2925 N NH2 . ARG B 82  ? 1.28650 0.63570 0.61000 -0.32880 -0.31580 0.09620  81  ARG B NH2 
2926 N N   . VAL B 83  ? 0.98190 0.44640 0.34380 -0.17240 -0.16880 0.02030  82  VAL B N   
2927 C CA  . VAL B 83  ? 0.97250 0.44040 0.33540 -0.15440 -0.15070 0.01900  82  VAL B CA  
2928 C C   . VAL B 83  ? 1.07680 0.45120 0.36100 -0.13230 -0.14630 0.00380  82  VAL B C   
2929 O O   . VAL B 83  ? 1.10480 0.44160 0.34500 -0.11140 -0.13740 -0.00920 82  VAL B O   
2930 C CB  . VAL B 83  ? 0.90470 0.44490 0.30970 -0.12660 -0.11730 0.01990  82  VAL B CB  
2931 C CG1 . VAL B 83  ? 0.88220 0.43390 0.29680 -0.10760 -0.09540 0.02390  82  VAL B CG1 
2932 C CG2 . VAL B 83  ? 0.80850 0.43690 0.29020 -0.14430 -0.12290 0.03290  82  VAL B CG2 
2933 N N   . ASN B 84  ? 1.14470 0.48470 0.41400 -0.13560 -0.15250 0.00590  83  ASN B N   
2934 C CA  . ASN B 84  ? 1.23620 0.49210 0.43830 -0.10760 -0.14500 -0.00910 83  ASN B CA  
2935 C C   . ASN B 84  ? 1.22130 0.50430 0.45440 -0.08690 -0.12130 -0.00460 83  ASN B C   
2936 O O   . ASN B 84  ? 1.15930 0.50670 0.46530 -0.10680 -0.12300 0.01390  83  ASN B O   
2937 C CB  . ASN B 84  ? 1.30190 0.47610 0.45930 -0.13010 -0.17930 -0.00750 83  ASN B CB  
2938 C CG  . ASN B 84  ? 1.39160 0.47910 0.47580 -0.09550 -0.17290 -0.02390 83  ASN B CG  
2939 O OD1 . ASN B 84  ? 1.38920 0.47940 0.45860 -0.05430 -0.14180 -0.03730 83  ASN B OD1 
2940 N ND2 . ASN B 84  ? 1.46910 0.49000 0.51310 -0.11140 -0.20230 -0.02030 83  ASN B ND2 
2941 N N   . HIS B 85  ? 1.19860 0.44180 0.38900 -0.04440 -0.09640 -0.01950 84  HIS B N   
2942 C CA  . HIS B 85  ? 1.16570 0.44870 0.39690 -0.01420 -0.06400 -0.01460 84  HIS B CA  
2943 C C   . HIS B 85  ? 1.25880 0.45980 0.41430 0.02700  -0.05210 -0.03530 84  HIS B C   
2944 O O   . HIS B 85  ? 1.29020 0.45090 0.40000 0.03940  -0.05570 -0.04730 84  HIS B O   
2945 C CB  . HIS B 85  ? 1.04500 0.42860 0.33660 0.00110  -0.03120 -0.00700 84  HIS B CB  
2946 C CG  . HIS B 85  ? 0.98300 0.42410 0.33110 0.02380  -0.00040 0.00280  84  HIS B CG  
2947 N ND1 . HIS B 85  ? 0.97070 0.41950 0.30320 0.06760  0.03420  -0.00550 84  HIS B ND1 
2948 C CD2 . HIS B 85  ? 0.91850 0.41680 0.33930 0.00820  0.00100  0.02080  84  HIS B CD2 
2949 C CE1 . HIS B 85  ? 0.90060 0.40640 0.29390 0.07720  0.05490  0.00750  84  HIS B CE1 
2950 N NE2 . HIS B 85  ? 0.86820 0.40320 0.31470 0.04190  0.03530  0.02310  84  HIS B NE2 
2951 N N   . VAL B 86  ? 1.27800 0.47780 0.45110 0.04910  -0.03640 -0.03220 85  VAL B N   
2952 C CA  . VAL B 86  ? 1.34640 0.47860 0.46030 0.09080  -0.02620 -0.04870 85  VAL B CA  
2953 C C   . VAL B 86  ? 1.30630 0.48400 0.42690 0.12520  0.00220  -0.05370 85  VAL B C   
2954 O O   . VAL B 86  ? 1.35110 0.48570 0.42860 0.14830  0.00040  -0.06410 85  VAL B O   
2955 C CB  . VAL B 86  ? 1.35100 0.48450 0.48800 0.11240  -0.01030 -0.04410 85  VAL B CB  
2956 C CG1 . VAL B 86  ? 1.39200 0.45670 0.51490 0.08370  -0.04690 -0.03770 85  VAL B CG1 
2957 C CG2 . VAL B 86  ? 1.23880 0.48850 0.47010 0.10960  0.01710  -0.02370 85  VAL B CG2 
2958 N N   . THR B 87  ? 1.29230 0.56260 0.47310 0.12660  0.02630  -0.04500 86  THR B N   
2959 C CA  . THR B 87  ? 1.22920 0.54990 0.42940 0.15090  0.04790  -0.04760 86  THR B CA  
2960 C C   . THR B 87  ? 1.26950 0.56010 0.43000 0.13710  0.03030  -0.05690 86  THR B C   
2961 O O   . THR B 87  ? 1.26230 0.58720 0.42970 0.15410  0.04490  -0.06080 86  THR B O   
2962 C CB  . THR B 87  ? 1.09630 0.52770 0.38260 0.15000  0.07220  -0.03360 86  THR B CB  
2963 O OG1 . THR B 87  ? 1.05530 0.51320 0.36370 0.11450  0.05820  -0.02670 86  THR B OG1 
2964 C CG2 . THR B 87  ? 1.05820 0.52640 0.39100 0.16440  0.09050  -0.02270 86  THR B CG2 
2965 N N   . LEU B 88  ? 1.28170 0.51340 0.40420 0.10400  -0.00250 -0.05910 87  LEU B N   
2966 C CA  . LEU B 88  ? 1.30860 0.51690 0.40050 0.08650  -0.02110 -0.06500 87  LEU B CA  
2967 C C   . LEU B 88  ? 1.43310 0.54120 0.45200 0.08570  -0.04740 -0.07530 87  LEU B C   
2968 O O   . LEU B 88  ? 1.48290 0.53960 0.48360 0.06520  -0.07210 -0.07160 87  LEU B O   
2969 C CB  . LEU B 88  ? 1.25650 0.49650 0.37990 0.04360  -0.04080 -0.05430 87  LEU B CB  
2970 C CG  . LEU B 88  ? 1.15190 0.49450 0.34690 0.04260  -0.01910 -0.04370 87  LEU B CG  
2971 C CD1 . LEU B 88  ? 1.09700 0.47680 0.33320 0.00280  -0.03890 -0.02980 87  LEU B CD1 
2972 C CD2 . LEU B 88  ? 1.14170 0.51300 0.33660 0.05210  -0.00970 -0.04870 87  LEU B CD2 
2973 N N   . SER B 89  ? 1.48020 0.56450 0.46000 0.10630  -0.04330 -0.08720 88  SER B N   
2974 C CA  . SER B 89  ? 1.59330 0.58480 0.50310 0.10430  -0.07010 -0.09690 88  SER B CA  
2975 C C   . SER B 89  ? 1.60020 0.55980 0.49710 0.05800  -0.10580 -0.09010 88  SER B C   
2976 O O   . SER B 89  ? 1.66610 0.55470 0.52260 0.04190  -0.13550 -0.08930 88  SER B O   
2977 C CB  . SER B 89  ? 1.64400 0.62460 0.51650 0.13500  -0.05750 -0.11180 88  SER B CB  
2978 N N   . GLN B 90  ? 1.55410 0.57050 0.48940 0.03520  -0.10470 -0.08300 89  GLN B N   
2979 C CA  . GLN B 90  ? 1.57310 0.57130 0.50320 -0.00720 -0.13710 -0.07500 89  GLN B CA  
2980 C C   . GLN B 90  ? 1.46880 0.54460 0.46800 -0.03520 -0.13660 -0.06030 89  GLN B C   
2981 O O   . GLN B 90  ? 1.39140 0.53710 0.43500 -0.01890 -0.10900 -0.05930 89  GLN B O   
2982 C CB  . GLN B 90  ? 1.61810 0.59770 0.51150 -0.00470 -0.14090 -0.08420 89  GLN B CB  
2983 C CG  . GLN B 90  ? 1.73800 0.63790 0.55920 0.01990  -0.14630 -0.09930 89  GLN B CG  
2984 C CD  . GLN B 90  ? 1.82130 0.64090 0.60100 -0.00330 -0.18280 -0.09460 89  GLN B CD  
2985 O OE1 . GLN B 90  ? 1.78580 0.61220 0.59060 -0.04260 -0.20630 -0.07850 89  GLN B OE1 
2986 N NE2 . GLN B 90  ? 1.91320 0.66180 0.63170 0.02060  -0.18840 -0.10740 89  GLN B NE2 
2987 N N   . PRO B 91  ? 1.40380 0.47540 0.41770 -0.07680 -0.16720 -0.04710 90  PRO B N   
2988 C CA  . PRO B 91  ? 1.30370 0.45550 0.38880 -0.10290 -0.16860 -0.03240 90  PRO B CA  
2989 C C   . PRO B 91  ? 1.25300 0.46510 0.36630 -0.09730 -0.15350 -0.03390 90  PRO B C   
2990 O O   . PRO B 91  ? 1.30130 0.48880 0.38200 -0.09650 -0.15890 -0.04010 90  PRO B O   
2991 C CB  . PRO B 91  ? 1.32680 0.45950 0.41680 -0.14610 -0.20560 -0.01730 90  PRO B CB  
2992 C CG  . PRO B 91  ? 1.42970 0.47210 0.45480 -0.14230 -0.22240 -0.02190 90  PRO B CG  
2993 C CD  . PRO B 91  ? 1.48780 0.48860 0.45920 -0.10130 -0.20180 -0.04240 90  PRO B CD  
2994 N N   . LYS B 92  ? 1.14240 0.52150 0.35610 -0.06530 -0.11220 -0.03780 91  LYS B N   
2995 C CA  . LYS B 92  ? 1.07330 0.52130 0.34340 -0.07170 -0.11220 -0.04390 91  LYS B CA  
2996 C C   . LYS B 92  ? 1.04080 0.50600 0.34220 -0.10090 -0.12360 -0.03580 91  LYS B C   
2997 O O   . LYS B 92  ? 1.02670 0.51250 0.34000 -0.10260 -0.12200 -0.03190 91  LYS B O   
2998 C CB  . LYS B 92  ? 1.02650 0.55050 0.33090 -0.04610 -0.09780 -0.05900 91  LYS B CB  
2999 C CG  . LYS B 92  ? 1.00770 0.56560 0.33940 -0.05670 -0.09250 -0.06720 91  LYS B CG  
3000 C CD  . LYS B 92  ? 1.01900 0.63840 0.37400 -0.04020 -0.08160 -0.09410 91  LYS B CD  
3001 C CE  . LYS B 92  ? 1.06320 0.67990 0.42300 -0.06150 -0.07050 -0.10410 91  LYS B CE  
3002 N NZ  . LYS B 92  ? 1.10060 0.76970 0.49290 -0.05920 -0.06270 -0.14670 91  LYS B NZ  
3003 N N   . ILE B 93  ? 1.09350 0.55200 0.40010 -0.11640 -0.13550 -0.03350 92  ILE B N   
3004 C CA  . ILE B 93  ? 1.06740 0.54520 0.40080 -0.13880 -0.15010 -0.02680 92  ILE B CA  
3005 C C   . ILE B 93  ? 1.03720 0.55410 0.39520 -0.13150 -0.14020 -0.02800 92  ILE B C   
3006 O O   . ILE B 93  ? 1.05340 0.55450 0.38640 -0.12080 -0.13300 -0.03020 92  ILE B O   
3007 C CB  . ILE B 93  ? 1.13420 0.57850 0.44840 -0.15490 -0.17750 -0.02870 92  ILE B CB  
3008 C CG1 . ILE B 93  ? 1.20050 0.58260 0.47770 -0.16980 -0.18910 -0.03330 92  ILE B CG1 
3009 C CG2 . ILE B 93  ? 1.11320 0.59260 0.46200 -0.17370 -0.19650 -0.02490 92  ILE B CG2 
3010 C CD1 . ILE B 93  ? 1.23020 0.60130 0.52370 -0.20990 -0.20780 -0.03200 92  ILE B CD1 
3011 N N   . VAL B 94  ? 0.92490 0.47840 0.31610 -0.13800 -0.13920 -0.02650 93  VAL B N   
3012 C CA  . VAL B 94  ? 0.92680 0.49410 0.32680 -0.13840 -0.13300 -0.02860 93  VAL B CA  
3013 C C   . VAL B 94  ? 0.92410 0.49710 0.33200 -0.14980 -0.15180 -0.01800 93  VAL B C   
3014 O O   . VAL B 94  ? 0.89790 0.49750 0.33110 -0.15790 -0.16060 -0.01510 93  VAL B O   
3015 C CB  . VAL B 94  ? 0.90660 0.51190 0.33610 -0.13190 -0.11980 -0.04660 93  VAL B CB  
3016 C CG1 . VAL B 94  ? 0.95470 0.54650 0.38050 -0.14320 -0.11350 -0.05420 93  VAL B CG1 
3017 C CG2 . VAL B 94  ? 0.91820 0.53210 0.34270 -0.11660 -0.10680 -0.06300 93  VAL B CG2 
3018 N N   . LYS B 95  ? 0.97870 0.52540 0.35380 -0.14570 -0.15810 -0.01160 94  LYS B N   
3019 C CA  . LYS B 95  ? 0.98450 0.54280 0.36100 -0.14660 -0.18090 -0.00330 94  LYS B CA  
3020 C C   . LYS B 95  ? 0.99740 0.56430 0.38160 -0.14810 -0.17390 -0.00090 94  LYS B C   
3021 O O   . LYS B 95  ? 1.04720 0.58600 0.41130 -0.14960 -0.15160 -0.00840 94  LYS B O   
3022 C CB  . LYS B 95  ? 1.04800 0.57380 0.36950 -0.12600 -0.19140 0.00230  94  LYS B CB  
3023 C CG  . LYS B 95  ? 1.06770 0.60220 0.38950 -0.12430 -0.22060 -0.00870 94  LYS B CG  
3024 C CD  . LYS B 95  ? 1.06550 0.64820 0.43150 -0.13870 -0.25540 -0.01350 94  LYS B CD  
3025 C CE  . LYS B 95  ? 1.12570 0.71760 0.48940 -0.13780 -0.29330 -0.03470 94  LYS B CE  
3026 N NZ  . LYS B 95  ? 1.11620 0.69280 0.50440 -0.16780 -0.29680 -0.04800 94  LYS B NZ  
3027 N N   . TRP B 96  ? 0.90770 0.50980 0.31690 -0.15040 -0.19450 0.00490  95  TRP B N   
3028 C CA  . TRP B 96  ? 0.89970 0.51110 0.32280 -0.14210 -0.18680 0.00780  95  TRP B CA  
3029 C C   . TRP B 96  ? 0.95600 0.52780 0.34290 -0.11810 -0.17900 0.02480  95  TRP B C   
3030 O O   . TRP B 96  ? 0.99560 0.57140 0.35070 -0.10270 -0.20710 0.03620  95  TRP B O   
3031 C CB  . TRP B 96  ? 0.86820 0.54120 0.34160 -0.14240 -0.20250 0.01310  95  TRP B CB  
3032 C CG  . TRP B 96  ? 0.85980 0.55010 0.36400 -0.12050 -0.18840 0.01580  95  TRP B CG  
3033 C CD1 . TRP B 96  ? 0.85740 0.53180 0.37780 -0.11260 -0.16230 -0.00090 95  TRP B CD1 
3034 C CD2 . TRP B 96  ? 0.86830 0.59660 0.39570 -0.10100 -0.20160 0.03050  95  TRP B CD2 
3035 N NE1 . TRP B 96  ? 0.89860 0.58470 0.44250 -0.08950 -0.15700 0.00290  95  TRP B NE1 
3036 C CE2 . TRP B 96  ? 0.88910 0.60990 0.43400 -0.07880 -0.17910 0.02550  95  TRP B CE2 
3037 C CE3 . TRP B 96  ? 0.88080 0.65450 0.42310 -0.09840 -0.23300 0.04170  95  TRP B CE3 
3038 C CZ2 . TRP B 96  ? 0.93440 0.68360 0.49820 -0.04920 -0.18290 0.03770  95  TRP B CZ2 
3039 C CZ3 . TRP B 96  ? 0.88870 0.70580 0.45970 -0.06920 -0.23880 0.05280  95  TRP B CZ3 
3040 C CH2 . TRP B 96  ? 0.91830 0.71910 0.49350 -0.04250 -0.21180 0.05390  95  TRP B CH2 
3041 N N   . ASP B 97  ? 0.97130 0.50410 0.36470 -0.11200 -0.13970 0.02450  96  ASP B N   
3042 C CA  . ASP B 97  ? 1.05510 0.53100 0.41210 -0.08470 -0.11430 0.04880  96  ASP B CA  
3043 C C   . ASP B 97  ? 1.09850 0.58000 0.49960 -0.07100 -0.10250 0.05070  96  ASP B C   
3044 O O   . ASP B 97  ? 1.13460 0.60530 0.58930 -0.08400 -0.07400 0.03050  96  ASP B O   
3045 C CB  . ASP B 97  ? 1.13020 0.54660 0.47600 -0.09090 -0.06520 0.05100  96  ASP B CB  
3046 C CG  . ASP B 97  ? 1.22070 0.56090 0.50930 -0.05640 -0.02740 0.08850  96  ASP B CG  
3047 O OD1 . ASP B 97  ? 1.24960 0.57580 0.52740 -0.02790 -0.02890 0.10700  96  ASP B OD1 
3048 O OD2 . ASP B 97  ? 1.24490 0.53630 0.49310 -0.05120 0.00880  0.10290  96  ASP B OD2 
3049 N N   . ARG B 98  ? 1.43730 0.93750 0.81730 -0.04100 -0.12720 0.06960  97  ARG B N   
3050 C CA  . ARG B 98  ? 1.49000 0.99450 0.90150 -0.01810 -0.11790 0.07370  97  ARG B CA  
3051 C C   . ARG B 98  ? 1.60010 1.01070 1.00100 -0.00380 -0.06340 0.08600  97  ARG B C   
3052 O O   . ARG B 98  ? 1.63360 1.02840 1.09290 -0.01750 -0.03830 0.06260  97  ARG B O   
3053 C CB  . ARG B 98  ? 1.46910 1.01940 0.85760 0.01830  -0.15630 0.09260  97  ARG B CB  
3054 C CG  . ARG B 98  ? 1.36690 0.99570 0.77260 -0.00440 -0.20460 0.08020  97  ARG B CG  
3055 C CD  . ARG B 98  ? 1.36580 1.05480 0.76800 0.02820  -0.24820 0.08870  97  ARG B CD  
3056 N NE  . ARG B 98  ? 1.39630 1.11650 0.83270 0.06050  -0.24130 0.09850  97  ARG B NE  
3057 C CZ  . ARG B 98  ? 1.37360 1.18690 0.85660 0.07790  -0.27580 0.09770  97  ARG B CZ  
3058 N NH1 . ARG B 98  ? 1.32590 1.21310 0.84190 0.05860  -0.32110 0.08310  97  ARG B NH1 
3059 N NH2 . ARG B 98  ? 1.39880 1.23340 0.90470 0.11480  -0.26360 0.10820  97  ARG B NH2 
3060 N N   . ASP B 99  ? 1.68710 1.02970 1.01330 0.02620  -0.04180 0.12090  98  ASP B N   
3061 C CA  . ASP B 99  ? 1.78150 1.01790 1.09390 0.04230  0.02420  0.14440  98  ASP B CA  
3062 C C   . ASP B 99  ? 1.78300 0.98130 1.14200 -0.00300 0.07190  0.12790  98  ASP B C   
3063 O O   . ASP B 99  ? 1.83350 0.95530 1.14970 0.00800  0.12340  0.15940  98  ASP B O   
3064 C CB  . ASP B 99  ? 1.84770 1.02090 1.04750 0.10460  0.03740  0.19580  98  ASP B CB  
3065 C CG  . ASP B 99  ? 1.82370 1.02620 0.95050 0.11390  0.00250  0.20090  98  ASP B CG  
3066 O OD1 . ASP B 99  ? 1.80020 0.99180 0.93560 0.07900  0.02200  0.19040  98  ASP B OD1 
3067 O OD2 . ASP B 99  ? 1.82140 1.06060 0.88390 0.16000  -0.04700 0.21080  98  ASP B OD2 
3068 N N   . MET B 100 ? 1.89100 1.14770 1.33730 -0.04770 0.05710  0.07910  99  MET B N   
3069 C CA  . MET B 100 ? 1.86380 1.10910 1.37940 -0.09000 0.09410  0.05000  99  MET B CA  
3070 C C   . MET B 100 ? 1.80440 1.11530 1.41130 -0.11650 0.06800  -0.00940 99  MET B C   
3071 O O   . MET B 100 ? 1.75830 1.14670 1.35690 -0.11350 0.01670  -0.02560 99  MET B O   
3072 C CB  . MET B 100 ? 1.83700 1.10810 1.31530 -0.10170 0.08580  0.05420  99  MET B CB  
3073 N N   . ALA C 1   ? 0.50380 0.50350 0.28150 -0.06560 -0.09780 -0.06440 1   ALA C N   
3074 C CA  . ALA C 1   ? 0.55700 0.55670 0.37630 -0.07150 -0.08360 -0.05430 1   ALA C CA  
3075 C C   . ALA C 1   ? 0.54960 0.54870 0.38470 -0.07410 -0.08950 -0.04290 1   ALA C C   
3076 O O   . ALA C 1   ? 0.50900 0.50230 0.31560 -0.07440 -0.10260 -0.03380 1   ALA C O   
3077 C CB  . ALA C 1   ? 0.61750 0.59970 0.40960 -0.07140 -0.06920 -0.03090 1   ALA C CB  
3078 N N   . SER C 2   ? 0.45460 0.46000 0.34490 -0.07640 -0.07750 -0.04630 2   SER C N   
3079 C CA  . SER C 2   ? 0.43820 0.44650 0.35010 -0.07790 -0.08370 -0.04070 2   SER C CA  
3080 C C   . SER C 2   ? 0.46710 0.45840 0.35140 -0.07850 -0.08170 -0.00940 2   SER C C   
3081 O O   . SER C 2   ? 0.51090 0.48750 0.36510 -0.07280 -0.07070 0.00870  2   SER C O   
3082 C CB  . SER C 2   ? 0.45630 0.47800 0.44480 -0.07930 -0.07070 -0.05860 2   SER C CB  
3083 O OG  . SER C 2   ? 0.53540 0.54460 0.55860 -0.08390 -0.03920 -0.04740 2   SER C OG  
3084 N N   . LEU C 3   ? 0.48780 0.48230 0.38030 -0.07980 -0.09320 -0.00500 3   LEU C N   
3085 C CA  . LEU C 3   ? 0.50250 0.48740 0.37430 -0.07510 -0.09730 0.01720  3   LEU C CA  
3086 C C   . LEU C 3   ? 0.59030 0.56390 0.48970 -0.07040 -0.07200 0.03570  3   LEU C C   
3087 O O   . LEU C 3   ? 0.61720 0.59750 0.57360 -0.07750 -0.06090 0.02680  3   LEU C O   
3088 C CB  . LEU C 3   ? 0.45250 0.44560 0.33260 -0.07890 -0.11660 0.01180  3   LEU C CB  
3089 C CG  . LEU C 3   ? 0.46670 0.45750 0.34420 -0.07340 -0.12450 0.02650  3   LEU C CG  
3090 C CD1 . LEU C 3   ? 0.47790 0.46890 0.31700 -0.06320 -0.14290 0.02580  3   LEU C CD1 
3091 C CD2 . LEU C 3   ? 0.43350 0.43310 0.34460 -0.08090 -0.13290 0.01900  3   LEU C CD2 
3092 N N   . ASN C 4   ? 0.69870 0.65370 0.55790 -0.05330 -0.06060 0.06040  4   ASN C N   
3093 C CA  . ASN C 4   ? 0.75640 0.68950 0.63160 -0.04060 -0.02560 0.08630  4   ASN C CA  
3094 C C   . ASN C 4   ? 0.75150 0.68270 0.60450 -0.02670 -0.03970 0.10100  4   ASN C C   
3095 O O   . ASN C 4   ? 0.74830 0.67510 0.53910 -0.00200 -0.05590 0.11070  4   ASN C O   
3096 C CB  . ASN C 4   ? 0.79220 0.69870 0.62710 -0.01900 0.00470  0.10910  4   ASN C CB  
3097 C CG  . ASN C 4   ? 0.83100 0.70370 0.67070 0.00390  0.05120  0.14450  4   ASN C CG  
3098 O OD1 . ASN C 4   ? 0.81990 0.68410 0.73690 -0.00930 0.08770  0.14490  4   ASN C OD1 
3099 N ND2 . ASN C 4   ? 0.87020 0.72260 0.62910 0.04350  0.05190  0.17210  4   ASN C ND2 
3100 N N   . LEU C 5   ? 0.83600 0.77380 0.74170 -0.03910 -0.03700 0.09770  5   LEU C N   
3101 C CA  . LEU C 5   ? 0.83600 0.77530 0.72530 -0.02780 -0.05350 0.10790  5   LEU C CA  
3102 C C   . LEU C 5   ? 0.88490 0.79680 0.78180 -0.00860 -0.01500 0.13910  5   LEU C C   
3103 O O   . LEU C 5   ? 0.86620 0.77660 0.83070 -0.02370 0.00650  0.13760  5   LEU C O   
3104 C CB  . LEU C 5   ? 0.77910 0.74230 0.71260 -0.05040 -0.07780 0.08570  5   LEU C CB  
3105 C CG  . LEU C 5   ? 0.74390 0.72040 0.65150 -0.04540 -0.11300 0.07900  5   LEU C CG  
3106 C CD1 . LEU C 5   ? 0.72670 0.70500 0.57890 -0.02820 -0.13240 0.07430  5   LEU C CD1 
3107 C CD2 . LEU C 5   ? 0.66580 0.65980 0.60850 -0.06650 -0.12950 0.05660  5   LEU C CD2 
3108 N N   . PRO C 6   ? 1.37250 1.26100 1.20130 0.02990  -0.00380 0.16660  6   PRO C N   
3109 C CA  . PRO C 6   ? 1.40040 1.25170 1.22730 0.05700  0.04530  0.20390  6   PRO C CA  
3110 C C   . PRO C 6   ? 1.38780 1.24540 1.23560 0.05690  0.03460  0.20720  6   PRO C C   
3111 O O   . PRO C 6   ? 1.38120 1.25610 1.18420 0.07300  -0.00660 0.20010  6   PRO C O   
3112 C CB  . PRO C 6   ? 1.43290 1.26040 1.15730 0.11100  0.05060  0.22940  6   PRO C CB  
3113 C CG  . PRO C 6   ? 1.40110 1.25760 1.08950 0.10450  0.00360  0.19950  6   PRO C CG  
3114 C CD  . PRO C 6   ? 1.36150 1.25700 1.11020 0.05780  -0.03650 0.16240  6   PRO C CD  
3115 N N   . ALA C 7   ? 0.80890 0.65570 0.73520 0.03820  0.07060  0.21250  7   ALA C N   
3116 C CA  . ALA C 7   ? 0.81420 0.65020 0.75610 0.04870  0.08230  0.22980  7   ALA C CA  
3117 C C   . ALA C 7   ? 0.77320 0.64700 0.72400 0.03050  0.02750  0.20440  7   ALA C C   
3118 O O   . ALA C 7   ? 0.78020 0.64900 0.71780 0.04750  0.02420  0.21830  7   ALA C O   
3119 C CB  . ALA C 7   ? 0.85260 0.65010 0.70670 0.10660  0.10760  0.27230  7   ALA C CB  
3120 N N   . VAL C 8   ? 0.66200 0.56990 0.63480 -0.00010 -0.01080 0.16940  8   VAL C N   
3121 C CA  . VAL C 8   ? 0.62380 0.56190 0.60480 -0.01440 -0.05530 0.14760  8   VAL C CA  
3122 C C   . VAL C 8   ? 0.59040 0.53810 0.64750 -0.03840 -0.04810 0.13680  8   VAL C C   
3123 O O   . VAL C 8   ? 0.56050 0.51570 0.67160 -0.05760 -0.03660 0.11820  8   VAL C O   
3124 C CB  . VAL C 8   ? 0.59040 0.55220 0.55800 -0.02960 -0.08970 0.11950  8   VAL C CB  
3125 C CG1 . VAL C 8   ? 0.53590 0.52120 0.52810 -0.04500 -0.12090 0.09980  8   VAL C CG1 
3126 C CG2 . VAL C 8   ? 0.60360 0.56250 0.50150 -0.00350 -0.10510 0.12270  8   VAL C CG2 
3127 N N   . SER C 9   ? 0.52560 0.47690 0.58810 -0.03390 -0.05880 0.14320  9   SER C N   
3128 C CA  . SER C 9   ? 0.48980 0.45190 0.61940 -0.05230 -0.05630 0.13190  9   SER C CA  
3129 C C   . SER C 9   ? 0.46170 0.44920 0.59150 -0.06300 -0.09530 0.11290  9   SER C C   
3130 O O   . SER C 9   ? 0.46920 0.46260 0.55860 -0.05380 -0.11960 0.11390  9   SER C O   
3131 C CB  . SER C 9   ? 0.50470 0.44560 0.64900 -0.03820 -0.02900 0.15790  9   SER C CB  
3132 O OG  . SER C 9   ? 0.52680 0.46880 0.61680 -0.01760 -0.05240 0.17050  9   SER C OG  
3133 N N   . TRP C 10  ? 0.55000 0.55230 0.73180 -0.07800 -0.09870 0.09360  10  TRP C N   
3134 C CA  . TRP C 10  ? 0.50300 0.52110 0.69010 -0.08290 -0.12380 0.08300  10  TRP C CA  
3135 C C   . TRP C 10  ? 0.52570 0.53960 0.71570 -0.07610 -0.12560 0.10000  10  TRP C C   
3136 O O   . TRP C 10  ? 0.56090 0.55790 0.75190 -0.06620 -0.10350 0.11990  10  TRP C O   
3137 C CB  . TRP C 10  ? 0.42930 0.46240 0.66010 -0.08870 -0.12600 0.05870  10  TRP C CB  
3138 C CG  . TRP C 10  ? 0.41510 0.45550 0.63070 -0.08770 -0.13230 0.03930  10  TRP C CG  
3139 C CD1 . TRP C 10  ? 0.44060 0.47470 0.62540 -0.08850 -0.12880 0.04030  10  TRP C CD1 
3140 C CD2 . TRP C 10  ? 0.38410 0.43740 0.60650 -0.07910 -0.14220 0.01660  10  TRP C CD2 
3141 N NE1 . TRP C 10  ? 0.41650 0.45910 0.59180 -0.08400 -0.13550 0.01950  10  TRP C NE1 
3142 C CE2 . TRP C 10  ? 0.39160 0.44490 0.58560 -0.07440 -0.14300 0.00530  10  TRP C CE2 
3143 C CE3 . TRP C 10  ? 0.36770 0.43090 0.61050 -0.06870 -0.14950 0.00550  10  TRP C CE3 
3144 C CZ2 . TRP C 10  ? 0.38820 0.44880 0.56840 -0.05560 -0.14920 -0.01510 10  TRP C CZ2 
3145 C CZ3 . TRP C 10  ? 0.37530 0.44600 0.60150 -0.04720 -0.15610 -0.01520 10  TRP C CZ3 
3146 C CH2 . TRP C 10  ? 0.39130 0.45960 0.58450 -0.03910 -0.15500 -0.02450 10  TRP C CH2 
3147 O OXT . TRP C 10  ? 0.48260 0.50700 0.67510 -0.07800 -0.14480 0.09540  10  TRP C OXT 
3148 N N   . ASP D 6   ? 0.73150 0.68990 0.72510 -0.10240 -0.10080 -0.00820 6   ASP G N   
3149 C CA  . ASP D 6   ? 0.85490 0.79020 0.82260 -0.10570 -0.10650 -0.01370 6   ASP G CA  
3150 C C   . ASP D 6   ? 0.88150 0.80750 0.84380 -0.10650 -0.10020 -0.01640 6   ASP G C   
3151 O O   . ASP D 6   ? 0.82350 0.73690 0.78070 -0.11290 -0.10780 -0.01790 6   ASP G O   
3152 C CB  . ASP D 6   ? 0.86030 0.78910 0.82820 -0.11370 -0.12300 -0.01250 6   ASP G CB  
3153 C CG  . ASP D 6   ? 0.78680 0.68970 0.72400 -0.11660 -0.12950 -0.01860 6   ASP G CG  
3154 O OD1 . ASP D 6   ? 0.98850 0.88070 0.90310 -0.11190 -0.12590 -0.02230 6   ASP G OD1 
3155 O OD2 . ASP D 6   ? 0.94020 0.83270 0.87560 -0.12360 -0.13830 -0.01940 6   ASP G OD2 
3156 N N   . LYS D 7   ? 0.77460 0.65310 0.76230 0.02610  -0.15970 0.05950  7   LYS G N   
3157 C CA  . LYS D 7   ? 0.75050 0.64880 0.74810 0.01220  -0.13930 0.04860  7   LYS G CA  
3158 C C   . LYS D 7   ? 0.73370 0.61470 0.72200 -0.01730 -0.13210 0.05910  7   LYS G C   
3159 O O   . LYS D 7   ? 0.75550 0.59530 0.73950 -0.02390 -0.14300 0.07190  7   LYS G O   
3160 C CB  . LYS D 7   ? 0.75930 0.63830 0.75390 0.03560  -0.13980 0.03270  7   LYS G CB  
3161 C CG  . LYS D 7   ? 0.76470 0.69090 0.77440 0.06390  -0.12520 0.02440  7   LYS G CG  
3162 C CD  . LYS D 7   ? 0.77640 0.70120 0.77710 0.07360  -0.11040 0.01180  7   LYS G CD  
3163 C CE  . LYS D 7   ? 0.79200 0.65150 0.75660 0.09900  -0.13260 -0.00450 7   LYS G CE  
3164 N NZ  . LYS D 7   ? 0.78670 0.64210 0.73380 0.11130  -0.12240 -0.01870 7   LYS G NZ  
3165 N N   . PRO D 8   ? 0.57270 0.48370 0.56250 -0.03410 -0.11550 0.05670  8   PRO G N   
3166 C CA  . PRO D 8   ? 0.55780 0.46020 0.54160 -0.05450 -0.10320 0.06570  8   PRO G CA  
3167 C C   . PRO D 8   ? 0.54060 0.42810 0.53840 -0.05690 -0.10040 0.05540  8   PRO G C   
3168 O O   . PRO D 8   ? 0.53570 0.42590 0.53780 -0.04030 -0.10150 0.03810  8   PRO G O   
3169 C CB  . PRO D 8   ? 0.54630 0.48000 0.52140 -0.06200 -0.09080 0.05850  8   PRO G CB  
3170 C CG  . PRO D 8   ? 0.55660 0.51010 0.53620 -0.05120 -0.10470 0.05100  8   PRO G CG  
3171 C CD  . PRO D 8   ? 0.55070 0.50270 0.55140 -0.03430 -0.11210 0.04820  8   PRO G CD  
3172 N N   . PHE D 9   ? 0.61580 0.49100 0.62090 -0.07430 -0.09680 0.06910  9   PHE G N   
3173 C CA  . PHE D 9   ? 0.58530 0.44740 0.60510 -0.07870 -0.09910 0.05910  9   PHE G CA  
3174 C C   . PHE D 9   ? 0.54810 0.44210 0.56930 -0.09030 -0.07540 0.05680  9   PHE G C   
3175 O O   . PHE D 9   ? 0.53880 0.44810 0.56180 -0.10250 -0.06260 0.07630  9   PHE G O   
3176 C CB  . PHE D 9   ? 0.58390 0.40910 0.62790 -0.09180 -0.12010 0.07730  9   PHE G CB  
3177 C CG  . PHE D 9   ? 0.55220 0.36390 0.61370 -0.09650 -0.12990 0.06470  9   PHE G CG  
3178 C CD1 . PHE D 9   ? 0.57610 0.35700 0.62020 -0.07280 -0.15020 0.03480  9   PHE G CD1 
3179 C CD2 . PHE D 9   ? 0.51800 0.35200 0.60850 -0.11830 -0.11810 0.08230  9   PHE G CD2 
3180 C CE1 . PHE D 9   ? 0.56420 0.32940 0.61480 -0.07180 -0.16370 0.02020  9   PHE G CE1 
3181 C CE2 . PHE D 9   ? 0.49710 0.32070 0.60560 -0.12130 -0.13130 0.06960  9   PHE G CE2 
3182 C CZ  . PHE D 9   ? 0.52340 0.30910 0.60960 -0.09860 -0.15660 0.03720  9   PHE G CZ  
3183 N N   . LEU D 10  ? 0.47050 0.37460 0.48880 -0.08170 -0.06850 0.03580  10  LEU G N   
3184 C CA  . LEU D 10  ? 0.43910 0.36640 0.45720 -0.08900 -0.04940 0.03050  10  LEU G CA  
3185 C C   . LEU D 10  ? 0.41740 0.33340 0.44790 -0.09240 -0.05260 0.02710  10  LEU G C   
3186 O O   . LEU D 10  ? 0.43730 0.32840 0.46690 -0.08030 -0.06990 0.01590  10  LEU G O   
3187 C CB  . LEU D 10  ? 0.43380 0.38030 0.44910 -0.07930 -0.04080 0.01700  10  LEU G CB  
3188 C CG  . LEU D 10  ? 0.40620 0.36850 0.42270 -0.08620 -0.02590 0.01150  10  LEU G CG  
3189 C CD1 . LEU D 10  ? 0.41490 0.38230 0.41790 -0.09500 -0.02380 0.01510  10  LEU G CD1 
3190 C CD2 . LEU D 10  ? 0.41160 0.39300 0.44240 -0.07870 -0.02030 0.00820  10  LEU G CD2 
3191 N N   . SER D 11  ? 0.51520 0.44830 0.55370 -0.10370 -0.03890 0.03490  11  SER G N   
3192 C CA  . SER D 11  ? 0.50740 0.43490 0.56440 -0.10690 -0.04510 0.03240  11  SER G CA  
3193 C C   . SER D 11  ? 0.49080 0.44440 0.54640 -0.10920 -0.02330 0.03250  11  SER G C   
3194 O O   . SER D 11  ? 0.49940 0.47090 0.54050 -0.10930 -0.00640 0.03830  11  SER G O   
3195 C CB  . SER D 11  ? 0.49920 0.41400 0.59290 -0.12150 -0.06450 0.05360  11  SER G CB  
3196 O OG  . SER D 11  ? 0.50050 0.44420 0.60800 -0.13310 -0.04570 0.08360  11  SER G OG  
3197 N N   . ALA D 12  ? 0.48670 0.43700 0.55100 -0.10590 -0.02790 0.02350  12  ALA G N   
3198 C CA  . ALA D 12  ? 0.48090 0.45110 0.54480 -0.10420 -0.01080 0.02220  12  ALA G CA  
3199 C C   . ALA D 12  ? 0.48090 0.46510 0.58500 -0.11250 -0.01770 0.03730  12  ALA G C   
3200 O O   . ALA D 12  ? 0.47630 0.44170 0.60460 -0.11700 -0.04520 0.03640  12  ALA G O   
3201 C CB  . ALA D 12  ? 0.49170 0.45140 0.53460 -0.09090 -0.00850 0.00320  12  ALA G CB  
3202 N N   . TRP D 13  ? 0.59030 0.60710 0.70360 -0.11190 0.00380  0.05150  13  TRP G N   
3203 C CA  . TRP D 13  ? 0.58370 0.62830 0.75000 -0.12000 0.00050  0.07420  13  TRP G CA  
3204 C C   . TRP D 13  ? 0.58780 0.66000 0.75050 -0.10570 0.02100  0.07230  13  TRP G C   
3205 O O   . TRP D 13  ? 0.61520 0.69360 0.73740 -0.09060 0.04440  0.06650  13  TRP G O   
3206 C CB  . TRP D 13  ? 0.57080 0.64360 0.77160 -0.13180 0.00990  0.11300  13  TRP G CB  
3207 C CG  . TRP D 13  ? 0.55450 0.64960 0.83620 -0.15050 -0.00770 0.14340  13  TRP G CG  
3208 C CD1 . TRP D 13  ? 0.53850 0.60380 0.86500 -0.17100 -0.04730 0.15040  13  TRP G CD1 
3209 C CD2 . TRP D 13  ? 0.54230 0.69280 0.87690 -0.14970 0.00800  0.17110  13  TRP G CD2 
3210 N NE1 . TRP D 13  ? 0.51860 0.61450 0.92310 -0.18460 -0.06040 0.17960  13  TRP G NE1 
3211 C CE2 . TRP D 13  ? 0.51080 0.66740 0.93210 -0.17540 -0.02480 0.19760  13  TRP G CE2 
3212 C CE3 . TRP D 13  ? 0.54780 0.74200 0.86590 -0.12670 0.04380  0.17550  13  TRP G CE3 
3213 C CZ2 . TRP D 13  ? 0.49360 0.70040 0.97720 -0.17420 -0.02040 0.22540  13  TRP G CZ2 
3214 C CZ3 . TRP D 13  ? 0.52920 0.78290 0.91950 -0.12780 0.05290  0.20980  13  TRP G CZ3 
3215 C CH2 . TRP D 13  ? 0.49590 0.76080 0.97610 -0.15460 0.02140  0.23750  13  TRP G CH2 
3216 N N   . PRO D 14  ? 0.45110 0.53660 0.65500 -0.10750 0.00780  0.07570  14  PRO G N   
3217 C CA  . PRO D 14  ? 0.43670 0.50870 0.69080 -0.12330 -0.03080 0.07940  14  PRO G CA  
3218 C C   . PRO D 14  ? 0.46290 0.48190 0.67880 -0.11420 -0.06060 0.04440  14  PRO G C   
3219 O O   . PRO D 14  ? 0.45850 0.45040 0.69940 -0.12100 -0.10080 0.03970  14  PRO G O   
3220 C CB  . PRO D 14  ? 0.43730 0.55250 0.74820 -0.12270 -0.03150 0.09650  14  PRO G CB  
3221 C CG  . PRO D 14  ? 0.46600 0.59070 0.72800 -0.09790 -0.00130 0.08100  14  PRO G CG  
3222 C CD  . PRO D 14  ? 0.47420 0.59100 0.68110 -0.09070 0.02720  0.07780  14  PRO G CD  
3223 N N   . SER D 15  ? 0.47010 0.47360 0.62750 -0.09610 -0.04350 0.02240  15  SER G N   
3224 C CA  . SER D 15  ? 0.50330 0.46770 0.62090 -0.07930 -0.06270 -0.00310 15  SER G CA  
3225 C C   . SER D 15  ? 0.51190 0.46770 0.57890 -0.06740 -0.03650 -0.01260 15  SER G C   
3226 O O   . SER D 15  ? 0.50850 0.47930 0.56690 -0.06610 -0.01220 -0.00940 15  SER G O   
3227 C CB  . SER D 15  ? 0.52960 0.49310 0.65190 -0.06620 -0.07860 -0.01180 15  SER G CB  
3228 O OG  . SER D 15  ? 0.56700 0.49250 0.63970 -0.04220 -0.09590 -0.03390 15  SER G OG  
3229 N N   . ALA D 16  ? 0.46990 0.40120 0.50780 -0.05680 -0.04450 -0.02290 16  ALA G N   
3230 C CA  . ALA D 16  ? 0.48770 0.41890 0.49340 -0.04630 -0.02170 -0.02460 16  ALA G CA  
3231 C C   . ALA D 16  ? 0.51520 0.44330 0.49760 -0.02780 -0.01210 -0.02720 16  ALA G C   
3232 O O   . ALA D 16  ? 0.51340 0.44780 0.48700 -0.02650 0.00970  -0.01960 16  ALA G O   
3233 C CB  . ALA D 16  ? 0.50360 0.41920 0.48950 -0.03320 -0.03040 -0.03010 16  ALA G CB  
3234 N N   . VAL D 17  ? 0.44650 0.36280 0.42200 -0.01350 -0.03190 -0.03570 17  VAL G N   
3235 C CA  . VAL D 17  ? 0.47040 0.38320 0.42250 0.00590  -0.02500 -0.03590 17  VAL G CA  
3236 C C   . VAL D 17  ? 0.46210 0.39180 0.44500 -0.00840 -0.02010 -0.03100 17  VAL G C   
3237 O O   . VAL D 17  ? 0.46420 0.40320 0.47910 -0.01560 -0.04000 -0.03270 17  VAL G O   
3238 C CB  . VAL D 17  ? 0.50140 0.38950 0.42090 0.03610  -0.05460 -0.05080 17  VAL G CB  
3239 C CG1 . VAL D 17  ? 0.51960 0.40470 0.40900 0.05980  -0.04560 -0.04720 17  VAL G CG1 
3240 C CG2 . VAL D 17  ? 0.51280 0.38290 0.39280 0.06030  -0.05950 -0.05800 17  VAL G CG2 
3241 N N   . VAL D 18  ? 0.45430 0.38840 0.43260 -0.01130 0.00430  -0.02330 18  VAL G N   
3242 C CA  . VAL D 18  ? 0.44870 0.39710 0.44820 -0.01840 0.01140  -0.02080 18  VAL G CA  
3243 C C   . VAL D 18  ? 0.46080 0.39500 0.44090 -0.00380 0.02130  -0.01860 18  VAL G C   
3244 O O   . VAL D 18  ? 0.46270 0.37980 0.42390 -0.00130 0.03230  -0.01150 18  VAL G O   
3245 C CB  . VAL D 18  ? 0.42620 0.38430 0.43550 -0.03490 0.02460  -0.01760 18  VAL G CB  
3246 C CG1 . VAL D 18  ? 0.41390 0.35330 0.40500 -0.03930 0.03520  -0.01630 18  VAL G CG1 
3247 C CG2 . VAL D 18  ? 0.45030 0.42540 0.47060 -0.03050 0.03350  -0.01570 18  VAL G CG2 
3248 N N   . PRO D 19  ? 0.52320 0.46610 0.51350 0.00620  0.01760  -0.02010 19  PRO G N   
3249 C CA  . PRO D 19  ? 0.53130 0.45450 0.50200 0.02160  0.02520  -0.01750 19  PRO G CA  
3250 C C   . PRO D 19  ? 0.52900 0.43540 0.49440 0.01410  0.03830  -0.01750 19  PRO G C   
3251 O O   . PRO D 19  ? 0.52580 0.44500 0.50030 0.00630  0.04210  -0.02270 19  PRO G O   
3252 C CB  . PRO D 19  ? 0.55220 0.49610 0.54230 0.03570  0.01520  -0.02020 19  PRO G CB  
3253 C CG  . PRO D 19  ? 0.55740 0.53920 0.58850 0.02120  0.01200  -0.01840 19  PRO G CG  
3254 C CD  . PRO D 19  ? 0.54490 0.51890 0.57320 0.00470  0.00430  -0.01980 19  PRO G CD  
3255 N N   . ARG D 20  ? 0.55000 0.42400 0.49920 0.01850  0.04230  -0.01000 20  ARG G N   
3256 C CA  . ARG D 20  ? 0.56320 0.40670 0.50800 0.01490  0.04250  -0.01400 20  ARG G CA  
3257 C C   . ARG D 20  ? 0.58720 0.43640 0.52620 0.03460  0.04150  -0.02780 20  ARG G C   
3258 O O   . ARG D 20  ? 0.58600 0.45090 0.52820 0.05260  0.04090  -0.02660 20  ARG G O   
3259 C CB  . ARG D 20  ? 0.58700 0.39210 0.52670 0.01600  0.04230  0.00240  20  ARG G CB  
3260 C CG  . ARG D 20  ? 0.60820 0.37380 0.55400 0.00260  0.03230  -0.00000 20  ARG G CG  
3261 C CD  . ARG D 20  ? 0.63310 0.36210 0.59120 -0.00360 0.02990  0.02570  20  ARG G CD  
3262 N NE  . ARG D 20  ? 0.68500 0.36930 0.62630 0.01470  0.01820  0.01790  20  ARG G NE  
3263 C CZ  . ARG D 20  ? 0.69840 0.37380 0.62810 0.03360  0.02370  0.03250  20  ARG G CZ  
3264 N NH1 . ARG D 20  ? 0.68460 0.39250 0.61060 0.04010  0.03990  0.05350  20  ARG G NH1 
3265 N NH2 . ARG D 20  ? 0.73730 0.36590 0.65200 0.05140  0.01010  0.02430  20  ARG G NH2 
3266 N N   . GLY D 21  ? 0.55700 0.39700 0.48550 0.03580  0.04070  -0.04050 21  GLY G N   
3267 C CA  . GLY D 21  ? 0.57390 0.43140 0.49200 0.06240  0.04640  -0.05070 21  GLY G CA  
3268 C C   . GLY D 21  ? 0.56130 0.48170 0.50390 0.06100  0.05880  -0.04310 21  GLY G C   
3269 O O   . GLY D 21  ? 0.57740 0.52620 0.51630 0.08530  0.07050  -0.04370 21  GLY G O   
3270 N N   . GLY D 22  ? 0.48320 0.42590 0.45140 0.03610  0.05670  -0.03320 22  GLY G N   
3271 C CA  . GLY D 22  ? 0.47660 0.47080 0.47710 0.02850  0.06300  -0.02130 22  GLY G CA  
3272 C C   . GLY D 22  ? 0.47100 0.46800 0.45610 0.02230  0.07060  -0.02170 22  GLY G C   
3273 O O   . GLY D 22  ? 0.49280 0.45950 0.43810 0.03560  0.07140  -0.03530 22  GLY G O   
3274 N N   . HIS D 23  ? 0.52620 0.55370 0.54040 0.00380  0.07120  -0.00770 23  HIS G N   
3275 C CA  . HIS D 23  ? 0.52060 0.54870 0.51720 -0.00190 0.07680  -0.00570 23  HIS G CA  
3276 C C   . HIS D 23  ? 0.48470 0.51810 0.50810 -0.02920 0.06640  0.00360  23  HIS G C   
3277 O O   . HIS D 23  ? 0.46360 0.51560 0.52740 -0.03970 0.05730  0.01450  23  HIS G O   
3278 C CB  . HIS D 23  ? 0.53460 0.60560 0.52950 0.02060  0.09850  0.00990  23  HIS G CB  
3279 C CG  . HIS D 23  ? 0.49430 0.62580 0.55410 0.01320  0.10690  0.04150  23  HIS G CG  
3280 N ND1 . HIS D 23  ? 0.45950 0.61230 0.55870 -0.01210 0.10280  0.06370  23  HIS G ND1 
3281 C CD2 . HIS D 23  ? 0.48850 0.66420 0.58990 0.02670  0.11520  0.05730  23  HIS G CD2 
3282 C CE1 . HIS D 23  ? 0.42300 0.62800 0.59050 -0.01760 0.10570  0.09350  23  HIS G CE1 
3283 N NE2 . HIS D 23  ? 0.44230 0.66700 0.61520 0.00550  0.11400  0.09090  23  HIS G NE2 
3284 N N   . VAL D 24  ? 0.56120 0.57380 0.56150 -0.03820 0.06270  -0.00260 24  VAL G N   
3285 C CA  . VAL D 24  ? 0.52180 0.53760 0.54050 -0.05780 0.05370  0.00590  24  VAL G CA  
3286 C C   . VAL D 24  ? 0.53820 0.55230 0.53170 -0.05700 0.05780  0.00770  24  VAL G C   
3287 O O   . VAL D 24  ? 0.58570 0.57690 0.54220 -0.04670 0.05590  -0.00770 24  VAL G O   
3288 C CB  . VAL D 24  ? 0.49170 0.48070 0.50960 -0.06680 0.03980  -0.00480 24  VAL G CB  
3289 C CG1 . VAL D 24  ? 0.50120 0.46330 0.49370 -0.06520 0.03970  -0.01660 24  VAL G CG1 
3290 C CG2 . VAL D 24  ? 0.46120 0.45000 0.49340 -0.07900 0.02810  0.00100  24  VAL G CG2 
3291 N N   . THR D 25  ? 0.56860 0.60290 0.58190 -0.06630 0.05900  0.02730  25  THR G N   
3292 C CA  . THR D 25  ? 0.59280 0.62580 0.57990 -0.06380 0.06120  0.03250  25  THR G CA  
3293 C C   . THR D 25  ? 0.55450 0.56930 0.55290 -0.08190 0.04360  0.03040  25  THR G C   
3294 O O   . THR D 25  ? 0.52170 0.53840 0.55490 -0.09450 0.03430  0.04000  25  THR G O   
3295 C CB  . THR D 25  ? 0.59280 0.66660 0.59300 -0.05590 0.08050  0.06530  25  THR G CB  
3296 O OG1 . THR D 25  ? 0.61720 0.71310 0.59970 -0.02910 0.10080  0.06690  25  THR G OG1 
3297 C CG2 . THR D 25  ? 0.62000 0.69160 0.58740 -0.04990 0.08270  0.07500  25  THR G CG2 
3298 N N   . LEU D 26  ? 0.50780 0.50290 0.47840 -0.08050 0.03480  0.01640  26  LEU G N   
3299 C CA  . LEU D 26  ? 0.48230 0.46830 0.46150 -0.09090 0.02120  0.01790  26  LEU G CA  
3300 C C   . LEU D 26  ? 0.52100 0.51580 0.48580 -0.08730 0.02330  0.03530  26  LEU G C   
3301 O O   . LEU D 26  ? 0.58230 0.57860 0.50900 -0.07210 0.02820  0.03330  26  LEU G O   
3302 C CB  . LEU D 26  ? 0.48220 0.45220 0.45430 -0.09250 0.00930  0.00040  26  LEU G CB  
3303 C CG  . LEU D 26  ? 0.43060 0.39650 0.42440 -0.09630 0.00890  -0.00530 26  LEU G CG  
3304 C CD1 . LEU D 26  ? 0.42230 0.38360 0.42570 -0.10050 0.00040  -0.01070 26  LEU G CD1 
3305 C CD2 . LEU D 26  ? 0.40980 0.37750 0.41870 -0.09600 0.00510  0.00090  26  LEU G CD2 
3306 N N   . ARG D 27  ? 0.61290 0.60870 0.60310 -0.09750 0.01720  0.05270  27  ARG G N   
3307 C CA  . ARG D 27  ? 0.64180 0.64280 0.62170 -0.09520 0.01820  0.07530  27  ARG G CA  
3308 C C   . ARG D 27  ? 0.64480 0.62510 0.62340 -0.09870 -0.00190 0.06760  27  ARG G C   
3309 O O   . ARG D 27  ? 0.60770 0.57390 0.60800 -0.10420 -0.01460 0.05680  27  ARG G O   
3310 C CB  . ARG D 27  ? 0.61160 0.63010 0.63200 -0.10530 0.02550  0.11110  27  ARG G CB  
3311 C CG  . ARG D 27  ? 0.64800 0.70280 0.65520 -0.09090 0.05350  0.13940  27  ARG G CG  
3312 C CD  . ARG D 27  ? 0.60680 0.68950 0.67470 -0.10550 0.06180  0.18710  27  ARG G CD  
3313 N NE  . ARG D 27  ? 0.56490 0.64490 0.69170 -0.12520 0.04630  0.18250  27  ARG G NE  
3314 C CZ  . ARG D 27  ? 0.53940 0.63790 0.73830 -0.14490 0.04050  0.21960  27  ARG G CZ  
3315 N NH1 . ARG D 27  ? 0.52680 0.65280 0.75530 -0.15020 0.05440  0.27140  27  ARG G NH1 
3316 N NH2 . ARG D 27  ? 0.49670 0.58580 0.74220 -0.15940 0.01750  0.20740  27  ARG G NH2 
3317 N N   . CYS D 28  ? 0.55020 0.52960 0.49790 -0.08920 -0.00520 0.07300  28  CYS G N   
3318 C CA  . CYS D 28  ? 0.56780 0.53310 0.51460 -0.08860 -0.02450 0.06920  28  CYS G CA  
3319 C C   . CYS D 28  ? 0.58950 0.55300 0.52720 -0.08550 -0.02390 0.10070  28  CYS G C   
3320 O O   . CYS D 28  ? 0.63350 0.60740 0.53230 -0.07110 -0.01430 0.11310  28  CYS G O   
3321 C CB  . CYS D 28  ? 0.60690 0.57140 0.53040 -0.08020 -0.03700 0.04630  28  CYS G CB  
3322 S SG  . CYS D 28  ? 0.61200 0.57270 0.54790 -0.07710 -0.06160 0.04140  28  CYS G SG  
3323 N N   . HIS D 29  ? 0.52200 0.46850 0.49150 -0.09520 -0.03550 0.11470  29  HIS G N   
3324 C CA  . HIS D 29  ? 0.53630 0.47500 0.50920 -0.09670 -0.03770 0.15140  29  HIS G CA  
3325 C C   . HIS D 29  ? 0.57360 0.48900 0.53430 -0.08760 -0.06070 0.14360  29  HIS G C   
3326 O O   . HIS D 29  ? 0.56050 0.45690 0.53860 -0.08680 -0.07830 0.12210  29  HIS G O   
3327 C CB  . HIS D 29  ? 0.51170 0.43930 0.53860 -0.11640 -0.04300 0.17610  29  HIS G CB  
3328 C CG  . HIS D 29  ? 0.55510 0.47640 0.60000 -0.12320 -0.04430 0.22470  29  HIS G CG  
3329 N ND1 . HIS D 29  ? 0.58270 0.46060 0.64570 -0.12830 -0.07390 0.23250  29  HIS G ND1 
3330 C CD2 . HIS D 29  ? 0.58340 0.53680 0.63090 -0.12260 -0.01830 0.27240  29  HIS G CD2 
3331 C CE1 . HIS D 29  ? 0.62420 0.50420 0.70610 -0.13600 -0.06840 0.28490  29  HIS G CE1 
3332 N NE2 . HIS D 29  ? 0.62460 0.55520 0.69810 -0.13210 -0.03180 0.31270  29  HIS G NE2 
3333 N N   . TYR D 30  ? 0.64110 0.55930 0.56790 -0.07510 -0.06000 0.16260  30  TYR G N   
3334 C CA  . TYR D 30  ? 0.66880 0.57090 0.58020 -0.06220 -0.08260 0.15450  30  TYR G CA  
3335 C C   . TYR D 30  ? 0.71230 0.61160 0.59090 -0.05060 -0.07980 0.19140  30  TYR G C   
3336 O O   . TYR D 30  ? 0.72660 0.64690 0.56290 -0.03760 -0.06230 0.20210  30  TYR G O   
3337 C CB  . TYR D 30  ? 0.67800 0.59660 0.57210 -0.05180 -0.09150 0.11770  30  TYR G CB  
3338 C CG  . TYR D 30  ? 0.69670 0.61040 0.58140 -0.03670 -0.11570 0.11240  30  TYR G CG  
3339 C CD1 . TYR D 30  ? 0.68540 0.58540 0.59930 -0.03270 -0.13050 0.10850  30  TYR G CD1 
3340 C CD2 . TYR D 30  ? 0.72650 0.64810 0.56980 -0.02130 -0.12720 0.10930  30  TYR G CD2 
3341 C CE1 . TYR D 30  ? 0.70440 0.60630 0.61500 -0.01550 -0.15190 0.10540  30  TYR G CE1 
3342 C CE2 . TYR D 30  ? 0.73630 0.65710 0.57700 -0.00710 -0.15370 0.10490  30  TYR G CE2 
3343 C CZ  . TYR D 30  ? 0.72690 0.64160 0.60560 -0.00520 -0.16390 0.10490  30  TYR G CZ  
3344 O OH  . TYR D 30  ? 0.73580 0.65560 0.61690 0.01230  -0.18930 0.10250  30  TYR G OH  
3345 N N   . ARG D 31  ? 0.97250 0.84250 0.86470 -0.05050 -0.09720 0.21150  31  ARG G N   
3346 C CA  . ARG D 31  ? 1.01280 0.87530 0.87720 -0.03910 -0.09560 0.25420  31  ARG G CA  
3347 C C   . ARG D 31  ? 1.00860 0.89690 0.86890 -0.04310 -0.06200 0.30050  31  ARG G C   
3348 O O   . ARG D 31  ? 1.03590 0.94500 0.84010 -0.01930 -0.04480 0.32120  31  ARG G O   
3349 C CB  . ARG D 31  ? 1.05030 0.91990 0.85780 -0.01140 -0.10890 0.23710  31  ARG G CB  
3350 C CG  . ARG D 31  ? 1.04730 0.90630 0.87370 -0.00640 -0.13870 0.19930  31  ARG G CG  
3351 C CD  . ARG D 31  ? 1.07920 0.93940 0.86660 0.01900  -0.16150 0.19490  31  ARG G CD  
3352 N NE  . ARG D 31  ? 1.11640 0.99750 0.84970 0.03440  -0.16000 0.18400  31  ARG G NE  
3353 C CZ  . ARG D 31  ? 1.17200 1.04850 0.84260 0.06050  -0.16630 0.20310  31  ARG G CZ  
3354 N NH1 . ARG D 31  ? 1.19090 1.04670 0.85030 0.07080  -0.17110 0.23950  31  ARG G NH1 
3355 N NH2 . ARG D 31  ? 1.18700 1.07440 0.79950 0.08050  -0.17140 0.18430  31  ARG G NH2 
3356 N N   . HIS D 32  ? 1.09540 0.98530 1.01600 -0.06950 -0.05340 0.31730  32  HIS G N   
3357 C CA  . HIS D 32  ? 1.07410 0.99810 1.01790 -0.07750 -0.02050 0.37140  32  HIS G CA  
3358 C C   . HIS D 32  ? 1.07940 1.05070 0.96790 -0.05260 0.01330  0.36340  32  HIS G C   
3359 O O   . HIS D 32  ? 1.08500 1.09120 0.95060 -0.03500 0.04600  0.41150  32  HIS G O   
3360 C CB  . HIS D 32  ? 1.09630 1.01290 1.04720 -0.07630 -0.01550 0.43870  32  HIS G CB  
3361 C CG  . HIS D 32  ? 1.10700 0.96530 1.10600 -0.09600 -0.05470 0.44370  32  HIS G CG  
3362 N ND1 . HIS D 32  ? 1.15000 0.96740 1.11260 -0.07970 -0.08500 0.41870  32  HIS G ND1 
3363 C CD2 . HIS D 32  ? 1.09570 0.93270 1.17310 -0.12270 -0.07110 0.45080  32  HIS G CD2 
3364 C CE1 . HIS D 32  ? 1.14900 0.91280 1.16050 -0.09630 -0.11790 0.42670  32  HIS G CE1 
3365 N NE2 . HIS D 32  ? 1.12010 0.89540 1.19980 -0.12190 -0.11110 0.43870  32  HIS G NE2 
3366 N N   . ARG D 33  ? 0.91670 0.88810 0.78260 -0.04730 0.00560  0.30510  33  ARG G N   
3367 C CA  . ARG D 33  ? 0.93400 0.93530 0.74310 -0.02090 0.02790  0.28870  33  ARG G CA  
3368 C C   . ARG D 33  ? 0.90450 0.90530 0.73550 -0.03380 0.02200  0.24040  33  ARG G C   
3369 O O   . ARG D 33  ? 0.88470 0.86150 0.74920 -0.05260 -0.00280 0.20910  33  ARG G O   
3370 C CB  . ARG D 33  ? 1.00160 0.99110 0.72470 0.01430  0.01390  0.26680  33  ARG G CB  
3371 N N   . PHE D 34  ? 0.91910 0.94750 0.72630 -0.01810 0.04660  0.23680  34  PHE G N   
3372 C CA  . PHE D 34  ? 0.90230 0.92970 0.72470 -0.02660 0.04340  0.19580  34  PHE G CA  
3373 C C   . PHE D 34  ? 0.94970 0.96470 0.70260 0.00090  0.03300  0.15280  34  PHE G C   
3374 O O   . PHE D 34  ? 0.94380 0.95990 0.69630 0.00260  0.03660  0.12700  34  PHE G O   
3375 C CB  . PHE D 34  ? 0.85090 0.91490 0.71430 -0.03240 0.07370  0.22340  34  PHE G CB  
3376 C CG  . PHE D 34  ? 0.79020 0.85250 0.74100 -0.06950 0.06540  0.24420  34  PHE G CG  
3377 C CD1 . PHE D 34  ? 0.75720 0.79540 0.74120 -0.08970 0.04300  0.20700  34  PHE G CD1 
3378 C CD2 . PHE D 34  ? 0.76800 0.85040 0.76750 -0.08190 0.07720  0.30300  34  PHE G CD2 
3379 C CE1 . PHE D 34  ? 0.71470 0.74120 0.76710 -0.11680 0.02690  0.21960  34  PHE G CE1 
3380 C CE2 . PHE D 34  ? 0.72060 0.79040 0.80420 -0.11700 0.05750  0.31880  34  PHE G CE2 
3381 C CZ  . PHE D 34  ? 0.69450 0.73250 0.79830 -0.13200 0.02960  0.27250  34  PHE G CZ  
3382 N N   . ASN D 35  ? 0.95270 0.95040 0.64850 0.02260  0.01430  0.14390  35  ASN G N   
3383 C CA  . ASN D 35  ? 1.00350 0.98260 0.62640 0.05400  -0.00370 0.10620  35  ASN G CA  
3384 C C   . ASN D 35  ? 1.01270 0.96230 0.63410 0.04690  -0.04900 0.07350  35  ASN G C   
3385 O O   . ASN D 35  ? 0.99740 0.94630 0.66230 0.02620  -0.06010 0.08390  35  ASN G O   
3386 C CB  . ASN D 35  ? 1.04660 1.03730 0.58250 0.10300  0.01600  0.12970  35  ASN G CB  
3387 C CG  . ASN D 35  ? 1.04820 1.04880 0.57810 0.10710  0.02370  0.17500  35  ASN G CG  
3388 O OD1 . ASN D 35  ? 1.01290 1.03690 0.60500 0.08270  0.04780  0.22070  35  ASN G OD1 
3389 N ND2 . ASN D 35  ? 1.10310 1.08110 0.56030 0.13790  -0.00190 0.16330  35  ASN G ND2 
3390 N N   . ASN D 36  ? 1.03820 0.96240 0.61170 0.06670  -0.07850 0.03390  36  ASN G N   
3391 C CA  . ASN D 36  ? 1.04080 0.94050 0.61400 0.06380  -0.12840 0.00400  36  ASN G CA  
3392 C C   . ASN D 36  ? 0.98880 0.89910 0.65750 0.02150  -0.13860 0.00060  36  ASN G C   
3393 O O   . ASN D 36  ? 0.96770 0.88620 0.66530 0.01290  -0.14850 0.01310  36  ASN G O   
3394 C CB  . ASN D 36  ? 1.08790 0.98280 0.60480 0.09140  -0.14160 0.01960  36  ASN G CB  
3395 C CG  . ASN D 36  ? 1.14430 1.02270 0.54840 0.14560  -0.14250 0.01370  36  ASN G CG  
3396 O OD1 . ASN D 36  ? 1.16060 1.01500 0.52320 0.16510  -0.15720 -0.02060 36  ASN G OD1 
3397 N ND2 . ASN D 36  ? 1.17370 1.06170 0.52190 0.17540  -0.12730 0.04820  36  ASN G ND2 
3398 N N   . PHE D 37  ? 0.77910 0.68980 0.49150 0.00090  -0.13440 -0.01520 37  PHE G N   
3399 C CA  . PHE D 37  ? 0.70910 0.63430 0.50400 -0.03090 -0.13850 -0.01630 37  PHE G CA  
3400 C C   . PHE D 37  ? 0.68440 0.59780 0.50830 -0.04390 -0.15880 -0.04150 37  PHE G C   
3401 O O   . PHE D 37  ? 0.71300 0.60150 0.49490 -0.03070 -0.16480 -0.05970 37  PHE G O   
3402 C CB  . PHE D 37  ? 0.68550 0.62920 0.51780 -0.04600 -0.10140 0.00600  37  PHE G CB  
3403 C CG  . PHE D 37  ? 0.68000 0.62380 0.50830 -0.04790 -0.07680 0.00380  37  PHE G CG  
3404 C CD1 . PHE D 37  ? 0.71750 0.66630 0.50410 -0.03060 -0.05240 0.01990  37  PHE G CD1 
3405 C CD2 . PHE D 37  ? 0.63570 0.58060 0.50620 -0.06470 -0.07510 -0.00860 37  PHE G CD2 
3406 C CE1 . PHE D 37  ? 0.71060 0.66640 0.50060 -0.03000 -0.02980 0.01960  37  PHE G CE1 
3407 C CE2 . PHE D 37  ? 0.63100 0.57550 0.49790 -0.06440 -0.05430 -0.01030 37  PHE G CE2 
3408 C CZ  . PHE D 37  ? 0.67200 0.62250 0.50040 -0.04710 -0.03300 0.00210  37  PHE G CZ  
3409 N N   . MET D 38  ? 0.81430 0.74620 0.71180 -0.06690 -0.16890 -0.03920 38  MET G N   
3410 C CA  . MET D 38  ? 0.78590 0.71350 0.73150 -0.08540 -0.18330 -0.05030 38  MET G CA  
3411 C C   . MET D 38  ? 0.71890 0.67480 0.72020 -0.10180 -0.14900 -0.03260 38  MET G C   
3412 O O   . MET D 38  ? 0.70190 0.68040 0.71620 -0.09950 -0.12780 -0.01660 38  MET G O   
3413 C CB  . MET D 38  ? 0.77060 0.70130 0.76410 -0.09630 -0.23110 -0.05720 38  MET G CB  
3414 C CG  . MET D 38  ? 0.82450 0.71270 0.75650 -0.07700 -0.27930 -0.08440 38  MET G CG  
3415 S SD  . MET D 38  ? 0.81700 0.70310 0.82020 -0.09490 -0.35000 -0.09480 38  MET G SD  
3416 C CE  . MET D 38  ? 0.78980 0.73630 0.84310 -0.09650 -0.33570 -0.06570 38  MET G CE  
3417 N N   . LEU D 39  ? 0.63710 0.58520 0.66460 -0.11420 -0.14710 -0.03670 39  LEU G N   
3418 C CA  . LEU D 39  ? 0.58810 0.55930 0.65800 -0.12400 -0.11620 -0.02040 39  LEU G CA  
3419 C C   . LEU D 39  ? 0.54930 0.54490 0.69790 -0.14210 -0.12780 -0.00550 39  LEU G C   
3420 O O   . LEU D 39  ? 0.56690 0.54820 0.74280 -0.15470 -0.16450 -0.01210 39  LEU G O   
3421 C CB  . LEU D 39  ? 0.59840 0.54680 0.63870 -0.12140 -0.09820 -0.02810 39  LEU G CB  
3422 C CG  . LEU D 39  ? 0.60580 0.55360 0.59910 -0.10710 -0.07190 -0.02680 39  LEU G CG  
3423 C CD1 . LEU D 39  ? 0.62420 0.55350 0.58920 -0.10050 -0.05980 -0.03550 39  LEU G CD1 
3424 C CD2 . LEU D 39  ? 0.55830 0.53030 0.57720 -0.10820 -0.05060 -0.01090 39  LEU G CD2 
3425 N N   . TYR D 40  ? 0.56130 0.59380 0.74740 -0.14080 -0.09800 0.01670  40  TYR G N   
3426 C CA  . TYR D 40  ? 0.53030 0.60310 0.79760 -0.15250 -0.09620 0.04380  40  TYR G CA  
3427 C C   . TYR D 40  ? 0.52310 0.61170 0.79470 -0.14450 -0.05680 0.06130  40  TYR G C   
3428 O O   . TYR D 40  ? 0.53490 0.61480 0.75570 -0.12570 -0.03430 0.05290  40  TYR G O   
3429 C CB  . TYR D 40  ? 0.53350 0.65360 0.84220 -0.14450 -0.09910 0.06000  40  TYR G CB  
3430 C CG  . TYR D 40  ? 0.55560 0.66260 0.85380 -0.14660 -0.13900 0.04370  40  TYR G CG  
3431 C CD1 . TYR D 40  ? 0.58810 0.66790 0.81240 -0.12950 -0.14020 0.02470  40  TYR G CD1 
3432 C CD2 . TYR D 40  ? 0.53950 0.66260 0.90630 -0.16500 -0.17790 0.05120  40  TYR G CD2 
3433 C CE1 . TYR D 40  ? 0.61390 0.68180 0.82020 -0.12580 -0.17550 0.01270  40  TYR G CE1 
3434 C CE2 . TYR D 40  ? 0.56710 0.67570 0.91880 -0.16260 -0.22020 0.03400  40  TYR G CE2 
3435 C CZ  . TYR D 40  ? 0.60920 0.69000 0.87430 -0.14040 -0.21690 0.01440  40  TYR G CZ  
3436 O OH  . TYR D 40  ? 0.64550 0.71150 0.88790 -0.13300 -0.25830 -0.00020 40  TYR G OH  
3437 N N   . LYS D 41  ? 0.57950 0.68920 0.91380 -0.15820 -0.05200 0.08770  41  LYS G N   
3438 C CA  . LYS D 41  ? 0.57200 0.70220 0.91080 -0.14560 -0.01360 0.11100  41  LYS G CA  
3439 C C   . LYS D 41  ? 0.55660 0.75680 0.95630 -0.13180 0.01060  0.15120  41  LYS G C   
3440 O O   . LYS D 41  ? 0.54230 0.77940 1.01440 -0.14600 -0.00610 0.17090  41  LYS G O   
3441 C CB  . LYS D 41  ? 0.56600 0.66960 0.92640 -0.16550 -0.01900 0.11960  41  LYS G CB  
3442 C CG  . LYS D 41  ? 0.58930 0.63210 0.87570 -0.16280 -0.02620 0.08390  41  LYS G CG  
3443 C CD  . LYS D 41  ? 0.59860 0.61550 0.90480 -0.17540 -0.02710 0.09620  41  LYS G CD  
3444 C CE  . LYS D 41  ? 0.62070 0.58480 0.85610 -0.16620 -0.03070 0.06320  41  LYS G CE  
3445 N NZ  . LYS D 41  ? 0.64180 0.55910 0.89560 -0.18270 -0.05790 0.06050  41  LYS G NZ  
3446 N N   . GLU D 42  ? 0.47270 0.69320 0.84210 -0.09970 0.04900  0.16400  42  GLU G N   
3447 C CA  . GLU D 42  ? 0.48130 0.76850 0.88250 -0.06890 0.07750  0.19670  42  GLU G CA  
3448 C C   . GLU D 42  ? 0.43320 0.78530 0.94550 -0.08700 0.08570  0.25100  42  GLU G C   
3449 O O   . GLU D 42  ? 0.41750 0.82810 0.98690 -0.07860 0.08830  0.27480  42  GLU G O   
3450 C CB  . GLU D 42  ? 0.50880 0.79690 0.84450 -0.02370 0.11360  0.19860  42  GLU G CB  
3451 C CG  . GLU D 42  ? 0.51570 0.87140 0.86750 0.02220  0.14570  0.22990  42  GLU G CG  
3452 C CD  . GLU D 42  ? 0.54630 0.91400 0.84390 0.07230  0.18450  0.24530  42  GLU G CD  
3453 O OE1 . GLU D 42  ? 0.55470 0.87390 0.79870 0.07070  0.18310  0.22760  42  GLU G OE1 
3454 O OE2 . GLU D 42  ? 0.54920 0.97760 0.85530 0.11870  0.21620  0.27570  42  GLU G OE2 
3455 N N   . ASP D 43  ? 0.66840 1.00140 1.20150 -0.10680 0.08560  0.26780  43  ASP G N   
3456 C CA  . ASP D 43  ? 0.68980 1.05570 1.29390 -0.11370 0.08550  0.30930  43  ASP G CA  
3457 C C   . ASP D 43  ? 0.68740 1.05280 1.35520 -0.14480 0.04030  0.30490  43  ASP G C   
3458 O O   . ASP D 43  ? 0.69310 1.10820 1.43010 -0.14300 0.04280  0.34280  43  ASP G O   
3459 C CB  . ASP D 43  ? 0.71290 1.04530 1.31800 -0.12670 0.08680  0.32250  43  ASP G CB  
3460 N N   . ARG D 44  ? 0.78940 1.09870 1.43100 -0.16940 -0.00180 0.26030  44  ARG G N   
3461 C CA  . ARG D 44  ? 0.79910 1.09520 1.48090 -0.19280 -0.05150 0.24710  44  ARG G CA  
3462 C C   . ARG D 44  ? 0.78460 1.07490 1.42660 -0.18650 -0.06750 0.21190  44  ARG G C   
3463 O O   . ARG D 44  ? 0.79940 1.03010 1.38510 -0.19670 -0.09650 0.17030  44  ARG G O   
3464 C CB  . ARG D 44  ? 0.82430 1.04920 1.49980 -0.21980 -0.09390 0.22530  44  ARG G CB  
3465 N N   . ILE D 45  ? 0.70740 1.06100 1.37650 -0.16510 -0.04840 0.23080  45  ILE G N   
3466 C CA  . ILE D 45  ? 0.71620 1.07290 1.35770 -0.15560 -0.06430 0.20450  45  ILE G CA  
3467 C C   . ILE D 45  ? 0.72750 1.07750 1.40510 -0.17210 -0.11450 0.19460  45  ILE G C   
3468 O O   . ILE D 45  ? 0.73990 1.11060 1.48390 -0.18370 -0.12530 0.22030  45  ILE G O   
3469 C CB  . ILE D 45  ? 0.73240 1.14380 1.35810 -0.11010 -0.02050 0.22090  45  ILE G CB  
3470 C CG1 . ILE D 45  ? 0.78160 1.16050 1.33510 -0.08960 -0.03790 0.18310  45  ILE G CG1 
3471 C CG2 . ILE D 45  ? 0.70240 1.19570 1.41860 -0.09910 -0.00240 0.27050  45  ILE G CG2 
3472 C CD1 . ILE D 45  ? 0.80160 1.22940 1.35030 -0.04280 -0.00970 0.19710  45  ILE G CD1 
3473 N N   . HIS D 46  ? 1.00520 1.32390 1.63720 -0.17200 -0.14780 0.15910  46  HIS G N   
3474 C CA  . HIS D 46  ? 1.02560 1.32500 1.66490 -0.18050 -0.20030 0.14040  46  HIS G CA  
3475 C C   . HIS D 46  ? 1.05810 1.29060 1.68350 -0.20270 -0.24130 0.11890  46  HIS G C   
3476 O O   . HIS D 46  ? 1.08920 1.29740 1.71310 -0.20610 -0.28840 0.10080  46  HIS G O   
3477 C CB  . HIS D 46  ? 1.02190 1.39070 1.74480 -0.17310 -0.20080 0.17300  46  HIS G CB  
3478 C CG  . HIS D 46  ? 1.01500 1.44160 1.74020 -0.14060 -0.17660 0.18410  46  HIS G CG  
3479 N ND1 . HIS D 46  ? 1.00740 1.48960 1.74600 -0.11260 -0.12080 0.21350  46  HIS G ND1 
3480 C CD2 . HIS D 46  ? 1.03870 1.46830 1.74170 -0.12310 -0.20080 0.16840  46  HIS G CD2 
3481 C CE1 . HIS D 46  ? 1.03540 1.53260 1.73680 -0.07450 -0.10950 0.20700  46  HIS G CE1 
3482 N NE2 . HIS D 46  ? 1.05520 1.52220 1.73850 -0.08230 -0.15630 0.18190  46  HIS G NE2 
3483 N N   . VAL D 47  ? 0.96280 1.16340 1.57590 -0.21290 -0.22710 0.12000  47  VAL G N   
3484 C CA  . VAL D 47  ? 0.99820 1.12570 1.57920 -0.22510 -0.26540 0.09320  47  VAL G CA  
3485 C C   . VAL D 47  ? 1.00330 1.07800 1.48800 -0.21620 -0.25510 0.05910  47  VAL G C   
3486 O O   . VAL D 47  ? 0.97520 1.05410 1.45170 -0.21650 -0.21690 0.07040  47  VAL G O   
3487 C CB  . VAL D 47  ? 1.00490 1.13460 1.65180 -0.24180 -0.26260 0.12370  47  VAL G CB  
3488 C CG1 . VAL D 47  ? 1.05790 1.18800 1.77490 -0.25580 -0.31020 0.13500  47  VAL G CG1 
3489 C CG2 . VAL D 47  ? 0.97010 1.16860 1.66600 -0.23680 -0.20510 0.17020  47  VAL G CG2 
3490 N N   . PRO D 48  ? 0.66020 0.68620 1.06830 -0.20500 -0.28680 0.01980  48  PRO G N   
3491 C CA  . PRO D 48  ? 0.68570 0.66830 1.00330 -0.19350 -0.27390 -0.00750 48  PRO G CA  
3492 C C   . PRO D 48  ? 0.69570 0.63100 0.99610 -0.19750 -0.27490 -0.01700 48  PRO G C   
3493 O O   . PRO D 48  ? 0.73090 0.64110 1.06070 -0.20440 -0.30600 -0.01780 48  PRO G O   
3494 C CB  . PRO D 48  ? 0.73970 0.68380 0.97840 -0.17380 -0.31120 -0.04200 48  PRO G CB  
3495 C CG  . PRO D 48  ? 0.73270 0.70310 1.02550 -0.17630 -0.34350 -0.03280 48  PRO G CG  
3496 C CD  . PRO D 48  ? 0.71250 0.71590 1.10830 -0.19860 -0.33780 -0.00030 48  PRO G CD  
3497 N N   . ILE D 49  ? 0.80430 0.72470 1.05840 -0.19240 -0.24430 -0.02340 49  ILE G N   
3498 C CA  . ILE D 49  ? 0.82510 0.70190 1.06070 -0.19260 -0.24310 -0.03200 49  ILE G CA  
3499 C C   . ILE D 49  ? 0.89360 0.70190 1.04980 -0.17190 -0.28320 -0.07390 49  ILE G C   
3500 O O   . ILE D 49  ? 0.92970 0.72510 1.02770 -0.15340 -0.30250 -0.09630 49  ILE G O   
3501 C CB  . ILE D 49  ? 0.80740 0.69470 1.01270 -0.18480 -0.19200 -0.02420 49  ILE G CB  
3502 C CG1 . ILE D 49  ? 0.84840 0.72480 0.95930 -0.15550 -0.17310 -0.04740 49  ILE G CG1 
3503 C CG2 . ILE D 49  ? 0.75660 0.70980 1.02070 -0.19110 -0.15140 0.01420  49  ILE G CG2 
3504 C CD1 . ILE D 49  ? 0.84830 0.72560 0.92380 -0.14330 -0.13120 -0.04520 49  ILE G CD1 
3505 N N   . PHE D 50  ? 1.00480 0.76830 1.15270 -0.16940 -0.29530 -0.08300 50  PHE G N   
3506 C CA  . PHE D 50  ? 1.08360 0.77880 1.15400 -0.14130 -0.33300 -0.12190 50  PHE G CA  
3507 C C   . PHE D 50  ? 1.12690 0.80700 1.19940 -0.13460 -0.38210 -0.13400 50  PHE G C   
3508 O O   . PHE D 50  ? 1.18870 0.83120 1.17520 -0.10080 -0.40480 -0.16620 50  PHE G O   
3509 C CB  . PHE D 50  ? 1.12240 0.79680 1.08570 -0.10770 -0.31440 -0.15010 50  PHE G CB  
3510 C CG  . PHE D 50  ? 1.12420 0.79280 1.07080 -0.10600 -0.27790 -0.14720 50  PHE G CG  
3511 C CD1 . PHE D 50  ? 1.05780 0.78410 1.06390 -0.12780 -0.22930 -0.11070 50  PHE G CD1 
3512 C CD2 . PHE D 50  ? 1.18170 0.80190 1.04820 -0.07050 -0.28010 -0.17520 50  PHE G CD2 
3513 C CE1 . PHE D 50  ? 1.05320 0.78540 1.04370 -0.11920 -0.18980 -0.10340 50  PHE G CE1 
3514 C CE2 . PHE D 50  ? 1.17390 0.80590 1.03180 -0.06290 -0.23690 -0.16520 50  PHE G CE2 
3515 C CZ  . PHE D 50  ? 1.11110 0.79870 1.03310 -0.08930 -0.19380 -0.12940 50  PHE G CZ  
3516 N N   . HIS D 51  ? 1.10380 0.81550 1.27330 -0.16270 -0.39700 -0.10560 51  HIS G N   
3517 C CA  . HIS D 51  ? 1.15530 0.85650 1.34350 -0.16040 -0.44650 -0.11260 51  HIS G CA  
3518 C C   . HIS D 51  ? 1.15180 0.86380 1.27390 -0.13780 -0.44700 -0.13140 51  HIS G C   
3519 O O   . HIS D 51  ? 1.22110 0.89340 1.29100 -0.11320 -0.48870 -0.15770 51  HIS G O   
3520 C CB  . HIS D 51  ? 1.26520 0.88950 1.42460 -0.14420 -0.50250 -0.13920 51  HIS G CB  
3521 C CG  . HIS D 51  ? 1.28620 0.89240 1.50530 -0.16450 -0.50790 -0.12070 51  HIS G CG  
3522 N ND1 . HIS D 51  ? 1.30980 0.87420 1.47550 -0.14930 -0.49670 -0.13650 51  HIS G ND1 
3523 C CD2 . HIS D 51  ? 1.29750 0.92300 1.62570 -0.19680 -0.52370 -0.08470 51  HIS G CD2 
3524 C CE1 . HIS D 51  ? 1.32480 0.87990 1.56180 -0.17240 -0.50730 -0.11250 51  HIS G CE1 
3525 N NE2 . HIS D 51  ? 1.32090 0.91380 1.65790 -0.20160 -0.52300 -0.07920 51  HIS G NE2 
3526 N N   . GLY D 52  ? 0.98030 0.74290 1.10070 -0.14300 -0.40200 -0.11660 52  GLY G N   
3527 C CA  . GLY D 52  ? 0.97590 0.75380 1.04160 -0.12410 -0.40140 -0.12650 52  GLY G CA  
3528 C C   . GLY D 52  ? 1.02720 0.76360 0.96610 -0.08440 -0.39660 -0.15740 52  GLY G C   
3529 O O   . GLY D 52  ? 1.08440 0.80650 0.95790 -0.05580 -0.41680 -0.17290 52  GLY G O   
3530 N N   . ARG D 53  ? 1.06430 0.78420 0.96440 -0.07770 -0.36710 -0.16330 53  ARG G N   
3531 C CA  . ARG D 53  ? 1.13450 0.82620 0.91420 -0.03420 -0.35280 -0.18550 53  ARG G CA  
3532 C C   . ARG D 53  ? 1.13730 0.87810 0.88840 -0.02230 -0.31110 -0.16280 53  ARG G C   
3533 O O   . ARG D 53  ? 1.07820 0.87020 0.88790 -0.04590 -0.26830 -0.13160 53  ARG G O   
3534 C CB  . ARG D 53  ? 1.13290 0.81360 0.89540 -0.02930 -0.31710 -0.18610 53  ARG G CB  
3535 C CG  . ARG D 53  ? 1.20450 0.85470 0.84840 0.02520  -0.30510 -0.20830 53  ARG G CG  
3536 C CD  . ARG D 53  ? 1.19760 0.88810 0.83250 0.03340  -0.23700 -0.18520 53  ARG G CD  
3537 N NE  . ARG D 53  ? 1.19740 0.86110 0.84900 0.02880  -0.23480 -0.19450 53  ARG G NE  
3538 C CZ  . ARG D 53  ? 1.20410 0.88440 0.82860 0.04950  -0.19110 -0.18690 53  ARG G CZ  
3539 N NH1 . ARG D 53  ? 1.20790 0.93410 0.79340 0.07450  -0.14570 -0.16710 53  ARG G NH1 
3540 N NH2 . ARG D 53  ? 1.19360 0.84630 0.83760 0.04420  -0.19400 -0.19520 53  ARG G NH2 
3541 N N   . LEU D 54  ? 1.18510 0.90730 0.84380 0.01810  -0.32440 -0.17650 54  LEU G N   
3542 C CA  . LEU D 54  ? 1.19670 0.95910 0.81910 0.03510  -0.28300 -0.14960 54  LEU G CA  
3543 C C   . LEU D 54  ? 1.20950 0.98750 0.78580 0.05690  -0.22540 -0.13450 54  LEU G C   
3544 O O   . LEU D 54  ? 1.27000 1.02150 0.75680 0.10120  -0.22510 -0.15050 54  LEU G O   
3545 C CB  . LEU D 54  ? 1.25520 0.99280 0.79610 0.07300  -0.32070 -0.16490 54  LEU G CB  
3546 C CG  . LEU D 54  ? 1.23780 1.00540 0.81280 0.06080  -0.33150 -0.14570 54  LEU G CG  
3547 C CD1 . LEU D 54  ? 1.21540 1.03320 0.80820 0.05320  -0.26860 -0.10240 54  LEU G CD1 
3548 C CD2 . LEU D 54  ? 1.18470 0.96290 0.87130 0.01650  -0.37020 -0.14930 54  LEU G CD2 
3549 N N   . PHE D 55  ? 0.97540 0.79770 0.61260 0.02980  -0.17870 -0.10330 55  PHE G N   
3550 C CA  . PHE D 55  ? 0.99050 0.83650 0.60510 0.04430  -0.12730 -0.08310 55  PHE G CA  
3551 C C   . PHE D 55  ? 1.01590 0.88660 0.57970 0.07130  -0.10140 -0.05420 55  PHE G C   
3552 O O   . PHE D 55  ? 1.00100 0.89720 0.60370 0.05180  -0.09020 -0.02700 55  PHE G O   
3553 C CB  . PHE D 55  ? 0.92630 0.80370 0.62460 0.00660  -0.09720 -0.06270 55  PHE G CB  
3554 C CG  . PHE D 55  ? 0.89440 0.75270 0.63710 -0.01460 -0.11250 -0.08150 55  PHE G CG  
3555 C CD1 . PHE D 55  ? 0.86310 0.71910 0.66840 -0.04400 -0.13980 -0.08530 55  PHE G CD1 
3556 C CD2 . PHE D 55  ? 0.88460 0.73160 0.61160 -0.00370 -0.09760 -0.08980 55  PHE G CD2 
3557 C CE1 . PHE D 55  ? 0.83200 0.67450 0.68450 -0.06410 -0.15040 -0.09260 55  PHE G CE1 
3558 C CE2 . PHE D 55  ? 0.85080 0.67670 0.61860 -0.02280 -0.11190 -0.10240 55  PHE G CE2 
3559 C CZ  . PHE D 55  ? 0.82970 0.65320 0.66110 -0.05420 -0.13730 -0.10150 55  PHE G CZ  
3560 N N   . GLN D 56  ? 1.29220 1.15420 0.76670 0.12030  -0.09200 -0.05780 56  GLN G N   
3561 C CA  . GLN D 56  ? 1.31960 1.21170 0.74220 0.15240  -0.05950 -0.02070 56  GLN G CA  
3562 C C   . GLN D 56  ? 1.27670 1.22270 0.74450 0.14240  -0.00170 0.02600  56  GLN G C   
3563 O O   . GLN D 56  ? 1.28410 1.26370 0.71710 0.17100  0.03310  0.06640  56  GLN G O   
3564 C CB  . GLN D 56  ? 1.38100 1.24590 0.68050 0.21940  -0.07060 -0.04080 56  GLN G CB  
3565 N N   . GLU D 57  ? 1.16990 1.12620 0.71770 0.10330  0.00690  0.02460  57  GLU G N   
3566 C CA  . GLU D 57  ? 1.12570 1.12800 0.72640 0.09110  0.05030  0.06190  57  GLU G CA  
3567 C C   . GLU D 57  ? 1.08680 1.08160 0.76590 0.04740  0.04000  0.04580  57  GLU G C   
3568 O O   . GLU D 57  ? 1.09890 1.05890 0.78490 0.03320  0.00760  0.01060  57  GLU G O   
3569 C CB  . GLU D 57  ? 1.14160 1.16510 0.69060 0.13690  0.08100  0.06820  57  GLU G CB  
3570 C CG  . GLU D 57  ? 1.17580 1.15070 0.66830 0.16270  0.05300  0.01420  57  GLU G CG  
3571 C CD  . GLU D 57  ? 1.16820 1.16400 0.66140 0.18420  0.08160  0.01570  57  GLU G CD  
3572 O OE1 . GLU D 57  ? 1.17930 1.20890 0.61890 0.23500  0.11610  0.03800  57  GLU G OE1 
3573 O OE2 . GLU D 57  ? 1.14520 1.12760 0.69260 0.15400  0.07160  -0.00240 57  GLU G OE2 
3574 N N   . SER D 58  ? 0.78650 0.81580 0.52700 0.02790  0.06640  0.07490  58  SER G N   
3575 C CA  . SER D 58  ? 0.75380 0.77590 0.55560 -0.00420 0.05820  0.06000  58  SER G CA  
3576 C C   . SER D 58  ? 0.77720 0.77170 0.55280 0.00740  0.04590  0.02200  58  SER G C   
3577 O O   . SER D 58  ? 0.80830 0.79510 0.52440 0.04330  0.05010  0.01030  58  SER G O   
3578 C CB  . SER D 58  ? 0.69260 0.75350 0.55280 -0.01700 0.08310  0.09340  58  SER G CB  
3579 O OG  . SER D 58  ? 0.71350 0.80200 0.55080 0.01300  0.10930  0.10180  58  SER G OG  
3580 N N   . PHE D 59  ? 0.71870 0.69510 0.53570 -0.01910 0.03000  0.00410  59  PHE G N   
3581 C CA  . PHE D 59  ? 0.72780 0.67310 0.53320 -0.01500 0.01490  -0.02600 59  PHE G CA  
3582 C C   . PHE D 59  ? 0.70140 0.66210 0.53570 -0.01700 0.03440  -0.02020 59  PHE G C   
3583 O O   . PHE D 59  ? 0.65280 0.62330 0.53670 -0.04060 0.03660  -0.01220 59  PHE G O   
3584 C CB  . PHE D 59  ? 0.70900 0.63090 0.54560 -0.04040 -0.01300 -0.04050 59  PHE G CB  
3585 C CG  . PHE D 59  ? 0.69020 0.57950 0.53270 -0.04390 -0.03060 -0.06210 59  PHE G CG  
3586 C CD1 . PHE D 59  ? 0.74140 0.59790 0.53370 -0.01760 -0.04230 -0.08380 59  PHE G CD1 
3587 C CD2 . PHE D 59  ? 0.62990 0.51930 0.52610 -0.06960 -0.03590 -0.05800 59  PHE G CD2 
3588 C CE1 . PHE D 59  ? 0.74070 0.55680 0.54310 -0.02310 -0.06490 -0.10200 59  PHE G CE1 
3589 C CE2 . PHE D 59  ? 0.62820 0.48830 0.53890 -0.07600 -0.05150 -0.06870 59  PHE G CE2 
3590 C CZ  . PHE D 59  ? 0.68340 0.50290 0.55080 -0.05580 -0.06870 -0.09110 59  PHE G CZ  
3591 N N   . ASN D 60  ? 0.77840 0.74000 0.57630 0.01350  0.04630  -0.02600 60  ASN G N   
3592 C CA  . ASN D 60  ? 0.75130 0.73250 0.57490 0.01770  0.06460  -0.01920 60  ASN G CA  
3593 C C   . ASN D 60  ? 0.75820 0.69410 0.57390 0.01770  0.04490  -0.04790 60  ASN G C   
3594 O O   . ASN D 60  ? 0.79880 0.69750 0.56290 0.04400  0.03060  -0.07170 60  ASN G O   
3595 C CB  . ASN D 60  ? 0.76020 0.77860 0.55580 0.05600  0.09370  -0.00210 60  ASN G CB  
3596 C CG  . ASN D 60  ? 0.73530 0.79540 0.58280 0.05440  0.11490  0.01770  60  ASN G CG  
3597 O OD1 . ASN D 60  ? 0.71270 0.75890 0.59720 0.03220  0.10310  0.00840  60  ASN G OD1 
3598 N ND2 . ASN D 60  ? 0.72770 0.84370 0.58010 0.08050  0.14660  0.04890  60  ASN G ND2 
3599 N N   . MET D 61  ? 0.81480 0.74940 0.67780 -0.00850 0.04170  -0.04480 61  MET G N   
3600 C CA  . MET D 61  ? 0.81370 0.71030 0.67930 -0.01120 0.02740  -0.06100 61  MET G CA  
3601 C C   . MET D 61  ? 0.81410 0.72400 0.68040 0.00860  0.04380  -0.05830 61  MET G C   
3602 O O   . MET D 61  ? 0.78990 0.73350 0.69400 -0.00070 0.05700  -0.04160 61  MET G O   
3603 C CB  . MET D 61  ? 0.76500 0.65910 0.67490 -0.04200 0.02020  -0.05320 61  MET G CB  
3604 C CG  . MET D 61  ? 0.74580 0.64240 0.66680 -0.05960 0.00840  -0.05000 61  MET G CG  
3605 S SD  . MET D 61  ? 0.67850 0.58330 0.64820 -0.08340 0.00760  -0.03590 61  MET G SD  
3606 C CE  . MET D 61  ? 0.64300 0.58130 0.62390 -0.08620 0.01870  -0.02340 61  MET G CE  
3607 N N   . SER D 62  ? 0.67090 0.55100 0.49460 0.03870  0.03820  -0.07660 62  SER G N   
3608 C CA  . SER D 62  ? 0.67320 0.57140 0.49380 0.06590  0.05560  -0.07360 62  SER G CA  
3609 C C   . SER D 62  ? 0.71580 0.55760 0.48290 0.09970  0.03860  -0.10160 62  SER G C   
3610 O O   . SER D 62  ? 0.75320 0.56620 0.46450 0.12480  0.02580  -0.12070 62  SER G O   
3611 C CB  . SER D 62  ? 0.67060 0.63370 0.49410 0.08690  0.08590  -0.05110 62  SER G CB  
3612 O OG  . SER D 62  ? 0.66660 0.65470 0.49250 0.11770  0.10290  -0.04620 62  SER G OG  
3613 N N   . PRO D 63  ? 0.73150 0.54930 0.50810 0.10490  0.03370  -0.10660 63  PRO G N   
3614 C CA  . PRO D 63  ? 0.69250 0.53350 0.52420 0.07840  0.04170  -0.08730 63  PRO G CA  
3615 C C   . PRO D 63  ? 0.67470 0.49230 0.53560 0.03770  0.02590  -0.08180 63  PRO G C   
3616 O O   . PRO D 63  ? 0.69120 0.46080 0.54030 0.02830  0.00210  -0.09380 63  PRO G O   
3617 C CB  . PRO D 63  ? 0.70960 0.51880 0.52700 0.10420  0.03670  -0.09690 63  PRO G CB  
3618 C CG  . PRO D 63  ? 0.76130 0.50550 0.52110 0.13130  0.01330  -0.12570 63  PRO G CG  
3619 C CD  . PRO D 63  ? 0.77590 0.54480 0.50220 0.14700  0.02120  -0.13080 63  PRO G CD  
3620 N N   . VAL D 64  ? 0.55760 0.41020 0.45790 0.01670  0.03680  -0.06280 64  VAL G N   
3621 C CA  . VAL D 64  ? 0.52580 0.36800 0.45070 -0.01240 0.02920  -0.05290 64  VAL G CA  
3622 C C   . VAL D 64  ? 0.53920 0.33620 0.46770 -0.01490 0.01780  -0.05020 64  VAL G C   
3623 O O   . VAL D 64  ? 0.55580 0.34190 0.47660 0.00240  0.02070  -0.05010 64  VAL G O   
3624 C CB  . VAL D 64  ? 0.49060 0.37390 0.44180 -0.02210 0.04060  -0.03760 64  VAL G CB  
3625 C CG1 . VAL D 64  ? 0.46180 0.33730 0.42890 -0.03780 0.03870  -0.02510 64  VAL G CG1 
3626 C CG2 . VAL D 64  ? 0.48680 0.40440 0.44470 -0.02830 0.04550  -0.03500 64  VAL G CG2 
3627 N N   . THR D 65  ? 0.63910 0.41080 0.58530 -0.03640 0.00310  -0.04460 65  THR G N   
3628 C CA  . THR D 65  ? 0.65190 0.38840 0.62120 -0.04750 -0.00630 -0.02830 65  THR G CA  
3629 C C   . THR D 65  ? 0.61330 0.38270 0.62130 -0.06780 0.00710  0.00170  65  THR G C   
3630 O O   . THR D 65  ? 0.57710 0.38480 0.58990 -0.07340 0.01620  0.00230  65  THR G O   
3631 C CB  . THR D 65  ? 0.70220 0.37890 0.67440 -0.05610 -0.04110 -0.04040 65  THR G CB  
3632 O OG1 . THR D 65  ? 0.67290 0.36110 0.67440 -0.08080 -0.05380 -0.03590 65  THR G OG1 
3633 C CG2 . THR D 65  ? 0.75140 0.39290 0.66810 -0.02460 -0.05640 -0.07640 65  THR G CG2 
3634 N N   . THR D 66  ? 0.58020 0.33410 0.61550 -0.07570 0.00890  0.02980  66  THR G N   
3635 C CA  . THR D 66  ? 0.54910 0.34050 0.62090 -0.08750 0.02660  0.06490  66  THR G CA  
3636 C C   . THR D 66  ? 0.52590 0.32990 0.63800 -0.11230 0.01340  0.06920  66  THR G C   
3637 O O   . THR D 66  ? 0.49220 0.34240 0.62520 -0.11490 0.03070  0.08840  66  THR G O   
3638 C CB  . THR D 66  ? 0.56770 0.34490 0.66610 -0.08940 0.03490  0.10450  66  THR G CB  
3639 O OG1 . THR D 66  ? 0.58590 0.32010 0.73040 -0.11540 0.00690  0.11530  66  THR G OG1 
3640 C CG2 . THR D 66  ? 0.59950 0.35590 0.65510 -0.06260 0.04170  0.09820  66  THR G CG2 
3641 N N   . ALA D 67  ? 0.56370 0.32550 0.68360 -0.12600 -0.02060 0.04950  67  ALA G N   
3642 C CA  . ALA D 67  ? 0.53760 0.31050 0.69600 -0.14830 -0.04040 0.05070  67  ALA G CA  
3643 C C   . ALA D 67  ? 0.51760 0.33030 0.64680 -0.13890 -0.02860 0.03210  67  ALA G C   
3644 O O   . ALA D 67  ? 0.48560 0.32580 0.64870 -0.15280 -0.03410 0.04150  67  ALA G O   
3645 C CB  . ALA D 67  ? 0.59070 0.29840 0.75170 -0.15890 -0.08950 0.02630  67  ALA G CB  
3646 N N   . HIS D 68  ? 0.53010 0.34960 0.60560 -0.11630 -0.01290 0.01120  68  HIS G N   
3647 C CA  . HIS D 68  ? 0.50270 0.35650 0.55830 -0.11000 -0.00290 0.00060  68  HIS G CA  
3648 C C   . HIS D 68  ? 0.47180 0.36880 0.54430 -0.10740 0.02030  0.02230  68  HIS G C   
3649 O O   . HIS D 68  ? 0.45200 0.37250 0.52060 -0.10620 0.02240  0.01800  68  HIS G O   
3650 C CB  . HIS D 68  ? 0.52150 0.37350 0.53040 -0.08960 0.00460  -0.02060 68  HIS G CB  
3651 C CG  . HIS D 68  ? 0.57000 0.38930 0.54590 -0.07960 -0.01400 -0.04490 68  HIS G CG  
3652 N ND1 . HIS D 68  ? 0.60720 0.40850 0.55020 -0.05700 -0.01090 -0.05820 68  HIS G ND1 
3653 C CD2 . HIS D 68  ? 0.59500 0.39510 0.55900 -0.08220 -0.03770 -0.05950 68  HIS G CD2 
3654 C CE1 . HIS D 68  ? 0.65310 0.42450 0.55920 -0.04200 -0.02940 -0.08050 68  HIS G CE1 
3655 N NE2 . HIS D 68  ? 0.64940 0.41650 0.56460 -0.05710 -0.04810 -0.08310 68  HIS G NE2 
3656 N N   . ALA D 69  ? 0.46690 0.37120 0.55070 -0.10080 0.03680  0.04530  69  ALA G N   
3657 C CA  . ALA D 69  ? 0.45550 0.39630 0.53770 -0.08550 0.05830  0.06220  69  ALA G CA  
3658 C C   . ALA D 69  ? 0.43850 0.41120 0.56310 -0.09580 0.06020  0.08180  69  ALA G C   
3659 O O   . ALA D 69  ? 0.42610 0.39890 0.60080 -0.11690 0.05090  0.10070  69  ALA G O   
3660 C CB  . ALA D 69  ? 0.48190 0.42400 0.55800 -0.06870 0.07710  0.08630  69  ALA G CB  
3661 N N   . GLY D 70  ? 0.44240 0.44050 0.55200 -0.08070 0.06780  0.07770  70  GLY G N   
3662 C CA  . GLY D 70  ? 0.42610 0.46070 0.57570 -0.08430 0.07130  0.09650  70  GLY G CA  
3663 C C   . GLY D 70  ? 0.44380 0.48900 0.56380 -0.06640 0.07020  0.07960  70  GLY G C   
3664 O O   . GLY D 70  ? 0.46310 0.48590 0.53810 -0.05500 0.06430  0.05580  70  GLY G O   
3665 N N   . ASN D 71  ? 0.38280 0.46320 0.53690 -0.06460 0.07340  0.09560  71  ASN G N   
3666 C CA  . ASN D 71  ? 0.41660 0.50840 0.54730 -0.04160 0.07330  0.08540  71  ASN G CA  
3667 C C   . ASN D 71  ? 0.39230 0.48380 0.54670 -0.06390 0.05040  0.07550  71  ASN G C   
3668 O O   . ASN D 71  ? 0.37010 0.49210 0.58010 -0.07740 0.04660  0.09520  71  ASN G O   
3669 C CB  . ASN D 71  ? 0.43270 0.57140 0.57620 -0.00830 0.10050  0.11540  71  ASN G CB  
3670 C CG  . ASN D 71  ? 0.47510 0.62010 0.58880 0.02410  0.09810  0.10290  71  ASN G CG  
3671 O OD1 . ASN D 71  ? 0.50330 0.61840 0.59790 0.01500  0.07410  0.07620  71  ASN G OD1 
3672 N ND2 . ASN D 71  ? 0.48190 0.66640 0.59030 0.06650  0.12430  0.12570  71  ASN G ND2 
3673 N N   . TYR D 72  ? 0.51110 0.57010 0.62750 -0.06740 0.03370  0.04880  72  TYR G N   
3674 C CA  . TYR D 72  ? 0.49110 0.54030 0.61310 -0.08630 0.01160  0.03780  72  TYR G CA  
3675 C C   . TYR D 72  ? 0.51880 0.57400 0.63130 -0.07300 0.00410  0.03430  72  TYR G C   
3676 O O   . TYR D 72  ? 0.56700 0.61310 0.65230 -0.05150 0.00880  0.02930  72  TYR G O   
3677 C CB  . TYR D 72  ? 0.47020 0.48370 0.55630 -0.09660 0.00280  0.01850  72  TYR G CB  
3678 C CG  . TYR D 72  ? 0.45650 0.45480 0.54660 -0.10800 0.00280  0.01660  72  TYR G CG  
3679 C CD1 . TYR D 72  ? 0.46450 0.45750 0.54600 -0.10050 0.01820  0.02000  72  TYR G CD1 
3680 C CD2 . TYR D 72  ? 0.46370 0.44550 0.55900 -0.12200 -0.01770 0.00840  72  TYR G CD2 
3681 C CE1 . TYR D 72  ? 0.46560 0.43920 0.54970 -0.10870 0.01640  0.01880  72  TYR G CE1 
3682 C CE2 . TYR D 72  ? 0.48410 0.44050 0.57870 -0.12870 -0.02370 0.00320  72  TYR G CE2 
3683 C CZ  . TYR D 72  ? 0.47720 0.43050 0.56830 -0.12280 -0.00490 0.00990  72  TYR G CZ  
3684 O OH  . TYR D 72  ? 0.49270 0.41600 0.58140 -0.12690 -0.01250 0.00500  72  TYR G OH  
3685 N N   . THR D 73  ? 0.47670 0.54020 0.60920 -0.08430 -0.01350 0.03500  73  THR G N   
3686 C CA  . THR D 73  ? 0.50310 0.56080 0.61860 -0.07550 -0.02640 0.02960  73  THR G CA  
3687 C C   . THR D 73  ? 0.48290 0.52380 0.58650 -0.09170 -0.04840 0.02060  73  THR G C   
3688 O O   . THR D 73  ? 0.46990 0.50930 0.58930 -0.10650 -0.06010 0.01770  73  THR G O   
3689 C CB  . THR D 73  ? 0.53350 0.62910 0.68280 -0.05790 -0.02490 0.04380  73  THR G CB  
3690 O OG1 . THR D 73  ? 0.49950 0.63180 0.70870 -0.07310 -0.03020 0.05970  73  THR G OG1 
3691 C CG2 . THR D 73  ? 0.58260 0.69000 0.72160 -0.02670 -0.00270 0.04980  73  THR G CG2 
3692 N N   . CYS D 74  ? 0.46600 0.48940 0.53770 -0.08550 -0.05680 0.01690  74  CYS G N   
3693 C CA  . CYS D 74  ? 0.48210 0.49170 0.52920 -0.09040 -0.07570 0.01150  74  CYS G CA  
3694 C C   . CYS D 74  ? 0.51320 0.53080 0.56370 -0.08050 -0.09240 0.01730  74  CYS G C   
3695 O O   . CYS D 74  ? 0.52650 0.55130 0.58800 -0.06790 -0.08730 0.02450  74  CYS G O   
3696 C CB  . CYS D 74  ? 0.50880 0.49360 0.50960 -0.08950 -0.06680 0.01040  74  CYS G CB  
3697 S SG  . CYS D 74  ? 0.53370 0.50530 0.52090 -0.08260 -0.06150 0.02580  74  CYS G SG  
3698 N N   . ARG D 75  ? 0.53930 0.55060 0.57360 -0.08150 -0.11590 0.01160  75  ARG G N   
3699 C CA  . ARG D 75  ? 0.57160 0.58530 0.59780 -0.07020 -0.13640 0.01620  75  ARG G CA  
3700 C C   . ARG D 75  ? 0.62050 0.60610 0.58200 -0.06230 -0.14550 0.01280  75  ARG G C   
3701 O O   . ARG D 75  ? 0.63510 0.60700 0.57070 -0.06330 -0.15390 -0.00120 75  ARG G O   
3702 C CB  . ARG D 75  ? 0.55320 0.59620 0.63160 -0.07390 -0.16370 0.01490  75  ARG G CB  
3703 C CG  . ARG D 75  ? 0.52200 0.60750 0.66890 -0.07480 -0.14840 0.02820  75  ARG G CG  
3704 C CD  . ARG D 75  ? 0.50450 0.63060 0.72070 -0.08080 -0.17530 0.03620  75  ARG G CD  
3705 N NE  . ARG D 75  ? 0.48790 0.66740 0.77350 -0.07670 -0.15210 0.05830  75  ARG G NE  
3706 C CZ  . ARG D 75  ? 0.49580 0.71290 0.80750 -0.05280 -0.14300 0.07300  75  ARG G CZ  
3707 N NH1 . ARG D 75  ? 0.51560 0.71920 0.79660 -0.03530 -0.15970 0.06740  75  ARG G NH1 
3708 N NH2 . ARG D 75  ? 0.48310 0.75320 0.85010 -0.04150 -0.11530 0.09610  75  ARG G NH2 
3709 N N   . GLY D 76  ? 0.61920 0.59430 0.55130 -0.05020 -0.14290 0.02770  76  GLY G N   
3710 C CA  . GLY D 76  ? 0.67680 0.63310 0.54490 -0.03610 -0.14560 0.03410  76  GLY G CA  
3711 C C   . GLY D 76  ? 0.69980 0.65370 0.54590 -0.02040 -0.18030 0.02890  76  GLY G C   
3712 O O   . GLY D 76  ? 0.67910 0.64770 0.56500 -0.02050 -0.19800 0.02980  76  GLY G O   
3713 N N   . SER D 77  ? 0.81410 0.75020 0.59210 -0.00130 -0.19090 0.02330  77  SER G N   
3714 C CA  . SER D 77  ? 0.84900 0.77590 0.59140 0.01950  -0.23030 0.01500  77  SER G CA  
3715 C C   . SER D 77  ? 0.86600 0.79490 0.60270 0.03050  -0.22840 0.04230  77  SER G C   
3716 O O   . SER D 77  ? 0.89650 0.81740 0.60220 0.03740  -0.19930 0.07160  77  SER G O   
3717 C CB  . SER D 77  ? 0.90720 0.80830 0.55670 0.04910  -0.23840 0.00360  77  SER G CB  
3718 O OG  . SER D 77  ? 0.95100 0.83750 0.54760 0.07720  -0.27650 -0.00190 77  SER G OG  
3719 N N   . HIS D 78  ? 1.02310 0.96440 0.79800 0.03140  -0.26050 0.03630  78  HIS G N   
3720 C CA  . HIS D 78  ? 1.04180 0.98060 0.81040 0.04640  -0.26650 0.05880  78  HIS G CA  
3721 C C   . HIS D 78  ? 1.07200 1.00890 0.81330 0.06790  -0.31530 0.04560  78  HIS G C   
3722 O O   . HIS D 78  ? 1.03640 0.99840 0.84080 0.06040  -0.34740 0.03060  78  HIS G O   
3723 C CB  . HIS D 78  ? 0.99380 0.95220 0.83800 0.03430  -0.25770 0.06550  78  HIS G CB  
3724 C CG  . HIS D 78  ? 1.02290 0.96720 0.85670 0.05170  -0.26190 0.08870  78  HIS G CG  
3725 N ND1 . HIS D 78  ? 0.99960 0.95760 0.88700 0.05650  -0.26650 0.09050  78  HIS G ND1 
3726 C CD2 . HIS D 78  ? 1.08450 1.00040 0.85860 0.06910  -0.26200 0.11370  78  HIS G CD2 
3727 C CE1 . HIS D 78  ? 1.04310 0.97460 0.90390 0.07480  -0.27390 0.11140  78  HIS G CE1 
3728 N NE2 . HIS D 78  ? 1.08710 0.99320 0.88250 0.08000  -0.27080 0.12850  78  HIS G NE2 
3729 N N   . PRO D 79  ? 1.20300 1.11420 0.85350 0.09740  -0.32280 0.05390  79  PRO G N   
3730 C CA  . PRO D 79  ? 1.23890 1.13900 0.84550 0.12230  -0.37730 0.03060  79  PRO G CA  
3731 C C   . PRO D 79  ? 1.23400 1.15030 0.88190 0.12930  -0.41610 0.03290  79  PRO G C   
3732 O O   . PRO D 79  ? 1.24250 1.16190 0.90060 0.13590  -0.47040 0.00720  79  PRO G O   
3733 C CB  . PRO D 79  ? 1.30490 1.17530 0.79080 0.16120  -0.36380 0.04680  79  PRO G CB  
3734 C CG  . PRO D 79  ? 1.30150 1.17560 0.78570 0.14720  -0.30330 0.06960  79  PRO G CG  
3735 C CD  . PRO D 79  ? 1.24520 1.13900 0.82780 0.11060  -0.28150 0.08380  79  PRO G CD  
3736 N N   . HIS D 80  ? 1.39070 1.31490 1.06540 0.12970  -0.39510 0.06200  80  HIS G N   
3737 C CA  . HIS D 80  ? 1.38460 1.32640 1.09730 0.14260  -0.43110 0.06490  80  HIS G CA  
3738 C C   . HIS D 80  ? 1.33060 1.30950 1.14800 0.12110  -0.41320 0.06880  80  HIS G C   
3739 O O   . HIS D 80  ? 1.32520 1.29300 1.14860 0.12210  -0.38130 0.09030  80  HIS G O   
3740 C CB  . HIS D 80  ? 1.44560 1.35800 1.08530 0.17450  -0.43000 0.09540  80  HIS G CB  
3741 C CG  . HIS D 80  ? 1.50690 1.39610 1.04930 0.20320  -0.44480 0.09040  80  HIS G CG  
3742 N ND1 . HIS D 80  ? 1.53040 1.40040 1.00160 0.20930  -0.42090 0.08820  80  HIS G ND1 
3743 C CD2 . HIS D 80  ? 1.55490 1.44200 1.06650 0.22730  -0.47220 0.08490  80  HIS G CD2 
3744 C CE1 . HIS D 80  ? 1.59750 1.45380 0.99610 0.23890  -0.43190 0.08130  80  HIS G CE1 
3745 N NE2 . HIS D 80  ? 1.61490 1.47810 1.03440 0.24910  -0.46500 0.07860  80  HIS G NE2 
3746 N N   . SER D 81  ? 1.18950 1.21040 1.08800 0.10480  -0.43640 0.04960  81  SER G N   
3747 C CA  . SER D 81  ? 1.13850 1.20400 1.13340 0.08740  -0.41210 0.05410  81  SER G CA  
3748 C C   . SER D 81  ? 1.08900 1.20680 1.17550 0.07160  -0.44820 0.04180  81  SER G C   
3749 O O   . SER D 81  ? 1.09810 1.20170 1.16750 0.06520  -0.48970 0.02250  81  SER G O   
3750 C CB  . SER D 81  ? 1.12160 1.17200 1.10890 0.06640  -0.36290 0.05460  81  SER G CB  
3751 O OG  . SER D 81  ? 1.12280 1.16160 1.09130 0.04830  -0.36870 0.03620  81  SER G OG  
3752 N N   . PRO D 82  ? 1.02250 1.20050 1.20820 0.06770  -0.43490 0.05500  82  PRO G N   
3753 C CA  . PRO D 82  ? 0.98170 1.22200 1.27650 0.05070  -0.46970 0.05560  82  PRO G CA  
3754 C C   . PRO D 82  ? 0.95110 1.18890 1.27680 0.01480  -0.47110 0.04430  82  PRO G C   
3755 O O   . PRO D 82  ? 0.92630 1.18250 1.30950 -0.00400 -0.49890 0.03850  82  PRO G O   
3756 C CB  . PRO D 82  ? 0.94330 1.25410 1.32740 0.06400  -0.43850 0.08140  82  PRO G CB  
3757 C CG  . PRO D 82  ? 0.97700 1.24700 1.28390 0.09430  -0.40360 0.08570  82  PRO G CG  
3758 C CD  . PRO D 82  ? 1.01890 1.21190 1.22280 0.08260  -0.38980 0.07180  82  PRO G CD  
3759 N N   . THR D 83  ? 0.85760 1.06340 1.13730 0.00440  -0.42520 0.04060  83  THR G N   
3760 C CA  . THR D 83  ? 0.84570 1.03800 1.14080 -0.02570 -0.42810 0.02820  83  THR G CA  
3761 C C   . THR D 83  ? 0.89700 1.01520 1.08090 -0.02170 -0.44470 0.00070  83  THR G C   
3762 O O   . THR D 83  ? 0.87940 0.97570 1.06830 -0.03990 -0.47000 -0.01750 83  THR G O   
3763 C CB  . THR D 83  ? 0.81520 1.02480 1.13540 -0.03710 -0.36840 0.04180  83  THR G CB  
3764 O OG1 . THR D 83  ? 0.84700 1.02140 1.08630 -0.01740 -0.32800 0.04260  83  THR G OG1 
3765 C CG2 . THR D 83  ? 0.76530 1.05710 1.20220 -0.03830 -0.35190 0.07130  83  THR G CG2 
3766 N N   . GLY D 84  ? 0.95860 1.03840 1.04380 0.00510  -0.43200 0.00040  84  GLY G N   
3767 C CA  . GLY D 84  ? 1.01610 1.03750 0.99190 0.01600  -0.42580 -0.01450 84  GLY G CA  
3768 C C   . GLY D 84  ? 1.01060 1.01960 0.96330 0.00580  -0.36740 -0.00660 84  GLY G C   
3769 O O   . GLY D 84  ? 1.04770 1.01860 0.91780 0.01630  -0.35420 -0.01300 84  GLY G O   
3770 N N   . TRP D 85  ? 0.83770 0.88030 0.85920 -0.00980 -0.33280 0.00800  85  TRP G N   
3771 C CA  . TRP D 85  ? 0.82270 0.85500 0.83280 -0.02100 -0.28570 0.01230  85  TRP G CA  
3772 C C   . TRP D 85  ? 0.80820 0.85940 0.84960 -0.01580 -0.25350 0.03100  85  TRP G C   
3773 O O   . TRP D 85  ? 0.79180 0.87490 0.88020 -0.00520 -0.26350 0.03990  85  TRP G O   
3774 C CB  . TRP D 85  ? 0.78730 0.82970 0.84420 -0.04540 -0.28560 0.00090  85  TRP G CB  
3775 C CG  . TRP D 85  ? 0.81920 0.82500 0.83050 -0.04530 -0.32110 -0.02350 85  TRP G CG  
3776 C CD1 . TRP D 85  ? 0.83330 0.83330 0.85810 -0.04430 -0.37840 -0.03940 85  TRP G CD1 
3777 C CD2 . TRP D 85  ? 0.85140 0.81750 0.79140 -0.04030 -0.30590 -0.03690 85  TRP G CD2 
3778 N NE1 . TRP D 85  ? 0.86450 0.81440 0.82050 -0.03560 -0.40330 -0.06650 85  TRP G NE1 
3779 C CE2 . TRP D 85  ? 0.88580 0.81780 0.78830 -0.03100 -0.35570 -0.06420 85  TRP G CE2 
3780 C CE3 . TRP D 85  ? 0.85050 0.80760 0.75730 -0.04000 -0.25830 -0.02870 85  TRP G CE3 
3781 C CZ2 . TRP D 85  ? 0.92670 0.81550 0.75060 -0.01530 -0.35460 -0.08420 85  TRP G CZ2 
3782 C CZ3 . TRP D 85  ? 0.89020 0.81470 0.73200 -0.02920 -0.25450 -0.04370 85  TRP G CZ3 
3783 C CH2 . TRP D 85  ? 0.93510 0.82560 0.73140 -0.01390 -0.30010 -0.07160 85  TRP G CH2 
3784 N N   . SER D 86  ? 0.56050 0.58990 0.57390 -0.01960 -0.21820 0.03570  86  SER G N   
3785 C CA  . SER D 86  ? 0.55250 0.58010 0.57760 -0.01060 -0.19530 0.04750  86  SER G CA  
3786 C C   . SER D 86  ? 0.51530 0.58240 0.60400 -0.01190 -0.18060 0.04690  86  SER G C   
3787 O O   . SER D 86  ? 0.48570 0.58130 0.61550 -0.02740 -0.18190 0.04310  86  SER G O   
3788 C CB  . SER D 86  ? 0.56560 0.55630 0.54920 -0.01720 -0.17060 0.05290  86  SER G CB  
3789 O OG  . SER D 86  ? 0.53770 0.53640 0.53770 -0.03320 -0.15120 0.04350  86  SER G OG  
3790 N N   . ALA D 87  ? 0.55640 0.62120 0.64960 0.00760  -0.16690 0.05260  87  ALA G N   
3791 C CA  . ALA D 87  ? 0.55060 0.64700 0.68230 0.01580  -0.14400 0.05380  87  ALA G CA  
3792 C C   . ALA D 87  ? 0.54460 0.62580 0.66340 -0.00460 -0.12360 0.04700  87  ALA G C   
3793 O O   . ALA D 87  ? 0.53380 0.57780 0.61280 -0.02080 -0.12440 0.04160  87  ALA G O   
3794 C CB  . ALA D 87  ? 0.58120 0.66150 0.69710 0.05030  -0.13750 0.05440  87  ALA G CB  
3795 N N   . ALA D 88  ? 0.52450 0.64020 0.67900 -0.00000 -0.10290 0.05140  88  ALA G N   
3796 C CA  . ALA D 88  ? 0.51530 0.61860 0.65900 -0.01450 -0.08370 0.04630  88  ALA G CA  
3797 C C   . ALA D 88  ? 0.54780 0.60310 0.64190 -0.00330 -0.07690 0.03640  88  ALA G C   
3798 O O   . ALA D 88  ? 0.57640 0.61650 0.65460 0.02470  -0.08060 0.03430  88  ALA G O   
3799 C CB  . ALA D 88  ? 0.50190 0.65650 0.69570 -0.00780 -0.06170 0.06050  88  ALA G CB  
3800 N N   . SER D 89  ? 0.51450 0.54410 0.58740 -0.02390 -0.07130 0.03010  89  SER G N   
3801 C CA  . SER D 89  ? 0.52650 0.51450 0.56790 -0.02100 -0.07010 0.02340  89  SER G CA  
3802 C C   . SER D 89  ? 0.55300 0.54390 0.59110 0.00170  -0.05720 0.01690  89  SER G C   
3803 O O   . SER D 89  ? 0.56800 0.60000 0.62890 0.01300  -0.04030 0.02340  89  SER G O   
3804 C CB  . SER D 89  ? 0.47970 0.45330 0.50910 -0.04730 -0.06550 0.02290  89  SER G CB  
3805 O OG  . SER D 89  ? 0.44670 0.44110 0.48960 -0.05580 -0.05060 0.01920  89  SER G OG  
3806 N N   . ASN D 90  ? 0.54950 0.49620 0.56020 0.00960  -0.06760 0.00690  90  ASN G N   
3807 C CA  . ASN D 90  ? 0.56210 0.50120 0.55520 0.03100  -0.06020 -0.00370 90  ASN G CA  
3808 C C   . ASN D 90  ? 0.54210 0.51220 0.55070 0.01290  -0.03720 0.00190  90  ASN G C   
3809 O O   . ASN D 90  ? 0.49760 0.47030 0.51890 -0.01900 -0.03590 0.00600  90  ASN G O   
3810 C CB  . ASN D 90  ? 0.55260 0.43340 0.52290 0.03010  -0.08540 -0.01650 90  ASN G CB  
3811 C CG  . ASN D 90  ? 0.50870 0.38290 0.49760 -0.01060 -0.08800 -0.00650 90  ASN G CG  
3812 O OD1 . ASN D 90  ? 0.49300 0.38070 0.49430 -0.02950 -0.08490 0.00730  90  ASN G OD1 
3813 N ND2 . ASN D 90  ? 0.47990 0.33830 0.46910 -0.02020 -0.09240 -0.01150 90  ASN G ND2 
3814 N N   . PRO D 91  ? 0.56100 0.55180 0.56400 0.03680  -0.01900 0.00350  91  PRO G N   
3815 C CA  . PRO D 91  ? 0.54130 0.55640 0.56140 0.01980  0.00130  0.01280  91  PRO G CA  
3816 C C   . PRO D 91  ? 0.52090 0.50210 0.51620 0.01290  -0.00450 -0.00010 91  PRO G C   
3817 O O   . PRO D 91  ? 0.52760 0.47620 0.48950 0.03640  -0.01870 -0.01460 91  PRO G O   
3818 C CB  . PRO D 91  ? 0.54230 0.59830 0.56800 0.05400  0.02610  0.02860  91  PRO G CB  
3819 C CG  . PRO D 91  ? 0.56290 0.59390 0.54250 0.10080  0.01560  0.01360  91  PRO G CG  
3820 C CD  . PRO D 91  ? 0.57560 0.57310 0.55500 0.08660  -0.01350 0.00140  91  PRO G CD  
3821 N N   . VAL D 92  ? 0.41120 0.53220 0.48160 -0.01680 -0.10740 0.15730  92  VAL G N   
3822 C CA  . VAL D 92  ? 0.39960 0.49240 0.44940 -0.02400 -0.08830 0.14570  92  VAL G CA  
3823 C C   . VAL D 92  ? 0.38420 0.49040 0.42730 -0.03310 -0.07070 0.12850  92  VAL G C   
3824 O O   . VAL D 92  ? 0.39390 0.51830 0.42310 -0.05050 -0.07180 0.12870  92  VAL G O   
3825 C CB  . VAL D 92  ? 0.41970 0.49320 0.43500 -0.04460 -0.08980 0.15550  92  VAL G CB  
3826 C CG1 . VAL D 92  ? 0.40630 0.46210 0.40430 -0.05040 -0.06930 0.14020  92  VAL G CG1 
3827 C CG2 . VAL D 92  ? 0.44790 0.49930 0.46410 -0.03950 -0.10870 0.17520  92  VAL G CG2 
3828 N N   . VAL D 93  ? 0.43890 0.53250 0.48850 -0.02340 -0.05620 0.11440  93  VAL G N   
3829 C CA  . VAL D 93  ? 0.43090 0.53070 0.47480 -0.03030 -0.04220 0.09990  93  VAL G CA  
3830 C C   . VAL D 93  ? 0.43750 0.50870 0.45400 -0.03890 -0.02970 0.09150  93  VAL G C   
3831 O O   . VAL D 93  ? 0.43220 0.48430 0.45060 -0.02930 -0.02330 0.08770  93  VAL G O   
3832 C CB  . VAL D 93  ? 0.40530 0.51600 0.47560 -0.01400 -0.03630 0.09060  93  VAL G CB  
3833 C CG1 . VAL D 93  ? 0.39990 0.51100 0.45840 -0.02480 -0.02360 0.07890  93  VAL G CG1 
3834 C CG2 . VAL D 93  ? 0.39040 0.53860 0.49240 -0.00220 -0.04830 0.09510  93  VAL G CG2 
3835 N N   . ILE D 94  ? 0.41280 0.48210 0.40410 -0.05650 -0.02670 0.08720  94  ILE G N   
3836 C CA  . ILE D 94  ? 0.41880 0.46400 0.38680 -0.06090 -0.01520 0.07520  94  ILE G CA  
3837 C C   . ILE D 94  ? 0.41150 0.44490 0.37980 -0.05740 -0.00680 0.06370  94  ILE G C   
3838 O O   . ILE D 94  ? 0.41320 0.45320 0.37640 -0.06820 -0.00870 0.06210  94  ILE G O   
3839 C CB  . ILE D 94  ? 0.43790 0.48280 0.37670 -0.07980 -0.01620 0.07240  94  ILE G CB  
3840 C CG1 . ILE D 94  ? 0.44760 0.50700 0.38260 -0.08770 -0.02660 0.08700  94  ILE G CG1 
3841 C CG2 . ILE D 94  ? 0.45830 0.48120 0.37700 -0.07920 -0.00410 0.05590  94  ILE G CG2 
3842 C CD1 . ILE D 94  ? 0.45020 0.50030 0.38580 -0.08140 -0.02390 0.09060  94  ILE G CD1 
3843 N N   . MET D 95  ? 0.54110 0.55800 0.51350 -0.04480 0.00120  0.05710  95  MET G N   
3844 C CA  . MET D 95  ? 0.53710 0.53960 0.50730 -0.04160 0.00730  0.04850  95  MET G CA  
3845 C C   . MET D 95  ? 0.55790 0.53410 0.50640 -0.04070 0.01320  0.03700  95  MET G C   
3846 O O   . MET D 95  ? 0.55990 0.53410 0.50960 -0.03240 0.01740  0.03370  95  MET G O   
3847 C CB  . MET D 95  ? 0.50850 0.51530 0.50110 -0.02690 0.01040  0.04930  95  MET G CB  
3848 C CG  . MET D 95  ? 0.50150 0.53450 0.51920 -0.02170 0.00460  0.05690  95  MET G CG  
3849 S SD  . MET D 95  ? 0.47980 0.51480 0.51950 -0.00530 0.01000  0.05200  95  MET G SD  
3850 C CE  . MET D 95  ? 0.46930 0.53460 0.53980 0.00520  0.00130  0.05700  95  MET G CE  
3851 N N   . VAL D 96  ? 0.45230 0.40900 0.38080 -0.04960 0.01250  0.03010  96  VAL G N   
3852 C CA  . VAL D 96  ? 0.47890 0.40730 0.38660 -0.04570 0.01580  0.01640  96  VAL G CA  
3853 C C   . VAL D 96  ? 0.47340 0.37830 0.38160 -0.03530 0.01680  0.01290  96  VAL G C   
3854 O O   . VAL D 96  ? 0.46750 0.36410 0.37200 -0.04390 0.01290  0.01810  96  VAL G O   
3855 C CB  . VAL D 96  ? 0.51210 0.42510 0.39270 -0.06230 0.01180  0.00980  96  VAL G CB  
3856 C CG1 . VAL D 96  ? 0.53530 0.41250 0.39470 -0.05410 0.01400  -0.00810 96  VAL G CG1 
3857 C CG2 . VAL D 96  ? 0.51730 0.45710 0.39580 -0.07340 0.01010  0.01410  96  VAL G CG2 
3858 N N   . THR D 97  ? 0.47370 0.37180 0.38610 -0.01870 0.02140  0.00500  97  THR G N   
3859 C CA  . THR D 97  ? 0.45580 0.33550 0.37080 -0.00710 0.02060  0.00370  97  THR G CA  
3860 C C   . THR D 97  ? 0.47650 0.31830 0.37030 -0.00000 0.01670  -0.00900 97  THR G C   
3861 O O   . THR D 97  ? 0.49590 0.32930 0.37550 -0.00070 0.01740  -0.02090 97  THR G O   
3862 C CB  . THR D 97  ? 0.42460 0.32430 0.36070 0.00770  0.02620  0.00390  97  THR G CB  
3863 O OG1 . THR D 97  ? 0.42060 0.32420 0.35430 0.01800  0.03040  -0.00850 97  THR G OG1 
3864 C CG2 . THR D 97  ? 0.40980 0.33980 0.36490 0.00270  0.02840  0.01440  97  THR G CG2 
3865 N N   . GLY D 98  ? 0.54560 0.36400 0.43680 0.00790  0.01180  -0.00730 98  GLY G N   
3866 C CA  . GLY D 98  ? 0.56420 0.33950 0.43630 0.01880  0.00430  -0.01790 98  GLY G CA  
3867 C C   . GLY D 98  ? 0.59990 0.33090 0.44300 0.00170  -0.00670 -0.01360 98  GLY G C   
3868 O O   . GLY D 98  ? 0.63020 0.31780 0.45180 0.00840  -0.01420 -0.02520 98  GLY G O   
3869 N N   . ASN D 99  ? 0.57900 0.31930 0.41960 -0.02050 -0.00850 0.00160  99  ASN G N   
3870 C CA  . ASN D 99  ? 0.61360 0.31650 0.42330 -0.04370 -0.01880 0.00660  99  ASN G CA  
3871 C C   . ASN D 99  ? 0.61710 0.29750 0.41460 -0.05380 -0.02780 0.02040  99  ASN G C   
3872 O O   . ASN D 99  ? 0.64310 0.29150 0.41150 -0.07780 -0.03760 0.02710  99  ASN G O   
3873 C CB  . ASN D 99  ? 0.61250 0.34760 0.42320 -0.06830 -0.01510 0.01210  99  ASN G CB  
3874 C CG  . ASN D 99  ? 0.60930 0.37090 0.43090 -0.06140 -0.00740 0.00210  99  ASN G CG  
3875 O OD1 . ASN D 99  ? 0.63280 0.36850 0.43570 -0.05910 -0.00930 -0.01140 99  ASN G OD1 
3876 N ND2 . ASN D 99  ? 0.58380 0.39540 0.43380 -0.05830 0.00040  0.00840  99  ASN G ND2 
3877 N N   . HIS D 100 ? 0.61100 0.30770 0.42670 -0.03970 -0.02550 0.02540  100 HIS G N   
3878 C CA  . HIS D 100 ? 0.62390 0.29740 0.42420 -0.04910 -0.03550 0.03840  100 HIS G CA  
3879 C C   . HIS D 100 ? 0.61140 0.28290 0.42650 -0.02130 -0.03690 0.03590  100 HIS G C   
3880 O O   . HIS D 100 ? 0.58750 0.28500 0.42710 0.00110  -0.02790 0.02490  100 HIS G O   
3881 C CB  . HIS D 100 ? 0.60900 0.32640 0.41750 -0.07300 -0.02930 0.05100  100 HIS G CB  
3882 C CG  . HIS D 100 ? 0.60870 0.35380 0.41780 -0.09500 -0.02420 0.05140  100 HIS G CG  
3883 N ND1 . HIS D 100 ? 0.63260 0.35160 0.41050 -0.12390 -0.03320 0.05700  100 HIS G ND1 
3884 C CD2 . HIS D 100 ? 0.57860 0.37540 0.41540 -0.09270 -0.01290 0.04760  100 HIS G CD2 
3885 C CE1 . HIS D 100 ? 0.61770 0.37720 0.40620 -0.13840 -0.02670 0.05600  100 HIS G CE1 
3886 N NE2 . HIS D 100 ? 0.59100 0.39690 0.41570 -0.11830 -0.01510 0.05060  100 HIS G NE2 
3887 N N   . ARG D 101 ? 0.72080 0.36450 0.51950 -0.02540 -0.04900 0.04750  101 ARG G N   
3888 C CA  . ARG D 101 ? 0.71020 0.35980 0.52400 -0.00180 -0.05150 0.04760  101 ARG G CA  
3889 C C   . ARG D 101 ? 0.67150 0.38480 0.51830 0.00090  -0.03510 0.04690  101 ARG G C   
3890 O O   . ARG D 101 ? 0.66060 0.40710 0.51360 -0.01840 -0.02590 0.05130  101 ARG G O   
3891 C CB  . ARG D 101 ? 0.74090 0.35160 0.52820 -0.01190 -0.06920 0.06400  101 ARG G CB  
3892 C CG  . ARG D 101 ? 0.79640 0.33320 0.54720 -0.01510 -0.08910 0.06640  101 ARG G CG  
3893 C CD  . ARG D 101 ? 0.81190 0.30990 0.56580 0.02290  -0.10160 0.05470  101 ARG G CD  
3894 N NE  . ARG D 101 ? 0.83760 0.31550 0.58570 0.03330  -0.11830 0.06770  101 ARG G NE  
3895 C CZ  . ARG D 101 ? 0.89000 0.30270 0.60110 0.02290  -0.14260 0.08340  101 ARG G CZ  
3896 N NH1 . ARG D 101 ? 0.93160 0.29610 0.60910 -0.00000 -0.15180 0.08660  101 ARG G NH1 
3897 N NH2 . ARG D 101 ? 0.90110 0.30320 0.61030 0.03390  -0.15810 0.09610  101 ARG G NH2 
3898 N N   . LYS D 102 ? 0.56240 0.29300 0.43050 0.02530  -0.03220 0.04010  102 LYS G N   
3899 C CA  . LYS D 102 ? 0.52620 0.31000 0.42280 0.02720  -0.01760 0.03780  102 LYS G CA  
3900 C C   . LYS D 102 ? 0.53150 0.33190 0.42630 0.01300  -0.01780 0.04890  102 LYS G C   
3901 O O   . LYS D 102 ? 0.55390 0.32870 0.42970 0.00860  -0.03040 0.05870  102 LYS G O   
3902 C CB  . LYS D 102 ? 0.50280 0.30540 0.42130 0.05250  -0.01390 0.02730  102 LYS G CB  
3903 C CG  . LYS D 102 ? 0.52000 0.30820 0.43620 0.06820  -0.02620 0.03010  102 LYS G CG  
3904 C CD  . LYS D 102 ? 0.48690 0.31050 0.42970 0.08920  -0.01950 0.01900  102 LYS G CD  
3905 C CE  . LYS D 102 ? 0.50460 0.30990 0.44760 0.11450  -0.03230 0.01280  102 LYS G CE  
3906 N NZ  . LYS D 102 ? 0.52180 0.31730 0.45900 0.11720  -0.04640 0.02520  102 LYS G NZ  
3907 N N   . PRO D 103 ? 0.48440 0.32640 0.39780 0.00580  -0.00490 0.04700  103 PRO G N   
3908 C CA  . PRO D 103 ? 0.48790 0.35320 0.40340 -0.00420 -0.00240 0.05220  103 PRO G CA  
3909 C C   . PRO D 103 ? 0.47590 0.35520 0.40690 0.01290  -0.00150 0.04820  103 PRO G C   
3910 O O   . PRO D 103 ? 0.46070 0.33510 0.40140 0.03160  -0.00290 0.04210  103 PRO G O   
3911 C CB  . PRO D 103 ? 0.46830 0.37010 0.39970 -0.01420 0.01060  0.04730  103 PRO G CB  
3912 C CG  . PRO D 103 ? 0.44860 0.35310 0.39570 -0.00120 0.01560  0.03960  103 PRO G CG  
3913 C CD  . PRO D 103 ? 0.46410 0.33130 0.39570 0.00660  0.00660  0.03950  103 PRO G CD  
3914 N N   . SER D 104 ? 0.48820 0.38950 0.42080 0.00460  0.00110  0.05060  104 SER G N   
3915 C CA  . SER D 104 ? 0.48580 0.40500 0.43180 0.01600  0.00210  0.04700  104 SER G CA  
3916 C C   . SER D 104 ? 0.47180 0.42480 0.43710 0.01280  0.01610  0.03760  104 SER G C   
3917 O O   . SER D 104 ? 0.46500 0.43130 0.43070 0.00060  0.02310  0.03540  104 SER G O   
3918 C CB  . SER D 104 ? 0.50960 0.42270 0.43830 0.00880  -0.00920 0.05730  104 SER G CB  
3919 O OG  . SER D 104 ? 0.52720 0.40140 0.43860 0.01620  -0.02570 0.06620  104 SER G OG  
3920 N N   . LEU D 105 ? 0.43300 0.40010 0.41400 0.02380  0.01930  0.03130  105 LEU G N   
3921 C CA  . LEU D 105 ? 0.41860 0.40750 0.41570 0.02210  0.02990  0.02220  105 LEU G CA  
3922 C C   . LEU D 105 ? 0.42720 0.43160 0.42710 0.02160  0.02920  0.01970  105 LEU G C   
3923 O O   . LEU D 105 ? 0.42840 0.43470 0.43100 0.03050  0.02340  0.02160  105 LEU G O   
3924 C CB  . LEU D 105 ? 0.37490 0.36260 0.38570 0.03090  0.03430  0.01780  105 LEU G CB  
3925 C CG  . LEU D 105 ? 0.34100 0.34080 0.36590 0.02990  0.04140  0.01060  105 LEU G CG  
3926 C CD1 . LEU D 105 ? 0.33640 0.34150 0.36490 0.02430  0.04640  0.00600  105 LEU G CD1 
3927 C CD2 . LEU D 105 ? 0.30690 0.30300 0.33910 0.03520  0.04240  0.01070  105 LEU G CD2 
3928 N N   . LEU D 106 ? 0.50220 0.52110 0.50180 0.01160  0.03500  0.01370  106 LEU G N   
3929 C CA  . LEU D 106 ? 0.51440 0.54820 0.51430 0.00800  0.03450  0.01000  106 LEU G CA  
3930 C C   . LEU D 106 ? 0.48800 0.53100 0.49600 0.00280  0.04430  -0.00350 106 LEU G C   
3931 O O   . LEU D 106 ? 0.46440 0.50750 0.47610 0.00170  0.05050  -0.00960 106 LEU G O   
3932 C CB  . LEU D 106 ? 0.54750 0.58670 0.52950 -0.00170 0.02690  0.01750  106 LEU G CB  
3933 C CG  . LEU D 106 ? 0.55130 0.59800 0.51990 -0.01750 0.03130  0.01590  106 LEU G CG  
3934 C CD1 . LEU D 106 ? 0.57200 0.62890 0.52070 -0.03110 0.02350  0.02310  106 LEU G CD1 
3935 C CD2 . LEU D 106 ? 0.55760 0.58870 0.51890 -0.01920 0.02910  0.02380  106 LEU G CD2 
3936 N N   . ALA D 107 ? 0.41540 0.46600 0.42670 0.00050  0.04450  -0.00890 107 ALA G N   
3937 C CA  . ALA D 107 ? 0.40090 0.45090 0.41770 -0.00340 0.05130  -0.02260 107 ALA G CA  
3938 C C   . ALA D 107 ? 0.42020 0.48520 0.42580 -0.01550 0.05350  -0.03130 107 ALA G C   
3939 O O   . ALA D 107 ? 0.44130 0.51890 0.43680 -0.02230 0.04760  -0.02480 107 ALA G O   
3940 C CB  . ALA D 107 ? 0.40280 0.44810 0.42630 -0.00310 0.04940  -0.02280 107 ALA G CB  
3941 N N   . HIS D 108 ? 0.49350 0.55900 0.50110 -0.01730 0.06130  -0.04700 108 HIS G N   
3942 C CA  . HIS D 108 ? 0.50370 0.58560 0.49990 -0.02950 0.06570  -0.06040 108 HIS G CA  
3943 C C   . HIS D 108 ? 0.51100 0.57930 0.51240 -0.02870 0.06970  -0.07890 108 HIS G C   
3944 O O   . HIS D 108 ? 0.49980 0.55320 0.51380 -0.01720 0.07330  -0.08880 108 HIS G O   
3945 C CB  . HIS D 108 ? 0.49190 0.59250 0.48380 -0.03360 0.07240  -0.06690 108 HIS G CB  
3946 C CG  . HIS D 108 ? 0.50390 0.61150 0.48480 -0.03920 0.06680  -0.04800 108 HIS G CG  
3947 N ND1 . HIS D 108 ? 0.53190 0.65060 0.49260 -0.05320 0.05980  -0.03700 108 HIS G ND1 
3948 C CD2 . HIS D 108 ? 0.49670 0.59800 0.48150 -0.03400 0.06530  -0.03760 108 HIS G CD2 
3949 C CE1 . HIS D 108 ? 0.53080 0.64440 0.48240 -0.05580 0.05320  -0.02010 108 HIS G CE1 
3950 N NE2 . HIS D 108 ? 0.52800 0.63130 0.49350 -0.04510 0.05710  -0.02110 108 HIS G NE2 
3951 N N   . PRO D 109 ? 0.51380 0.58460 0.50470 -0.04080 0.06770  -0.08440 109 PRO G N   
3952 C CA  . PRO D 109 ? 0.52660 0.61950 0.50350 -0.05390 0.06170  -0.07370 109 PRO G CA  
3953 C C   . PRO D 109 ? 0.53450 0.62790 0.51670 -0.05080 0.05220  -0.05510 109 PRO G C   
3954 O O   . PRO D 109 ? 0.54020 0.65310 0.51460 -0.05660 0.04490  -0.04430 109 PRO G O   
3955 C CB  . PRO D 109 ? 0.55080 0.64730 0.51600 -0.06860 0.06420  -0.09140 109 PRO G CB  
3956 C CG  . PRO D 109 ? 0.55010 0.61470 0.52440 -0.06200 0.06620  -0.10340 109 PRO G CG  
3957 C CD  . PRO D 109 ? 0.53160 0.58370 0.52130 -0.04360 0.07040  -0.10420 109 PRO G CD  
3958 N N   . GLY D 110 ? 0.43870 0.51410 0.43390 -0.04170 0.05170  -0.05170 110 GLY G N   
3959 C CA  . GLY D 110 ? 0.44020 0.52400 0.44170 -0.03940 0.04480  -0.03830 110 GLY G CA  
3960 C C   . GLY D 110 ? 0.42790 0.49240 0.44010 -0.03320 0.04600  -0.03650 110 GLY G C   
3961 O O   . GLY D 110 ? 0.43330 0.47330 0.44730 -0.03130 0.05000  -0.04490 110 GLY G O   
3962 N N   . PRO D 111 ? 0.42600 0.50300 0.44560 -0.02950 0.04200  -0.02590 111 PRO G N   
3963 C CA  . PRO D 111 ? 0.41260 0.47540 0.43940 -0.02630 0.04310  -0.02250 111 PRO G CA  
3964 C C   . PRO D 111 ? 0.43290 0.48830 0.45550 -0.04270 0.04230  -0.02590 111 PRO G C   
3965 O O   . PRO D 111 ? 0.43560 0.47520 0.45990 -0.04390 0.04200  -0.02170 111 PRO G O   
3966 C CB  . PRO D 111 ? 0.39230 0.47790 0.42730 -0.01630 0.04000  -0.01290 111 PRO G CB  
3967 C CG  . PRO D 111 ? 0.40470 0.51990 0.43850 -0.01960 0.03480  -0.01180 111 PRO G CG  
3968 C CD  . PRO D 111 ? 0.42840 0.53500 0.45050 -0.02590 0.03540  -0.01710 111 PRO G CD  
3969 N N   . LEU D 112 ? 0.52320 0.58810 0.53750 -0.05810 0.04070  -0.03210 112 LEU G N   
3970 C CA  . LEU D 112 ? 0.54660 0.59810 0.55180 -0.07840 0.03850  -0.03560 112 LEU G CA  
3971 C C   . LEU D 112 ? 0.57560 0.58550 0.57120 -0.08020 0.03970  -0.04900 112 LEU G C   
3972 O O   . LEU D 112 ? 0.58180 0.59550 0.57100 -0.08220 0.04180  -0.06030 112 LEU G O   
3973 C CB  . LEU D 112 ? 0.54230 0.62930 0.54300 -0.09640 0.03530  -0.03620 112 LEU G CB  
3974 C CG  . LEU D 112 ? 0.51270 0.64970 0.52600 -0.09390 0.03290  -0.02650 112 LEU G CG  
3975 C CD1 . LEU D 112 ? 0.51310 0.68450 0.52160 -0.11640 0.02880  -0.02850 112 LEU G CD1 
3976 C CD2 . LEU D 112 ? 0.50020 0.63690 0.52040 -0.09190 0.03460  -0.01930 112 LEU G CD2 
3977 N N   . VAL D 113 ? 0.47550 0.44660 0.46930 -0.07910 0.03740  -0.04860 113 VAL G N   
3978 C CA  . VAL D 113 ? 0.48130 0.41130 0.47180 -0.07110 0.03750  -0.06260 113 VAL G CA  
3979 C C   . VAL D 113 ? 0.51450 0.40310 0.48900 -0.08930 0.02990  -0.06700 113 VAL G C   
3980 O O   . VAL D 113 ? 0.52330 0.39380 0.49340 -0.09830 0.02350  -0.05420 113 VAL G O   
3981 C CB  . VAL D 113 ? 0.46060 0.37600 0.46450 -0.04920 0.03820  -0.05840 113 VAL G CB  
3982 C CG1 . VAL D 113 ? 0.46190 0.34600 0.46790 -0.03610 0.03850  -0.07580 113 VAL G CG1 
3983 C CG2 . VAL D 113 ? 0.42780 0.38130 0.44310 -0.03650 0.04390  -0.05120 113 VAL G CG2 
3984 N N   . LYS D 114 ? 0.67760 0.54950 0.64040 -0.09670 0.03010  -0.08520 114 LYS G N   
3985 C CA  . LYS D 114 ? 0.71490 0.53670 0.65870 -0.11410 0.02120  -0.09150 114 LYS G CA  
3986 C C   . LYS D 114 ? 0.73200 0.50040 0.67850 -0.09950 0.01320  -0.08860 114 LYS G C   
3987 O O   . LYS D 114 ? 0.71520 0.47920 0.67800 -0.07230 0.01640  -0.09540 114 LYS G O   
3988 C CB  . LYS D 114 ? 0.74100 0.54870 0.67180 -0.11990 0.02340  -0.11650 114 LYS G CB  
3989 C CG  . LYS D 114 ? 0.74290 0.59570 0.66390 -0.14250 0.02680  -0.11790 114 LYS G CG  
3990 C CD  . LYS D 114 ? 0.77870 0.61040 0.68040 -0.15450 0.02740  -0.14350 114 LYS G CD  
3991 C CE  . LYS D 114 ? 0.76700 0.62590 0.67620 -0.13690 0.03830  -0.16170 114 LYS G CE  
3992 N NZ  . LYS D 114 ? 0.78100 0.62220 0.66990 -0.14880 0.04020  -0.19040 114 LYS G NZ  
3993 N N   . SER D 115 ? 0.69800 0.42840 0.62770 -0.11960 0.00160  -0.07720 115 SER G N   
3994 C CA  . SER D 115 ? 0.72560 0.39540 0.65220 -0.10950 -0.01080 -0.07260 115 SER G CA  
3995 C C   . SER D 115 ? 0.73960 0.36980 0.67180 -0.08400 -0.01230 -0.09790 115 SER G C   
3996 O O   . SER D 115 ? 0.75910 0.37750 0.68030 -0.09030 -0.01000 -0.11940 115 SER G O   
3997 C CB  . SER D 115 ? 0.76220 0.38830 0.66040 -0.14290 -0.02510 -0.05980 115 SER G CB  
3998 O OG  . SER D 115 ? 0.79540 0.35230 0.68610 -0.13410 -0.04110 -0.05510 115 SER G OG  
3999 N N   . GLY D 116 ? 0.73900 0.35380 0.68930 -0.05490 -0.01580 -0.09690 116 GLY G N   
4000 C CA  . GLY D 116 ? 0.74210 0.32720 0.70360 -0.02570 -0.01730 -0.12220 116 GLY G CA  
4001 C C   . GLY D 116 ? 0.70400 0.34460 0.68710 -0.00530 0.00020  -0.14190 116 GLY G C   
4002 O O   . GLY D 116 ? 0.70030 0.33030 0.69850 0.02210  0.00100  -0.16360 116 GLY G O   
4003 N N   . GLU D 117 ? 0.71760 0.41810 0.70240 -0.01760 0.01330  -0.13520 117 GLU G N   
4004 C CA  . GLU D 117 ? 0.67950 0.42990 0.67760 -0.00510 0.02840  -0.15160 117 GLU G CA  
4005 C C   . GLU D 117 ? 0.62970 0.41820 0.64950 0.01150  0.03350  -0.13740 117 GLU G C   
4006 O O   . GLU D 117 ? 0.62780 0.40380 0.65300 0.01510  0.02580  -0.11720 117 GLU G O   
4007 C CB  . GLU D 117 ? 0.68090 0.46770 0.66400 -0.02940 0.03640  -0.15320 117 GLU G CB  
4008 C CG  . GLU D 117 ? 0.73030 0.48130 0.68950 -0.04980 0.03110  -0.16800 117 GLU G CG  
4009 C CD  . GLU D 117 ? 0.72410 0.51390 0.67170 -0.06550 0.04090  -0.18250 117 GLU G CD  
4010 O OE1 . GLU D 117 ? 0.70270 0.54720 0.65730 -0.06680 0.04900  -0.17290 117 GLU G OE1 
4011 O OE2 . GLU D 117 ? 0.76900 0.53180 0.69820 -0.07760 0.03910  -0.20340 117 GLU G OE2 
4012 N N   . ARG D 118 ? 0.74720 0.58240 0.77670 0.01870  0.04600  -0.14770 118 ARG G N   
4013 C CA  . ARG D 118 ? 0.70540 0.57550 0.75250 0.03140  0.05080  -0.13630 118 ARG G CA  
4014 C C   . ARG D 118 ? 0.68050 0.59520 0.72120 0.01700  0.05830  -0.12360 118 ARG G C   
4015 O O   . ARG D 118 ? 0.69800 0.62750 0.72470 0.00160  0.06210  -0.12940 118 ARG G O   
4016 C CB  . ARG D 118 ? 0.68740 0.57460 0.75290 0.05360  0.05720  -0.15840 118 ARG G CB  
4017 C CG  . ARG D 118 ? 0.70860 0.55710 0.78860 0.07610  0.04640  -0.16380 118 ARG G CG  
4018 C CD  . ARG D 118 ? 0.69910 0.57050 0.80080 0.10050  0.05290  -0.19110 118 ARG G CD  
4019 N NE  . ARG D 118 ? 0.68650 0.54940 0.81090 0.12390  0.04350  -0.18430 118 ARG G NE  
4020 C CZ  . ARG D 118 ? 0.72600 0.54320 0.85980 0.14520  0.03000  -0.19380 118 ARG G CZ  
4021 N NH1 . ARG D 118 ? 0.76800 0.53940 0.88970 0.14680  0.02470  -0.21330 118 ARG G NH1 
4022 N NH2 . ARG D 118 ? 0.72220 0.53720 0.87670 0.16530  0.01970  -0.18350 118 ARG G NH2 
4023 N N   . VAL D 119 ? 0.47620 0.40950 0.52600 0.02230  0.05850  -0.10610 119 VAL G N   
4024 C CA  . VAL D 119 ? 0.45600 0.42390 0.50040 0.01290  0.06280  -0.09300 119 VAL G CA  
4025 C C   . VAL D 119 ? 0.42320 0.41300 0.47960 0.02390  0.06660  -0.08930 119 VAL G C   
4026 O O   . VAL D 119 ? 0.41360 0.39230 0.48360 0.03730  0.06360  -0.08780 119 VAL G O   
4027 C CB  . VAL D 119 ? 0.46910 0.43260 0.50700 0.00290  0.05670  -0.07260 119 VAL G CB  
4028 C CG1 . VAL D 119 ? 0.45330 0.39990 0.49970 0.01110  0.05130  -0.05930 119 VAL G CG1 
4029 C CG2 . VAL D 119 ? 0.46260 0.45790 0.49480 -0.00370 0.05860  -0.06190 119 VAL G CG2 
4030 N N   . ILE D 120 ? 0.41260 0.43320 0.46210 0.01630  0.07190  -0.08710 120 ILE G N   
4031 C CA  . ILE D 120 ? 0.38750 0.42940 0.44270 0.01990  0.07460  -0.08040 120 ILE G CA  
4032 C C   . ILE D 120 ? 0.38930 0.42890 0.43660 0.01470  0.06910  -0.05840 120 ILE G C   
4033 O O   . ILE D 120 ? 0.40740 0.45090 0.44210 0.00520  0.06660  -0.05170 120 ILE G O   
4034 C CB  . ILE D 120 ? 0.38720 0.46300 0.43580 0.01140  0.08280  -0.09200 120 ILE G CB  
4035 C CG1 . ILE D 120 ? 0.39770 0.48020 0.45750 0.02050  0.08950  -0.11880 120 ILE G CG1 
4036 C CG2 . ILE D 120 ? 0.37770 0.47490 0.42700 0.00840  0.08410  -0.08120 120 ILE G CG2 
4037 C CD1 . ILE D 120 ? 0.38630 0.46260 0.46910 0.04010  0.08780  -0.12300 120 ILE G CD1 
4038 N N   . LEU D 121 ? 0.39030 0.42420 0.44530 0.02190  0.06640  -0.04830 121 LEU G N   
4039 C CA  . LEU D 121 ? 0.38980 0.42090 0.43700 0.01890  0.06180  -0.03110 121 LEU G CA  
4040 C C   . LEU D 121 ? 0.39300 0.43970 0.43580 0.01450  0.06350  -0.02760 121 LEU G C   
4041 O O   . LEU D 121 ? 0.37820 0.43190 0.43150 0.01900  0.06560  -0.03060 121 LEU G O   
4042 C CB  . LEU D 121 ? 0.37360 0.38680 0.42750 0.02600  0.05720  -0.02260 121 LEU G CB  
4043 C CG  . LEU D 121 ? 0.39100 0.39250 0.44280 0.02380  0.05390  -0.01970 121 LEU G CG  
4044 C CD1 . LEU D 121 ? 0.41420 0.41550 0.46280 0.01770  0.05540  -0.02990 121 LEU G CD1 
4045 C CD2 . LEU D 121 ? 0.37710 0.36160 0.43560 0.02790  0.05040  -0.01510 121 LEU G CD2 
4046 N N   . GLN D 122 ? 0.37180 0.42450 0.39800 0.00410  0.06130  -0.02050 122 GLN G N   
4047 C CA  . GLN D 122 ? 0.38500 0.45040 0.40050 -0.00670 0.06170  -0.01560 122 GLN G CA  
4048 C C   . GLN D 122 ? 0.40660 0.45100 0.41220 -0.00660 0.05320  0.00050  122 GLN G C   
4049 O O   . GLN D 122 ? 0.42810 0.45660 0.42510 -0.00380 0.04600  0.00870  122 GLN G O   
4050 C CB  . GLN D 122 ? 0.39770 0.48000 0.39600 -0.02200 0.06260  -0.01690 122 GLN G CB  
4051 C CG  . GLN D 122 ? 0.41060 0.50650 0.39260 -0.03940 0.06200  -0.00950 122 GLN G CG  
4052 C CD  . GLN D 122 ? 0.42940 0.54410 0.39060 -0.05840 0.06220  -0.00920 122 GLN G CD  
4053 O OE1 . GLN D 122 ? 0.45230 0.55690 0.40280 -0.05970 0.05560  -0.00340 122 GLN G OE1 
4054 N NE2 . GLN D 122 ? 0.41660 0.56380 0.37200 -0.07460 0.06970  -0.01580 122 GLN G NE2 
4055 N N   . CYS D 123 ? 0.48170 0.52710 0.48960 -0.00830 0.05370  0.00310  123 CYS G N   
4056 C CA  . CYS D 123 ? 0.50610 0.52940 0.50060 -0.01120 0.04580  0.01590  123 CYS G CA  
4057 C C   . CYS D 123 ? 0.52160 0.55100 0.49520 -0.03140 0.04320  0.02290  123 CYS G C   
4058 O O   . CYS D 123 ? 0.50450 0.56470 0.48200 -0.04190 0.05060  0.01610  123 CYS G O   
4059 C CB  . CYS D 123 ? 0.49780 0.51760 0.50440 -0.00440 0.04680  0.01530  123 CYS G CB  
4060 S SG  . CYS D 123 ? 0.52640 0.51220 0.51770 -0.00290 0.03750  0.02600  123 CYS G SG  
4061 N N   . TRP D 124 ? 0.46020 0.46080 0.41100 -0.03710 0.03200  0.03600  124 TRP G N   
4062 C CA  . TRP D 124 ? 0.47150 0.47040 0.39580 -0.06070 0.02640  0.04630  124 TRP G CA  
4063 C C   . TRP D 124 ? 0.49210 0.44440 0.39360 -0.06200 0.01140  0.06040  124 TRP G C   
4064 O O   . TRP D 124 ? 0.50020 0.42650 0.40640 -0.04230 0.00530  0.06050  124 TRP G O   
4065 C CB  . TRP D 124 ? 0.47800 0.49300 0.39040 -0.07200 0.02600  0.04770  124 TRP G CB  
4066 C CG  . TRP D 124 ? 0.49800 0.48680 0.40240 -0.06130 0.01440  0.05560  124 TRP G CG  
4067 C CD1 . TRP D 124 ? 0.50280 0.49750 0.42510 -0.04330 0.01680  0.04800  124 TRP G CD1 
4068 C CD2 . TRP D 124 ? 0.52480 0.47800 0.40160 -0.06740 -0.00330 0.07310  124 TRP G CD2 
4069 N NE1 . TRP D 124 ? 0.51940 0.49240 0.43020 -0.03690 0.00280  0.05860  124 TRP G NE1 
4070 C CE2 . TRP D 124 ? 0.53470 0.47940 0.41810 -0.04930 -0.01070 0.07410  124 TRP G CE2 
4071 C CE3 . TRP D 124 ? 0.54280 0.46870 0.38880 -0.08730 -0.01530 0.08860  124 TRP G CE3 
4072 C CZ2 . TRP D 124 ? 0.55690 0.46800 0.42090 -0.04570 -0.03020 0.08910  124 TRP G CZ2 
4073 C CZ3 . TRP D 124 ? 0.57900 0.46310 0.40160 -0.08560 -0.03570 0.10460  124 TRP G CZ3 
4074 C CH2 . TRP D 124 ? 0.57900 0.45670 0.41240 -0.06250 -0.04330 0.10430  124 TRP G CH2 
4075 N N   . SER D 125 ? 0.54660 0.48930 0.42220 -0.08630 0.00510  0.07100  125 SER G N   
4076 C CA  . SER D 125 ? 0.57630 0.46660 0.42520 -0.09050 -0.01120 0.08400  125 SER G CA  
4077 C C   . SER D 125 ? 0.59300 0.47460 0.40600 -0.12480 -0.02030 0.09920  125 SER G C   
4078 O O   . SER D 125 ? 0.57410 0.49950 0.38700 -0.14740 -0.01010 0.09680  125 SER G O   
4079 C CB  . SER D 125 ? 0.56950 0.44660 0.42590 -0.08380 -0.00910 0.07850  125 SER G CB  
4080 O OG  . SER D 125 ? 0.59390 0.41640 0.42130 -0.08920 -0.02510 0.08840  125 SER G OG  
4081 N N   . ASP D 126 ? 0.95600 0.53000 0.83780 0.03890  0.10730  0.19720  126 ASP G N   
4082 C CA  . ASP D 126 ? 1.01760 0.52960 0.88210 0.01610  0.13350  0.22810  126 ASP G CA  
4083 C C   . ASP D 126 ? 1.02430 0.50750 0.92300 -0.02370 0.15660  0.19400  126 ASP G C   
4084 O O   . ASP D 126 ? 1.06050 0.50710 0.95240 -0.05500 0.18290  0.20980  126 ASP G O   
4085 C CB  . ASP D 126 ? 1.07620 0.52360 0.93350 0.04460  0.12960  0.26900  126 ASP G CB  
4086 C CG  . ASP D 126 ? 1.05980 0.50270 0.95510 0.08150  0.11110  0.24970  126 ASP G CG  
4087 O OD1 . ASP D 126 ? 1.00510 0.47790 0.92300 0.08450  0.10810  0.21070  126 ASP G OD1 
4088 O OD2 . ASP D 126 ? 1.11300 0.52560 1.01640 0.10650  0.09940  0.27310  126 ASP G OD2 
4089 N N   . ILE D 127 ? 0.87060 0.37340 0.80350 -0.02610 0.14740  0.14700  127 ILE G N   
4090 C CA  . ILE D 127 ? 0.86750 0.36760 0.83090 -0.06660 0.16040  0.10740  127 ILE G CA  
4091 C C   . ILE D 127 ? 0.83250 0.41190 0.80300 -0.09050 0.15550  0.09220  127 ILE G C   
4092 O O   . ILE D 127 ? 0.79140 0.43390 0.75510 -0.07210 0.13520  0.08880  127 ILE G O   
4093 C CB  . ILE D 127 ? 0.84850 0.34730 0.83400 -0.06020 0.14960  0.06460  127 ILE G CB  
4094 C CG1 . ILE D 127 ? 0.89020 0.30490 0.88320 -0.03960 0.16290  0.07110  127 ILE G CG1 
4095 C CG2 . ILE D 127 ? 0.83260 0.35670 0.84280 -0.10240 0.15130  0.01950  127 ILE G CG2 
4096 C CD1 . ILE D 127 ? 0.86220 0.28440 0.86940 -0.02540 0.15490  0.03030  127 ILE G CD1 
4097 N N   . MET D 128 ? 0.87540 0.45220 0.86810 -0.13210 0.17570  0.08040  128 MET G N   
4098 C CA  . MET D 128 ? 0.83880 0.49320 0.85520 -0.15500 0.17430  0.06250  128 MET G CA  
4099 C C   . MET D 128 ? 0.80220 0.50900 0.85250 -0.15870 0.14790  0.01950  128 MET G C   
4100 O O   . MET D 128 ? 0.80990 0.52190 0.89350 -0.19050 0.14950  -0.01050 128 MET G O   
4101 C CB  . MET D 128 ? 0.86730 0.50550 0.90330 -0.19940 0.20770  0.06540  128 MET G CB  
4102 C CG  . MET D 128 ? 0.91260 0.49980 0.90370 -0.19950 0.23580  0.11550  128 MET G CG  
4103 S SD  . MET D 128 ? 0.90950 0.55750 0.85330 -0.16910 0.22510  0.14160  128 MET G SD  
4104 C CE  . MET D 128 ? 0.95060 0.53130 0.83830 -0.12350 0.20950  0.18770  128 MET G CE  
4105 N N   . PHE D 129 ? 0.61060 0.35820 0.65010 -0.12750 0.12210  0.01750  129 PHE G N   
4106 C CA  . PHE D 129 ? 0.57750 0.37440 0.63960 -0.12890 0.09570  -0.01340 129 PHE G CA  
4107 C C   . PHE D 129 ? 0.54660 0.41690 0.64880 -0.14180 0.08900  -0.02320 129 PHE G C   
4108 O O   . PHE D 129 ? 0.53430 0.43050 0.63670 -0.13230 0.09780  -0.00840 129 PHE G O   
4109 C CB  . PHE D 129 ? 0.56060 0.36580 0.59800 -0.09320 0.07510  -0.00950 129 PHE G CB  
4110 C CG  . PHE D 129 ? 0.58450 0.33200 0.59920 -0.08020 0.07930  -0.01140 129 PHE G CG  
4111 C CD1 . PHE D 129 ? 0.60520 0.32780 0.62500 -0.10070 0.08110  -0.04070 129 PHE G CD1 
4112 C CD2 . PHE D 129 ? 0.58090 0.30500 0.57350 -0.04750 0.08100  0.01170  129 PHE G CD2 
4113 C CE1 . PHE D 129 ? 0.62760 0.29630 0.63300 -0.08790 0.09050  -0.04920 129 PHE G CE1 
4114 C CE2 . PHE D 129 ? 0.59350 0.26940 0.57890 -0.03160 0.08640  0.00750  129 PHE G CE2 
4115 C CZ  . PHE D 129 ? 0.62540 0.27070 0.61820 -0.05110 0.09390  -0.02410 129 PHE G CZ  
4116 N N   . GLU D 130 ? 0.71660 0.62420 0.85560 -0.16360 0.07320  -0.05050 130 GLU G N   
4117 C CA  . GLU D 130 ? 0.67360 0.65700 0.86610 -0.17110 0.06340  -0.06030 130 GLU G CA  
4118 C C   . GLU D 130 ? 0.64440 0.66860 0.83850 -0.13820 0.03700  -0.05460 130 GLU G C   
4119 O O   . GLU D 130 ? 0.60630 0.67420 0.83370 -0.12870 0.04020  -0.05180 130 GLU G O   
4120 C CB  . GLU D 130 ? 0.66770 0.68620 0.90520 -0.20450 0.04920  -0.08970 130 GLU G CB  
4121 C CG  . GLU D 130 ? 0.62380 0.73060 0.93120 -0.20710 0.03220  -0.10010 130 GLU G CG  
4122 C CD  . GLU D 130 ? 0.62180 0.76360 0.99160 -0.24920 0.04600  -0.12260 130 GLU G CD  
4123 O OE1 . GLU D 130 ? 0.66850 0.76690 1.02620 -0.28160 0.06070  -0.13590 130 GLU G OE1 
4124 O OE2 . GLU D 130 ? 0.57410 0.78760 1.01300 -0.25110 0.04530  -0.12970 130 GLU G OE2 
4125 N N   . HIS D 131 ? 0.48850 0.49630 0.64880 -0.12230 0.01500  -0.05460 131 HIS G N   
4126 C CA  . HIS D 131 ? 0.46910 0.50180 0.62540 -0.09340 -0.00580 -0.04530 131 HIS G CA  
4127 C C   . HIS D 131 ? 0.49720 0.48360 0.59980 -0.07280 -0.00170 -0.03450 131 HIS G C   
4128 O O   . HIS D 131 ? 0.51890 0.45870 0.59080 -0.07870 0.00880  -0.03810 131 HIS G O   
4129 C CB  . HIS D 131 ? 0.45350 0.52880 0.62950 -0.09640 -0.04090 -0.05370 131 HIS G CB  
4130 C CG  . HIS D 131 ? 0.42940 0.56440 0.67300 -0.11160 -0.05120 -0.06440 131 HIS G CG  
4131 N ND1 . HIS D 131 ? 0.43910 0.59380 0.70290 -0.14340 -0.06020 -0.08500 131 HIS G ND1 
4132 C CD2 . HIS D 131 ? 0.37560 0.55920 0.68000 -0.10000 -0.05190 -0.06170 131 HIS G CD2 
4133 C CE1 . HIS D 131 ? 0.39950 0.61860 0.73690 -0.15000 -0.06880 -0.09220 131 HIS G CE1 
4134 N NE2 . HIS D 131 ? 0.36170 0.59820 0.72660 -0.12230 -0.06240 -0.07820 131 HIS G NE2 
4135 N N   . PHE D 132 ? 0.42120 0.42200 0.52140 -0.04850 -0.00820 -0.02380 132 PHE G N   
4136 C CA  . PHE D 132 ? 0.42830 0.40230 0.49120 -0.02880 -0.00770 -0.01620 132 PHE G CA  
4137 C C   . PHE D 132 ? 0.41420 0.40960 0.47840 -0.01960 -0.02910 -0.01460 132 PHE G C   
4138 O O   . PHE D 132 ? 0.37630 0.40610 0.47580 -0.01630 -0.04180 -0.01150 132 PHE G O   
4139 C CB  . PHE D 132 ? 0.40400 0.37550 0.46080 -0.01220 0.00650  -0.00510 132 PHE G CB  
4140 C CG  . PHE D 132 ? 0.43020 0.36900 0.46660 -0.01650 0.02610  0.00400  132 PHE G CG  
4141 C CD1 . PHE D 132 ? 0.43890 0.33550 0.44750 -0.00740 0.03030  0.01010  132 PHE G CD1 
4142 C CD2 . PHE D 132 ? 0.44470 0.39370 0.49160 -0.02890 0.04230  0.00840  132 PHE G CD2 
4143 C CE1 . PHE D 132 ? 0.46650 0.32550 0.45820 -0.00750 0.04630  0.02610  132 PHE G CE1 
4144 C CE2 . PHE D 132 ? 0.47490 0.38700 0.49540 -0.03420 0.06090  0.02480  132 PHE G CE2 
4145 C CZ  . PHE D 132 ? 0.49000 0.35410 0.48290 -0.02190 0.06100  0.03650  132 PHE G CZ  
4146 N N   . PHE D 133 ? 0.45190 0.42540 0.48070 -0.01480 -0.03060 -0.01530 133 PHE G N   
4147 C CA  . PHE D 133 ? 0.45160 0.43730 0.46970 -0.00970 -0.04610 -0.00900 133 PHE G CA  
4148 C C   . PHE D 133 ? 0.42890 0.40070 0.43250 0.00640  -0.03400 -0.00460 133 PHE G C   
4149 O O   . PHE D 133 ? 0.42850 0.37790 0.41460 0.01060  -0.01930 -0.01130 133 PHE G O   
4150 C CB  . PHE D 133 ? 0.50160 0.48300 0.48550 -0.02730 -0.05690 -0.01820 133 PHE G CB  
4151 C CG  . PHE D 133 ? 0.50140 0.50840 0.50340 -0.04630 -0.07520 -0.02550 133 PHE G CG  
4152 C CD1 . PHE D 133 ? 0.50970 0.50550 0.52260 -0.06320 -0.06360 -0.04280 133 PHE G CD1 
4153 C CD2 . PHE D 133 ? 0.48420 0.52770 0.49710 -0.04750 -0.10500 -0.01340 133 PHE G CD2 
4154 C CE1 . PHE D 133 ? 0.50690 0.53410 0.54510 -0.08490 -0.08010 -0.05400 133 PHE G CE1 
4155 C CE2 . PHE D 133 ? 0.47800 0.55770 0.51640 -0.06460 -0.12690 -0.02170 133 PHE G CE2 
4156 C CZ  . PHE D 133 ? 0.48610 0.56110 0.53910 -0.08530 -0.11370 -0.04520 133 PHE G CZ  
4157 N N   . LEU D 134 ? 0.45610 0.44180 0.47480 0.01580  -0.03990 0.00560  134 LEU G N   
4158 C CA  . LEU D 134 ? 0.43210 0.41120 0.44360 0.02550  -0.02920 0.00660  134 LEU G CA  
4159 C C   . LEU D 134 ? 0.47580 0.45040 0.46360 0.01860  -0.03480 0.01560  134 LEU G C   
4160 O O   . LEU D 134 ? 0.47370 0.45560 0.46920 0.01640  -0.05120 0.03080  134 LEU G O   
4161 C CB  . LEU D 134 ? 0.36850 0.36180 0.41480 0.03620  -0.02590 0.00710  134 LEU G CB  
4162 C CG  . LEU D 134 ? 0.35110 0.34550 0.39940 0.04240  -0.01540 0.00260  134 LEU G CG  
4163 C CD1 . LEU D 134 ? 0.33560 0.33100 0.37230 0.04970  -0.00640 -0.00600 134 LEU G CD1 
4164 C CD2 . LEU D 134 ? 0.31050 0.31770 0.39550 0.04680  -0.01390 -0.00180 134 LEU G CD2 
4165 N N   . HIS D 135 ? 0.45590 0.41960 0.41560 0.01570  -0.02040 0.00800  135 HIS G N   
4166 C CA  . HIS D 135 ? 0.49810 0.45690 0.42230 0.00380  -0.01910 0.01570  135 HIS G CA  
4167 C C   . HIS D 135 ? 0.49750 0.45600 0.42730 0.00650  0.00200  0.01240  135 HIS G C   
4168 O O   . HIS D 135 ? 0.47510 0.43630 0.41400 0.01340  0.01830  -0.00560 135 HIS G O   
4169 C CB  . HIS D 135 ? 0.53850 0.48970 0.41710 -0.01130 -0.01620 0.00130  135 HIS G CB  
4170 C CG  . HIS D 135 ? 0.56620 0.51690 0.39350 -0.02830 -0.01620 0.01030  135 HIS G CG  
4171 N ND1 . HIS D 135 ? 0.58970 0.53380 0.37770 -0.04000 0.00760  -0.00920 135 HIS G ND1 
4172 C CD2 . HIS D 135 ? 0.58030 0.53590 0.38620 -0.03560 -0.03630 0.03860  135 HIS G CD2 
4173 C CE1 . HIS D 135 ? 0.61950 0.56600 0.35510 -0.05780 0.00430  0.00620  135 HIS G CE1 
4174 N NE2 . HIS D 135 ? 0.62160 0.57320 0.36570 -0.05440 -0.02470 0.03910  135 HIS G NE2 
4175 N N   . LYS D 136 ? 0.54330 0.49850 0.47180 0.00050  0.00210  0.03090  136 LYS G N   
4176 C CA  . LYS D 136 ? 0.54890 0.50560 0.48470 -0.00420 0.02530  0.02680  136 LYS G CA  
4177 C C   . LYS D 136 ? 0.58540 0.53650 0.46750 -0.02230 0.04150  0.02610  136 LYS G C   
4178 O O   . LYS D 136 ? 0.61810 0.55890 0.45320 -0.03520 0.02980  0.04620  136 LYS G O   
4179 C CB  . LYS D 136 ? 0.53850 0.48650 0.50340 -0.00550 0.02370  0.04550  136 LYS G CB  
4180 C CG  . LYS D 136 ? 0.55170 0.49860 0.52250 -0.01880 0.04980  0.04360  136 LYS G CG  
4181 C CD  . LYS D 136 ? 0.54830 0.47830 0.55820 -0.02100 0.05050  0.05780  136 LYS G CD  
4182 C CE  . LYS D 136 ? 0.57920 0.48910 0.57190 -0.04290 0.07300  0.07580  136 LYS G CE  
4183 N NZ  . LYS D 136 ? 0.56850 0.50410 0.56900 -0.05550 0.10300  0.04970  136 LYS G NZ  
4184 N N   . GLU D 137 ? 0.70980 0.67270 0.59980 -0.02310 0.06810  0.00230  137 GLU G N   
4185 C CA  . GLU D 137 ? 0.74040 0.70220 0.58210 -0.04150 0.09190  -0.00720 137 GLU G CA  
4186 C C   . GLU D 137 ? 0.77630 0.72720 0.58110 -0.06360 0.10010  0.02090  137 GLU G C   
4187 O O   . GLU D 137 ? 0.77180 0.71820 0.61040 -0.06410 0.10220  0.03750  137 GLU G O   
4188 C CB  . GLU D 137 ? 0.70490 0.68750 0.58240 -0.03470 0.12210  -0.03900 137 GLU G CB  
4189 C CG  . GLU D 137 ? 0.70690 0.68650 0.57740 -0.02580 0.12910  -0.06740 137 GLU G CG  
4190 C CD  . GLU D 137 ? 0.65200 0.65220 0.58840 -0.00160 0.14160  -0.09010 137 GLU G CD  
4191 O OE1 . GLU D 137 ? 0.62740 0.65470 0.59510 -0.00440 0.16630  -0.10180 137 GLU G OE1 
4192 O OE2 . GLU D 137 ? 0.62420 0.61510 0.58270 0.01960  0.12590  -0.09360 137 GLU G OE2 
4193 N N   . GLY D 138 ? 0.90860 0.85310 0.64120 -0.08410 0.10590  0.02580  138 GLY G N   
4194 C CA  . GLY D 138 ? 0.95190 0.88210 0.63160 -0.10740 0.11290  0.06010  138 GLY G CA  
4195 C C   . GLY D 138 ? 1.00610 0.93190 0.59950 -0.12320 0.09290  0.07470  138 GLY G C   
4196 O O   . GLY D 138 ? 0.99480 0.92790 0.58200 -0.11550 0.06760  0.06050  138 GLY G O   
4197 N N   . ILE D 139 ? 1.15460 1.07030 0.67780 -0.14890 0.10520  0.10320  139 ILE G N   
4198 C CA  . ILE D 139 ? 1.20030 1.11630 0.63240 -0.16540 0.07800  0.12670  139 ILE G CA  
4199 C C   . ILE D 139 ? 1.20340 1.10960 0.65890 -0.14620 0.02600  0.17160  139 ILE G C   
4200 O O   . ILE D 139 ? 1.18360 1.06920 0.69880 -0.13060 0.02230  0.19900  139 ILE G O   
4201 C CB  . ILE D 139 ? 1.26870 1.17690 0.61380 -0.19830 0.10610  0.15060  139 ILE G CB  
4202 C CG1 . ILE D 139 ? 1.26760 1.19110 0.62270 -0.21190 0.16450  0.10200  139 ILE G CG1 
4203 C CG2 . ILE D 139 ? 1.31900 1.24250 0.59190 -0.20540 0.07540  0.15960  139 ILE G CG2 
4204 C CD1 . ILE D 139 ? 1.24440 1.19120 0.59470 -0.21070 0.17450  0.04110  139 ILE G CD1 
4205 N N   . SER D 140 ? 1.23050 1.15480 0.64770 -0.14730 -0.01340 0.17390  140 SER G N   
4206 C CA  . SER D 140 ? 1.23130 1.15770 0.66690 -0.13020 -0.06650 0.21730  140 SER G CA  
4207 C C   . SER D 140 ? 1.17640 1.09220 0.72330 -0.09790 -0.07340 0.21920  140 SER G C   
4208 O O   . SER D 140 ? 1.17070 1.06450 0.75270 -0.08360 -0.08630 0.26120  140 SER G O   
4209 C CB  . SER D 140 ? 1.28510 1.19580 0.67380 -0.13410 -0.07800 0.27290  140 SER G CB  
4210 O OG  . SER D 140 ? 1.36810 1.29920 0.67430 -0.15380 -0.07700 0.26290  140 SER G OG  
4211 N N   . LYS D 141 ? 1.10320 1.03240 0.70380 -0.08720 -0.06280 0.17250  141 LYS G N   
4212 C CA  . LYS D 141 ? 1.04950 0.97480 0.74430 -0.06080 -0.06550 0.16630  141 LYS G CA  
4213 C C   . LYS D 141 ? 1.02150 0.97240 0.74950 -0.04980 -0.09400 0.14790  141 LYS G C   
4214 O O   . LYS D 141 ? 1.03490 1.00060 0.73370 -0.06190 -0.09220 0.11620  141 LYS G O   
4215 C CB  . LYS D 141 ? 1.01900 0.93860 0.75090 -0.05820 -0.02520 0.13210  141 LYS G CB  
4216 C CG  . LYS D 141 ? 1.04330 0.94360 0.76150 -0.07120 0.00600  0.14650  141 LYS G CG  
4217 C CD  . LYS D 141 ? 1.01020 0.90780 0.80410 -0.05930 0.02670  0.12920  141 LYS G CD  
4218 C CE  . LYS D 141 ? 0.97800 0.87470 0.83740 -0.03580 0.00180  0.13370  141 LYS G CE  
4219 N NZ  . LYS D 141 ? 0.99960 0.87310 0.86170 -0.03100 -0.02160 0.17850  141 LYS G NZ  
4220 N N   . ASP D 142 ? 0.89810 0.85310 0.69340 -0.02800 -0.11690 0.16530  142 ASP G N   
4221 C CA  . ASP D 142 ? 0.86870 0.85380 0.70050 -0.02050 -0.14330 0.15150  142 ASP G CA  
4222 C C   . ASP D 142 ? 0.83590 0.82220 0.73000 -0.00830 -0.12290 0.11900  142 ASP G C   
4223 O O   . ASP D 142 ? 0.80510 0.77500 0.73660 0.00340  -0.10310 0.11820  142 ASP G O   
4224 C CB  . ASP D 142 ? 0.85560 0.85440 0.72700 -0.00390 -0.18160 0.18890  142 ASP G CB  
4225 C CG  . ASP D 142 ? 0.91600 0.89790 0.73500 -0.00800 -0.19760 0.23750  142 ASP G CG  
4226 O OD1 . ASP D 142 ? 0.93900 0.88430 0.73370 -0.01390 -0.16830 0.24880  142 ASP G OD1 
4227 O OD2 . ASP D 142 ? 0.92880 0.93600 0.73130 -0.00660 -0.23970 0.26600  142 ASP G OD2 
4228 N N   . PRO D 143 ? 0.68190 0.68720 0.58480 -0.01350 -0.12710 0.09200  143 PRO G N   
4229 C CA  . PRO D 143 ? 0.63730 0.64190 0.58770 -0.00410 -0.10810 0.06740  143 PRO G CA  
4230 C C   . PRO D 143 ? 0.58490 0.60940 0.60500 0.01120  -0.12100 0.07380  143 PRO G C   
4231 O O   . PRO D 143 ? 0.59000 0.63760 0.63200 0.01440  -0.14950 0.09040  143 PRO G O   
4232 C CB  . PRO D 143 ? 0.66960 0.67830 0.59470 -0.02060 -0.10470 0.03980  143 PRO G CB  
4233 C CG  . PRO D 143 ? 0.69170 0.72370 0.58760 -0.03610 -0.13590 0.04770  143 PRO G CG  
4234 C CD  . PRO D 143 ? 0.71190 0.73900 0.57560 -0.03280 -0.14810 0.08200  143 PRO G CD  
4235 N N   . SER D 144 ? 0.51700 0.53670 0.57360 0.02140  -0.09960 0.05930  144 SER G N   
4236 C CA  . SER D 144 ? 0.46680 0.50810 0.58770 0.03220  -0.10150 0.05390  144 SER G CA  
4237 C C   . SER D 144 ? 0.47070 0.52640 0.59500 0.02080  -0.09470 0.03300  144 SER G C   
4238 O O   . SER D 144 ? 0.49850 0.53520 0.58580 0.01250  -0.07870 0.02100  144 SER G O   
4239 C CB  . SER D 144 ? 0.42340 0.45390 0.57410 0.04470  -0.07960 0.04610  144 SER G CB  
4240 O OG  . SER D 144 ? 0.44420 0.45400 0.59740 0.05150  -0.08120 0.06380  144 SER G OG  
4241 N N   . ARG D 145 ? 0.51370 0.60210 0.68850 0.02070  -0.10520 0.02950  145 ARG G N   
4242 C CA  . ARG D 145 ? 0.52860 0.63010 0.71230 0.00490  -0.09520 0.01080  145 ARG G CA  
4243 C C   . ARG D 145 ? 0.48460 0.60510 0.72110 0.01110  -0.07520 -0.00010 145 ARG G C   
4244 O O   . ARG D 145 ? 0.44620 0.58820 0.73640 0.02650  -0.07970 0.00250  145 ARG G O   
4245 C CB  . ARG D 145 ? 0.54260 0.67690 0.74020 -0.01080 -0.12170 0.00850  145 ARG G CB  
4246 C CG  . ARG D 145 ? 0.56320 0.69880 0.76060 -0.03520 -0.10650 -0.01330 145 ARG G CG  
4247 C CD  . ARG D 145 ? 0.56790 0.75070 0.80210 -0.05370 -0.13130 -0.02290 145 ARG G CD  
4248 N NE  . ARG D 145 ? 0.52170 0.75610 0.83690 -0.03930 -0.14330 -0.01800 145 ARG G NE  
4249 C CZ  . ARG D 145 ? 0.50880 0.80140 0.88280 -0.04990 -0.16570 -0.02650 145 ARG G CZ  
4250 N NH1 . ARG D 145 ? 0.53870 0.84610 0.89660 -0.08020 -0.17860 -0.04320 145 ARG G NH1 
4251 N NH2 . ARG D 145 ? 0.45400 0.79400 0.91150 -0.02990 -0.17530 -0.02150 145 ARG G NH2 
4252 N N   . LEU D 146 ? 0.41850 0.52870 0.63880 -0.00130 -0.05120 -0.01210 146 LEU G N   
4253 C CA  . LEU D 146 ? 0.39390 0.52370 0.64910 -0.00360 -0.02680 -0.02390 146 LEU G CA  
4254 C C   . LEU D 146 ? 0.42960 0.55810 0.67810 -0.02840 -0.01220 -0.03110 146 LEU G C   
4255 O O   . LEU D 146 ? 0.47720 0.57170 0.68090 -0.03960 -0.01260 -0.02790 146 LEU G O   
4256 C CB  . LEU D 146 ? 0.38650 0.49650 0.61270 0.00690  -0.00590 -0.02540 146 LEU G CB  
4257 C CG  . LEU D 146 ? 0.34020 0.45450 0.59030 0.02650  -0.01080 -0.02660 146 LEU G CG  
4258 C CD1 . LEU D 146 ? 0.34430 0.44470 0.56110 0.03110  0.00660  -0.03340 146 LEU G CD1 
4259 C CD2 . LEU D 146 ? 0.30100 0.45260 0.62690 0.03310  -0.00800 -0.03810 146 LEU G CD2 
4260 N N   . VAL D 147 ? 0.36630 0.52960 0.66360 -0.03830 0.00510  -0.04280 147 VAL G N   
4261 C CA  . VAL D 147 ? 0.40110 0.55770 0.69190 -0.06620 0.02700  -0.04780 147 VAL G CA  
4262 C C   . VAL D 147 ? 0.44130 0.55260 0.66850 -0.06680 0.05310  -0.03640 147 VAL G C   
4263 O O   . VAL D 147 ? 0.43040 0.54200 0.63970 -0.05050 0.06160  -0.03400 147 VAL G O   
4264 C CB  . VAL D 147 ? 0.36470 0.57730 0.73000 -0.07980 0.04270  -0.06450 147 VAL G CB  
4265 C CG1 . VAL D 147 ? 0.33600 0.56770 0.71740 -0.06660 0.06810  -0.07210 147 VAL G CG1 
4266 C CG2 . VAL D 147 ? 0.40170 0.60560 0.76390 -0.11500 0.06730  -0.06910 147 VAL G CG2 
4267 N N   . GLY D 148 ? 0.47320 0.54430 0.66650 -0.08530 0.06400  -0.02890 148 GLY G N   
4268 C CA  . GLY D 148 ? 0.51770 0.54500 0.65330 -0.08300 0.08500  -0.01040 148 GLY G CA  
4269 C C   . GLY D 148 ? 0.52600 0.57030 0.66400 -0.09930 0.11820  -0.00850 148 GLY G C   
4270 O O   . GLY D 148 ? 0.51740 0.57560 0.68990 -0.12690 0.13570  -0.01660 148 GLY G O   
4271 N N   . GLN D 149 ? 0.58260 0.63060 0.68400 -0.08660 0.12870  -0.00050 149 GLN G N   
4272 C CA  . GLN D 149 ? 0.60020 0.66210 0.68550 -0.10540 0.16390  0.00270  149 GLN G CA  
4273 C C   . GLN D 149 ? 0.66020 0.66300 0.68050 -0.11610 0.17840  0.03710  149 GLN G C   
4274 O O   . GLN D 149 ? 0.68870 0.64830 0.66940 -0.09670 0.15960  0.05750  149 GLN G O   
4275 C CB  . GLN D 149 ? 0.57860 0.67500 0.64750 -0.09070 0.16890  -0.00860 149 GLN G CB  
4276 C CG  . GLN D 149 ? 0.51560 0.65510 0.64980 -0.07400 0.15370  -0.03840 149 GLN G CG  
4277 C CD  . GLN D 149 ? 0.47690 0.66430 0.69170 -0.08830 0.16970  -0.06270 149 GLN G CD  
4278 O OE1 . GLN D 149 ? 0.49850 0.70380 0.71790 -0.11320 0.20430  -0.06760 149 GLN G OE1 
4279 N NE2 . GLN D 149 ? 0.42630 0.63770 0.70780 -0.07240 0.14490  -0.07630 149 GLN G NE2 
4280 N N   . ILE D 150 ? 0.72130 0.72070 0.73590 -0.14670 0.21340  0.04500  150 ILE G N   
4281 C CA  . ILE D 150 ? 0.77920 0.71190 0.73860 -0.16000 0.23000  0.08330  150 ILE G CA  
4282 C C   . ILE D 150 ? 0.82780 0.76520 0.71900 -0.16690 0.25540  0.10710  150 ILE G C   
4283 O O   . ILE D 150 ? 0.81180 0.79150 0.71450 -0.19260 0.28880  0.09220  150 ILE G O   
4284 C CB  . ILE D 150 ? 0.79060 0.70190 0.79230 -0.19680 0.25240  0.07850  150 ILE G CB  
4285 C CG1 . ILE D 150 ? 0.76670 0.67330 0.82050 -0.19080 0.22230  0.05460  150 ILE G CG1 
4286 C CG2 . ILE D 150 ? 0.86580 0.69870 0.81040 -0.21330 0.27730  0.12240  150 ILE G CG2 
4287 C CD1 . ILE D 150 ? 0.76880 0.66710 0.87400 -0.23050 0.23880  0.03860  150 ILE G CD1 
4288 N N   . HIS D 151 ? 1.03640 0.93580 0.85680 -0.14460 0.23970  0.14330  151 HIS G N   
4289 C CA  . HIS D 151 ? 1.09750 0.99870 0.83770 -0.15310 0.25950  0.17340  151 HIS G CA  
4290 C C   . HIS D 151 ? 1.15710 0.99330 0.82930 -0.13250 0.24180  0.22890  151 HIS G C   
4291 O O   . HIS D 151 ? 1.14760 0.97690 0.82050 -0.09670 0.20420  0.23230  151 HIS G O   
4292 C CB  . HIS D 151 ? 1.07250 1.04420 0.79650 -0.14200 0.25290  0.14460  151 HIS G CB  
4293 C CG  . HIS D 151 ? 1.11730 1.11240 0.77070 -0.16670 0.28690  0.15640  151 HIS G CG  
4294 N ND1 . HIS D 151 ? 1.12350 1.12150 0.78210 -0.20680 0.33510  0.15630  151 HIS G ND1 
4295 C CD2 . HIS D 151 ? 1.15290 1.17290 0.72470 -0.16050 0.28090  0.16790  151 HIS G CD2 
4296 C CE1 . HIS D 151 ? 1.18120 1.20680 0.77760 -0.21300 0.34840  0.16600  151 HIS G CE1 
4297 N NE2 . HIS D 151 ? 1.19870 1.23650 0.73370 -0.18890 0.31930  0.17320  151 HIS G NE2 
4298 N N   . ASP D 152 ? 1.26610 1.05630 0.88290 -0.15520 0.27070  0.27380  152 ASP G N   
4299 C CA  . ASP D 152 ? 1.32990 1.06520 0.88390 -0.13400 0.25070  0.33380  152 ASP G CA  
4300 C C   . ASP D 152 ? 1.31750 0.98190 0.91320 -0.10920 0.22910  0.34610  152 ASP G C   
4301 O O   . ASP D 152 ? 1.33100 0.97520 0.90790 -0.07170 0.19410  0.37220  152 ASP G O   
4302 C CB  . ASP D 152 ? 1.34680 1.12690 0.83500 -0.10630 0.22070  0.34550  152 ASP G CB  
4303 C CG  . ASP D 152 ? 1.41550 1.23520 0.83450 -0.12700 0.23210  0.36990  152 ASP G CG  
4304 O OD1 . ASP D 152 ? 1.47720 1.27950 0.89720 -0.15550 0.26330  0.38980  152 ASP G OD1 
4305 O OD2 . ASP D 152 ? 1.42270 1.29630 0.79010 -0.11150 0.21120  0.36810  152 ASP G OD2 
4306 N N   . GLY D 153 ? 1.08350 0.71820 0.74360 -0.13120 0.24860  0.32090  153 GLY G N   
4307 C CA  . GLY D 153 ? 1.07630 0.64740 0.77870 -0.11280 0.23250  0.32140  153 GLY G CA  
4308 C C   . GLY D 153 ? 1.01980 0.61340 0.75480 -0.07640 0.19870  0.29220  153 GLY G C   
4309 O O   . GLY D 153 ? 1.02640 0.56680 0.78010 -0.05200 0.18470  0.30040  153 GLY G O   
4310 N N   . VAL D 154 ? 0.91950 0.59530 0.66890 -0.07150 0.18360  0.25410  154 VAL G N   
4311 C CA  . VAL D 154 ? 0.86050 0.56360 0.65520 -0.04730 0.15420  0.21740  154 VAL G CA  
4312 C C   . VAL D 154 ? 0.81410 0.57880 0.65660 -0.06840 0.15860  0.16920  154 VAL G C   
4313 O O   . VAL D 154 ? 0.80920 0.61550 0.64800 -0.09030 0.17790  0.16100  154 VAL G O   
4314 C CB  . VAL D 154 ? 0.85310 0.59080 0.62320 -0.00860 0.12160  0.22490  154 VAL G CB  
4315 C CG1 . VAL D 154 ? 0.91350 0.60610 0.63460 0.01500  0.11270  0.27960  154 VAL G CG1 
4316 C CG2 . VAL D 154 ? 0.83330 0.64990 0.59010 -0.01470 0.11870  0.20190  154 VAL G CG2 
4317 N N   . SER D 155 ? 0.68970 0.46110 0.57810 -0.06130 0.14140  0.13800  155 SER G N   
4318 C CA  . SER D 155 ? 0.63590 0.47110 0.56780 -0.06810 0.13310  0.09920  155 SER G CA  
4319 C C   . SER D 155 ? 0.61140 0.47800 0.54180 -0.03680 0.10510  0.08870  155 SER G C   
4320 O O   . SER D 155 ? 0.60590 0.44500 0.52230 -0.01350 0.08990  0.09920  155 SER G O   
4321 C CB  . SER D 155 ? 0.62050 0.45050 0.60170 -0.08840 0.13220  0.07260  155 SER G CB  
4322 O OG  . SER D 155 ? 0.63400 0.41900 0.61220 -0.07550 0.11910  0.07090  155 SER G OG  
4323 N N   . LYS D 156 ? 0.56030 0.48440 0.51180 -0.03700 0.10140  0.06650  156 LYS G N   
4324 C CA  . LYS D 156 ? 0.53810 0.49120 0.48880 -0.01280 0.08050  0.05630  156 LYS G CA  
4325 C C   . LYS D 156 ? 0.49230 0.49200 0.49120 -0.01640 0.07670  0.02670  156 LYS G C   
4326 O O   . LYS D 156 ? 0.47370 0.49570 0.50490 -0.03450 0.09110  0.01470  156 LYS G O   
4327 C CB  . LYS D 156 ? 0.55710 0.52460 0.46080 -0.00280 0.08150  0.07100  156 LYS G CB  
4328 C CG  . LYS D 156 ? 0.57840 0.56900 0.46300 -0.02410 0.10720  0.07100  156 LYS G CG  
4329 C CD  . LYS D 156 ? 0.61930 0.62640 0.44270 -0.01630 0.10430  0.08640  156 LYS G CD  
4330 C CE  . LYS D 156 ? 0.65810 0.68160 0.44500 -0.04240 0.13590  0.09100  156 LYS G CE  
4331 N NZ  . LYS D 156 ? 0.69220 0.74270 0.40910 -0.03820 0.13050  0.10180  156 LYS G NZ  
4332 N N   . ALA D 157 ? 0.45240 0.46670 0.46170 0.00170  0.05810  0.01620  157 ALA G N   
4333 C CA  . ALA D 157 ? 0.39120 0.44010 0.44700 0.00350  0.05300  -0.00600 157 ALA G CA  
4334 C C   . ALA D 157 ? 0.36090 0.42170 0.41200 0.02020  0.04230  -0.01390 157 ALA G C   
4335 O O   . ALA D 157 ? 0.36840 0.41200 0.39660 0.03160  0.03030  -0.00460 157 ALA G O   
4336 C CB  . ALA D 157 ? 0.36670 0.41050 0.45630 0.00040  0.03820  -0.00910 157 ALA G CB  
4337 N N   . ASN D 158 ? 0.40630 0.49700 0.48710 0.02050  0.04910  -0.03470 158 ASN G N   
4338 C CA  . ASN D 158 ? 0.37540 0.47850 0.45940 0.03010  0.04380  -0.04940 158 ASN G CA  
4339 C C   . ASN D 158 ? 0.32090 0.41990 0.45460 0.03710  0.03380  -0.05580 158 ASN G C   
4340 O O   . ASN D 158 ? 0.29420 0.40620 0.47540 0.03650  0.03960  -0.06630 158 ASN G O   
4341 C CB  . ASN D 158 ? 0.38410 0.51810 0.46330 0.02290  0.06250  -0.07270 158 ASN G CB  
4342 C CG  . ASN D 158 ? 0.45100 0.59150 0.46490 0.01940  0.06370  -0.06220 158 ASN G CG  
4343 O OD1 . ASN D 158 ? 0.48210 0.59970 0.46320 0.02550  0.05160  -0.03420 158 ASN G OD1 
4344 N ND2 . ASN D 158 ? 0.46430 0.63680 0.45870 0.01010  0.07810  -0.08480 158 ASN G ND2 
4345 N N   . PHE D 159 ? 0.37770 0.45950 0.50310 0.04410  0.01960  -0.04690 159 PHE G N   
4346 C CA  . PHE D 159 ? 0.34580 0.41740 0.50620 0.04920  0.01060  -0.04550 159 PHE G CA  
4347 C C   . PHE D 159 ? 0.33160 0.40920 0.51080 0.05110  0.01720  -0.06480 159 PHE G C   
4348 O O   . PHE D 159 ? 0.34310 0.42640 0.49750 0.04990  0.01670  -0.07050 159 PHE G O   
4349 C CB  . PHE D 159 ? 0.35120 0.40020 0.48710 0.05010  -0.00280 -0.02640 159 PHE G CB  
4350 C CG  . PHE D 159 ? 0.38010 0.42080 0.50220 0.04440  -0.00990 -0.01400 159 PHE G CG  
4351 C CD1 . PHE D 159 ? 0.41330 0.44360 0.50160 0.04060  -0.00510 -0.01030 159 PHE G CD1 
4352 C CD2 . PHE D 159 ? 0.38820 0.43090 0.53330 0.04240  -0.02310 -0.00580 159 PHE G CD2 
4353 C CE1 . PHE D 159 ? 0.44990 0.46830 0.52960 0.03080  -0.00870 -0.00480 159 PHE G CE1 
4354 C CE2 . PHE D 159 ? 0.41840 0.46030 0.55260 0.03260  -0.03150 -0.00070 159 PHE G CE2 
4355 C CZ  . PHE D 159 ? 0.45540 0.48330 0.55750 0.02460  -0.02190 -0.00320 159 PHE G CZ  
4356 N N   . SER D 160 ? 0.40810 0.48510 0.63770 0.05420  0.02290  -0.07620 160 SER G N   
4357 C CA  . SER D 160 ? 0.40610 0.48100 0.66300 0.05290  0.03290  -0.09960 160 SER G CA  
4358 C C   . SER D 160 ? 0.40990 0.45300 0.68230 0.05540  0.02450  -0.08130 160 SER G C   
4359 O O   . SER D 160 ? 0.41110 0.43550 0.70510 0.06310  0.01450  -0.05800 160 SER G O   
4360 C CB  . SER D 160 ? 0.39440 0.47920 0.70480 0.05560  0.04980  -0.12590 160 SER G CB  
4361 O OG  . SER D 160 ? 0.40160 0.47570 0.74390 0.05250  0.06160  -0.15210 160 SER G OG  
4362 N N   . ILE D 161 ? 0.38820 0.42890 0.64920 0.04740  0.02810  -0.09050 161 ILE G N   
4363 C CA  . ILE D 161 ? 0.40830 0.41870 0.67920 0.04380  0.02700  -0.07380 161 ILE G CA  
4364 C C   . ILE D 161 ? 0.41990 0.42110 0.73390 0.03490  0.04320  -0.10190 161 ILE G C   
4365 O O   . ILE D 161 ? 0.41260 0.44320 0.72310 0.02510  0.05030  -0.13540 161 ILE G O   
4366 C CB  . ILE D 161 ? 0.42100 0.43800 0.64880 0.03800  0.02200  -0.06210 161 ILE G CB  
4367 C CG1 . ILE D 161 ? 0.43240 0.44820 0.62120 0.04450  0.00920  -0.03790 161 ILE G CG1 
4368 C CG2 . ILE D 161 ? 0.46030 0.45090 0.69850 0.02810  0.02930  -0.05070 161 ILE G CG2 
4369 C CD1 . ILE D 161 ? 0.44640 0.43990 0.64490 0.04920  -0.00100 -0.01280 161 ILE G CD1 
4370 N N   . GLY D 162 ? 0.46480 0.42460 0.81880 0.03730  0.04800  -0.08770 162 GLY G N   
4371 C CA  . GLY D 162 ? 0.48370 0.42230 0.88490 0.02610  0.06720  -0.11450 162 GLY G CA  
4372 C C   . GLY D 162 ? 0.50720 0.40580 0.97130 0.03930  0.07460  -0.11090 162 GLY G C   
4373 O O   . GLY D 162 ? 0.48550 0.38300 0.95990 0.05890  0.06180  -0.08790 162 GLY G O   
4374 N N   . PRO D 163 ? 0.62420 0.49480 1.13330 0.02760  0.09410  -0.13210 163 PRO G N   
4375 C CA  . PRO D 163 ? 0.64050 0.51410 1.15510 0.00100  0.11110  -0.16620 163 PRO G CA  
4376 C C   . PRO D 163 ? 0.64220 0.50580 1.12280 -0.01230 0.10730  -0.13750 163 PRO G C   
4377 O O   . PRO D 163 ? 0.67030 0.48980 1.14530 -0.00740 0.10370  -0.08960 163 PRO G O   
4378 C CB  . PRO D 163 ? 0.67720 0.51830 1.24450 -0.00470 0.12890  -0.17250 163 PRO G CB  
4379 C CG  . PRO D 163 ? 0.70310 0.51080 1.28680 0.02090  0.11700  -0.12630 163 PRO G CG  
4380 C CD  . PRO D 163 ? 0.65460 0.49960 1.21120 0.03820  0.09830  -0.12090 163 PRO G CD  
4381 N N   . MET D 164 ? 0.43240 0.34660 0.88560 -0.02870 0.10630  -0.16410 164 MET G N   
4382 C CA  . MET D 164 ? 0.44990 0.37550 0.86850 -0.03920 0.10300  -0.14070 164 MET G CA  
4383 C C   . MET D 164 ? 0.49200 0.36750 0.93960 -0.05990 0.12410  -0.12570 164 MET G C   
4384 O O   . MET D 164 ? 0.49230 0.35050 0.99090 -0.07920 0.14390  -0.15830 164 MET G O   
4385 C CB  . MET D 164 ? 0.43090 0.42540 0.83520 -0.04980 0.09760  -0.17730 164 MET G CB  
4386 C CG  . MET D 164 ? 0.44260 0.46030 0.81620 -0.05300 0.09320  -0.15630 164 MET G CG  
4387 S SD  . MET D 164 ? 0.44350 0.45250 0.75670 -0.02630 0.07410  -0.11040 164 MET G SD  
4388 C CE  . MET D 164 ? 0.44930 0.48150 0.74090 -0.03490 0.08000  -0.09960 164 MET G CE  
4389 N N   . MET D 165 ? 0.47570 0.32650 0.88720 -0.05910 0.12220  -0.07740 165 MET G N   
4390 C CA  . MET D 165 ? 0.50880 0.32320 0.92940 -0.08470 0.14530  -0.05920 165 MET G CA  
4391 C C   . MET D 165 ? 0.52930 0.36200 0.88870 -0.08690 0.14180  -0.02730 165 MET G C   
4392 O O   . MET D 165 ? 0.51440 0.38060 0.83170 -0.06780 0.12100  -0.02130 165 MET G O   
4393 C CB  . MET D 165 ? 0.56780 0.29960 1.01800 -0.08260 0.15520  -0.02510 165 MET G CB  
4394 C CG  . MET D 165 ? 0.57080 0.27870 1.00440 -0.04920 0.13010  0.01430  165 MET G CG  
4395 S SD  . MET D 165 ? 0.58920 0.29650 0.93640 -0.04290 0.11080  0.07730  165 MET G SD  
4396 C CE  . MET D 165 ? 0.69080 0.31470 1.03740 -0.06100 0.13070  0.13230  165 MET G CE  
4397 N N   . PHE D 166 ? 0.53940 0.34750 0.89500 -0.11300 0.16650  -0.00890 166 PHE G N   
4398 C CA  . PHE D 166 ? 0.53450 0.37320 0.84120 -0.12190 0.17320  0.00380  166 PHE G CA  
4399 C C   . PHE D 166 ? 0.53820 0.36520 0.77400 -0.10190 0.15240  0.04570  166 PHE G C   
4400 O O   . PHE D 166 ? 0.51740 0.38150 0.71310 -0.10090 0.15190  0.04190  166 PHE G O   
4401 C CB  . PHE D 166 ? 0.59840 0.40970 0.91320 -0.15820 0.21010  0.01710  166 PHE G CB  
4402 C CG  . PHE D 166 ? 0.68220 0.41170 0.96790 -0.16390 0.21770  0.07640  166 PHE G CG  
4403 C CD1 . PHE D 166 ? 0.72470 0.39360 1.05520 -0.16090 0.21830  0.08660  166 PHE G CD1 
4404 C CD2 . PHE D 166 ? 0.73060 0.44470 0.94250 -0.17260 0.22470  0.12130  166 PHE G CD2 
4405 C CE1 . PHE D 166 ? 0.81380 0.41730 1.10940 -0.15750 0.21420  0.14370  166 PHE G CE1 
4406 C CE2 . PHE D 166 ? 0.82300 0.46250 0.99980 -0.17870 0.22840  0.18360  166 PHE G CE2 
4407 C CZ  . PHE D 166 ? 0.86380 0.45310 1.08070 -0.16700 0.21620  0.19450  166 PHE G CZ  
4408 N N   . ALA D 167 ? 0.57040 0.34870 0.79480 -0.08640 0.13540  0.08330  167 ALA G N   
4409 C CA  . ALA D 167 ? 0.58320 0.36090 0.74330 -0.06990 0.11060  0.11840  167 ALA G CA  
4410 C C   . ALA D 167 ? 0.54190 0.36930 0.69470 -0.04780 0.08720  0.09090  167 ALA G C   
4411 O O   . ALA D 167 ? 0.55310 0.39240 0.65210 -0.04110 0.07190  0.10630  167 ALA G O   
4412 C CB  . ALA D 167 ? 0.62970 0.35350 0.79100 -0.05530 0.09190  0.16580  167 ALA G CB  
4413 N N   . LEU D 168 ? 0.51990 0.37530 0.72130 -0.03930 0.08530  0.05040  168 LEU G N   
4414 C CA  . LEU D 168 ? 0.48350 0.38120 0.67560 -0.02090 0.06660  0.02840  168 LEU G CA  
4415 C C   . LEU D 168 ? 0.47950 0.42460 0.66470 -0.02550 0.07450  -0.00130 168 LEU G C   
4416 O O   . LEU D 168 ? 0.45540 0.42880 0.62500 -0.01060 0.06060  -0.01230 168 LEU G O   
4417 C CB  . LEU D 168 ? 0.44160 0.34450 0.68130 -0.00810 0.05920  0.00490  168 LEU G CB  
4418 C CG  . LEU D 168 ? 0.45230 0.30980 0.72040 0.00170  0.05330  0.03000  168 LEU G CG  
4419 C CD1 . LEU D 168 ? 0.40960 0.27430 0.73360 0.01110  0.05590  -0.00450 168 LEU G CD1 
4420 C CD2 . LEU D 168 ? 0.46320 0.31620 0.69570 0.01690  0.02870  0.06610  168 LEU G CD2 
4421 N N   . ALA D 169 ? 0.46040 0.41490 0.66260 -0.04530 0.09700  -0.01300 169 ALA G N   
4422 C CA  . ALA D 169 ? 0.43280 0.43940 0.64340 -0.04680 0.10360  -0.04090 169 ALA G CA  
4423 C C   . ALA D 169 ? 0.44530 0.45410 0.60790 -0.04570 0.10970  -0.02640 169 ALA G C   
4424 O O   . ALA D 169 ? 0.49370 0.46770 0.61670 -0.05720 0.11860  0.00210  169 ALA G O   
4425 C CB  . ALA D 169 ? 0.42010 0.44480 0.68040 -0.07120 0.12690  -0.06430 169 ALA G CB  
4426 N N   . GLY D 170 ? 0.39840 0.40930 0.42450 0.01280  0.07070  0.07800  170 GLY G N   
4427 C CA  . GLY D 170 ? 0.39410 0.40770 0.40640 0.01760  0.07490  0.07850  170 GLY G CA  
4428 C C   . GLY D 170 ? 0.40070 0.40720 0.40480 0.02440  0.07700  0.07130  170 GLY G C   
4429 O O   . GLY D 170 ? 0.39760 0.39900 0.40410 0.02360  0.07560  0.06760  170 GLY G O   
4430 N N   . THR D 171 ? 0.41640 0.42100 0.40810 0.02940  0.07990  0.06940  171 THR G N   
4431 C CA  . THR D 171 ? 0.42740 0.42230 0.40990 0.03600  0.08000  0.06350  171 THR G CA  
4432 C C   . THR D 171 ? 0.43050 0.40970 0.40450 0.03310  0.07720  0.06010  171 THR G C   
4433 O O   . THR D 171 ? 0.43490 0.41140 0.40380 0.03120  0.07640  0.06110  171 THR G O   
4434 C CB  . THR D 171 ? 0.43950 0.44010 0.41570 0.04400  0.08460  0.06040  171 THR G CB  
4435 O OG1 . THR D 171 ? 0.43120 0.45150 0.42040 0.04590  0.08830  0.06210  171 THR G OG1 
4436 C CG2 . THR D 171 ? 0.45310 0.43920 0.42150 0.05160  0.08150  0.05450  171 THR G CG2 
4437 N N   . TYR D 172 ? 0.42010 0.38930 0.39130 0.03090  0.07520  0.05640  172 TYR G N   
4438 C CA  . TYR D 172 ? 0.42200 0.37960 0.38740 0.02630  0.07380  0.05200  172 TYR G CA  
4439 C C   . TYR D 172 ? 0.43800 0.38090 0.38590 0.02900  0.07220  0.04920  172 TYR G C   
4440 O O   . TYR D 172 ? 0.44710 0.38600 0.39000 0.03330  0.07020  0.05000  172 TYR G O   
4441 C CB  . TYR D 172 ? 0.42080 0.37920 0.39560 0.01770  0.07430  0.04790  172 TYR G CB  
4442 C CG  . TYR D 172 ? 0.41840 0.38630 0.41330 0.01490  0.07370  0.04780  172 TYR G CG  
4443 C CD1 . TYR D 172 ? 0.40720 0.38390 0.41180 0.01520  0.07350  0.05210  172 TYR G CD1 
4444 C CD2 . TYR D 172 ? 0.42060 0.38790 0.42720 0.01180  0.07170  0.04310  172 TYR G CD2 
4445 C CE1 . TYR D 172 ? 0.40420 0.38540 0.42730 0.01240  0.07070  0.05210  172 TYR G CE1 
4446 C CE2 . TYR D 172 ? 0.41950 0.39250 0.44810 0.01050  0.06810  0.04240  172 TYR G CE2 
4447 C CZ  . TYR D 172 ? 0.41530 0.39350 0.45070 0.01070  0.06740  0.04700  172 TYR G CZ  
4448 O OH  . TYR D 172 ? 0.42710 0.40690 0.48390 0.00930  0.06170  0.04670  172 TYR G OH  
4449 N N   . ARG D 173 ? 0.49830 0.43170 0.43820 0.02620  0.07100  0.04610  173 ARG G N   
4450 C CA  . ARG D 173 ? 0.51550 0.43100 0.43770 0.02550  0.06810  0.04340  173 ARG G CA  
4451 C C   . ARG D 173 ? 0.51840 0.42950 0.44000 0.01450  0.06800  0.03930  173 ARG G C   
4452 O O   . ARG D 173 ? 0.51540 0.43650 0.45140 0.01170  0.06900  0.03770  173 ARG G O   
4453 C CB  . ARG D 173 ? 0.52450 0.43260 0.43510 0.03460  0.06700  0.04220  173 ARG G CB  
4454 C CG  . ARG D 173 ? 0.52220 0.44350 0.43980 0.04430  0.07050  0.04350  173 ARG G CG  
4455 C CD  . ARG D 173 ? 0.53610 0.45220 0.44390 0.05370  0.07160  0.03840  173 ARG G CD  
4456 N NE  . ARG D 173 ? 0.57190 0.47230 0.47500 0.05970  0.06580  0.03560  173 ARG G NE  
4457 C CZ  . ARG D 173 ? 0.58480 0.47850 0.48510 0.07080  0.06480  0.02890  173 ARG G CZ  
4458 N NH1 . ARG D 173 ? 0.58580 0.49180 0.48710 0.07680  0.07270  0.02280  173 ARG G NH1 
4459 N NH2 . ARG D 173 ? 0.59320 0.46660 0.48940 0.07520  0.05510  0.02760  173 ARG G NH2 
4460 N N   . CYS D 174 ? 0.52370 0.42030 0.43040 0.00730  0.06600  0.03760  174 CYS G N   
4461 C CA  . CYS D 174 ? 0.52960 0.42510 0.43660 -0.00450 0.06740  0.03240  174 CYS G CA  
4462 C C   . CYS D 174 ? 0.54820 0.42310 0.43400 -0.00670 0.06230  0.03230  174 CYS G C   
4463 O O   . CYS D 174 ? 0.55510 0.41360 0.42530 0.00050  0.05700  0.03540  174 CYS G O   
4464 C CB  . CYS D 174 ? 0.52920 0.43040 0.43920 -0.01840 0.07230  0.02820  174 CYS G CB  
4465 S SG  . CYS D 174 ? 0.54960 0.42930 0.42970 -0.02900 0.06820  0.03210  174 CYS G SG  
4466 N N   . TYR D 175 ? 0.51610 0.39270 0.40470 -0.01680 0.06320  0.02770  175 TYR G N   
4467 C CA  . TYR D 175 ? 0.52800 0.38820 0.40100 -0.01920 0.05790  0.02700  175 TYR G CA  
4468 C C   . TYR D 175 ? 0.54070 0.40290 0.41390 -0.03740 0.06040  0.02190  175 TYR G C   
4469 O O   . TYR D 175 ? 0.53220 0.41540 0.42710 -0.04450 0.06720  0.01610  175 TYR G O   
4470 C CB  . TYR D 175 ? 0.52830 0.39400 0.40930 -0.01120 0.05520  0.02670  175 TYR G CB  
4471 C CG  . TYR D 175 ? 0.52070 0.38800 0.40020 0.00330  0.05490  0.03030  175 TYR G CG  
4472 C CD1 . TYR D 175 ? 0.50920 0.39530 0.40760 0.00790  0.05800  0.03270  175 TYR G CD1 
4473 C CD2 . TYR D 175 ? 0.52430 0.37500 0.38420 0.01150  0.05190  0.03000  175 TYR G CD2 
4474 C CE1 . TYR D 175 ? 0.49930 0.38920 0.39490 0.01790  0.05910  0.03590  175 TYR G CE1 
4475 C CE2 . TYR D 175 ? 0.51700 0.37350 0.37660 0.02280  0.05440  0.03070  175 TYR G CE2 
4476 C CZ  . TYR D 175 ? 0.50600 0.38300 0.38260 0.02500  0.05850  0.03420  175 TYR G CZ  
4477 O OH  . TYR D 175 ? 0.50530 0.38990 0.37980 0.03320  0.06220  0.03480  175 TYR G OH  
4478 N N   . GLY D 176 ? 0.52250 0.36340 0.37300 -0.04540 0.05510  0.02290  176 GLY G N   
4479 C CA  . GLY D 176 ? 0.53200 0.37530 0.38110 -0.06490 0.05760  0.01790  176 GLY G CA  
4480 C C   . GLY D 176 ? 0.54420 0.38200 0.39290 -0.06480 0.05170  0.01630  176 GLY G C   
4481 O O   . GLY D 176 ? 0.54910 0.36980 0.38460 -0.05280 0.04430  0.01980  176 GLY G O   
4482 N N   . SER D 177 ? 0.56680 0.42080 0.43160 -0.07870 0.05520  0.00950  177 SER G N   
4483 C CA  . SER D 177 ? 0.58970 0.43690 0.45160 -0.08370 0.04830  0.00810  177 SER G CA  
4484 C C   . SER D 177 ? 0.58820 0.43640 0.44400 -0.10780 0.05190  0.00360  177 SER G C   
4485 O O   . SER D 177 ? 0.57920 0.44470 0.44430 -0.12070 0.06240  -0.00170 177 SER G O   
4486 C CB  . SER D 177 ? 0.59660 0.46610 0.49090 -0.07590 0.04560  0.00430  177 SER G CB  
4487 O OG  . SER D 177 ? 0.58500 0.48550 0.51540 -0.08370 0.05300  -0.00480 177 SER G OG  
4488 N N   . VAL D 178 ? 0.62990 0.45910 0.46780 -0.11550 0.04350  0.00530  178 VAL G N   
4489 C CA  . VAL D 178 ? 0.63940 0.46730 0.46810 -0.14100 0.04570  0.00220  178 VAL G CA  
4490 C C   . VAL D 178 ? 0.64320 0.49560 0.50240 -0.14750 0.04530  -0.00580 178 VAL G C   
4491 O O   . VAL D 178 ? 0.65120 0.50800 0.52600 -0.13280 0.03770  -0.00560 178 VAL G O   
4492 C CB  . VAL D 178 ? 0.65960 0.44450 0.44440 -0.14860 0.03460  0.01050  178 VAL G CB  
4493 C CG1 . VAL D 178 ? 0.65260 0.41150 0.41250 -0.13790 0.03070  0.01870  178 VAL G CG1 
4494 C CG2 . VAL D 178 ? 0.67670 0.44400 0.45450 -0.13940 0.02250  0.01160  178 VAL G CG2 
4495 N N   . THR D 179 ? 0.69990 0.56860 0.56670 -0.17170 0.05290  -0.01300 179 THR G N   
4496 C CA  . THR D 179 ? 0.69990 0.60330 0.60760 -0.18070 0.05600  -0.02440 179 THR G CA  
4497 C C   . THR D 179 ? 0.71800 0.61860 0.63870 -0.16940 0.04110  -0.02250 179 THR G C   
4498 O O   . THR D 179 ? 0.70640 0.63470 0.66930 -0.15970 0.03910  -0.02870 179 THR G O   
4499 C CB  . THR D 179 ? 0.69740 0.60500 0.59410 -0.21220 0.06290  -0.02910 179 THR G CB  
4500 O OG1 . THR D 179 ? 0.67650 0.59530 0.56660 -0.22630 0.07860  -0.03350 179 THR G OG1 
4501 C CG2 . THR D 179 ? 0.68330 0.62750 0.62470 -0.22170 0.06460  -0.04170 179 THR G CG2 
4502 N N   . HIS D 180 ? 0.55860 0.42480 0.44370 -0.17150 0.02920  -0.01450 180 HIS G N   
4503 C CA  . HIS D 180 ? 0.57100 0.43430 0.46380 -0.16850 0.01530  -0.01400 180 HIS G CA  
4504 C C   . HIS D 180 ? 0.57890 0.42240 0.45810 -0.14500 0.00450  -0.00700 180 HIS G C   
4505 O O   . HIS D 180 ? 0.58970 0.42800 0.47000 -0.14270 -0.00810 -0.00580 180 HIS G O   
4506 C CB  . HIS D 180 ? 0.59100 0.42960 0.45370 -0.18850 0.00830  -0.01170 180 HIS G CB  
4507 C CG  . HIS D 180 ? 0.59720 0.45850 0.47320 -0.21600 0.01880  -0.01900 180 HIS G CG  
4508 N ND1 . HIS D 180 ? 0.62510 0.46550 0.46550 -0.23590 0.02380  -0.01510 180 HIS G ND1 
4509 C CD2 . HIS D 180 ? 0.58280 0.48720 0.50470 -0.22820 0.02540  -0.03080 180 HIS G CD2 
4510 C CE1 . HIS D 180 ? 0.62860 0.49890 0.48850 -0.26150 0.03500  -0.02410 180 HIS G CE1 
4511 N NE2 . HIS D 180 ? 0.60150 0.51330 0.51380 -0.25630 0.03730  -0.03510 180 HIS G NE2 
4512 N N   . THR D 181 ? 0.60660 0.43990 0.47240 -0.12940 0.00930  -0.00250 181 THR G N   
4513 C CA  . THR D 181 ? 0.60630 0.42700 0.46180 -0.10880 0.00250  0.00260  181 THR G CA  
4514 C C   . THR D 181 ? 0.59280 0.43590 0.47320 -0.09550 0.01030  0.00260  181 THR G C   
4515 O O   . THR D 181 ? 0.58050 0.41240 0.44470 -0.08350 0.01460  0.00660  181 THR G O   
4516 C CB  . THR D 181 ? 0.61170 0.39340 0.42300 -0.10240 -0.00090 0.00710  181 THR G CB  
4517 O OG1 . THR D 181 ? 0.60710 0.37990 0.40580 -0.10690 0.00670  0.00860  181 THR G OG1 
4518 C CG2 . THR D 181 ? 0.63200 0.38830 0.41920 -0.11350 -0.01210 0.00660  181 THR G CG2 
4519 N N   . PRO D 182 ? 0.57110 0.44630 0.49400 -0.09700 0.01100  -0.00260 182 PRO G N   
4520 C CA  . PRO D 182 ? 0.55210 0.44840 0.50150 -0.08660 0.01860  -0.00410 182 PRO G CA  
4521 C C   . PRO D 182 ? 0.56290 0.44930 0.50200 -0.06880 0.01370  0.00390  182 PRO G C   
4522 O O   . PRO D 182 ? 0.54700 0.44190 0.49460 -0.06050 0.02110  0.00470  182 PRO G O   
4523 C CB  . PRO D 182 ? 0.55000 0.47910 0.54970 -0.09130 0.01590  -0.01290 182 PRO G CB  
4524 C CG  . PRO D 182 ? 0.56220 0.48410 0.55920 -0.09780 0.00140  -0.01140 182 PRO G CG  
4525 C CD  . PRO D 182 ? 0.57810 0.47180 0.53020 -0.10780 0.00360  -0.00830 182 PRO G CD  
4526 N N   . TYR D 183 ? 0.62770 0.49750 0.54790 -0.06470 0.00190  0.00930  183 TYR G N   
4527 C CA  . TYR D 183 ? 0.62470 0.48580 0.53030 -0.05150 -0.00150 0.01630  183 TYR G CA  
4528 C C   . TYR D 183 ? 0.60780 0.44460 0.47400 -0.04510 0.00430  0.01830  183 TYR G C   
4529 O O   . TYR D 183 ? 0.59530 0.42690 0.44780 -0.03520 0.00450  0.02220  183 TYR G O   
4530 C CB  . TYR D 183 ? 0.63380 0.49050 0.53760 -0.05270 -0.01730 0.02040  183 TYR G CB  
4531 C CG  . TYR D 183 ? 0.64470 0.52390 0.59200 -0.05750 -0.02760 0.01840  183 TYR G CG  
4532 C CD1 . TYR D 183 ? 0.63430 0.53600 0.61990 -0.05200 -0.02470 0.01640  183 TYR G CD1 
4533 C CD2 . TYR D 183 ? 0.65950 0.53760 0.61260 -0.06730 -0.04100 0.01710  183 TYR G CD2 
4534 C CE1 . TYR D 183 ? 0.63820 0.56100 0.67020 -0.05430 -0.03540 0.01230  183 TYR G CE1 
4535 C CE2 . TYR D 183 ? 0.66830 0.56910 0.66790 -0.07030 -0.05230 0.01400  183 TYR G CE2 
4536 C CZ  . TYR D 183 ? 0.64750 0.57080 0.68820 -0.06300 -0.04940 0.01100  183 TYR G CZ  
4537 O OH  . TYR D 183 ? 0.64010 0.58650 0.73340 -0.06380 -0.06170 0.00560  183 TYR G OH  
4538 N N   . GLN D 184 ? 0.65270 0.47490 0.50180 -0.05110 0.00830  0.01540  184 GLN G N   
4539 C CA  . GLN D 184 ? 0.64610 0.44530 0.46510 -0.04360 0.01220  0.01600  184 GLN G CA  
4540 C C   . GLN D 184 ? 0.63240 0.43950 0.46010 -0.04140 0.02180  0.01680  184 GLN G C   
4541 O O   . GLN D 184 ? 0.63810 0.45260 0.47560 -0.05340 0.02540  0.01490  184 GLN G O   
4542 C CB  . GLN D 184 ? 0.65750 0.42910 0.44980 -0.05190 0.00640  0.01360  184 GLN G CB  
4543 C CG  . GLN D 184 ? 0.67220 0.43380 0.45210 -0.05470 -0.00360 0.01220  184 GLN G CG  
4544 C CD  . GLN D 184 ? 0.69040 0.42070 0.44110 -0.06150 -0.01020 0.00910  184 GLN G CD  
4545 O OE1 . GLN D 184 ? 0.68710 0.39600 0.42010 -0.05770 -0.00850 0.00810  184 GLN G OE1 
4546 N NE2 . GLN D 184 ? 0.70780 0.43330 0.45390 -0.07170 -0.01980 0.00790  184 GLN G NE2 
4547 N N   . LEU D 185 ? 0.53140 0.33840 0.35520 -0.02790 0.02610  0.01900  185 LEU G N   
4548 C CA  . LEU D 185 ? 0.51970 0.33350 0.35080 -0.02520 0.03330  0.02060  185 LEU G CA  
4549 C C   . LEU D 185 ? 0.52440 0.31330 0.33160 -0.01930 0.03160  0.02130  185 LEU G C   
4550 O O   . LEU D 185 ? 0.53300 0.30360 0.32250 -0.01150 0.02730  0.01900  185 LEU G O   
4551 C CB  . LEU D 185 ? 0.50180 0.33630 0.35150 -0.01490 0.03810  0.02310  185 LEU G CB  
4552 C CG  . LEU D 185 ? 0.49840 0.35830 0.37980 -0.02010 0.04000  0.02230  185 LEU G CG  
4553 C CD1 . LEU D 185 ? 0.51650 0.38080 0.40850 -0.02790 0.03260  0.02000  185 LEU G CD1 
4554 C CD2 . LEU D 185 ? 0.48230 0.35620 0.37730 -0.01010 0.04190  0.02630  185 LEU G CD2 
4555 N N   . SER D 186 ? 0.49910 0.28740 0.30720 -0.02300 0.03430  0.02360  186 SER G N   
4556 C CA  . SER D 186 ? 0.51530 0.28090 0.30630 -0.01660 0.02970  0.02570  186 SER G CA  
4557 C C   . SER D 186 ? 0.50970 0.27930 0.30530 0.00310  0.03150  0.02430  186 SER G C   
4558 O O   . SER D 186 ? 0.49110 0.28150 0.30000 0.00920  0.03740  0.02340  186 SER G O   
4559 C CB  . SER D 186 ? 0.51230 0.28090 0.30480 -0.02570 0.03160  0.02990  186 SER G CB  
4560 O OG  . SER D 186 ? 0.48450 0.28200 0.30030 -0.02160 0.04040  0.02990  186 SER G OG  
4561 N N   . ALA D 187 ? 0.54780 0.29700 0.33310 0.01220  0.02550  0.02380  187 ALA G N   
4562 C CA  . ALA D 187 ? 0.54220 0.30240 0.33950 0.02930  0.02910  0.02200  187 ALA G CA  
4563 C C   . ALA D 187 ? 0.52190 0.30790 0.33790 0.02680  0.03580  0.02750  187 ALA G C   
4564 O O   . ALA D 187 ? 0.51920 0.30660 0.33500 0.01330  0.03550  0.03170  187 ALA G O   
4565 C CB  . ALA D 187 ? 0.56260 0.29750 0.35280 0.03910  0.01900  0.02040  187 ALA G CB  
4566 N N   . PRO D 188 ? 0.49450 0.30170 0.32590 0.03790  0.04250  0.02650  188 PRO G N   
4567 C CA  . PRO D 188 ? 0.48150 0.31130 0.33020 0.03490  0.04790  0.03150  188 PRO G CA  
4568 C C   . PRO D 188 ? 0.48370 0.30610 0.33290 0.03480  0.04250  0.03550  188 PRO G C   
4569 O O   . PRO D 188 ? 0.49800 0.30440 0.34260 0.04400  0.03480  0.03440  188 PRO G O   
4570 C CB  . PRO D 188 ? 0.46950 0.32040 0.33080 0.04540  0.05520  0.02990  188 PRO G CB  
4571 C CG  . PRO D 188 ? 0.48880 0.32820 0.34130 0.05710  0.05400  0.02260  188 PRO G CG  
4572 C CD  . PRO D 188 ? 0.49980 0.31280 0.33260 0.05120  0.04680  0.02000  188 PRO G CD  
4573 N N   . SER D 189 ? 0.48130 0.31470 0.33670 0.02410  0.04530  0.03950  189 SER G N   
4574 C CA  . SER D 189 ? 0.49000 0.31920 0.34490 0.02250  0.04000  0.04420  189 SER G CA  
4575 C C   . SER D 189 ? 0.48730 0.32910 0.35880 0.03880  0.04000  0.04430  189 SER G C   
4576 O O   . SER D 189 ? 0.47230 0.33240 0.35640 0.04730  0.04780  0.04100  189 SER G O   
4577 C CB  . SER D 189 ? 0.47930 0.32250 0.33920 0.00830  0.04580  0.04590  189 SER G CB  
4578 O OG  . SER D 189 ? 0.46050 0.32940 0.34210 0.01410  0.05420  0.04460  189 SER G OG  
4579 N N   . ASP D 190 ? 0.54890 0.38100 0.42010 0.04140  0.03020  0.04820  190 ASP G N   
4580 C CA  . ASP D 190 ? 0.54300 0.39290 0.43540 0.05430  0.03050  0.04820  190 ASP G CA  
4581 C C   . ASP D 190 ? 0.52250 0.40120 0.42950 0.05030  0.04250  0.04930  190 ASP G C   
4582 O O   . ASP D 190 ? 0.51610 0.39710 0.41830 0.03660  0.04570  0.05150  190 ASP G O   
4583 C CB  . ASP D 190 ? 0.56310 0.39990 0.45430 0.05360  0.01600  0.05440  190 ASP G CB  
4584 C CG  . ASP D 190 ? 0.58760 0.39310 0.46840 0.06010  -0.00010 0.05410  190 ASP G CG  
4585 O OD1 . ASP D 190 ? 0.58980 0.38500 0.46580 0.06690  0.00130  0.04740  190 ASP G OD1 
4586 O OD2 . ASP D 190 ? 0.60350 0.39240 0.48040 0.05790  -0.01610 0.06080  190 ASP G OD2 
4587 N N   . PRO D 191 ? 0.49550 0.39630 0.42080 0.06070  0.04920  0.04680  191 PRO G N   
4588 C CA  . PRO D 191 ? 0.47620 0.39990 0.41310 0.05540  0.05850  0.04910  191 PRO G CA  
4589 C C   . PRO D 191 ? 0.47500 0.40570 0.41960 0.04890  0.05560  0.05420  191 PRO G C   
4590 O O   . PRO D 191 ? 0.48890 0.41420 0.43550 0.05170  0.04680  0.05660  191 PRO G O   
4591 C CB  . PRO D 191 ? 0.47150 0.41470 0.42140 0.06590  0.06560  0.04560  191 PRO G CB  
4592 C CG  . PRO D 191 ? 0.48760 0.42510 0.44330 0.07870  0.05930  0.04100  191 PRO G CG  
4593 C CD  . PRO D 191 ? 0.50230 0.40860 0.43940 0.07660  0.04870  0.04100  191 PRO G CD  
4594 N N   . LEU D 192 ? 0.51360 0.45470 0.46300 0.03970  0.06150  0.05540  192 LEU G N   
4595 C CA  . LEU D 192 ? 0.51220 0.46110 0.46890 0.03240  0.06050  0.05840  192 LEU G CA  
4596 C C   . LEU D 192 ? 0.49080 0.46050 0.46490 0.03330  0.06680  0.05990  192 LEU G C   
4597 O O   . LEU D 192 ? 0.47450 0.44700 0.45100 0.03020  0.07130  0.05850  192 LEU G O   
4598 C CB  . LEU D 192 ? 0.51450 0.45320 0.45970 0.01810  0.06120  0.05600  192 LEU G CB  
4599 C CG  . LEU D 192 ? 0.52590 0.46430 0.46820 0.00740  0.05850  0.05730  192 LEU G CG  
4600 C CD1 . LEU D 192 ? 0.55110 0.47950 0.48580 0.01030  0.04680  0.06320  192 LEU G CD1 
4601 C CD2 . LEU D 192 ? 0.52260 0.45180 0.45070 -0.00830 0.06230  0.05140  192 LEU G CD2 
4602 N N   . ASP D 193 ? 0.53690 0.52030 0.52390 0.03640  0.06530  0.06320  193 ASP G N   
4603 C CA  . ASP D 193 ? 0.51630 0.51770 0.51790 0.03410  0.07010  0.06610  193 ASP G CA  
4604 C C   . ASP D 193 ? 0.50720 0.50670 0.51160 0.02340  0.06880  0.06630  193 ASP G C   
4605 O O   . ASP D 193 ? 0.51720 0.51350 0.51940 0.01920  0.06400  0.06690  193 ASP G O   
4606 C CB  . ASP D 193 ? 0.51690 0.53690 0.53320 0.04030  0.07010  0.06860  193 ASP G CB  
4607 C CG  . ASP D 193 ? 0.53490 0.56210 0.55230 0.05050  0.07480  0.06480  193 ASP G CG  
4608 O OD1 . ASP D 193 ? 0.52300 0.54100 0.52790 0.05130  0.07830  0.06200  193 ASP G OD1 
4609 O OD2 . ASP D 193 ? 0.53710 0.58040 0.56940 0.05750  0.07520  0.06330  193 ASP G OD2 
4610 N N   . ILE D 194 ? 0.43280 0.43270 0.44200 0.01870  0.07180  0.06500  194 ILE G N   
4611 C CA  . ILE D 194 ? 0.43250 0.43180 0.44920 0.01000  0.07130  0.06230  194 ILE G CA  
4612 C C   . ILE D 194 ? 0.42160 0.43300 0.45270 0.00880  0.07030  0.06820  194 ILE G C   
4613 O O   . ILE D 194 ? 0.41690 0.43200 0.45190 0.01030  0.07080  0.07220  194 ILE G O   
4614 C CB  . ILE D 194 ? 0.43480 0.42620 0.45320 0.00620  0.07340  0.05490  194 ILE G CB  
4615 C CG1 . ILE D 194 ? 0.44210 0.42270 0.44450 0.00480  0.07490  0.04980  194 ILE G CG1 
4616 C CG2 . ILE D 194 ? 0.43260 0.42470 0.46300 -0.00170 0.07370  0.04850  194 ILE G CG2 
4617 C CD1 . ILE D 194 ? 0.45220 0.42580 0.44060 -0.00330 0.07410  0.04720  194 ILE G CD1 
4618 N N   . VAL D 195 ? 0.46480 0.48100 0.50100 0.00420  0.06780  0.06960  195 VAL G N   
4619 C CA  . VAL D 195 ? 0.45710 0.48490 0.50610 0.00100  0.06600  0.07590  195 VAL G CA  
4620 C C   . VAL D 195 ? 0.46520 0.48600 0.52200 -0.00730 0.06340  0.07160  195 VAL G C   
4621 O O   . VAL D 195 ? 0.48140 0.49420 0.53310 -0.01160 0.06390  0.06350  195 VAL G O   
4622 C CB  . VAL D 195 ? 0.46220 0.50240 0.51450 0.00240  0.06360  0.08010  195 VAL G CB  
4623 C CG1 . VAL D 195 ? 0.47290 0.52620 0.53880 -0.00380 0.06180  0.08620  195 VAL G CG1 
4624 C CG2 . VAL D 195 ? 0.47260 0.52070 0.52300 0.01250  0.06610  0.08120  195 VAL G CG2 
4625 N N   . VAL D 196 ? 0.43940 0.46180 0.50740 -0.01050 0.06060  0.07620  196 VAL G N   
4626 C CA  . VAL D 196 ? 0.45170 0.46660 0.53070 -0.01750 0.05630  0.07190  196 VAL G CA  
4627 C C   . VAL D 196 ? 0.45320 0.47700 0.53660 -0.02370 0.05290  0.07870  196 VAL G C   
4628 O O   . VAL D 196 ? 0.44030 0.47620 0.52570 -0.02440 0.05250  0.08910  196 VAL G O   
4629 C CB  . VAL D 196 ? 0.46640 0.47190 0.55660 -0.01760 0.05110  0.07270  196 VAL G CB  
4630 C CG1 . VAL D 196 ? 0.46220 0.47340 0.54990 -0.01930 0.04790  0.08720  196 VAL G CG1 
4631 C CG2 . VAL D 196 ? 0.48650 0.48200 0.59200 -0.02300 0.04540  0.06580  196 VAL G CG2 
4632 N N   . THR D 197 ? 0.47360 0.49320 0.55720 -0.02970 0.05120  0.07210  197 THR G N   
4633 C CA  . THR D 197 ? 0.47320 0.49960 0.56170 -0.03720 0.04630  0.07760  197 THR G CA  
4634 C C   . THR D 197 ? 0.49570 0.51060 0.59580 -0.04410 0.04070  0.07470  197 THR G C   
4635 O O   . THR D 197 ? 0.50470 0.50610 0.60820 -0.04430 0.04140  0.06190  197 THR G O   
4636 C CB  . THR D 197 ? 0.47820 0.50510 0.55660 -0.04130 0.04520  0.07320  197 THR G CB  
4637 O OG1 . THR D 197 ? 0.50130 0.51350 0.57270 -0.04580 0.04780  0.05920  197 THR G OG1 
4638 C CG2 . THR D 197 ? 0.47740 0.51190 0.54630 -0.03390 0.04680  0.07700  197 THR G CG2 
4639 N N   . GLY D 198 ? 0.41810 0.43860 0.52570 -0.05040 0.03520  0.08540  198 GLY G N   
4640 C CA  . GLY D 198 ? 0.43640 0.44250 0.55490 -0.05750 0.02710  0.08450  198 GLY G CA  
4641 C C   . GLY D 198 ? 0.45000 0.44550 0.57480 -0.05500 0.02230  0.08950  198 GLY G C   
4642 O O   . GLY D 198 ? 0.44820 0.44500 0.56840 -0.04720 0.02660  0.08940  198 GLY G O   
4643 N N   . PRO D 199 ? 0.49620 0.47800 0.63060 -0.06260 0.01130  0.09440  199 PRO G N   
4644 C CA  . PRO D 199 ? 0.50510 0.47980 0.64600 -0.07200 0.00470  0.09170  199 PRO G CA  
4645 C C   . PRO D 199 ? 0.49350 0.48240 0.63070 -0.08390 0.00220  0.10720  199 PRO G C   
4646 O O   . PRO D 199 ? 0.49770 0.47940 0.63990 -0.09340 -0.00500 0.10670  199 PRO G O   
4647 C CB  . PRO D 199 ? 0.52870 0.47710 0.68480 -0.07260 -0.00820 0.08810  199 PRO G CB  
4648 C CG  . PRO D 199 ? 0.52600 0.47230 0.67880 -0.07080 -0.01250 0.10170  199 PRO G CG  
4649 C CD  . PRO D 199 ? 0.51130 0.47860 0.65050 -0.06290 0.00170  0.10220  199 PRO G CD  
4650 N N   . TYR D 200 ? 0.46690 0.47680 0.59680 -0.08390 0.00860  0.11900  200 TYR G N   
4651 C CA  . TYR D 200 ? 0.45580 0.48610 0.58600 -0.09540 0.00880  0.13140  200 TYR G CA  
4652 C C   . TYR D 200 ? 0.44980 0.48980 0.58420 -0.09830 0.00880  0.12590  200 TYR G C   
4653 O O   . TYR D 200 ? 0.44250 0.48470 0.57320 -0.08960 0.01350  0.11560  200 TYR G O   
4654 C CB  . TYR D 200 ? 0.43590 0.49180 0.56030 -0.09180 0.01970  0.13830  200 TYR G CB  
4655 C CG  . TYR D 200 ? 0.44650 0.49190 0.56180 -0.08870 0.02010  0.14230  200 TYR G CG  
4656 C CD1 . TYR D 200 ? 0.46770 0.50200 0.57820 -0.10200 0.01170  0.15510  200 TYR G CD1 
4657 C CD2 . TYR D 200 ? 0.44410 0.48840 0.55380 -0.07450 0.02700  0.13430  200 TYR G CD2 
4658 C CE1 . TYR D 200 ? 0.47170 0.49400 0.57130 -0.10100 0.00920  0.16020  200 TYR G CE1 
4659 C CE2 . TYR D 200 ? 0.45120 0.48550 0.55210 -0.07270 0.02580  0.13830  200 TYR G CE2 
4660 C CZ  . TYR D 200 ? 0.47230 0.49550 0.56780 -0.08610 0.01640  0.15140  200 TYR G CZ  
4661 O OH  . TYR D 200 ? 0.48310 0.49380 0.56760 -0.08620 0.01220  0.15680  200 TYR G OH  
4662 N N   . GLU D 201 ? 0.49490 0.53920 0.63500 -0.11250 0.00200  0.13370  201 GLU G N   
4663 C CA  . GLU D 201 ? 0.49790 0.54490 0.64140 -0.11780 -0.00210 0.12850  201 GLU G CA  
4664 C C   . GLU D 201 ? 0.48300 0.55720 0.62760 -0.11150 0.00430  0.12770  201 GLU G C   
4665 O O   . GLU D 201 ? 0.46250 0.56180 0.61220 -0.10820 0.01120  0.13450  201 GLU G O   
4666 C CB  . GLU D 201 ? 0.50810 0.55550 0.65830 -0.13560 -0.01150 0.13850  201 GLU G CB  
4667 C CG  . GLU D 201 ? 0.49440 0.57160 0.64990 -0.14440 -0.00710 0.15340  201 GLU G CG  
4668 C CD  . GLU D 201 ? 0.50060 0.58470 0.66380 -0.16360 -0.01540 0.16210  201 GLU G CD  
4669 O OE1 . GLU D 201 ? 0.50840 0.57250 0.67170 -0.16870 -0.02540 0.15630  201 GLU G OE1 
4670 O OE2 . GLU D 201 ? 0.48130 0.59160 0.65000 -0.17480 -0.01120 0.17380  201 GLU G OE2 
4671 N N   . LYS D 202 ? 0.39900 0.46700 0.53880 -0.11070 0.00110  0.11860  202 LYS G N   
4672 C CA  . LYS D 202 ? 0.39270 0.48040 0.53290 -0.10440 0.00280  0.11830  202 LYS G CA  
4673 C C   . LYS D 202 ? 0.38770 0.50540 0.54530 -0.11160 -0.00060 0.12880  202 LYS G C   
4674 O O   . LYS D 202 ? 0.38710 0.50540 0.55130 -0.12570 -0.00700 0.13410  202 LYS G O   
4675 C CB  . LYS D 202 ? 0.41060 0.48240 0.53700 -0.10640 -0.00250 0.10820  202 LYS G CB  
4676 C CG  . LYS D 202 ? 0.42040 0.48670 0.54800 -0.12180 -0.01300 0.10840  202 LYS G CG  
4677 C CD  . LYS D 202 ? 0.44260 0.49040 0.55070 -0.12630 -0.01680 0.09670  202 LYS G CD  
4678 C CE  . LYS D 202 ? 0.45880 0.49970 0.56580 -0.14240 -0.02740 0.09580  202 LYS G CE  
4679 N NZ  . LYS D 202 ? 0.49110 0.51300 0.57390 -0.14900 -0.02960 0.08280  202 LYS G NZ  
4680 N N   . PRO D 203 ? 0.38360 0.52700 0.55150 -0.10240 0.00340  0.13100  203 PRO G N   
4681 C CA  . PRO D 203 ? 0.37860 0.55510 0.56940 -0.10780 0.00010  0.13770  203 PRO G CA  
4682 C C   . PRO D 203 ? 0.39740 0.57280 0.58980 -0.11100 -0.01350 0.13600  203 PRO G C   
4683 O O   . PRO D 203 ? 0.41230 0.56100 0.58400 -0.11050 -0.01890 0.12970  203 PRO G O   
4684 C CB  . PRO D 203 ? 0.36860 0.57080 0.57170 -0.09370 0.01030  0.13690  203 PRO G CB  
4685 C CG  . PRO D 203 ? 0.37620 0.55470 0.55970 -0.07990 0.01320  0.12970  203 PRO G CG  
4686 C CD  . PRO D 203 ? 0.38090 0.52490 0.54290 -0.08610 0.01150  0.12640  203 PRO G CD  
4687 N N   . SER D 204 ? 0.47420 0.68070 0.69180 -0.11550 -0.01890 0.14150  204 SER G N   
4688 C CA  . SER D 204 ? 0.49080 0.70180 0.71510 -0.11850 -0.03470 0.14210  204 SER G CA  
4689 C C   . SER D 204 ? 0.50600 0.73860 0.74910 -0.10230 -0.03740 0.14090  204 SER G C   
4690 O O   . SER D 204 ? 0.48330 0.74680 0.75130 -0.09400 -0.02750 0.14070  204 SER G O   
4691 C CB  . SER D 204 ? 0.48630 0.71840 0.73130 -0.13510 -0.04240 0.14890  204 SER G CB  
4692 O OG  . SER D 204 ? 0.50210 0.70650 0.72780 -0.15100 -0.04780 0.14900  204 SER G OG  
4693 N N   . LEU D 205 ? 0.49010 0.70610 0.72130 -0.09910 -0.05160 0.13960  205 LEU G N   
4694 C CA  . LEU D 205 ? 0.50440 0.73510 0.75410 -0.08390 -0.05960 0.13930  205 LEU G CA  
4695 C C   . LEU D 205 ? 0.50800 0.75270 0.77790 -0.09060 -0.08120 0.14450  205 LEU G C   
4696 O O   . LEU D 205 ? 0.52510 0.75210 0.77670 -0.10690 -0.09250 0.14740  205 LEU G O   
4697 C CB  . LEU D 205 ? 0.53600 0.73360 0.75450 -0.07500 -0.06200 0.13550  205 LEU G CB  
4698 C CG  . LEU D 205 ? 0.53900 0.74420 0.77350 -0.05780 -0.07140 0.13520  205 LEU G CG  
4699 C CD1 . LEU D 205 ? 0.50020 0.74020 0.76980 -0.04270 -0.05690 0.13100  205 LEU G CD1 
4700 C CD2 . LEU D 205 ? 0.57040 0.73860 0.76770 -0.05340 -0.07300 0.13270  205 LEU G CD2 
4701 N N   . SER D 206 ? 0.53410 0.81180 0.84420 -0.07820 -0.08710 0.14460  206 SER G N   
4702 C CA  . SER D 206 ? 0.53870 0.83040 0.87340 -0.08180 -0.11130 0.14960  206 SER G CA  
4703 C C   . SER D 206 ? 0.52100 0.84270 0.90000 -0.06100 -0.11720 0.14600  206 SER G C   
4704 O O   . SER D 206 ? 0.50220 0.84160 0.89710 -0.04660 -0.09900 0.13860  206 SER G O   
4705 C CB  . SER D 206 ? 0.52540 0.84250 0.88110 -0.09930 -0.11280 0.15370  206 SER G CB  
4706 O OG  . SER D 206 ? 0.49990 0.86220 0.89610 -0.09480 -0.09600 0.15040  206 SER G OG  
4707 N N   . ALA D 207 ? 0.49460 0.82120 0.89440 -0.06000 -0.14420 0.15050  207 ALA G N   
4708 C CA  . ALA D 207 ? 0.47970 0.82910 0.92440 -0.03900 -0.15660 0.14660  207 ALA G CA  
4709 C C   . ALA D 207 ? 0.45470 0.85310 0.95900 -0.04040 -0.16710 0.14640  207 ALA G C   
4710 O O   . ALA D 207 ? 0.45390 0.85650 0.95640 -0.05970 -0.17660 0.15350  207 ALA G O   
4711 C CB  . ALA D 207 ? 0.51060 0.81960 0.93130 -0.03410 -0.18500 0.15270  207 ALA G CB  
4712 N N   . GLN D 208 ? 0.69070 1.12700 1.24990 -0.01980 -0.16540 0.13670  208 GLN G N   
4713 C CA  . GLN D 208 ? 0.66360 1.15390 1.29010 -0.01760 -0.17390 0.13290  208 GLN G CA  
4714 C C   . GLN D 208 ? 0.66120 1.15700 1.33070 0.00570  -0.20070 0.12880  208 GLN G C   
4715 O O   . GLN D 208 ? 0.65730 1.14560 1.33100 0.02670  -0.19400 0.11970  208 GLN G O   
4716 C CB  . GLN D 208 ? 0.63070 1.17330 1.29180 -0.01680 -0.13990 0.12070  208 GLN G CB  
4717 C CG  . GLN D 208 ? 0.61550 1.20930 1.32330 -0.03160 -0.14040 0.12100  208 GLN G CG  
4718 C CD  . GLN D 208 ? 0.63470 1.20510 1.30220 -0.06010 -0.14640 0.13540  208 GLN G CD  
4719 O OE1 . GLN D 208 ? 0.65230 1.17800 1.25910 -0.07020 -0.13790 0.14150  208 GLN G OE1 
4720 N NE2 . GLN D 208 ? 0.61990 1.22130 1.32380 -0.07300 -0.16150 0.13950  208 GLN G NE2 
4721 N N   . PRO D 209 ? 0.50400 1.00990 1.20620 0.00290  -0.23360 0.13550  209 PRO G N   
4722 C CA  . PRO D 209 ? 0.50270 1.01620 1.20160 -0.02210 -0.24570 0.14620  209 PRO G CA  
4723 C C   . PRO D 209 ? 0.54080 0.99370 1.16050 -0.04380 -0.25470 0.16040  209 PRO G C   
4724 O O   . PRO D 209 ? 0.54980 1.00180 1.15220 -0.06700 -0.25590 0.16740  209 PRO G O   
4725 C CB  . PRO D 209 ? 0.48940 1.02470 1.24720 -0.01300 -0.28360 0.14830  209 PRO G CB  
4726 C CG  . PRO D 209 ? 0.50360 1.00740 1.25940 0.01080  -0.30200 0.14660  209 PRO G CG  
4727 C CD  . PRO D 209 ? 0.48750 0.99560 1.23440 0.02530  -0.26500 0.13280  209 PRO G CD  
4728 N N   . GLY D 210 ? 0.60470 1.00840 1.17750 -0.03680 -0.26010 0.16320  210 GLY G N   
4729 C CA  . GLY D 210 ? 0.64230 0.99070 1.14070 -0.05660 -0.26560 0.17310  210 GLY G CA  
4730 C C   . GLY D 210 ? 0.67070 0.97230 1.12780 -0.04680 -0.27210 0.17460  210 GLY G C   
4731 O O   . GLY D 210 ? 0.66120 0.97070 1.14630 -0.02340 -0.27200 0.16820  210 GLY G O   
4732 N N   . PRO D 211 ? 0.65080 0.90290 1.04020 -0.06560 -0.27780 0.18210  211 PRO G N   
4733 C CA  . PRO D 211 ? 0.67600 0.88320 1.01950 -0.06050 -0.27950 0.18330  211 PRO G CA  
4734 C C   . PRO D 211 ? 0.69170 0.87080 1.03070 -0.05780 -0.31950 0.19370  211 PRO G C   
4735 O O   . PRO D 211 ? 0.70520 0.84770 1.00910 -0.05350 -0.32300 0.19550  211 PRO G O   
4736 C CB  . PRO D 211 ? 0.70520 0.87670 0.98040 -0.08480 -0.26520 0.18440  211 PRO G CB  
4737 C CG  . PRO D 211 ? 0.70350 0.89430 0.98740 -0.10350 -0.26520 0.18610  211 PRO G CG  
4738 C CD  . PRO D 211 ? 0.66410 0.89960 1.01580 -0.09350 -0.28180 0.18820  211 PRO G CD  
4739 N N   . LYS D 212 ? 0.68820 0.88110 1.06010 -0.06120 -0.35160 0.20160  212 LYS G N   
4740 C CA  . LYS D 212 ? 0.70630 0.86990 1.07510 -0.05950 -0.39500 0.21360  212 LYS G CA  
4741 C C   . LYS D 212 ? 0.67680 0.87520 1.12460 -0.02830 -0.40820 0.20760  212 LYS G C   
4742 O O   . LYS D 212 ? 0.64290 0.88780 1.15470 -0.02150 -0.41550 0.20420  212 LYS G O   
4743 C CB  . LYS D 212 ? 0.72840 0.87940 1.07950 -0.08470 -0.42670 0.22690  212 LYS G CB  
4744 N N   . VAL D 213 ? 0.81580 0.99230 1.26080 -0.00980 -0.41150 0.20510  213 VAL G N   
4745 C CA  . VAL D 213 ? 0.79510 1.00110 1.31020 0.02250  -0.41420 0.19290  213 VAL G CA  
4746 C C   . VAL D 213 ? 0.82730 0.99050 1.33250 0.02750  -0.44850 0.19810  213 VAL G C   
4747 O O   . VAL D 213 ? 0.85390 0.96190 1.30020 0.01810  -0.46160 0.20830  213 VAL G O   
4748 C CB  . VAL D 213 ? 0.78520 0.99510 1.29860 0.04040  -0.38080 0.17970  213 VAL G CB  
4749 C CG1 . VAL D 213 ? 0.75340 0.99300 1.33700 0.07350  -0.38160 0.16370  213 VAL G CG1 
4750 C CG2 . VAL D 213 ? 0.76710 1.00520 1.26760 0.03070  -0.33510 0.17050  213 VAL G CG2 
4751 N N   . GLN D 214 ? 1.08160 1.27010 1.64400 0.04090  -0.46260 0.19110  214 GLN G N   
4752 C CA  . GLN D 214 ? 1.12930 1.28160 1.69490 0.05040  -0.49380 0.19370  214 GLN G CA  
4753 C C   . GLN D 214 ? 1.11940 1.27500 1.71480 0.08020  -0.48240 0.17820  214 GLN G C   
4754 O O   . GLN D 214 ? 1.07420 1.26890 1.69850 0.09540  -0.44990 0.16320  214 GLN G O   
4755 C CB  . GLN D 214 ? 1.14940 1.32570 1.76600 0.05360  -0.51580 0.19220  214 GLN G CB  
4756 C CG  . GLN D 214 ? 1.11980 1.36540 1.82160 0.07920  -0.49540 0.17050  214 GLN G CG  
4757 C CD  . GLN D 214 ? 1.16070 1.43030 1.91260 0.08120  -0.51820 0.16920  214 GLN G CD  
4758 O OE1 . GLN D 214 ? 1.14500 1.46280 1.92890 0.07490  -0.50630 0.16500  214 GLN G OE1 
4759 N NE2 . GLN D 214 ? 1.20660 1.44230 1.96620 0.08920  -0.55170 0.17300  214 GLN G NE2 
4760 N N   . ALA D 215 ? 0.93110 1.04310 1.51730 0.08670  -0.50970 0.18170  215 ALA G N   
4761 C CA  . ALA D 215 ? 0.93100 1.04110 1.54450 0.11410  -0.50250 0.16650  215 ALA G CA  
4762 C C   . ALA D 215 ? 0.91110 1.08320 1.61140 0.14130  -0.48970 0.14390  215 ALA G C   
4763 O O   . ALA D 215 ? 0.91960 1.11000 1.66070 0.14330  -0.50890 0.14300  215 ALA G O   
4764 C CB  . ALA D 215 ? 0.98780 1.03530 1.57250 0.11160  -0.53790 0.17630  215 ALA G CB  
4765 N N   . GLY D 216 ? 0.95270 1.15790 1.67960 0.16080  -0.45610 0.12490  216 GLY G N   
4766 C CA  . GLY D 216 ? 0.92260 1.18900 1.72630 0.18450  -0.43730 0.10060  216 GLY G CA  
4767 C C   . GLY D 216 ? 0.87870 1.20990 1.71290 0.17800  -0.40800 0.09330  216 GLY G C   
4768 O O   . GLY D 216 ? 0.86570 1.25220 1.76220 0.19410  -0.39010 0.07270  216 GLY G O   
4769 N N   . GLU D 217 ? 1.09060 1.41680 1.88240 0.15330  -0.40200 0.10910  217 GLU G N   
4770 C CA  . GLU D 217 ? 1.05490 1.43720 1.86960 0.14250  -0.37570 0.10470  217 GLU G CA  
4771 C C   . GLU D 217 ? 1.01930 1.41330 1.81190 0.13970  -0.33880 0.10030  217 GLU G C   
4772 O O   . GLU D 217 ? 1.02690 1.37650 1.77020 0.13770  -0.33980 0.10850  217 GLU G O   
4773 C CB  . GLU D 217 ? 1.07410 1.44340 1.85990 0.11440  -0.39630 0.12530  217 GLU G CB  
4774 C CG  . GLU D 217 ? 1.05540 1.48240 1.87030 0.10140  -0.37440 0.12130  217 GLU G CG  
4775 C CD  . GLU D 217 ? 1.06830 1.47450 1.84270 0.07110  -0.39270 0.14220  217 GLU G CD  
4776 O OE1 . GLU D 217 ? 1.10670 1.45540 1.83060 0.05990  -0.42240 0.15900  217 GLU G OE1 
4777 O OE2 . GLU D 217 ? 1.04500 1.49080 1.83480 0.05660  -0.37650 0.14140  217 GLU G OE2 
4778 N N   . SER D 218 ? 0.72990 1.18370 1.55820 0.13780  -0.30640 0.08780  218 SER G N   
4779 C CA  . SER D 218 ? 0.70750 1.17920 1.52340 0.13540  -0.26860 0.08160  218 SER G CA  
4780 C C   . SER D 218 ? 0.71000 1.16930 1.48070 0.10690  -0.26410 0.10120  218 SER G C   
4781 O O   . SER D 218 ? 0.71700 1.18670 1.48950 0.08830  -0.27640 0.11190  218 SER G O   
4782 C CB  . SER D 218 ? 0.67060 1.21100 1.54090 0.14340  -0.23370 0.05840  218 SER G CB  
4783 O OG  . SER D 218 ? 0.67610 1.25570 1.57620 0.12970  -0.23670 0.06010  218 SER G OG  
4784 N N   . VAL D 219 ? 0.49450 0.92130 1.20370 0.10130  -0.23930 0.10220  219 VAL G N   
4785 C CA  . VAL D 219 ? 0.52410 0.92750 1.16730 0.07410  -0.22250 0.11400  219 VAL G CA  
4786 C C   . VAL D 219 ? 0.50320 0.92080 1.12980 0.07460  -0.17940 0.10270  219 VAL G C   
4787 O O   . VAL D 219 ? 0.49790 0.89850 1.11180 0.08950  -0.16910 0.09480  219 VAL G O   
4788 C CB  . VAL D 219 ? 0.55950 0.89530 1.13230 0.06240  -0.24350 0.13030  219 VAL G CB  
4789 C CG1 . VAL D 219 ? 0.57480 0.87760 1.13870 0.08230  -0.25300 0.12670  219 VAL G CG1 
4790 C CG2 . VAL D 219 ? 0.57820 0.89110 1.08600 0.04010  -0.21810 0.13560  219 VAL G CG2 
4791 N N   . THR D 220 ? 0.59380 1.03990 1.21850 0.05710  -0.15650 0.10290  220 THR G N   
4792 C CA  . THR D 220 ? 0.58160 1.03680 1.18350 0.05220  -0.11870 0.09590  220 THR G CA  
4793 C C   . THR D 220 ? 0.60000 1.02060 1.13950 0.02770  -0.11230 0.10920  220 THR G C   
4794 O O   . THR D 220 ? 0.60630 1.02650 1.14140 0.01020  -0.12500 0.11910  220 THR G O   
4795 C CB  . THR D 220 ? 0.55380 1.07430 1.20960 0.05170  -0.09590 0.08320  220 THR G CB  
4796 O OG1 . THR D 220 ? 0.56070 1.09980 1.22220 0.02940  -0.09970 0.09270  220 THR G OG1 
4797 C CG2 . THR D 220 ? 0.51830 1.07860 1.24690 0.07570  -0.10620 0.06770  220 THR G CG2 
4798 N N   . LEU D 221 ? 0.46130 0.85270 0.95480 0.02700  -0.09360 0.10830  221 LEU G N   
4799 C CA  . LEU D 221 ? 0.48140 0.83930 0.91950 0.00680  -0.08650 0.11770  221 LEU G CA  
4800 C C   . LEU D 221 ? 0.46240 0.84440 0.89940 -0.00350 -0.05730 0.11440  221 LEU G C   
4801 O O   . LEU D 221 ? 0.45020 0.84540 0.89220 0.00620  -0.03670 0.10540  221 LEU G O   
4802 C CB  . LEU D 221 ? 0.50390 0.81200 0.89210 0.01100  -0.08740 0.11930  221 LEU G CB  
4803 C CG  . LEU D 221 ? 0.53780 0.81330 0.91470 0.01660  -0.11700 0.12500  221 LEU G CG  
4804 C CD1 . LEU D 221 ? 0.56690 0.79390 0.88630 0.01220  -0.11390 0.12770  221 LEU G CD1 
4805 C CD2 . LEU D 221 ? 0.54360 0.81760 0.92410 0.00180  -0.14150 0.13500  221 LEU G CD2 
4806 N N   . SER D 222 ? 0.51460 0.89900 0.94210 -0.02450 -0.05700 0.12220  222 SER G N   
4807 C CA  . SER D 222 ? 0.50020 0.90570 0.92700 -0.03820 -0.03430 0.12210  222 SER G CA  
4808 C C   . SER D 222 ? 0.51100 0.87460 0.88540 -0.05130 -0.02780 0.12820  222 SER G C   
4809 O O   . SER D 222 ? 0.52710 0.86520 0.87950 -0.06430 -0.04100 0.13490  222 SER G O   
4810 C CB  . SER D 222 ? 0.48020 0.92230 0.94120 -0.05300 -0.03960 0.12580  222 SER G CB  
4811 O OG  . SER D 222 ? 0.46290 0.95020 0.95270 -0.05620 -0.01770 0.11960  222 SER G OG  
4812 N N   . CYS D 223 ? 0.53550 0.89320 0.89200 -0.04840 -0.00790 0.12470  223 CYS G N   
4813 C CA  . CYS D 223 ? 0.53820 0.86270 0.85420 -0.06010 -0.00060 0.12920  223 CYS G CA  
4814 C C   . CYS D 223 ? 0.52250 0.86770 0.84460 -0.07780 0.01140  0.13380  223 CYS G C   
4815 O O   . CYS D 223 ? 0.50250 0.88230 0.84530 -0.07700 0.02610  0.13030  223 CYS G O   
4816 C CB  . CYS D 223 ? 0.54320 0.84570 0.83500 -0.04730 0.01040  0.12400  223 CYS G CB  
4817 S SG  . CYS D 223 ? 0.57500 0.82910 0.82010 -0.05630 0.01190  0.12700  223 CYS G SG  
4818 N N   . SER D 224 ? 0.42700 0.75020 0.72990 -0.09500 0.00510  0.14100  224 SER G N   
4819 C CA  . SER D 224 ? 0.41250 0.75220 0.72190 -0.11530 0.01070  0.14790  224 SER G CA  
4820 C C   . SER D 224 ? 0.42410 0.72380 0.69940 -0.12730 0.00990  0.15310  224 SER G C   
4821 O O   . SER D 224 ? 0.43430 0.69760 0.68750 -0.12430 0.00090  0.15090  224 SER G O   
4822 C CB  . SER D 224 ? 0.41000 0.77240 0.74560 -0.12710 -0.00220 0.15180  224 SER G CB  
4823 O OG  . SER D 224 ? 0.41130 0.78750 0.75100 -0.14900 0.00250  0.15930  224 SER G OG  
4824 N N   . SER D 225 ? 0.34350 0.65050 0.61570 -0.14230 0.01870  0.15960  225 SER G N   
4825 C CA  . SER D 225 ? 0.35610 0.62480 0.60070 -0.15350 0.01520  0.16520  225 SER G CA  
4826 C C   . SER D 225 ? 0.37110 0.65350 0.61770 -0.17610 0.01950  0.17580  225 SER G C   
4827 O O   . SER D 225 ? 0.36970 0.69020 0.63110 -0.18080 0.03210  0.17700  225 SER G O   
4828 C CB  . SER D 225 ? 0.35070 0.59240 0.57230 -0.14010 0.02170  0.16100  225 SER G CB  
4829 O OG  . SER D 225 ? 0.36390 0.56780 0.56490 -0.14870 0.01520  0.16470  225 SER G OG  
4830 N N   . ARG D 226 ? 0.58660 0.71470 0.88430 -0.06320 -0.00830 0.15840  226 ARG G N   
4831 C CA  . ARG D 226 ? 0.58590 0.69750 0.88110 -0.09220 -0.01660 0.16970  226 ARG G CA  
4832 C C   . ARG D 226 ? 0.59260 0.66380 0.84440 -0.09830 -0.00800 0.16900  226 ARG G C   
4833 O O   . ARG D 226 ? 0.59710 0.65770 0.83780 -0.12140 -0.00630 0.18430  226 ARG G O   
4834 C CB  . ARG D 226 ? 0.59850 0.69700 0.91280 -0.10440 -0.05860 0.16450  226 ARG G CB  
4835 N N   . SER D 227 ? 0.40200 0.45420 0.62850 -0.08020 -0.00260 0.15280  227 SER G N   
4836 C CA  . SER D 227 ? 0.40740 0.42910 0.59570 -0.08390 0.00780  0.14840  227 SER G CA  
4837 C C   . SER D 227 ? 0.40470 0.44340 0.58740 -0.08090 0.04550  0.15510  227 SER G C   
4838 O O   . SER D 227 ? 0.40200 0.46610 0.60440 -0.06610 0.06370  0.15560  227 SER G O   
4839 C CB  . SER D 227 ? 0.41760 0.42030 0.58520 -0.06930 0.00030  0.12560  227 SER G CB  
4840 O OG  . SER D 227 ? 0.43140 0.42150 0.60070 -0.06980 -0.03740 0.11290  227 SER G OG  
4841 N N   . SER D 228 ? 0.56770 0.59310 0.72230 -0.09240 0.05440  0.15830  228 SER G N   
4842 C CA  . SER D 228 ? 0.57960 0.62880 0.72780 -0.09020 0.08750  0.16070  228 SER G CA  
4843 C C   . SER D 228 ? 0.59040 0.62190 0.72060 -0.07050 0.10470  0.13890  228 SER G C   
4844 O O   . SER D 228 ? 0.61480 0.63740 0.71720 -0.07180 0.11560  0.13010  228 SER G O   
4845 C CB  . SER D 228 ? 0.59820 0.64950 0.72220 -0.11340 0.08820  0.17600  228 SER G CB  
4846 O OG  . SER D 228 ? 0.63170 0.71060 0.74270 -0.10770 0.11940  0.17060  228 SER G OG  
4847 N N   . TYR D 229 ? 0.44150 0.46770 0.58720 -0.05350 0.10550  0.13110  229 TYR G N   
4848 C CA  . TYR D 229 ? 0.45290 0.46050 0.58870 -0.03810 0.12290  0.11490  229 TYR G CA  
4849 C C   . TYR D 229 ? 0.49090 0.51790 0.63120 -0.02810 0.14880  0.11040  229 TYR G C   
4850 O O   . TYR D 229 ? 0.49080 0.55590 0.65520 -0.02390 0.15680  0.12010  229 TYR G O   
4851 C CB  . TYR D 229 ? 0.44210 0.44330 0.59390 -0.02490 0.11900  0.11650  229 TYR G CB  
4852 C CG  . TYR D 229 ? 0.42410 0.41690 0.56910 -0.03210 0.09500  0.11350  229 TYR G CG  
4853 C CD1 . TYR D 229 ? 0.43160 0.40280 0.55170 -0.03880 0.08920  0.09640  229 TYR G CD1 
4854 C CD2 . TYR D 229 ? 0.41080 0.42510 0.57650 -0.03060 0.07640  0.12280  229 TYR G CD2 
4855 C CE1 . TYR D 229 ? 0.42790 0.40250 0.54420 -0.04210 0.06620  0.08780  229 TYR G CE1 
4856 C CE2 . TYR D 229 ? 0.40700 0.42200 0.56810 -0.03350 0.05250  0.11380  229 TYR G CE2 
4857 C CZ  . TYR D 229 ? 0.41710 0.41400 0.55370 -0.03850 0.04760  0.09590  229 TYR G CZ  
4858 O OH  . TYR D 229 ? 0.43370 0.44160 0.56830 -0.03810 0.02260  0.08160  229 TYR G OH  
4859 N N   . ASP D 230 ? 0.60300 0.61020 0.72210 -0.02340 0.16090  0.09110  230 ASP G N   
4860 C CA  . ASP D 230 ? 0.64710 0.67310 0.77070 -0.00870 0.18330  0.07790  230 ASP G CA  
4861 C C   . ASP D 230 ? 0.67560 0.68610 0.82180 0.01520  0.19030  0.07100  230 ASP G C   
4862 O O   . ASP D 230 ? 0.72510 0.75590 0.88430 0.03410  0.20470  0.05830  230 ASP G O   
4863 C CB  . ASP D 230 ? 0.66980 0.68100 0.76350 -0.01060 0.19040  0.05520  230 ASP G CB  
4864 C CG  . ASP D 230 ? 0.67920 0.70370 0.74470 -0.03070 0.18230  0.06380  230 ASP G CG  
4865 O OD1 . ASP D 230 ? 0.66660 0.72850 0.73640 -0.04190 0.18350  0.08450  230 ASP G OD1 
4866 O OD2 . ASP D 230 ? 0.69650 0.69430 0.73540 -0.03630 0.17330  0.05070  230 ASP G OD2 
4867 N N   . MET D 231 ? 0.80900 0.78640 0.95890 0.01590  0.17870  0.07900  231 MET G N   
4868 C CA  . MET D 231 ? 0.85420 0.79900 1.01540 0.03500  0.18230  0.07580  231 MET G CA  
4869 C C   . MET D 231 ? 0.81480 0.74250 0.97770 0.03000  0.16790  0.09540  231 MET G C   
4870 O O   . MET D 231 ? 0.76130 0.68930 0.91040 0.01130  0.15680  0.09850  231 MET G O   
4871 C CB  . MET D 231 ? 0.90120 0.80430 1.04690 0.03550  0.19010  0.05190  231 MET G CB  
4872 C CG  . MET D 231 ? 0.97660 0.84180 1.13630 0.05770  0.19400  0.04460  231 MET G CG  
4873 S SD  . MET D 231 ? 1.02200 0.85130 1.17030 0.05900  0.20290  0.00720  231 MET G SD  
4874 C CE  . MET D 231 ? 0.95610 0.74370 1.08400 0.02700  0.19530  0.01190  231 MET G CE  
4875 N N   . TYR D 232 ? 0.58370 0.49970 0.76210 0.04910  0.16650  0.10670  232 TYR G N   
4876 C CA  . TYR D 232 ? 0.55020 0.45370 0.72640 0.04690  0.15420  0.12740  232 TYR G CA  
4877 C C   . TYR D 232 ? 0.59340 0.43980 0.76130 0.05250  0.15690  0.13150  232 TYR G C   
4878 O O   . TYR D 232 ? 0.63520 0.45420 0.81210 0.07220  0.16300  0.12240  232 TYR G O   
4879 C CB  . TYR D 232 ? 0.55010 0.49210 0.74920 0.06330  0.14540  0.14400  232 TYR G CB  
4880 C CG  . TYR D 232 ? 0.51560 0.50690 0.72370 0.04940  0.13710  0.14500  232 TYR G CG  
4881 C CD1 . TYR D 232 ? 0.45900 0.45500 0.65500 0.03090  0.12270  0.14770  232 TYR G CD1 
4882 C CD2 . TYR D 232 ? 0.52460 0.55870 0.75430 0.05360  0.14210  0.14170  232 TYR G CD2 
4883 C CE1 . TYR D 232 ? 0.42800 0.45750 0.63370 0.01910  0.10980  0.14750  232 TYR G CE1 
4884 C CE2 . TYR D 232 ? 0.47210 0.54240 0.71060 0.03560  0.13210  0.14620  232 TYR G CE2 
4885 C CZ  . TYR D 232 ? 0.43310 0.49450 0.65950 0.01910  0.11420  0.14900  232 TYR G CZ  
4886 O OH  . TYR D 232 ? 0.40370 0.48990 0.64010 0.00220  0.09900  0.15200  232 TYR G OH  
4887 N N   . HIS D 233 ? 0.66980 0.49990 0.82110 0.03450  0.15090  0.14430  233 HIS G N   
4888 C CA  . HIS D 233 ? 0.70500 0.47980 0.84580 0.03100  0.15200  0.15680  233 HIS G CA  
4889 C C   . HIS D 233 ? 0.69900 0.48190 0.83660 0.03720  0.14090  0.18950  233 HIS G C   
4890 O O   . HIS D 233 ? 0.66810 0.49210 0.79780 0.02370  0.13400  0.19730  233 HIS G O   
4891 C CB  . HIS D 233 ? 0.68450 0.44250 0.80660 -0.00080 0.15660  0.14590  233 HIS G CB  
4892 C CG  . HIS D 233 ? 0.68760 0.44890 0.80880 -0.00710 0.16460  0.11260  233 HIS G CG  
4893 N ND1 . HIS D 233 ? 0.72720 0.44340 0.84800 -0.00940 0.17280  0.09270  233 HIS G ND1 
4894 C CD2 . HIS D 233 ? 0.64710 0.44980 0.76590 -0.01120 0.16330  0.09610  233 HIS G CD2 
4895 C CE1 . HIS D 233 ? 0.72510 0.46250 0.84190 -0.01310 0.17760  0.06430  233 HIS G CE1 
4896 N NE2 . HIS D 233 ? 0.67640 0.46350 0.78990 -0.01480 0.17190  0.06850  233 HIS G NE2 
4897 N N   . LEU D 234 ? 0.72880 0.47420 0.87170 0.06020  0.13680  0.20660  234 LEU G N   
4898 C CA  . LEU D 234 ? 0.72970 0.47810 0.86470 0.06940  0.12470  0.24100  234 LEU G CA  
4899 C C   . LEU D 234 ? 0.77570 0.46520 0.88560 0.04780  0.12520  0.26520  234 LEU G C   
4900 O O   . LEU D 234 ? 0.82570 0.44560 0.93590 0.04990  0.12720  0.26300  234 LEU G O   
4901 C CB  . LEU D 234 ? 0.76310 0.50840 0.91800 0.11060  0.11600  0.24690  234 LEU G CB  
4902 C CG  . LEU D 234 ? 0.77830 0.52720 0.92470 0.12830  0.10030  0.28220  234 LEU G CG  
4903 C CD1 . LEU D 234 ? 0.73070 0.55960 0.88000 0.12370  0.09380  0.28580  234 LEU G CD1 
4904 C CD2 . LEU D 234 ? 0.81770 0.54730 0.98410 0.17250  0.09050  0.28150  234 LEU G CD2 
4905 N N   . SER D 235 ? 0.84210 0.56240 0.93160 0.02630  0.12220  0.28740  235 SER G N   
4906 C CA  . SER D 235 ? 0.87250 0.55810 0.93630 -0.00740 0.12650  0.30970  235 SER G CA  
4907 C C   . SER D 235 ? 0.89210 0.58950 0.93430 -0.00410 0.11610  0.35410  235 SER G C   
4908 O O   . SER D 235 ? 0.85950 0.63020 0.90000 0.00290  0.10960  0.35630  235 SER G O   
4909 C CB  . SER D 235 ? 0.82690 0.55950 0.88450 -0.04270 0.13610  0.28670  235 SER G CB  
4910 O OG  . SER D 235 ? 0.87050 0.58500 0.90650 -0.07990 0.14250  0.30620  235 SER G OG  
4911 N N   . ARG D 236 ? 1.02540 0.65520 1.04680 -0.00940 0.10900  0.38070  236 ARG G N   
4912 C CA  . ARG D 236 ? 1.07180 0.70560 1.06400 -0.00380 0.09450  0.41940  236 ARG G CA  
4913 C C   . ARG D 236 ? 1.11170 0.75150 1.06620 -0.05100 0.10020  0.43890  236 ARG G C   
4914 O O   . ARG D 236 ? 1.15240 0.74460 1.09880 -0.08380 0.10790  0.43040  236 ARG G O   
4915 C CB  . ARG D 236 ? 1.15390 0.70650 1.14160 0.02600  0.07660  0.43250  236 ARG G CB  
4916 C CG  . ARG D 236 ? 1.19220 0.75800 1.15810 0.05040  0.05800  0.46670  236 ARG G CG  
4917 C CD  . ARG D 236 ? 1.30220 0.77220 1.25380 0.07300  0.03680  0.48060  236 ARG G CD  
4918 N NE  . ARG D 236 ? 1.40020 0.79170 1.31700 0.03340  0.03690  0.49550  236 ARG G NE  
4919 C CZ  . ARG D 236 ? 1.48290 0.85260 1.35060 0.00980  0.03190  0.53450  236 ARG G CZ  
4920 N NH1 . ARG D 236 ? 1.48290 0.90390 1.33010 0.02400  0.02370  0.56210  236 ARG G NH1 
4921 N NH2 . ARG D 236 ? 1.56670 0.86360 1.40460 -0.02890 0.03690  0.54540  236 ARG G NH2 
4922 N N   . GLU D 237 ? 1.10540 0.81030 1.03790 -0.05430 0.09670  0.46290  237 GLU G N   
4923 C CA  . GLU D 237 ? 1.15780 0.88750 1.05510 -0.09780 0.10540  0.47970  237 GLU G CA  
4924 C C   . GLU D 237 ? 1.27330 0.90590 1.13680 -0.11660 0.10180  0.50670  237 GLU G C   
4925 O O   . GLU D 237 ? 1.33890 0.93190 1.18020 -0.09500 0.08580  0.53750  237 GLU G O   
4926 C CB  . GLU D 237 ? 1.13360 0.95650 1.01350 -0.09070 0.09990  0.49950  237 GLU G CB  
4927 C CG  . GLU D 237 ? 1.02820 0.95870 0.93240 -0.08580 0.10400  0.47200  237 GLU G CG  
4928 C CD  . GLU D 237 ? 1.03130 1.06210 0.91120 -0.09370 0.10080  0.48490  237 GLU G CD  
4929 O OE1 . GLU D 237 ? 1.10210 1.12170 0.95030 -0.09100 0.09320  0.51930  237 GLU G OE1 
4930 O OE2 . GLU D 237 ? 0.96590 1.08860 0.85660 -0.10190 0.10450  0.45860  237 GLU G OE2 
4931 N N   . GLY D 238 ? 1.18870 0.77980 1.04820 -0.15530 0.11560  0.49450  238 GLY G N   
4932 C CA  . GLY D 238 ? 1.31610 0.81450 1.14380 -0.17880 0.11570  0.51930  238 GLY G CA  
4933 C C   . GLY D 238 ? 1.37180 0.76130 1.21240 -0.16610 0.10440  0.50460  238 GLY G C   
4934 O O   . GLY D 238 ? 1.46700 0.77550 1.28760 -0.19140 0.10820  0.51590  238 GLY G O   
4935 N N   . GLY D 239 ? 1.36420 0.75440 1.24250 -0.12560 0.09260  0.47830  239 GLY G N   
4936 C CA  . GLY D 239 ? 1.40550 0.70750 1.30400 -0.10650 0.08010  0.45760  239 GLY G CA  
4937 C C   . GLY D 239 ? 1.38380 0.68060 1.30650 -0.13510 0.09280  0.42000  239 GLY G C   
4938 O O   . GLY D 239 ? 1.28320 0.65460 1.23420 -0.13660 0.10690  0.39220  239 GLY G O   
4939 N N   . HIS D 241 ? 1.71880 0.93760 1.71720 -0.02840 0.06740  0.36170  241 HIS G N   
4940 C CA  . HIS D 241 ? 1.64380 0.90730 1.67730 0.02180  0.06960  0.34030  241 HIS G CA  
4941 C C   . HIS D 241 ? 1.52450 0.87380 1.58120 0.01200  0.09540  0.31450  241 HIS G C   
4942 O O   . HIS D 241 ? 1.46440 0.88210 1.51050 -0.00380 0.10400  0.33060  241 HIS G O   
4943 C CB  . HIS D 241 ? 1.64800 0.93400 1.66810 0.05210  0.05550  0.37310  241 HIS G CB  
4944 N N   . GLU D 242 ? 1.63230 0.97590 1.71800 0.02320  0.10590  0.27260  242 GLU G N   
4945 C CA  . GLU D 242 ? 1.54910 0.95840 1.65070 0.01340  0.12880  0.24580  242 GLU G CA  
4946 C C   . GLU D 242 ? 1.53850 0.96190 1.66940 0.05290  0.13270  0.20710  242 GLU G C   
4947 O O   . GLU D 242 ? 1.56570 0.95270 1.70910 0.05670  0.13540  0.17320  242 GLU G O   
4948 C CB  . GLU D 242 ? 1.54340 0.94610 1.63670 -0.03220 0.13890  0.22830  242 GLU G CB  
4949 C CG  . GLU D 242 ? 1.50840 0.96540 1.57930 -0.07210 0.14480  0.24920  242 GLU G CG  
4950 C CD  . GLU D 242 ? 1.43180 0.97230 1.51010 -0.07050 0.15690  0.23130  242 GLU G CD  
4951 O OE1 . GLU D 242 ? 1.40370 0.96850 1.49800 -0.04020 0.15650  0.20610  242 GLU G OE1 
4952 O OE2 . GLU D 242 ? 1.39130 0.98360 1.45590 -0.09960 0.16120  0.23710  242 GLU G OE2 
4953 N N   . ARG D 243 ? 1.10070 0.58960 1.24090 0.07970  0.13100  0.20780  243 ARG G N   
4954 C CA  . ARG D 243 ? 1.10290 0.62400 1.26890 0.11690  0.13260  0.17510  243 ARG G CA  
4955 C C   . ARG D 243 ? 1.04270 0.64040 1.21220 0.10270  0.14720  0.14910  243 ARG G C   
4956 O O   . ARG D 243 ? 1.00110 0.64170 1.15800 0.07790  0.14980  0.16150  243 ARG G O   
4957 C CB  . ARG D 243 ? 1.09990 0.64670 1.27810 0.15510  0.11990  0.19300  243 ARG G CB  
4958 C CG  . ARG D 243 ? 1.16990 0.64000 1.34020 0.17480  0.10010  0.22470  243 ARG G CG  
4959 C CD  . ARG D 243 ? 1.16080 0.62740 1.30150 0.14940  0.09440  0.27400  243 ARG G CD  
4960 N NE  . ARG D 243 ? 1.24330 0.63610 1.36010 0.15360  0.07100  0.30040  243 ARG G NE  
4961 C CZ  . ARG D 243 ? 1.27510 0.66390 1.38700 0.18730  0.04970  0.32000  243 ARG G CZ  
4962 N NH1 . ARG D 243 ? 1.21660 0.67580 1.35170 0.22100  0.05000  0.31640  243 ARG G NH1 
4963 N NH2 . ARG D 243 ? 1.36840 0.67990 1.45000 0.18680  0.02570  0.34320  243 ARG G NH2 
4964 N N   . ARG D 244 ? 0.99210 0.60680 1.17760 0.12000  0.15470  0.11220  244 ARG G N   
4965 C CA  . ARG D 244 ? 0.96320 0.64520 1.14940 0.10930  0.16720  0.09000  244 ARG G CA  
4966 C C   . ARG D 244 ? 0.98050 0.71520 1.19060 0.14230  0.17050  0.07280  244 ARG G C   
4967 O O   . ARG D 244 ? 1.02380 0.73590 1.25080 0.17500  0.16650  0.05660  244 ARG G O   
4968 C CB  . ARG D 244 ? 0.97390 0.63590 1.14990 0.09010  0.17650  0.05940  244 ARG G CB  
4969 C CG  . ARG D 244 ? 0.97210 0.58480 1.13000 0.05630  0.17450  0.06950  244 ARG G CG  
4970 C CD  . ARG D 244 ? 0.99860 0.57400 1.15580 0.04700  0.17970  0.03380  244 ARG G CD  
4971 N NE  . ARG D 244 ? 0.99260 0.62180 1.14670 0.04860  0.18950  0.00170  244 ARG G NE  
4972 C CZ  . ARG D 244 ? 1.02590 0.66580 1.19090 0.07340  0.19430  -0.03180 244 ARG G CZ  
4973 N NH1 . ARG D 244 ? 1.06690 0.66440 1.25070 0.10190  0.18830  -0.04470 244 ARG G NH1 
4974 N NH2 . ARG D 244 ? 1.00490 0.70070 1.16030 0.07110  0.20340  -0.05360 244 ARG G NH2 
4975 N N   . LEU D 245 ? 0.83490 0.64130 1.04780 0.13300  0.17640  0.07490  245 LEU G N   
4976 C CA  . LEU D 245 ? 0.83400 0.70690 1.07060 0.15540  0.18210  0.06230  245 LEU G CA  
4977 C C   . LEU D 245 ? 0.81250 0.74510 1.04140 0.12940  0.19170  0.05990  245 LEU G C   
4978 O O   . LEU D 245 ? 0.79260 0.72230 1.00500 0.10140  0.18660  0.07670  245 LEU G O   
4979 C CB  . LEU D 245 ? 0.82090 0.71910 1.07800 0.17650  0.17090  0.08360  245 LEU G CB  
4980 C CG  . LEU D 245 ? 0.85430 0.72180 1.12960 0.21910  0.16070  0.07770  245 LEU G CG  
4981 C CD1 . LEU D 245 ? 0.82780 0.74100 1.12380 0.23890  0.14990  0.09590  245 LEU G CD1 
4982 C CD2 . LEU D 245 ? 0.87070 0.75890 1.16380 0.24590  0.16940  0.03700  245 LEU G CD2 
4983 N N   . PRO D 246 ? 0.71900 0.70770 0.95870 0.13790  0.20400  0.03980  246 PRO G N   
4984 C CA  . PRO D 246 ? 0.67670 0.71910 0.90630 0.11040  0.21140  0.04480  246 PRO G CA  
4985 C C   . PRO D 246 ? 0.63120 0.71980 0.87870 0.10120  0.20430  0.07010  246 PRO G C   
4986 O O   . PRO D 246 ? 0.63000 0.74400 0.90550 0.12350  0.20060  0.07370  246 PRO G O   
4987 C CB  . PRO D 246 ? 0.67900 0.77360 0.91490 0.12440  0.22820  0.01660  246 PRO G CB  
4988 C CG  . PRO D 246 ? 0.71020 0.80740 0.97600 0.16520  0.22620  0.00050  246 PRO G CG  
4989 C CD  . PRO D 246 ? 0.73510 0.74390 0.99600 0.17370  0.21050  0.01070  246 PRO G CD  
4990 N N   . ALA D 247 ? 0.62320 0.72160 0.85570 0.06940  0.19940  0.08520  247 ALA G N   
4991 C CA  . ALA D 247 ? 0.58340 0.72460 0.83500 0.05640  0.19020  0.10590  247 ALA G CA  
4992 C C   . ALA D 247 ? 0.55570 0.77110 0.82330 0.04900  0.20400  0.10380  247 ALA G C   
4993 O O   . ALA D 247 ? 0.55860 0.79080 0.80920 0.04260  0.21860  0.09190  247 ALA G O   
4994 C CB  . ALA D 247 ? 0.53690 0.65260 0.76830 0.02740  0.17410  0.12040  247 ALA G CB  
4995 N N   . VAL D 248 ? 0.59340 0.86060 0.89460 0.04950  0.19990  0.11450  248 VAL G N   
4996 C CA  . VAL D 248 ? 0.56990 0.91870 0.89140 0.03510  0.21290  0.11640  248 VAL G CA  
4997 C C   . VAL D 248 ? 0.53590 0.90360 0.87220 0.00280  0.19740  0.14120  248 VAL G C   
4998 O O   . VAL D 248 ? 0.52650 0.87000 0.87510 0.00810  0.17780  0.14880  248 VAL G O   
4999 C CB  . VAL D 248 ? 0.58210 0.99310 0.94050 0.06960  0.22450  0.09670  248 VAL G CB  
5000 C CG1 . VAL D 248 ? 0.63440 0.99100 0.98720 0.11210  0.22260  0.07550  248 VAL G CG1 
5001 C CG2 . VAL D 248 ? 0.56270 1.02380 0.96300 0.07070  0.21380  0.10720  248 VAL G CG2 
5002 N N   . ARG D 249 ? 0.69190 1.10100 1.02520 -0.03190 0.20460  0.15420  249 ARG G N   
5003 C CA  . ARG D 249 ? 0.65520 1.07210 1.00200 -0.06810 0.18670  0.17840  249 ARG G CA  
5004 C C   . ARG D 249 ? 0.63590 1.13020 1.03530 -0.06730 0.18840  0.17890  249 ARG G C   
5005 O O   . ARG D 249 ? 0.63770 1.20740 1.05760 -0.05920 0.21050  0.16810  249 ARG G O   
5006 C CB  . ARG D 249 ? 0.65650 1.07700 0.97530 -0.10950 0.19070  0.19780  249 ARG G CB  
5007 C CG  . ARG D 249 ? 0.64710 1.06260 0.97930 -0.15070 0.16760  0.22480  249 ARG G CG  
5008 C CD  . ARG D 249 ? 0.66490 1.04290 0.95510 -0.18750 0.15980  0.24790  249 ARG G CD  
5009 N NE  . ARG D 249 ? 0.67100 0.97460 0.95270 -0.19890 0.12260  0.25660  249 ARG G NE  
5010 C CZ  . ARG D 249 ? 0.69780 0.94150 0.93850 -0.21670 0.10450  0.26900  249 ARG G CZ  
5011 N NH1 . ARG D 249 ? 0.72580 0.96960 0.92300 -0.22600 0.11900  0.27460  249 ARG G NH1 
5012 N NH2 . ARG D 249 ? 0.68310 0.86480 0.92280 -0.21860 0.06800  0.26860  249 ARG G NH2 
5013 N N   . LYS D 250 ? 0.45450 0.93690 0.87740 -0.07370 0.16380  0.18730  250 LYS G N   
5014 C CA  . LYS D 250 ? 0.43230 0.98540 0.90800 -0.07260 0.15980  0.18540  250 LYS G CA  
5015 C C   . LYS D 250 ? 0.42000 1.00410 0.91550 -0.12470 0.15120  0.20690  250 LYS G C   
5016 O O   . LYS D 250 ? 0.43340 0.97010 0.89890 -0.15820 0.14240  0.22540  250 LYS G O   
5017 C CB  . LYS D 250 ? 0.43580 0.95980 0.92550 -0.04270 0.13630  0.17810  250 LYS G CB  
5018 C CG  . LYS D 250 ? 0.46530 0.95300 0.93520 0.00480  0.14280  0.16330  250 LYS G CG  
5019 C CD  . LYS D 250 ? 0.47970 1.02080 0.96190 0.02830  0.16870  0.14650  250 LYS G CD  
5020 C CE  . LYS D 250 ? 0.50400 1.02480 0.98860 0.08060  0.16610  0.13130  250 LYS G CE  
5021 N NZ  . LYS D 250 ? 0.48560 1.07330 1.01720 0.10440  0.15760  0.12360  250 LYS G NZ  
5022 N N   . VAL D 251 ? 0.38440 1.04660 0.93170 -0.13160 0.15120  0.20390  251 VAL G N   
5023 C CA  . VAL D 251 ? 0.41800 1.09160 0.97100 -0.18070 0.14110  0.21500  251 VAL G CA  
5024 C C   . VAL D 251 ? 0.41880 1.01920 0.96600 -0.20520 0.10560  0.23090  251 VAL G C   
5025 O O   . VAL D 251 ? 0.45930 1.02090 0.98220 -0.24500 0.09500  0.24740  251 VAL G O   
5026 C CB  . VAL D 251 ? 0.42150 1.18170 1.02620 -0.17840 0.14470  0.19850  251 VAL G CB  
5027 C CG1 . VAL D 251 ? 0.45790 1.21990 1.07600 -0.22970 0.13010  0.21140  251 VAL G CG1 
5028 C CG2 . VAL D 251 ? 0.43610 1.26780 1.04240 -0.16000 0.17760  0.18030  251 VAL G CG2 
5029 N N   . ASN D 252 ? 0.38160 0.95800 0.94770 -0.17810 0.08450  0.22430  252 ASN G N   
5030 C CA  . ASN D 252 ? 0.38530 0.89510 0.94680 -0.19390 0.04660  0.22890  252 ASN G CA  
5031 C C   . ASN D 252 ? 0.39630 0.81710 0.89980 -0.19480 0.03900  0.23530  252 ASN G C   
5032 O O   . ASN D 252 ? 0.39600 0.75980 0.89160 -0.19430 0.00620  0.23040  252 ASN G O   
5033 C CB  . ASN D 252 ? 0.36080 0.87440 0.94650 -0.15750 0.02450  0.20750  252 ASN G CB  
5034 C CG  . ASN D 252 ? 0.35310 0.85300 0.91170 -0.10630 0.03910  0.19390  252 ASN G CG  
5035 O OD1 . ASN D 252 ? 0.37210 0.83290 0.88810 -0.09810 0.05700  0.19680  252 ASN G OD1 
5036 N ND2 . ASN D 252 ? 0.34900 0.87930 0.93180 -0.07250 0.02970  0.17980  252 ASN G ND2 
5037 N N   . ARG D 253 ? 0.50490 0.91960 0.97040 -0.19300 0.06700  0.24120  253 ARG G N   
5038 C CA  . ARG D 253 ? 0.51780 0.85990 0.92790 -0.19380 0.06400  0.24560  253 ARG G CA  
5039 C C   . ARG D 253 ? 0.51860 0.81500 0.90450 -0.15190 0.05950  0.22430  253 ARG G C   
5040 O O   . ARG D 253 ? 0.52900 0.76700 0.87390 -0.15080 0.05210  0.22260  253 ARG G O   
5041 C CB  . ARG D 253 ? 0.54320 0.82810 0.94120 -0.23040 0.03080  0.26310  253 ARG G CB  
5042 C CG  . ARG D 253 ? 0.57880 0.87600 0.96480 -0.26830 0.03500  0.28020  253 ARG G CG  
5043 C CD  . ARG D 253 ? 0.61230 0.86310 1.00790 -0.29520 -0.00560 0.28800  253 ARG G CD  
5044 N NE  . ARG D 253 ? 0.60150 0.88690 1.05580 -0.29140 -0.02230 0.27540  253 ARG G NE  
5045 C CZ  . ARG D 253 ? 0.57500 0.83140 1.05210 -0.27500 -0.05540 0.26060  253 ARG G CZ  
5046 N NH1 . ARG D 253 ? 0.58230 0.77250 1.03030 -0.26280 -0.07700 0.25570  253 ARG G NH1 
5047 N NH2 . ARG D 253 ? 0.56030 0.86070 1.09110 -0.26930 -0.06860 0.24630  253 ARG G NH2 
5048 N N   . THR D 254 ? 0.38040 0.70390 0.78940 -0.11870 0.06310  0.20910  254 THR G N   
5049 C CA  . THR D 254 ? 0.39740 0.68080 0.77990 -0.08410 0.06350  0.19480  254 THR G CA  
5050 C C   . THR D 254 ? 0.40620 0.68710 0.76350 -0.06730 0.09510  0.18950  254 THR G C   
5051 O O   . THR D 254 ? 0.40650 0.73540 0.77640 -0.06960 0.11810  0.19080  254 THR G O   
5052 C CB  . THR D 254 ? 0.38650 0.69450 0.79670 -0.05480 0.05340  0.18520  254 THR G CB  
5053 O OG1 . THR D 254 ? 0.38300 0.75280 0.82520 -0.04160 0.07200  0.18390  254 THR G OG1 
5054 C CG2 . THR D 254 ? 0.37670 0.68970 0.81260 -0.06730 0.01910  0.18330  254 THR G CG2 
5055 N N   . PHE D 255 ? 0.37450 0.60340 0.69780 -0.05100 0.09520  0.18060  255 PHE G N   
5056 C CA  . PHE D 255 ? 0.38970 0.60490 0.69070 -0.03220 0.11990  0.17060  255 PHE G CA  
5057 C C   . PHE D 255 ? 0.42280 0.62470 0.72900 0.00100  0.12020  0.16340  255 PHE G C   
5058 O O   . PHE D 255 ? 0.41420 0.59170 0.71450 0.00530  0.10220  0.16470  255 PHE G O   
5059 C CB  . PHE D 255 ? 0.39490 0.55980 0.65310 -0.04370 0.11980  0.16630  255 PHE G CB  
5060 C CG  . PHE D 255 ? 0.39510 0.57130 0.63930 -0.07250 0.12350  0.17650  255 PHE G CG  
5061 C CD1 . PHE D 255 ? 0.39960 0.56600 0.64530 -0.10000 0.09950  0.19130  255 PHE G CD1 
5062 C CD2 . PHE D 255 ? 0.41280 0.61020 0.64210 -0.07140 0.14920  0.17170  255 PHE G CD2 
5063 C CE1 . PHE D 255 ? 0.42800 0.59910 0.65660 -0.12960 0.10110  0.20770  255 PHE G CE1 
5064 C CE2 . PHE D 255 ? 0.43630 0.65090 0.64760 -0.09970 0.15360  0.18580  255 PHE G CE2 
5065 C CZ  . PHE D 255 ? 0.44610 0.64420 0.65500 -0.13020 0.12970  0.20690  255 PHE G CZ  
5066 N N   . GLN D 256 ? 0.52800 0.74710 0.84390 0.02500  0.13890  0.15570  256 GLN G N   
5067 C CA  . GLN D 256 ? 0.54990 0.76590 0.87940 0.05720  0.13500  0.15480  256 GLN G CA  
5068 C C   . GLN D 256 ? 0.59960 0.79820 0.92310 0.08400  0.15240  0.14150  256 GLN G C   
5069 O O   . GLN D 256 ? 0.59930 0.82330 0.92510 0.08320  0.16960  0.12900  256 GLN G O   
5070 C CB  . GLN D 256 ? 0.52720 0.80660 0.89880 0.06420  0.12680  0.15880  256 GLN G CB  
5071 C CG  . GLN D 256 ? 0.53910 0.81930 0.92330 0.09970  0.11730  0.16050  256 GLN G CG  
5072 C CD  . GLN D 256 ? 0.49800 0.84930 0.92620 0.10680  0.10780  0.16020  256 GLN G CD  
5073 O OE1 . GLN D 256 ? 0.47350 0.84100 0.91350 0.09340  0.08880  0.16620  256 GLN G OE1 
5074 N NE2 . GLN D 256 ? 0.50110 0.90000 0.95660 0.12910  0.11930  0.14890  256 GLN G NE2 
5075 N N   . ALA D 257 ? 0.58850 0.74280 0.90300 0.10730  0.14610  0.14430  257 ALA G N   
5076 C CA  . ALA D 257 ? 0.62780 0.75400 0.94170 0.13820  0.15460  0.13250  257 ALA G CA  
5077 C C   . ALA D 257 ? 0.62360 0.74050 0.94930 0.16840  0.13990  0.14450  257 ALA G C   
5078 O O   . ALA D 257 ? 0.61160 0.71510 0.92690 0.16140  0.12560  0.16330  257 ALA G O   
5079 C CB  . ALA D 257 ? 0.66060 0.71660 0.94100 0.13030  0.16030  0.12630  257 ALA G CB  
5080 N N   . ASP D 258 ? 0.92030 1.04790 1.26630 0.20450  0.14160  0.13200  258 ASP G N   
5081 C CA  . ASP D 258 ? 0.92960 1.05100 1.28740 0.23970  0.12470  0.14270  258 ASP G CA  
5082 C C   . ASP D 258 ? 0.97860 1.01830 1.31860 0.26540  0.12050  0.14160  258 ASP G C   
5083 O O   . ASP D 258 ? 1.01120 1.04460 1.36180 0.28620  0.12790  0.11580  258 ASP G O   
5084 C CB  . ASP D 258 ? 0.89640 1.10180 1.29770 0.26480  0.12400  0.12750  258 ASP G CB  
5085 C CG  . ASP D 258 ? 0.85100 1.12710 1.27290 0.23970  0.12010  0.13580  258 ASP G CG  
5086 O OD1 . ASP D 258 ? 0.83430 1.09880 1.24720 0.23440  0.10370  0.15560  258 ASP G OD1 
5087 O OD2 . ASP D 258 ? 0.83030 1.17480 1.27720 0.22360  0.13260  0.12240  258 ASP G OD2 
5088 N N   . PHE D 259 ? 0.67530 0.65460 0.98870 0.26310  0.10720  0.16920  259 PHE G N   
5089 C CA  . PHE D 259 ? 0.71470 0.60320 1.00720 0.27860  0.09970  0.17760  259 PHE G CA  
5090 C C   . PHE D 259 ? 0.76570 0.64270 1.06860 0.32420  0.07820  0.19000  259 PHE G C   
5091 O O   . PHE D 259 ? 0.77220 0.64810 1.06090 0.32470  0.06410  0.22110  259 PHE G O   
5092 C CB  . PHE D 259 ? 0.71820 0.55200 0.97230 0.24250  0.09920  0.20480  259 PHE G CB  
5093 C CG  . PHE D 259 ? 0.71140 0.54190 0.95240 0.20310  0.11650  0.18960  259 PHE G CG  
5094 C CD1 . PHE D 259 ? 0.74040 0.51280 0.97260 0.19810  0.12470  0.17230  259 PHE G CD1 
5095 C CD2 . PHE D 259 ? 0.65990 0.54220 0.89750 0.17310  0.12100  0.19090  259 PHE G CD2 
5096 C CE1 . PHE D 259 ? 0.72430 0.49760 0.94360 0.16460  0.13870  0.15680  259 PHE G CE1 
5097 C CE2 . PHE D 259 ? 0.65520 0.53190 0.87860 0.14130  0.13290  0.17680  259 PHE G CE2 
5098 C CZ  . PHE D 259 ? 0.68790 0.51290 0.90140 0.13730  0.14250  0.16010  259 PHE G CZ  
5099 N N   . PRO D 260 ? 0.90170 0.77460 1.22840 0.36610  0.07280  0.16500  260 PRO G N   
5100 C CA  . PRO D 260 ? 0.93460 0.78690 1.26860 0.41440  0.04720  0.17640  260 PRO G CA  
5101 C C   . PRO D 260 ? 0.98920 0.72410 1.28570 0.41510  0.03080  0.20930  260 PRO G C   
5102 O O   . PRO D 260 ? 1.02760 0.68900 1.31180 0.40350  0.03550  0.20090  260 PRO G O   
5103 C CB  . PRO D 260 ? 0.95170 0.83610 1.32390 0.45850  0.04650  0.13150  260 PRO G CB  
5104 C CG  . PRO D 260 ? 0.96090 0.83540 1.33070 0.43280  0.06930  0.10340  260 PRO G CG  
5105 C CD  . PRO D 260 ? 0.90840 0.80230 1.25640 0.37470  0.08790  0.12230  260 PRO G CD  
5106 N N   . LEU D 261 ? 1.02860 0.75130 1.30170 0.41970  0.00960  0.24370  261 LEU G N   
5107 C CA  . LEU D 261 ? 1.11690 0.73740 1.34530 0.41060  -0.01170 0.27380  261 LEU G CA  
5108 C C   . LEU D 261 ? 1.19740 0.78000 1.43130 0.45970  -0.04660 0.26290  261 LEU G C   
5109 O O   . LEU D 261 ? 1.17250 0.81810 1.44730 0.49970  -0.05290 0.23020  261 LEU G O   
5110 C CB  . LEU D 261 ? 1.09740 0.72890 1.28860 0.37910  -0.01390 0.31860  261 LEU G CB  
5111 C CG  . LEU D 261 ? 1.06400 0.68220 1.23170 0.32420  0.00910  0.33650  261 LEU G CG  
5112 C CD1 . LEU D 261 ? 1.00880 0.66110 1.20780 0.31000  0.03730  0.30460  261 LEU G CD1 
5113 C CD2 . LEU D 261 ? 1.02170 0.69750 1.16890 0.30400  0.00880  0.36660  261 LEU G CD2 
5114 N N   . GLY D 262 ? 1.46490 0.94530 1.65950 0.45440  -0.07130 0.28970  262 GLY G N   
5115 C CA  . GLY D 262 ? 1.56350 0.98810 1.76470 0.49850  -0.11120 0.28190  262 GLY G CA  
5116 C C   . GLY D 262 ? 1.64090 0.97210 1.84530 0.50540  -0.12190 0.25650  262 GLY G C   
5117 O O   . GLY D 262 ? 1.62980 0.92820 1.81640 0.47050  -0.09750 0.25200  262 GLY G O   
5118 N N   . PRO D 263 ? 1.69440 1.00260 1.95060 0.54000  -0.15020 0.24260  263 PRO G N   
5119 C CA  . PRO D 263 ? 1.71830 1.07280 2.02140 0.57810  -0.15830 0.26450  263 PRO G CA  
5120 C C   . PRO D 263 ? 1.79490 1.09250 2.05000 0.56030  -0.18860 0.32210  263 PRO G C   
5121 O O   . PRO D 263 ? 1.83370 1.15240 2.10960 0.59670  -0.19850 0.34370  263 PRO G O   
5122 C CB  . PRO D 263 ? 1.78640 1.10830 2.11870 0.63220  -0.14180 0.24480  263 PRO G CB  
5123 C CG  . PRO D 263 ? 1.84850 1.07710 2.14620 0.61080  -0.12160 0.24060  263 PRO G CG  
5124 C CD  . PRO D 263 ? 1.73770 1.00890 2.03330 0.55570  -0.10310 0.23280  263 PRO G CD  
5125 N N   . ALA D 264 ? 1.64420 0.85980 1.79610 0.51540  -0.19800 0.34330  264 ALA G N   
5126 C CA  . ALA D 264 ? 1.72730 0.88590 1.80430 0.49670  -0.21780 0.39770  264 ALA G CA  
5127 C C   . ALA D 264 ? 1.70930 0.84050 1.71270 0.44240  -0.18620 0.43160  264 ALA G C   
5128 O O   . ALA D 264 ? 1.80800 0.85490 1.74080 0.41460  -0.18810 0.47080  264 ALA G O   
5129 C CB  . ALA D 264 ? 1.80830 0.94420 1.98470 0.50450  -0.17910 0.46240  264 ALA G CB  
5130 N N   . THR D 265 ? 1.92980 1.15420 1.96560 0.41870  -0.14770 0.41590  265 THR G N   
5131 C CA  . THR D 265 ? 1.89280 1.13280 1.89690 0.35810  -0.11650 0.44430  265 THR G CA  
5132 C C   . THR D 265 ? 1.92020 1.18130 1.87880 0.34420  -0.12530 0.49220  265 THR G C   
5133 O O   . THR D 265 ? 1.89920 1.22050 1.86990 0.37760  -0.14040 0.49450  265 THR G O   
5134 C CB  . THR D 265 ? 1.74760 1.09080 1.79580 0.34290  -0.07900 0.41680  265 THR G CB  
5135 O OG1 . THR D 265 ? 1.68190 1.11840 1.76820 0.38280  -0.08180 0.39780  265 THR G OG1 
5136 C CG2 . THR D 265 ? 1.72160 1.03640 1.80000 0.33840  -0.06280 0.37700  265 THR G CG2 
5137 N N   . HIS D 266 ? 1.81250 1.03030 1.71930 0.29400  -0.11480 0.52810  266 HIS G N   
5138 C CA  . HIS D 266 ? 1.85010 1.08680 1.70640 0.27760  -0.12050 0.57450  266 HIS G CA  
5139 C C   . HIS D 266 ? 1.73030 1.08710 1.59880 0.24950  -0.09210 0.57710  266 HIS G C   
5140 O O   . HIS D 266 ? 1.73740 1.13930 1.57480 0.24560  -0.09710 0.60690  266 HIS G O   
5141 C CB  . HIS D 266 ? 1.97720 1.10810 1.76530 0.23930  -0.12120 0.61330  266 HIS G CB  
5142 N N   . GLY D 267 ? 1.52670 0.93490 1.43660 0.23220  -0.06440 0.54540  267 GLY G N   
5143 C CA  . GLY D 267 ? 1.40580 0.92740 1.33240 0.21760  -0.04330 0.53990  267 GLY G CA  
5144 C C   . GLY D 267 ? 1.39790 0.93980 1.28880 0.16290  -0.02490 0.56340  267 GLY G C   
5145 O O   . GLY D 267 ? 1.48380 0.95470 1.33490 0.12970  -0.02410 0.58630  267 GLY G O   
5146 N N   . GLY D 268 ? 1.29840 0.94390 1.20470 0.15480  -0.01090 0.55500  268 GLY G N   
5147 C CA  . GLY D 268 ? 1.27450 0.96490 1.16020 0.10710  0.00830  0.56380  268 GLY G CA  
5148 C C   . GLY D 268 ? 1.14600 0.93440 1.06960 0.10900  0.02160  0.53440  268 GLY G C   
5149 O O   . GLY D 268 ? 1.09010 0.91430 1.05010 0.14550  0.01520  0.51390  268 GLY G O   
5150 N N   . THR D 269 ? 1.02000 0.85210 0.93390 0.06850  0.03860  0.53080  269 THR G N   
5151 C CA  . THR D 269 ? 0.91390 0.83450 0.85690 0.06760  0.04720  0.50400  269 THR G CA  
5152 C C   . THR D 269 ? 0.86760 0.75160 0.84310 0.05810  0.06220  0.47260  269 THR G C   
5153 O O   . THR D 269 ? 0.90290 0.72600 0.86840 0.02820  0.07340  0.46910  269 THR G O   
5154 C CB  . THR D 269 ? 0.89840 0.89580 0.81530 0.03320  0.05480  0.50970  269 THR G CB  
5155 O OG1 . THR D 269 ? 0.94670 0.98300 0.83180 0.04340  0.04140  0.53770  269 THR G OG1 
5156 C CG2 . THR D 269 ? 0.81140 0.89720 0.75740 0.03600  0.05580  0.46870  269 THR G CG2 
5157 N N   . TYR D 270 ? 0.80730 0.73220 0.82040 0.07970  0.05930  0.43360  270 TYR G N   
5158 C CA  . TYR D 270 ? 0.77740 0.67250 0.81970 0.07520  0.07050  0.39600  270 TYR G CA  
5159 C C   . TYR D 270 ? 0.72410 0.68890 0.78310 0.06060  0.07330  0.35720  270 TYR G C   
5160 O O   . TYR D 270 ? 0.69350 0.73040 0.75960 0.07100  0.06090  0.34900  270 TYR G O   
5161 C CB  . TYR D 270 ? 0.78230 0.65360 0.85560 0.11460  0.06380  0.38400  270 TYR G CB  
5162 C CG  . TYR D 270 ? 0.84150 0.62880 0.90570 0.13580  0.05770  0.41080  270 TYR G CG  
5163 C CD1 . TYR D 270 ? 0.89590 0.67950 0.94260 0.16110  0.03930  0.44320  270 TYR G CD1 
5164 C CD2 . TYR D 270 ? 0.87670 0.58940 0.95020 0.13340  0.06630  0.39700  270 TYR G CD2 
5165 C CE1 . TYR D 270 ? 0.98390 0.68900 1.01840 0.17880  0.02610  0.45290  270 TYR G CE1 
5166 C CE2 . TYR D 270 ? 0.95660 0.59220 1.02240 0.15390  0.05340  0.40790  270 TYR G CE2 
5167 C CZ  . TYR D 270 ? 1.01500 0.64490 1.05970 0.17560  0.03190  0.43490  270 TYR G CZ  
5168 O OH  . TYR D 270 ? 1.11020 0.65860 1.14310 0.19630  0.01310  0.44190  270 TYR G OH  
5169 N N   . ARG D 271 ? 0.69160 0.63130 0.75730 0.03860  0.08660  0.33190  271 ARG G N   
5170 C CA  . ARG D 271 ? 0.64690 0.63250 0.73060 0.02980  0.08640  0.29330  271 ARG G CA  
5171 C C   . ARG D 271 ? 0.64310 0.58510 0.74650 0.03310  0.09620  0.27040  271 ARG G C   
5172 O O   . ARG D 271 ? 0.66790 0.54640 0.76830 0.03530  0.10530  0.27830  271 ARG G O   
5173 C CB  . ARG D 271 ? 0.64100 0.65690 0.70610 -0.00290 0.09110  0.28240  271 ARG G CB  
5174 C CG  . ARG D 271 ? 0.64740 0.73410 0.69650 -0.00490 0.08050  0.29360  271 ARG G CG  
5175 C CD  . ARG D 271 ? 0.65080 0.76830 0.68060 -0.03850 0.08870  0.28440  271 ARG G CD  
5176 N NE  . ARG D 271 ? 0.66880 0.85790 0.67730 -0.04270 0.08220  0.30010  271 ARG G NE  
5177 C CZ  . ARG D 271 ? 0.65970 0.93390 0.67470 -0.03540 0.06740  0.27170  271 ARG G CZ  
5178 N NH1 . ARG D 271 ? 0.62750 0.91670 0.66990 -0.02440 0.05480  0.22920  271 ARG G NH1 
5179 N NH2 . ARG D 271 ? 0.65480 1.00070 0.64720 -0.03910 0.06340  0.28590  271 ARG G NH2 
5180 N N   . CYS D 272 ? 0.59100 0.56730 0.71400 0.03370  0.09260  0.24170  272 CYS G N   
5181 C CA  . CYS D 272 ? 0.58430 0.53070 0.72020 0.03300  0.10310  0.22030  272 CYS G CA  
5182 C C   . CYS D 272 ? 0.54400 0.51250 0.67730 0.01220  0.10170  0.19320  272 CYS G C   
5183 O O   . CYS D 272 ? 0.53470 0.54810 0.66660 0.00620  0.08810  0.18590  272 CYS G O   
5184 C CB  . CYS D 272 ? 0.59840 0.55830 0.76230 0.05870  0.10050  0.21740  272 CYS G CB  
5185 S SG  . CYS D 272 ? 0.56630 0.59640 0.75410 0.06130  0.08350  0.20610  272 CYS G SG  
5186 N N   . PHE D 273 ? 0.51220 0.44820 0.64430 0.00430  0.11360  0.17610  273 PHE G N   
5187 C CA  . PHE D 273 ? 0.49000 0.43510 0.61520 -0.01300 0.11240  0.15040  273 PHE G CA  
5188 C C   . PHE D 273 ? 0.48790 0.42150 0.62280 -0.00700 0.11940  0.13690  273 PHE G C   
5189 O O   . PHE D 273 ? 0.51750 0.42370 0.65850 0.00470  0.13200  0.13940  273 PHE G O   
5190 C CB  . PHE D 273 ? 0.50410 0.42380 0.61010 -0.03430 0.12210  0.14140  273 PHE G CB  
5191 C CG  . PHE D 273 ? 0.52000 0.44980 0.61300 -0.04620 0.12150  0.15960  273 PHE G CG  
5192 C CD1 . PHE D 273 ? 0.55440 0.45440 0.64410 -0.03970 0.12630  0.18990  273 PHE G CD1 
5193 C CD2 . PHE D 273 ? 0.52110 0.49250 0.60360 -0.06400 0.11520  0.14570  273 PHE G CD2 
5194 C CE1 . PHE D 273 ? 0.57930 0.49030 0.65150 -0.05500 0.12640  0.21290  273 PHE G CE1 
5195 C CE2 . PHE D 273 ? 0.53990 0.53390 0.60850 -0.07860 0.11710  0.16320  273 PHE G CE2 
5196 C CZ  . PHE D 273 ? 0.56370 0.52650 0.62520 -0.07640 0.12370  0.19980  273 PHE G CZ  
5197 N N   . GLY D 274 ? 0.47940 0.43440 0.61410 -0.01450 0.10970  0.12230  274 GLY G N   
5198 C CA  . GLY D 274 ? 0.47790 0.42610 0.61310 -0.01500 0.11730  0.11160  274 GLY G CA  
5199 C C   . GLY D 274 ? 0.49010 0.41630 0.60400 -0.02760 0.12310  0.09030  274 GLY G C   
5200 O O   . GLY D 274 ? 0.48760 0.41410 0.58930 -0.03890 0.11610  0.08030  274 GLY G O   
5201 N N   . SER D 275 ? 0.48680 0.40160 0.59720 -0.02440 0.13640  0.08060  275 SER G N   
5202 C CA  . SER D 275 ? 0.50590 0.40600 0.59610 -0.03370 0.14050  0.05740  275 SER G CA  
5203 C C   . SER D 275 ? 0.51510 0.42750 0.59960 -0.03010 0.14700  0.05240  275 SER G C   
5204 O O   . SER D 275 ? 0.51960 0.45360 0.61850 -0.02290 0.15110  0.06650  275 SER G O   
5205 C CB  . SER D 275 ? 0.53370 0.39990 0.62140 -0.03530 0.15390  0.04560  275 SER G CB  
5206 O OG  . SER D 275 ? 0.57440 0.42290 0.67500 -0.01900 0.16770  0.04740  275 SER G OG  
5207 N N   . PHE D 276 ? 0.50750 0.41290 0.57040 -0.03610 0.14830  0.03160  276 PHE G N   
5208 C CA  . PHE D 276 ? 0.52820 0.45050 0.57510 -0.03690 0.15080  0.02830  276 PHE G CA  
5209 C C   . PHE D 276 ? 0.58940 0.50560 0.62620 -0.02950 0.16800  0.00290  276 PHE G C   
5210 O O   . PHE D 276 ? 0.60020 0.49110 0.63820 -0.02930 0.17200  -0.01710 276 PHE G O   
5211 C CB  . PHE D 276 ? 0.53240 0.45490 0.55590 -0.04830 0.12860  0.02610  276 PHE G CB  
5212 C CG  . PHE D 276 ? 0.50260 0.43150 0.53640 -0.05390 0.10670  0.04620  276 PHE G CG  
5213 C CD1 . PHE D 276 ? 0.49410 0.43910 0.53430 -0.05900 0.10310  0.06970  276 PHE G CD1 
5214 C CD2 . PHE D 276 ? 0.48620 0.41020 0.52430 -0.05530 0.08870  0.03870  276 PHE G CD2 
5215 C CE1 . PHE D 276 ? 0.48210 0.42920 0.53540 -0.06520 0.07930  0.08460  276 PHE G CE1 
5216 C CE2 . PHE D 276 ? 0.47380 0.40600 0.52330 -0.05710 0.06540  0.05060  276 PHE G CE2 
5217 C CZ  . PHE D 276 ? 0.46690 0.40620 0.52520 -0.06190 0.05950  0.07330  276 PHE G CZ  
5218 N N   . ARG D 277 ? 0.88560 0.82970 0.91220 -0.02560 0.17700  0.00310  277 ARG G N   
5219 C CA  . ARG D 277 ? 0.92590 0.87690 0.94220 -0.01510 0.19220  -0.02490 277 ARG G CA  
5220 C C   . ARG D 277 ? 0.94170 0.87280 0.93510 -0.02120 0.18430  -0.05130 277 ARG G C   
5221 O O   . ARG D 277 ? 0.92940 0.86120 0.90070 -0.03190 0.16740  -0.04640 277 ARG G O   
5222 C CB  . ARG D 277 ? 0.93230 0.93100 0.93370 -0.01420 0.20140  -0.01740 277 ARG G CB  
5223 C CG  . ARG D 277 ? 0.95020 0.98480 0.97710 0.00110  0.21970  -0.01590 277 ARG G CG  
5224 C CD  . ARG D 277 ? 0.95570 1.05160 0.96500 -0.00470 0.23010  -0.00590 277 ARG G CD  
5225 N NE  . ARG D 277 ? 0.98980 1.10570 0.97200 0.00360  0.23930  -0.03530 277 ARG G NE  
5226 C CZ  . ARG D 277 ? 0.99920 1.17150 0.95520 -0.00220 0.24900  -0.02950 277 ARG G CZ  
5227 N NH1 . ARG D 277 ? 0.98030 1.19080 0.93370 -0.02140 0.25070  0.00780  277 ARG G NH1 
5228 N NH2 . ARG D 277 ? 1.01020 1.20420 0.94200 0.00980  0.25670  -0.06140 277 ARG G NH2 
5229 N N   . HIS D 278 ? 0.70480 0.61800 0.70580 -0.01310 0.19400  -0.08190 278 HIS G N   
5230 C CA  . HIS D 278 ? 0.69680 0.59780 0.68260 -0.01780 0.18940  -0.11500 278 HIS G CA  
5231 C C   . HIS D 278 ? 0.66660 0.54520 0.65520 -0.03450 0.17540  -0.11510 278 HIS G C   
5232 O O   . HIS D 278 ? 0.64660 0.52220 0.62550 -0.04070 0.17020  -0.14430 278 HIS G O   
5233 C CB  . HIS D 278 ? 0.70160 0.63470 0.65110 -0.01630 0.18460  -0.12470 278 HIS G CB  
5234 C CG  . HIS D 278 ? 0.71960 0.69060 0.66110 -0.00230 0.20020  -0.12780 278 HIS G CG  
5235 N ND1 . HIS D 278 ? 0.74430 0.74960 0.67480 -0.00530 0.20260  -0.09520 278 HIS G ND1 
5236 C CD2 . HIS D 278 ? 0.72300 0.71000 0.66700 0.01410  0.21370  -0.16190 278 HIS G CD2 
5237 C CE1 . HIS D 278 ? 0.74160 0.79020 0.66670 0.00760  0.21950  -0.10780 278 HIS G CE1 
5238 N NE2 . HIS D 278 ? 0.74240 0.78130 0.67550 0.02240  0.22570  -0.15040 278 HIS G NE2 
5239 N N   . SER D 279 ? 0.63170 0.50290 0.63430 -0.04120 0.16910  -0.08700 279 SER G N   
5240 C CA  . SER D 279 ? 0.60430 0.46520 0.61300 -0.05640 0.15880  -0.08880 279 SER G CA  
5241 C C   . SER D 279 ? 0.60270 0.44060 0.63640 -0.05980 0.16650  -0.06940 279 SER G C   
5242 O O   . SER D 279 ? 0.56910 0.41560 0.60940 -0.06190 0.15890  -0.04400 279 SER G O   
5243 C CB  . SER D 279 ? 0.59390 0.47560 0.58960 -0.06030 0.13730  -0.07690 279 SER G CB  
5244 O OG  . SER D 279 ? 0.59070 0.48480 0.55980 -0.05780 0.12550  -0.09620 279 SER G OG  
5245 N N   . PRO D 280 ? 0.66360 0.46960 0.71040 -0.06020 0.17860  -0.08140 280 PRO G N   
5246 C CA  . PRO D 280 ? 0.65720 0.43260 0.72360 -0.06070 0.18340  -0.05740 280 PRO G CA  
5247 C C   . PRO D 280 ? 0.63210 0.40440 0.70050 -0.08380 0.17830  -0.04380 280 PRO G C   
5248 O O   . PRO D 280 ? 0.63560 0.38540 0.71440 -0.08480 0.18040  -0.01720 280 PRO G O   
5249 C CB  . PRO D 280 ? 0.70590 0.44020 0.78440 -0.05310 0.19320  -0.07830 280 PRO G CB  
5250 C CG  . PRO D 280 ? 0.70780 0.45390 0.77480 -0.05800 0.19370  -0.11770 280 PRO G CG  
5251 C CD  . PRO D 280 ? 0.68610 0.48090 0.73050 -0.05480 0.18640  -0.11640 280 PRO G CD  
5252 N N   . TYR D 281 ? 0.61310 0.41280 0.67150 -0.10110 0.17100  -0.06070 281 TYR G N   
5253 C CA  . TYR D 281 ? 0.59470 0.40750 0.65580 -0.12390 0.16810  -0.05030 281 TYR G CA  
5254 C C   . TYR D 281 ? 0.57220 0.43600 0.62540 -0.12170 0.15240  -0.04580 281 TYR G C   
5255 O O   . TYR D 281 ? 0.55710 0.45030 0.61110 -0.13890 0.14860  -0.04520 281 TYR G O   
5256 C CB  . TYR D 281 ? 0.61170 0.42130 0.67530 -0.14950 0.17290  -0.07900 281 TYR G CB  
5257 C CG  . TYR D 281 ? 0.64700 0.40180 0.72140 -0.15130 0.18380  -0.09060 281 TYR G CG  
5258 C CD1 . TYR D 281 ? 0.67080 0.37540 0.75730 -0.16180 0.19040  -0.06590 281 TYR G CD1 
5259 C CD2 . TYR D 281 ? 0.65670 0.40840 0.72830 -0.14000 0.18450  -0.12700 281 TYR G CD2 
5260 C CE1 . TYR D 281 ? 0.72500 0.37080 0.82460 -0.16090 0.19520  -0.08010 281 TYR G CE1 
5261 C CE2 . TYR D 281 ? 0.69430 0.39790 0.77910 -0.13850 0.19160  -0.14460 281 TYR G CE2 
5262 C CZ  . TYR D 281 ? 0.73330 0.38070 0.83410 -0.14850 0.19570  -0.12220 281 TYR G CZ  
5263 O OH  . TYR D 281 ? 0.77450 0.36620 0.89110 -0.14440 0.19760  -0.14190 281 TYR G OH  
5264 N N   . GLU D 282 ? 0.57490 0.45170 0.62120 -0.10190 0.14180  -0.04390 282 GLU G N   
5265 C CA  . GLU D 282 ? 0.55300 0.46560 0.59620 -0.09580 0.12220  -0.03690 282 GLU G CA  
5266 C C   . GLU D 282 ? 0.53820 0.44580 0.59250 -0.08410 0.12290  -0.00330 282 GLU G C   
5267 O O   . GLU D 282 ? 0.53590 0.43120 0.59240 -0.07090 0.12600  0.00660  282 GLU G O   
5268 C CB  . GLU D 282 ? 0.56300 0.48540 0.59130 -0.08480 0.10580  -0.05330 282 GLU G CB  
5269 C CG  . GLU D 282 ? 0.57960 0.51740 0.59480 -0.08990 0.09630  -0.08900 282 GLU G CG  
5270 C CD  . GLU D 282 ? 0.58260 0.52140 0.57770 -0.07600 0.07590  -0.09720 282 GLU G CD  
5271 O OE1 . GLU D 282 ? 0.56800 0.51830 0.56160 -0.06850 0.05210  -0.09040 282 GLU G OE1 
5272 O OE2 . GLU D 282 ? 0.57650 0.50330 0.55660 -0.07270 0.08190  -0.11020 282 GLU G OE2 
5273 N N   . TRP D 283 ? 0.49170 0.41680 0.55290 -0.08890 0.12010  0.01320  283 TRP G N   
5274 C CA  . TRP D 283 ? 0.47530 0.40380 0.54760 -0.07580 0.11720  0.04200  283 TRP G CA  
5275 C C   . TRP D 283 ? 0.47370 0.44450 0.54860 -0.07030 0.09380  0.03960  283 TRP G C   
5276 O O   . TRP D 283 ? 0.48580 0.48720 0.55460 -0.07690 0.08090  0.01830  283 TRP G O   
5277 C CB  . TRP D 283 ? 0.48730 0.40150 0.56380 -0.08100 0.12890  0.06660  283 TRP G CB  
5278 C CG  . TRP D 283 ? 0.51120 0.37250 0.59010 -0.08150 0.14650  0.07090  283 TRP G CG  
5279 C CD1 . TRP D 283 ? 0.52830 0.36410 0.60690 -0.07750 0.15440  0.05010  283 TRP G CD1 
5280 C CD2 . TRP D 283 ? 0.53400 0.35990 0.61540 -0.08380 0.15490  0.09610  283 TRP G CD2 
5281 N NE1 . TRP D 283 ? 0.56490 0.35230 0.64970 -0.07580 0.16630  0.05560  283 TRP G NE1 
5282 C CE2 . TRP D 283 ? 0.57270 0.34720 0.65900 -0.08000 0.16570  0.08550  283 TRP G CE2 
5283 C CE3 . TRP D 283 ? 0.54550 0.37750 0.62360 -0.08770 0.15240  0.12700  283 TRP G CE3 
5284 C CZ2 . TRP D 283 ? 0.62140 0.34130 0.71170 -0.07940 0.17090  0.10410  283 TRP G CZ2 
5285 C CZ3 . TRP D 283 ? 0.60340 0.38160 0.68080 -0.08940 0.15930  0.15090  283 TRP G CZ3 
5286 C CH2 . TRP D 283 ? 0.64240 0.36050 0.72710 -0.08490 0.16700  0.13910  283 TRP G CH2 
5287 N N   . SER D 284 ? 0.38890 0.36440 0.47630 -0.05680 0.08690  0.05830  284 SER G N   
5288 C CA  . SER D 284 ? 0.39010 0.40260 0.48570 -0.05010 0.06280  0.05710  284 SER G CA  
5289 C C   . SER D 284 ? 0.40660 0.45420 0.50110 -0.05360 0.06140  0.06110  284 SER G C   
5290 O O   . SER D 284 ? 0.40310 0.43970 0.49070 -0.06330 0.08010  0.07430  284 SER G O   
5291 C CB  . SER D 284 ? 0.36980 0.38240 0.48360 -0.03810 0.05820  0.07710  284 SER G CB  
5292 O OG  . SER D 284 ? 0.36820 0.37980 0.49010 -0.03100 0.07180  0.10040  284 SER G OG  
5293 N N   . ASP D 285 ? 0.45130 0.54230 0.55240 -0.04620 0.03710  0.04960  285 ASP G N   
5294 C CA  . ASP D 285 ? 0.45650 0.59440 0.55880 -0.04390 0.03330  0.05750  285 ASP G CA  
5295 C C   . ASP D 285 ? 0.44830 0.56910 0.55460 -0.03820 0.04840  0.09400  285 ASP G C   
5296 O O   . ASP D 285 ? 0.43200 0.52340 0.55080 -0.02820 0.05100  0.10620  285 ASP G O   
5297 C CB  . ASP D 285 ? 0.44880 0.63190 0.56440 -0.02910 0.00100  0.03810  285 ASP G CB  
5298 C CG  . ASP D 285 ? 0.41590 0.62600 0.52730 -0.02900 -0.02000 -0.00180 285 ASP G CG  
5299 O OD1 . ASP D 285 ? 0.44290 0.66030 0.54030 -0.04240 -0.00730 -0.01450 285 ASP G OD1 
5300 O OD2 . ASP D 285 ? 0.36670 0.59250 0.49120 -0.01460 -0.05200 -0.02280 285 ASP G OD2 
5301 N N   . PRO D 286 ? 0.40000 0.54100 0.49500 -0.04390 0.05790  0.11290  286 PRO G N   
5302 C CA  . PRO D 286 ? 0.40150 0.52550 0.49820 -0.03300 0.06580  0.14830  286 PRO G CA  
5303 C C   . PRO D 286 ? 0.40160 0.56070 0.51750 -0.01070 0.04540  0.14910  286 PRO G C   
5304 O O   . PRO D 286 ? 0.40100 0.61370 0.52220 -0.00580 0.02470  0.12910  286 PRO G O   
5305 C CB  . PRO D 286 ? 0.42750 0.57350 0.50220 -0.04750 0.07520  0.16860  286 PRO G CB  
5306 C CG  . PRO D 286 ? 0.42050 0.62990 0.48980 -0.05890 0.06540  0.13820  286 PRO G CG  
5307 C CD  . PRO D 286 ? 0.41110 0.60130 0.49100 -0.05950 0.05850  0.10260  286 PRO G CD  
5308 N N   . SER D 287 ? 0.40050 0.53280 0.52950 0.00410  0.04990  0.16870  287 SER G N   
5309 C CA  . SER D 287 ? 0.39910 0.56880 0.54650 0.02450  0.03340  0.17530  287 SER G CA  
5310 C C   . SER D 287 ? 0.42330 0.64040 0.55430 0.02910  0.02700  0.18890  287 SER G C   
5311 O O   . SER D 287 ? 0.43630 0.64730 0.54030 0.01500  0.04030  0.20450  287 SER G O   
5312 C CB  . SER D 287 ? 0.39810 0.53720 0.56030 0.04060  0.04250  0.19540  287 SER G CB  
5313 O OG  . SER D 287 ? 0.43260 0.54600 0.57560 0.04570  0.05440  0.22450  287 SER G OG  
5314 N N   . ASP D 288 ? 0.57840 0.84720 0.72580 0.04720  0.00590  0.18310  288 ASP G N   
5315 C CA  . ASP D 288 ? 0.58780 0.90630 0.71900 0.05780  -0.00040 0.20060  288 ASP G CA  
5316 C C   . ASP D 288 ? 0.63660 0.90970 0.74960 0.06270  0.01680  0.24280  288 ASP G C   
5317 O O   . ASP D 288 ? 0.62850 0.85010 0.75620 0.07090  0.02490  0.25070  288 ASP G O   
5318 C CB  . ASP D 288 ? 0.51670 0.89260 0.67390 0.08090  -0.02690 0.18610  288 ASP G CB  
5319 C CG  . ASP D 288 ? 0.45650 0.87290 0.63230 0.07850  -0.05080 0.14250  288 ASP G CG  
5320 O OD1 . ASP D 288 ? 0.46850 0.88600 0.63040 0.06290  -0.04830 0.12440  288 ASP G OD1 
5321 O OD2 . ASP D 288 ? 0.39610 0.84260 0.60260 0.09310  -0.07490 0.12410  288 ASP G OD2 
5322 N N   . PRO D 289 ? 0.60910 0.89970 0.68950 0.05810  0.02140  0.27070  289 PRO G N   
5323 C CA  . PRO D 289 ? 0.63690 0.87030 0.69710 0.06250  0.03320  0.31420  289 PRO G CA  
5324 C C   . PRO D 289 ? 0.63690 0.87760 0.71220 0.09800  0.01920  0.32760  289 PRO G C   
5325 O O   . PRO D 289 ? 0.58410 0.89110 0.67620 0.11570  0.00050  0.31130  289 PRO G O   
5326 C CB  . PRO D 289 ? 0.66800 0.93020 0.68660 0.04330  0.03880  0.34180  289 PRO G CB  
5327 C CG  . PRO D 289 ? 0.64150 1.00450 0.66390 0.04790  0.02250  0.31340  289 PRO G CG  
5328 C CD  . PRO D 289 ? 0.61040 0.97780 0.67000 0.04940  0.01410  0.26410  289 PRO G CD  
5329 N N   . LEU D 290 ? 0.69260 0.86580 0.76450 0.11020  0.02610  0.35410  290 LEU G N   
5330 C CA  . LEU D 290 ? 0.69830 0.87650 0.78140 0.14710  0.01220  0.36920  290 LEU G CA  
5331 C C   . LEU D 290 ? 0.75810 0.87630 0.80520 0.15350  0.01420  0.41670  290 LEU G C   
5332 O O   . LEU D 290 ? 0.78760 0.82720 0.82520 0.13930  0.02770  0.42780  290 LEU G O   
5333 C CB  . LEU D 290 ? 0.67070 0.82930 0.79720 0.16470  0.01310  0.34500  290 LEU G CB  
5334 C CG  . LEU D 290 ? 0.66670 0.84700 0.81560 0.20480  -0.00230 0.35020  290 LEU G CG  
5335 C CD1 . LEU D 290 ? 0.59480 0.86450 0.77010 0.21440  -0.02090 0.32710  290 LEU G CD1 
5336 C CD2 . LEU D 290 ? 0.67130 0.81290 0.85210 0.21940  0.00580  0.33590  290 LEU G CD2 
5337 N N   . LEU D 291 ? 0.74600 0.89880 0.77250 0.17490  -0.00160 0.44450  291 LEU G N   
5338 C CA  . LEU D 291 ? 0.84120 0.93570 0.82760 0.18080  -0.00510 0.49350  291 LEU G CA  
5339 C C   . LEU D 291 ? 0.87410 0.93370 0.87960 0.22230  -0.02010 0.48970  291 LEU G C   
5340 O O   . LEU D 291 ? 0.84750 0.96980 0.87380 0.25240  -0.03610 0.47440  291 LEU G O   
5341 C CB  . LEU D 291 ? 0.87490 1.02880 0.81990 0.17210  -0.01290 0.51580  291 LEU G CB  
5342 C CG  . LEU D 291 ? 0.98420 1.08910 0.88250 0.17300  -0.02150 0.55470  291 LEU G CG  
5343 C CD1 . LEU D 291 ? 1.01040 1.13270 0.91430 0.21910  -0.04550 0.55540  291 LEU G CD1 
5344 C CD2 . LEU D 291 ? 1.06200 1.04500 0.94210 0.15380  -0.01380 0.57380  291 LEU G CD2 
5345 N N   . VAL D 292 ? 0.93570 0.89870 0.93480 0.22350  -0.01720 0.49820  292 VAL G N   
5346 C CA  . VAL D 292 ? 0.98200 0.90490 0.99480 0.26390  -0.03400 0.49310  292 VAL G CA  
5347 C C   . VAL D 292 ? 1.09670 0.95680 1.05880 0.26560  -0.05030 0.53100  292 VAL G C   
5348 O O   . VAL D 292 ? 1.15480 0.95030 1.08100 0.23160  -0.04270 0.55460  292 VAL G O   
5349 C CB  . VAL D 292 ? 0.97350 0.83610 1.01880 0.27000  -0.02390 0.46860  292 VAL G CB  
5350 C CG1 . VAL D 292 ? 1.01930 0.85580 1.08260 0.31570  -0.04360 0.45700  292 VAL G CG1 
5351 C CG2 . VAL D 292 ? 0.86810 0.78900 0.95740 0.26170  -0.00650 0.43640  292 VAL G CG2 
5352 N N   . SER D 293 ? 1.40960 1.28880 1.36800 0.30300  -0.07420 0.53570  293 SER G N   
5353 C CA  . SER D 293 ? 1.53640 1.35790 1.44420 0.30970  -0.09540 0.57370  293 SER G CA  
5354 C C   . SER D 293 ? 1.60120 1.37150 1.52630 0.35660  -0.12130 0.56260  293 SER G C   
5355 O O   . SER D 293 ? 1.55060 1.38530 1.51560 0.39220  -0.13120 0.53360  293 SER G O   
5356 C CB  . SER D 293 ? 1.54090 1.44320 1.42030 0.31120  -0.10410 0.59220  293 SER G CB  
5357 O OG  . SER D 293 ? 1.46590 1.45910 1.38650 0.34480  -0.11340 0.55950  293 SER G OG  
5358 N N   . VAL D 294 ? 1.17030 1.24580 1.34050 0.04220  -0.18730 0.23510  294 VAL G N   
5359 C CA  . VAL D 294 ? 1.08920 1.17730 1.29240 0.04930  -0.18480 0.24640  294 VAL G CA  
5360 C C   . VAL D 294 ? 1.13820 1.21830 1.33190 0.05240  -0.19490 0.25540  294 VAL G C   
5361 O O   . VAL D 294 ? 1.22870 1.29390 1.39740 0.05490  -0.18800 0.25230  294 VAL G O   
5362 C CB  . VAL D 294 ? 1.06440 1.15490 1.27920 0.05590  -0.16220 0.24280  294 VAL G CB  
5368 C C1  . NAG E .   ? 0.74140 0.96490 1.15680 -0.03870 -0.15160 0.18790  401 NAG G C1  
5369 C C2  . NAG E .   ? 0.79910 1.01170 1.19370 -0.04310 -0.17100 0.18630  401 NAG G C2  
5370 C C3  . NAG E .   ? 0.84210 1.05170 1.22840 -0.03570 -0.16750 0.18780  401 NAG G C3  
5371 C C4  . NAG E .   ? 0.85910 1.08640 1.28220 -0.02910 -0.16090 0.20030  401 NAG G C4  
5372 C C5  . NAG E .   ? 0.78160 1.01780 1.22230 -0.02480 -0.14110 0.20060  401 NAG G C5  
5373 C C6  . NAG E .   ? 0.74200 0.99580 1.22050 -0.01790 -0.13280 0.21320  401 NAG G C6  
5374 C C7  . NAG E .   ? 0.87840 1.06850 1.23210 -0.05710 -0.18870 0.17180  401 NAG G C7  
5375 C C8  . NAG E .   ? 0.82900 0.99950 1.14360 -0.06030 -0.18950 0.15870  401 NAG G C8  
5376 N N2  . NAG E .   ? 0.80230 0.99710 1.16100 -0.04820 -0.17490 0.17400  401 NAG G N2  
5377 O O3  . NAG E .   ? 0.97420 1.17500 1.34450 -0.04010 -0.18660 0.18820  401 NAG G O3  
5378 O O4  . NAG E .   ? 0.72710 0.95020 1.14110 -0.02180 -0.15650 0.20110  401 NAG G O4  
5379 O O5  . NAG E .   ? 0.71150 0.95120 1.16030 -0.03220 -0.14540 0.19970  401 NAG G O5  
5380 O O6  . NAG E .   ? 0.70970 0.97730 1.21860 -0.02210 -0.14880 0.22550  401 NAG G O6  
5381 O O7  . NAG E .   ? 0.90400 1.10500 1.28420 -0.06240 -0.19990 0.18040  401 NAG G O7  
5382 C C1  . NAG F .   ? 0.91230 0.85670 0.82510 -0.00120 0.08280  0.07770  402 NAG G C1  
5383 C C2  . NAG F .   ? 1.10420 1.04240 1.00600 0.00030  0.09020  0.08300  402 NAG G C2  
5384 C C3  . NAG F .   ? 1.08520 1.01440 0.97090 0.00390  0.08760  0.08780  402 NAG G C3  
5385 C C4  . NAG F .   ? 1.09000 1.01950 0.96620 0.00610  0.07850  0.08470  402 NAG G C4  
5386 C C5  . NAG F .   ? 0.87540 0.81260 0.76610 0.00430  0.07210  0.08010  402 NAG G C5  
5387 C C6  . NAG F .   ? 1.03140 0.97050 0.91590 0.00580  0.06330  0.07700  402 NAG G C6  
5388 C C7  . NAG F .   ? 1.17130 1.11320 1.09010 -0.00430 0.10450  0.08650  402 NAG G C7  
5389 C C8  . NAG F .   ? 1.20180 1.14320 1.13300 -0.00760 0.11080  0.09080  402 NAG G C8  
5390 N N2  . NAG F .   ? 1.12880 1.06690 1.04140 -0.00240 0.09760  0.08630  402 NAG G N2  
5391 O O3  . NAG F .   ? 1.17160 1.09420 1.04410 0.00580  0.09480  0.09220  402 NAG G O3  
5392 O O4  . NAG F .   ? 1.23940 1.16070 1.10240 0.00900  0.07490  0.08970  402 NAG G O4  
5393 O O5  . NAG F .   ? 0.84970 0.79420 0.75310 0.00120  0.07550  0.07550  402 NAG G O5  
5394 O O6  . NAG F .   ? 1.06460 1.00550 0.94240 0.00560  0.06390  0.07310  402 NAG G O6  
5395 O O7  . NAG F .   ? 1.15830 1.10400 1.07380 -0.00330 0.10540  0.08360  402 NAG G O7  
5396 C C1  . NAG G .   ? 1.47880 1.14670 1.22010 -0.01030 0.07720  -0.05460 403 NAG G C1  
5397 C C2  . NAG G .   ? 1.55380 1.22070 1.28600 -0.00220 0.08690  -0.05440 403 NAG G C2  
5398 C C3  . NAG G .   ? 1.52780 1.20760 1.27650 0.00720  0.09920  -0.04850 403 NAG G C3  
5399 C C4  . NAG G .   ? 1.35430 1.02120 1.10280 0.01030  0.10440  -0.04780 403 NAG G C4  
5400 C C5  . NAG G .   ? 1.44860 1.11580 1.20370 0.00150  0.09380  -0.04860 403 NAG G C5  
5401 C C6  . NAG G .   ? 1.34520 0.99630 1.09750 0.00410  0.09840  -0.04840 403 NAG G C6  
5402 C C7  . NAG G .   ? 1.38650 1.09610 1.14590 -0.00770 0.07730  -0.04970 403 NAG G C7  
5403 C C8  . NAG G .   ? 1.32900 1.04890 1.08750 -0.01080 0.07150  -0.05030 403 NAG G C8  
5404 N N2  . NAG G .   ? 1.48880 1.17060 1.22450 -0.00550 0.08100  -0.05420 403 NAG G N2  
5405 O O3  . NAG G .   ? 1.43650 1.10980 1.17400 0.01510  0.10950  -0.04850 403 NAG G O3  
5406 O O4  . NAG G .   ? 1.19830 0.88140 0.96670 0.01780  0.11340  -0.04120 403 NAG G O4  
5407 O O5  . NAG G .   ? 1.53380 1.18690 1.27180 -0.00670 0.08330  -0.05450 403 NAG G O5  
5408 O O6  . NAG G .   ? 1.33300 0.95450 1.05930 0.00870  0.10500  -0.05320 403 NAG G O6  
5409 O O7  . NAG G .   ? 1.32130 1.04610 1.10090 -0.00690 0.07870  -0.04530 403 NAG G O7  
5410 C C1  . NAG H .   ? 0.66140 0.60920 0.72390 -0.10230 -0.01000 0.01220  404 NAG G C1  
5411 C C2  . NAG H .   ? 0.56520 0.52790 0.64120 -0.09840 -0.00070 0.01830  404 NAG G C2  
5412 C C3  . NAG H .   ? 0.71360 0.69300 0.80000 -0.09620 -0.00030 0.02050  404 NAG G C3  
5413 C C4  . NAG H .   ? 0.78650 0.77010 0.88590 -0.10320 -0.00990 0.02200  404 NAG G C4  
5414 C C5  . NAG H .   ? 0.70360 0.67160 0.78800 -0.10720 -0.01980 0.01580  404 NAG G C5  
5415 C C6  . NAG H .   ? 0.68180 0.65190 0.77740 -0.11480 -0.03120 0.01710  404 NAG G C6  
5416 C C7  . NAG H .   ? 0.60650 0.56130 0.67160 -0.09080 0.01330  0.02000  404 NAG G C7  
5417 C C8  . NAG H .   ? 0.60890 0.56140 0.66210 -0.08320 0.02090  0.01900  404 NAG G C8  
5418 N N2  . NAG H .   ? 0.56050 0.51990 0.62490 -0.09140 0.00780  0.01720  404 NAG G N2  
5419 O O3  . NAG H .   ? 0.61570 0.60670 0.71340 -0.09280 0.00850  0.02620  404 NAG G O3  
5420 O O4  . NAG H .   ? 0.90710 0.90550 1.01510 -0.10020 -0.00930 0.02370  404 NAG G O4  
5421 O O5  . NAG H .   ? 0.69140 0.64310 0.76580 -0.10950 -0.01960 0.01370  404 NAG G O5  
5422 O O6  . NAG H .   ? 0.73260 0.68640 0.81080 -0.11810 -0.04030 0.01090  404 NAG G O6  
5423 O O7  . NAG H .   ? 0.68280 0.63540 0.75820 -0.09640 0.01190  0.02360  404 NAG G O7  
# 
