data_9GOY
# 
_entry.id   9GOY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9GOY         pdb_00009goy 10.2210/pdb9goy/pdb 
WWPDB D_1292139600 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GOY 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              cyrille.dreyfus@iginnovate.com 
_pdbx_contact_author.name_first         Cyrille 
_pdbx_contact_author.name_last          Dreyfus 
_pdbx_contact_author.name_mi            N. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0007-2979-0885 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dreyfus, C.' 1 0009-0007-2979-0885 
'Fritz, G.'   2 0000-0002-4571-8812 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Mabs 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1942-0870 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            17 
_citation.language                  ? 
_citation.page_first                2457471 
_citation.page_last                 2457471 
_citation.title                     
'Biparatopic binding of ISB 1442 to CD38 in trans enables increased cell antibody density and increased avidity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1080/19420862.2025.2457471 
_citation.pdbx_database_id_PubMed   39882744 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Loyau, J.'        1  ?                   
primary 'Monney, T.'       2  ?                   
primary 'Montefiori, M.'   3  ?                   
primary 'Bokhovchuk, F.'   4  ?                   
primary 'Streuli, J.'      5  ?                   
primary 'Blackburn, M.'    6  ?                   
primary 'Goepfert, A.'     7  ?                   
primary 'Caro, L.N.'       8  ?                   
primary 'Chakraborti, S.'  9  ?                   
primary 'De Angelis, S.'   10 ?                   
primary 'Grandclement, C.' 11 ?                   
primary 'Blein, S.'        12 ?                   
primary 'Mbow, M.L.'       13 ?                   
primary 'Srivastava, A.'   14 ?                   
primary 'Perro, M.'        15 ?                   
primary 'Sammicheli, S.'   16 ?                   
primary 'Zhukovsky, E.A.'  17 ?                   
primary 'Dyson, M.'        18 ?                   
primary 'Dreyfus, C.'      19 0009-0007-2979-0885 
# 
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 'ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1' 30781.818 1  3.2.2.-,3.2.2.6,2.4.99.20 
'N100D, N164A, N209D and N219D' ? 
;Extracellular domain of Uniprot entry P28907, containing the following mutations on the four N-linked glycosylation sites (N100D, N164A, N209D and N219D) and fused to a C-terminal 8-histidine peptide tag
;
2 polymer     man 'Fab E2-RecA heavy chain'                           24100.086 1  ?                         ? ? ? 
3 polymer     man 'Fab E2-RecA light chain'                           23414.951 1  ?                         ? ? ? 
4 non-polymer syn 'POTASSIUM ION'                                     39.098    2  ?                         ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                      35.453    2  ?                         ? ? ? 
6 water       nat water                                               18.015    81 ?                         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;2'-phospho-ADP-ribosyl cyclase,2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase,2'-phospho-cyclic-ADP-ribose transferase,ADP-ribosyl cyclase 1,ADPRC 1,Cyclic ADP-ribose hydrolase 1,cADPR hydrolase 1,T10
;
# 
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 
;RWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL
WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFATSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV
HVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF
LQCVKNPEDSSCTSEIHHHHHHHH
;
;RWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKILL
WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFATSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV
HVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF
LQCVKNPEDSSCTSEIHHHHHHHH
;
A ? 
2 'polypeptide(L)' no no 
;QVQLVQSGAEVKKPGSSVKVSCKASGLPDATYAIGWVRQAPGQGLEWMGRIIPRLDAEHYAQKFQGRVTITADESTSTAY
MELSSLRSEDTAVYYCARGLGYYLYSSYYFDIWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPV
TVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
;
;QVQLVQSGAEVKKPGSSVKVSCKASGLPDATYAIGWVRQAPGQGLEWMGRIIPRLDAEHYAQKFQGRVTITADESTSTAY
MELSSLRSEDTAVYYCARGLGYYLYSSYYFDIWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPV
TVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
;
H ? 
3 'polypeptide(L)' no no 
;EIVMTQSPATLSVSPGERATLSCRASQSVSSNLAWYQQKPGQAPRLLIYGASTRATGIPARFSGSGSGTEFTLTISSLQS
EDFAVYYCQQYNNWPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;EIVMTQSPATLSVSPGERATLSCRASQSVSSNLAWYQQKPGQAPRLLIYGASTRATGIPARFSGSGSGTEFTLTISSLQS
EDFAVYYCQQYNNWPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
L ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'POTASSIUM ION' K   
5 'CHLORIDE ION'  CL  
6 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   TRP n 
1 3   ARG n 
1 4   GLN n 
1 5   GLN n 
1 6   TRP n 
1 7   SER n 
1 8   GLY n 
1 9   PRO n 
1 10  GLY n 
1 11  THR n 
1 12  THR n 
1 13  LYS n 
1 14  ARG n 
1 15  PHE n 
1 16  PRO n 
1 17  GLU n 
1 18  THR n 
1 19  VAL n 
1 20  LEU n 
1 21  ALA n 
1 22  ARG n 
1 23  CYS n 
1 24  VAL n 
1 25  LYS n 
1 26  TYR n 
1 27  THR n 
1 28  GLU n 
1 29  ILE n 
1 30  HIS n 
1 31  PRO n 
1 32  GLU n 
1 33  MET n 
1 34  ARG n 
1 35  HIS n 
1 36  VAL n 
1 37  ASP n 
1 38  CYS n 
1 39  GLN n 
1 40  SER n 
1 41  VAL n 
1 42  TRP n 
1 43  ASP n 
1 44  ALA n 
1 45  PHE n 
1 46  LYS n 
1 47  GLY n 
1 48  ALA n 
1 49  PHE n 
1 50  ILE n 
1 51  SER n 
1 52  LYS n 
1 53  HIS n 
1 54  PRO n 
1 55  CYS n 
1 56  ASP n 
1 57  ILE n 
1 58  THR n 
1 59  GLU n 
1 60  GLU n 
1 61  ASP n 
1 62  TYR n 
1 63  GLN n 
1 64  PRO n 
1 65  LEU n 
1 66  MET n 
1 67  LYS n 
1 68  LEU n 
1 69  GLY n 
1 70  THR n 
1 71  GLN n 
1 72  THR n 
1 73  VAL n 
1 74  PRO n 
1 75  CYS n 
1 76  ASN n 
1 77  LYS n 
1 78  ILE n 
1 79  LEU n 
1 80  LEU n 
1 81  TRP n 
1 82  SER n 
1 83  ARG n 
1 84  ILE n 
1 85  LYS n 
1 86  ASP n 
1 87  LEU n 
1 88  ALA n 
1 89  HIS n 
1 90  GLN n 
1 91  PHE n 
1 92  THR n 
1 93  GLN n 
1 94  VAL n 
1 95  GLN n 
1 96  ARG n 
1 97  ASP n 
1 98  MET n 
1 99  PHE n 
1 100 THR n 
1 101 LEU n 
1 102 GLU n 
1 103 ASP n 
1 104 THR n 
1 105 LEU n 
1 106 LEU n 
1 107 GLY n 
1 108 TYR n 
1 109 LEU n 
1 110 ALA n 
1 111 ASP n 
1 112 ASP n 
1 113 LEU n 
1 114 THR n 
1 115 TRP n 
1 116 CYS n 
1 117 GLY n 
1 118 GLU n 
1 119 PHE n 
1 120 ALA n 
1 121 THR n 
1 122 SER n 
1 123 LYS n 
1 124 ILE n 
1 125 ASN n 
1 126 TYR n 
1 127 GLN n 
1 128 SER n 
1 129 CYS n 
1 130 PRO n 
1 131 ASP n 
1 132 TRP n 
1 133 ARG n 
1 134 LYS n 
1 135 ASP n 
1 136 CYS n 
1 137 SER n 
1 138 ASN n 
1 139 ASN n 
1 140 PRO n 
1 141 VAL n 
1 142 SER n 
1 143 VAL n 
1 144 PHE n 
1 145 TRP n 
1 146 LYS n 
1 147 THR n 
1 148 VAL n 
1 149 SER n 
1 150 ARG n 
1 151 ARG n 
1 152 PHE n 
1 153 ALA n 
1 154 GLU n 
1 155 ALA n 
1 156 ALA n 
1 157 CYS n 
1 158 ASP n 
1 159 VAL n 
1 160 VAL n 
1 161 HIS n 
1 162 VAL n 
1 163 MET n 
1 164 LEU n 
1 165 ASP n 
1 166 GLY n 
1 167 SER n 
1 168 ARG n 
1 169 SER n 
1 170 LYS n 
1 171 ILE n 
1 172 PHE n 
1 173 ASP n 
1 174 LYS n 
1 175 ASP n 
1 176 SER n 
1 177 THR n 
1 178 PHE n 
1 179 GLY n 
1 180 SER n 
1 181 VAL n 
1 182 GLU n 
1 183 VAL n 
1 184 HIS n 
1 185 ASN n 
1 186 LEU n 
1 187 GLN n 
1 188 PRO n 
1 189 GLU n 
1 190 LYS n 
1 191 VAL n 
1 192 GLN n 
1 193 THR n 
1 194 LEU n 
1 195 GLU n 
1 196 ALA n 
1 197 TRP n 
1 198 VAL n 
1 199 ILE n 
1 200 HIS n 
1 201 GLY n 
1 202 GLY n 
1 203 ARG n 
1 204 GLU n 
1 205 ASP n 
1 206 SER n 
1 207 ARG n 
1 208 ASP n 
1 209 LEU n 
1 210 CYS n 
1 211 GLN n 
1 212 ASP n 
1 213 PRO n 
1 214 THR n 
1 215 ILE n 
1 216 LYS n 
1 217 GLU n 
1 218 LEU n 
1 219 GLU n 
1 220 SER n 
1 221 ILE n 
1 222 ILE n 
1 223 SER n 
1 224 LYS n 
1 225 ARG n 
1 226 ASN n 
1 227 ILE n 
1 228 GLN n 
1 229 PHE n 
1 230 SER n 
1 231 CYS n 
1 232 LYS n 
1 233 ASN n 
1 234 ILE n 
1 235 TYR n 
1 236 ARG n 
1 237 PRO n 
1 238 ASP n 
1 239 LYS n 
1 240 PHE n 
1 241 LEU n 
1 242 GLN n 
1 243 CYS n 
1 244 VAL n 
1 245 LYS n 
1 246 ASN n 
1 247 PRO n 
1 248 GLU n 
1 249 ASP n 
1 250 SER n 
1 251 SER n 
1 252 CYS n 
1 253 THR n 
1 254 SER n 
1 255 GLU n 
1 256 ILE n 
1 257 HIS n 
1 258 HIS n 
1 259 HIS n 
1 260 HIS n 
1 261 HIS n 
1 262 HIS n 
1 263 HIS n 
1 264 HIS n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   ALA n 
2 10  GLU n 
2 11  VAL n 
2 12  LYS n 
2 13  LYS n 
2 14  PRO n 
2 15  GLY n 
2 16  SER n 
2 17  SER n 
2 18  VAL n 
2 19  LYS n 
2 20  VAL n 
2 21  SER n 
2 22  CYS n 
2 23  LYS n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  LEU n 
2 28  PRO n 
2 29  ASP n 
2 30  ALA n 
2 31  THR n 
2 32  TYR n 
2 33  ALA n 
2 34  ILE n 
2 35  GLY n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  GLN n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  MET n 
2 49  GLY n 
2 50  ARG n 
2 51  ILE n 
2 52  ILE n 
2 53  PRO n 
2 54  ARG n 
2 55  LEU n 
2 56  ASP n 
2 57  ALA n 
2 58  GLU n 
2 59  HIS n 
2 60  TYR n 
2 61  ALA n 
2 62  GLN n 
2 63  LYS n 
2 64  PHE n 
2 65  GLN n 
2 66  GLY n 
2 67  ARG n 
2 68  VAL n 
2 69  THR n 
2 70  ILE n 
2 71  THR n 
2 72  ALA n 
2 73  ASP n 
2 74  GLU n 
2 75  SER n 
2 76  THR n 
2 77  SER n 
2 78  THR n 
2 79  ALA n 
2 80  TYR n 
2 81  MET n 
2 82  GLU n 
2 83  LEU n 
2 84  SER n 
2 85  SER n 
2 86  LEU n 
2 87  ARG n 
2 88  SER n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  ARG n 
2 99  GLY n 
2 100 LEU n 
2 101 GLY n 
2 102 TYR n 
2 103 TYR n 
2 104 LEU n 
2 105 TYR n 
2 106 SER n 
2 107 SER n 
2 108 TYR n 
2 109 TYR n 
2 110 PHE n 
2 111 ASP n 
2 112 ILE n 
2 113 TRP n 
2 114 GLY n 
2 115 GLN n 
2 116 GLY n 
2 117 THR n 
2 118 LEU n 
2 119 VAL n 
2 120 THR n 
2 121 VAL n 
2 122 SER n 
2 123 SER n 
2 124 ALA n 
2 125 SER n 
2 126 THR n 
2 127 LYS n 
2 128 GLY n 
2 129 PRO n 
2 130 SER n 
2 131 VAL n 
2 132 PHE n 
2 133 PRO n 
2 134 LEU n 
2 135 ALA n 
2 136 PRO n 
2 137 SER n 
2 138 SER n 
2 139 LYS n 
2 140 SER n 
2 141 THR n 
2 142 SER n 
2 143 GLY n 
2 144 GLY n 
2 145 THR n 
2 146 ALA n 
2 147 ALA n 
2 148 LEU n 
2 149 GLY n 
2 150 CYS n 
2 151 LEU n 
2 152 VAL n 
2 153 LYS n 
2 154 ASP n 
2 155 TYR n 
2 156 PHE n 
2 157 PRO n 
2 158 GLU n 
2 159 PRO n 
2 160 VAL n 
2 161 THR n 
2 162 VAL n 
2 163 SER n 
2 164 TRP n 
2 165 ASN n 
2 166 SER n 
2 167 GLY n 
2 168 ALA n 
2 169 LEU n 
2 170 THR n 
2 171 SER n 
2 172 GLY n 
2 173 VAL n 
2 174 HIS n 
2 175 THR n 
2 176 PHE n 
2 177 PRO n 
2 178 ALA n 
2 179 VAL n 
2 180 LEU n 
2 181 GLN n 
2 182 SER n 
2 183 SER n 
2 184 GLY n 
2 185 LEU n 
2 186 TYR n 
2 187 SER n 
2 188 LEU n 
2 189 SER n 
2 190 SER n 
2 191 VAL n 
2 192 VAL n 
2 193 THR n 
2 194 VAL n 
2 195 PRO n 
2 196 SER n 
2 197 SER n 
2 198 SER n 
2 199 LEU n 
2 200 GLY n 
2 201 THR n 
2 202 GLN n 
2 203 THR n 
2 204 TYR n 
2 205 ILE n 
2 206 CYS n 
2 207 ASN n 
2 208 VAL n 
2 209 ASN n 
2 210 HIS n 
2 211 LYS n 
2 212 PRO n 
2 213 SER n 
2 214 ASN n 
2 215 THR n 
2 216 LYS n 
2 217 VAL n 
2 218 ASP n 
2 219 LYS n 
2 220 LYS n 
2 221 VAL n 
2 222 GLU n 
2 223 PRO n 
2 224 LYS n 
2 225 SER n 
2 226 CYS n 
3 1   GLU n 
3 2   ILE n 
3 3   VAL n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   ALA n 
3 10  THR n 
3 11  LEU n 
3 12  SER n 
3 13  VAL n 
3 14  SER n 
3 15  PRO n 
3 16  GLY n 
3 17  GLU n 
3 18  ARG n 
3 19  ALA n 
3 20  THR n 
3 21  LEU n 
3 22  SER n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  VAL n 
3 30  SER n 
3 31  SER n 
3 32  ASN n 
3 33  LEU n 
3 34  ALA n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  GLN n 
3 43  ALA n 
3 44  PRO n 
3 45  ARG n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  GLY n 
3 51  ALA n 
3 52  SER n 
3 53  THR n 
3 54  ARG n 
3 55  ALA n 
3 56  THR n 
3 57  GLY n 
3 58  ILE n 
3 59  PRO n 
3 60  ALA n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  GLU n 
3 71  PHE n 
3 72  THR n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  SER n 
3 81  GLU n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  VAL n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  TYR n 
3 92  ASN n 
3 93  ASN n 
3 94  TRP n 
3 95  PRO n 
3 96  TRP n 
3 97  THR n 
3 98  PHE n 
3 99  GLY n 
3 100 GLN n 
3 101 GLY n 
3 102 THR n 
3 103 LYS n 
3 104 VAL n 
3 105 GLU n 
3 106 ILE n 
3 107 LYS n 
3 108 ARG n 
3 109 THR n 
3 110 VAL n 
3 111 ALA n 
3 112 ALA n 
3 113 PRO n 
3 114 SER n 
3 115 VAL n 
3 116 PHE n 
3 117 ILE n 
3 118 PHE n 
3 119 PRO n 
3 120 PRO n 
3 121 SER n 
3 122 ASP n 
3 123 GLU n 
3 124 GLN n 
3 125 LEU n 
3 126 LYS n 
3 127 SER n 
3 128 GLY n 
3 129 THR n 
3 130 ALA n 
3 131 SER n 
3 132 VAL n 
3 133 VAL n 
3 134 CYS n 
3 135 LEU n 
3 136 LEU n 
3 137 ASN n 
3 138 ASN n 
3 139 PHE n 
3 140 TYR n 
3 141 PRO n 
3 142 ARG n 
3 143 GLU n 
3 144 ALA n 
3 145 LYS n 
3 146 VAL n 
3 147 GLN n 
3 148 TRP n 
3 149 LYS n 
3 150 VAL n 
3 151 ASP n 
3 152 ASN n 
3 153 ALA n 
3 154 LEU n 
3 155 GLN n 
3 156 SER n 
3 157 GLY n 
3 158 ASN n 
3 159 SER n 
3 160 GLN n 
3 161 GLU n 
3 162 SER n 
3 163 VAL n 
3 164 THR n 
3 165 GLU n 
3 166 GLN n 
3 167 ASP n 
3 168 SER n 
3 169 LYS n 
3 170 ASP n 
3 171 SER n 
3 172 THR n 
3 173 TYR n 
3 174 SER n 
3 175 LEU n 
3 176 SER n 
3 177 SER n 
3 178 THR n 
3 179 LEU n 
3 180 THR n 
3 181 LEU n 
3 182 SER n 
3 183 LYS n 
3 184 ALA n 
3 185 ASP n 
3 186 TYR n 
3 187 GLU n 
3 188 LYS n 
3 189 HIS n 
3 190 LYS n 
3 191 VAL n 
3 192 TYR n 
3 193 ALA n 
3 194 CYS n 
3 195 GLU n 
3 196 VAL n 
3 197 THR n 
3 198 HIS n 
3 199 GLN n 
3 200 GLY n 
3 201 LEU n 
3 202 SER n 
3 203 SER n 
3 204 PRO n 
3 205 VAL n 
3 206 THR n 
3 207 LYS n 
3 208 SER n 
3 209 PHE n 
3 210 ASN n 
3 211 ARG n 
3 212 GLY n 
3 213 GLU n 
3 214 CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 264 human ? CD38 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ?        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 226 ?     ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? Expi293F ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? ?        ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 214 ?     ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ?        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? 
? ? ? ? ? ? ?        ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
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 
K   non-polymer         . 'POTASSIUM ION' ? 'K 1'            39.098  
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 
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_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   ARG 1   45  ?   ?   ?   A . n 
A 1 2   TRP 2   46  46  TRP TRP A . n 
A 1 3   ARG 3   47  47  ARG ARG A . n 
A 1 4   GLN 4   48  48  GLN GLN A . n 
A 1 5   GLN 5   49  49  GLN GLN A . n 
A 1 6   TRP 6   50  50  TRP TRP A . n 
A 1 7   SER 7   51  51  SER SER A . n 
A 1 8   GLY 8   52  52  GLY GLY A . n 
A 1 9   PRO 9   53  53  PRO PRO A . n 
A 1 10  GLY 10  54  54  GLY GLY A . n 
A 1 11  THR 11  55  55  THR THR A . n 
A 1 12  THR 12  56  56  THR THR A . n 
A 1 13  LYS 13  57  57  LYS LYS A . n 
A 1 14  ARG 14  58  58  ARG ARG A . n 
A 1 15  PHE 15  59  59  PHE PHE A . n 
A 1 16  PRO 16  60  60  PRO PRO A . n 
A 1 17  GLU 17  61  61  GLU GLU A . n 
A 1 18  THR 18  62  62  THR THR A . n 
A 1 19  VAL 19  63  63  VAL VAL A . n 
A 1 20  LEU 20  64  64  LEU LEU A . n 
A 1 21  ALA 21  65  65  ALA ALA A . n 
A 1 22  ARG 22  66  66  ARG ARG A . n 
A 1 23  CYS 23  67  67  CYS CYS A . n 
A 1 24  VAL 24  68  68  VAL VAL A . n 
A 1 25  LYS 25  69  69  LYS LYS A . n 
A 1 26  TYR 26  70  70  TYR TYR A . n 
A 1 27  THR 27  71  71  THR THR A . n 
A 1 28  GLU 28  72  72  GLU GLU A . n 
A 1 29  ILE 29  73  73  ILE ILE A . n 
A 1 30  HIS 30  74  74  HIS HIS A . n 
A 1 31  PRO 31  75  75  PRO PRO A . n 
A 1 32  GLU 32  76  76  GLU GLU A . n 
A 1 33  MET 33  77  77  MET MET A . n 
A 1 34  ARG 34  78  78  ARG ARG A . n 
A 1 35  HIS 35  79  79  HIS HIS A . n 
A 1 36  VAL 36  80  80  VAL VAL A . n 
A 1 37  ASP 37  81  81  ASP ASP A . n 
A 1 38  CYS 38  82  82  CYS CYS A . n 
A 1 39  GLN 39  83  83  GLN GLN A . n 
A 1 40  SER 40  84  84  SER SER A . n 
A 1 41  VAL 41  85  85  VAL VAL A . n 
A 1 42  TRP 42  86  86  TRP TRP A . n 
A 1 43  ASP 43  87  87  ASP ASP A . n 
A 1 44  ALA 44  88  88  ALA ALA A . n 
A 1 45  PHE 45  89  89  PHE PHE A . n 
A 1 46  LYS 46  90  90  LYS LYS A . n 
A 1 47  GLY 47  91  91  GLY GLY A . n 
A 1 48  ALA 48  92  92  ALA ALA A . n 
A 1 49  PHE 49  93  93  PHE PHE A . n 
A 1 50  ILE 50  94  94  ILE ILE A . n 
A 1 51  SER 51  95  95  SER SER A . n 
A 1 52  LYS 52  96  96  LYS LYS A . n 
A 1 53  HIS 53  97  97  HIS HIS A . n 
A 1 54  PRO 54  98  98  PRO PRO A . n 
A 1 55  CYS 55  99  99  CYS CYS A . n 
A 1 56  ASP 56  100 100 ASP ASP A . n 
A 1 57  ILE 57  101 101 ILE ILE A . n 
A 1 58  THR 58  102 102 THR THR A . n 
A 1 59  GLU 59  103 103 GLU GLU A . n 
A 1 60  GLU 60  104 104 GLU GLU A . n 
A 1 61  ASP 61  105 105 ASP ASP A . n 
A 1 62  TYR 62  106 106 TYR TYR A . n 
A 1 63  GLN 63  107 107 GLN GLN A . n 
A 1 64  PRO 64  108 108 PRO PRO A . n 
A 1 65  LEU 65  109 109 LEU LEU A . n 
A 1 66  MET 66  110 110 MET MET A . n 
A 1 67  LYS 67  111 111 LYS LYS A . n 
A 1 68  LEU 68  112 112 LEU LEU A . n 
A 1 69  GLY 69  113 113 GLY GLY A . n 
A 1 70  THR 70  114 114 THR THR A . n 
A 1 71  GLN 71  115 115 GLN GLN A . n 
A 1 72  THR 72  116 116 THR THR A . n 
A 1 73  VAL 73  117 117 VAL VAL A . n 
A 1 74  PRO 74  118 118 PRO PRO A . n 
A 1 75  CYS 75  119 119 CYS CYS A . n 
A 1 76  ASN 76  120 120 ASN ASN A . n 
A 1 77  LYS 77  121 121 LYS LYS A . n 
A 1 78  ILE 78  122 122 ILE ILE A . n 
A 1 79  LEU 79  123 123 LEU LEU A . n 
A 1 80  LEU 80  124 124 LEU LEU A . n 
A 1 81  TRP 81  125 125 TRP TRP A . n 
A 1 82  SER 82  126 126 SER SER A . n 
A 1 83  ARG 83  127 127 ARG ARG A . n 
A 1 84  ILE 84  128 128 ILE ILE A . n 
A 1 85  LYS 85  129 129 LYS LYS A . n 
A 1 86  ASP 86  130 130 ASP ASP A . n 
A 1 87  LEU 87  131 131 LEU LEU A . n 
A 1 88  ALA 88  132 132 ALA ALA A . n 
A 1 89  HIS 89  133 133 HIS HIS A . n 
A 1 90  GLN 90  134 134 GLN GLN A . n 
A 1 91  PHE 91  135 135 PHE PHE A . n 
A 1 92  THR 92  136 136 THR THR A . n 
A 1 93  GLN 93  137 137 GLN GLN A . n 
A 1 94  VAL 94  138 138 VAL VAL A . n 
A 1 95  GLN 95  139 139 GLN GLN A . n 
A 1 96  ARG 96  140 140 ARG ARG A . n 
A 1 97  ASP 97  141 141 ASP ASP A . n 
A 1 98  MET 98  142 142 MET MET A . n 
A 1 99  PHE 99  143 143 PHE PHE A . n 
A 1 100 THR 100 144 144 THR THR A . n 
A 1 101 LEU 101 145 145 LEU LEU A . n 
A 1 102 GLU 102 146 146 GLU GLU A . n 
A 1 103 ASP 103 147 147 ASP ASP A . n 
A 1 104 THR 104 148 148 THR THR A . n 
A 1 105 LEU 105 149 149 LEU LEU A . n 
A 1 106 LEU 106 150 150 LEU LEU A . n 
A 1 107 GLY 107 151 151 GLY GLY A . n 
A 1 108 TYR 108 152 152 TYR TYR A . n 
A 1 109 LEU 109 153 153 LEU LEU A . n 
A 1 110 ALA 110 154 154 ALA ALA A . n 
A 1 111 ASP 111 155 155 ASP ASP A . n 
A 1 112 ASP 112 156 156 ASP ASP A . n 
A 1 113 LEU 113 157 157 LEU LEU A . n 
A 1 114 THR 114 158 158 THR THR A . n 
A 1 115 TRP 115 159 159 TRP TRP A . n 
A 1 116 CYS 116 160 160 CYS CYS A . n 
A 1 117 GLY 117 161 161 GLY GLY A . n 
A 1 118 GLU 118 162 162 GLU GLU A . n 
A 1 119 PHE 119 163 163 PHE PHE A . n 
A 1 120 ALA 120 164 164 ALA ALA A . n 
A 1 121 THR 121 165 165 THR THR A . n 
A 1 122 SER 122 166 166 SER SER A . n 
A 1 123 LYS 123 167 167 LYS LYS A . n 
A 1 124 ILE 124 168 168 ILE ILE A . n 
A 1 125 ASN 125 169 169 ASN ASN A . n 
A 1 126 TYR 126 170 170 TYR TYR A . n 
A 1 127 GLN 127 171 171 GLN GLN A . n 
A 1 128 SER 128 172 172 SER SER A . n 
A 1 129 CYS 129 173 173 CYS CYS A . n 
A 1 130 PRO 130 174 174 PRO PRO A . n 
A 1 131 ASP 131 175 175 ASP ASP A . n 
A 1 132 TRP 132 176 176 TRP TRP A . n 
A 1 133 ARG 133 177 177 ARG ARG A . n 
A 1 134 LYS 134 178 178 LYS LYS A . n 
A 1 135 ASP 135 179 179 ASP ASP A . n 
A 1 136 CYS 136 180 180 CYS CYS A . n 
A 1 137 SER 137 181 181 SER SER A . n 
A 1 138 ASN 138 182 182 ASN ASN A . n 
A 1 139 ASN 139 183 183 ASN ASN A . n 
A 1 140 PRO 140 184 184 PRO PRO A . n 
A 1 141 VAL 141 185 185 VAL VAL A . n 
A 1 142 SER 142 186 186 SER SER A . n 
A 1 143 VAL 143 187 187 VAL VAL A . n 
A 1 144 PHE 144 188 188 PHE PHE A . n 
A 1 145 TRP 145 189 189 TRP TRP A . n 
A 1 146 LYS 146 190 190 LYS LYS A . n 
A 1 147 THR 147 191 191 THR THR A . n 
A 1 148 VAL 148 192 192 VAL VAL A . n 
A 1 149 SER 149 193 193 SER SER A . n 
A 1 150 ARG 150 194 194 ARG ARG A . n 
A 1 151 ARG 151 195 195 ARG ARG A . n 
A 1 152 PHE 152 196 196 PHE PHE A . n 
A 1 153 ALA 153 197 197 ALA ALA A . n 
A 1 154 GLU 154 198 198 GLU GLU A . n 
A 1 155 ALA 155 199 199 ALA ALA A . n 
A 1 156 ALA 156 200 200 ALA ALA A . n 
A 1 157 CYS 157 201 201 CYS CYS A . n 
A 1 158 ASP 158 202 202 ASP ASP A . n 
A 1 159 VAL 159 203 203 VAL VAL A . n 
A 1 160 VAL 160 204 204 VAL VAL A . n 
A 1 161 HIS 161 205 205 HIS HIS A . n 
A 1 162 VAL 162 206 206 VAL VAL A . n 
A 1 163 MET 163 207 207 MET MET A . n 
A 1 164 LEU 164 208 208 LEU LEU A . n 
A 1 165 ASP 165 209 209 ASP ASP A . n 
A 1 166 GLY 166 210 210 GLY GLY A . n 
A 1 167 SER 167 211 211 SER SER A . n 
A 1 168 ARG 168 212 212 ARG ARG A . n 
A 1 169 SER 169 213 213 SER SER A . n 
A 1 170 LYS 170 214 214 LYS LYS A . n 
A 1 171 ILE 171 215 215 ILE ILE A . n 
A 1 172 PHE 172 216 216 PHE PHE A . n 
A 1 173 ASP 173 217 217 ASP ASP A . n 
A 1 174 LYS 174 218 218 LYS LYS A . n 
A 1 175 ASP 175 219 219 ASP ASP A . n 
A 1 176 SER 176 220 220 SER SER A . n 
A 1 177 THR 177 221 221 THR THR A . n 
A 1 178 PHE 178 222 222 PHE PHE A . n 
A 1 179 GLY 179 223 223 GLY GLY A . n 
A 1 180 SER 180 224 224 SER SER A . n 
A 1 181 VAL 181 225 225 VAL VAL A . n 
A 1 182 GLU 182 226 226 GLU GLU A . n 
A 1 183 VAL 183 227 227 VAL VAL A . n 
A 1 184 HIS 184 228 228 HIS HIS A . n 
A 1 185 ASN 185 229 229 ASN ASN A . n 
A 1 186 LEU 186 230 230 LEU LEU A . n 
A 1 187 GLN 187 231 231 GLN GLN A . n 
A 1 188 PRO 188 232 232 PRO PRO A . n 
A 1 189 GLU 189 233 233 GLU GLU A . n 
A 1 190 LYS 190 234 234 LYS LYS A . n 
A 1 191 VAL 191 235 235 VAL VAL A . n 
A 1 192 GLN 192 236 236 GLN GLN A . n 
A 1 193 THR 193 237 237 THR THR A . n 
A 1 194 LEU 194 238 238 LEU LEU A . n 
A 1 195 GLU 195 239 239 GLU GLU A . n 
A 1 196 ALA 196 240 240 ALA ALA A . n 
A 1 197 TRP 197 241 241 TRP TRP A . n 
A 1 198 VAL 198 242 242 VAL VAL A . n 
A 1 199 ILE 199 243 243 ILE ILE A . n 
A 1 200 HIS 200 244 244 HIS HIS A . n 
A 1 201 GLY 201 245 245 GLY GLY A . n 
A 1 202 GLY 202 246 246 GLY GLY A . n 
A 1 203 ARG 203 247 247 ARG ARG A . n 
A 1 204 GLU 204 248 248 GLU GLU A . n 
A 1 205 ASP 205 249 249 ASP ASP A . n 
A 1 206 SER 206 250 250 SER SER A . n 
A 1 207 ARG 207 251 251 ARG ARG A . n 
A 1 208 ASP 208 252 252 ASP ASP A . n 
A 1 209 LEU 209 253 253 LEU LEU A . n 
A 1 210 CYS 210 254 254 CYS CYS A . n 
A 1 211 GLN 211 255 255 GLN GLN A . n 
A 1 212 ASP 212 256 256 ASP ASP A . n 
A 1 213 PRO 213 257 257 PRO PRO A . n 
A 1 214 THR 214 258 258 THR THR A . n 
A 1 215 ILE 215 259 259 ILE ILE A . n 
A 1 216 LYS 216 260 260 LYS LYS A . n 
A 1 217 GLU 217 261 261 GLU GLU A . n 
A 1 218 LEU 218 262 262 LEU LEU A . n 
A 1 219 GLU 219 263 263 GLU GLU A . n 
A 1 220 SER 220 264 264 SER SER A . n 
A 1 221 ILE 221 265 265 ILE ILE A . n 
A 1 222 ILE 222 266 266 ILE ILE A . n 
A 1 223 SER 223 267 267 SER SER A . n 
A 1 224 LYS 224 268 268 LYS LYS A . n 
A 1 225 ARG 225 269 269 ARG ARG A . n 
A 1 226 ASN 226 270 270 ASN ASN A . n 
A 1 227 ILE 227 271 271 ILE ILE A . n 
A 1 228 GLN 228 272 272 GLN GLN A . n 
A 1 229 PHE 229 273 273 PHE PHE A . n 
A 1 230 SER 230 274 274 SER SER A . n 
A 1 231 CYS 231 275 275 CYS CYS A . n 
A 1 232 LYS 232 276 276 LYS LYS A . n 
A 1 233 ASN 233 277 277 ASN ASN A . n 
A 1 234 ILE 234 278 278 ILE ILE A . n 
A 1 235 TYR 235 279 279 TYR TYR A . n 
A 1 236 ARG 236 280 280 ARG ARG A . n 
A 1 237 PRO 237 281 281 PRO PRO A . n 
A 1 238 ASP 238 282 282 ASP ASP A . n 
A 1 239 LYS 239 283 283 LYS LYS A . n 
A 1 240 PHE 240 284 284 PHE PHE A . n 
A 1 241 LEU 241 285 285 LEU LEU A . n 
A 1 242 GLN 242 286 286 GLN GLN A . n 
A 1 243 CYS 243 287 287 CYS CYS A . n 
A 1 244 VAL 244 288 288 VAL VAL A . n 
A 1 245 LYS 245 289 289 LYS LYS A . n 
A 1 246 ASN 246 290 290 ASN ASN A . n 
A 1 247 PRO 247 291 ?   ?   ?   A . n 
A 1 248 GLU 248 292 ?   ?   ?   A . n 
A 1 249 ASP 249 293 ?   ?   ?   A . n 
A 1 250 SER 250 294 ?   ?   ?   A . n 
A 1 251 SER 251 295 ?   ?   ?   A . n 
A 1 252 CYS 252 296 ?   ?   ?   A . n 
A 1 253 THR 253 297 ?   ?   ?   A . n 
A 1 254 SER 254 298 ?   ?   ?   A . n 
A 1 255 GLU 255 299 ?   ?   ?   A . n 
A 1 256 ILE 256 300 ?   ?   ?   A . n 
A 1 257 HIS 257 301 ?   ?   ?   A . n 
A 1 258 HIS 258 302 ?   ?   ?   A . n 
A 1 259 HIS 259 303 ?   ?   ?   A . n 
A 1 260 HIS 260 304 ?   ?   ?   A . n 
A 1 261 HIS 261 305 ?   ?   ?   A . n 
A 1 262 HIS 262 306 ?   ?   ?   A . n 
A 1 263 HIS 263 307 ?   ?   ?   A . n 
A 1 264 HIS 264 308 ?   ?   ?   A . n 
B 2 1   GLN 1   1   1   GLN GLN H . n 
B 2 2   VAL 2   2   2   VAL VAL H . n 
B 2 3   GLN 3   3   3   GLN GLN H . n 
B 2 4   LEU 4   4   4   LEU LEU H . n 
B 2 5   VAL 5   5   5   VAL VAL H . n 
B 2 6   GLN 6   6   6   GLN GLN H . n 
B 2 7   SER 7   7   7   SER SER H . n 
B 2 8   GLY 8   8   8   GLY GLY H . n 
B 2 9   ALA 9   9   9   ALA ALA H . n 
B 2 10  GLU 10  10  10  GLU GLU H . n 
B 2 11  VAL 11  11  11  VAL VAL H . n 
B 2 12  LYS 12  12  12  LYS LYS H . n 
B 2 13  LYS 13  13  13  LYS LYS H . n 
B 2 14  PRO 14  14  14  PRO PRO H . n 
B 2 15  GLY 15  15  15  GLY GLY H . n 
B 2 16  SER 16  16  16  SER SER H . n 
B 2 17  SER 17  17  17  SER SER H . n 
B 2 18  VAL 18  18  18  VAL VAL H . n 
B 2 19  LYS 19  19  19  LYS LYS H . n 
B 2 20  VAL 20  20  20  VAL VAL H . n 
B 2 21  SER 21  21  21  SER SER H . n 
B 2 22  CYS 22  22  22  CYS CYS H . n 
B 2 23  LYS 23  23  23  LYS LYS H . n 
B 2 24  ALA 24  24  24  ALA ALA H . n 
B 2 25  SER 25  25  25  SER SER H . n 
B 2 26  GLY 26  26  26  GLY GLY H . n 
B 2 27  LEU 27  27  27  LEU LEU H . n 
B 2 28  PRO 28  28  28  PRO PRO H . n 
B 2 29  ASP 29  29  29  ASP ASP H . n 
B 2 30  ALA 30  30  30  ALA ALA H . n 
B 2 31  THR 31  31  31  THR THR H . n 
B 2 32  TYR 32  32  32  TYR TYR H . n 
B 2 33  ALA 33  33  33  ALA ALA H . n 
B 2 34  ILE 34  34  34  ILE ILE H . n 
B 2 35  GLY 35  35  35  GLY GLY H . n 
B 2 36  TRP 36  36  36  TRP TRP H . n 
B 2 37  VAL 37  37  37  VAL VAL H . n 
B 2 38  ARG 38  38  38  ARG ARG H . n 
B 2 39  GLN 39  39  39  GLN GLN H . n 
B 2 40  ALA 40  40  40  ALA ALA H . n 
B 2 41  PRO 41  41  41  PRO PRO H . n 
B 2 42  GLY 42  42  42  GLY GLY H . n 
B 2 43  GLN 43  43  43  GLN GLN H . n 
B 2 44  GLY 44  44  44  GLY GLY H . n 
B 2 45  LEU 45  45  45  LEU LEU H . n 
B 2 46  GLU 46  46  46  GLU GLU H . n 
B 2 47  TRP 47  47  47  TRP TRP H . n 
B 2 48  MET 48  48  48  MET MET H . n 
B 2 49  GLY 49  49  49  GLY GLY H . n 
B 2 50  ARG 50  50  50  ARG ARG H . n 
B 2 51  ILE 51  51  51  ILE ILE H . n 
B 2 52  ILE 52  52  52  ILE ILE H . n 
B 2 53  PRO 53  52  52  PRO PRO H A n 
B 2 54  ARG 54  53  53  ARG ARG H . n 
B 2 55  LEU 55  54  54  LEU LEU H . n 
B 2 56  ASP 56  55  55  ASP ASP H . n 
B 2 57  ALA 57  56  56  ALA ALA H . n 
B 2 58  GLU 58  57  57  GLU GLU H . n 
B 2 59  HIS 59  58  58  HIS HIS H . n 
B 2 60  TYR 60  59  59  TYR TYR H . n 
B 2 61  ALA 61  60  60  ALA ALA H . n 
B 2 62  GLN 62  61  61  GLN GLN H . n 
B 2 63  LYS 63  62  62  LYS LYS H . n 
B 2 64  PHE 64  63  63  PHE PHE H . n 
B 2 65  GLN 65  64  64  GLN GLN H . n 
B 2 66  GLY 66  65  65  GLY GLY H . n 
B 2 67  ARG 67  66  66  ARG ARG H . n 
B 2 68  VAL 68  67  67  VAL VAL H . n 
B 2 69  THR 69  68  68  THR THR H . n 
B 2 70  ILE 70  69  69  ILE ILE H . n 
B 2 71  THR 71  70  70  THR THR H . n 
B 2 72  ALA 72  71  71  ALA ALA H . n 
B 2 73  ASP 73  72  72  ASP ASP H . n 
B 2 74  GLU 74  73  73  GLU GLU H . n 
B 2 75  SER 75  74  74  SER SER H . n 
B 2 76  THR 76  75  75  THR THR H . n 
B 2 77  SER 77  76  76  SER SER H . n 
B 2 78  THR 78  77  77  THR THR H . n 
B 2 79  ALA 79  78  78  ALA ALA H . n 
B 2 80  TYR 80  79  79  TYR TYR H . n 
B 2 81  MET 81  80  80  MET MET H . n 
B 2 82  GLU 82  81  81  GLU GLU H . n 
B 2 83  LEU 83  82  82  LEU LEU H . n 
B 2 84  SER 84  82  82  SER SER H A n 
B 2 85  SER 85  82  82  SER SER H B n 
B 2 86  LEU 86  82  82  LEU LEU H C n 
B 2 87  ARG 87  83  83  ARG ARG H . n 
B 2 88  SER 88  84  84  SER SER H . n 
B 2 89  GLU 89  85  85  GLU GLU H . n 
B 2 90  ASP 90  86  86  ASP ASP H . n 
B 2 91  THR 91  87  87  THR THR H . n 
B 2 92  ALA 92  88  88  ALA ALA H . n 
B 2 93  VAL 93  89  89  VAL VAL H . n 
B 2 94  TYR 94  90  90  TYR TYR H . n 
B 2 95  TYR 95  91  91  TYR TYR H . n 
B 2 96  CYS 96  92  92  CYS CYS H . n 
B 2 97  ALA 97  93  93  ALA ALA H . n 
B 2 98  ARG 98  94  94  ARG ARG H . n 
B 2 99  GLY 99  95  95  GLY GLY H . n 
B 2 100 LEU 100 96  96  LEU LEU H . n 
B 2 101 GLY 101 97  97  GLY GLY H . n 
B 2 102 TYR 102 98  98  TYR TYR H . n 
B 2 103 TYR 103 99  99  TYR TYR H . n 
B 2 104 LEU 104 100 100 LEU LEU H . n 
B 2 105 TYR 105 100 100 TYR TYR H A n 
B 2 106 SER 106 100 100 SER SER H B n 
B 2 107 SER 107 100 100 SER SER H C n 
B 2 108 TYR 108 100 100 TYR TYR H D n 
B 2 109 TYR 109 100 100 TYR TYR H E n 
B 2 110 PHE 110 100 100 PHE PHE H F n 
B 2 111 ASP 111 101 101 ASP ASP H . n 
B 2 112 ILE 112 102 102 ILE ILE H . n 
B 2 113 TRP 113 103 103 TRP TRP H . n 
B 2 114 GLY 114 104 104 GLY GLY H . n 
B 2 115 GLN 115 105 105 GLN GLN H . n 
B 2 116 GLY 116 106 106 GLY GLY H . n 
B 2 117 THR 117 107 107 THR THR H . n 
B 2 118 LEU 118 108 108 LEU LEU H . n 
B 2 119 VAL 119 109 109 VAL VAL H . n 
B 2 120 THR 120 110 110 THR THR H . n 
B 2 121 VAL 121 111 111 VAL VAL H . n 
B 2 122 SER 122 112 112 SER SER H . n 
B 2 123 SER 123 113 113 SER SER H . n 
B 2 124 ALA 124 114 114 ALA ALA H . n 
B 2 125 SER 125 115 115 SER SER H . n 
B 2 126 THR 126 116 116 THR THR H . n 
B 2 127 LYS 127 117 117 LYS LYS H . n 
B 2 128 GLY 128 118 118 GLY GLY H . n 
B 2 129 PRO 129 119 119 PRO PRO H . n 
B 2 130 SER 130 120 120 SER SER H . n 
B 2 131 VAL 131 121 121 VAL VAL H . n 
B 2 132 PHE 132 122 122 PHE PHE H . n 
B 2 133 PRO 133 123 123 PRO PRO H . n 
B 2 134 LEU 134 124 124 LEU LEU H . n 
B 2 135 ALA 135 125 125 ALA ALA H . n 
B 2 136 PRO 136 126 126 PRO PRO H . n 
B 2 137 SER 137 127 127 SER SER H . n 
B 2 138 SER 138 128 128 SER SER H . n 
B 2 139 LYS 139 129 129 LYS LYS H . n 
B 2 140 SER 140 130 130 SER SER H . n 
B 2 141 THR 141 131 131 THR THR H . n 
B 2 142 SER 142 132 132 SER SER H . n 
B 2 143 GLY 143 133 133 GLY GLY H . n 
B 2 144 GLY 144 134 134 GLY GLY H . n 
B 2 145 THR 145 135 135 THR THR H . n 
B 2 146 ALA 146 136 136 ALA ALA H . n 
B 2 147 ALA 147 137 137 ALA ALA H . n 
B 2 148 LEU 148 138 138 LEU LEU H . n 
B 2 149 GLY 149 139 139 GLY GLY H . n 
B 2 150 CYS 150 140 140 CYS CYS H . n 
B 2 151 LEU 151 141 141 LEU LEU H . n 
B 2 152 VAL 152 142 142 VAL VAL H . n 
B 2 153 LYS 153 143 143 LYS LYS H . n 
B 2 154 ASP 154 144 144 ASP ASP H . n 
B 2 155 TYR 155 145 145 TYR TYR H . n 
B 2 156 PHE 156 146 146 PHE PHE H . n 
B 2 157 PRO 157 147 147 PRO PRO H . n 
B 2 158 GLU 158 148 148 GLU GLU H . n 
B 2 159 PRO 159 149 149 PRO PRO H . n 
B 2 160 VAL 160 150 150 VAL VAL H . n 
B 2 161 THR 161 151 151 THR THR H . n 
B 2 162 VAL 162 152 152 VAL VAL H . n 
B 2 163 SER 163 153 153 SER SER H . n 
B 2 164 TRP 164 154 154 TRP TRP H . n 
B 2 165 ASN 165 155 155 ASN ASN H . n 
B 2 166 SER 166 156 156 SER SER H . n 
B 2 167 GLY 167 157 157 GLY GLY H . n 
B 2 168 ALA 168 158 158 ALA ALA H . n 
B 2 169 LEU 169 159 159 LEU LEU H . n 
B 2 170 THR 170 160 160 THR THR H . n 
B 2 171 SER 171 161 161 SER SER H . n 
B 2 172 GLY 172 162 162 GLY GLY H . n 
B 2 173 VAL 173 163 163 VAL VAL H . n 
B 2 174 HIS 174 164 164 HIS HIS H . n 
B 2 175 THR 175 165 165 THR THR H . n 
B 2 176 PHE 176 166 166 PHE PHE H . n 
B 2 177 PRO 177 167 167 PRO PRO H . n 
B 2 178 ALA 178 168 168 ALA ALA H . n 
B 2 179 VAL 179 169 169 VAL VAL H . n 
B 2 180 LEU 180 170 170 LEU LEU H . n 
B 2 181 GLN 181 171 171 GLN GLN H . n 
B 2 182 SER 182 172 172 SER SER H . n 
B 2 183 SER 183 173 173 SER SER H . n 
B 2 184 GLY 184 174 174 GLY GLY H . n 
B 2 185 LEU 185 175 175 LEU LEU H . n 
B 2 186 TYR 186 176 176 TYR TYR H . n 
B 2 187 SER 187 177 177 SER SER H . n 
B 2 188 LEU 188 178 178 LEU LEU H . n 
B 2 189 SER 189 179 179 SER SER H . n 
B 2 190 SER 190 180 180 SER SER H . n 
B 2 191 VAL 191 181 181 VAL VAL H . n 
B 2 192 VAL 192 182 182 VAL VAL H . n 
B 2 193 THR 193 183 183 THR THR H . n 
B 2 194 VAL 194 184 184 VAL VAL H . n 
B 2 195 PRO 195 185 185 PRO PRO H . n 
B 2 196 SER 196 186 186 SER SER H . n 
B 2 197 SER 197 187 187 SER SER H . n 
B 2 198 SER 198 188 188 SER SER H . n 
B 2 199 LEU 199 189 189 LEU LEU H . n 
B 2 200 GLY 200 190 190 GLY GLY H . n 
B 2 201 THR 201 191 191 THR THR H . n 
B 2 202 GLN 202 192 192 GLN GLN H . n 
B 2 203 THR 203 193 193 THR THR H . n 
B 2 204 TYR 204 194 194 TYR TYR H . n 
B 2 205 ILE 205 195 195 ILE ILE H . n 
B 2 206 CYS 206 196 196 CYS CYS H . n 
B 2 207 ASN 207 197 197 ASN ASN H . n 
B 2 208 VAL 208 198 198 VAL VAL H . n 
B 2 209 ASN 209 199 199 ASN ASN H . n 
B 2 210 HIS 210 200 200 HIS HIS H . n 
B 2 211 LYS 211 201 201 LYS LYS H . n 
B 2 212 PRO 212 202 202 PRO PRO H . n 
B 2 213 SER 213 203 203 SER SER H . n 
B 2 214 ASN 214 204 204 ASN ASN H . n 
B 2 215 THR 215 205 205 THR THR H . n 
B 2 216 LYS 216 206 206 LYS LYS H . n 
B 2 217 VAL 217 207 207 VAL VAL H . n 
B 2 218 ASP 218 208 208 ASP ASP H . n 
B 2 219 LYS 219 209 209 LYS LYS H . n 
B 2 220 LYS 220 210 210 LYS LYS H . n 
B 2 221 VAL 221 211 211 VAL VAL H . n 
B 2 222 GLU 222 212 212 GLU GLU H . n 
B 2 223 PRO 223 213 213 PRO PRO H . n 
B 2 224 LYS 224 214 214 LYS LYS H . n 
B 2 225 SER 225 215 ?   ?   ?   H . n 
B 2 226 CYS 226 216 ?   ?   ?   H . n 
C 3 1   GLU 1   1   1   GLU GLU L . n 
C 3 2   ILE 2   2   2   ILE ILE L . n 
C 3 3   VAL 3   3   3   VAL VAL L . n 
C 3 4   MET 4   4   4   MET MET L . n 
C 3 5   THR 5   5   5   THR THR L . n 
C 3 6   GLN 6   6   6   GLN GLN L . n 
C 3 7   SER 7   7   7   SER SER L . n 
C 3 8   PRO 8   8   8   PRO PRO L . n 
C 3 9   ALA 9   9   9   ALA ALA L . n 
C 3 10  THR 10  10  10  THR THR L . n 
C 3 11  LEU 11  11  11  LEU LEU L . n 
C 3 12  SER 12  12  12  SER SER L . n 
C 3 13  VAL 13  13  13  VAL VAL L . n 
C 3 14  SER 14  14  14  SER SER L . n 
C 3 15  PRO 15  15  15  PRO PRO L . n 
C 3 16  GLY 16  16  16  GLY GLY L . n 
C 3 17  GLU 17  17  17  GLU GLU L . n 
C 3 18  ARG 18  18  18  ARG ARG L . n 
C 3 19  ALA 19  19  19  ALA ALA L . n 
C 3 20  THR 20  20  20  THR THR L . n 
C 3 21  LEU 21  21  21  LEU LEU L . n 
C 3 22  SER 22  22  22  SER SER L . n 
C 3 23  CYS 23  23  23  CYS CYS L . n 
C 3 24  ARG 24  24  24  ARG ARG L . n 
C 3 25  ALA 25  25  25  ALA ALA L . n 
C 3 26  SER 26  26  26  SER SER L . n 
C 3 27  GLN 27  27  27  GLN GLN L . n 
C 3 28  SER 28  28  28  SER SER L . n 
C 3 29  VAL 29  29  29  VAL VAL L . n 
C 3 30  SER 30  30  30  SER SER L . n 
C 3 31  SER 31  31  31  SER SER L . n 
C 3 32  ASN 32  32  32  ASN ASN L . n 
C 3 33  LEU 33  33  33  LEU LEU L . n 
C 3 34  ALA 34  34  34  ALA ALA L . n 
C 3 35  TRP 35  35  35  TRP TRP L . n 
C 3 36  TYR 36  36  36  TYR TYR L . n 
C 3 37  GLN 37  37  37  GLN GLN L . n 
C 3 38  GLN 38  38  38  GLN GLN L . n 
C 3 39  LYS 39  39  39  LYS LYS L . n 
C 3 40  PRO 40  40  40  PRO PRO L . n 
C 3 41  GLY 41  41  41  GLY GLY L . n 
C 3 42  GLN 42  42  42  GLN GLN L . n 
C 3 43  ALA 43  43  43  ALA ALA L . n 
C 3 44  PRO 44  44  44  PRO PRO L . n 
C 3 45  ARG 45  45  45  ARG ARG L . n 
C 3 46  LEU 46  46  46  LEU LEU L . n 
C 3 47  LEU 47  47  47  LEU LEU L . n 
C 3 48  ILE 48  48  48  ILE ILE L . n 
C 3 49  TYR 49  49  49  TYR TYR L . n 
C 3 50  GLY 50  50  50  GLY GLY L . n 
C 3 51  ALA 51  51  51  ALA ALA L . n 
C 3 52  SER 52  52  52  SER SER L . n 
C 3 53  THR 53  53  53  THR THR L . n 
C 3 54  ARG 54  54  54  ARG ARG L . n 
C 3 55  ALA 55  55  55  ALA ALA L . n 
C 3 56  THR 56  56  56  THR THR L . n 
C 3 57  GLY 57  57  57  GLY GLY L . n 
C 3 58  ILE 58  58  58  ILE ILE L . n 
C 3 59  PRO 59  59  59  PRO PRO L . n 
C 3 60  ALA 60  60  60  ALA ALA L . n 
C 3 61  ARG 61  61  61  ARG ARG L . n 
C 3 62  PHE 62  62  62  PHE PHE L . n 
C 3 63  SER 63  63  63  SER SER L . n 
C 3 64  GLY 64  64  64  GLY GLY L . n 
C 3 65  SER 65  65  65  SER SER L . n 
C 3 66  GLY 66  66  66  GLY GLY L . n 
C 3 67  SER 67  67  67  SER SER L . n 
C 3 68  GLY 68  68  68  GLY GLY L . n 
C 3 69  THR 69  69  69  THR THR L . n 
C 3 70  GLU 70  70  70  GLU GLU L . n 
C 3 71  PHE 71  71  71  PHE PHE L . n 
C 3 72  THR 72  72  72  THR THR L . n 
C 3 73  LEU 73  73  73  LEU LEU L . n 
C 3 74  THR 74  74  74  THR THR L . n 
C 3 75  ILE 75  75  75  ILE ILE L . n 
C 3 76  SER 76  76  76  SER SER L . n 
C 3 77  SER 77  77  77  SER SER L . n 
C 3 78  LEU 78  78  78  LEU LEU L . n 
C 3 79  GLN 79  79  79  GLN GLN L . n 
C 3 80  SER 80  80  80  SER SER L . n 
C 3 81  GLU 81  81  81  GLU GLU L . n 
C 3 82  ASP 82  82  82  ASP ASP L . n 
C 3 83  PHE 83  83  83  PHE PHE L . n 
C 3 84  ALA 84  84  84  ALA ALA L . n 
C 3 85  VAL 85  85  85  VAL VAL L . n 
C 3 86  TYR 86  86  86  TYR TYR L . n 
C 3 87  TYR 87  87  87  TYR TYR L . n 
C 3 88  CYS 88  88  88  CYS CYS L . n 
C 3 89  GLN 89  89  89  GLN GLN L . n 
C 3 90  GLN 90  90  90  GLN GLN L . n 
C 3 91  TYR 91  91  91  TYR TYR L . n 
C 3 92  ASN 92  92  92  ASN ASN L . n 
C 3 93  ASN 93  93  93  ASN ASN L . n 
C 3 94  TRP 94  94  94  TRP TRP L . n 
C 3 95  PRO 95  95  95  PRO PRO L . n 
C 3 96  TRP 96  96  96  TRP TRP L . n 
C 3 97  THR 97  97  97  THR THR L . n 
C 3 98  PHE 98  98  98  PHE PHE L . n 
C 3 99  GLY 99  99  99  GLY GLY L . n 
C 3 100 GLN 100 100 100 GLN GLN L . n 
C 3 101 GLY 101 101 101 GLY GLY L . n 
C 3 102 THR 102 102 102 THR THR L . n 
C 3 103 LYS 103 103 103 LYS LYS L . n 
C 3 104 VAL 104 104 104 VAL VAL L . n 
C 3 105 GLU 105 105 105 GLU GLU L . n 
C 3 106 ILE 106 106 106 ILE ILE L . n 
C 3 107 LYS 107 107 107 LYS LYS L . n 
C 3 108 ARG 108 108 108 ARG ARG L . n 
C 3 109 THR 109 109 109 THR THR L . n 
C 3 110 VAL 110 110 110 VAL VAL L . n 
C 3 111 ALA 111 111 111 ALA ALA L . n 
C 3 112 ALA 112 112 112 ALA ALA L . n 
C 3 113 PRO 113 113 113 PRO PRO L . n 
C 3 114 SER 114 114 114 SER SER L . n 
C 3 115 VAL 115 115 115 VAL VAL L . n 
C 3 116 PHE 116 116 116 PHE PHE L . n 
C 3 117 ILE 117 117 117 ILE ILE L . n 
C 3 118 PHE 118 118 118 PHE PHE L . n 
C 3 119 PRO 119 119 119 PRO PRO L . n 
C 3 120 PRO 120 120 120 PRO PRO L . n 
C 3 121 SER 121 121 121 SER SER L . n 
C 3 122 ASP 122 122 122 ASP ASP L . n 
C 3 123 GLU 123 123 123 GLU GLU L . n 
C 3 124 GLN 124 124 124 GLN GLN L . n 
C 3 125 LEU 125 125 125 LEU LEU L . n 
C 3 126 LYS 126 126 126 LYS LYS L . n 
C 3 127 SER 127 127 127 SER SER L . n 
C 3 128 GLY 128 128 128 GLY GLY L . n 
C 3 129 THR 129 129 129 THR THR L . n 
C 3 130 ALA 130 130 130 ALA ALA L . n 
C 3 131 SER 131 131 131 SER SER L . n 
C 3 132 VAL 132 132 132 VAL VAL L . n 
C 3 133 VAL 133 133 133 VAL VAL L . n 
C 3 134 CYS 134 134 134 CYS CYS L . n 
C 3 135 LEU 135 135 135 LEU LEU L . n 
C 3 136 LEU 136 136 136 LEU LEU L . n 
C 3 137 ASN 137 137 137 ASN ASN L . n 
C 3 138 ASN 138 138 138 ASN ASN L . n 
C 3 139 PHE 139 139 139 PHE PHE L . n 
C 3 140 TYR 140 140 140 TYR TYR L . n 
C 3 141 PRO 141 141 141 PRO PRO L . n 
C 3 142 ARG 142 142 142 ARG ARG L . n 
C 3 143 GLU 143 143 143 GLU GLU L . n 
C 3 144 ALA 144 144 144 ALA ALA L . n 
C 3 145 LYS 145 145 145 LYS LYS L . n 
C 3 146 VAL 146 146 146 VAL VAL L . n 
C 3 147 GLN 147 147 147 GLN GLN L . n 
C 3 148 TRP 148 148 148 TRP TRP L . n 
C 3 149 LYS 149 149 149 LYS LYS L . n 
C 3 150 VAL 150 150 150 VAL VAL L . n 
C 3 151 ASP 151 151 151 ASP ASP L . n 
C 3 152 ASN 152 152 152 ASN ASN L . n 
C 3 153 ALA 153 153 153 ALA ALA L . n 
C 3 154 LEU 154 154 154 LEU LEU L . n 
C 3 155 GLN 155 155 155 GLN GLN L . n 
C 3 156 SER 156 156 156 SER SER L . n 
C 3 157 GLY 157 157 157 GLY GLY L . n 
C 3 158 ASN 158 158 158 ASN ASN L . n 
C 3 159 SER 159 159 159 SER SER L . n 
C 3 160 GLN 160 160 160 GLN GLN L . n 
C 3 161 GLU 161 161 161 GLU GLU L . n 
C 3 162 SER 162 162 162 SER SER L . n 
C 3 163 VAL 163 163 163 VAL VAL L . n 
C 3 164 THR 164 164 164 THR THR L . n 
C 3 165 GLU 165 165 165 GLU GLU L . n 
C 3 166 GLN 166 166 166 GLN GLN L . n 
C 3 167 ASP 167 167 167 ASP ASP L . n 
C 3 168 SER 168 168 168 SER SER L . n 
C 3 169 LYS 169 169 169 LYS LYS L . n 
C 3 170 ASP 170 170 170 ASP ASP L . n 
C 3 171 SER 171 171 171 SER SER L . n 
C 3 172 THR 172 172 172 THR THR L . n 
C 3 173 TYR 173 173 173 TYR TYR L . n 
C 3 174 SER 174 174 174 SER SER L . n 
C 3 175 LEU 175 175 175 LEU LEU L . n 
C 3 176 SER 176 176 176 SER SER L . n 
C 3 177 SER 177 177 177 SER SER L . n 
C 3 178 THR 178 178 178 THR THR L . n 
C 3 179 LEU 179 179 179 LEU LEU L . n 
C 3 180 THR 180 180 180 THR THR L . n 
C 3 181 LEU 181 181 181 LEU LEU L . n 
C 3 182 SER 182 182 182 SER SER L . n 
C 3 183 LYS 183 183 183 LYS LYS L . n 
C 3 184 ALA 184 184 184 ALA ALA L . n 
C 3 185 ASP 185 185 185 ASP ASP L . n 
C 3 186 TYR 186 186 186 TYR TYR L . n 
C 3 187 GLU 187 187 187 GLU GLU L . n 
C 3 188 LYS 188 188 188 LYS LYS L . n 
C 3 189 HIS 189 189 189 HIS HIS L . n 
C 3 190 LYS 190 190 190 LYS LYS L . n 
C 3 191 VAL 191 191 191 VAL VAL L . n 
C 3 192 TYR 192 192 192 TYR TYR L . n 
C 3 193 ALA 193 193 193 ALA ALA L . n 
C 3 194 CYS 194 194 194 CYS CYS L . n 
C 3 195 GLU 195 195 195 GLU GLU L . n 
C 3 196 VAL 196 196 196 VAL VAL L . n 
C 3 197 THR 197 197 197 THR THR L . n 
C 3 198 HIS 198 198 198 HIS HIS L . n 
C 3 199 GLN 199 199 199 GLN GLN L . n 
C 3 200 GLY 200 200 200 GLY GLY L . n 
C 3 201 LEU 201 201 201 LEU LEU L . n 
C 3 202 SER 202 202 202 SER SER L . n 
C 3 203 SER 203 203 203 SER SER L . n 
C 3 204 PRO 204 204 204 PRO PRO L . n 
C 3 205 VAL 205 205 205 VAL VAL L . n 
C 3 206 THR 206 206 206 THR THR L . n 
C 3 207 LYS 207 207 207 LYS LYS L . n 
C 3 208 SER 208 208 208 SER SER L . n 
C 3 209 PHE 209 209 209 PHE PHE L . n 
C 3 210 ASN 210 210 210 ASN ASN L . n 
C 3 211 ARG 211 211 211 ARG ARG L . n 
C 3 212 GLY 212 212 212 GLY GLY L . n 
C 3 213 GLU 213 213 ?   ?   ?   L . n 
C 3 214 CYS 214 214 ?   ?   ?   L . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 K   1  401 1   K   K   A . 
E 4 K   1  402 2   K   K   A . 
F 5 CL  1  403 1   CL  CL  A . 
G 5 CL  1  301 2   CL  CL  L . 
H 6 HOH 1  501 72  HOH HOH A . 
H 6 HOH 2  502 14  HOH HOH A . 
H 6 HOH 3  503 62  HOH HOH A . 
H 6 HOH 4  504 76  HOH HOH A . 
H 6 HOH 5  505 47  HOH HOH A . 
H 6 HOH 6  506 73  HOH HOH A . 
H 6 HOH 7  507 102 HOH HOH A . 
H 6 HOH 8  508 98  HOH HOH A . 
H 6 HOH 9  509 79  HOH HOH A . 
H 6 HOH 10 510 27  HOH HOH A . 
H 6 HOH 11 511 19  HOH HOH A . 
H 6 HOH 12 512 29  HOH HOH A . 
H 6 HOH 13 513 86  HOH HOH A . 
H 6 HOH 14 514 99  HOH HOH A . 
H 6 HOH 15 515 11  HOH HOH A . 
H 6 HOH 16 516 58  HOH HOH A . 
H 6 HOH 17 517 2   HOH HOH A . 
H 6 HOH 18 518 95  HOH HOH A . 
H 6 HOH 19 519 48  HOH HOH A . 
H 6 HOH 20 520 43  HOH HOH A . 
H 6 HOH 21 521 100 HOH HOH A . 
H 6 HOH 22 522 101 HOH HOH A . 
H 6 HOH 23 523 88  HOH HOH A . 
H 6 HOH 24 524 25  HOH HOH A . 
H 6 HOH 25 525 53  HOH HOH A . 
H 6 HOH 26 526 21  HOH HOH A . 
H 6 HOH 27 527 52  HOH HOH A . 
H 6 HOH 28 528 28  HOH HOH A . 
H 6 HOH 29 529 91  HOH HOH A . 
I 6 HOH 1  301 83  HOH HOH H . 
I 6 HOH 2  302 39  HOH HOH H . 
I 6 HOH 3  303 40  HOH HOH H . 
I 6 HOH 4  304 78  HOH HOH H . 
I 6 HOH 5  305 87  HOH HOH H . 
I 6 HOH 6  306 6   HOH HOH H . 
I 6 HOH 7  307 17  HOH HOH H . 
I 6 HOH 8  308 74  HOH HOH H . 
I 6 HOH 9  309 4   HOH HOH H . 
I 6 HOH 10 310 16  HOH HOH H . 
I 6 HOH 11 311 5   HOH HOH H . 
I 6 HOH 12 312 3   HOH HOH H . 
I 6 HOH 13 313 34  HOH HOH H . 
I 6 HOH 14 314 49  HOH HOH H . 
I 6 HOH 15 315 56  HOH HOH H . 
I 6 HOH 16 316 44  HOH HOH H . 
I 6 HOH 17 317 9   HOH HOH H . 
I 6 HOH 18 318 33  HOH HOH H . 
I 6 HOH 19 319 94  HOH HOH H . 
I 6 HOH 20 320 50  HOH HOH H . 
I 6 HOH 21 321 81  HOH HOH H . 
I 6 HOH 22 322 71  HOH HOH H . 
I 6 HOH 23 323 80  HOH HOH H . 
J 6 HOH 1  401 70  HOH HOH L . 
J 6 HOH 2  402 93  HOH HOH L . 
J 6 HOH 3  403 67  HOH HOH L . 
J 6 HOH 4  404 59  HOH HOH L . 
J 6 HOH 5  405 23  HOH HOH L . 
J 6 HOH 6  406 32  HOH HOH L . 
J 6 HOH 7  407 20  HOH HOH L . 
J 6 HOH 8  408 97  HOH HOH L . 
J 6 HOH 9  409 68  HOH HOH L . 
J 6 HOH 10 410 15  HOH HOH L . 
J 6 HOH 11 411 41  HOH HOH L . 
J 6 HOH 12 412 60  HOH HOH L . 
J 6 HOH 13 413 75  HOH HOH L . 
J 6 HOH 14 414 36  HOH HOH L . 
J 6 HOH 15 415 26  HOH HOH L . 
J 6 HOH 16 416 92  HOH HOH L . 
J 6 HOH 17 417 85  HOH HOH L . 
J 6 HOH 18 418 51  HOH HOH L . 
J 6 HOH 19 419 65  HOH HOH L . 
J 6 HOH 20 420 24  HOH HOH L . 
J 6 HOH 21 421 7   HOH HOH L . 
J 6 HOH 22 422 84  HOH HOH L . 
J 6 HOH 23 423 63  HOH HOH L . 
J 6 HOH 24 424 82  HOH HOH L . 
J 6 HOH 25 425 64  HOH HOH L . 
J 6 HOH 26 426 10  HOH HOH L . 
J 6 HOH 27 427 69  HOH HOH L . 
J 6 HOH 28 428 18  HOH HOH L . 
J 6 HOH 29 429 66  HOH HOH L . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0352 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GOY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     131.290 
_cell.length_a_esd                 ? 
_cell.length_b                     61.070 
_cell.length_b_esd                 ? 
_cell.length_c                     124.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9GOY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9GOY 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.16 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    '70% v/v MPD, 0.1M HEPES, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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 EIGER2 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         2022-09-18 
_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   0.9998 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GOY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.7 
_reflns.d_resolution_low                               47.22 
_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                                     24595 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.85 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.62 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.307 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.7 
_reflns_shell.d_res_low                                     2.8 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.72 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1821 
_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                               3.32 
_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                                  0.44 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.64 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               2.88 
_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]                            1.71 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            4.22 
_refine.aniso_B[2][2]                            -3.97 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.48 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               82.112 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.938 
_refine.correlation_coeff_Fo_to_Fc_free          0.919 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GOY 
_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                            2.70 
_refine.ls_d_res_low                             47.22 
_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                     24595 
_refine.ls_number_reflns_R_free                  1295 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24481 
_refine.ls_R_factor_R_free                       0.27926 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.24304 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.909 
_refine.pdbx_overall_ESU_R_Free                  0.360 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             47.062 
_refine.overall_SU_ML                            0.410 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        47.22 
_refine_hist.number_atoms_solvent             81 
_refine_hist.number_atoms_total               5394 
_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        5309 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 0.002  0.012  5465  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  4932  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.610  1.647  7432  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.247  1.563  11495 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.326  5.000  687   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 1.761  5.000  29    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.545 10.000 909   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.030  0.200  823   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  6279  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1165  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.821  6.217  2734  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.821  6.217  2733  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.439  9.324  3416  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.438  9.324  3417  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.669  6.279  2731  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.669  6.279  2732  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.194  9.383  4013  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.729  75.583 5939  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.682  75.180 5936  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.700 
_refine_ls_shell.d_res_low                        2.770 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             96 
_refine_ls_shell.number_reflns_R_work             1821 
_refine_ls_shell.percent_reflns_obs               99.64 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.526 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.495 
# 
_struct.entry_id                     9GOY 
_struct.title                        'Crystal structure of Fab E2-RecA in complex with CD38' 
_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        9GOY 
_struct_keywords.text            'Fab, Biparatopic bispecific antibody, antibody, Innate cell modulator, CD38, 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 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J 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 CD38_HUMAN P28907 ? 1 
;RWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILL
WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV
HVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF
LQCVKNPEDSSCTSEI
;
45 
2 PDB 9GOY       9GOY   ? 2 ? 1  
3 PDB 9GOY       9GOY   ? 3 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GOY A 1 ? 256 ? P28907 45 ? 300 ? 45 300 
2 2 9GOY H 1 ? 226 ? 9GOY   1  ? 216 ? 1  216 
3 3 9GOY L 1 ? 214 ? 9GOY   1  ? 214 ? 1  214 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GOY ASP A 56  ? UNP P28907 ASN 100 'engineered mutation' 100 1  
1 9GOY ALA A 120 ? UNP P28907 ASN 164 'engineered mutation' 164 2  
1 9GOY ASP A 165 ? UNP P28907 ASN 209 'engineered mutation' 209 3  
1 9GOY ASP A 175 ? UNP P28907 ASN 219 'engineered mutation' 219 4  
1 9GOY HIS A 257 ? UNP P28907 ?   ?   'expression tag'      301 5  
1 9GOY HIS A 258 ? UNP P28907 ?   ?   'expression tag'      302 6  
1 9GOY HIS A 259 ? UNP P28907 ?   ?   'expression tag'      303 7  
1 9GOY HIS A 260 ? UNP P28907 ?   ?   'expression tag'      304 8  
1 9GOY HIS A 261 ? UNP P28907 ?   ?   'expression tag'      305 9  
1 9GOY HIS A 262 ? UNP P28907 ?   ?   'expression tag'      306 10 
1 9GOY HIS A 263 ? UNP P28907 ?   ?   'expression tag'      307 11 
1 9GOY HIS A 264 ? UNP P28907 ?   ?   'expression tag'      308 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ARG A 14  ? HIS A 30  ? ARG A 58  HIS A 74  1 ? 17 
HELX_P HELX_P2  AA2 PRO A 31  ? ARG A 34  ? PRO A 75  ARG A 78  5 ? 4  
HELX_P HELX_P3  AA3 ASP A 37  ? ILE A 50  ? ASP A 81  ILE A 94  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 62  ? GLY A 69  ? TYR A 106 GLY A 113 1 ? 8  
HELX_P HELX_P5  AA5 ILE A 84  ? GLN A 95  ? ILE A 128 GLN A 139 1 ? 12 
HELX_P HELX_P6  AA6 THR A 100 ? ASP A 103 ? THR A 144 ASP A 147 5 ? 4  
HELX_P HELX_P7  AA7 THR A 104 ? ASP A 111 ? THR A 148 ASP A 155 1 ? 8  
HELX_P HELX_P8  AA8 ASN A 139 ? ALA A 156 ? ASN A 183 ALA A 200 1 ? 18 
HELX_P HELX_P9  AA9 SER A 176 ? VAL A 181 ? SER A 220 VAL A 225 1 ? 6  
HELX_P HELX_P10 AB1 GLU A 182 ? LEU A 186 ? GLU A 226 LEU A 230 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 212 ? LYS A 224 ? ASP A 256 LYS A 268 1 ? 13 
HELX_P HELX_P12 AB3 ARG A 236 ? ASN A 246 ? ARG A 280 ASN A 290 1 ? 11 
HELX_P HELX_P13 AB4 ARG B 87  ? THR B 91  ? ARG H 83  THR H 87  5 ? 5  
HELX_P HELX_P14 AB5 SER B 137 ? THR B 141 ? SER H 127 THR H 131 5 ? 5  
HELX_P HELX_P15 AB6 SER B 197 ? GLY B 200 ? SER H 187 GLY H 190 5 ? 4  
HELX_P HELX_P16 AB7 LYS B 211 ? ASN B 214 ? LYS H 201 ASN H 204 5 ? 4  
HELX_P HELX_P17 AB8 GLN C 79  ? PHE C 83  ? GLN L 79  PHE L 83  5 ? 5  
HELX_P HELX_P18 AB9 SER C 121 ? GLY C 128 ? SER L 121 GLY L 128 1 ? 8  
HELX_P HELX_P19 AC1 LYS C 183 ? HIS C 189 ? LYS L 183 HIS L 189 1 ? 7  
# 
_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 23  SG  ? ? ? 1_555 A CYS 38  SG ? ? A CYS 67  A CYS 82  1_555 ? ? ? ? ? ? ? 2.971 ? ? 
disulf2 disulf ? ? A CYS 55  SG  ? ? ? 1_555 A CYS 136 SG ? ? A CYS 99  A CYS 180 1_555 ? ? ? ? ? ? ? 2.467 ? ? 
disulf3 disulf ? ? A CYS 75  SG  ? ? ? 1_555 A CYS 157 SG ? ? A CYS 119 A CYS 201 1_555 ? ? ? ? ? ? ? 2.817 ? ? 
disulf4 disulf ? ? A CYS 116 SG  ? ? ? 1_555 A CYS 129 SG ? ? A CYS 160 A CYS 173 1_555 ? ? ? ? ? ? ? 2.768 ? ? 
disulf5 disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? H CYS 22  H CYS 92  1_555 ? ? ? ? ? ? ? 2.617 ? ? 
disulf6 disulf ? ? B CYS 150 SG  ? ? ? 1_555 B CYS 206 SG ? ? H CYS 140 H CYS 196 1_555 ? ? ? ? ? ? ? 2.657 ? ? 
disulf7 disulf ? ? C CYS 23  SG  ? ? ? 1_555 C CYS 88  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.804 ? ? 
disulf8 disulf ? ? C CYS 134 SG  ? ? ? 1_555 C CYS 194 SG ? ? L CYS 134 L CYS 194 1_555 ? ? ? ? ? ? ? 2.667 ? ? 
metalc1 metalc ? ? A TRP 2   O   ? ? ? 1_555 E K   .   K  ? ? A TRP 46  A K   402 2_556 ? ? ? ? ? ? ? 3.245 ? ? 
metalc2 metalc ? ? A ASP 56  OD1 ? ? ? 1_555 E K   .   K  ? ? A ASP 100 A K   402 1_555 ? ? ? ? ? ? ? 3.316 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   TRP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    2 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    TRP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     46 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   K 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   K 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    K 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     402 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        2_556 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OD1 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   ASP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    56 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    ASP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     100 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 132.6 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 CYS A 23  ? CYS A 38  ? CYS A 67  ? 1_555 CYS A 82  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 55  ? CYS A 136 ? CYS A 99  ? 1_555 CYS A 180 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 75  ? CYS A 157 ? CYS A 119 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 116 ? CYS A 129 ? CYS A 160 ? 1_555 CYS A 173 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS B 22  ? CYS B 96  ? CYS H 22  ? 1_555 CYS H 92  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS B 150 ? CYS B 206 ? CYS H 140 ? 1_555 CYS H 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS C 23  ? CYS C 88  ? CYS L 23  ? 1_555 CYS L 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8 CYS C 134 ? CYS C 194 ? CYS L 134 ? 1_555 CYS L 194 ? 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 PHE 156 B . ? PHE 146 H PRO 157 B ? PRO 147 H 1 -7.93 
2 GLU 158 B . ? GLU 148 H PRO 159 B ? PRO 149 H 1 -2.76 
3 SER 7   C . ? SER 7   L PRO 8   C ? PRO 8   L 1 -4.92 
4 TRP 94  C . ? TRP 94  L PRO 95  C ? PRO 95  L 1 -1.01 
5 TYR 140 C . ? TYR 140 L PRO 141 C ? PRO 141 L 1 5.16  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
AA9 ? 4 ? 
AB1 ? 6 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? 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 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? 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 GLY A 8   ? PRO A 9   ? GLY A 52  PRO A 53  
AA1 2 SER A 128 ? CYS A 129 ? SER A 172 CYS A 173 
AA2 1 LEU A 79  ? TRP A 81  ? LEU A 123 TRP A 125 
AA2 2 ASP A 158 ? ASP A 165 ? ASP A 202 ASP A 209 
AA2 3 VAL A 191 ? ILE A 199 ? VAL A 235 ILE A 243 
AA2 4 GLN A 228 ? ILE A 234 ? GLN A 272 ILE A 278 
AA3 1 GLN B 3   ? GLN B 6   ? GLN H 3   GLN H 6   
AA3 2 VAL B 18  ? SER B 25  ? VAL H 18  SER H 25  
AA3 3 THR B 78  ? LEU B 83  ? THR H 77  LEU H 82  
AA3 4 VAL B 68  ? ASP B 73  ? VAL H 67  ASP H 72  
AA4 1 GLU B 10  ? LYS B 12  ? GLU H 10  LYS H 12  
AA4 2 THR B 117 ? VAL B 121 ? THR H 107 VAL H 111 
AA4 3 ALA B 92  ? LEU B 100 ? ALA H 88  LEU H 96  
AA4 4 ILE B 34  ? ALA B 40  ? ILE H 34  ALA H 40  
AA4 5 GLY B 44  ? ILE B 52  ? GLY H 44  ILE H 52  
AA4 6 ALA B 57  ? TYR B 60  ? ALA H 56  TYR H 59  
AA5 1 GLU B 10  ? LYS B 12  ? GLU H 10  LYS H 12  
AA5 2 THR B 117 ? VAL B 121 ? THR H 107 VAL H 111 
AA5 3 ALA B 92  ? LEU B 100 ? ALA H 88  LEU H 96  
AA5 4 TYR B 109 E TRP B 113 ? TYR H 100 TRP H 103 
AA6 1 SER B 130 ? LEU B 134 ? SER H 120 LEU H 124 
AA6 2 THR B 145 ? TYR B 155 ? THR H 135 TYR H 145 
AA6 3 TYR B 186 ? PRO B 195 ? TYR H 176 PRO H 185 
AA6 4 VAL B 173 ? THR B 175 ? VAL H 163 THR H 165 
AA7 1 SER B 130 ? LEU B 134 ? SER H 120 LEU H 124 
AA7 2 THR B 145 ? TYR B 155 ? THR H 135 TYR H 145 
AA7 3 TYR B 186 ? PRO B 195 ? TYR H 176 PRO H 185 
AA7 4 VAL B 179 ? LEU B 180 ? VAL H 169 LEU H 170 
AA8 1 THR B 161 ? TRP B 164 ? THR H 151 TRP H 154 
AA8 2 ILE B 205 ? HIS B 210 ? ILE H 195 HIS H 200 
AA8 3 THR B 215 ? LYS B 220 ? THR H 205 LYS H 210 
AA9 1 MET C 4   ? SER C 7   ? MET L 4   SER L 7   
AA9 2 ALA C 19  ? ALA C 25  ? ALA L 19  ALA L 25  
AA9 3 GLU C 70  ? ILE C 75  ? GLU L 70  ILE L 75  
AA9 4 PHE C 62  ? SER C 67  ? PHE L 62  SER L 67  
AB1 1 THR C 10  ? VAL C 13  ? THR L 10  VAL L 13  
AB1 2 THR C 102 ? ILE C 106 ? THR L 102 ILE L 106 
AB1 3 ALA C 84  ? GLN C 90  ? ALA L 84  GLN L 90  
AB1 4 LEU C 33  ? GLN C 38  ? LEU L 33  GLN L 38  
AB1 5 ARG C 45  ? TYR C 49  ? ARG L 45  TYR L 49  
AB1 6 THR C 53  ? ARG C 54  ? THR L 53  ARG L 54  
AB2 1 THR C 10  ? VAL C 13  ? THR L 10  VAL L 13  
AB2 2 THR C 102 ? ILE C 106 ? THR L 102 ILE L 106 
AB2 3 ALA C 84  ? GLN C 90  ? ALA L 84  GLN L 90  
AB2 4 THR C 97  ? PHE C 98  ? THR L 97  PHE L 98  
AB3 1 SER C 114 ? PHE C 118 ? SER L 114 PHE L 118 
AB3 2 THR C 129 ? PHE C 139 ? THR L 129 PHE L 139 
AB3 3 TYR C 173 ? SER C 182 ? TYR L 173 SER L 182 
AB3 4 SER C 159 ? GLN C 160 ? SER L 159 GLN L 160 
AB4 1 LYS C 145 ? VAL C 150 ? LYS L 145 VAL L 150 
AB4 2 TYR C 192 ? THR C 197 ? TYR L 192 THR L 197 
AB4 3 VAL C 205 ? PHE C 209 ? VAL L 205 PHE L 209 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 8   ? N GLY A 52  O CYS A 129 ? O CYS A 173 
AA2 1 2 N LEU A 80  ? N LEU A 124 O HIS A 161 ? O HIS A 205 
AA2 2 3 N VAL A 162 ? N VAL A 206 O TRP A 197 ? O TRP A 241 
AA2 3 4 N ALA A 196 ? N ALA A 240 O LYS A 232 ? O LYS A 276 
AA3 1 2 N VAL B 5   ? N VAL H 5   O LYS B 23  ? O LYS H 23  
AA3 2 3 N VAL B 20  ? N VAL H 20  O MET B 81  ? O MET H 80  
AA3 3 4 O TYR B 80  ? O TYR H 79  N THR B 71  ? N THR H 70  
AA4 1 2 N LYS B 12  ? N LYS H 12  O THR B 120 ? O THR H 110 
AA4 2 3 O THR B 117 ? O THR H 107 N TYR B 94  ? N TYR H 90  
AA4 3 4 O TYR B 95  ? O TYR H 91  N VAL B 37  ? N VAL H 37  
AA4 4 5 N ARG B 38  ? N ARG H 38  O GLU B 46  ? O GLU H 46  
AA4 5 6 N ILE B 52  ? N ILE H 52  O ALA B 57  ? O ALA H 56  
AA5 1 2 N LYS B 12  ? N LYS H 12  O THR B 120 ? O THR H 110 
AA5 2 3 O THR B 117 ? O THR H 107 N TYR B 94  ? N TYR H 90  
AA5 3 4 N LEU B 100 ? N LEU H 96  O TYR B 109 E O TYR H 100 
AA6 1 2 N PHE B 132 ? N PHE H 122 O LEU B 151 ? O LEU H 141 
AA6 2 3 N LEU B 148 ? N LEU H 138 O VAL B 192 ? O VAL H 182 
AA6 3 4 O VAL B 191 ? O VAL H 181 N HIS B 174 ? N HIS H 164 
AA7 1 2 N PHE B 132 ? N PHE H 122 O LEU B 151 ? O LEU H 141 
AA7 2 3 N LEU B 148 ? N LEU H 138 O VAL B 192 ? O VAL H 182 
AA7 3 4 O SER B 187 ? O SER H 177 N VAL B 179 ? N VAL H 169 
AA8 1 2 N SER B 163 ? N SER H 153 O ASN B 207 ? O ASN H 197 
AA8 2 3 N VAL B 208 ? N VAL H 198 O VAL B 217 ? O VAL H 207 
AA9 1 2 N THR C 5   ? N THR L 5   O ARG C 24  ? O ARG L 24  
AA9 2 3 N CYS C 23  ? N CYS L 23  O PHE C 71  ? O PHE L 71  
AA9 3 4 O THR C 72  ? O THR L 72  N SER C 65  ? N SER L 65  
AB1 1 2 N LEU C 11  ? N LEU L 11  O GLU C 105 ? O GLU L 105 
AB1 2 3 O VAL C 104 ? O VAL L 104 N ALA C 84  ? N ALA L 84  
AB1 3 4 O TYR C 87  ? O TYR L 87  N TYR C 36  ? N TYR L 36  
AB1 4 5 N TRP C 35  ? N TRP L 35  O LEU C 47  ? O LEU L 47  
AB1 5 6 N TYR C 49  ? N TYR L 49  O THR C 53  ? O THR L 53  
AB2 1 2 N LEU C 11  ? N LEU L 11  O GLU C 105 ? O GLU L 105 
AB2 2 3 O VAL C 104 ? O VAL L 104 N ALA C 84  ? N ALA L 84  
AB2 3 4 N GLN C 90  ? N GLN L 90  O THR C 97  ? O THR L 97  
AB3 1 2 N PHE C 118 ? N PHE L 118 O VAL C 133 ? O VAL L 133 
AB3 2 3 N VAL C 132 ? N VAL L 132 O LEU C 179 ? O LEU L 179 
AB3 3 4 O THR C 178 ? O THR L 178 N GLN C 160 ? N GLN L 160 
AB4 1 2 N GLN C 147 ? N GLN L 147 O GLU C 195 ? O GLU L 195 
AB4 2 3 N TYR C 192 ? N TYR L 192 O PHE C 209 ? O PHE L 209 
# 
_pdbx_entry_details.entry_id                   9GOY 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 100 ? ? -140.57 51.62   
2  1 LYS A 121 ? ? -111.18 58.33   
3  1 ASP A 179 ? ? -104.14 -78.16  
4  1 ASP A 202 ? ? 59.41   -118.40 
5  1 ARG A 212 ? ? -66.20  87.71   
6  1 SER A 213 ? ? 43.61   -127.87 
7  1 VAL A 225 ? ? -93.36  -62.75  
8  1 CYS H 22  ? ? -162.83 92.03   
9  1 SER H 130 ? ? -108.58 51.46   
10 1 ASP H 144 ? ? 58.83   70.77   
11 1 THR H 160 ? ? -130.52 -34.00  
12 1 SER L 30  ? ? 50.95   -127.25 
13 1 SER L 30  ? ? 51.21   -127.41 
14 1 ALA L 51  ? ? 83.75   -54.52  
15 1 SER L 76  ? ? -68.24  -82.12  
16 1 TYR L 91  ? ? -141.89 36.89   
17 1 ASN L 138 ? ? 58.01   83.85   
18 1 ASN L 158 ? ? -143.62 32.78   
19 1 LYS L 190 ? ? -108.90 -61.26  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -7.0984 -19.4714 42.6023 0.1717 ? 0.0048  ? -0.0411 ? 0.1874 ? 0.0044  ? 0.1820 ? 7.8596 ? 1.1299 
? -2.8553 ? 0.4934 ? -0.1861 ? 1.6357 ? -0.0612 ? 0.1552  ? -0.3600 ? -0.2053 ? -0.0345 ? 0.1007  ? -0.1135 ? -0.1437 ? 0.0957  ? 
2  'X-RAY DIFFRACTION' ? refined -0.0614 -23.4726 52.1341 0.2327 ? 0.0675  ? 0.1186  ? 0.2243 ? 0.0479  ? 0.2254 ? 4.4750 ? 0.2399 
? -2.1966 ? 0.4927 ? -0.0433 ? 2.5526 ? -0.1807 ? -0.1867 ? -0.0507 ? 0.0654  ? -0.0745 ? 0.1086  ? 0.1671  ? 0.1787  ? 0.2551  ? 
3  'X-RAY DIFFRACTION' ? refined 6.5181  -1.9326  47.4105 0.2770 ? -0.0826 ? -0.0166 ? 0.2174 ? 0.0075  ? 0.3099 ? 5.0231 ? 
-0.2412 ? -1.4431 ? 2.8385 ? -0.8292 ? 7.1004 ? -0.1044 ? 0.4386  ? 0.0550  ? -0.2527 ? -0.0682 ? 0.1554  ? -0.7574 ? 0.5054  ? 
0.1726  ? 
4  'X-RAY DIFFRACTION' ? refined -8.9402 -16.6137 50.5437 0.0920 ? 0.0197  ? 0.0544  ? 0.1331 ? 0.0223  ? 0.0551 ? 6.4213 ? 0.7750 
? -0.7902 ? 2.6352 ? 0.3807  ? 3.8167 ? -0.0128 ? -0.1037 ? -0.0841 ? -0.0285 ? -0.0551 ? 0.1887  ? 0.1959  ? -0.0774 ? 0.0680  ? 
5  'X-RAY DIFFRACTION' ? refined 2.1803  5.7506   55.5829 0.3531 ? 0.0035  ? 0.0488  ? 0.3691 ? -0.0331 ? 0.4148 ? 3.2467 ? 0.7924 
? -0.0866 ? 2.2837 ? 0.5430  ? 4.3114 ? 0.0054  ? 0.0640  ? 0.5812  ? -0.2664 ? -0.0028 ? 0.1936  ? -0.5873 ? -0.0627 ? -0.0027 ? 
6  'X-RAY DIFFRACTION' ? refined 9.8774  -26.4165 18.3245 0.1244 ? -0.0457 ? 0.0730  ? 0.1531 ? 0.0370  ? 0.2702 ? 2.7760 ? 1.1399 
? -1.5873 ? 4.2353 ? -0.0270 ? 3.0928 ? 0.0316  ? -0.0052 ? -0.1633 ? 0.1398  ? 0.2814  ? 0.2871  ? 0.1319  ? -0.3343 ? -0.3130 ? 
7  'X-RAY DIFFRACTION' ? refined 11.4113 -19.8018 26.3385 0.1357 ? -0.0142 ? 0.0204  ? 0.0383 ? 0.0459  ? 0.1910 ? 4.8118 ? 
-2.3852 ? -1.1754 ? 1.2016 ? 0.7929  ? 7.0482 ? 0.2139  ? 0.0925  ? 0.1976  ? -0.1197 ? -0.0418 ? -0.0576 ? -0.0526 ? -0.2445 ? 
-0.1721 ? 
8  'X-RAY DIFFRACTION' ? refined 7.2026  -17.2948 19.7876 0.1289 ? 0.0921  ? 0.0824  ? 0.2290 ? -0.0369 ? 0.2419 ? 3.2790 ? 1.0637 
? -0.2426 ? 6.5661 ? -0.8276 ? 3.2303 ? 0.1190  ? -0.2741 ? 0.2516  ? 0.1915  ? -0.0793 ? -0.3105 ? -0.2420 ? -0.1912 ? -0.0398 ? 
9  'X-RAY DIFFRACTION' ? refined 22.9866 -27.6700 6.8156  0.1818 ? -0.0128 ? 0.1518  ? 0.1013 ? 0.0144  ? 0.1901 ? 0.8303 ? 
-0.3312 ? -1.0319 ? 1.0732 ? 0.5719  ? 2.4642 ? -0.0646 ? 0.0058  ? 0.0567  ? -0.1965 ? 0.0709  ? -0.0411 ? 0.1117  ? -0.1794 ? 
-0.0063 ? 
10 'X-RAY DIFFRACTION' ? refined 25.5573 -34.3004 -5.3518 0.2789 ? -0.0183 ? 0.0884  ? 0.1252 ? 0.0197  ? 0.1868 ? 1.6446 ? 
-3.2861 ? -0.6948 ? 6.6255 ? 1.5306  ? 0.7051 ? 0.2782  ? 0.0744  ? -0.1765 ? -0.5703 ? -0.1842 ? 0.2658  ? -0.0741 ? -0.1944 ? 
-0.0940 ? 
11 'X-RAY DIFFRACTION' ? refined 36.7324 -18.9034 28.2415 0.1430 ? -0.0164 ? 0.1582  ? 0.3912 ? -0.0700 ? 0.3172 ? 1.3824 ? 1.8372 
? 0.1965  ? 3.1386 ? 1.6571  ? 2.9085 ? 0.0476  ? -0.1114 ? -0.2079 ? -0.0223 ? 0.2778  ? -0.4756 ? -0.0756 ? 0.7310  ? -0.3254 ? 
12 'X-RAY DIFFRACTION' ? refined 29.9339 -25.0829 29.1245 0.1590 ? 0.0266  ? 0.0714  ? 0.0361 ? -0.0217 ? 0.2216 ? 4.0449 ? 
-0.8805 ? -0.7592 ? 1.8891 ? -0.0686 ? 3.5807 ? -0.0846 ? -0.2636 ? -0.1119 ? 0.1567  ? 0.1429  ? -0.4248 ? 0.1766  ? 0.2528  ? 
-0.0583 ? 
13 'X-RAY DIFFRACTION' ? refined 39.0417 -29.1662 -4.8082 0.0910 ? -0.0034 ? 0.0484  ? 0.0287 ? 0.0081  ? 0.1207 ? 3.6242 ? 
-0.8624 ? 4.5237  ? 1.6766 ? -0.3255 ? 8.6307 ? 0.2785  ? 0.1617  ? 0.0222  ? -0.1879 ? -0.0747 ? 0.0056  ? 0.4260  ? 0.1261  ? 
-0.2038 ? 
14 'X-RAY DIFFRACTION' ? refined 40.6526 -23.8992 -3.2478 0.1066 ? 0.0402  ? 0.0728  ? 0.0919 ? -0.0332 ? 0.1281 ? 3.4991 ? 1.5884 
? 4.4983  ? 1.7377 ? 0.4795  ? 8.2781 ? -0.1813 ? -0.0526 ? 0.0058  ? -0.1162 ? -0.0267 ? -0.1865 ? -0.2282 ? -0.0082 ? 0.2079  ? 
15 'X-RAY DIFFRACTION' ? refined 41.2150 -23.0788 -9.2735 0.2353 ? -0.0140 ? 0.1559  ? 0.0922 ? -0.0210 ? 0.1846 ? 1.9389 ? 0.2997 
? 0.5319  ? 2.2171 ? -1.1877 ? 5.8743 ? -0.1184 ? 0.2152  ? 0.1303  ? -0.2402 ? 0.0712  ? -0.1112 ? -0.2493 ? 0.3332  ? 0.0471  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 2  ? ? A 46  ? ? ? A 72  ? ? ? 
2  'X-RAY DIFFRACTION' 3  ? ? A 73  ? ? ? A 100 ? ? ? 
3  'X-RAY DIFFRACTION' 4  ? ? A 101 ? ? ? A 150 ? ? ? 
4  'X-RAY DIFFRACTION' 5  ? ? A 151 ? ? ? A 246 ? ? ? 
5  'X-RAY DIFFRACTION' 6  ? ? H 1   ? ? ? H 38  ? ? ? 
6  'X-RAY DIFFRACTION' 7  ? ? H 39  ? ? ? H 61  ? ? ? 
7  'X-RAY DIFFRACTION' 8  ? ? H 62  ? ? ? H 89  ? ? ? 
8  'X-RAY DIFFRACTION' 9  ? ? H 90  ? ? ? H 181 ? ? ? 
9  'X-RAY DIFFRACTION' 10 ? ? H 182 ? ? ? H 214 ? ? ? 
10 'X-RAY DIFFRACTION' 11 ? ? L 1   ? ? ? L 26  ? ? ? 
11 'X-RAY DIFFRACTION' 12 ? ? L 27  ? ? ? L 105 ? ? ? 
12 'X-RAY DIFFRACTION' 13 ? ? L 106 ? ? ? L 126 ? ? ? 
13 'X-RAY DIFFRACTION' 14 ? ? L 127 ? ? ? L 147 ? ? ? 
14 'X-RAY DIFFRACTION' 15 ? ? L 148 ? ? ? L 212 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ARG 45  ? A ARG 1   
2  1 Y 1 A PRO 291 ? A PRO 247 
3  1 Y 1 A GLU 292 ? A GLU 248 
4  1 Y 1 A ASP 293 ? A ASP 249 
5  1 Y 1 A SER 294 ? A SER 250 
6  1 Y 1 A SER 295 ? A SER 251 
7  1 Y 1 A CYS 296 ? A CYS 252 
8  1 Y 1 A THR 297 ? A THR 253 
9  1 Y 1 A SER 298 ? A SER 254 
10 1 Y 1 A GLU 299 ? A GLU 255 
11 1 Y 1 A ILE 300 ? A ILE 256 
12 1 Y 1 A HIS 301 ? A HIS 257 
13 1 Y 1 A HIS 302 ? A HIS 258 
14 1 Y 1 A HIS 303 ? A HIS 259 
15 1 Y 1 A HIS 304 ? A HIS 260 
16 1 Y 1 A HIS 305 ? A HIS 261 
17 1 Y 1 A HIS 306 ? A HIS 262 
18 1 Y 1 A HIS 307 ? A HIS 263 
19 1 Y 1 A HIS 308 ? A HIS 264 
20 1 Y 1 H SER 215 ? B SER 225 
21 1 Y 1 H CYS 216 ? B CYS 226 
22 1 Y 1 L GLU 213 ? C GLU 213 
23 1 Y 1 L CYS 214 ? C CYS 214 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
K   K    K  N N 184 
LEU N    N  N N 185 
LEU CA   C  N S 186 
LEU C    C  N N 187 
LEU O    O  N N 188 
LEU CB   C  N N 189 
LEU CG   C  N N 190 
LEU CD1  C  N N 191 
LEU CD2  C  N N 192 
LEU OXT  O  N N 193 
LEU H    H  N N 194 
LEU H2   H  N N 195 
LEU HA   H  N N 196 
LEU HB2  H  N N 197 
LEU HB3  H  N N 198 
LEU HG   H  N N 199 
LEU HD11 H  N N 200 
LEU HD12 H  N N 201 
LEU HD13 H  N N 202 
LEU HD21 H  N N 203 
LEU HD22 H  N N 204 
LEU HD23 H  N N 205 
LEU HXT  H  N N 206 
LYS N    N  N N 207 
LYS CA   C  N S 208 
LYS C    C  N N 209 
LYS O    O  N N 210 
LYS CB   C  N N 211 
LYS CG   C  N N 212 
LYS CD   C  N N 213 
LYS CE   C  N N 214 
LYS NZ   N  N N 215 
LYS OXT  O  N N 216 
LYS H    H  N N 217 
LYS H2   H  N N 218 
LYS HA   H  N N 219 
LYS HB2  H  N N 220 
LYS HB3  H  N N 221 
LYS HG2  H  N N 222 
LYS HG3  H  N N 223 
LYS HD2  H  N N 224 
LYS HD3  H  N N 225 
LYS HE2  H  N N 226 
LYS HE3  H  N N 227 
LYS HZ1  H  N N 228 
LYS HZ2  H  N N 229 
LYS HZ3  H  N N 230 
LYS HXT  H  N N 231 
MET N    N  N N 232 
MET CA   C  N S 233 
MET C    C  N N 234 
MET O    O  N N 235 
MET CB   C  N N 236 
MET CG   C  N N 237 
MET SD   S  N N 238 
MET CE   C  N N 239 
MET OXT  O  N N 240 
MET H    H  N N 241 
MET H2   H  N N 242 
MET HA   H  N N 243 
MET HB2  H  N N 244 
MET HB3  H  N N 245 
MET HG2  H  N N 246 
MET HG3  H  N N 247 
MET HE1  H  N N 248 
MET HE2  H  N N 249 
MET HE3  H  N N 250 
MET HXT  H  N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SER N    N  N N 292 
SER CA   C  N S 293 
SER C    C  N N 294 
SER O    O  N N 295 
SER CB   C  N N 296 
SER OG   O  N N 297 
SER OXT  O  N N 298 
SER H    H  N N 299 
SER H2   H  N N 300 
SER HA   H  N N 301 
SER HB2  H  N N 302 
SER HB3  H  N N 303 
SER HG   H  N N 304 
SER HXT  H  N N 305 
THR N    N  N N 306 
THR CA   C  N S 307 
THR C    C  N N 308 
THR O    O  N N 309 
THR CB   C  N R 310 
THR OG1  O  N N 311 
THR CG2  C  N N 312 
THR OXT  O  N N 313 
THR H    H  N N 314 
THR H2   H  N N 315 
THR HA   H  N N 316 
THR HB   H  N N 317 
THR HG1  H  N N 318 
THR HG21 H  N N 319 
THR HG22 H  N N 320 
THR HG23 H  N N 321 
THR HXT  H  N N 322 
TRP N    N  N N 323 
TRP CA   C  N S 324 
TRP C    C  N N 325 
TRP O    O  N N 326 
TRP CB   C  N N 327 
TRP CG   C  Y N 328 
TRP CD1  C  Y N 329 
TRP CD2  C  Y N 330 
TRP NE1  N  Y N 331 
TRP CE2  C  Y N 332 
TRP CE3  C  Y N 333 
TRP CZ2  C  Y N 334 
TRP CZ3  C  Y N 335 
TRP CH2  C  Y N 336 
TRP OXT  O  N N 337 
TRP H    H  N N 338 
TRP H2   H  N N 339 
TRP HA   H  N N 340 
TRP HB2  H  N N 341 
TRP HB3  H  N N 342 
TRP HD1  H  N N 343 
TRP HE1  H  N N 344 
TRP HE3  H  N N 345 
TRP HZ2  H  N N 346 
TRP HZ3  H  N N 347 
TRP HH2  H  N N 348 
TRP HXT  H  N N 349 
TYR N    N  N N 350 
TYR CA   C  N S 351 
TYR C    C  N N 352 
TYR O    O  N N 353 
TYR CB   C  N N 354 
TYR CG   C  Y N 355 
TYR CD1  C  Y N 356 
TYR CD2  C  Y N 357 
TYR CE1  C  Y N 358 
TYR CE2  C  Y N 359 
TYR CZ   C  Y N 360 
TYR OH   O  N N 361 
TYR OXT  O  N N 362 
TYR H    H  N N 363 
TYR H2   H  N N 364 
TYR HA   H  N N 365 
TYR HB2  H  N N 366 
TYR HB3  H  N N 367 
TYR HD1  H  N N 368 
TYR HD2  H  N N 369 
TYR HE1  H  N N 370 
TYR HE2  H  N N 371 
TYR HH   H  N N 372 
TYR HXT  H  N N 373 
VAL N    N  N N 374 
VAL CA   C  N S 375 
VAL C    C  N N 376 
VAL O    O  N N 377 
VAL CB   C  N N 378 
VAL CG1  C  N N 379 
VAL CG2  C  N N 380 
VAL OXT  O  N N 381 
VAL H    H  N N 382 
VAL H2   H  N N 383 
VAL HA   H  N N 384 
VAL HB   H  N N 385 
VAL HG11 H  N N 386 
VAL HG12 H  N N 387 
VAL HG13 H  N N 388 
VAL HG21 H  N N 389 
VAL HG22 H  N N 390 
VAL HG23 H  N N 391 
VAL HXT  H  N N 392 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 7DUN ? 
2 ? 'experimental model' PDB 7DHA ? 
# 
_atom_sites.entry_id                    9GOY 
_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]   0.007617 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002564 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016375 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008501 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
K  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . TRP A 1 2   ? -29.953 -22.058 48.951  1.00 91.00  ? 46  TRP A N   1 
ATOM   2    C  CA  . TRP A 1 2   ? -29.734 -21.022 49.999  1.00 90.07  ? 46  TRP A CA  1 
ATOM   3    C  C   . TRP A 1 2   ? -28.683 -21.493 51.007  1.00 87.73  ? 46  TRP A C   1 
ATOM   4    O  O   . TRP A 1 2   ? -28.003 -20.672 51.618  1.00 86.36  ? 46  TRP A O   1 
ATOM   5    C  CB  . TRP A 1 2   ? -31.065 -20.652 50.669  1.00 92.23  ? 46  TRP A CB  1 
ATOM   6    C  CG  . TRP A 1 2   ? -31.090 -19.272 51.250  1.00 94.27  ? 46  TRP A CG  1 
ATOM   7    C  CD1 . TRP A 1 2   ? -30.542 -18.867 52.431  1.00 94.81  ? 46  TRP A CD1 1 
ATOM   8    C  CD2 . TRP A 1 2   ? -31.670 -18.095 50.655  1.00 98.02  ? 46  TRP A CD2 1 
ATOM   9    N  NE1 . TRP A 1 2   ? -30.752 -17.527 52.622  1.00 96.88  ? 46  TRP A NE1 1 
ATOM   10   C  CE2 . TRP A 1 2   ? -31.441 -17.025 51.548  1.00 98.77  ? 46  TRP A CE2 1 
ATOM   11   C  CE3 . TRP A 1 2   ? -32.362 -17.841 49.463  1.00 100.07 ? 46  TRP A CE3 1 
ATOM   12   C  CZ2 . TRP A 1 2   ? -31.881 -15.727 51.284  1.00 100.53 ? 46  TRP A CZ2 1 
ATOM   13   C  CZ3 . TRP A 1 2   ? -32.795 -16.558 49.202  1.00 101.62 ? 46  TRP A CZ3 1 
ATOM   14   C  CH2 . TRP A 1 2   ? -32.557 -15.517 50.102  1.00 101.65 ? 46  TRP A CH2 1 
ATOM   15   N  N   . ARG A 1 3   ? -28.562 -22.818 51.177  1.00 87.31  ? 47  ARG A N   1 
ATOM   16   C  CA  . ARG A 1 3   ? -27.480 -23.416 51.943  1.00 86.72  ? 47  ARG A CA  1 
ATOM   17   C  C   . ARG A 1 3   ? -26.176 -23.271 51.157  1.00 86.31  ? 47  ARG A C   1 
ATOM   18   O  O   . ARG A 1 3   ? -26.095 -23.700 50.008  1.00 86.72  ? 47  ARG A O   1 
ATOM   19   C  CB  . ARG A 1 3   ? -27.808 -24.885 52.238  1.00 87.54  ? 47  ARG A CB  1 
ATOM   20   C  CG  . ARG A 1 3   ? -26.730 -25.649 52.997  1.00 87.45  ? 47  ARG A CG  1 
ATOM   21   C  CD  . ARG A 1 3   ? -26.438 -25.073 54.370  1.00 87.11  ? 47  ARG A CD  1 
ATOM   22   N  NE  . ARG A 1 3   ? -27.595 -25.060 55.256  1.00 88.43  ? 47  ARG A NE  1 
ATOM   23   C  CZ  . ARG A 1 3   ? -28.168 -26.139 55.780  1.00 89.49  ? 47  ARG A CZ  1 
ATOM   24   N  NH1 . ARG A 1 3   ? -27.684 -27.343 55.530  1.00 90.99  ? 47  ARG A NH1 1 
ATOM   25   N  NH2 . ARG A 1 3   ? -29.224 -26.008 56.566  1.00 89.03  ? 47  ARG A NH2 1 
ATOM   26   N  N   . GLN A 1 4   ? -25.170 -22.656 51.797  1.00 85.85  ? 48  GLN A N   1 
ATOM   27   C  CA  . GLN A 1 4   ? -23.877 -22.353 51.194  1.00 85.75  ? 48  GLN A CA  1 
ATOM   28   C  C   . GLN A 1 4   ? -24.036 -21.426 49.987  1.00 85.71  ? 48  GLN A C   1 
ATOM   29   O  O   . GLN A 1 4   ? -23.245 -21.490 49.047  1.00 85.24  ? 48  GLN A O   1 
ATOM   30   C  CB  . GLN A 1 4   ? -23.119 -23.632 50.824  1.00 86.39  ? 48  GLN A CB  1 
ATOM   31   C  CG  . GLN A 1 4   ? -22.604 -24.402 52.031  1.00 87.90  ? 48  GLN A CG  1 
ATOM   32   C  CD  . GLN A 1 4   ? -21.577 -25.444 51.657  1.00 89.25  ? 48  GLN A CD  1 
ATOM   33   O  OE1 . GLN A 1 4   ? -21.831 -26.331 50.846  1.00 91.22  ? 48  GLN A OE1 1 
ATOM   34   N  NE2 . GLN A 1 4   ? -20.399 -25.337 52.251  1.00 88.92  ? 48  GLN A NE2 1 
ATOM   35   N  N   . GLN A 1 5   ? -25.051 -20.553 50.027  1.00 86.64  ? 49  GLN A N   1 
ATOM   36   C  CA  . GLN A 1 5   ? -25.152 -19.433 49.106  1.00 86.63  ? 49  GLN A CA  1 
ATOM   37   C  C   . GLN A 1 5   ? -24.351 -18.271 49.690  1.00 86.49  ? 49  GLN A C   1 
ATOM   38   O  O   . GLN A 1 5   ? -24.588 -17.876 50.830  1.00 87.75  ? 49  GLN A O   1 
ATOM   39   C  CB  . GLN A 1 5   ? -26.620 -19.053 48.892  1.00 87.50  ? 49  GLN A CB  1 
ATOM   40   C  CG  . GLN A 1 5   ? -26.821 -17.814 48.028  1.00 88.98  ? 49  GLN A CG  1 
ATOM   41   C  CD  . GLN A 1 5   ? -28.275 -17.446 47.856  1.00 91.34  ? 49  GLN A CD  1 
ATOM   42   O  OE1 . GLN A 1 5   ? -29.180 -18.196 48.217  1.00 91.57  ? 49  GLN A OE1 1 
ATOM   43   N  NE2 . GLN A 1 5   ? -28.514 -16.275 47.289  1.00 93.49  ? 49  GLN A NE2 1 
ATOM   44   N  N   . TRP A 1 6   ? -23.404 -17.739 48.906  1.00 85.42  ? 50  TRP A N   1 
ATOM   45   C  CA  . TRP A 1 6   ? -22.541 -16.658 49.359  1.00 84.66  ? 50  TRP A CA  1 
ATOM   46   C  C   . TRP A 1 6   ? -22.704 -15.439 48.453  1.00 84.26  ? 50  TRP A C   1 
ATOM   47   O  O   . TRP A 1 6   ? -23.277 -15.536 47.370  1.00 84.47  ? 50  TRP A O   1 
ATOM   48   C  CB  . TRP A 1 6   ? -21.082 -17.124 49.424  1.00 84.08  ? 50  TRP A CB  1 
ATOM   49   C  CG  . TRP A 1 6   ? -20.864 -18.369 50.228  1.00 84.22  ? 50  TRP A CG  1 
ATOM   50   C  CD1 . TRP A 1 6   ? -20.279 -19.527 49.804  1.00 84.55  ? 50  TRP A CD1 1 
ATOM   51   C  CD2 . TRP A 1 6   ? -21.223 -18.585 51.605  1.00 84.79  ? 50  TRP A CD2 1 
ATOM   52   N  NE1 . TRP A 1 6   ? -20.247 -20.446 50.818  1.00 84.72  ? 50  TRP A NE1 1 
ATOM   53   C  CE2 . TRP A 1 6   ? -20.820 -19.898 51.935  1.00 85.03  ? 50  TRP A CE2 1 
ATOM   54   C  CE3 . TRP A 1 6   ? -21.843 -17.805 52.589  1.00 85.32  ? 50  TRP A CE3 1 
ATOM   55   C  CZ2 . TRP A 1 6   ? -21.021 -20.442 53.203  1.00 84.85  ? 50  TRP A CZ2 1 
ATOM   56   C  CZ3 . TRP A 1 6   ? -22.039 -18.343 53.843  1.00 85.43  ? 50  TRP A CZ3 1 
ATOM   57   C  CH2 . TRP A 1 6   ? -21.635 -19.645 54.142  1.00 85.49  ? 50  TRP A CH2 1 
ATOM   58   N  N   . SER A 1 7   ? -22.180 -14.297 48.916  1.00 84.10  ? 51  SER A N   1 
ATOM   59   C  CA  . SER A 1 7   ? -22.358 -13.018 48.244  1.00 86.75  ? 51  SER A CA  1 
ATOM   60   C  C   . SER A 1 7   ? -21.172 -12.722 47.328  1.00 87.51  ? 51  SER A C   1 
ATOM   61   O  O   . SER A 1 7   ? -21.362 -12.294 46.192  1.00 89.11  ? 51  SER A O   1 
ATOM   62   C  CB  . SER A 1 7   ? -22.550 -11.906 49.244  1.00 87.88  ? 51  SER A CB  1 
ATOM   63   O  OG  . SER A 1 7   ? -23.554 -12.238 50.190  1.00 87.68  ? 51  SER A OG  1 
ATOM   64   N  N   . GLY A 1 8   ? -19.953 -12.934 47.841  1.00 87.05  ? 52  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 8   ? -18.739 -12.659 47.091  1.00 86.93  ? 52  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 8   ? -18.590 -13.582 45.882  1.00 87.06  ? 52  GLY A C   1 
ATOM   67   O  O   . GLY A 1 8   ? -19.264 -14.608 45.799  1.00 85.95  ? 52  GLY A O   1 
ATOM   68   N  N   . PRO A 1 9   ? -17.710 -13.248 44.906  1.00 87.75  ? 53  PRO A N   1 
ATOM   69   C  CA  . PRO A 1 9   ? -17.521 -14.079 43.716  1.00 86.93  ? 53  PRO A CA  1 
ATOM   70   C  C   . PRO A 1 9   ? -16.903 -15.434 44.051  1.00 84.90  ? 53  PRO A C   1 
ATOM   71   O  O   . PRO A 1 9   ? -16.185 -15.562 45.041  1.00 84.33  ? 53  PRO A O   1 
ATOM   72   C  CB  . PRO A 1 9   ? -16.560 -13.272 42.827  1.00 88.01  ? 53  PRO A CB  1 
ATOM   73   C  CG  . PRO A 1 9   ? -16.577 -11.870 43.406  1.00 89.37  ? 53  PRO A CG  1 
ATOM   74   C  CD  . PRO A 1 9   ? -16.856 -12.051 44.883  1.00 88.79  ? 53  PRO A CD  1 
ATOM   75   N  N   . GLY A 1 10  ? -17.179 -16.431 43.202  1.00 84.01  ? 54  GLY A N   1 
ATOM   76   C  CA  . GLY A 1 10  ? -16.676 -17.780 43.400  1.00 82.81  ? 54  GLY A CA  1 
ATOM   77   C  C   . GLY A 1 10  ? -15.168 -17.871 43.177  1.00 82.42  ? 54  GLY A C   1 
ATOM   78   O  O   . GLY A 1 10  ? -14.527 -16.883 42.819  1.00 82.76  ? 54  GLY A O   1 
ATOM   79   N  N   . THR A 1 11  ? -14.618 -19.071 43.396  1.00 81.37  ? 55  THR A N   1 
ATOM   80   C  CA  . THR A 1 11  ? -13.197 -19.320 43.207  1.00 80.26  ? 55  THR A CA  1 
ATOM   81   C  C   . THR A 1 11  ? -12.816 -18.959 41.774  1.00 80.75  ? 55  THR A C   1 
ATOM   82   O  O   . THR A 1 11  ? -13.596 -19.182 40.850  1.00 81.76  ? 55  THR A O   1 
ATOM   83   C  CB  . THR A 1 11  ? -12.839 -20.776 43.538  1.00 80.07  ? 55  THR A CB  1 
ATOM   84   O  OG1 . THR A 1 11  ? -13.241 -21.048 44.881  1.00 79.31  ? 55  THR A OG1 1 
ATOM   85   C  CG2 . THR A 1 11  ? -11.363 -21.077 43.385  1.00 79.46  ? 55  THR A CG2 1 
ATOM   86   N  N   . THR A 1 12  ? -11.616 -18.388 41.610  1.00 80.57  ? 56  THR A N   1 
ATOM   87   C  CA  . THR A 1 12  ? -11.124 -17.968 40.307  1.00 81.74  ? 56  THR A CA  1 
ATOM   88   C  C   . THR A 1 12  ? -11.021 -19.188 39.391  1.00 82.77  ? 56  THR A C   1 
ATOM   89   O  O   . THR A 1 12  ? -10.638 -20.268 39.835  1.00 82.19  ? 56  THR A O   1 
ATOM   90   C  CB  . THR A 1 12  ? -9.780  -17.238 40.438  1.00 80.81  ? 56  THR A CB  1 
ATOM   91   O  OG1 . THR A 1 12  ? -9.909  -16.211 41.423  1.00 79.09  ? 56  THR A OG1 1 
ATOM   92   C  CG2 . THR A 1 12  ? -9.308  -16.627 39.136  1.00 81.62  ? 56  THR A CG2 1 
ATOM   93   N  N   . LYS A 1 13  ? -11.379 -19.002 38.115  1.00 84.59  ? 57  LYS A N   1 
ATOM   94   C  CA  . LYS A 1 13  ? -11.337 -20.077 37.136  1.00 87.10  ? 57  LYS A CA  1 
ATOM   95   C  C   . LYS A 1 13  ? -9.893  -20.545 36.968  1.00 86.94  ? 57  LYS A C   1 
ATOM   96   O  O   . LYS A 1 13  ? -8.989  -19.722 36.833  1.00 86.92  ? 57  LYS A O   1 
ATOM   97   C  CB  . LYS A 1 13  ? -11.925 -19.610 35.801  1.00 89.74  ? 57  LYS A CB  1 
ATOM   98   C  CG  . LYS A 1 13  ? -13.403 -19.244 35.841  1.00 91.75  ? 57  LYS A CG  1 
ATOM   99   C  CD  . LYS A 1 13  ? -13.916 -18.643 34.551  1.00 94.87  ? 57  LYS A CD  1 
ATOM   100  C  CE  . LYS A 1 13  ? -15.364 -18.208 34.642  1.00 96.47  ? 57  LYS A CE  1 
ATOM   101  N  NZ  . LYS A 1 13  ? -15.819 -17.553 33.393  1.00 99.92  ? 57  LYS A NZ  1 
ATOM   102  N  N   . ARG A 1 14  ? -9.697  -21.871 36.982  1.00 87.75  ? 58  ARG A N   1 
ATOM   103  C  CA  . ARG A 1 14  ? -8.377  -22.482 36.917  1.00 87.92  ? 58  ARG A CA  1 
ATOM   104  C  C   . ARG A 1 14  ? -7.500  -21.921 38.036  1.00 83.57  ? 58  ARG A C   1 
ATOM   105  O  O   . ARG A 1 14  ? -6.422  -21.387 37.782  1.00 82.16  ? 58  ARG A O   1 
ATOM   106  C  CB  . ARG A 1 14  ? -7.759  -22.285 35.527  1.00 91.27  ? 58  ARG A CB  1 
ATOM   107  C  CG  . ARG A 1 14  ? -8.319  -23.214 34.459  1.00 95.79  ? 58  ARG A CG  1 
ATOM   108  C  CD  . ARG A 1 14  ? -8.023  -22.734 33.050  1.00 99.61  ? 58  ARG A CD  1 
ATOM   109  N  NE  . ARG A 1 14  ? -8.929  -21.664 32.642  1.00 102.25 ? 58  ARG A NE  1 
ATOM   110  C  CZ  . ARG A 1 14  ? -8.566  -20.415 32.359  1.00 103.21 ? 58  ARG A CZ  1 
ATOM   111  N  NH1 . ARG A 1 14  ? -7.297  -20.050 32.442  1.00 102.39 ? 58  ARG A NH1 1 
ATOM   112  N  NH2 . ARG A 1 14  ? -9.480  -19.531 31.995  1.00 104.66 ? 58  ARG A NH2 1 
ATOM   113  N  N   . PHE A 1 15  ? -7.981  -22.051 39.277  1.00 81.23  ? 59  PHE A N   1 
ATOM   114  C  CA  . PHE A 1 15  ? -7.247  -21.599 40.449  1.00 79.61  ? 59  PHE A CA  1 
ATOM   115  C  C   . PHE A 1 15  ? -6.042  -22.506 40.705  1.00 79.49  ? 59  PHE A C   1 
ATOM   116  O  O   . PHE A 1 15  ? -4.961  -22.006 41.009  1.00 78.31  ? 59  PHE A O   1 
ATOM   117  C  CB  . PHE A 1 15  ? -8.175  -21.518 41.666  1.00 78.44  ? 59  PHE A CB  1 
ATOM   118  C  CG  . PHE A 1 15  ? -7.491  -21.167 42.964  1.00 76.15  ? 59  PHE A CG  1 
ATOM   119  C  CD1 . PHE A 1 15  ? -6.845  -19.950 43.118  1.00 74.95  ? 59  PHE A CD1 1 
ATOM   120  C  CD2 . PHE A 1 15  ? -7.495  -22.052 44.032  1.00 75.69  ? 59  PHE A CD2 1 
ATOM   121  C  CE1 . PHE A 1 15  ? -6.216  -19.627 44.311  1.00 74.75  ? 59  PHE A CE1 1 
ATOM   122  C  CE2 . PHE A 1 15  ? -6.866  -21.727 45.224  1.00 75.39  ? 59  PHE A CE2 1 
ATOM   123  C  CZ  . PHE A 1 15  ? -6.228  -20.516 45.361  1.00 74.90  ? 59  PHE A CZ  1 
ATOM   124  N  N   . PRO A 1 16  ? -6.175  -23.853 40.615  1.00 80.58  ? 60  PRO A N   1 
ATOM   125  C  CA  . PRO A 1 16  ? -5.035  -24.754 40.809  1.00 81.06  ? 60  PRO A CA  1 
ATOM   126  C  C   . PRO A 1 16  ? -3.900  -24.543 39.808  1.00 81.14  ? 60  PRO A C   1 
ATOM   127  O  O   . PRO A 1 16  ? -2.734  -24.513 40.193  1.00 80.07  ? 60  PRO A O   1 
ATOM   128  C  CB  . PRO A 1 16  ? -5.635  -26.158 40.622  1.00 82.87  ? 60  PRO A CB  1 
ATOM   129  C  CG  . PRO A 1 16  ? -7.112  -25.972 40.890  1.00 82.74  ? 60  PRO A CG  1 
ATOM   130  C  CD  . PRO A 1 16  ? -7.423  -24.590 40.360  1.00 81.50  ? 60  PRO A CD  1 
ATOM   131  N  N   . GLU A 1 17  ? -4.258  -24.400 38.525  1.00 82.15  ? 61  GLU A N   1 
ATOM   132  C  CA  . GLU A 1 17  ? -3.286  -24.214 37.459  1.00 83.24  ? 61  GLU A CA  1 
ATOM   133  C  C   . GLU A 1 17  ? -2.555  -22.885 37.645  1.00 81.08  ? 61  GLU A C   1 
ATOM   134  O  O   . GLU A 1 17  ? -1.361  -22.792 37.366  1.00 81.50  ? 61  GLU A O   1 
ATOM   135  C  CB  . GLU A 1 17  ? -3.956  -24.247 36.082  1.00 85.97  ? 61  GLU A CB  1 
ATOM   136  C  CG  . GLU A 1 17  ? -4.449  -25.622 35.655  1.00 89.34  ? 61  GLU A CG  1 
ATOM   137  C  CD  . GLU A 1 17  ? -5.789  -26.064 36.223  1.00 91.42  ? 61  GLU A CD  1 
ATOM   138  O  OE1 . GLU A 1 17  ? -6.367  -25.320 37.042  1.00 90.77  ? 61  GLU A OE1 1 
ATOM   139  O  OE2 . GLU A 1 17  ? -6.258  -27.153 35.836  1.00 95.19  ? 61  GLU A OE2 1 
ATOM   140  N  N   . THR A 1 18  ? -3.289  -21.864 38.110  1.00 78.40  ? 62  THR A N   1 
ATOM   141  C  CA  . THR A 1 18  ? -2.757  -20.520 38.270  1.00 75.87  ? 62  THR A CA  1 
ATOM   142  C  C   . THR A 1 18  ? -1.713  -20.487 39.385  1.00 74.56  ? 62  THR A C   1 
ATOM   143  O  O   . THR A 1 18  ? -0.653  -19.890 39.219  1.00 75.65  ? 62  THR A O   1 
ATOM   144  C  CB  . THR A 1 18  ? -3.882  -19.515 38.547  1.00 74.81  ? 62  THR A CB  1 
ATOM   145  O  OG1 . THR A 1 18  ? -4.732  -19.492 37.401  1.00 75.67  ? 62  THR A OG1 1 
ATOM   146  C  CG2 . THR A 1 18  ? -3.379  -18.117 38.836  1.00 74.13  ? 62  THR A CG2 1 
ATOM   147  N  N   . VAL A 1 19  ? -2.028  -21.123 40.519  1.00 73.69  ? 63  VAL A N   1 
ATOM   148  C  CA  . VAL A 1 19  ? -1.168  -21.087 41.691  1.00 72.92  ? 63  VAL A CA  1 
ATOM   149  C  C   . VAL A 1 19  ? 0.158   -21.775 41.371  1.00 73.25  ? 63  VAL A C   1 
ATOM   150  O  O   . VAL A 1 19  ? 1.219   -21.271 41.735  1.00 72.87  ? 63  VAL A O   1 
ATOM   151  C  CB  . VAL A 1 19  ? -1.865  -21.721 42.912  1.00 72.76  ? 63  VAL A CB  1 
ATOM   152  C  CG1 . VAL A 1 19  ? -0.917  -21.887 44.092  1.00 72.79  ? 63  VAL A CG1 1 
ATOM   153  C  CG2 . VAL A 1 19  ? -3.100  -20.932 43.326  1.00 72.52  ? 63  VAL A CG2 1 
ATOM   154  N  N   . LEU A 1 20  ? 0.085   -22.926 40.690  1.00 74.20  ? 64  LEU A N   1 
ATOM   155  C  CA  . LEU A 1 20  ? 1.268   -23.684 40.306  1.00 75.22  ? 64  LEU A CA  1 
ATOM   156  C  C   . LEU A 1 20  ? 2.110   -22.881 39.317  1.00 74.10  ? 64  LEU A C   1 
ATOM   157  O  O   . LEU A 1 20  ? 3.321   -22.767 39.488  1.00 73.77  ? 64  LEU A O   1 
ATOM   158  C  CB  . LEU A 1 20  ? 0.831   -25.019 39.691  1.00 77.56  ? 64  LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 20  ? 0.259   -26.048 40.664  1.00 78.75  ? 64  LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 20  ? -0.257  -27.270 39.919  1.00 80.62  ? 64  LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 20  ? 1.302   -26.457 41.695  1.00 79.40  ? 64  LEU A CD2 1 
ATOM   162  N  N   . ALA A 1 21  ? 1.450   -22.335 38.286  1.00 72.61  ? 65  ALA A N   1 
ATOM   163  C  CA  . ALA A 1 21  ? 2.108   -21.558 37.247  1.00 71.38  ? 65  ALA A CA  1 
ATOM   164  C  C   . ALA A 1 21  ? 2.893   -20.398 37.858  1.00 70.61  ? 65  ALA A C   1 
ATOM   165  O  O   . ALA A 1 21  ? 4.011   -20.116 37.429  1.00 71.89  ? 65  ALA A O   1 
ATOM   166  C  CB  . ALA A 1 21  ? 1.084   -21.060 36.256  1.00 71.40  ? 65  ALA A CB  1 
ATOM   167  N  N   . ARG A 1 22  ? 2.291   -19.734 38.854  1.00 69.47  ? 66  ARG A N   1 
ATOM   168  C  CA  . ARG A 1 22  ? 2.917   -18.618 39.547  1.00 68.21  ? 66  ARG A CA  1 
ATOM   169  C  C   . ARG A 1 22  ? 4.096   -19.104 40.387  1.00 67.68  ? 66  ARG A C   1 
ATOM   170  O  O   . ARG A 1 22  ? 5.127   -18.438 40.451  1.00 67.50  ? 66  ARG A O   1 
ATOM   171  C  CB  . ARG A 1 22  ? 1.907   -17.903 40.451  1.00 67.64  ? 66  ARG A CB  1 
ATOM   172  C  CG  . ARG A 1 22  ? 0.854   -17.094 39.709  1.00 67.53  ? 66  ARG A CG  1 
ATOM   173  C  CD  . ARG A 1 22  ? -0.038  -16.344 40.678  1.00 67.25  ? 66  ARG A CD  1 
ATOM   174  N  NE  . ARG A 1 22  ? -1.094  -15.591 40.016  1.00 67.62  ? 66  ARG A NE  1 
ATOM   175  C  CZ  . ARG A 1 22  ? -1.859  -14.683 40.612  1.00 66.89  ? 66  ARG A CZ  1 
ATOM   176  N  NH1 . ARG A 1 22  ? -1.669  -14.385 41.885  1.00 65.22  ? 66  ARG A NH1 1 
ATOM   177  N  NH2 . ARG A 1 22  ? -2.806  -14.065 39.927  1.00 67.57  ? 66  ARG A NH2 1 
ATOM   178  N  N   . CYS A 1 23  ? 3.925   -20.256 41.045  1.00 68.03  ? 67  CYS A N   1 
ATOM   179  C  CA  . CYS A 1 23  ? 4.943   -20.793 41.934  1.00 69.38  ? 67  CYS A CA  1 
ATOM   180  C  C   . CYS A 1 23  ? 6.191   -21.173 41.138  1.00 69.57  ? 67  CYS A C   1 
ATOM   181  O  O   . CYS A 1 23  ? 7.308   -20.937 41.591  1.00 68.50  ? 67  CYS A O   1 
ATOM   182  C  CB  . CYS A 1 23  ? 4.421   -22.000 42.704  1.00 70.76  ? 67  CYS A CB  1 
ATOM   183  S  SG  . CYS A 1 23  ? 5.477   -22.463 44.102  1.00 73.41  ? 67  CYS A SG  1 
ATOM   184  N  N   . VAL A 1 24  ? 5.982   -21.763 39.954  1.00 70.42  ? 68  VAL A N   1 
ATOM   185  C  CA  . VAL A 1 24  ? 7.065   -22.121 39.050  1.00 70.81  ? 68  VAL A CA  1 
ATOM   186  C  C   . VAL A 1 24  ? 7.766   -20.846 38.585  1.00 69.57  ? 68  VAL A C   1 
ATOM   187  O  O   . VAL A 1 24  ? 8.992   -20.762 38.608  1.00 69.96  ? 68  VAL A O   1 
ATOM   188  C  CB  . VAL A 1 24  ? 6.548   -22.939 37.849  1.00 71.90  ? 68  VAL A CB  1 
ATOM   189  C  CG1 . VAL A 1 24  ? 7.623   -23.141 36.790  1.00 72.52  ? 68  VAL A CG1 1 
ATOM   190  C  CG2 . VAL A 1 24  ? 5.966   -24.278 38.280  1.00 73.19  ? 68  VAL A CG2 1 
ATOM   191  N  N   . LYS A 1 25  ? 6.961   -19.860 38.172  1.00 67.73  ? 69  LYS A N   1 
ATOM   192  C  CA  . LYS A 1 25  ? 7.453   -18.614 37.608  1.00 66.56  ? 69  LYS A CA  1 
ATOM   193  C  C   . LYS A 1 25  ? 8.213   -17.809 38.661  1.00 65.19  ? 69  LYS A C   1 
ATOM   194  O  O   . LYS A 1 25  ? 9.189   -17.140 38.336  1.00 64.80  ? 69  LYS A O   1 
ATOM   195  C  CB  . LYS A 1 25  ? 6.273   -17.820 37.037  1.00 66.90  ? 69  LYS A CB  1 
ATOM   196  C  CG  . LYS A 1 25  ? 6.625   -16.503 36.359  1.00 67.26  ? 69  LYS A CG  1 
ATOM   197  C  CD  . LYS A 1 25  ? 5.444   -15.869 35.655  1.00 68.27  ? 69  LYS A CD  1 
ATOM   198  C  CE  . LYS A 1 25  ? 5.744   -14.487 35.116  1.00 69.56  ? 69  LYS A CE  1 
ATOM   199  N  NZ  . LYS A 1 25  ? 4.591   -13.928 34.373  1.00 70.88  ? 69  LYS A NZ  1 
ATOM   200  N  N   . TYR A 1 26  ? 7.758   -17.872 39.919  1.00 65.15  ? 70  TYR A N   1 
ATOM   201  C  CA  . TYR A 1 26  ? 8.350   -17.087 40.991  1.00 64.87  ? 70  TYR A CA  1 
ATOM   202  C  C   . TYR A 1 26  ? 9.725   -17.641 41.363  1.00 65.87  ? 70  TYR A C   1 
ATOM   203  O  O   . TYR A 1 26  ? 10.652  -16.872 41.608  1.00 64.54  ? 70  TYR A O   1 
ATOM   204  C  CB  . TYR A 1 26  ? 7.423   -17.044 42.211  1.00 63.91  ? 70  TYR A CB  1 
ATOM   205  C  CG  . TYR A 1 26  ? 7.931   -16.187 43.344  1.00 63.19  ? 70  TYR A CG  1 
ATOM   206  C  CD1 . TYR A 1 26  ? 8.876   -16.662 44.240  1.00 63.39  ? 70  TYR A CD1 1 
ATOM   207  C  CD2 . TYR A 1 26  ? 7.496   -14.880 43.498  1.00 62.50  ? 70  TYR A CD2 1 
ATOM   208  C  CE1 . TYR A 1 26  ? 9.356   -15.872 45.272  1.00 63.69  ? 70  TYR A CE1 1 
ATOM   209  C  CE2 . TYR A 1 26  ? 7.968   -14.075 44.522  1.00 62.74  ? 70  TYR A CE2 1 
ATOM   210  C  CZ  . TYR A 1 26  ? 8.902   -14.573 45.413  1.00 63.23  ? 70  TYR A CZ  1 
ATOM   211  O  OH  . TYR A 1 26  ? 9.377   -13.786 46.431  1.00 64.10  ? 70  TYR A OH  1 
ATOM   212  N  N   . THR A 1 27  ? 9.837   -18.976 41.420  1.00 67.39  ? 71  THR A N   1 
ATOM   213  C  CA  . THR A 1 27  ? 11.076  -19.640 41.798  1.00 68.87  ? 71  THR A CA  1 
ATOM   214  C  C   . THR A 1 27  ? 12.149  -19.415 40.732  1.00 69.13  ? 71  THR A C   1 
ATOM   215  O  O   . THR A 1 27  ? 13.336  -19.369 41.049  1.00 69.58  ? 71  THR A O   1 
ATOM   216  C  CB  . THR A 1 27  ? 10.847  -21.137 42.051  1.00 69.76  ? 71  THR A CB  1 
ATOM   217  O  OG1 . THR A 1 27  ? 10.183  -21.690 40.914  1.00 69.66  ? 71  THR A OG1 1 
ATOM   218  C  CG2 . THR A 1 27  ? 10.034  -21.406 43.299  1.00 70.61  ? 71  THR A CG2 1 
ATOM   219  N  N   . GLU A 1 28  ? 11.721  -19.279 39.471  1.00 68.46  ? 72  GLU A N   1 
ATOM   220  C  CA  . GLU A 1 28  ? 12.625  -18.968 38.375  1.00 68.26  ? 72  GLU A CA  1 
ATOM   221  C  C   . GLU A 1 28  ? 13.231  -17.580 38.568  1.00 68.55  ? 72  GLU A C   1 
ATOM   222  O  O   . GLU A 1 28  ? 14.422  -17.391 38.324  1.00 71.06  ? 72  GLU A O   1 
ATOM   223  C  CB  . GLU A 1 28  ? 11.892  -19.069 37.037  1.00 67.26  ? 72  GLU A CB  1 
ATOM   224  C  CG  . GLU A 1 28  ? 11.679  -20.503 36.593  1.00 67.69  ? 72  GLU A CG  1 
ATOM   225  C  CD  . GLU A 1 28  ? 10.780  -20.691 35.386  1.00 67.52  ? 72  GLU A CD  1 
ATOM   226  O  OE1 . GLU A 1 28  ? 10.179  -19.698 34.928  1.00 65.22  ? 72  GLU A OE1 1 
ATOM   227  O  OE2 . GLU A 1 28  ? 10.687  -21.838 34.905  1.00 68.96  ? 72  GLU A OE2 1 
ATOM   228  N  N   . ILE A 1 29  ? 12.405  -16.621 39.006  1.00 67.51  ? 73  ILE A N   1 
ATOM   229  C  CA  . ILE A 1 29  ? 12.830  -15.239 39.169  1.00 67.13  ? 73  ILE A CA  1 
ATOM   230  C  C   . ILE A 1 29  ? 13.645  -15.101 40.454  1.00 68.54  ? 73  ILE A C   1 
ATOM   231  O  O   . ILE A 1 29  ? 14.664  -14.414 40.466  1.00 68.66  ? 73  ILE A O   1 
ATOM   232  C  CB  . ILE A 1 29  ? 11.617  -14.284 39.150  1.00 65.90  ? 73  ILE A CB  1 
ATOM   233  C  CG1 . ILE A 1 29  ? 10.842  -14.383 37.833  1.00 65.32  ? 73  ILE A CG1 1 
ATOM   234  C  CG2 . ILE A 1 29  ? 12.052  -12.853 39.436  1.00 66.66  ? 73  ILE A CG2 1 
ATOM   235  C  CD1 . ILE A 1 29  ? 9.521   -13.647 37.832  1.00 65.20  ? 73  ILE A CD1 1 
ATOM   236  N  N   . HIS A 1 30  ? 13.184  -15.750 41.531  1.00 71.21  ? 74  HIS A N   1 
ATOM   237  C  CA  . HIS A 1 30  ? 13.823  -15.644 42.833  1.00 74.06  ? 74  HIS A CA  1 
ATOM   238  C  C   . HIS A 1 30  ? 14.611  -16.919 43.123  1.00 75.67  ? 74  HIS A C   1 
ATOM   239  O  O   . HIS A 1 30  ? 14.027  -17.935 43.497  1.00 74.94  ? 74  HIS A O   1 
ATOM   240  C  CB  . HIS A 1 30  ? 12.784  -15.331 43.915  1.00 75.14  ? 74  HIS A CB  1 
ATOM   241  C  CG  . HIS A 1 30  ? 12.160  -13.985 43.754  1.00 75.95  ? 74  HIS A CG  1 
ATOM   242  N  ND1 . HIS A 1 30  ? 12.477  -12.913 44.559  1.00 77.59  ? 74  HIS A ND1 1 
ATOM   243  C  CD2 . HIS A 1 30  ? 11.267  -13.531 42.863  1.00 75.58  ? 74  HIS A CD2 1 
ATOM   244  C  CE1 . HIS A 1 30  ? 11.780  -11.855 44.168  1.00 78.53  ? 74  HIS A CE1 1 
ATOM   245  N  NE2 . HIS A 1 30  ? 11.038  -12.208 43.139  1.00 76.55  ? 74  HIS A NE2 1 
ATOM   246  N  N   . PRO A 1 31  ? 15.959  -16.899 42.983  1.00 82.12  ? 75  PRO A N   1 
ATOM   247  C  CA  . PRO A 1 31  ? 16.769  -18.112 43.118  1.00 82.69  ? 75  PRO A CA  1 
ATOM   248  C  C   . PRO A 1 31  ? 16.894  -18.670 44.536  1.00 83.78  ? 75  PRO A C   1 
ATOM   249  O  O   . PRO A 1 31  ? 17.305  -19.816 44.709  1.00 83.44  ? 75  PRO A O   1 
ATOM   250  C  CB  . PRO A 1 31  ? 18.150  -17.672 42.605  1.00 83.49  ? 75  PRO A CB  1 
ATOM   251  C  CG  . PRO A 1 31  ? 18.199  -16.189 42.892  1.00 84.08  ? 75  PRO A CG  1 
ATOM   252  C  CD  . PRO A 1 31  ? 16.776  -15.711 42.688  1.00 83.29  ? 75  PRO A CD  1 
ATOM   253  N  N   . GLU A 1 32  ? 16.540  -17.861 45.543  1.00 85.46  ? 76  GLU A N   1 
ATOM   254  C  CA  . GLU A 1 32  ? 16.632  -18.277 46.935  1.00 86.78  ? 76  GLU A CA  1 
ATOM   255  C  C   . GLU A 1 32  ? 15.436  -19.154 47.314  1.00 86.54  ? 76  GLU A C   1 
ATOM   256  O  O   . GLU A 1 32  ? 15.480  -19.830 48.340  1.00 86.70  ? 76  GLU A O   1 
ATOM   257  C  CB  . GLU A 1 32  ? 16.756  -17.064 47.865  1.00 87.82  ? 76  GLU A CB  1 
ATOM   258  C  CG  . GLU A 1 32  ? 15.489  -16.231 48.017  1.00 87.79  ? 76  GLU A CG  1 
ATOM   259  C  CD  . GLU A 1 32  ? 15.169  -15.268 46.885  1.00 87.40  ? 76  GLU A CD  1 
ATOM   260  O  OE1 . GLU A 1 32  ? 15.894  -15.276 45.871  1.00 87.23  ? 76  GLU A OE1 1 
ATOM   261  O  OE2 . GLU A 1 32  ? 14.195  -14.503 47.025  1.00 87.54  ? 76  GLU A OE2 1 
ATOM   262  N  N   . MET A 1 33  ? 14.379  -19.143 46.487  1.00 86.49  ? 77  MET A N   1 
ATOM   263  C  CA  . MET A 1 33  ? 13.156  -19.878 46.774  1.00 86.01  ? 77  MET A CA  1 
ATOM   264  C  C   . MET A 1 33  ? 13.029  -21.104 45.867  1.00 85.27  ? 77  MET A C   1 
ATOM   265  O  O   . MET A 1 33  ? 11.940  -21.660 45.742  1.00 83.61  ? 77  MET A O   1 
ATOM   266  C  CB  . MET A 1 33  ? 11.931  -18.977 46.569  1.00 86.59  ? 77  MET A CB  1 
ATOM   267  C  CG  . MET A 1 33  ? 11.665  -18.020 47.719  1.00 88.63  ? 77  MET A CG  1 
ATOM   268  S  SD  . MET A 1 33  ? 11.266  -18.851 49.282  1.00 90.26  ? 77  MET A SD  1 
ATOM   269  C  CE  . MET A 1 33  ? 12.845  -18.749 50.125  1.00 91.66  ? 77  MET A CE  1 
ATOM   270  N  N   . ARG A 1 34  ? 14.142  -21.544 45.261  1.00 85.89  ? 78  ARG A N   1 
ATOM   271  C  CA  . ARG A 1 34  ? 14.117  -22.651 44.315  1.00 85.28  ? 78  ARG A CA  1 
ATOM   272  C  C   . ARG A 1 34  ? 14.012  -23.990 45.045  1.00 84.61  ? 78  ARG A C   1 
ATOM   273  O  O   . ARG A 1 34  ? 13.700  -25.004 44.424  1.00 84.48  ? 78  ARG A O   1 
ATOM   274  C  CB  . ARG A 1 34  ? 15.363  -22.651 43.423  1.00 86.03  ? 78  ARG A CB  1 
ATOM   275  C  CG  . ARG A 1 34  ? 15.420  -21.511 42.416  1.00 85.31  ? 78  ARG A CG  1 
ATOM   276  C  CD  . ARG A 1 34  ? 16.456  -21.759 41.334  1.00 86.80  ? 78  ARG A CD  1 
ATOM   277  N  NE  . ARG A 1 34  ? 16.960  -20.533 40.727  1.00 87.05  ? 78  ARG A NE  1 
ATOM   278  C  CZ  . ARG A 1 34  ? 16.572  -20.045 39.554  1.00 86.36  ? 78  ARG A CZ  1 
ATOM   279  N  NH1 . ARG A 1 34  ? 15.628  -20.651 38.859  1.00 86.00  ? 78  ARG A NH1 1 
ATOM   280  N  NH2 . ARG A 1 34  ? 17.119  -18.937 39.085  1.00 86.92  ? 78  ARG A NH2 1 
ATOM   281  N  N   . HIS A 1 35  ? 14.284  -23.988 46.357  1.00 84.20  ? 79  HIS A N   1 
ATOM   282  C  CA  . HIS A 1 35  ? 14.179  -25.185 47.179  1.00 84.60  ? 79  HIS A CA  1 
ATOM   283  C  C   . HIS A 1 35  ? 12.719  -25.615 47.329  1.00 83.55  ? 79  HIS A C   1 
ATOM   284  O  O   . HIS A 1 35  ? 12.445  -26.773 47.640  1.00 83.23  ? 79  HIS A O   1 
ATOM   285  C  CB  . HIS A 1 35  ? 14.820  -24.941 48.550  1.00 84.96  ? 79  HIS A CB  1 
ATOM   286  C  CG  . HIS A 1 35  ? 14.068  -23.969 49.397  1.00 83.19  ? 79  HIS A CG  1 
ATOM   287  N  ND1 . HIS A 1 35  ? 12.959  -24.326 50.132  1.00 82.43  ? 79  HIS A ND1 1 
ATOM   288  C  CD2 . HIS A 1 35  ? 14.271  -22.669 49.639  1.00 82.24  ? 79  HIS A CD2 1 
ATOM   289  C  CE1 . HIS A 1 35  ? 12.509  -23.266 50.784  1.00 81.83  ? 79  HIS A CE1 1 
ATOM   290  N  NE2 . HIS A 1 35  ? 13.289  -22.247 50.497  1.00 81.78  ? 79  HIS A NE2 1 
ATOM   291  N  N   . VAL A 1 36  ? 11.792  -24.670 47.122  1.00 83.00  ? 80  VAL A N   1 
ATOM   292  C  CA  . VAL A 1 36  ? 10.368  -24.908 47.294  1.00 82.48  ? 80  VAL A CA  1 
ATOM   293  C  C   . VAL A 1 36  ? 9.856   -25.805 46.167  1.00 82.21  ? 80  VAL A C   1 
ATOM   294  O  O   . VAL A 1 36  ? 10.028  -25.490 44.991  1.00 81.78  ? 80  VAL A O   1 
ATOM   295  C  CB  . VAL A 1 36  ? 9.595   -23.574 47.342  1.00 81.86  ? 80  VAL A CB  1 
ATOM   296  C  CG1 . VAL A 1 36  ? 8.090   -23.782 47.288  1.00 81.40  ? 80  VAL A CG1 1 
ATOM   297  C  CG2 . VAL A 1 36  ? 9.979   -22.744 48.558  1.00 82.28  ? 80  VAL A CG2 1 
ATOM   298  N  N   . ASP A 1 37  ? 9.218   -26.919 46.553  1.00 82.54  ? 81  ASP A N   1 
ATOM   299  C  CA  . ASP A 1 37  ? 8.494   -27.775 45.627  1.00 82.54  ? 81  ASP A CA  1 
ATOM   300  C  C   . ASP A 1 37  ? 7.099   -27.187 45.427  1.00 82.44  ? 81  ASP A C   1 
ATOM   301  O  O   . ASP A 1 37  ? 6.346   -27.042 46.387  1.00 83.48  ? 81  ASP A O   1 
ATOM   302  C  CB  . ASP A 1 37  ? 8.434   -29.215 46.145  1.00 83.35  ? 81  ASP A CB  1 
ATOM   303  C  CG  . ASP A 1 37  ? 7.794   -30.210 45.190  1.00 84.46  ? 81  ASP A CG  1 
ATOM   304  O  OD1 . ASP A 1 37  ? 7.288   -29.779 44.134  1.00 84.64  ? 81  ASP A OD1 1 
ATOM   305  O  OD2 . ASP A 1 37  ? 7.815   -31.415 45.508  1.00 85.91  ? 81  ASP A OD2 1 
ATOM   306  N  N   . CYS A 1 38  ? 6.765   -26.866 44.172  1.00 82.09  ? 82  CYS A N   1 
ATOM   307  C  CA  . CYS A 1 38  ? 5.554   -26.123 43.856  1.00 81.66  ? 82  CYS A CA  1 
ATOM   308  C  C   . CYS A 1 38  ? 4.314   -27.005 43.994  1.00 81.43  ? 82  CYS A C   1 
ATOM   309  O  O   . CYS A 1 38  ? 3.222   -26.490 44.227  1.00 81.29  ? 82  CYS A O   1 
ATOM   310  C  CB  . CYS A 1 38  ? 5.632   -25.532 42.454  1.00 82.60  ? 82  CYS A CB  1 
ATOM   311  S  SG  . CYS A 1 38  ? 6.946   -24.296 42.283  1.00 84.49  ? 82  CYS A SG  1 
ATOM   312  N  N   . GLN A 1 39  ? 4.487   -28.324 43.844  1.00 81.95  ? 83  GLN A N   1 
ATOM   313  C  CA  . GLN A 1 39  ? 3.408   -29.273 44.073  1.00 82.25  ? 83  GLN A CA  1 
ATOM   314  C  C   . GLN A 1 39  ? 3.067   -29.334 45.560  1.00 80.51  ? 83  GLN A C   1 
ATOM   315  O  O   . GLN A 1 39  ? 1.894   -29.398 45.922  1.00 78.75  ? 83  GLN A O   1 
ATOM   316  C  CB  . GLN A 1 39  ? 3.773   -30.663 43.544  1.00 84.40  ? 83  GLN A CB  1 
ATOM   317  C  CG  . GLN A 1 39  ? 3.266   -30.930 42.134  1.00 86.20  ? 83  GLN A CG  1 
ATOM   318  C  CD  . GLN A 1 39  ? 1.757   -30.919 42.072  1.00 87.07  ? 83  GLN A CD  1 
ATOM   319  O  OE1 . GLN A 1 39  ? 1.081   -31.615 42.828  1.00 87.45  ? 83  GLN A OE1 1 
ATOM   320  N  NE2 . GLN A 1 39  ? 1.213   -30.106 41.182  1.00 87.33  ? 83  GLN A NE2 1 
ATOM   321  N  N   . SER A 1 40  ? 4.102   -29.319 46.409  1.00 79.58  ? 84  SER A N   1 
ATOM   322  C  CA  . SER A 1 40  ? 3.925   -29.358 47.852  1.00 79.45  ? 84  SER A CA  1 
ATOM   323  C  C   . SER A 1 40  ? 3.218   -28.094 48.340  1.00 78.64  ? 84  SER A C   1 
ATOM   324  O  O   . SER A 1 40  ? 2.400   -28.160 49.256  1.00 77.77  ? 84  SER A O   1 
ATOM   325  C  CB  . SER A 1 40  ? 5.246   -29.551 48.551  1.00 79.03  ? 84  SER A CB  1 
ATOM   326  O  OG  . SER A 1 40  ? 5.816   -30.806 48.213  1.00 79.70  ? 84  SER A OG  1 
ATOM   327  N  N   . VAL A 1 41  ? 3.547   -26.953 47.722  1.00 78.56  ? 85  VAL A N   1 
ATOM   328  C  CA  . VAL A 1 41  ? 2.936   -25.676 48.057  1.00 78.62  ? 85  VAL A CA  1 
ATOM   329  C  C   . VAL A 1 41  ? 1.438   -25.732 47.765  1.00 78.57  ? 85  VAL A C   1 
ATOM   330  O  O   . VAL A 1 41  ? 0.639   -25.271 48.577  1.00 78.78  ? 85  VAL A O   1 
ATOM   331  C  CB  . VAL A 1 41  ? 3.616   -24.511 47.310  1.00 78.94  ? 85  VAL A CB  1 
ATOM   332  C  CG1 . VAL A 1 41  ? 2.744   -23.263 47.256  1.00 79.30  ? 85  VAL A CG1 1 
ATOM   333  C  CG2 . VAL A 1 41  ? 4.972   -24.186 47.913  1.00 78.97  ? 85  VAL A CG2 1 
ATOM   334  N  N   . TRP A 1 42  ? 1.068   -26.285 46.604  1.00 78.84  ? 86  TRP A N   1 
ATOM   335  C  CA  . TRP A 1 42  ? -0.331  -26.383 46.217  1.00 79.42  ? 86  TRP A CA  1 
ATOM   336  C  C   . TRP A 1 42  ? -1.081  -27.329 47.154  1.00 79.96  ? 86  TRP A C   1 
ATOM   337  O  O   . TRP A 1 42  ? -2.246  -27.090 47.461  1.00 80.69  ? 86  TRP A O   1 
ATOM   338  C  CB  . TRP A 1 42  ? -0.470  -26.821 44.754  1.00 80.60  ? 86  TRP A CB  1 
ATOM   339  C  CG  . TRP A 1 42  ? -1.883  -27.122 44.358  1.00 82.33  ? 86  TRP A CG  1 
ATOM   340  C  CD1 . TRP A 1 42  ? -2.362  -28.289 43.837  1.00 84.12  ? 86  TRP A CD1 1 
ATOM   341  C  CD2 . TRP A 1 42  ? -3.017  -26.246 44.487  1.00 82.61  ? 86  TRP A CD2 1 
ATOM   342  N  NE1 . TRP A 1 42  ? -3.710  -28.195 43.618  1.00 84.91  ? 86  TRP A NE1 1 
ATOM   343  C  CE2 . TRP A 1 42  ? -4.141  -26.954 44.007  1.00 83.98  ? 86  TRP A CE2 1 
ATOM   344  C  CE3 . TRP A 1 42  ? -3.194  -24.937 44.951  1.00 81.50  ? 86  TRP A CE3 1 
ATOM   345  C  CZ2 . TRP A 1 42  ? -5.417  -26.393 43.980  1.00 83.82  ? 86  TRP A CZ2 1 
ATOM   346  C  CZ3 . TRP A 1 42  ? -4.456  -24.384 44.923  1.00 81.80  ? 86  TRP A CZ3 1 
ATOM   347  C  CH2 . TRP A 1 42  ? -5.551  -25.104 44.443  1.00 82.89  ? 86  TRP A CH2 1 
ATOM   348  N  N   . ASP A 1 43  ? -0.407  -28.399 47.596  1.00 80.87  ? 87  ASP A N   1 
ATOM   349  C  CA  . ASP A 1 43  ? -0.998  -29.368 48.507  1.00 81.76  ? 87  ASP A CA  1 
ATOM   350  C  C   . ASP A 1 43  ? -1.313  -28.700 49.845  1.00 80.22  ? 87  ASP A C   1 
ATOM   351  O  O   . ASP A 1 43  ? -2.398  -28.889 50.390  1.00 80.29  ? 87  ASP A O   1 
ATOM   352  C  CB  . ASP A 1 43  ? -0.084  -30.583 48.699  1.00 84.09  ? 87  ASP A CB  1 
ATOM   353  C  CG  . ASP A 1 43  ? 0.093   -31.451 47.462  1.00 85.38  ? 87  ASP A CG  1 
ATOM   354  O  OD1 . ASP A 1 43  ? -0.498  -31.117 46.413  1.00 86.11  ? 87  ASP A OD1 1 
ATOM   355  O  OD2 . ASP A 1 43  ? 0.823   -32.458 47.556  1.00 85.51  ? 87  ASP A OD2 1 
ATOM   356  N  N   . ALA A 1 44  ? -0.356  -27.917 50.361  1.00 78.81  ? 88  ALA A N   1 
ATOM   357  C  CA  . ALA A 1 44  ? -0.511  -27.221 51.630  1.00 78.62  ? 88  ALA A CA  1 
ATOM   358  C  C   . ALA A 1 44  ? -1.537  -26.096 51.509  1.00 79.04  ? 88  ALA A C   1 
ATOM   359  O  O   . ALA A 1 44  ? -2.180  -25.736 52.495  1.00 79.40  ? 88  ALA A O   1 
ATOM   360  C  CB  . ALA A 1 44  ? 0.826   -26.690 52.086  1.00 78.03  ? 88  ALA A CB  1 
ATOM   361  N  N   . PHE A 1 45  ? -1.668  -25.535 50.299  1.00 79.63  ? 89  PHE A N   1 
ATOM   362  C  CA  . PHE A 1 45  ? -2.625  -24.474 50.025  1.00 79.70  ? 89  PHE A CA  1 
ATOM   363  C  C   . PHE A 1 45  ? -4.032  -25.066 49.978  1.00 80.65  ? 89  PHE A C   1 
ATOM   364  O  O   . PHE A 1 45  ? -4.933  -24.584 50.660  1.00 80.05  ? 89  PHE A O   1 
ATOM   365  C  CB  . PHE A 1 45  ? -2.270  -23.766 48.712  1.00 79.77  ? 89  PHE A CB  1 
ATOM   366  C  CG  . PHE A 1 45  ? -2.744  -22.338 48.595  1.00 79.90  ? 89  PHE A CG  1 
ATOM   367  C  CD1 . PHE A 1 45  ? -4.084  -22.012 48.736  1.00 80.31  ? 89  PHE A CD1 1 
ATOM   368  C  CD2 . PHE A 1 45  ? -1.844  -21.316 48.327  1.00 79.66  ? 89  PHE A CD2 1 
ATOM   369  C  CE1 . PHE A 1 45  ? -4.511  -20.698 48.623  1.00 80.62  ? 89  PHE A CE1 1 
ATOM   370  C  CE2 . PHE A 1 45  ? -2.273  -20.003 48.213  1.00 79.77  ? 89  PHE A CE2 1 
ATOM   371  C  CZ  . PHE A 1 45  ? -3.605  -19.696 48.360  1.00 80.56  ? 89  PHE A CZ  1 
ATOM   372  N  N   . LYS A 1 46  ? -4.201  -26.117 49.166  1.00 82.45  ? 90  LYS A N   1 
ATOM   373  C  CA  . LYS A 1 46  ? -5.492  -26.759 48.977  1.00 84.23  ? 90  LYS A CA  1 
ATOM   374  C  C   . LYS A 1 46  ? -6.002  -27.308 50.308  1.00 84.84  ? 90  LYS A C   1 
ATOM   375  O  O   . LYS A 1 46  ? -7.152  -27.075 50.670  1.00 85.15  ? 90  LYS A O   1 
ATOM   376  C  CB  . LYS A 1 46  ? -5.393  -27.874 47.929  1.00 86.10  ? 90  LYS A CB  1 
ATOM   377  C  CG  . LYS A 1 46  ? -6.711  -28.567 47.606  1.00 88.89  ? 90  LYS A CG  1 
ATOM   378  C  CD  . LYS A 1 46  ? -6.664  -29.452 46.380  1.00 91.07  ? 90  LYS A CD  1 
ATOM   379  C  CE  . LYS A 1 46  ? -8.019  -30.035 46.032  1.00 93.35  ? 90  LYS A CE  1 
ATOM   380  N  NZ  . LYS A 1 46  ? -7.983  -30.789 44.756  1.00 95.88  ? 90  LYS A NZ  1 
ATOM   381  N  N   . GLY A 1 47  ? -5.129  -28.015 51.037  1.00 85.06  ? 91  GLY A N   1 
ATOM   382  C  CA  . GLY A 1 47  ? -5.496  -28.670 52.284  1.00 85.41  ? 91  GLY A CA  1 
ATOM   383  C  C   . GLY A 1 47  ? -5.976  -27.698 53.362  1.00 85.59  ? 91  GLY A C   1 
ATOM   384  O  O   . GLY A 1 47  ? -6.621  -28.115 54.321  1.00 86.73  ? 91  GLY A O   1 
ATOM   385  N  N   . ALA A 1 48  ? -5.653  -26.407 53.200  1.00 85.61  ? 92  ALA A N   1 
ATOM   386  C  CA  . ALA A 1 48  ? -5.995  -25.385 54.178  1.00 85.67  ? 92  ALA A CA  1 
ATOM   387  C  C   . ALA A 1 48  ? -7.504  -25.142 54.219  1.00 86.35  ? 92  ALA A C   1 
ATOM   388  O  O   . ALA A 1 48  ? -8.088  -25.104 55.299  1.00 86.14  ? 92  ALA A O   1 
ATOM   389  C  CB  . ALA A 1 48  ? -5.251  -24.110 53.862  1.00 84.90  ? 92  ALA A CB  1 
ATOM   390  N  N   . PHE A 1 49  ? -8.123  -24.971 53.043  1.00 86.98  ? 93  PHE A N   1 
ATOM   391  C  CA  . PHE A 1 49  ? -9.503  -24.508 52.960  1.00 87.22  ? 93  PHE A CA  1 
ATOM   392  C  C   . PHE A 1 49  ? -10.447 -25.600 52.454  1.00 88.24  ? 93  PHE A C   1 
ATOM   393  O  O   . PHE A 1 49  ? -11.663 -25.425 52.523  1.00 90.26  ? 93  PHE A O   1 
ATOM   394  C  CB  . PHE A 1 49  ? -9.607  -23.265 52.069  1.00 86.49  ? 93  PHE A CB  1 
ATOM   395  C  CG  . PHE A 1 49  ? -9.267  -23.478 50.614  1.00 85.64  ? 93  PHE A CG  1 
ATOM   396  C  CD1 . PHE A 1 49  ? -7.949  -23.497 50.184  1.00 84.89  ? 93  PHE A CD1 1 
ATOM   397  C  CD2 . PHE A 1 49  ? -10.269 -23.664 49.674  1.00 86.17  ? 93  PHE A CD2 1 
ATOM   398  C  CE1 . PHE A 1 49  ? -7.642  -23.692 48.846  1.00 85.20  ? 93  PHE A CE1 1 
ATOM   399  C  CE2 . PHE A 1 49  ? -9.961  -23.863 48.336  1.00 86.47  ? 93  PHE A CE2 1 
ATOM   400  C  CZ  . PHE A 1 49  ? -8.648  -23.876 47.924  1.00 85.91  ? 93  PHE A CZ  1 
ATOM   401  N  N   . ILE A 1 50  ? -9.900  -26.715 51.950  1.00 87.78  ? 94  ILE A N   1 
ATOM   402  C  CA  . ILE A 1 50  ? -10.712 -27.757 51.338  1.00 88.45  ? 94  ILE A CA  1 
ATOM   403  C  C   . ILE A 1 50  ? -11.299 -28.646 52.435  1.00 88.41  ? 94  ILE A C   1 
ATOM   404  O  O   . ILE A 1 50  ? -10.656 -28.880 53.458  1.00 87.27  ? 94  ILE A O   1 
ATOM   405  C  CB  . ILE A 1 50  ? -9.893  -28.562 50.304  1.00 89.01  ? 94  ILE A CB  1 
ATOM   406  C  CG1 . ILE A 1 50  ? -10.790 -29.290 49.299  1.00 90.72  ? 94  ILE A CG1 1 
ATOM   407  C  CG2 . ILE A 1 50  ? -8.918  -29.517 50.982  1.00 89.25  ? 94  ILE A CG2 1 
ATOM   408  C  CD1 . ILE A 1 50  ? -11.520 -28.373 48.344  1.00 91.22  ? 94  ILE A CD1 1 
ATOM   409  N  N   . SER A 1 51  ? -12.532 -29.123 52.201  1.00 88.45  ? 95  SER A N   1 
ATOM   410  C  CA  . SER A 1 51  ? -13.257 -29.997 53.115  1.00 88.43  ? 95  SER A CA  1 
ATOM   411  C  C   . SER A 1 51  ? -13.461 -29.334 54.478  1.00 86.37  ? 95  SER A C   1 
ATOM   412  O  O   . SER A 1 51  ? -13.580 -30.023 55.490  1.00 86.66  ? 95  SER A O   1 
ATOM   413  C  CB  . SER A 1 51  ? -12.573 -31.340 53.250  1.00 89.22  ? 95  SER A CB  1 
ATOM   414  O  OG  . SER A 1 51  ? -12.508 -32.006 51.998  1.00 90.19  ? 95  SER A OG  1 
ATOM   415  N  N   . LYS A 1 52  ? -13.525 -27.996 54.489  1.00 83.57  ? 96  LYS A N   1 
ATOM   416  C  CA  . LYS A 1 52  ? -13.701 -27.221 55.708  1.00 81.76  ? 96  LYS A CA  1 
ATOM   417  C  C   . LYS A 1 52  ? -14.677 -26.087 55.421  1.00 81.02  ? 96  LYS A C   1 
ATOM   418  O  O   . LYS A 1 52  ? -14.718 -25.578 54.301  1.00 80.27  ? 96  LYS A O   1 
ATOM   419  C  CB  . LYS A 1 52  ? -12.357 -26.677 56.201  1.00 80.41  ? 96  LYS A CB  1 
ATOM   420  C  CG  . LYS A 1 52  ? -11.382 -27.732 56.703  1.00 81.18  ? 96  LYS A CG  1 
ATOM   421  C  CD  . LYS A 1 52  ? -9.984  -27.210 56.926  1.00 80.59  ? 96  LYS A CD  1 
ATOM   422  C  CE  . LYS A 1 52  ? -8.994  -28.307 57.253  1.00 81.49  ? 96  LYS A CE  1 
ATOM   423  N  NZ  . LYS A 1 52  ? -7.601  -27.803 57.252  1.00 81.24  ? 96  LYS A NZ  1 
ATOM   424  N  N   . HIS A 1 53  ? -15.454 -25.698 56.440  1.00 80.62  ? 97  HIS A N   1 
ATOM   425  C  CA  . HIS A 1 53  ? -16.535 -24.747 56.247  1.00 80.61  ? 97  HIS A CA  1 
ATOM   426  C  C   . HIS A 1 53  ? -15.953 -23.370 55.933  1.00 80.14  ? 97  HIS A C   1 
ATOM   427  O  O   . HIS A 1 53  ? -15.034 -22.919 56.615  1.00 79.40  ? 97  HIS A O   1 
ATOM   428  C  CB  . HIS A 1 53  ? -17.475 -24.698 57.458  1.00 80.73  ? 97  HIS A CB  1 
ATOM   429  C  CG  . HIS A 1 53  ? -18.770 -24.032 57.130  1.00 80.57  ? 97  HIS A CG  1 
ATOM   430  N  ND1 . HIS A 1 53  ? -19.050 -22.725 57.463  1.00 80.01  ? 97  HIS A ND1 1 
ATOM   431  C  CD2 . HIS A 1 53  ? -19.829 -24.473 56.440  1.00 81.32  ? 97  HIS A CD2 1 
ATOM   432  C  CE1 . HIS A 1 53  ? -20.255 -22.409 57.010  1.00 80.85  ? 97  HIS A CE1 1 
ATOM   433  N  NE2 . HIS A 1 53  ? -20.748 -23.457 56.388  1.00 81.46  ? 97  HIS A NE2 1 
ATOM   434  N  N   . PRO A 1 54  ? -16.481 -22.653 54.911  1.00 80.71  ? 98  PRO A N   1 
ATOM   435  C  CA  . PRO A 1 54  ? -15.896 -21.384 54.469  1.00 80.69  ? 98  PRO A CA  1 
ATOM   436  C  C   . PRO A 1 54  ? -15.923 -20.237 55.480  1.00 80.83  ? 98  PRO A C   1 
ATOM   437  O  O   . PRO A 1 54  ? -15.299 -19.207 55.247  1.00 81.14  ? 98  PRO A O   1 
ATOM   438  C  CB  . PRO A 1 54  ? -16.770 -20.963 53.275  1.00 82.42  ? 98  PRO A CB  1 
ATOM   439  C  CG  . PRO A 1 54  ? -17.478 -22.226 52.842  1.00 82.83  ? 98  PRO A CG  1 
ATOM   440  C  CD  . PRO A 1 54  ? -17.660 -23.026 54.113  1.00 81.91  ? 98  PRO A CD  1 
ATOM   441  N  N   . CYS A 1 55  ? -16.661 -20.410 56.584  1.00 81.03  ? 99  CYS A N   1 
ATOM   442  C  CA  . CYS A 1 55  ? -16.866 -19.345 57.553  1.00 80.90  ? 99  CYS A CA  1 
ATOM   443  C  C   . CYS A 1 55  ? -16.166 -19.657 58.873  1.00 79.49  ? 99  CYS A C   1 
ATOM   444  O  O   . CYS A 1 55  ? -16.342 -18.927 59.847  1.00 78.71  ? 99  CYS A O   1 
ATOM   445  C  CB  . CYS A 1 55  ? -18.353 -19.148 57.811  1.00 82.57  ? 99  CYS A CB  1 
ATOM   446  S  SG  . CYS A 1 55  ? -19.317 -18.985 56.286  1.00 84.49  ? 99  CYS A SG  1 
ATOM   447  N  N   . ASP A 1 56  ? -15.370 -20.733 58.898  1.00 78.99  ? 100 ASP A N   1 
ATOM   448  C  CA  . ASP A 1 56  ? -14.763 -21.196 60.134  1.00 80.15  ? 100 ASP A CA  1 
ATOM   449  C  C   . ASP A 1 56  ? -13.333 -21.655 59.855  1.00 79.70  ? 100 ASP A C   1 
ATOM   450  O  O   . ASP A 1 56  ? -12.945 -22.759 60.232  1.00 79.80  ? 100 ASP A O   1 
ATOM   451  C  CB  . ASP A 1 56  ? -15.624 -22.294 60.764  1.00 81.27  ? 100 ASP A CB  1 
ATOM   452  C  CG  . ASP A 1 56  ? -15.407 -22.495 62.255  1.00 82.13  ? 100 ASP A CG  1 
ATOM   453  O  OD1 . ASP A 1 56  ? -14.671 -21.690 62.865  1.00 82.24  ? 100 ASP A OD1 1 
ATOM   454  O  OD2 . ASP A 1 56  ? -15.978 -23.461 62.794  1.00 83.15  ? 100 ASP A OD2 1 
ATOM   455  N  N   . ILE A 1 57  ? -12.558 -20.781 59.198  1.00 79.30  ? 101 ILE A N   1 
ATOM   456  C  CA  . ILE A 1 57  ? -11.163 -21.047 58.883  1.00 78.22  ? 101 ILE A CA  1 
ATOM   457  C  C   . ILE A 1 57  ? -10.300 -20.462 59.998  1.00 78.57  ? 101 ILE A C   1 
ATOM   458  O  O   . ILE A 1 57  ? -10.643 -19.430 60.569  1.00 79.05  ? 101 ILE A O   1 
ATOM   459  C  CB  . ILE A 1 57  ? -10.791 -20.461 57.504  1.00 77.84  ? 101 ILE A CB  1 
ATOM   460  C  CG1 . ILE A 1 57  ? -11.778 -20.883 56.410  1.00 77.79  ? 101 ILE A CG1 1 
ATOM   461  C  CG2 . ILE A 1 57  ? -9.358  -20.811 57.133  1.00 77.30  ? 101 ILE A CG2 1 
ATOM   462  C  CD1 . ILE A 1 57  ? -11.879 -22.377 56.206  1.00 77.96  ? 101 ILE A CD1 1 
ATOM   463  N  N   . THR A 1 58  ? -9.182  -21.135 60.294  1.00 79.42  ? 102 THR A N   1 
ATOM   464  C  CA  . THR A 1 58  ? -8.257  -20.705 61.331  1.00 81.25  ? 102 THR A CA  1 
ATOM   465  C  C   . THR A 1 58  ? -6.898  -20.400 60.702  1.00 82.28  ? 102 THR A C   1 
ATOM   466  O  O   . THR A 1 58  ? -6.703  -20.602 59.505  1.00 81.41  ? 102 THR A O   1 
ATOM   467  C  CB  . THR A 1 58  ? -8.144  -21.762 62.438  1.00 81.86  ? 102 THR A CB  1 
ATOM   468  O  OG1 . THR A 1 58  ? -7.608  -22.959 61.872  1.00 81.68  ? 102 THR A OG1 1 
ATOM   469  C  CG2 . THR A 1 58  ? -9.471  -22.066 63.099  1.00 82.20  ? 102 THR A CG2 1 
ATOM   470  N  N   . GLU A 1 59  ? -5.968  -19.909 61.530  1.00 85.19  ? 103 GLU A N   1 
ATOM   471  C  CA  . GLU A 1 59  ? -4.610  -19.620 61.098  1.00 86.27  ? 103 GLU A CA  1 
ATOM   472  C  C   . GLU A 1 59  ? -3.802  -20.916 61.017  1.00 87.76  ? 103 GLU A C   1 
ATOM   473  O  O   . GLU A 1 59  ? -2.808  -20.977 60.295  1.00 88.36  ? 103 GLU A O   1 
ATOM   474  C  CB  . GLU A 1 59  ? -3.932  -18.633 62.052  1.00 87.64  ? 103 GLU A CB  1 
ATOM   475  C  CG  . GLU A 1 59  ? -4.578  -17.255 62.092  1.00 88.30  ? 103 GLU A CG  1 
ATOM   476  C  CD  . GLU A 1 59  ? -5.798  -17.111 62.989  1.00 89.34  ? 103 GLU A CD  1 
ATOM   477  O  OE1 . GLU A 1 59  ? -6.283  -18.137 63.508  1.00 88.93  ? 103 GLU A OE1 1 
ATOM   478  O  OE2 . GLU A 1 59  ? -6.253  -15.964 63.180  1.00 89.97  ? 103 GLU A OE2 1 
ATOM   479  N  N   . GLU A 1 60  ? -4.235  -21.942 61.765  1.00 89.29  ? 104 GLU A N   1 
ATOM   480  C  CA  . GLU A 1 60  ? -3.559  -23.231 61.794  1.00 90.73  ? 104 GLU A CA  1 
ATOM   481  C  C   . GLU A 1 60  ? -3.843  -24.022 60.518  1.00 88.46  ? 104 GLU A C   1 
ATOM   482  O  O   . GLU A 1 60  ? -3.133  -24.981 60.223  1.00 88.83  ? 104 GLU A O   1 
ATOM   483  C  CB  . GLU A 1 60  ? -3.983  -24.038 63.023  1.00 94.50  ? 104 GLU A CB  1 
ATOM   484  C  CG  . GLU A 1 60  ? -3.481  -23.453 64.332  1.00 98.97  ? 104 GLU A CG  1 
ATOM   485  C  CD  . GLU A 1 60  ? -3.741  -24.305 65.564  1.00 102.95 ? 104 GLU A CD  1 
ATOM   486  O  OE1 . GLU A 1 60  ? -3.372  -23.863 66.672  1.00 105.44 ? 104 GLU A OE1 1 
ATOM   487  O  OE2 . GLU A 1 60  ? -4.307  -25.408 65.418  1.00 105.46 ? 104 GLU A OE2 1 
ATOM   488  N  N   . ASP A 1 61  ? -4.886  -23.630 59.776  1.00 86.57  ? 105 ASP A N   1 
ATOM   489  C  CA  . ASP A 1 61  ? -5.176  -24.231 58.483  1.00 85.78  ? 105 ASP A CA  1 
ATOM   490  C  C   . ASP A 1 61  ? -4.088  -23.857 57.479  1.00 85.34  ? 105 ASP A C   1 
ATOM   491  O  O   . ASP A 1 61  ? -3.745  -24.664 56.617  1.00 86.12  ? 105 ASP A O   1 
ATOM   492  C  CB  . ASP A 1 61  ? -6.554  -23.807 57.968  1.00 85.38  ? 105 ASP A CB  1 
ATOM   493  C  CG  . ASP A 1 61  ? -7.710  -24.348 58.791  1.00 86.08  ? 105 ASP A CG  1 
ATOM   494  O  OD1 . ASP A 1 61  ? -7.779  -25.580 58.966  1.00 86.08  ? 105 ASP A OD1 1 
ATOM   495  O  OD2 . ASP A 1 61  ? -8.538  -23.533 59.243  1.00 87.03  ? 105 ASP A OD2 1 
ATOM   496  N  N   . TYR A 1 62  ? -3.557  -22.632 57.600  1.00 85.78  ? 106 TYR A N   1 
ATOM   497  C  CA  . TYR A 1 62  ? -2.543  -22.119 56.690  1.00 85.44  ? 106 TYR A CA  1 
ATOM   498  C  C   . TYR A 1 62  ? -1.139  -22.291 57.270  1.00 86.23  ? 106 TYR A C   1 
ATOM   499  O  O   . TYR A 1 62  ? -0.159  -21.959 56.607  1.00 86.02  ? 106 TYR A O   1 
ATOM   500  C  CB  . TYR A 1 62  ? -2.821  -20.647 56.369  1.00 84.49  ? 106 TYR A CB  1 
ATOM   501  C  CG  . TYR A 1 62  ? -4.019  -20.422 55.481  1.00 83.34  ? 106 TYR A CG  1 
ATOM   502  C  CD1 . TYR A 1 62  ? -4.063  -20.952 54.202  1.00 82.66  ? 106 TYR A CD1 1 
ATOM   503  C  CD2 . TYR A 1 62  ? -5.110  -19.685 55.916  1.00 83.17  ? 106 TYR A CD2 1 
ATOM   504  C  CE1 . TYR A 1 62  ? -5.157  -20.757 53.375  1.00 82.33  ? 106 TYR A CE1 1 
ATOM   505  C  CE2 . TYR A 1 62  ? -6.212  -19.478 55.101  1.00 82.64  ? 106 TYR A CE2 1 
ATOM   506  C  CZ  . TYR A 1 62  ? -6.235  -20.018 53.827  1.00 82.15  ? 106 TYR A CZ  1 
ATOM   507  O  OH  . TYR A 1 62  ? -7.317  -19.826 53.007  1.00 81.96  ? 106 TYR A OH  1 
ATOM   508  N  N   . GLN A 1 63  ? -1.049  -22.820 58.498  1.00 87.14  ? 107 GLN A N   1 
ATOM   509  C  CA  . GLN A 1 63  ? 0.222   -23.044 59.171  1.00 87.97  ? 107 GLN A CA  1 
ATOM   510  C  C   . GLN A 1 63  ? 1.160   -23.885 58.302  1.00 86.59  ? 107 GLN A C   1 
ATOM   511  O  O   . GLN A 1 63  ? 2.328   -23.533 58.163  1.00 85.99  ? 107 GLN A O   1 
ATOM   512  C  CB  . GLN A 1 63  ? -0.018  -23.693 60.538  1.00 90.37  ? 107 GLN A CB  1 
ATOM   513  C  CG  . GLN A 1 63  ? 1.249   -24.115 61.275  1.00 92.63  ? 107 GLN A CG  1 
ATOM   514  C  CD  . GLN A 1 63  ? 2.136   -22.959 61.673  1.00 94.13  ? 107 GLN A CD  1 
ATOM   515  O  OE1 . GLN A 1 63  ? 1.868   -21.799 61.364  1.00 93.89  ? 107 GLN A OE1 1 
ATOM   516  N  NE2 . GLN A 1 63  ? 3.212   -23.272 62.377  1.00 95.98  ? 107 GLN A NE2 1 
ATOM   517  N  N   . PRO A 1 64  ? 0.714   -25.019 57.707  1.00 85.50  ? 108 PRO A N   1 
ATOM   518  C  CA  . PRO A 1 64  ? 1.596   -25.834 56.867  1.00 85.14  ? 108 PRO A CA  1 
ATOM   519  C  C   . PRO A 1 64  ? 2.107   -25.116 55.617  1.00 83.23  ? 108 PRO A C   1 
ATOM   520  O  O   . PRO A 1 64  ? 3.219   -25.385 55.167  1.00 83.75  ? 108 PRO A O   1 
ATOM   521  C  CB  . PRO A 1 64  ? 0.729   -27.043 56.478  1.00 85.87  ? 108 PRO A CB  1 
ATOM   522  C  CG  . PRO A 1 64  ? -0.693  -26.557 56.649  1.00 85.14  ? 108 PRO A CG  1 
ATOM   523  C  CD  . PRO A 1 64  ? -0.632  -25.603 57.823  1.00 85.75  ? 108 PRO A CD  1 
ATOM   524  N  N   . LEU A 1 65  ? 1.288   -24.208 55.067  1.00 80.88  ? 109 LEU A N   1 
ATOM   525  C  CA  . LEU A 1 65  ? 1.669   -23.415 53.908  1.00 79.11  ? 109 LEU A CA  1 
ATOM   526  C  C   . LEU A 1 65  ? 2.685   -22.346 54.311  1.00 79.53  ? 109 LEU A C   1 
ATOM   527  O  O   . LEU A 1 65  ? 3.550   -21.989 53.513  1.00 79.14  ? 109 LEU A O   1 
ATOM   528  C  CB  . LEU A 1 65  ? 0.412   -22.785 53.296  1.00 77.85  ? 109 LEU A CB  1 
ATOM   529  C  CG  . LEU A 1 65  ? 0.636   -21.903 52.066  1.00 76.82  ? 109 LEU A CG  1 
ATOM   530  C  CD1 . LEU A 1 65  ? 1.061   -22.735 50.866  1.00 76.46  ? 109 LEU A CD1 1 
ATOM   531  C  CD2 . LEU A 1 65  ? -0.615  -21.102 51.740  1.00 76.58  ? 109 LEU A CD2 1 
ATOM   532  N  N   . MET A 1 66  ? 2.572   -21.836 55.545  1.00 80.98  ? 110 MET A N   1 
ATOM   533  C  CA  . MET A 1 66  ? 3.478   -20.815 56.053  1.00 81.81  ? 110 MET A CA  1 
ATOM   534  C  C   . MET A 1 66  ? 4.896   -21.378 56.150  1.00 81.47  ? 110 MET A C   1 
ATOM   535  O  O   . MET A 1 66  ? 5.863   -20.638 55.985  1.00 81.48  ? 110 MET A O   1 
ATOM   536  C  CB  . MET A 1 66  ? 3.057   -20.327 57.445  1.00 83.90  ? 110 MET A CB  1 
ATOM   537  C  CG  . MET A 1 66  ? 1.809   -19.455 57.470  1.00 83.82  ? 110 MET A CG  1 
ATOM   538  S  SD  . MET A 1 66  ? 1.845   -18.056 56.321  1.00 84.49  ? 110 MET A SD  1 
ATOM   539  C  CE  . MET A 1 66  ? 0.704   -18.642 55.069  1.00 83.59  ? 110 MET A CE  1 
ATOM   540  N  N   . LYS A 1 67  ? 5.002   -22.681 56.444  1.00 81.61  ? 111 LYS A N   1 
ATOM   541  C  CA  . LYS A 1 67  ? 6.284   -23.354 56.588  1.00 82.89  ? 111 LYS A CA  1 
ATOM   542  C  C   . LYS A 1 67  ? 6.934   -23.553 55.220  1.00 81.83  ? 111 LYS A C   1 
ATOM   543  O  O   . LYS A 1 67  ? 8.126   -23.301 55.061  1.00 82.28  ? 111 LYS A O   1 
ATOM   544  C  CB  . LYS A 1 67  ? 6.104   -24.702 57.293  1.00 84.16  ? 111 LYS A CB  1 
ATOM   545  C  CG  . LYS A 1 67  ? 5.649   -24.615 58.744  1.00 85.78  ? 111 LYS A CG  1 
ATOM   546  C  CD  . LYS A 1 67  ? 5.334   -25.960 59.362  1.00 87.15  ? 111 LYS A CD  1 
ATOM   547  C  CE  . LYS A 1 67  ? 4.767   -25.845 60.761  1.00 88.19  ? 111 LYS A CE  1 
ATOM   548  N  NZ  . LYS A 1 67  ? 4.358   -27.164 61.298  1.00 89.39  ? 111 LYS A NZ  1 
ATOM   549  N  N   . LEU A 1 68  ? 6.143   -24.015 54.243  1.00 80.02  ? 112 LEU A N   1 
ATOM   550  C  CA  . LEU A 1 68  ? 6.642   -24.271 52.901  1.00 79.41  ? 112 LEU A CA  1 
ATOM   551  C  C   . LEU A 1 68  ? 7.109   -22.972 52.249  1.00 78.55  ? 112 LEU A C   1 
ATOM   552  O  O   . LEU A 1 68  ? 8.081   -22.980 51.495  1.00 79.03  ? 112 LEU A O   1 
ATOM   553  C  CB  . LEU A 1 68  ? 5.541   -24.931 52.064  1.00 79.31  ? 112 LEU A CB  1 
ATOM   554  C  CG  . LEU A 1 68  ? 5.147   -26.350 52.475  1.00 80.58  ? 112 LEU A CG  1 
ATOM   555  C  CD1 . LEU A 1 68  ? 4.218   -26.966 51.441  1.00 80.56  ? 112 LEU A CD1 1 
ATOM   556  C  CD2 . LEU A 1 68  ? 6.371   -27.232 52.678  1.00 81.59  ? 112 LEU A CD2 1 
ATOM   557  N  N   . GLY A 1 69  ? 6.410   -21.868 52.542  1.00 77.53  ? 113 GLY A N   1 
ATOM   558  C  CA  . GLY A 1 69  ? 6.690   -20.584 51.918  1.00 77.32  ? 113 GLY A CA  1 
ATOM   559  C  C   . GLY A 1 69  ? 7.337   -19.587 52.877  1.00 78.32  ? 113 GLY A C   1 
ATOM   560  O  O   . GLY A 1 69  ? 6.984   -18.410 52.867  1.00 79.54  ? 113 GLY A O   1 
ATOM   561  N  N   . THR A 1 70  ? 8.290   -20.063 53.690  1.00 79.12  ? 114 THR A N   1 
ATOM   562  C  CA  . THR A 1 70  ? 9.077   -19.189 54.546  1.00 80.66  ? 114 THR A CA  1 
ATOM   563  C  C   . THR A 1 70  ? 10.127  -18.483 53.693  1.00 81.28  ? 114 THR A C   1 
ATOM   564  O  O   . THR A 1 70  ? 10.770  -19.113 52.856  1.00 79.78  ? 114 THR A O   1 
ATOM   565  C  CB  . THR A 1 70  ? 9.733   -19.966 55.695  1.00 81.85  ? 114 THR A CB  1 
ATOM   566  O  OG1 . THR A 1 70  ? 8.732   -20.760 56.331  1.00 82.15  ? 114 THR A OG1 1 
ATOM   567  C  CG2 . THR A 1 70  ? 10.391  -19.062 56.715  1.00 83.47  ? 114 THR A CG2 1 
ATOM   568  N  N   . GLN A 1 71  ? 10.297  -17.175 53.920  1.00 83.31  ? 115 GLN A N   1 
ATOM   569  C  CA  . GLN A 1 71  ? 11.155  -16.356 53.079  1.00 84.74  ? 115 GLN A CA  1 
ATOM   570  C  C   . GLN A 1 71  ? 11.802  -15.258 53.919  1.00 87.35  ? 115 GLN A C   1 
ATOM   571  O  O   . GLN A 1 71  ? 11.172  -14.710 54.820  1.00 87.93  ? 115 GLN A O   1 
ATOM   572  C  CB  . GLN A 1 71  ? 10.335  -15.772 51.927  1.00 83.93  ? 115 GLN A CB  1 
ATOM   573  C  CG  . GLN A 1 71  ? 11.178  -15.143 50.828  1.00 83.97  ? 115 GLN A CG  1 
ATOM   574  C  CD  . GLN A 1 71  ? 10.356  -14.778 49.616  1.00 82.78  ? 115 GLN A CD  1 
ATOM   575  O  OE1 . GLN A 1 71  ? 9.132   -14.897 49.607  1.00 80.72  ? 115 GLN A OE1 1 
ATOM   576  N  NE2 . GLN A 1 71  ? 11.033  -14.326 48.573  1.00 83.58  ? 115 GLN A NE2 1 
ATOM   577  N  N   . THR A 1 72  ? 13.065  -14.948 53.603  1.00 90.73  ? 116 THR A N   1 
ATOM   578  C  CA  . THR A 1 72  ? 13.828  -13.942 54.323  1.00 95.92  ? 116 THR A CA  1 
ATOM   579  C  C   . THR A 1 72  ? 14.177  -12.802 53.367  1.00 97.66  ? 116 THR A C   1 
ATOM   580  O  O   . THR A 1 72  ? 15.252  -12.795 52.768  1.00 98.34  ? 116 THR A O   1 
ATOM   581  C  CB  . THR A 1 72  ? 15.075  -14.560 54.970  1.00 98.52  ? 116 THR A CB  1 
ATOM   582  O  OG1 . THR A 1 72  ? 14.647  -15.602 55.849  1.00 98.40  ? 116 THR A OG1 1 
ATOM   583  C  CG2 . THR A 1 72  ? 15.907  -13.556 55.740  1.00 100.87 ? 116 THR A CG2 1 
ATOM   584  N  N   . VAL A 1 73  ? 13.244  -11.853 53.226  1.00 96.98  ? 117 VAL A N   1 
ATOM   585  C  CA  . VAL A 1 73  ? 13.477  -10.635 52.466  1.00 96.01  ? 117 VAL A CA  1 
ATOM   586  C  C   . VAL A 1 73  ? 14.237  -9.653  53.355  1.00 96.25  ? 117 VAL A C   1 
ATOM   587  O  O   . VAL A 1 73  ? 14.210  -9.779  54.577  1.00 96.33  ? 117 VAL A O   1 
ATOM   588  C  CB  . VAL A 1 73  ? 12.159  -10.025 51.944  1.00 93.82  ? 117 VAL A CB  1 
ATOM   589  C  CG1 . VAL A 1 73  ? 11.526  -10.895 50.868  1.00 93.90  ? 117 VAL A CG1 1 
ATOM   590  C  CG2 . VAL A 1 73  ? 11.161  -9.746  53.060  1.00 92.33  ? 117 VAL A CG2 1 
ATOM   591  N  N   . PRO A 1 74  ? 14.952  -8.657  52.779  1.00 97.14  ? 118 PRO A N   1 
ATOM   592  C  CA  . PRO A 1 74  ? 15.576  -7.603  53.580  1.00 97.83  ? 118 PRO A CA  1 
ATOM   593  C  C   . PRO A 1 74  ? 14.514  -6.794  54.324  1.00 95.42  ? 118 PRO A C   1 
ATOM   594  O  O   . PRO A 1 74  ? 13.653  -6.174  53.703  1.00 93.30  ? 118 PRO A O   1 
ATOM   595  C  CB  . PRO A 1 74  ? 16.350  -6.757  52.556  1.00 98.90  ? 118 PRO A CB  1 
ATOM   596  C  CG  . PRO A 1 74  ? 15.694  -7.068  51.225  1.00 97.73  ? 118 PRO A CG  1 
ATOM   597  C  CD  . PRO A 1 74  ? 15.216  -8.501  51.340  1.00 97.18  ? 118 PRO A CD  1 
ATOM   598  N  N   . CYS A 1 75  ? 14.594  -6.814  55.660  1.00 95.86  ? 119 CYS A N   1 
ATOM   599  C  CA  . CYS A 1 75  ? 13.532  -6.315  56.520  1.00 94.02  ? 119 CYS A CA  1 
ATOM   600  C  C   . CYS A 1 75  ? 13.560  -4.790  56.622  1.00 94.55  ? 119 CYS A C   1 
ATOM   601  O  O   . CYS A 1 75  ? 12.562  -4.184  57.008  1.00 93.46  ? 119 CYS A O   1 
ATOM   602  C  CB  . CYS A 1 75  ? 13.624  -6.945  57.905  1.00 94.81  ? 119 CYS A CB  1 
ATOM   603  S  SG  . CYS A 1 75  ? 15.316  -7.056  58.545  1.00 98.08  ? 119 CYS A SG  1 
ATOM   604  N  N   . ASN A 1 76  ? 14.701  -4.177  56.277  1.00 96.15  ? 120 ASN A N   1 
ATOM   605  C  CA  . ASN A 1 76  ? 14.826  -2.727  56.266  1.00 96.24  ? 120 ASN A CA  1 
ATOM   606  C  C   . ASN A 1 76  ? 14.276  -2.160  54.956  1.00 94.40  ? 120 ASN A C   1 
ATOM   607  O  O   . ASN A 1 76  ? 14.012  -0.963  54.871  1.00 94.76  ? 120 ASN A O   1 
ATOM   608  C  CB  . ASN A 1 76  ? 16.271  -2.275  56.499  1.00 99.12  ? 120 ASN A CB  1 
ATOM   609  C  CG  . ASN A 1 76  ? 17.226  -2.722  55.412  1.00 99.88  ? 120 ASN A CG  1 
ATOM   610  O  OD1 . ASN A 1 76  ? 17.434  -3.917  55.216  1.00 98.90  ? 120 ASN A OD1 1 
ATOM   611  N  ND2 . ASN A 1 76  ? 17.816  -1.770  54.707  1.00 101.51 ? 120 ASN A ND2 1 
ATOM   612  N  N   . LYS A 1 77  ? 14.109  -3.024  53.944  1.00 93.29  ? 121 LYS A N   1 
ATOM   613  C  CA  . LYS A 1 77  ? 13.618  -2.616  52.637  1.00 93.02  ? 121 LYS A CA  1 
ATOM   614  C  C   . LYS A 1 77  ? 12.219  -3.189  52.406  1.00 90.44  ? 121 LYS A C   1 
ATOM   615  O  O   . LYS A 1 77  ? 11.998  -3.916  51.437  1.00 89.44  ? 121 LYS A O   1 
ATOM   616  C  CB  . LYS A 1 77  ? 14.578  -3.093  51.542  1.00 94.77  ? 121 LYS A CB  1 
ATOM   617  C  CG  . LYS A 1 77  ? 16.011  -2.586  51.647  1.00 98.22  ? 121 LYS A CG  1 
ATOM   618  C  CD  . LYS A 1 77  ? 16.160  -1.113  51.339  1.00 100.32 ? 121 LYS A CD  1 
ATOM   619  C  CE  . LYS A 1 77  ? 17.605  -0.662  51.296  1.00 103.95 ? 121 LYS A CE  1 
ATOM   620  N  NZ  . LYS A 1 77  ? 17.719  0.771   50.940  1.00 106.29 ? 121 LYS A NZ  1 
ATOM   621  N  N   . ILE A 1 78  ? 11.279  -2.849  53.299  1.00 88.93  ? 122 ILE A N   1 
ATOM   622  C  CA  . ILE A 1 78  ? 9.898   -3.294  53.183  1.00 86.35  ? 122 ILE A CA  1 
ATOM   623  C  C   . ILE A 1 78  ? 9.000   -2.084  52.930  1.00 85.43  ? 122 ILE A C   1 
ATOM   624  O  O   . ILE A 1 78  ? 9.217   -1.012  53.494  1.00 86.88  ? 122 ILE A O   1 
ATOM   625  C  CB  . ILE A 1 78  ? 9.463   -4.092  54.432  1.00 85.92  ? 122 ILE A CB  1 
ATOM   626  C  CG1 . ILE A 1 78  ? 10.198  -5.434  54.513  1.00 86.70  ? 122 ILE A CG1 1 
ATOM   627  C  CG2 . ILE A 1 78  ? 7.949   -4.273  54.466  1.00 83.82  ? 122 ILE A CG2 1 
ATOM   628  C  CD1 . ILE A 1 78  ? 9.759   -6.322  55.657  1.00 86.74  ? 122 ILE A CD1 1 
ATOM   629  N  N   . LEU A 1 79  ? 7.988   -2.286  52.074  1.00 83.08  ? 123 LEU A N   1 
ATOM   630  C  CA  . LEU A 1 79  ? 7.001   -1.267  51.755  1.00 81.83  ? 123 LEU A CA  1 
ATOM   631  C  C   . LEU A 1 79  ? 5.603   -1.821  52.019  1.00 80.01  ? 123 LEU A C   1 
ATOM   632  O  O   . LEU A 1 79  ? 5.191   -2.797  51.395  1.00 77.91  ? 123 LEU A O   1 
ATOM   633  C  CB  . LEU A 1 79  ? 7.159   -0.856  50.287  1.00 82.15  ? 123 LEU A CB  1 
ATOM   634  C  CG  . LEU A 1 79  ? 6.086   0.091   49.747  1.00 82.67  ? 123 LEU A CG  1 
ATOM   635  C  CD1 . LEU A 1 79  ? 6.241   1.482   50.341  1.00 84.63  ? 123 LEU A CD1 1 
ATOM   636  C  CD2 . LEU A 1 79  ? 6.128   0.150   48.227  1.00 83.38  ? 123 LEU A CD2 1 
ATOM   637  N  N   . LEU A 1 80  ? 4.889   -1.182  52.952  1.00 80.18  ? 124 LEU A N   1 
ATOM   638  C  CA  . LEU A 1 80  ? 3.478   -1.452  53.177  1.00 79.23  ? 124 LEU A CA  1 
ATOM   639  C  C   . LEU A 1 80  ? 2.657   -0.520  52.290  1.00 79.96  ? 124 LEU A C   1 
ATOM   640  O  O   . LEU A 1 80  ? 3.205   0.370   51.644  1.00 81.03  ? 124 LEU A O   1 
ATOM   641  C  CB  . LEU A 1 80  ? 3.156   -1.236  54.660  1.00 79.30  ? 124 LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 80  ? 4.034   -2.003  55.652  1.00 78.80  ? 124 LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 80  ? 3.532   -1.814  57.075  1.00 79.55  ? 124 LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 80  ? 4.098   -3.484  55.302  1.00 77.69  ? 124 LEU A CD2 1 
ATOM   645  N  N   . TRP A 1 81  ? 1.339   -0.742  52.260  1.00 80.67  ? 125 TRP A N   1 
ATOM   646  C  CA  . TRP A 1 81  ? 0.433   0.098   51.495  1.00 82.90  ? 125 TRP A CA  1 
ATOM   647  C  C   . TRP A 1 81  ? -0.990  -0.076  52.016  1.00 84.41  ? 125 TRP A C   1 
ATOM   648  O  O   . TRP A 1 81  ? -1.302  -1.088  52.643  1.00 84.08  ? 125 TRP A O   1 
ATOM   649  C  CB  . TRP A 1 81  ? 0.534   -0.216  49.995  1.00 82.33  ? 125 TRP A CB  1 
ATOM   650  C  CG  . TRP A 1 81  ? 0.313   -1.659  49.657  1.00 81.09  ? 125 TRP A CG  1 
ATOM   651  C  CD1 . TRP A 1 81  ? 1.275   -2.601  49.436  1.00 80.26  ? 125 TRP A CD1 1 
ATOM   652  C  CD2 . TRP A 1 81  ? -0.950  -2.327  49.475  1.00 81.65  ? 125 TRP A CD2 1 
ATOM   653  N  NE1 . TRP A 1 81  ? 0.701   -3.809  49.148  1.00 80.46  ? 125 TRP A NE1 1 
ATOM   654  C  CE2 . TRP A 1 81  ? -0.662  -3.673  49.162  1.00 80.75  ? 125 TRP A CE2 1 
ATOM   655  C  CE3 . TRP A 1 81  ? -2.290  -1.927  49.553  1.00 82.81  ? 125 TRP A CE3 1 
ATOM   656  C  CZ2 . TRP A 1 81  ? -1.665  -4.614  48.929  1.00 81.02  ? 125 TRP A CZ2 1 
ATOM   657  C  CZ3 . TRP A 1 81  ? -3.280  -2.858  49.323  1.00 82.85  ? 125 TRP A CZ3 1 
ATOM   658  C  CH2 . TRP A 1 81  ? -2.969  -4.183  49.014  1.00 82.11  ? 125 TRP A CH2 1 
ATOM   659  N  N   . SER A 1 82  ? -1.839  0.924   51.754  1.00 87.23  ? 126 SER A N   1 
ATOM   660  C  CA  . SER A 1 82  ? -3.250  0.843   52.094  1.00 89.49  ? 126 SER A CA  1 
ATOM   661  C  C   . SER A 1 82  ? -4.084  1.497   50.995  1.00 92.61  ? 126 SER A C   1 
ATOM   662  O  O   . SER A 1 82  ? -4.068  2.716   50.843  1.00 94.32  ? 126 SER A O   1 
ATOM   663  C  CB  . SER A 1 82  ? -3.520  1.453   53.446  1.00 90.15  ? 126 SER A CB  1 
ATOM   664  O  OG  . SER A 1 82  ? -4.806  1.078   53.917  1.00 91.22  ? 126 SER A OG  1 
ATOM   665  N  N   . ARG A 1 83  ? -4.779  0.654   50.217  1.00 94.57  ? 127 ARG A N   1 
ATOM   666  C  CA  . ARG A 1 83  ? -5.647  1.074   49.125  1.00 98.62  ? 127 ARG A CA  1 
ATOM   667  C  C   . ARG A 1 83  ? -4.820  1.718   48.010  1.00 99.03  ? 127 ARG A C   1 
ATOM   668  O  O   . ARG A 1 83  ? -5.340  2.525   47.243  1.00 101.84 ? 127 ARG A O   1 
ATOM   669  C  CB  . ARG A 1 83  ? -6.768  1.984   49.643  1.00 103.20 ? 127 ARG A CB  1 
ATOM   670  C  CG  . ARG A 1 83  ? -7.829  1.244   50.446  1.00 105.42 ? 127 ARG A CG  1 
ATOM   671  C  CD  . ARG A 1 83  ? -8.816  2.167   51.137  1.00 109.17 ? 127 ARG A CD  1 
ATOM   672  N  NE  . ARG A 1 83  ? -10.079 1.503   51.440  1.00 111.54 ? 127 ARG A NE  1 
ATOM   673  C  CZ  . ARG A 1 83  ? -10.221 0.481   52.281  1.00 111.49 ? 127 ARG A CZ  1 
ATOM   674  N  NH1 . ARG A 1 83  ? -9.182  0.020   52.956  1.00 108.54 ? 127 ARG A NH1 1 
ATOM   675  N  NH2 . ARG A 1 83  ? -11.409 -0.071  52.453  1.00 114.35 ? 127 ARG A NH2 1 
ATOM   676  N  N   . ILE A 1 84  ? -3.539  1.332   47.925  1.00 97.40  ? 128 ILE A N   1 
ATOM   677  C  CA  . ILE A 1 84  ? -2.657  1.703   46.829  1.00 98.41  ? 128 ILE A CA  1 
ATOM   678  C  C   . ILE A 1 84  ? -1.801  0.484   46.492  1.00 96.57  ? 128 ILE A C   1 
ATOM   679  O  O   . ILE A 1 84  ? -0.594  0.482   46.725  1.00 95.19  ? 128 ILE A O   1 
ATOM   680  C  CB  . ILE A 1 84  ? -1.793  2.933   47.187  1.00 99.34  ? 128 ILE A CB  1 
ATOM   681  C  CG1 . ILE A 1 84  ? -2.629  4.200   47.393  1.00 102.69 ? 128 ILE A CG1 1 
ATOM   682  C  CG2 . ILE A 1 84  ? -0.710  3.165   46.144  1.00 100.25 ? 128 ILE A CG2 1 
ATOM   683  C  CD1 . ILE A 1 84  ? -3.267  4.741   46.128  1.00 105.51 ? 128 ILE A CD1 1 
ATOM   684  N  N   . LYS A 1 85  ? -2.443  -0.565  45.964  1.00 96.73  ? 129 LYS A N   1 
ATOM   685  C  CA  . LYS A 1 85  ? -1.741  -1.785  45.602  1.00 95.98  ? 129 LYS A CA  1 
ATOM   686  C  C   . LYS A 1 85  ? -0.950  -1.556  44.315  1.00 97.46  ? 129 LYS A C   1 
ATOM   687  O  O   . LYS A 1 85  ? 0.214   -1.941  44.230  1.00 97.58  ? 129 LYS A O   1 
ATOM   688  C  CB  . LYS A 1 85  ? -2.713  -2.958  45.429  1.00 96.55  ? 129 LYS A CB  1 
ATOM   689  C  CG  . LYS A 1 85  ? -2.057  -4.277  45.037  1.00 95.85  ? 129 LYS A CG  1 
ATOM   690  C  CD  . LYS A 1 85  ? -3.029  -5.391  44.711  1.00 97.51  ? 129 LYS A CD  1 
ATOM   691  C  CE  . LYS A 1 85  ? -3.704  -5.972  45.935  1.00 97.87  ? 129 LYS A CE  1 
ATOM   692  N  NZ  . LYS A 1 85  ? -4.527  -7.157  45.591  1.00 99.93  ? 129 LYS A NZ  1 
ATOM   693  N  N   . ASP A 1 86  ? -1.597  -0.926  43.326  1.00 99.71  ? 130 ASP A N   1 
ATOM   694  C  CA  . ASP A 1 86  ? -1.057  -0.823  41.980  1.00 100.60 ? 130 ASP A CA  1 
ATOM   695  C  C   . ASP A 1 86  ? 0.214   0.023   41.977  1.00 100.19 ? 130 ASP A C   1 
ATOM   696  O  O   . ASP A 1 86  ? 1.219   -0.384  41.399  1.00 101.13 ? 130 ASP A O   1 
ATOM   697  C  CB  . ASP A 1 86  ? -2.097  -0.258  41.009  1.00 103.68 ? 130 ASP A CB  1 
ATOM   698  C  CG  . ASP A 1 86  ? -3.316  -1.147  40.826  1.00 105.41 ? 130 ASP A CG  1 
ATOM   699  O  OD1 . ASP A 1 86  ? -3.377  -2.209  41.481  1.00 102.78 ? 130 ASP A OD1 1 
ATOM   700  O  OD2 . ASP A 1 86  ? -4.198  -0.770  40.031  1.00 109.58 ? 130 ASP A OD2 1 
ATOM   701  N  N   . LEU A 1 87  ? 0.162   1.193   42.625  1.00 99.76  ? 131 LEU A N   1 
ATOM   702  C  CA  . LEU A 1 87  ? 1.271   2.135   42.601  1.00 99.76  ? 131 LEU A CA  1 
ATOM   703  C  C   . LEU A 1 87  ? 2.423   1.615   43.461  1.00 96.75  ? 131 LEU A C   1 
ATOM   704  O  O   . LEU A 1 87  ? 3.586   1.846   43.137  1.00 98.22  ? 131 LEU A O   1 
ATOM   705  C  CB  . LEU A 1 87  ? 0.789   3.501   43.098  1.00 101.71 ? 131 LEU A CB  1 
ATOM   706  C  CG  . LEU A 1 87  ? 1.714   4.678   42.789  1.00 104.55 ? 131 LEU A CG  1 
ATOM   707  C  CD1 . LEU A 1 87  ? 1.619   5.074   41.324  1.00 107.48 ? 131 LEU A CD1 1 
ATOM   708  C  CD2 . LEU A 1 87  ? 1.397   5.866   43.683  1.00 106.54 ? 131 LEU A CD2 1 
ATOM   709  N  N   . ALA A 1 88  ? 2.091   0.922   44.558  1.00 93.82  ? 132 ALA A N   1 
ATOM   710  C  CA  . ALA A 1 88  ? 3.096   0.352   45.443  1.00 91.47  ? 132 ALA A CA  1 
ATOM   711  C  C   . ALA A 1 88  ? 3.894   -0.726  44.713  1.00 90.75  ? 132 ALA A C   1 
ATOM   712  O  O   . ALA A 1 88  ? 5.095   -0.860  44.934  1.00 90.80  ? 132 ALA A O   1 
ATOM   713  C  CB  . ALA A 1 88  ? 2.440   -0.198  46.686  1.00 89.86  ? 132 ALA A CB  1 
ATOM   714  N  N   . HIS A 1 89  ? 3.212   -1.490  43.848  1.00 91.03  ? 133 HIS A N   1 
ATOM   715  C  CA  . HIS A 1 89  ? 3.846   -2.535  43.058  1.00 90.89  ? 133 HIS A CA  1 
ATOM   716  C  C   . HIS A 1 89  ? 4.715   -1.921  41.962  1.00 93.16  ? 133 HIS A C   1 
ATOM   717  O  O   . HIS A 1 89  ? 5.807   -2.417  41.695  1.00 94.61  ? 133 HIS A O   1 
ATOM   718  C  CB  . HIS A 1 89  ? 2.798   -3.491  42.479  1.00 90.77  ? 133 HIS A CB  1 
ATOM   719  C  CG  . HIS A 1 89  ? 2.143   -4.353  43.506  1.00 88.86  ? 133 HIS A CG  1 
ATOM   720  N  ND1 . HIS A 1 89  ? 1.184   -5.290  43.188  1.00 89.19  ? 133 HIS A ND1 1 
ATOM   721  C  CD2 . HIS A 1 89  ? 2.307   -4.426  44.834  1.00 86.95  ? 133 HIS A CD2 1 
ATOM   722  C  CE1 . HIS A 1 89  ? 0.789   -5.901  44.295  1.00 88.22  ? 133 HIS A CE1 1 
ATOM   723  N  NE2 . HIS A 1 89  ? 1.457   -5.390  45.306  1.00 86.39  ? 133 HIS A NE2 1 
ATOM   724  N  N   . GLN A 1 90  ? 4.217   -0.849  41.332  1.00 94.69  ? 134 GLN A N   1 
ATOM   725  C  CA  . GLN A 1 90  ? 4.962   -0.128  40.311  1.00 96.69  ? 134 GLN A CA  1 
ATOM   726  C  C   . GLN A 1 90  ? 6.266   0.416   40.892  1.00 96.88  ? 134 GLN A C   1 
ATOM   727  O  O   . GLN A 1 90  ? 7.280   0.450   40.199  1.00 98.21  ? 134 GLN A O   1 
ATOM   728  C  CB  . GLN A 1 90  ? 4.121   1.014   39.738  1.00 98.94  ? 134 GLN A CB  1 
ATOM   729  C  CG  . GLN A 1 90  ? 2.982   0.547   38.843  1.00 100.18 ? 134 GLN A CG  1 
ATOM   730  C  CD  . GLN A 1 90  ? 2.054   1.673   38.457  1.00 102.72 ? 134 GLN A CD  1 
ATOM   731  O  OE1 . GLN A 1 90  ? 2.315   2.844   38.726  1.00 103.30 ? 134 GLN A OE1 1 
ATOM   732  N  NE2 . GLN A 1 90  ? 0.954   1.323   37.811  1.00 104.69 ? 134 GLN A NE2 1 
ATOM   733  N  N   . PHE A 1 91  ? 6.222   0.844   42.161  1.00 96.45  ? 135 PHE A N   1 
ATOM   734  C  CA  . PHE A 1 91  ? 7.390   1.373   42.847  1.00 97.12  ? 135 PHE A CA  1 
ATOM   735  C  C   . PHE A 1 91  ? 8.435   0.273   43.030  1.00 96.19  ? 135 PHE A C   1 
ATOM   736  O  O   . PHE A 1 91  ? 9.612   0.485   42.745  1.00 97.40  ? 135 PHE A O   1 
ATOM   737  C  CB  . PHE A 1 91  ? 6.986   2.000   44.185  1.00 96.72  ? 135 PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 91  ? 8.133   2.534   45.008  1.00 98.39  ? 135 PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 91  ? 8.919   1.683   45.772  1.00 97.45  ? 135 PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 91  ? 8.442   3.886   45.001  1.00 101.51 ? 135 PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 91  ? 9.978   2.175   46.521  1.00 98.89  ? 135 PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 91  ? 9.503   4.376   45.749  1.00 102.85 ? 135 PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 91  ? 10.268  3.520   46.508  1.00 101.50 ? 135 PHE A CZ  1 
ATOM   744  N  N   . THR A 1 92  ? 7.992   -0.896  43.511  1.00 94.67  ? 136 THR A N   1 
ATOM   745  C  CA  . THR A 1 92  ? 8.885   -2.009  43.797  1.00 94.67  ? 136 THR A CA  1 
ATOM   746  C  C   . THR A 1 92  ? 9.348   -2.680  42.504  1.00 98.05  ? 136 THR A C   1 
ATOM   747  O  O   . THR A 1 92  ? 10.391  -3.331  42.488  1.00 97.87  ? 136 THR A O   1 
ATOM   748  C  CB  . THR A 1 92  ? 8.219   -3.023  44.736  1.00 91.54  ? 136 THR A CB  1 
ATOM   749  O  OG1 . THR A 1 92  ? 7.006   -3.466  44.127  1.00 90.46  ? 136 THR A OG1 1 
ATOM   750  C  CG2 . THR A 1 92  ? 7.928   -2.450  46.106  1.00 90.28  ? 136 THR A CG2 1 
ATOM   751  N  N   . GLN A 1 93  ? 8.562   -2.532  41.429  1.00 101.68 ? 137 GLN A N   1 
ATOM   752  C  CA  . GLN A 1 93  ? 8.929   -3.062  40.125  1.00 105.31 ? 137 GLN A CA  1 
ATOM   753  C  C   . GLN A 1 93  ? 10.051  -2.212  39.529  1.00 108.66 ? 137 GLN A C   1 
ATOM   754  O  O   . GLN A 1 93  ? 10.926  -2.738  38.844  1.00 111.22 ? 137 GLN A O   1 
ATOM   755  C  CB  . GLN A 1 93  ? 7.705   -3.110  39.207  1.00 106.76 ? 137 GLN A CB  1 
ATOM   756  C  CG  . GLN A 1 93  ? 7.958   -3.763  37.852  1.00 110.31 ? 137 GLN A CG  1 
ATOM   757  C  CD  . GLN A 1 93  ? 8.318   -5.227  37.953  1.00 111.21 ? 137 GLN A CD  1 
ATOM   758  O  OE1 . GLN A 1 93  ? 9.425   -5.592  38.344  1.00 111.41 ? 137 GLN A OE1 1 
ATOM   759  N  NE2 . GLN A 1 93  ? 7.384   -6.084  37.573  1.00 111.99 ? 137 GLN A NE2 1 
ATOM   760  N  N   . VAL A 1 94  ? 10.012  -0.899  39.794  1.00 109.69 ? 138 VAL A N   1 
ATOM   761  C  CA  . VAL A 1 94  ? 11.055  0.016   39.358  1.00 111.91 ? 138 VAL A CA  1 
ATOM   762  C  C   . VAL A 1 94  ? 12.274  -0.163  40.263  1.00 111.84 ? 138 VAL A C   1 
ATOM   763  O  O   . VAL A 1 94  ? 13.325  -0.607  39.805  1.00 113.34 ? 138 VAL A O   1 
ATOM   764  C  CB  . VAL A 1 94  ? 10.553  1.475   39.349  1.00 113.30 ? 138 VAL A CB  1 
ATOM   765  C  CG1 . VAL A 1 94  ? 11.688  2.471   39.156  1.00 116.67 ? 138 VAL A CG1 1 
ATOM   766  C  CG2 . VAL A 1 94  ? 9.469   1.692   38.302  1.00 114.36 ? 138 VAL A CG2 1 
ATOM   767  N  N   . GLN A 1 95  ? 12.117  0.183   41.547  1.00 110.85 ? 139 GLN A N   1 
ATOM   768  C  CA  . GLN A 1 95  ? 13.178  0.037   42.531  1.00 111.32 ? 139 GLN A CA  1 
ATOM   769  C  C   . GLN A 1 95  ? 13.088  -1.359  43.144  1.00 108.45 ? 139 GLN A C   1 
ATOM   770  O  O   . GLN A 1 95  ? 12.213  -1.625  43.964  1.00 107.41 ? 139 GLN A O   1 
ATOM   771  C  CB  . GLN A 1 95  ? 13.067  1.139   43.586  1.00 113.05 ? 139 GLN A CB  1 
ATOM   772  C  CG  . GLN A 1 95  ? 14.086  1.009   44.710  1.00 114.74 ? 139 GLN A CG  1 
ATOM   773  C  CD  . GLN A 1 95  ? 14.229  2.267   45.532  1.00 118.12 ? 139 GLN A CD  1 
ATOM   774  O  OE1 . GLN A 1 95  ? 13.583  3.282   45.277  1.00 121.42 ? 139 GLN A OE1 1 
ATOM   775  N  NE2 . GLN A 1 95  ? 15.090  2.207   46.534  1.00 119.83 ? 139 GLN A NE2 1 
ATOM   776  N  N   . ARG A 1 96  ? 14.029  -2.231  42.759  1.00 107.90 ? 140 ARG A N   1 
ATOM   777  C  CA  . ARG A 1 96  ? 13.868  -3.670  42.907  1.00 105.75 ? 140 ARG A CA  1 
ATOM   778  C  C   . ARG A 1 96  ? 14.246  -4.156  44.307  1.00 103.70 ? 140 ARG A C   1 
ATOM   779  O  O   . ARG A 1 96  ? 13.915  -5.286  44.660  1.00 102.63 ? 140 ARG A O   1 
ATOM   780  C  CB  . ARG A 1 96  ? 14.707  -4.398  41.851  1.00 107.67 ? 140 ARG A CB  1 
ATOM   781  C  CG  . ARG A 1 96  ? 14.193  -4.250  40.425  1.00 108.14 ? 140 ARG A CG  1 
ATOM   782  C  CD  . ARG A 1 96  ? 12.841  -4.915  40.226  1.00 106.39 ? 140 ARG A CD  1 
ATOM   783  N  NE  . ARG A 1 96  ? 12.459  -5.035  38.825  1.00 107.41 ? 140 ARG A NE  1 
ATOM   784  C  CZ  . ARG A 1 96  ? 13.024  -5.863  37.953  1.00 109.25 ? 140 ARG A CZ  1 
ATOM   785  N  NH1 . ARG A 1 96  ? 14.000  -6.668  38.334  1.00 109.26 ? 140 ARG A NH1 1 
ATOM   786  N  NH2 . ARG A 1 96  ? 12.604  -5.889  36.699  1.00 111.28 ? 140 ARG A NH2 1 
ATOM   787  N  N   . ASP A 1 97  ? 14.934  -3.323  45.101  1.00 103.71 ? 141 ASP A N   1 
ATOM   788  C  CA  . ASP A 1 97  ? 15.411  -3.754  46.408  1.00 103.03 ? 141 ASP A CA  1 
ATOM   789  C  C   . ASP A 1 97  ? 14.314  -3.597  47.464  1.00 99.97  ? 141 ASP A C   1 
ATOM   790  O  O   . ASP A 1 97  ? 14.437  -4.156  48.551  1.00 99.15  ? 141 ASP A O   1 
ATOM   791  C  CB  . ASP A 1 97  ? 16.711  -3.045  46.808  1.00 105.55 ? 141 ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 97  ? 16.632  -1.529  46.867  1.00 106.83 ? 141 ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 97  ? 15.624  -0.974  46.395  1.00 107.18 ? 141 ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 97  ? 17.582  -0.916  47.392  1.00 108.44 ? 141 ASP A OD2 1 
ATOM   795  N  N   . MET A 1 98  ? 13.249  -2.845  47.145  1.00 98.53  ? 142 MET A N   1 
ATOM   796  C  CA  . MET A 1 98  ? 12.088  -2.726  48.018  1.00 96.76  ? 142 MET A CA  1 
ATOM   797  C  C   . MET A 1 98  ? 11.111  -3.869  47.741  1.00 94.33  ? 142 MET A C   1 
ATOM   798  O  O   . MET A 1 98  ? 10.930  -4.266  46.591  1.00 94.09  ? 142 MET A O   1 
ATOM   799  C  CB  . MET A 1 98  ? 11.366  -1.388  47.813  1.00 98.35  ? 142 MET A CB  1 
ATOM   800  C  CG  . MET A 1 98  ? 11.130  -0.610  49.100  1.00 98.94  ? 142 MET A CG  1 
ATOM   801  S  SD  . MET A 1 98  ? 12.624  0.155   49.780  1.00 101.87 ? 142 MET A SD  1 
ATOM   802  C  CE  . MET A 1 98  ? 12.450  1.827   49.157  1.00 104.00 ? 142 MET A CE  1 
ATOM   803  N  N   . PHE A 1 99  ? 10.473  -4.372  48.809  1.00 92.15  ? 143 PHE A N   1 
ATOM   804  C  CA  . PHE A 1 99  ? 9.536   -5.484  48.723  1.00 90.44  ? 143 PHE A CA  1 
ATOM   805  C  C   . PHE A 1 99  ? 8.198   -5.103  49.354  1.00 87.14  ? 143 PHE A C   1 
ATOM   806  O  O   . PHE A 1 99  ? 8.165   -4.526  50.439  1.00 86.10  ? 143 PHE A O   1 
ATOM   807  C  CB  . PHE A 1 99  ? 10.087  -6.724  49.436  1.00 91.81  ? 143 PHE A CB  1 
ATOM   808  C  CG  . PHE A 1 99  ? 11.213  -7.432  48.726  1.00 94.75  ? 143 PHE A CG  1 
ATOM   809  C  CD1 . PHE A 1 99  ? 12.481  -6.872  48.662  1.00 96.43  ? 143 PHE A CD1 1 
ATOM   810  C  CD2 . PHE A 1 99  ? 11.006  -8.662  48.118  1.00 95.91  ? 143 PHE A CD2 1 
ATOM   811  C  CE1 . PHE A 1 99  ? 13.514  -7.526  48.008  1.00 98.44  ? 143 PHE A CE1 1 
ATOM   812  C  CE2 . PHE A 1 99  ? 12.040  -9.314  47.462  1.00 97.71  ? 143 PHE A CE2 1 
ATOM   813  C  CZ  . PHE A 1 99  ? 13.292  -8.746  47.408  1.00 99.09  ? 143 PHE A CZ  1 
ATOM   814  N  N   . THR A 1 100 ? 7.101   -5.439  48.659  1.00 84.97  ? 144 THR A N   1 
ATOM   815  C  CA  . THR A 1 100 ? 5.766   -5.427  49.238  1.00 82.36  ? 144 THR A CA  1 
ATOM   816  C  C   . THR A 1 100 ? 5.418   -6.849  49.676  1.00 81.40  ? 144 THR A C   1 
ATOM   817  O  O   . THR A 1 100 ? 6.240   -7.755  49.552  1.00 81.33  ? 144 THR A O   1 
ATOM   818  C  CB  . THR A 1 100 ? 4.730   -4.852  48.259  1.00 81.67  ? 144 THR A CB  1 
ATOM   819  O  OG1 . THR A 1 100 ? 4.675   -5.683  47.098  1.00 80.73  ? 144 THR A OG1 1 
ATOM   820  C  CG2 . THR A 1 100 ? 5.030   -3.427  47.848  1.00 82.17  ? 144 THR A CG2 1 
ATOM   821  N  N   . LEU A 1 101 ? 4.198   -7.032  50.195  1.00 79.05  ? 145 LEU A N   1 
ATOM   822  C  CA  . LEU A 1 101 ? 3.722   -8.343  50.610  1.00 77.11  ? 145 LEU A CA  1 
ATOM   823  C  C   . LEU A 1 101 ? 3.581   -9.267  49.400  1.00 75.68  ? 145 LEU A C   1 
ATOM   824  O  O   . LEU A 1 101 ? 3.839   -10.463 49.505  1.00 75.15  ? 145 LEU A O   1 
ATOM   825  C  CB  . LEU A 1 101 ? 2.382   -8.175  51.333  1.00 76.35  ? 145 LEU A CB  1 
ATOM   826  C  CG  . LEU A 1 101 ? 1.741   -9.461  51.855  1.00 74.58  ? 145 LEU A CG  1 
ATOM   827  C  CD1 . LEU A 1 101 ? 2.539   -10.035 53.014  1.00 75.26  ? 145 LEU A CD1 1 
ATOM   828  C  CD2 . LEU A 1 101 ? 0.300   -9.214  52.273  1.00 74.38  ? 145 LEU A CD2 1 
ATOM   829  N  N   . GLU A 1 102 ? 3.186   -8.700  48.253  1.00 75.70  ? 146 GLU A N   1 
ATOM   830  C  CA  . GLU A 1 102 ? 2.867   -9.484  47.069  1.00 74.91  ? 146 GLU A CA  1 
ATOM   831  C  C   . GLU A 1 102 ? 4.137   -9.843  46.296  1.00 75.15  ? 146 GLU A C   1 
ATOM   832  O  O   . GLU A 1 102 ? 4.069   -10.594 45.324  1.00 74.38  ? 146 GLU A O   1 
ATOM   833  C  CB  . GLU A 1 102 ? 1.895   -8.722  46.164  1.00 76.03  ? 146 GLU A CB  1 
ATOM   834  C  CG  . GLU A 1 102 ? 0.505   -8.547  46.755  1.00 75.55  ? 146 GLU A CG  1 
ATOM   835  C  CD  . GLU A 1 102 ? 0.426   -7.616  47.954  1.00 76.98  ? 146 GLU A CD  1 
ATOM   836  O  OE1 . GLU A 1 102 ? 0.993   -6.512  47.874  1.00 78.84  ? 146 GLU A OE1 1 
ATOM   837  O  OE2 . GLU A 1 102 ? -0.210  -7.993  48.959  1.00 77.40  ? 146 GLU A OE2 1 
ATOM   838  N  N   . ASP A 1 103 ? 5.286   -9.300  46.719  1.00 75.83  ? 147 ASP A N   1 
ATOM   839  C  CA  . ASP A 1 103 ? 6.566   -9.623  46.106  1.00 76.88  ? 147 ASP A CA  1 
ATOM   840  C  C   . ASP A 1 103 ? 7.197   -10.830 46.802  1.00 74.99  ? 147 ASP A C   1 
ATOM   841  O  O   . ASP A 1 103 ? 8.242   -11.310 46.366  1.00 76.00  ? 147 ASP A O   1 
ATOM   842  C  CB  . ASP A 1 103 ? 7.504   -8.412  46.111  1.00 79.68  ? 147 ASP A CB  1 
ATOM   843  C  CG  . ASP A 1 103 ? 7.036   -7.268  45.225  1.00 80.80  ? 147 ASP A CG  1 
ATOM   844  O  OD1 . ASP A 1 103 ? 6.738   -7.526  44.040  1.00 80.45  ? 147 ASP A OD1 1 
ATOM   845  O  OD2 . ASP A 1 103 ? 6.988   -6.124  45.722  1.00 81.55  ? 147 ASP A OD2 1 
ATOM   846  N  N   . THR A 1 104 ? 6.569   -11.306 47.888  1.00 71.91  ? 148 THR A N   1 
ATOM   847  C  CA  . THR A 1 104 ? 6.921   -12.584 48.489  1.00 70.80  ? 148 THR A CA  1 
ATOM   848  C  C   . THR A 1 104 ? 6.190   -13.695 47.741  1.00 70.10  ? 148 THR A C   1 
ATOM   849  O  O   . THR A 1 104 ? 5.274   -13.422 46.968  1.00 68.96  ? 148 THR A O   1 
ATOM   850  C  CB  . THR A 1 104 ? 6.588   -12.617 49.987  1.00 69.41  ? 148 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 104 ? 5.167   -12.646 50.134  1.00 66.71  ? 148 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 104 ? 7.162   -11.442 50.747  1.00 70.38  ? 148 THR A CG2 1 
ATOM   853  N  N   . LEU A 1 105 ? 6.593   -14.947 47.992  1.00 70.81  ? 149 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 105 ? 6.023   -16.098 47.308  1.00 70.47  ? 149 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 105 ? 4.525   -16.187 47.591  1.00 68.34  ? 149 LEU A C   1 
ATOM   856  O  O   . LEU A 1 105 ? 3.718   -16.140 46.666  1.00 66.68  ? 149 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 105 ? 6.752   -17.368 47.763  1.00 72.26  ? 149 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 105 ? 6.167   -18.689 47.261  1.00 72.56  ? 149 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 105 ? 6.206   -18.768 45.742  1.00 72.75  ? 149 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 105 ? 6.905   -19.871 47.871  1.00 74.88  ? 149 LEU A CD2 1 
ATOM   861  N  N   . LEU A 1 106 ? 4.170   -16.301 48.878  1.00 68.38  ? 150 LEU A N   1 
ATOM   862  C  CA  . LEU A 1 106 ? 2.797   -16.550 49.292  1.00 67.48  ? 150 LEU A CA  1 
ATOM   863  C  C   . LEU A 1 106 ? 1.882   -15.429 48.800  1.00 66.10  ? 150 LEU A C   1 
ATOM   864  O  O   . LEU A 1 106 ? 0.777   -15.694 48.331  1.00 64.21  ? 150 LEU A O   1 
ATOM   865  C  CB  . LEU A 1 106 ? 2.747   -16.678 50.819  1.00 68.11  ? 150 LEU A CB  1 
ATOM   866  C  CG  . LEU A 1 106 ? 3.569   -17.821 51.419  1.00 70.52  ? 150 LEU A CG  1 
ATOM   867  C  CD1 . LEU A 1 106 ? 3.303   -17.957 52.911  1.00 71.28  ? 150 LEU A CD1 1 
ATOM   868  C  CD2 . LEU A 1 106 ? 3.291   -19.138 50.705  1.00 70.99  ? 150 LEU A CD2 1 
ATOM   869  N  N   . GLY A 1 107 ? 2.357   -14.181 48.905  1.00 66.50  ? 151 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 107 ? 1.613   -13.027 48.425  1.00 66.42  ? 151 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 107 ? 1.433   -13.049 46.908  1.00 67.39  ? 151 GLY A C   1 
ATOM   872  O  O   . GLY A 1 107 ? 0.347   -12.764 46.409  1.00 67.28  ? 151 GLY A O   1 
ATOM   873  N  N   . TYR A 1 108 ? 2.512   -13.395 46.193  1.00 68.65  ? 152 TYR A N   1 
ATOM   874  C  CA  . TYR A 1 108 ? 2.519   -13.454 44.739  1.00 69.33  ? 152 TYR A CA  1 
ATOM   875  C  C   . TYR A 1 108 ? 1.480   -14.467 44.260  1.00 68.14  ? 152 TYR A C   1 
ATOM   876  O  O   . TYR A 1 108 ? 0.739   -14.192 43.318  1.00 68.64  ? 152 TYR A O   1 
ATOM   877  C  CB  . TYR A 1 108 ? 3.935   -13.785 44.251  1.00 72.07  ? 152 TYR A CB  1 
ATOM   878  C  CG  . TYR A 1 108 ? 4.162   -13.762 42.759  1.00 74.09  ? 152 TYR A CG  1 
ATOM   879  C  CD1 . TYR A 1 108 ? 3.702   -14.782 41.939  1.00 74.98  ? 152 TYR A CD1 1 
ATOM   880  C  CD2 . TYR A 1 108 ? 4.874   -12.731 42.165  1.00 76.22  ? 152 TYR A CD2 1 
ATOM   881  C  CE1 . TYR A 1 108 ? 3.926   -14.769 40.571  1.00 77.23  ? 152 TYR A CE1 1 
ATOM   882  C  CE2 . TYR A 1 108 ? 5.108   -12.704 40.799  1.00 78.86  ? 152 TYR A CE2 1 
ATOM   883  C  CZ  . TYR A 1 108 ? 4.631   -13.726 39.997  1.00 79.30  ? 152 TYR A CZ  1 
ATOM   884  O  OH  . TYR A 1 108 ? 4.860   -13.701 38.642  1.00 80.84  ? 152 TYR A OH  1 
ATOM   885  N  N   . LEU A 1 109 ? 1.429   -15.626 44.930  1.00 67.20  ? 153 LEU A N   1 
ATOM   886  C  CA  . LEU A 1 109 ? 0.564   -16.726 44.532  1.00 67.60  ? 153 LEU A CA  1 
ATOM   887  C  C   . LEU A 1 109 ? -0.902  -16.299 44.532  1.00 67.01  ? 153 LEU A C   1 
ATOM   888  O  O   . LEU A 1 109 ? -1.621  -16.569 43.572  1.00 66.29  ? 153 LEU A O   1 
ATOM   889  C  CB  . LEU A 1 109 ? 0.773   -17.903 45.492  1.00 67.27  ? 153 LEU A CB  1 
ATOM   890  C  CG  . LEU A 1 109 ? 2.124   -18.613 45.407  1.00 68.80  ? 153 LEU A CG  1 
ATOM   891  C  CD1 . LEU A 1 109 ? 2.129   -19.862 46.276  1.00 69.41  ? 153 LEU A CD1 1 
ATOM   892  C  CD2 . LEU A 1 109 ? 2.475   -18.964 43.968  1.00 70.14  ? 153 LEU A CD2 1 
ATOM   893  N  N   . ALA A 1 110 ? -1.329  -15.626 45.609  1.00 67.13  ? 154 ALA A N   1 
ATOM   894  C  CA  . ALA A 1 110 ? -2.743  -15.469 45.917  1.00 66.77  ? 154 ALA A CA  1 
ATOM   895  C  C   . ALA A 1 110 ? -3.253  -14.065 45.586  1.00 67.37  ? 154 ALA A C   1 
ATOM   896  O  O   . ALA A 1 110 ? -4.422  -13.776 45.828  1.00 69.57  ? 154 ALA A O   1 
ATOM   897  C  CB  . ALA A 1 110 ? -2.970  -15.800 47.373  1.00 66.31  ? 154 ALA A CB  1 
ATOM   898  N  N   . ASP A 1 111 ? -2.393  -13.202 45.028  1.00 67.62  ? 155 ASP A N   1 
ATOM   899  C  CA  . ASP A 1 111 ? -2.771  -11.825 44.746  1.00 67.76  ? 155 ASP A CA  1 
ATOM   900  C  C   . ASP A 1 111 ? -3.831  -11.802 43.645  1.00 68.00  ? 155 ASP A C   1 
ATOM   901  O  O   . ASP A 1 111 ? -3.655  -12.422 42.598  1.00 68.93  ? 155 ASP A O   1 
ATOM   902  C  CB  . ASP A 1 111 ? -1.556  -10.974 44.367  1.00 69.38  ? 155 ASP A CB  1 
ATOM   903  C  CG  . ASP A 1 111 ? -1.877  -9.504  44.149  1.00 70.79  ? 155 ASP A CG  1 
ATOM   904  O  OD1 . ASP A 1 111 ? -2.463  -8.889  45.061  1.00 70.58  ? 155 ASP A OD1 1 
ATOM   905  O  OD2 . ASP A 1 111 ? -1.529  -8.983  43.072  1.00 72.91  ? 155 ASP A OD2 1 
ATOM   906  N  N   . ASP A 1 112 ? -4.932  -11.087 43.916  1.00 68.30  ? 156 ASP A N   1 
ATOM   907  C  CA  . ASP A 1 112 ? -6.033  -10.894 42.982  1.00 69.27  ? 156 ASP A CA  1 
ATOM   908  C  C   . ASP A 1 112 ? -6.749  -12.217 42.708  1.00 66.91  ? 156 ASP A C   1 
ATOM   909  O  O   . ASP A 1 112 ? -7.375  -12.369 41.661  1.00 67.21  ? 156 ASP A O   1 
ATOM   910  C  CB  . ASP A 1 112 ? -5.567  -10.229 41.680  1.00 72.90  ? 156 ASP A CB  1 
ATOM   911  C  CG  . ASP A 1 112 ? -4.977  -8.837  41.850  1.00 74.96  ? 156 ASP A CG  1 
ATOM   912  O  OD1 . ASP A 1 112 ? -4.912  -8.354  43.000  1.00 74.78  ? 156 ASP A OD1 1 
ATOM   913  O  OD2 . ASP A 1 112 ? -4.590  -8.241  40.825  1.00 77.31  ? 156 ASP A OD2 1 
ATOM   914  N  N   . LEU A 1 113 ? -6.685  -13.155 43.664  1.00 65.39  ? 157 LEU A N   1 
ATOM   915  C  CA  . LEU A 1 113 ? -7.336  -14.450 43.527  1.00 66.31  ? 157 LEU A CA  1 
ATOM   916  C  C   . LEU A 1 113 ? -8.338  -14.648 44.663  1.00 66.96  ? 157 LEU A C   1 
ATOM   917  O  O   . LEU A 1 113 ? -8.110  -14.202 45.787  1.00 64.47  ? 157 LEU A O   1 
ATOM   918  C  CB  . LEU A 1 113 ? -6.279  -15.560 43.534  1.00 65.78  ? 157 LEU A CB  1 
ATOM   919  C  CG  . LEU A 1 113 ? -5.382  -15.649 42.298  1.00 66.83  ? 157 LEU A CG  1 
ATOM   920  C  CD1 . LEU A 1 113 ? -4.489  -16.879 42.369  1.00 66.67  ? 157 LEU A CD1 1 
ATOM   921  C  CD2 . LEU A 1 113 ? -6.203  -15.668 41.015  1.00 67.98  ? 157 LEU A CD2 1 
ATOM   922  N  N   . THR A 1 114 ? -9.451  -15.320 44.337  1.00 69.20  ? 158 THR A N   1 
ATOM   923  C  CA  . THR A 1 114 ? -10.463 -15.714 45.304  1.00 69.88  ? 158 THR A CA  1 
ATOM   924  C  C   . THR A 1 114 ? -10.550 -17.237 45.318  1.00 70.78  ? 158 THR A C   1 
ATOM   925  O  O   . THR A 1 114 ? -10.331 -17.876 44.291  1.00 72.86  ? 158 THR A O   1 
ATOM   926  C  CB  . THR A 1 114 ? -11.827 -15.094 44.970  1.00 71.36  ? 158 THR A CB  1 
ATOM   927  O  OG1 . THR A 1 114 ? -11.663 -13.681 44.847  1.00 72.91  ? 158 THR A OG1 1 
ATOM   928  C  CG2 . THR A 1 114 ? -12.884 -15.394 46.010  1.00 71.18  ? 158 THR A CG2 1 
ATOM   929  N  N   . TRP A 1 115 ? -10.867 -17.807 46.485  1.00 70.78  ? 159 TRP A N   1 
ATOM   930  C  CA  . TRP A 1 115 ? -10.951 -19.251 46.630  1.00 71.99  ? 159 TRP A CA  1 
ATOM   931  C  C   . TRP A 1 115 ? -11.744 -19.615 47.884  1.00 73.75  ? 159 TRP A C   1 
ATOM   932  O  O   . TRP A 1 115 ? -11.688 -18.906 48.887  1.00 73.56  ? 159 TRP A O   1 
ATOM   933  C  CB  . TRP A 1 115 ? -9.548  -19.877 46.657  1.00 70.42  ? 159 TRP A CB  1 
ATOM   934  C  CG  . TRP A 1 115 ? -8.721  -19.488 47.845  1.00 68.78  ? 159 TRP A CG  1 
ATOM   935  C  CD1 . TRP A 1 115 ? -8.630  -20.160 49.030  1.00 69.14  ? 159 TRP A CD1 1 
ATOM   936  C  CD2 . TRP A 1 115 ? -7.835  -18.358 47.960  1.00 67.25  ? 159 TRP A CD2 1 
ATOM   937  N  NE1 . TRP A 1 115 ? -7.772  -19.517 49.880  1.00 67.65  ? 159 TRP A NE1 1 
ATOM   938  C  CE2 . TRP A 1 115 ? -7.267  -18.411 49.252  1.00 66.74  ? 159 TRP A CE2 1 
ATOM   939  C  CE3 . TRP A 1 115 ? -7.473  -17.307 47.109  1.00 66.68  ? 159 TRP A CE3 1 
ATOM   940  C  CZ2 . TRP A 1 115 ? -6.358  -17.456 49.706  1.00 65.70  ? 159 TRP A CZ2 1 
ATOM   941  C  CZ3 . TRP A 1 115 ? -6.576  -16.363 47.560  1.00 65.76  ? 159 TRP A CZ3 1 
ATOM   942  C  CH2 . TRP A 1 115 ? -6.028  -16.439 48.841  1.00 65.65  ? 159 TRP A CH2 1 
ATOM   943  N  N   . CYS A 1 116 ? -12.486 -20.727 47.800  1.00 76.63  ? 160 CYS A N   1 
ATOM   944  C  CA  . CYS A 1 116 ? -13.070 -21.376 48.964  1.00 78.72  ? 160 CYS A CA  1 
ATOM   945  C  C   . CYS A 1 116 ? -13.552 -22.772 48.572  1.00 81.66  ? 160 CYS A C   1 
ATOM   946  O  O   . CYS A 1 116 ? -13.621 -23.095 47.388  1.00 81.52  ? 160 CYS A O   1 
ATOM   947  C  CB  . CYS A 1 116 ? -14.219 -20.567 49.560  1.00 78.54  ? 160 CYS A CB  1 
ATOM   948  S  SG  . CYS A 1 116 ? -15.740 -20.613 48.576  1.00 79.48  ? 160 CYS A SG  1 
ATOM   949  N  N   . GLY A 1 117 ? -13.878 -23.587 49.583  1.00 84.58  ? 161 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 117 ? -14.329 -24.954 49.371  1.00 88.66  ? 161 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 117 ? -15.491 -25.319 50.291  1.00 91.41  ? 161 GLY A C   1 
ATOM   952  O  O   . GLY A 1 117 ? -15.662 -24.715 51.347  1.00 92.17  ? 161 GLY A O   1 
ATOM   953  N  N   . GLU A 1 118 ? -16.271 -26.325 49.878  1.00 95.22  ? 162 GLU A N   1 
ATOM   954  C  CA  . GLU A 1 118 ? -17.448 -26.760 50.614  1.00 98.21  ? 162 GLU A CA  1 
ATOM   955  C  C   . GLU A 1 118 ? -17.016 -27.663 51.766  1.00 100.32 ? 162 GLU A C   1 
ATOM   956  O  O   . GLU A 1 118 ? -15.910 -28.199 51.753  1.00 102.04 ? 162 GLU A O   1 
ATOM   957  C  CB  . GLU A 1 118 ? -18.416 -27.488 49.679  1.00 100.91 ? 162 GLU A CB  1 
ATOM   958  C  CG  . GLU A 1 118 ? -18.828 -26.667 48.468  1.00 100.60 ? 162 GLU A CG  1 
ATOM   959  C  CD  . GLU A 1 118 ? -19.713 -27.390 47.466  1.00 103.94 ? 162 GLU A CD  1 
ATOM   960  O  OE1 . GLU A 1 118 ? -20.139 -28.525 47.761  1.00 106.86 ? 162 GLU A OE1 1 
ATOM   961  O  OE2 . GLU A 1 118 ? -19.963 -26.820 46.386  1.00 103.95 ? 162 GLU A OE2 1 
ATOM   962  N  N   . PHE A 1 119 ? -17.905 -27.830 52.755  1.00 102.19 ? 163 PHE A N   1 
ATOM   963  C  CA  . PHE A 1 119 ? -17.598 -28.606 53.947  1.00 104.94 ? 163 PHE A CA  1 
ATOM   964  C  C   . PHE A 1 119 ? -17.650 -30.100 53.633  1.00 109.08 ? 163 PHE A C   1 
ATOM   965  O  O   . PHE A 1 119 ? -16.666 -30.811 53.831  1.00 110.28 ? 163 PHE A O   1 
ATOM   966  C  CB  . PHE A 1 119 ? -18.568 -28.286 55.088  1.00 105.52 ? 163 PHE A CB  1 
ATOM   967  C  CG  . PHE A 1 119 ? -18.292 -29.050 56.360  1.00 107.35 ? 163 PHE A CG  1 
ATOM   968  C  CD1 . PHE A 1 119 ? -17.364 -28.588 57.282  1.00 106.08 ? 163 PHE A CD1 1 
ATOM   969  C  CD2 . PHE A 1 119 ? -18.922 -30.261 56.612  1.00 110.59 ? 163 PHE A CD2 1 
ATOM   970  C  CE1 . PHE A 1 119 ? -17.100 -29.301 58.442  1.00 108.51 ? 163 PHE A CE1 1 
ATOM   971  C  CE2 . PHE A 1 119 ? -18.650 -30.976 57.768  1.00 112.75 ? 163 PHE A CE2 1 
ATOM   972  C  CZ  . PHE A 1 119 ? -17.742 -30.495 58.683  1.00 111.51 ? 163 PHE A CZ  1 
ATOM   973  N  N   . ALA A 1 120 ? -18.815 -30.561 53.159  1.00 110.89 ? 164 ALA A N   1 
ATOM   974  C  CA  . ALA A 1 120 ? -19.075 -31.979 52.965  1.00 114.70 ? 164 ALA A CA  1 
ATOM   975  C  C   . ALA A 1 120 ? -18.116 -32.557 51.926  1.00 115.27 ? 164 ALA A C   1 
ATOM   976  O  O   . ALA A 1 120 ? -17.377 -33.495 52.217  1.00 117.47 ? 164 ALA A O   1 
ATOM   977  C  CB  . ALA A 1 120 ? -20.515 -32.185 52.559  1.00 116.58 ? 164 ALA A CB  1 
ATOM   978  N  N   . THR A 1 121 ? -18.136 -31.979 50.719  1.00 113.08 ? 165 THR A N   1 
ATOM   979  C  CA  . THR A 1 121 ? -17.316 -32.455 49.617  1.00 112.04 ? 165 THR A CA  1 
ATOM   980  C  C   . THR A 1 121 ? -15.887 -31.941 49.771  1.00 108.06 ? 165 THR A C   1 
ATOM   981  O  O   . THR A 1 121 ? -15.620 -31.060 50.586  1.00 103.49 ? 165 THR A O   1 
ATOM   982  C  CB  . THR A 1 121 ? -17.907 -32.030 48.266  1.00 111.55 ? 165 THR A CB  1 
ATOM   983  O  OG1 . THR A 1 121 ? -17.918 -30.603 48.207  1.00 106.59 ? 165 THR A OG1 1 
ATOM   984  C  CG2 . THR A 1 121 ? -19.308 -32.558 48.042  1.00 114.80 ? 165 THR A CG2 1 
ATOM   985  N  N   . SER A 1 122 ? -14.980 -32.513 48.970  1.00 109.04 ? 166 SER A N   1 
ATOM   986  C  CA  . SER A 1 122 ? -13.607 -32.044 48.873  1.00 106.98 ? 166 SER A CA  1 
ATOM   987  C  C   . SER A 1 122 ? -13.398 -31.338 47.533  1.00 104.29 ? 166 SER A C   1 
ATOM   988  O  O   . SER A 1 122 ? -12.334 -31.456 46.927  1.00 104.38 ? 166 SER A O   1 
ATOM   989  C  CB  . SER A 1 122 ? -12.637 -33.186 49.058  1.00 109.83 ? 166 SER A CB  1 
ATOM   990  O  OG  . SER A 1 122 ? -12.783 -34.151 48.026  1.00 113.28 ? 166 SER A OG  1 
ATOM   991  N  N   . LYS A 1 123 ? -14.423 -30.596 47.092  1.00 102.21 ? 167 LYS A N   1 
ATOM   992  C  CA  . LYS A 1 123 ? -14.412 -29.922 45.804  1.00 100.29 ? 167 LYS A CA  1 
ATOM   993  C  C   . LYS A 1 123 ? -14.391 -28.412 46.022  1.00 95.68  ? 167 LYS A C   1 
ATOM   994  O  O   . LYS A 1 123 ? -14.956 -27.911 46.993  1.00 94.27  ? 167 LYS A O   1 
ATOM   995  C  CB  . LYS A 1 123 ? -15.635 -30.335 44.978  1.00 102.65 ? 167 LYS A CB  1 
ATOM   996  C  CG  . LYS A 1 123 ? -15.660 -31.795 44.546  1.00 107.15 ? 167 LYS A CG  1 
ATOM   997  C  CD  . LYS A 1 123 ? -16.894 -32.182 43.755  1.00 110.66 ? 167 LYS A CD  1 
ATOM   998  C  CE  . LYS A 1 123 ? -18.163 -32.177 44.583  1.00 111.76 ? 167 LYS A CE  1 
ATOM   999  N  NZ  . LYS A 1 123 ? -19.330 -32.653 43.803  1.00 115.08 ? 167 LYS A NZ  1 
ATOM   1000 N  N   . ILE A 1 124 ? -13.732 -27.701 45.098  1.00 92.60  ? 168 ILE A N   1 
ATOM   1001 C  CA  . ILE A 1 124 ? -13.632 -26.252 45.146  1.00 88.35  ? 168 ILE A CA  1 
ATOM   1002 C  C   . ILE A 1 124 ? -14.974 -25.659 44.719  1.00 86.56  ? 168 ILE A C   1 
ATOM   1003 O  O   . ILE A 1 124 ? -15.670 -26.230 43.881  1.00 88.76  ? 168 ILE A O   1 
ATOM   1004 C  CB  . ILE A 1 124 ? -12.462 -25.761 44.266  1.00 88.37  ? 168 ILE A CB  1 
ATOM   1005 C  CG1 . ILE A 1 124 ? -11.116 -26.291 44.770  1.00 88.91  ? 168 ILE A CG1 1 
ATOM   1006 C  CG2 . ILE A 1 124 ? -12.456 -24.242 44.150  1.00 86.36  ? 168 ILE A CG2 1 
ATOM   1007 C  CD1 . ILE A 1 124 ? -9.946  -25.972 43.866  1.00 88.77  ? 168 ILE A CD1 1 
ATOM   1008 N  N   . ASN A 1 125 ? -15.320 -24.511 45.316  1.00 81.82  ? 169 ASN A N   1 
ATOM   1009 C  CA  . ASN A 1 125 ? -16.578 -23.829 45.058  1.00 79.89  ? 169 ASN A CA  1 
ATOM   1010 C  C   . ASN A 1 125 ? -16.331 -22.704 44.054  1.00 77.17  ? 169 ASN A C   1 
ATOM   1011 O  O   . ASN A 1 125 ? -15.723 -21.692 44.395  1.00 73.86  ? 169 ASN A O   1 
ATOM   1012 C  CB  . ASN A 1 125 ? -17.191 -23.309 46.362  1.00 78.29  ? 169 ASN A CB  1 
ATOM   1013 C  CG  . ASN A 1 125 ? -18.571 -22.705 46.196  1.00 78.69  ? 169 ASN A CG  1 
ATOM   1014 O  OD1 . ASN A 1 125 ? -19.112 -22.656 45.094  1.00 79.69  ? 169 ASN A OD1 1 
ATOM   1015 N  ND2 . ASN A 1 125 ? -19.149 -22.240 47.291  1.00 78.42  ? 169 ASN A ND2 1 
ATOM   1016 N  N   . TYR A 1 126 ? -16.812 -22.892 42.819  1.00 78.22  ? 170 TYR A N   1 
ATOM   1017 C  CA  . TYR A 1 126 ? -16.635 -21.907 41.764  1.00 79.13  ? 170 TYR A CA  1 
ATOM   1018 C  C   . TYR A 1 126 ? -17.879 -21.032 41.619  1.00 80.23  ? 170 TYR A C   1 
ATOM   1019 O  O   . TYR A 1 126 ? -17.862 -20.075 40.848  1.00 81.35  ? 170 TYR A O   1 
ATOM   1020 C  CB  . TYR A 1 126 ? -16.294 -22.590 40.435  1.00 81.50  ? 170 TYR A CB  1 
ATOM   1021 C  CG  . TYR A 1 126 ? -14.932 -23.237 40.397  1.00 81.12  ? 170 TYR A CG  1 
ATOM   1022 C  CD1 . TYR A 1 126 ? -14.715 -24.486 40.954  1.00 81.53  ? 170 TYR A CD1 1 
ATOM   1023 C  CD2 . TYR A 1 126 ? -13.848 -22.585 39.830  1.00 80.96  ? 170 TYR A CD2 1 
ATOM   1024 C  CE1 . TYR A 1 126 ? -13.464 -25.081 40.930  1.00 81.65  ? 170 TYR A CE1 1 
ATOM   1025 C  CE2 . TYR A 1 126 ? -12.589 -23.164 39.801  1.00 80.64  ? 170 TYR A CE2 1 
ATOM   1026 C  CZ  . TYR A 1 126 ? -12.395 -24.418 40.354  1.00 81.25  ? 170 TYR A CZ  1 
ATOM   1027 O  OH  . TYR A 1 126 ? -11.151 -25.002 40.329  1.00 81.78  ? 170 TYR A OH  1 
ATOM   1028 N  N   . GLN A 1 127 ? -18.949 -21.350 42.361  1.00 81.86  ? 171 GLN A N   1 
ATOM   1029 C  CA  . GLN A 1 127 ? -20.195 -20.607 42.257  1.00 83.13  ? 171 GLN A CA  1 
ATOM   1030 C  C   . GLN A 1 127 ? -20.075 -19.291 43.024  1.00 80.78  ? 171 GLN A C   1 
ATOM   1031 O  O   . GLN A 1 127 ? -20.295 -18.224 42.455  1.00 81.88  ? 171 GLN A O   1 
ATOM   1032 C  CB  . GLN A 1 127 ? -21.373 -21.429 42.784  1.00 85.70  ? 171 GLN A CB  1 
ATOM   1033 C  CG  . GLN A 1 127 ? -22.726 -20.876 42.354  1.00 89.41  ? 171 GLN A CG  1 
ATOM   1034 C  CD  . GLN A 1 127 ? -23.881 -21.408 43.168  1.00 92.57  ? 171 GLN A CD  1 
ATOM   1035 O  OE1 . GLN A 1 127 ? -23.702 -22.047 44.204  1.00 93.49  ? 171 GLN A OE1 1 
ATOM   1036 N  NE2 . GLN A 1 127 ? -25.090 -21.124 42.711  1.00 95.67  ? 171 GLN A NE2 1 
ATOM   1037 N  N   . SER A 1 128 ? -19.733 -19.379 44.316  1.00 78.51  ? 172 SER A N   1 
ATOM   1038 C  CA  . SER A 1 128 ? -19.635 -18.205 45.169  1.00 77.58  ? 172 SER A CA  1 
ATOM   1039 C  C   . SER A 1 128 ? -18.700 -18.474 46.346  1.00 76.18  ? 172 SER A C   1 
ATOM   1040 O  O   . SER A 1 128 ? -18.385 -19.624 46.646  1.00 75.70  ? 172 SER A O   1 
ATOM   1041 C  CB  . SER A 1 128 ? -21.001 -17.770 45.642  1.00 78.65  ? 172 SER A CB  1 
ATOM   1042 O  OG  . SER A 1 128 ? -21.622 -18.787 46.415  1.00 78.60  ? 172 SER A OG  1 
ATOM   1043 N  N   . CYS A 1 129 ? -18.251 -17.389 46.993  1.00 75.68  ? 173 CYS A N   1 
ATOM   1044 C  CA  . CYS A 1 129 ? -17.417 -17.466 48.182  1.00 74.49  ? 173 CYS A CA  1 
ATOM   1045 C  C   . CYS A 1 129 ? -17.836 -16.383 49.173  1.00 74.55  ? 173 CYS A C   1 
ATOM   1046 O  O   . CYS A 1 129 ? -18.382 -15.357 48.771  1.00 74.16  ? 173 CYS A O   1 
ATOM   1047 C  CB  . CYS A 1 129 ? -15.940 -17.300 47.844  1.00 73.48  ? 173 CYS A CB  1 
ATOM   1048 S  SG  . CYS A 1 129 ? -15.306 -18.587 46.740  1.00 75.46  ? 173 CYS A SG  1 
ATOM   1049 N  N   . PRO A 1 130 ? -17.587 -16.568 50.492  1.00 75.09  ? 174 PRO A N   1 
ATOM   1050 C  CA  . PRO A 1 130 ? -18.074 -15.634 51.507  1.00 76.05  ? 174 PRO A CA  1 
ATOM   1051 C  C   . PRO A 1 130 ? -17.412 -14.262 51.410  1.00 76.18  ? 174 PRO A C   1 
ATOM   1052 O  O   . PRO A 1 130 ? -16.187 -14.159 51.405  1.00 74.88  ? 174 PRO A O   1 
ATOM   1053 C  CB  . PRO A 1 130 ? -17.716 -16.295 52.851  1.00 75.66  ? 174 PRO A CB  1 
ATOM   1054 C  CG  . PRO A 1 130 ? -17.361 -17.727 52.503  1.00 75.32  ? 174 PRO A CG  1 
ATOM   1055 C  CD  . PRO A 1 130 ? -16.828 -17.679 51.087  1.00 74.61  ? 174 PRO A CD  1 
ATOM   1056 N  N   . ASP A 1 131 ? -18.248 -13.220 51.318  1.00 77.93  ? 175 ASP A N   1 
ATOM   1057 C  CA  . ASP A 1 131 ? -17.799 -11.843 51.429  1.00 78.14  ? 175 ASP A CA  1 
ATOM   1058 C  C   . ASP A 1 131 ? -17.389 -11.586 52.877  1.00 78.69  ? 175 ASP A C   1 
ATOM   1059 O  O   . ASP A 1 131 ? -18.030 -12.086 53.800  1.00 79.65  ? 175 ASP A O   1 
ATOM   1060 C  CB  . ASP A 1 131 ? -18.897 -10.880 50.968  1.00 79.55  ? 175 ASP A CB  1 
ATOM   1061 C  CG  . ASP A 1 131 ? -18.472 -9.424  50.876  1.00 80.13  ? 175 ASP A CG  1 
ATOM   1062 O  OD1 . ASP A 1 131 ? -17.264 -9.147  51.016  1.00 80.06  ? 175 ASP A OD1 1 
ATOM   1063 O  OD2 . ASP A 1 131 ? -19.358 -8.576  50.668  1.00 81.94  ? 175 ASP A OD2 1 
ATOM   1064 N  N   . TRP A 1 132 ? -16.317 -10.809 53.063  1.00 79.39  ? 176 TRP A N   1 
ATOM   1065 C  CA  . TRP A 1 132 ? -15.796 -10.507 54.387  1.00 81.14  ? 176 TRP A CA  1 
ATOM   1066 C  C   . TRP A 1 132 ? -16.863 -9.812  55.232  1.00 83.67  ? 176 TRP A C   1 
ATOM   1067 O  O   . TRP A 1 132 ? -17.098 -10.196 56.376  1.00 84.51  ? 176 TRP A O   1 
ATOM   1068 C  CB  . TRP A 1 132 ? -14.526 -9.652  54.286  1.00 82.63  ? 176 TRP A CB  1 
ATOM   1069 C  CG  . TRP A 1 132 ? -13.993 -9.210  55.615  1.00 85.29  ? 176 TRP A CG  1 
ATOM   1070 C  CD1 . TRP A 1 132 ? -13.292 -9.961  56.514  1.00 85.36  ? 176 TRP A CD1 1 
ATOM   1071 C  CD2 . TRP A 1 132 ? -14.155 -7.913  56.218  1.00 88.42  ? 176 TRP A CD2 1 
ATOM   1072 N  NE1 . TRP A 1 132 ? -12.990 -9.217  57.624  1.00 87.04  ? 176 TRP A NE1 1 
ATOM   1073 C  CE2 . TRP A 1 132 ? -13.509 -7.958  57.473  1.00 88.94  ? 176 TRP A CE2 1 
ATOM   1074 C  CE3 . TRP A 1 132 ? -14.774 -6.721  55.820  1.00 90.03  ? 176 TRP A CE3 1 
ATOM   1075 C  CZ2 . TRP A 1 132 ? -13.465 -6.856  58.326  1.00 91.22  ? 176 TRP A CZ2 1 
ATOM   1076 C  CZ3 . TRP A 1 132 ? -14.731 -5.634  56.665  1.00 92.63  ? 176 TRP A CZ3 1 
ATOM   1077 C  CH2 . TRP A 1 132 ? -14.084 -5.702  57.900  1.00 93.04  ? 176 TRP A CH2 1 
ATOM   1078 N  N   . ARG A 1 133 ? -17.499 -8.787  54.651  1.00 85.42  ? 177 ARG A N   1 
ATOM   1079 C  CA  . ARG A 1 133 ? -18.409 -7.921  55.383  1.00 87.34  ? 177 ARG A CA  1 
ATOM   1080 C  C   . ARG A 1 133 ? -19.796 -8.555  55.465  1.00 86.57  ? 177 ARG A C   1 
ATOM   1081 O  O   . ARG A 1 133 ? -20.354 -8.679  56.553  1.00 86.83  ? 177 ARG A O   1 
ATOM   1082 C  CB  . ARG A 1 133 ? -18.478 -6.543  54.717  1.00 90.24  ? 177 ARG A CB  1 
ATOM   1083 C  CG  . ARG A 1 133 ? -19.432 -5.573  55.401  1.00 95.70  ? 177 ARG A CG  1 
ATOM   1084 C  CD  . ARG A 1 133 ? -19.099 -4.115  55.141  1.00 99.44  ? 177 ARG A CD  1 
ATOM   1085 N  NE  . ARG A 1 133 ? -17.840 -3.719  55.765  1.00 99.97  ? 177 ARG A NE  1 
ATOM   1086 C  CZ  . ARG A 1 133 ? -17.732 -2.966  56.857  1.00 102.83 ? 177 ARG A CZ  1 
ATOM   1087 N  NH1 . ARG A 1 133 ? -18.814 -2.531  57.479  1.00 106.11 ? 177 ARG A NH1 1 
ATOM   1088 N  NH2 . ARG A 1 133 ? -16.536 -2.659  57.330  1.00 102.19 ? 177 ARG A NH2 1 
ATOM   1089 N  N   . LYS A 1 134 ? -20.339 -8.949  54.306  1.00 84.77  ? 178 LYS A N   1 
ATOM   1090 C  CA  . LYS A 1 134 ? -21.740 -9.324  54.197  1.00 85.49  ? 178 LYS A CA  1 
ATOM   1091 C  C   . LYS A 1 134 ? -21.977 -10.739 54.723  1.00 84.03  ? 178 LYS A C   1 
ATOM   1092 O  O   . LYS A 1 134 ? -23.014 -10.992 55.333  1.00 84.73  ? 178 LYS A O   1 
ATOM   1093 C  CB  . LYS A 1 134 ? -22.217 -9.184  52.747  1.00 85.83  ? 178 LYS A CB  1 
ATOM   1094 C  CG  . LYS A 1 134 ? -22.290 -7.750  52.237  1.00 88.22  ? 178 LYS A CG  1 
ATOM   1095 C  CD  . LYS A 1 134 ? -23.105 -7.583  50.971  1.00 90.49  ? 178 LYS A CD  1 
ATOM   1096 C  CE  . LYS A 1 134 ? -22.440 -8.167  49.743  1.00 89.35  ? 178 LYS A CE  1 
ATOM   1097 N  NZ  . LYS A 1 134 ? -23.291 -8.021  48.539  1.00 91.62  ? 178 LYS A NZ  1 
ATOM   1098 N  N   . ASP A 1 135 ? -21.027 -11.655 54.487  1.00 81.50  ? 179 ASP A N   1 
ATOM   1099 C  CA  . ASP A 1 135 ? -21.219 -13.057 54.827  1.00 81.00  ? 179 ASP A CA  1 
ATOM   1100 C  C   . ASP A 1 135 ? -20.434 -13.415 56.089  1.00 81.78  ? 179 ASP A C   1 
ATOM   1101 O  O   . ASP A 1 135 ? -21.019 -13.515 57.168  1.00 83.49  ? 179 ASP A O   1 
ATOM   1102 C  CB  . ASP A 1 135 ? -20.851 -13.970 53.654  1.00 78.59  ? 179 ASP A CB  1 
ATOM   1103 C  CG  . ASP A 1 135 ? -21.638 -13.683 52.388  1.00 78.79  ? 179 ASP A CG  1 
ATOM   1104 O  OD1 . ASP A 1 135 ? -22.870 -13.545 52.482  1.00 80.95  ? 179 ASP A OD1 1 
ATOM   1105 O  OD2 . ASP A 1 135 ? -21.010 -13.617 51.316  1.00 77.86  ? 179 ASP A OD2 1 
ATOM   1106 N  N   . CYS A 1 136 ? -19.115 -13.611 55.940  1.00 80.79  ? 180 CYS A N   1 
ATOM   1107 C  CA  . CYS A 1 136 ? -18.296 -14.255 56.957  1.00 80.67  ? 180 CYS A CA  1 
ATOM   1108 C  C   . CYS A 1 136 ? -16.897 -13.646 56.975  1.00 77.33  ? 180 CYS A C   1 
ATOM   1109 O  O   . CYS A 1 136 ? -16.248 -13.550 55.936  1.00 75.99  ? 180 CYS A O   1 
ATOM   1110 C  CB  . CYS A 1 136 ? -18.177 -15.751 56.694  1.00 81.76  ? 180 CYS A CB  1 
ATOM   1111 S  SG  . CYS A 1 136 ? -19.780 -16.571 56.493  1.00 87.50  ? 180 CYS A SG  1 
ATOM   1112 N  N   . SER A 1 137 ? -16.438 -13.269 58.173  1.00 76.50  ? 181 SER A N   1 
ATOM   1113 C  CA  . SER A 1 137 ? -15.148 -12.623 58.342  1.00 75.08  ? 181 SER A CA  1 
ATOM   1114 C  C   . SER A 1 137 ? -14.012 -13.638 58.220  1.00 72.48  ? 181 SER A C   1 
ATOM   1115 O  O   . SER A 1 137 ? -12.937 -13.303 57.726  1.00 72.54  ? 181 SER A O   1 
ATOM   1116 C  CB  . SER A 1 137 ? -15.088 -11.891 59.658  1.00 77.20  ? 181 SER A CB  1 
ATOM   1117 O  OG  . SER A 1 137 ? -15.382 -12.766 60.736  1.00 79.22  ? 181 SER A OG  1 
ATOM   1118 N  N   . ASN A 1 138 ? -14.262 -14.876 58.665  1.00 71.29  ? 182 ASN A N   1 
ATOM   1119 C  CA  . ASN A 1 138 ? -13.231 -15.900 58.735  1.00 69.57  ? 182 ASN A CA  1 
ATOM   1120 C  C   . ASN A 1 138 ? -13.306 -16.792 57.497  1.00 67.54  ? 182 ASN A C   1 
ATOM   1121 O  O   . ASN A 1 138 ? -13.517 -17.998 57.608  1.00 66.53  ? 182 ASN A O   1 
ATOM   1122 C  CB  . ASN A 1 138 ? -13.350 -16.716 60.025  1.00 71.12  ? 182 ASN A CB  1 
ATOM   1123 C  CG  . ASN A 1 138 ? -13.353 -15.853 61.269  1.00 72.31  ? 182 ASN A CG  1 
ATOM   1124 O  OD1 . ASN A 1 138 ? -12.411 -15.102 61.511  1.00 71.07  ? 182 ASN A OD1 1 
ATOM   1125 N  ND2 . ASN A 1 138 ? -14.405 -15.959 62.065  1.00 74.21  ? 182 ASN A ND2 1 
ATOM   1126 N  N   . ASN A 1 139 ? -13.102 -16.182 56.322  1.00 66.70  ? 183 ASN A N   1 
ATOM   1127 C  CA  . ASN A 1 139 ? -13.163 -16.889 55.051  1.00 65.58  ? 183 ASN A CA  1 
ATOM   1128 C  C   . ASN A 1 139 ? -11.742 -17.193 54.580  1.00 65.16  ? 183 ASN A C   1 
ATOM   1129 O  O   . ASN A 1 139 ? -10.803 -16.492 54.954  1.00 64.99  ? 183 ASN A O   1 
ATOM   1130 C  CB  . ASN A 1 139 ? -13.972 -16.124 53.996  1.00 64.55  ? 183 ASN A CB  1 
ATOM   1131 C  CG  . ASN A 1 139 ? -13.460 -14.725 53.720  1.00 63.89  ? 183 ASN A CG  1 
ATOM   1132 O  OD1 . ASN A 1 139 ? -12.725 -14.505 52.760  1.00 64.46  ? 183 ASN A OD1 1 
ATOM   1133 N  ND2 . ASN A 1 139 ? -13.839 -13.772 54.556  1.00 64.11  ? 183 ASN A ND2 1 
ATOM   1134 N  N   . PRO A 1 140 ? -11.539 -18.252 53.758  1.00 65.90  ? 184 PRO A N   1 
ATOM   1135 C  CA  . PRO A 1 140 ? -10.205 -18.641 53.292  1.00 65.32  ? 184 PRO A CA  1 
ATOM   1136 C  C   . PRO A 1 140 ? -9.294  -17.492 52.859  1.00 63.75  ? 184 PRO A C   1 
ATOM   1137 O  O   . PRO A 1 140 ? -8.142  -17.428 53.284  1.00 64.20  ? 184 PRO A O   1 
ATOM   1138 C  CB  . PRO A 1 140 ? -10.528 -19.544 52.092  1.00 65.23  ? 184 PRO A CB  1 
ATOM   1139 C  CG  . PRO A 1 140 ? -11.820 -20.218 52.491  1.00 66.28  ? 184 PRO A CG  1 
ATOM   1140 C  CD  . PRO A 1 140 ? -12.587 -19.155 53.250  1.00 66.31  ? 184 PRO A CD  1 
ATOM   1141 N  N   . VAL A 1 141 ? -9.819  -16.589 52.022  1.00 62.40  ? 185 VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 141 ? -9.039  -15.479 51.495  1.00 61.08  ? 185 VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 141 ? -8.653  -14.549 52.644  1.00 61.26  ? 185 VAL A C   1 
ATOM   1144 O  O   . VAL A 1 141 ? -7.478  -14.223 52.804  1.00 59.97  ? 185 VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 141 ? -9.798  -14.721 50.387  1.00 60.35  ? 185 VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 141 ? -9.032  -13.495 49.911  1.00 59.76  ? 185 VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 141 ? -10.135 -15.624 49.210  1.00 60.07  ? 185 VAL A CG2 1 
ATOM   1148 N  N   . SER A 1 142 ? -9.652  -14.141 53.439  1.00 61.98  ? 186 SER A N   1 
ATOM   1149 C  CA  . SER A 1 142 ? -9.457  -13.199 54.533  1.00 62.23  ? 186 SER A CA  1 
ATOM   1150 C  C   . SER A 1 142 ? -8.475  -13.755 55.562  1.00 62.50  ? 186 SER A C   1 
ATOM   1151 O  O   . SER A 1 142 ? -7.586  -13.038 56.018  1.00 62.41  ? 186 SER A O   1 
ATOM   1152 C  CB  . SER A 1 142 ? -10.772 -12.843 55.182  1.00 62.99  ? 186 SER A CB  1 
ATOM   1153 O  OG  . SER A 1 142 ? -11.609 -12.132 54.282  1.00 63.35  ? 186 SER A OG  1 
ATOM   1154 N  N   . VAL A 1 143 ? -8.646  -15.034 55.919  1.00 62.70  ? 187 VAL A N   1 
ATOM   1155 C  CA  . VAL A 1 143 ? -7.836  -15.668 56.948  1.00 64.33  ? 187 VAL A CA  1 
ATOM   1156 C  C   . VAL A 1 143 ? -6.407  -15.847 56.434  1.00 64.20  ? 187 VAL A C   1 
ATOM   1157 O  O   . VAL A 1 143 ? -5.457  -15.761 57.210  1.00 64.44  ? 187 VAL A O   1 
ATOM   1158 C  CB  . VAL A 1 143 ? -8.455  -17.004 57.408  1.00 65.53  ? 187 VAL A CB  1 
ATOM   1159 C  CG1 . VAL A 1 143 ? -7.575  -17.719 58.426  1.00 67.08  ? 187 VAL A CG1 1 
ATOM   1160 C  CG2 . VAL A 1 143 ? -9.863  -16.812 57.957  1.00 66.36  ? 187 VAL A CG2 1 
ATOM   1161 N  N   . PHE A 1 144 ? -6.263  -16.092 55.125  1.00 63.75  ? 188 PHE A N   1 
ATOM   1162 C  CA  . PHE A 1 144 ? -4.953  -16.190 54.501  1.00 63.82  ? 188 PHE A CA  1 
ATOM   1163 C  C   . PHE A 1 144 ? -4.206  -14.864 54.629  1.00 63.83  ? 188 PHE A C   1 
ATOM   1164 O  O   . PHE A 1 144 ? -3.078  -14.833 55.116  1.00 63.96  ? 188 PHE A O   1 
ATOM   1165 C  CB  . PHE A 1 144 ? -5.077  -16.581 53.026  1.00 63.81  ? 188 PHE A CB  1 
ATOM   1166 C  CG  . PHE A 1 144 ? -3.791  -16.470 52.247  1.00 64.30  ? 188 PHE A CG  1 
ATOM   1167 C  CD1 . PHE A 1 144 ? -2.748  -17.357 52.468  1.00 65.88  ? 188 PHE A CD1 1 
ATOM   1168 C  CD2 . PHE A 1 144 ? -3.609  -15.458 51.317  1.00 64.19  ? 188 PHE A CD2 1 
ATOM   1169 C  CE1 . PHE A 1 144 ? -1.562  -17.248 51.758  1.00 66.26  ? 188 PHE A CE1 1 
ATOM   1170 C  CE2 . PHE A 1 144 ? -2.420  -15.347 50.612  1.00 64.51  ? 188 PHE A CE2 1 
ATOM   1171 C  CZ  . PHE A 1 144 ? -1.401  -16.243 50.832  1.00 65.39  ? 188 PHE A CZ  1 
ATOM   1172 N  N   . TRP A 1 145 ? -4.850  -13.778 54.184  1.00 64.27  ? 189 TRP A N   1 
ATOM   1173 C  CA  . TRP A 1 145 ? -4.221  -12.467 54.127  1.00 65.94  ? 189 TRP A CA  1 
ATOM   1174 C  C   . TRP A 1 145 ? -3.871  -11.966 55.526  1.00 68.60  ? 189 TRP A C   1 
ATOM   1175 O  O   . TRP A 1 145 ? -2.892  -11.243 55.690  1.00 70.91  ? 189 TRP A O   1 
ATOM   1176 C  CB  . TRP A 1 145 ? -5.107  -11.466 53.374  1.00 65.68  ? 189 TRP A CB  1 
ATOM   1177 C  CG  . TRP A 1 145 ? -5.106  -11.664 51.889  1.00 65.80  ? 189 TRP A CG  1 
ATOM   1178 C  CD1 . TRP A 1 145 ? -6.176  -11.966 51.096  1.00 65.79  ? 189 TRP A CD1 1 
ATOM   1179 C  CD2 . TRP A 1 145 ? -3.970  -11.579 51.009  1.00 65.46  ? 189 TRP A CD2 1 
ATOM   1180 N  NE1 . TRP A 1 145 ? -5.786  -12.074 49.788  1.00 65.81  ? 189 TRP A NE1 1 
ATOM   1181 C  CE2 . TRP A 1 145 ? -4.438  -11.842 49.704  1.00 65.73  ? 189 TRP A CE2 1 
ATOM   1182 C  CE3 . TRP A 1 145 ? -2.610  -11.306 51.194  1.00 66.19  ? 189 TRP A CE3 1 
ATOM   1183 C  CZ2 . TRP A 1 145 ? -3.592  -11.838 48.595  1.00 66.13  ? 189 TRP A CZ2 1 
ATOM   1184 C  CZ3 . TRP A 1 145 ? -1.774  -11.303 50.098  1.00 66.63  ? 189 TRP A CZ3 1 
ATOM   1185 C  CH2 . TRP A 1 145 ? -2.261  -11.566 48.817  1.00 66.15  ? 189 TRP A CH2 1 
ATOM   1186 N  N   . LYS A 1 146 ? -4.673  -12.350 56.527  1.00 70.52  ? 190 LYS A N   1 
ATOM   1187 C  CA  . LYS A 1 146 ? -4.415  -11.966 57.905  1.00 72.94  ? 190 LYS A CA  1 
ATOM   1188 C  C   . LYS A 1 146 ? -3.164  -12.677 58.420  1.00 74.48  ? 190 LYS A C   1 
ATOM   1189 O  O   . LYS A 1 146 ? -2.374  -12.083 59.152  1.00 76.60  ? 190 LYS A O   1 
ATOM   1190 C  CB  . LYS A 1 146 ? -5.638  -12.273 58.776  1.00 74.45  ? 190 LYS A CB  1 
ATOM   1191 C  CG  . LYS A 1 146 ? -5.490  -11.920 60.251  1.00 77.63  ? 190 LYS A CG  1 
ATOM   1192 C  CD  . LYS A 1 146 ? -6.808  -11.730 60.976  1.00 79.96  ? 190 LYS A CD  1 
ATOM   1193 C  CE  . LYS A 1 146 ? -7.535  -10.466 60.564  1.00 80.97  ? 190 LYS A CE  1 
ATOM   1194 N  NZ  . LYS A 1 146 ? -8.714  -10.201 61.423  1.00 83.44  ? 190 LYS A NZ  1 
ATOM   1195 N  N   . THR A 1 147 ? -2.986  -13.944 58.023  1.00 74.02  ? 191 THR A N   1 
ATOM   1196 C  CA  . THR A 1 147 ? -1.883  -14.761 58.505  1.00 75.88  ? 191 THR A CA  1 
ATOM   1197 C  C   . THR A 1 147 ? -0.560  -14.289 57.902  1.00 77.40  ? 191 THR A C   1 
ATOM   1198 O  O   . THR A 1 147 ? 0.431   -14.162 58.620  1.00 80.06  ? 191 THR A O   1 
ATOM   1199 C  CB  . THR A 1 147 ? -2.120  -16.245 58.196  1.00 75.28  ? 191 THR A CB  1 
ATOM   1200 O  OG1 . THR A 1 147 ? -3.442  -16.585 58.611  1.00 74.50  ? 191 THR A OG1 1 
ATOM   1201 C  CG2 . THR A 1 147 ? -1.124  -17.157 58.879  1.00 77.47  ? 191 THR A CG2 1 
ATOM   1202 N  N   . VAL A 1 148 ? -0.551  -14.044 56.584  1.00 76.12  ? 192 VAL A N   1 
ATOM   1203 C  CA  . VAL A 1 148 ? 0.663   -13.672 55.869  1.00 76.53  ? 192 VAL A CA  1 
ATOM   1204 C  C   . VAL A 1 148 ? 1.065   -12.240 56.220  1.00 77.74  ? 192 VAL A C   1 
ATOM   1205 O  O   . VAL A 1 148 ? 2.255   -11.945 56.315  1.00 79.31  ? 192 VAL A O   1 
ATOM   1206 C  CB  . VAL A 1 148 ? 0.519   -13.850 54.342  1.00 74.95  ? 192 VAL A CB  1 
ATOM   1207 C  CG1 . VAL A 1 148 ? 0.221   -15.295 53.972  1.00 74.82  ? 192 VAL A CG1 1 
ATOM   1208 C  CG2 . VAL A 1 148 ? -0.520  -12.916 53.738  1.00 73.78  ? 192 VAL A CG2 1 
ATOM   1209 N  N   . SER A 1 149 ? 0.074   -11.355 56.403  1.00 76.66  ? 193 SER A N   1 
ATOM   1210 C  CA  . SER A 1 149 ? 0.332   -9.960  56.731  1.00 76.99  ? 193 SER A CA  1 
ATOM   1211 C  C   . SER A 1 149 ? 0.873   -9.831  58.154  1.00 79.05  ? 193 SER A C   1 
ATOM   1212 O  O   . SER A 1 149 ? 1.574   -8.870  58.462  1.00 80.11  ? 193 SER A O   1 
ATOM   1213 C  CB  . SER A 1 149 ? -0.902  -9.117  56.544  1.00 75.88  ? 193 SER A CB  1 
ATOM   1214 O  OG  . SER A 1 149 ? -1.315  -9.121  55.186  1.00 73.78  ? 193 SER A OG  1 
ATOM   1215 N  N   . ARG A 1 150 ? 0.532   -10.799 59.015  1.00 79.21  ? 194 ARG A N   1 
ATOM   1216 C  CA  . ARG A 1 150 ? 1.038   -10.838 60.377  1.00 81.79  ? 194 ARG A CA  1 
ATOM   1217 C  C   . ARG A 1 150 ? 2.531   -11.168 60.368  1.00 80.72  ? 194 ARG A C   1 
ATOM   1218 O  O   . ARG A 1 150 ? 3.319   -10.463 60.993  1.00 82.34  ? 194 ARG A O   1 
ATOM   1219 C  CB  . ARG A 1 150 ? 0.244   -11.849 61.210  1.00 85.01  ? 194 ARG A CB  1 
ATOM   1220 C  CG  . ARG A 1 150 ? 0.580   -11.832 62.694  1.00 90.92  ? 194 ARG A CG  1 
ATOM   1221 C  CD  . ARG A 1 150 ? -0.389  -12.648 63.528  1.00 93.98  ? 194 ARG A CD  1 
ATOM   1222 N  NE  . ARG A 1 150 ? -0.349  -14.064 63.187  1.00 95.95  ? 194 ARG A NE  1 
ATOM   1223 C  CZ  . ARG A 1 150 ? -1.404  -14.797 62.839  1.00 96.38  ? 194 ARG A CZ  1 
ATOM   1224 N  NH1 . ARG A 1 150 ? -2.609  -14.255 62.782  1.00 95.87  ? 194 ARG A NH1 1 
ATOM   1225 N  NH2 . ARG A 1 150 ? -1.246  -16.078 62.552  1.00 97.30  ? 194 ARG A NH2 1 
ATOM   1226 N  N   A ARG A 1 151 ? 2.904   -12.239 59.656  0.48 89.79  ? 195 ARG A N   1 
ATOM   1227 N  N   B ARG A 1 151 ? 2.899   -12.239 59.653  0.52 89.90  ? 195 ARG A N   1 
ATOM   1228 C  CA  A ARG A 1 151 ? 4.285   -12.691 59.593  0.48 90.05  ? 195 ARG A CA  1 
ATOM   1229 C  CA  B ARG A 1 151 ? 4.277   -12.702 59.580  0.52 90.26  ? 195 ARG A CA  1 
ATOM   1230 C  C   A ARG A 1 151 ? 5.157   -11.653 58.888  0.48 88.84  ? 195 ARG A C   1 
ATOM   1231 C  C   B ARG A 1 151 ? 5.153   -11.659 58.887  0.52 88.95  ? 195 ARG A C   1 
ATOM   1232 O  O   A ARG A 1 151 ? 6.301   -11.436 59.284  0.48 88.54  ? 195 ARG A O   1 
ATOM   1233 O  O   B ARG A 1 151 ? 6.294   -11.443 59.290  0.52 88.61  ? 195 ARG A O   1 
ATOM   1234 C  CB  A ARG A 1 151 ? 4.378   -14.041 58.874  0.48 91.27  ? 195 ARG A CB  1 
ATOM   1235 C  CB  B ARG A 1 151 ? 4.350   -14.040 58.836  0.52 91.64  ? 195 ARG A CB  1 
ATOM   1236 C  CG  A ARG A 1 151 ? 3.785   -15.207 59.652  0.48 92.64  ? 195 ARG A CG  1 
ATOM   1237 C  CG  B ARG A 1 151 ? 3.690   -15.205 59.561  0.52 93.13  ? 195 ARG A CG  1 
ATOM   1238 C  CD  A ARG A 1 151 ? 4.014   -16.537 58.959  0.48 94.08  ? 195 ARG A CD  1 
ATOM   1239 C  CD  B ARG A 1 151 ? 4.480   -15.668 60.773  0.52 94.05  ? 195 ARG A CD  1 
ATOM   1240 N  NE  A ARG A 1 151 ? 5.427   -16.826 58.761  0.48 94.37  ? 195 ARG A NE  1 
ATOM   1241 N  NE  B ARG A 1 151 ? 3.907   -16.851 61.400  0.52 95.36  ? 195 ARG A NE  1 
ATOM   1242 C  CZ  A ARG A 1 151 ? 5.990   -17.062 57.581  0.48 94.35  ? 195 ARG A CZ  1 
ATOM   1243 C  CZ  B ARG A 1 151 ? 4.438   -17.485 62.441  0.52 96.43  ? 195 ARG A CZ  1 
ATOM   1244 N  NH1 A ARG A 1 151 ? 5.253   -17.061 56.484  0.48 93.69  ? 195 ARG A NH1 1 
ATOM   1245 N  NH1 B ARG A 1 151 ? 5.569   -17.057 62.972  0.52 95.95  ? 195 ARG A NH1 1 
ATOM   1246 N  NH2 A ARG A 1 151 ? 7.287   -17.303 57.502  0.48 95.39  ? 195 ARG A NH2 1 
ATOM   1247 N  NH2 B ARG A 1 151 ? 3.836   -18.548 62.946  0.52 98.33  ? 195 ARG A NH2 1 
ATOM   1248 N  N   . PHE A 1 152 ? 4.608   -11.024 57.840  1.00 87.98  ? 196 PHE A N   1 
ATOM   1249 C  CA  . PHE A 1 152 ? 5.334   -10.036 57.054  1.00 87.19  ? 196 PHE A CA  1 
ATOM   1250 C  C   . PHE A 1 152 ? 5.601   -8.778  57.880  1.00 86.55  ? 196 PHE A C   1 
ATOM   1251 O  O   . PHE A 1 152 ? 6.690   -8.212  57.804  1.00 86.40  ? 196 PHE A O   1 
ATOM   1252 C  CB  . PHE A 1 152 ? 4.551   -9.699  55.781  1.00 86.64  ? 196 PHE A CB  1 
ATOM   1253 C  CG  . PHE A 1 152 ? 5.287   -8.838  54.785  1.00 86.30  ? 196 PHE A CG  1 
ATOM   1254 C  CD1 . PHE A 1 152 ? 6.456   -9.285  54.187  1.00 87.47  ? 196 PHE A CD1 1 
ATOM   1255 C  CD2 . PHE A 1 152 ? 4.808   -7.584  54.435  1.00 85.60  ? 196 PHE A CD2 1 
ATOM   1256 C  CE1 . PHE A 1 152 ? 7.131   -8.495  53.267  1.00 87.37  ? 196 PHE A CE1 1 
ATOM   1257 C  CE2 . PHE A 1 152 ? 5.484   -6.796  53.515  1.00 85.62  ? 196 PHE A CE2 1 
ATOM   1258 C  CZ  . PHE A 1 152 ? 6.644   -7.252  52.934  1.00 86.28  ? 196 PHE A CZ  1 
ATOM   1259 N  N   . ALA A 1 153 ? 4.600   -8.350  58.663  1.00 86.38  ? 197 ALA A N   1 
ATOM   1260 C  CA  . ALA A 1 153 ? 4.695   -7.139  59.464  1.00 85.53  ? 197 ALA A CA  1 
ATOM   1261 C  C   . ALA A 1 153 ? 5.643   -7.344  60.645  1.00 87.30  ? 197 ALA A C   1 
ATOM   1262 O  O   . ALA A 1 153 ? 6.357   -6.420  61.031  1.00 88.20  ? 197 ALA A O   1 
ATOM   1263 C  CB  . ALA A 1 153 ? 3.322   -6.725  59.933  1.00 84.75  ? 197 ALA A CB  1 
ATOM   1264 N  N   . GLU A 1 154 ? 5.634   -8.555  61.219  1.00 89.29  ? 198 GLU A N   1 
ATOM   1265 C  CA  . GLU A 1 154 ? 6.519   -8.903  62.322  1.00 90.63  ? 198 GLU A CA  1 
ATOM   1266 C  C   . GLU A 1 154 ? 7.977   -8.874  61.867  1.00 91.91  ? 198 GLU A C   1 
ATOM   1267 O  O   . GLU A 1 154 ? 8.848   -8.443  62.620  1.00 92.97  ? 198 GLU A O   1 
ATOM   1268 C  CB  . GLU A 1 154 ? 6.172   -10.286 62.877  1.00 91.72  ? 198 GLU A CB  1 
ATOM   1269 C  CG  . GLU A 1 154 ? 4.902   -10.308 63.707  1.00 91.89  ? 198 GLU A CG  1 
ATOM   1270 C  CD  . GLU A 1 154 ? 4.454   -11.695 64.137  1.00 93.74  ? 198 GLU A CD  1 
ATOM   1271 O  OE1 . GLU A 1 154 ? 4.314   -12.569 63.258  1.00 94.57  ? 198 GLU A OE1 1 
ATOM   1272 O  OE2 . GLU A 1 154 ? 4.238   -11.894 65.348  1.00 95.08  ? 198 GLU A OE2 1 
ATOM   1273 N  N   . ALA A 1 155 ? 8.228   -9.325  60.631  1.00 92.28  ? 199 ALA A N   1 
ATOM   1274 C  CA  . ALA A 1 155 ? 9.579   -9.518  60.125  1.00 93.77  ? 199 ALA A CA  1 
ATOM   1275 C  C   . ALA A 1 155 ? 10.286  -8.184  59.878  1.00 93.52  ? 199 ALA A C   1 
ATOM   1276 O  O   . ALA A 1 155 ? 11.515  -8.147  59.847  1.00 95.24  ? 199 ALA A O   1 
ATOM   1277 C  CB  . ALA A 1 155 ? 9.530   -10.342 58.861  1.00 94.83  ? 199 ALA A CB  1 
ATOM   1278 N  N   . ALA A 1 156 ? 9.513   -7.102  59.701  1.00 91.51  ? 200 ALA A N   1 
ATOM   1279 C  CA  . ALA A 1 156 ? 10.050  -5.806  59.311  1.00 89.77  ? 200 ALA A CA  1 
ATOM   1280 C  C   . ALA A 1 156 ? 10.911  -5.213  60.426  1.00 89.67  ? 200 ALA A C   1 
ATOM   1281 O  O   . ALA A 1 156 ? 10.702  -5.507  61.602  1.00 89.97  ? 200 ALA A O   1 
ATOM   1282 C  CB  . ALA A 1 156 ? 8.919   -4.874  58.947  1.00 88.24  ? 200 ALA A CB  1 
ATOM   1283 N  N   . CYS A 1 157 ? 11.871  -4.364  60.031  1.00 89.57  ? 201 CYS A N   1 
ATOM   1284 C  CA  . CYS A 1 157 ? 12.786  -3.724  60.964  1.00 89.96  ? 201 CYS A CA  1 
ATOM   1285 C  C   . CYS A 1 157 ? 13.261  -2.382  60.412  1.00 89.06  ? 201 CYS A C   1 
ATOM   1286 O  O   . CYS A 1 157 ? 13.007  -2.057  59.253  1.00 87.00  ? 201 CYS A O   1 
ATOM   1287 C  CB  . CYS A 1 157 ? 13.999  -4.605  61.236  1.00 92.02  ? 201 CYS A CB  1 
ATOM   1288 S  SG  . CYS A 1 157 ? 15.214  -4.584  59.892  1.00 94.08  ? 201 CYS A SG  1 
ATOM   1289 N  N   . ASP A 1 158 ? 13.962  -1.624  61.267  1.00 89.93  ? 202 ASP A N   1 
ATOM   1290 C  CA  . ASP A 1 158 ? 14.549  -0.337  60.920  1.00 90.41  ? 202 ASP A CA  1 
ATOM   1291 C  C   . ASP A 1 158 ? 13.441  0.616   60.468  1.00 88.93  ? 202 ASP A C   1 
ATOM   1292 O  O   . ASP A 1 158 ? 12.540  0.917   61.247  1.00 87.97  ? 202 ASP A O   1 
ATOM   1293 C  CB  . ASP A 1 158 ? 15.689  -0.504  59.906  1.00 91.64  ? 202 ASP A CB  1 
ATOM   1294 C  CG  . ASP A 1 158 ? 16.846  -1.355  60.400  1.00 92.61  ? 202 ASP A CG  1 
ATOM   1295 O  OD1 . ASP A 1 158 ? 16.756  -1.879  61.529  1.00 92.92  ? 202 ASP A OD1 1 
ATOM   1296 O  OD2 . ASP A 1 158 ? 17.831  -1.488  59.649  1.00 93.82  ? 202 ASP A OD2 1 
ATOM   1297 N  N   . VAL A 1 159 ? 13.509  1.080   59.213  1.00 89.38  ? 203 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 159 ? 12.569  2.059   58.692  1.00 89.25  ? 203 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 159 ? 11.607  1.349   57.741  1.00 88.05  ? 203 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 159 ? 11.973  1.024   56.613  1.00 88.36  ? 203 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 159 ? 13.300  3.221   57.990  1.00 90.92  ? 203 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 159 ? 12.329  4.187   57.324  1.00 90.56  ? 203 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 159 ? 14.227  3.967   58.941  1.00 92.28  ? 203 VAL A CG2 1 
ATOM   1304 N  N   . VAL A 1 160 ? 10.381  1.109   58.221  1.00 86.47  ? 204 VAL A N   1 
ATOM   1305 C  CA  . VAL A 1 160 ? 9.317   0.558   57.397  1.00 85.32  ? 204 VAL A CA  1 
ATOM   1306 C  C   . VAL A 1 160 ? 8.604   1.722   56.715  1.00 85.34  ? 204 VAL A C   1 
ATOM   1307 O  O   . VAL A 1 160 ? 8.519   2.811   57.280  1.00 86.22  ? 204 VAL A O   1 
ATOM   1308 C  CB  . VAL A 1 160 ? 8.341   -0.293  58.233  1.00 84.33  ? 204 VAL A CB  1 
ATOM   1309 C  CG1 . VAL A 1 160 ? 7.293   -0.970  57.359  1.00 83.95  ? 204 VAL A CG1 1 
ATOM   1310 C  CG2 . VAL A 1 160 ? 9.074   -1.320  59.085  1.00 84.29  ? 204 VAL A CG2 1 
ATOM   1311 N  N   . HIS A 1 161 ? 8.104   1.485   55.497  1.00 85.03  ? 205 HIS A N   1 
ATOM   1312 C  CA  . HIS A 1 161 ? 7.384   2.502   54.747  1.00 85.79  ? 205 HIS A CA  1 
ATOM   1313 C  C   . HIS A 1 161 ? 5.936   2.061   54.560  1.00 84.42  ? 205 HIS A C   1 
ATOM   1314 O  O   . HIS A 1 161 ? 5.640   0.869   54.589  1.00 83.81  ? 205 HIS A O   1 
ATOM   1315 C  CB  . HIS A 1 161 ? 8.069   2.775   53.403  1.00 87.94  ? 205 HIS A CB  1 
ATOM   1316 C  CG  . HIS A 1 161 ? 9.460   3.303   53.530  1.00 90.25  ? 205 HIS A CG  1 
ATOM   1317 N  ND1 . HIS A 1 161 ? 9.788   4.614   53.258  1.00 92.25  ? 205 HIS A ND1 1 
ATOM   1318 C  CD2 . HIS A 1 161 ? 10.598  2.709   53.912  1.00 90.88  ? 205 HIS A CD2 1 
ATOM   1319 C  CE1 . HIS A 1 161 ? 11.086  4.792   53.462  1.00 93.22  ? 205 HIS A CE1 1 
ATOM   1320 N  NE2 . HIS A 1 161 ? 11.597  3.647   53.858  1.00 92.84  ? 205 HIS A NE2 1 
ATOM   1321 N  N   . VAL A 1 162 ? 5.045   3.044   54.377  1.00 84.16  ? 206 VAL A N   1 
ATOM   1322 C  CA  . VAL A 1 162 ? 3.648   2.784   54.065  1.00 83.88  ? 206 VAL A CA  1 
ATOM   1323 C  C   . VAL A 1 162 ? 3.179   3.827   53.054  1.00 85.07  ? 206 VAL A C   1 
ATOM   1324 O  O   . VAL A 1 162 ? 3.404   5.021   53.238  1.00 85.87  ? 206 VAL A O   1 
ATOM   1325 C  CB  . VAL A 1 162 ? 2.765   2.767   55.331  1.00 83.38  ? 206 VAL A CB  1 
ATOM   1326 C  CG1 . VAL A 1 162 ? 2.806   4.087   56.088  1.00 84.22  ? 206 VAL A CG1 1 
ATOM   1327 C  CG2 . VAL A 1 162 ? 1.328   2.374   55.016  1.00 83.51  ? 206 VAL A CG2 1 
ATOM   1328 N  N   . MET A 1 163 ? 2.530   3.351   51.985  1.00 86.12  ? 207 MET A N   1 
ATOM   1329 C  CA  . MET A 1 163 ? 2.057   4.205   50.909  1.00 88.76  ? 207 MET A CA  1 
ATOM   1330 C  C   . MET A 1 163 ? 0.536   4.320   51.003  1.00 89.83  ? 207 MET A C   1 
ATOM   1331 O  O   . MET A 1 163 ? -0.175  3.344   50.775  1.00 89.73  ? 207 MET A O   1 
ATOM   1332 C  CB  . MET A 1 163 ? 2.470   3.618   49.554  1.00 89.82  ? 207 MET A CB  1 
ATOM   1333 C  CG  . MET A 1 163 ? 1.888   4.346   48.353  1.00 92.15  ? 207 MET A CG  1 
ATOM   1334 S  SD  . MET A 1 163 ? 2.668   3.896   46.773  1.00 93.46  ? 207 MET A SD  1 
ATOM   1335 C  CE  . MET A 1 163 ? 4.408   3.982   47.190  1.00 92.46  ? 207 MET A CE  1 
ATOM   1336 N  N   . LEU A 1 164 ? 0.057   5.524   51.348  1.00 92.12  ? 208 LEU A N   1 
ATOM   1337 C  CA  . LEU A 1 164 ? -1.357  5.779   51.584  1.00 93.45  ? 208 LEU A CA  1 
ATOM   1338 C  C   . LEU A 1 164 ? -1.957  6.537   50.401  1.00 95.34  ? 208 LEU A C   1 
ATOM   1339 O  O   . LEU A 1 164 ? -1.232  7.029   49.538  1.00 95.76  ? 208 LEU A O   1 
ATOM   1340 C  CB  . LEU A 1 164 ? -1.503  6.588   52.878  1.00 94.11  ? 208 LEU A CB  1 
ATOM   1341 C  CG  . LEU A 1 164 ? -1.012  5.906   54.156  1.00 92.44  ? 208 LEU A CG  1 
ATOM   1342 C  CD1 . LEU A 1 164 ? -1.189  6.820   55.360  1.00 93.31  ? 208 LEU A CD1 1 
ATOM   1343 C  CD2 . LEU A 1 164 ? -1.734  4.587   54.386  1.00 91.65  ? 208 LEU A CD2 1 
ATOM   1344 N  N   . ASP A 1 165 ? -3.293  6.629   50.388  1.00 96.86  ? 209 ASP A N   1 
ATOM   1345 C  CA  . ASP A 1 165 ? -4.026  7.327   49.343  1.00 100.32 ? 209 ASP A CA  1 
ATOM   1346 C  C   . ASP A 1 165 ? -4.670  8.575   49.942  1.00 103.77 ? 209 ASP A C   1 
ATOM   1347 O  O   . ASP A 1 165 ? -5.526  8.474   50.819  1.00 104.32 ? 209 ASP A O   1 
ATOM   1348 C  CB  . ASP A 1 165 ? -5.083  6.418   48.709  1.00 100.58 ? 209 ASP A CB  1 
ATOM   1349 C  CG  . ASP A 1 165 ? -5.596  6.896   47.360  1.00 102.95 ? 209 ASP A CG  1 
ATOM   1350 O  OD1 . ASP A 1 165 ? -5.233  8.016   46.949  1.00 104.77 ? 209 ASP A OD1 1 
ATOM   1351 O  OD2 . ASP A 1 165 ? -6.349  6.135   46.725  1.00 103.56 ? 209 ASP A OD2 1 
ATOM   1352 N  N   . GLY A 1 166 ? -4.257  9.747   49.445  1.00 107.03 ? 210 GLY A N   1 
ATOM   1353 C  CA  . GLY A 1 166 ? -4.745  11.022  49.945  1.00 110.49 ? 210 GLY A CA  1 
ATOM   1354 C  C   . GLY A 1 166 ? -6.196  11.293  49.550  1.00 114.07 ? 210 GLY A C   1 
ATOM   1355 O  O   . GLY A 1 166 ? -6.945  11.886  50.323  1.00 115.40 ? 210 GLY A O   1 
ATOM   1356 N  N   . SER A 1 167 ? -6.580  10.848  48.347  1.00 116.16 ? 211 SER A N   1 
ATOM   1357 C  CA  . SER A 1 167 ? -7.867  11.192  47.762  1.00 120.47 ? 211 SER A CA  1 
ATOM   1358 C  C   . SER A 1 167 ? -9.002  10.413  48.424  1.00 121.35 ? 211 SER A C   1 
ATOM   1359 O  O   . SER A 1 167 ? -10.044 10.989  48.730  1.00 123.81 ? 211 SER A O   1 
ATOM   1360 C  CB  . SER A 1 167 ? -7.853  10.969  46.271  1.00 121.65 ? 211 SER A CB  1 
ATOM   1361 O  OG  . SER A 1 167 ? -7.613  9.604   45.965  1.00 119.80 ? 211 SER A OG  1 
ATOM   1362 N  N   . ARG A 1 168 ? -8.798  9.105   48.633  1.00 121.02 ? 212 ARG A N   1 
ATOM   1363 C  CA  . ARG A 1 168 ? -9.856  8.223   49.105  1.00 122.72 ? 212 ARG A CA  1 
ATOM   1364 C  C   . ARG A 1 168 ? -10.268 8.597   50.528  1.00 122.59 ? 212 ARG A C   1 
ATOM   1365 O  O   . ARG A 1 168 ? -9.738  8.050   51.493  1.00 120.19 ? 212 ARG A O   1 
ATOM   1366 C  CB  . ARG A 1 168 ? -9.414  6.756   49.043  1.00 121.30 ? 212 ARG A CB  1 
ATOM   1367 C  CG  . ARG A 1 168 ? -9.418  6.163   47.641  1.00 123.28 ? 212 ARG A CG  1 
ATOM   1368 C  CD  . ARG A 1 168 ? -9.017  4.699   47.624  1.00 121.67 ? 212 ARG A CD  1 
ATOM   1369 N  NE  . ARG A 1 168 ? -10.010 3.842   48.262  1.00 122.34 ? 212 ARG A NE  1 
ATOM   1370 C  CZ  . ARG A 1 168 ? -10.607 2.803   47.686  1.00 123.65 ? 212 ARG A CZ  1 
ATOM   1371 N  NH1 . ARG A 1 168 ? -10.344 2.490   46.429  1.00 124.37 ? 212 ARG A NH1 1 
ATOM   1372 N  NH2 . ARG A 1 168 ? -11.474 2.078   48.373  1.00 123.97 ? 212 ARG A NH2 1 
ATOM   1373 N  N   . SER A 1 169 ? -11.221 9.534   50.630  1.00 125.11 ? 213 SER A N   1 
ATOM   1374 C  CA  . SER A 1 169 ? -11.873 9.880   51.884  1.00 125.57 ? 213 SER A CA  1 
ATOM   1375 C  C   . SER A 1 169 ? -10.844 9.986   53.010  1.00 122.67 ? 213 SER A C   1 
ATOM   1376 O  O   . SER A 1 169 ? -9.857  10.709  52.875  1.00 122.33 ? 213 SER A O   1 
ATOM   1377 C  CB  . SER A 1 169 ? -12.972 8.888   52.189  1.00 125.64 ? 213 SER A CB  1 
ATOM   1378 O  OG  . SER A 1 169 ? -13.649 9.228   53.390  1.00 126.85 ? 213 SER A OG  1 
ATOM   1379 N  N   . LYS A 1 170 ? -11.089 9.278   54.122  1.00 120.23 ? 214 LYS A N   1 
ATOM   1380 C  CA  . LYS A 1 170 ? -10.134 9.184   55.215  1.00 116.82 ? 214 LYS A CA  1 
ATOM   1381 C  C   . LYS A 1 170 ? -8.896  8.431   54.730  1.00 112.96 ? 214 LYS A C   1 
ATOM   1382 O  O   . LYS A 1 170 ? -9.002  7.322   54.211  1.00 111.69 ? 214 LYS A O   1 
ATOM   1383 C  CB  . LYS A 1 170 ? -10.785 8.509   56.429  1.00 116.17 ? 214 LYS A CB  1 
ATOM   1384 C  CG  . LYS A 1 170 ? -11.217 7.061   56.232  1.00 114.40 ? 214 LYS A CG  1 
ATOM   1385 C  CD  . LYS A 1 170 ? -12.212 6.575   57.266  1.00 114.96 ? 214 LYS A CD  1 
ATOM   1386 C  CE  . LYS A 1 170 ? -11.677 6.616   58.682  1.00 113.91 ? 214 LYS A CE  1 
ATOM   1387 N  NZ  . LYS A 1 170 ? -12.658 6.072   59.650  1.00 114.82 ? 214 LYS A NZ  1 
ATOM   1388 N  N   . ILE A 1 171 ? -7.723  9.051   54.911  1.00 110.75 ? 215 ILE A N   1 
ATOM   1389 C  CA  . ILE A 1 171 ? -6.487  8.569   54.316  1.00 107.59 ? 215 ILE A CA  1 
ATOM   1390 C  C   . ILE A 1 171 ? -6.064  7.284   55.023  1.00 103.89 ? 215 ILE A C   1 
ATOM   1391 O  O   . ILE A 1 171 ? -5.935  6.240   54.387  1.00 102.93 ? 215 ILE A O   1 
ATOM   1392 C  CB  . ILE A 1 171 ? -5.393  9.656   54.368  1.00 108.44 ? 215 ILE A CB  1 
ATOM   1393 C  CG1 . ILE A 1 171 ? -5.831  10.931  53.637  1.00 111.70 ? 215 ILE A CG1 1 
ATOM   1394 C  CG2 . ILE A 1 171 ? -4.071  9.118   53.834  1.00 106.46 ? 215 ILE A CG2 1 
ATOM   1395 C  CD1 . ILE A 1 171 ? -4.857  12.083  53.752  1.00 112.86 ? 215 ILE A CD1 1 
ATOM   1396 N  N   . PHE A 1 172 ? -5.851  7.377   56.341  1.00 102.29 ? 216 PHE A N   1 
ATOM   1397 C  CA  . PHE A 1 172 ? -5.624  6.206   57.171  1.00 99.40  ? 216 PHE A CA  1 
ATOM   1398 C  C   . PHE A 1 172 ? -6.974  5.663   57.634  1.00 99.89  ? 216 PHE A C   1 
ATOM   1399 O  O   . PHE A 1 172 ? -7.869  6.433   57.977  1.00 103.03 ? 216 PHE A O   1 
ATOM   1400 C  CB  . PHE A 1 172 ? -4.727  6.546   58.364  1.00 98.34  ? 216 PHE A CB  1 
ATOM   1401 C  CG  . PHE A 1 172 ? -4.561  5.425   59.360  1.00 96.39  ? 216 PHE A CG  1 
ATOM   1402 C  CD1 . PHE A 1 172 ? -3.878  4.267   59.018  1.00 94.07  ? 216 PHE A CD1 1 
ATOM   1403 C  CD2 . PHE A 1 172 ? -5.104  5.517   60.633  1.00 97.41  ? 216 PHE A CD2 1 
ATOM   1404 C  CE1 . PHE A 1 172 ? -3.731  3.234   59.931  1.00 93.08  ? 216 PHE A CE1 1 
ATOM   1405 C  CE2 . PHE A 1 172 ? -4.956  4.483   61.545  1.00 96.28  ? 216 PHE A CE2 1 
ATOM   1406 C  CZ  . PHE A 1 172 ? -4.269  3.343   61.193  1.00 94.07  ? 216 PHE A CZ  1 
ATOM   1407 N  N   . ASP A 1 173 ? -7.101  4.331   57.634  1.00 97.23  ? 217 ASP A N   1 
ATOM   1408 C  CA  . ASP A 1 173 ? -8.323  3.660   58.045  1.00 96.75  ? 217 ASP A CA  1 
ATOM   1409 C  C   . ASP A 1 173 ? -7.950  2.532   59.002  1.00 95.03  ? 217 ASP A C   1 
ATOM   1410 O  O   . ASP A 1 173 ? -7.232  1.609   58.624  1.00 93.52  ? 217 ASP A O   1 
ATOM   1411 C  CB  . ASP A 1 173 ? -9.098  3.153   56.825  1.00 96.92  ? 217 ASP A CB  1 
ATOM   1412 C  CG  . ASP A 1 173 ? -10.493 2.630   57.126  1.00 97.88  ? 217 ASP A CG  1 
ATOM   1413 O  OD1 . ASP A 1 173 ? -10.889 2.642   58.308  1.00 97.92  ? 217 ASP A OD1 1 
ATOM   1414 O  OD2 . ASP A 1 173 ? -11.176 2.217   56.168  1.00 98.30  ? 217 ASP A OD2 1 
ATOM   1415 N  N   . LYS A 1 174 ? -8.440  2.625   60.244  1.00 96.12  ? 218 LYS A N   1 
ATOM   1416 C  CA  . LYS A 1 174 ? -8.131  1.653   61.281  1.00 95.56  ? 218 LYS A CA  1 
ATOM   1417 C  C   . LYS A 1 174 ? -8.808  0.316   60.977  1.00 95.46  ? 218 LYS A C   1 
ATOM   1418 O  O   . LYS A 1 174 ? -8.298  -0.734  61.363  1.00 94.44  ? 218 LYS A O   1 
ATOM   1419 C  CB  . LYS A 1 174 ? -8.549  2.176   62.661  1.00 97.55  ? 218 LYS A CB  1 
ATOM   1420 C  CG  . LYS A 1 174 ? -9.985  2.676   62.771  1.00 100.89 ? 218 LYS A CG  1 
ATOM   1421 C  CD  . LYS A 1 174 ? -10.486 2.813   64.195  1.00 102.84 ? 218 LYS A CD  1 
ATOM   1422 C  CE  . LYS A 1 174 ? -10.733 1.480   64.870  1.00 103.08 ? 218 LYS A CE  1 
ATOM   1423 N  NZ  . LYS A 1 174 ? -11.414 1.645   66.175  1.00 105.32 ? 218 LYS A NZ  1 
ATOM   1424 N  N   . ASP A 1 175 ? -9.949  0.363   60.274  1.00 97.03  ? 219 ASP A N   1 
ATOM   1425 C  CA  . ASP A 1 175 ? -10.736 -0.824  59.978  1.00 97.51  ? 219 ASP A CA  1 
ATOM   1426 C  C   . ASP A 1 175 ? -10.153 -1.586  58.787  1.00 95.64  ? 219 ASP A C   1 
ATOM   1427 O  O   . ASP A 1 175 ? -10.614 -2.683  58.476  1.00 96.56  ? 219 ASP A O   1 
ATOM   1428 C  CB  . ASP A 1 175 ? -12.201 -0.457  59.720  1.00 100.41 ? 219 ASP A CB  1 
ATOM   1429 C  CG  . ASP A 1 175 ? -12.928 0.100   60.933  1.00 102.39 ? 219 ASP A CG  1 
ATOM   1430 O  OD1 . ASP A 1 175 ? -12.315 0.148   62.019  1.00 100.99 ? 219 ASP A OD1 1 
ATOM   1431 O  OD2 . ASP A 1 175 ? -14.106 0.481   60.783  1.00 105.31 ? 219 ASP A OD2 1 
ATOM   1432 N  N   . SER A 1 176 ? -9.146  -1.005  58.122  1.00 93.50  ? 220 SER A N   1 
ATOM   1433 C  CA  . SER A 1 176 ? -8.477  -1.656  57.006  1.00 91.62  ? 220 SER A CA  1 
ATOM   1434 C  C   . SER A 1 176 ? -7.498  -2.710  57.521  1.00 89.52  ? 220 SER A C   1 
ATOM   1435 O  O   . SER A 1 176 ? -7.187  -2.744  58.711  1.00 89.28  ? 220 SER A O   1 
ATOM   1436 C  CB  . SER A 1 176 ? -7.785  -0.638  56.136  1.00 91.35  ? 220 SER A CB  1 
ATOM   1437 O  OG  . SER A 1 176 ? -6.592  -0.166  56.747  1.00 89.70  ? 220 SER A OG  1 
ATOM   1438 N  N   . THR A 1 177 ? -7.020  -3.565  56.605  1.00 87.94  ? 221 THR A N   1 
ATOM   1439 C  CA  . THR A 1 177 ? -6.077  -4.626  56.929  1.00 85.42  ? 221 THR A CA  1 
ATOM   1440 C  C   . THR A 1 177 ? -4.764  -4.043  57.447  1.00 84.04  ? 221 THR A C   1 
ATOM   1441 O  O   . THR A 1 177 ? -4.120  -4.643  58.304  1.00 83.99  ? 221 THR A O   1 
ATOM   1442 C  CB  . THR A 1 177 ? -5.781  -5.520  55.718  1.00 84.21  ? 221 THR A CB  1 
ATOM   1443 O  OG1 . THR A 1 177 ? -6.992  -5.726  54.991  1.00 85.89  ? 221 THR A OG1 1 
ATOM   1444 C  CG2 . THR A 1 177 ? -5.182  -6.853  56.112  1.00 83.53  ? 221 THR A CG2 1 
ATOM   1445 N  N   . PHE A 1 178 ? -4.366  -2.885  56.903  1.00 83.00  ? 222 PHE A N   1 
ATOM   1446 C  CA  . PHE A 1 178 ? -3.164  -2.199  57.347  1.00 81.34  ? 222 PHE A CA  1 
ATOM   1447 C  C   . PHE A 1 178 ? -3.349  -1.722  58.785  1.00 81.24  ? 222 PHE A C   1 
ATOM   1448 O  O   . PHE A 1 178 ? -2.514  -1.996  59.644  1.00 80.42  ? 222 PHE A O   1 
ATOM   1449 C  CB  . PHE A 1 178 ? -2.832  -1.017  56.431  1.00 81.40  ? 222 PHE A CB  1 
ATOM   1450 C  CG  . PHE A 1 178 ? -1.761  -0.102  56.970  1.00 80.73  ? 222 PHE A CG  1 
ATOM   1451 C  CD1 . PHE A 1 178 ? -0.463  -0.556  57.152  1.00 79.87  ? 222 PHE A CD1 1 
ATOM   1452 C  CD2 . PHE A 1 178 ? -2.055  1.206   57.326  1.00 81.21  ? 222 PHE A CD2 1 
ATOM   1453 C  CE1 . PHE A 1 178 ? 0.518   0.281   57.661  1.00 79.37  ? 222 PHE A CE1 1 
ATOM   1454 C  CE2 . PHE A 1 178 ? -1.071  2.042   57.835  1.00 80.93  ? 222 PHE A CE2 1 
ATOM   1455 C  CZ  . PHE A 1 178 ? 0.213   1.577   58.003  1.00 79.85  ? 222 PHE A CZ  1 
ATOM   1456 N  N   . GLY A 1 179 ? -4.457  -1.012  59.025  1.00 82.07  ? 223 GLY A N   1 
ATOM   1457 C  CA  . GLY A 1 179 ? -4.724  -0.387  60.309  1.00 82.70  ? 223 GLY A CA  1 
ATOM   1458 C  C   . GLY A 1 179 ? -4.917  -1.402  61.434  1.00 82.86  ? 223 GLY A C   1 
ATOM   1459 O  O   . GLY A 1 179 ? -4.523  -1.143  62.568  1.00 83.86  ? 223 GLY A O   1 
ATOM   1460 N  N   . SER A 1 180 ? -5.524  -2.550  61.110  1.00 83.15  ? 224 SER A N   1 
ATOM   1461 C  CA  . SER A 1 180 ? -5.884  -3.542  62.111  1.00 84.49  ? 224 SER A CA  1 
ATOM   1462 C  C   . SER A 1 180 ? -4.732  -4.519  62.347  1.00 84.37  ? 224 SER A C   1 
ATOM   1463 O  O   . SER A 1 180 ? -4.318  -4.720  63.488  1.00 84.81  ? 224 SER A O   1 
ATOM   1464 C  CB  . SER A 1 180 ? -7.150  -4.264  61.718  1.00 85.62  ? 224 SER A CB  1 
ATOM   1465 O  OG  . SER A 1 180 ? -7.021  -4.866  60.439  1.00 85.44  ? 224 SER A OG  1 
ATOM   1466 N  N   . VAL A 1 181 ? -4.220  -5.116  61.261  1.00 83.95  ? 225 VAL A N   1 
ATOM   1467 C  CA  . VAL A 1 181 ? -3.273  -6.217  61.355  1.00 82.91  ? 225 VAL A CA  1 
ATOM   1468 C  C   . VAL A 1 181 ? -1.844  -5.679  61.303  1.00 82.03  ? 225 VAL A C   1 
ATOM   1469 O  O   . VAL A 1 181 ? -1.092  -5.829  62.263  1.00 81.90  ? 225 VAL A O   1 
ATOM   1470 C  CB  . VAL A 1 181 ? -3.517  -7.262  60.247  1.00 82.54  ? 225 VAL A CB  1 
ATOM   1471 C  CG1 . VAL A 1 181 ? -2.613  -8.476  60.413  1.00 82.68  ? 225 VAL A CG1 1 
ATOM   1472 C  CG2 . VAL A 1 181 ? -4.977  -7.686  60.184  1.00 83.62  ? 225 VAL A CG2 1 
ATOM   1473 N  N   . GLU A 1 182 ? -1.484  -5.051  60.176  1.00 81.86  ? 226 GLU A N   1 
ATOM   1474 C  CA  . GLU A 1 182 ? -0.098  -4.732  59.864  1.00 82.17  ? 226 GLU A CA  1 
ATOM   1475 C  C   . GLU A 1 182 ? 0.505   -3.828  60.938  1.00 83.41  ? 226 GLU A C   1 
ATOM   1476 O  O   . GLU A 1 182 ? 1.602   -4.096  61.420  1.00 82.86  ? 226 GLU A O   1 
ATOM   1477 C  CB  . GLU A 1 182 ? 0.005   -4.073  58.487  1.00 81.94  ? 226 GLU A CB  1 
ATOM   1478 C  CG  . GLU A 1 182 ? -0.353  -5.002  57.339  1.00 82.39  ? 226 GLU A CG  1 
ATOM   1479 C  CD  . GLU A 1 182 ? -0.348  -4.359  55.962  1.00 82.16  ? 226 GLU A CD  1 
ATOM   1480 O  OE1 . GLU A 1 182 ? 0.663   -3.720  55.612  1.00 82.28  ? 226 GLU A OE1 1 
ATOM   1481 O  OE2 . GLU A 1 182 ? -1.350  -4.513  55.236  1.00 82.09  ? 226 GLU A OE2 1 
ATOM   1482 N  N   . VAL A 1 183 ? -0.225  -2.767  61.305  1.00 86.08  ? 227 VAL A N   1 
ATOM   1483 C  CA  . VAL A 1 183 ? 0.272   -1.745  62.215  1.00 87.83  ? 227 VAL A CA  1 
ATOM   1484 C  C   . VAL A 1 183 ? 0.517   -2.343  63.601  1.00 89.97  ? 227 VAL A C   1 
ATOM   1485 O  O   . VAL A 1 183 ? 1.483   -1.977  64.268  1.00 89.70  ? 227 VAL A O   1 
ATOM   1486 C  CB  . VAL A 1 183 ? -0.696  -0.546  62.285  1.00 88.17  ? 227 VAL A CB  1 
ATOM   1487 C  CG1 . VAL A 1 183 ? -0.361  0.403   63.428  1.00 88.76  ? 227 VAL A CG1 1 
ATOM   1488 C  CG2 . VAL A 1 183 ? -0.751  0.209   60.964  1.00 88.23  ? 227 VAL A CG2 1 
ATOM   1489 N  N   . HIS A 1 184 ? -0.362  -3.262  64.023  1.00 92.84  ? 228 HIS A N   1 
ATOM   1490 C  CA  . HIS A 1 184 ? -0.344  -3.792  65.378  1.00 95.51  ? 228 HIS A CA  1 
ATOM   1491 C  C   . HIS A 1 184 ? 0.724   -4.874  65.540  1.00 94.64  ? 228 HIS A C   1 
ATOM   1492 O  O   . HIS A 1 184 ? 1.041   -5.252  66.666  1.00 94.43  ? 228 HIS A O   1 
ATOM   1493 C  CB  . HIS A 1 184 ? -1.737  -4.299  65.771  1.00 98.58  ? 228 HIS A CB  1 
ATOM   1494 C  CG  . HIS A 1 184 ? -2.746  -3.210  65.934  1.00 101.93 ? 228 HIS A CG  1 
ATOM   1495 N  ND1 . HIS A 1 184 ? -3.494  -3.041  67.082  1.00 105.81 ? 228 HIS A ND1 1 
ATOM   1496 C  CD2 . HIS A 1 184 ? -3.129  -2.236  65.097  1.00 103.05 ? 228 HIS A CD2 1 
ATOM   1497 C  CE1 . HIS A 1 184 ? -4.297  -1.997  66.931  1.00 106.35 ? 228 HIS A CE1 1 
ATOM   1498 N  NE2 . HIS A 1 184 ? -4.092  -1.492  65.732  1.00 105.16 ? 228 HIS A NE2 1 
ATOM   1499 N  N   . ASN A 1 185 ? 1.274   -5.367  64.421  1.00 94.25  ? 229 ASN A N   1 
ATOM   1500 C  CA  . ASN A 1 185 ? 2.260   -6.436  64.448  1.00 94.37  ? 229 ASN A CA  1 
ATOM   1501 C  C   . ASN A 1 185 ? 3.667   -5.896  64.182  1.00 93.59  ? 229 ASN A C   1 
ATOM   1502 O  O   . ASN A 1 185 ? 4.616   -6.676  64.130  1.00 94.33  ? 229 ASN A O   1 
ATOM   1503 C  CB  . ASN A 1 185 ? 1.896   -7.546  63.458  1.00 94.50  ? 229 ASN A CB  1 
ATOM   1504 C  CG  . ASN A 1 185 ? 0.638   -8.291  63.850  1.00 95.49  ? 229 ASN A CG  1 
ATOM   1505 O  OD1 . ASN A 1 185 ? 0.565   -8.869  64.932  1.00 96.78  ? 229 ASN A OD1 1 
ATOM   1506 N  ND2 . ASN A 1 185 ? -0.358  -8.290  62.979  1.00 95.56  ? 229 ASN A ND2 1 
ATOM   1507 N  N   . LEU A 1 186 ? 3.804   -4.571  64.025  1.00 92.62  ? 230 LEU A N   1 
ATOM   1508 C  CA  . LEU A 1 186 ? 5.107   -3.939  63.877  1.00 92.44  ? 230 LEU A CA  1 
ATOM   1509 C  C   . LEU A 1 186 ? 5.834   -3.954  65.220  1.00 93.87  ? 230 LEU A C   1 
ATOM   1510 O  O   . LEU A 1 186 ? 5.577   -3.110  66.076  1.00 93.95  ? 230 LEU A O   1 
ATOM   1511 C  CB  . LEU A 1 186 ? 4.923   -2.504  63.372  1.00 91.80  ? 230 LEU A CB  1 
ATOM   1512 C  CG  . LEU A 1 186 ? 4.531   -2.358  61.902  1.00 91.15  ? 230 LEU A CG  1 
ATOM   1513 C  CD1 . LEU A 1 186 ? 4.098   -0.933  61.596  1.00 91.10  ? 230 LEU A CD1 1 
ATOM   1514 C  CD2 . LEU A 1 186 ? 5.673   -2.767  60.985  1.00 90.77  ? 230 LEU A CD2 1 
ATOM   1515 N  N   . GLN A 1 187 ? 6.752   -4.914  65.386  1.00 96.01  ? 231 GLN A N   1 
ATOM   1516 C  CA  . GLN A 1 187 ? 7.450   -5.110  66.647  1.00 97.90  ? 231 GLN A CA  1 
ATOM   1517 C  C   . GLN A 1 187 ? 8.457   -3.981  66.851  1.00 96.91  ? 231 GLN A C   1 
ATOM   1518 O  O   . GLN A 1 187 ? 9.327   -3.772  66.008  1.00 96.40  ? 231 GLN A O   1 
ATOM   1519 C  CB  . GLN A 1 187 ? 8.157   -6.467  66.666  1.00 100.60 ? 231 GLN A CB  1 
ATOM   1520 C  CG  . GLN A 1 187 ? 7.219   -7.650  66.477  1.00 102.00 ? 231 GLN A CG  1 
ATOM   1521 C  CD  . GLN A 1 187 ? 7.940   -8.969  66.613  1.00 105.44 ? 231 GLN A CD  1 
ATOM   1522 O  OE1 . GLN A 1 187 ? 8.095   -9.717  65.650  1.00 106.51 ? 231 GLN A OE1 1 
ATOM   1523 N  NE2 . GLN A 1 187 ? 8.398   -9.259  67.820  1.00 108.21 ? 231 GLN A NE2 1 
ATOM   1524 N  N   . PRO A 1 188 ? 8.382   -3.227  67.974  1.00 96.41  ? 232 PRO A N   1 
ATOM   1525 C  CA  . PRO A 1 188 ? 9.267   -2.080  68.193  1.00 96.85  ? 232 PRO A CA  1 
ATOM   1526 C  C   . PRO A 1 188 ? 10.721  -2.434  68.507  1.00 98.44  ? 232 PRO A C   1 
ATOM   1527 O  O   . PRO A 1 188 ? 11.585  -1.560  68.464  1.00 98.80  ? 232 PRO A O   1 
ATOM   1528 C  CB  . PRO A 1 188 ? 8.623   -1.353  69.384  1.00 96.94  ? 232 PRO A CB  1 
ATOM   1529 C  CG  . PRO A 1 188 ? 7.878   -2.435  70.137  1.00 97.24  ? 232 PRO A CG  1 
ATOM   1530 C  CD  . PRO A 1 188 ? 7.434   -3.428  69.082  1.00 96.21  ? 232 PRO A CD  1 
ATOM   1531 N  N   . GLU A 1 189 ? 10.982  -3.707  68.832  1.00 100.00 ? 233 GLU A N   1 
ATOM   1532 C  CA  . GLU A 1 189 ? 12.339  -4.189  69.040  1.00 102.14 ? 233 GLU A CA  1 
ATOM   1533 C  C   . GLU A 1 189 ? 13.148  -4.002  67.758  1.00 102.41 ? 233 GLU A C   1 
ATOM   1534 O  O   . GLU A 1 189 ? 14.277  -3.518  67.799  1.00 103.18 ? 233 GLU A O   1 
ATOM   1535 C  CB  . GLU A 1 189 ? 12.349  -5.665  69.454  1.00 103.28 ? 233 GLU A CB  1 
ATOM   1536 C  CG  . GLU A 1 189 ? 11.891  -5.923  70.881  1.00 104.70 ? 233 GLU A CG  1 
ATOM   1537 C  CD  . GLU A 1 189 ? 10.390  -6.054  71.078  1.00 103.65 ? 233 GLU A CD  1 
ATOM   1538 O  OE1 . GLU A 1 189 ? 9.658   -5.118  70.705  1.00 101.92 ? 233 GLU A OE1 1 
ATOM   1539 O  OE2 . GLU A 1 189 ? 9.955   -7.094  71.612  1.00 104.44 ? 233 GLU A OE2 1 
ATOM   1540 N  N   . LYS A 1 190 ? 12.547  -4.389  66.626  1.00 102.19 ? 234 LYS A N   1 
ATOM   1541 C  CA  . LYS A 1 190 ? 13.220  -4.378  65.337  1.00 102.85 ? 234 LYS A CA  1 
ATOM   1542 C  C   . LYS A 1 190 ? 12.872  -3.102  64.571  1.00 101.69 ? 234 LYS A C   1 
ATOM   1543 O  O   . LYS A 1 190 ? 13.758  -2.467  64.003  1.00 102.45 ? 234 LYS A O   1 
ATOM   1544 C  CB  . LYS A 1 190 ? 12.838  -5.634  64.548  1.00 103.25 ? 234 LYS A CB  1 
ATOM   1545 C  CG  . LYS A 1 190 ? 13.216  -6.947  65.222  1.00 105.63 ? 234 LYS A CG  1 
ATOM   1546 C  CD  . LYS A 1 190 ? 12.981  -8.176  64.369  1.00 105.62 ? 234 LYS A CD  1 
ATOM   1547 C  CE  . LYS A 1 190 ? 11.515  -8.439  64.092  1.00 103.73 ? 234 LYS A CE  1 
ATOM   1548 N  NZ  . LYS A 1 190 ? 11.323  -9.677  63.301  1.00 104.17 ? 234 LYS A NZ  1 
ATOM   1549 N  N   . VAL A 1 191 ? 11.582  -2.739  64.558  1.00 100.51 ? 235 VAL A N   1 
ATOM   1550 C  CA  . VAL A 1 191 ? 11.109  -1.579  63.817  1.00 99.10  ? 235 VAL A CA  1 
ATOM   1551 C  C   . VAL A 1 191 ? 11.450  -0.315  64.604  1.00 99.31  ? 235 VAL A C   1 
ATOM   1552 O  O   . VAL A 1 191 ? 11.206  -0.243  65.807  1.00 99.58  ? 235 VAL A O   1 
ATOM   1553 C  CB  . VAL A 1 191 ? 9.597   -1.662  63.525  1.00 98.25  ? 235 VAL A CB  1 
ATOM   1554 C  CG1 . VAL A 1 191 ? 9.098   -0.432  62.780  1.00 97.38  ? 235 VAL A CG1 1 
ATOM   1555 C  CG2 . VAL A 1 191 ? 9.234   -2.931  62.767  1.00 98.29  ? 235 VAL A CG2 1 
ATOM   1556 N  N   . GLN A 1 192 ? 12.002  0.680   63.896  1.00 98.90  ? 236 GLN A N   1 
ATOM   1557 C  CA  . GLN A 1 192 ? 12.436  1.934   64.490  1.00 98.63  ? 236 GLN A CA  1 
ATOM   1558 C  C   . GLN A 1 192 ? 11.486  3.062   64.090  1.00 96.28  ? 236 GLN A C   1 
ATOM   1559 O  O   . GLN A 1 192 ? 11.051  3.831   64.945  1.00 96.26  ? 236 GLN A O   1 
ATOM   1560 C  CB  . GLN A 1 192 ? 13.863  2.259   64.045  1.00 100.48 ? 236 GLN A CB  1 
ATOM   1561 C  CG  . GLN A 1 192 ? 14.386  3.585   64.582  1.00 102.65 ? 236 GLN A CG  1 
ATOM   1562 C  CD  . GLN A 1 192 ? 15.708  3.976   63.969  1.00 104.60 ? 236 GLN A CD  1 
ATOM   1563 O  OE1 . GLN A 1 192 ? 16.347  3.199   63.263  1.00 104.81 ? 236 GLN A OE1 1 
ATOM   1564 N  NE2 . GLN A 1 192 ? 16.131  5.200   64.242  1.00 106.57 ? 236 GLN A NE2 1 
ATOM   1565 N  N   . THR A 1 193 ? 11.201  3.167   62.785  1.00 93.83  ? 237 THR A N   1 
ATOM   1566 C  CA  . THR A 1 193 ? 10.429  4.272   62.237  1.00 92.51  ? 237 THR A CA  1 
ATOM   1567 C  C   . THR A 1 193 ? 9.394   3.741   61.247  1.00 90.43  ? 237 THR A C   1 
ATOM   1568 O  O   . THR A 1 193 ? 9.593   2.688   60.644  1.00 88.92  ? 237 THR A O   1 
ATOM   1569 C  CB  . THR A 1 193 ? 11.351  5.293   61.555  1.00 93.62  ? 237 THR A CB  1 
ATOM   1570 O  OG1 . THR A 1 193 ? 12.384  5.659   62.470  1.00 94.82  ? 237 THR A OG1 1 
ATOM   1571 C  CG2 . THR A 1 193 ? 10.623  6.537   61.092  1.00 94.25  ? 237 THR A CG2 1 
ATOM   1572 N  N   . LEU A 1 194 ? 8.289   4.484   61.098  1.00 90.17  ? 238 LEU A N   1 
ATOM   1573 C  CA  . LEU A 1 194 ? 7.309   4.233   60.053  1.00 89.62  ? 238 LEU A CA  1 
ATOM   1574 C  C   . LEU A 1 194 ? 7.037   5.534   59.299  1.00 90.64  ? 238 LEU A C   1 
ATOM   1575 O  O   . LEU A 1 194 ? 6.302   6.392   59.784  1.00 91.30  ? 238 LEU A O   1 
ATOM   1576 C  CB  . LEU A 1 194 ? 6.020   3.678   60.668  1.00 89.04  ? 238 LEU A CB  1 
ATOM   1577 C  CG  . LEU A 1 194 ? 4.914   3.344   59.665  1.00 88.56  ? 238 LEU A CG  1 
ATOM   1578 C  CD1 . LEU A 1 194 ? 5.235   2.063   58.908  1.00 87.54  ? 238 LEU A CD1 1 
ATOM   1579 C  CD2 . LEU A 1 194 ? 3.562   3.232   60.353  1.00 88.25  ? 238 LEU A CD2 1 
ATOM   1580 N  N   . GLU A 1 195 ? 7.635   5.660   58.108  1.00 91.23  ? 239 GLU A N   1 
ATOM   1581 C  CA  . GLU A 1 195 ? 7.442   6.822   57.257  1.00 92.91  ? 239 GLU A CA  1 
ATOM   1582 C  C   . GLU A 1 195 ? 6.213   6.598   56.380  1.00 91.87  ? 239 GLU A C   1 
ATOM   1583 O  O   . GLU A 1 195 ? 6.084   5.550   55.752  1.00 91.13  ? 239 GLU A O   1 
ATOM   1584 C  CB  . GLU A 1 195 ? 8.695   7.069   56.413  1.00 94.77  ? 239 GLU A CB  1 
ATOM   1585 C  CG  . GLU A 1 195 ? 8.589   8.275   55.498  1.00 97.24  ? 239 GLU A CG  1 
ATOM   1586 C  CD  . GLU A 1 195 ? 9.909   8.725   54.896  1.00 99.48  ? 239 GLU A CD  1 
ATOM   1587 O  OE1 . GLU A 1 195 ? 10.590  7.886   54.272  1.00 99.60  ? 239 GLU A OE1 1 
ATOM   1588 O  OE2 . GLU A 1 195 ? 10.250  9.915   55.047  1.00 101.97 ? 239 GLU A OE2 1 
ATOM   1589 N  N   . ALA A 1 196 ? 5.322   7.597   56.345  1.00 92.72  ? 240 ALA A N   1 
ATOM   1590 C  CA  . ALA A 1 196 ? 4.092   7.523   55.571  1.00 92.76  ? 240 ALA A CA  1 
ATOM   1591 C  C   . ALA A 1 196 ? 4.228   8.357   54.300  1.00 94.48  ? 240 ALA A C   1 
ATOM   1592 O  O   . ALA A 1 196 ? 4.612   9.523   54.361  1.00 96.89  ? 240 ALA A O   1 
ATOM   1593 C  CB  . ALA A 1 196 ? 2.932   7.994   56.412  1.00 93.01  ? 240 ALA A CB  1 
ATOM   1594 N  N   . TRP A 1 197 ? 3.911   7.740   53.154  1.00 93.74  ? 241 TRP A N   1 
ATOM   1595 C  CA  . TRP A 1 197 ? 3.886   8.423   51.870  1.00 95.35  ? 241 TRP A CA  1 
ATOM   1596 C  C   . TRP A 1 197 ? 2.435   8.640   51.447  1.00 96.27  ? 241 TRP A C   1 
ATOM   1597 O  O   . TRP A 1 197 ? 1.746   7.685   51.096  1.00 95.37  ? 241 TRP A O   1 
ATOM   1598 C  CB  . TRP A 1 197 ? 4.665   7.621   50.819  1.00 94.68  ? 241 TRP A CB  1 
ATOM   1599 C  CG  . TRP A 1 197 ? 6.143   7.542   51.061  1.00 94.73  ? 241 TRP A CG  1 
ATOM   1600 C  CD1 . TRP A 1 197 ? 6.878   8.270   51.953  1.00 95.42  ? 241 TRP A CD1 1 
ATOM   1601 C  CD2 . TRP A 1 197 ? 7.075   6.666   50.400  1.00 94.45  ? 241 TRP A CD2 1 
ATOM   1602 N  NE1 . TRP A 1 197 ? 8.198   7.913   51.886  1.00 95.41  ? 241 TRP A NE1 1 
ATOM   1603 C  CE2 . TRP A 1 197 ? 8.350   6.931   50.944  1.00 94.74  ? 241 TRP A CE2 1 
ATOM   1604 C  CE3 . TRP A 1 197 ? 6.959   5.689   49.405  1.00 93.89  ? 241 TRP A CE3 1 
ATOM   1605 C  CZ2 . TRP A 1 197 ? 9.494   6.253   50.523  1.00 94.67  ? 241 TRP A CZ2 1 
ATOM   1606 C  CZ3 . TRP A 1 197 ? 8.089   5.019   48.990  1.00 93.61  ? 241 TRP A CZ3 1 
ATOM   1607 C  CH2 . TRP A 1 197 ? 9.339   5.299   49.544  1.00 94.21  ? 241 TRP A CH2 1 
ATOM   1608 N  N   . VAL A 1 198 ? 1.984   9.900   51.492  1.00 98.54  ? 242 VAL A N   1 
ATOM   1609 C  CA  . VAL A 1 198 ? 0.613   10.248  51.153  1.00 100.29 ? 242 VAL A CA  1 
ATOM   1610 C  C   . VAL A 1 198 ? 0.571   10.691  49.692  1.00 102.88 ? 242 VAL A C   1 
ATOM   1611 O  O   . VAL A 1 198 ? 1.163   11.709  49.336  1.00 104.46 ? 242 VAL A O   1 
ATOM   1612 C  CB  . VAL A 1 198 ? 0.063   11.339  52.093  1.00 101.29 ? 242 VAL A CB  1 
ATOM   1613 C  CG1 . VAL A 1 198 ? -1.409  11.622  51.826  1.00 102.74 ? 242 VAL A CG1 1 
ATOM   1614 C  CG2 . VAL A 1 198 ? 0.283   10.986  53.558  1.00 99.32  ? 242 VAL A CG2 1 
ATOM   1615 N  N   . ILE A 1 199 ? -0.136  9.916   48.859  1.00 103.76 ? 243 ILE A N   1 
ATOM   1616 C  CA  . ILE A 1 199 ? -0.212  10.161  47.427  1.00 106.98 ? 243 ILE A CA  1 
ATOM   1617 C  C   . ILE A 1 199 ? -1.448  11.010  47.134  1.00 111.22 ? 243 ILE A C   1 
ATOM   1618 O  O   . ILE A 1 199 ? -2.520  10.758  47.680  1.00 111.31 ? 243 ILE A O   1 
ATOM   1619 C  CB  . ILE A 1 199 ? -0.209  8.830   46.643  1.00 105.36 ? 243 ILE A CB  1 
ATOM   1620 C  CG1 . ILE A 1 199 ? 1.202   8.245   46.527  1.00 103.59 ? 243 ILE A CG1 1 
ATOM   1621 C  CG2 . ILE A 1 199 ? -0.846  8.989   45.269  1.00 107.47 ? 243 ILE A CG2 1 
ATOM   1622 C  CD1 . ILE A 1 199 ? 1.893   8.004   47.847  1.00 101.52 ? 243 ILE A CD1 1 
ATOM   1623 N  N   . HIS A 1 200 ? -1.277  12.007  46.255  1.00 115.70 ? 244 HIS A N   1 
ATOM   1624 C  CA  . HIS A 1 200 ? -2.339  12.928  45.880  1.00 119.71 ? 244 HIS A CA  1 
ATOM   1625 C  C   . HIS A 1 200 ? -2.951  12.480  44.554  1.00 122.11 ? 244 HIS A C   1 
ATOM   1626 O  O   . HIS A 1 200 ? -2.438  11.570  43.906  1.00 120.21 ? 244 HIS A O   1 
ATOM   1627 C  CB  . HIS A 1 200 ? -1.797  14.361  45.805  1.00 122.61 ? 244 HIS A CB  1 
ATOM   1628 C  CG  . HIS A 1 200 ? -1.299  14.895  47.110  1.00 122.05 ? 244 HIS A CG  1 
ATOM   1629 N  ND1 . HIS A 1 200 ? -0.279  14.306  47.826  1.00 119.31 ? 244 HIS A ND1 1 
ATOM   1630 C  CD2 . HIS A 1 200 ? -1.679  15.963  47.823  1.00 124.09 ? 244 HIS A CD2 1 
ATOM   1631 C  CE1 . HIS A 1 200 ? -0.062  15.002  48.933  1.00 119.34 ? 244 HIS A CE1 1 
ATOM   1632 N  NE2 . HIS A 1 200 ? -0.901  16.014  48.951  1.00 122.25 ? 244 HIS A NE2 1 
ATOM   1633 N  N   . GLY A 1 201 ? -4.053  13.134  44.164  1.00 127.17 ? 245 GLY A N   1 
ATOM   1634 C  CA  . GLY A 1 201 ? -4.741  12.839  42.917  1.00 130.43 ? 245 GLY A CA  1 
ATOM   1635 C  C   . GLY A 1 201 ? -4.015  13.434  41.711  1.00 134.62 ? 245 GLY A C   1 
ATOM   1636 O  O   . GLY A 1 201 ? -2.809  13.247  41.558  1.00 134.32 ? 245 GLY A O   1 
ATOM   1637 N  N   . GLY A 1 202 ? -4.765  14.146  40.860  1.00 139.60 ? 246 GLY A N   1 
ATOM   1638 C  CA  . GLY A 1 202 ? -4.219  14.768  39.663  1.00 143.64 ? 246 GLY A CA  1 
ATOM   1639 C  C   . GLY A 1 202 ? -4.021  16.272  39.840  1.00 148.09 ? 246 GLY A C   1 
ATOM   1640 O  O   . GLY A 1 202 ? -4.646  17.066  39.140  1.00 152.22 ? 246 GLY A O   1 
ATOM   1641 N  N   . ARG A 1 203 ? -3.136  16.637  40.778  1.00 147.31 ? 247 ARG A N   1 
ATOM   1642 C  CA  . ARG A 1 203 ? -2.868  18.022  41.138  1.00 150.01 ? 247 ARG A CA  1 
ATOM   1643 C  C   . ARG A 1 203 ? -4.165  18.686  41.603  1.00 152.70 ? 247 ARG A C   1 
ATOM   1644 O  O   . ARG A 1 203 ? -4.481  19.802  41.196  1.00 156.21 ? 247 ARG A O   1 
ATOM   1645 C  CB  . ARG A 1 203 ? -2.222  18.768  39.963  1.00 153.45 ? 247 ARG A CB  1 
ATOM   1646 C  CG  . ARG A 1 203 ? -1.545  20.076  40.349  1.00 156.15 ? 247 ARG A CG  1 
ATOM   1647 C  CD  . ARG A 1 203 ? -1.066  20.866  39.144  1.00 160.45 ? 247 ARG A CD  1 
ATOM   1648 N  NE  . ARG A 1 203 ? -0.028  20.178  38.388  1.00 159.49 ? 247 ARG A NE  1 
ATOM   1649 C  CZ  . ARG A 1 203 ? 1.219   19.989  38.807  1.00 157.57 ? 247 ARG A CZ  1 
ATOM   1650 N  NH1 . ARG A 1 203 ? 1.605   20.451  39.983  1.00 156.68 ? 247 ARG A NH1 1 
ATOM   1651 N  NH2 . ARG A 1 203 ? 2.082   19.344  38.041  1.00 156.68 ? 247 ARG A NH2 1 
ATOM   1652 N  N   . GLU A 1 204 ? -4.907  17.981  42.466  1.00 150.88 ? 248 GLU A N   1 
ATOM   1653 C  CA  . GLU A 1 204 ? -6.155  18.484  43.019  1.00 153.01 ? 248 GLU A CA  1 
ATOM   1654 C  C   . GLU A 1 204 ? -5.858  19.220  44.323  1.00 153.11 ? 248 GLU A C   1 
ATOM   1655 O  O   . GLU A 1 204 ? -6.190  20.395  44.463  1.00 155.74 ? 248 GLU A O   1 
ATOM   1656 C  CB  . GLU A 1 204 ? -7.141  17.337  43.259  1.00 150.68 ? 248 GLU A CB  1 
ATOM   1657 C  CG  . GLU A 1 204 ? -7.534  16.578  42.001  1.00 150.90 ? 248 GLU A CG  1 
ATOM   1658 C  CD  . GLU A 1 204 ? -8.432  17.336  41.037  1.00 155.70 ? 248 GLU A CD  1 
ATOM   1659 O  OE1 . GLU A 1 204 ? -7.961  18.324  40.440  1.00 158.57 ? 248 GLU A OE1 1 
ATOM   1660 O  OE2 . GLU A 1 204 ? -9.603  16.935  40.884  1.00 156.47 ? 248 GLU A OE2 1 
ATOM   1661 N  N   . ASP A 1 205 ? -5.222  18.508  45.263  1.00 149.99 ? 249 ASP A N   1 
ATOM   1662 C  CA  . ASP A 1 205 ? -4.914  19.038  46.581  1.00 149.31 ? 249 ASP A CA  1 
ATOM   1663 C  C   . ASP A 1 205 ? -3.497  19.607  46.583  1.00 148.75 ? 249 ASP A C   1 
ATOM   1664 O  O   . ASP A 1 205 ? -2.529  18.862  46.440  1.00 145.72 ? 249 ASP A O   1 
ATOM   1665 C  CB  . ASP A 1 205 ? -5.056  17.959  47.658  1.00 145.43 ? 249 ASP A CB  1 
ATOM   1666 C  CG  . ASP A 1 205 ? -6.464  17.410  47.816  1.00 145.82 ? 249 ASP A CG  1 
ATOM   1667 O  OD1 . ASP A 1 205 ? -7.341  17.796  47.016  1.00 149.50 ? 249 ASP A OD1 1 
ATOM   1668 O  OD2 . ASP A 1 205 ? -6.673  16.601  48.742  1.00 143.01 ? 249 ASP A OD2 1 
ATOM   1669 N  N   . SER A 1 206 ? -3.396  20.933  46.746  1.00 151.12 ? 250 SER A N   1 
ATOM   1670 C  CA  . SER A 1 206 ? -2.122  21.602  46.962  1.00 150.27 ? 250 SER A CA  1 
ATOM   1671 C  C   . SER A 1 206 ? -1.844  21.741  48.460  1.00 147.85 ? 250 SER A C   1 
ATOM   1672 O  O   . SER A 1 206 ? -0.773  22.203  48.848  1.00 147.61 ? 250 SER A O   1 
ATOM   1673 C  CB  . SER A 1 206 ? -2.094  22.945  46.273  1.00 154.73 ? 250 SER A CB  1 
ATOM   1674 O  OG  . SER A 1 206 ? -3.139  23.783  46.742  1.00 157.50 ? 250 SER A OG  1 
ATOM   1675 N  N   . ARG A 1 207 ? -2.813  21.333  49.292  1.00 145.57 ? 251 ARG A N   1 
ATOM   1676 C  CA  . ARG A 1 207 ? -2.688  21.413  50.739  1.00 143.50 ? 251 ARG A CA  1 
ATOM   1677 C  C   . ARG A 1 207 ? -1.766  20.300  51.236  1.00 138.61 ? 251 ARG A C   1 
ATOM   1678 O  O   . ARG A 1 207 ? -1.410  19.396  50.482  1.00 136.37 ? 251 ARG A O   1 
ATOM   1679 C  CB  . ARG A 1 207 ? -4.070  21.305  51.395  1.00 143.68 ? 251 ARG A CB  1 
ATOM   1680 C  CG  . ARG A 1 207 ? -4.657  19.900  51.390  1.00 140.06 ? 251 ARG A CG  1 
ATOM   1681 C  CD  . ARG A 1 207 ? -6.115  19.851  51.805  1.00 141.15 ? 251 ARG A CD  1 
ATOM   1682 N  NE  . ARG A 1 207 ? -6.999  20.434  50.805  1.00 145.15 ? 251 ARG A NE  1 
ATOM   1683 C  CZ  . ARG A 1 207 ? -8.326  20.420  50.872  1.00 147.03 ? 251 ARG A CZ  1 
ATOM   1684 N  NH1 . ARG A 1 207 ? -8.934  19.835  51.889  1.00 145.30 ? 251 ARG A NH1 1 
ATOM   1685 N  NH2 . ARG A 1 207 ? -9.043  20.987  49.917  1.00 150.69 ? 251 ARG A NH2 1 
ATOM   1686 N  N   . ASP A 1 208 ? -1.401  20.382  52.520  1.00 137.29 ? 252 ASP A N   1 
ATOM   1687 C  CA  . ASP A 1 208 ? -0.589  19.370  53.175  1.00 133.36 ? 252 ASP A CA  1 
ATOM   1688 C  C   . ASP A 1 208 ? -1.519  18.347  53.825  1.00 131.39 ? 252 ASP A C   1 
ATOM   1689 O  O   . ASP A 1 208 ? -2.385  18.715  54.618  1.00 132.95 ? 252 ASP A O   1 
ATOM   1690 C  CB  . ASP A 1 208 ? 0.359   20.015  54.190  1.00 133.80 ? 252 ASP A CB  1 
ATOM   1691 C  CG  . ASP A 1 208 ? 1.378   19.067  54.799  1.00 130.30 ? 252 ASP A CG  1 
ATOM   1692 O  OD1 . ASP A 1 208 ? 1.293   17.853  54.529  1.00 128.08 ? 252 ASP A OD1 1 
ATOM   1693 O  OD2 . ASP A 1 208 ? 2.256   19.555  55.536  1.00 130.88 ? 252 ASP A OD2 1 
ATOM   1694 N  N   . LEU A 1 209 ? -1.318  17.065  53.490  1.00 128.33 ? 253 LEU A N   1 
ATOM   1695 C  CA  . LEU A 1 209 ? -2.196  15.990  53.929  1.00 125.50 ? 253 LEU A CA  1 
ATOM   1696 C  C   . LEU A 1 209 ? -1.596  15.252  55.126  1.00 122.49 ? 253 LEU A C   1 
ATOM   1697 O  O   . LEU A 1 209 ? -2.123  14.221  55.541  1.00 119.15 ? 253 LEU A O   1 
ATOM   1698 C  CB  . LEU A 1 209 ? -2.422  15.033  52.752  1.00 123.99 ? 253 LEU A CB  1 
ATOM   1699 C  CG  . LEU A 1 209 ? -3.130  15.629  51.534  1.00 126.72 ? 253 LEU A CG  1 
ATOM   1700 C  CD1 . LEU A 1 209 ? -3.331  14.575  50.456  1.00 125.32 ? 253 LEU A CD1 1 
ATOM   1701 C  CD2 . LEU A 1 209 ? -4.467  16.244  51.921  1.00 129.35 ? 253 LEU A CD2 1 
ATOM   1702 N  N   . CYS A 1 210 ? -0.500  15.787  55.682  1.00 123.55 ? 254 CYS A N   1 
ATOM   1703 C  CA  . CYS A 1 210 ? 0.133   15.214  56.860  1.00 122.62 ? 254 CYS A CA  1 
ATOM   1704 C  C   . CYS A 1 210 ? -0.553  15.707  58.134  1.00 124.36 ? 254 CYS A C   1 
ATOM   1705 O  O   . CYS A 1 210 ? -0.373  15.116  59.198  1.00 123.22 ? 254 CYS A O   1 
ATOM   1706 C  CB  . CYS A 1 210 ? 1.617   15.556  56.898  1.00 123.20 ? 254 CYS A CB  1 
ATOM   1707 S  SG  . CYS A 1 210 ? 2.535   14.915  55.473  1.00 123.34 ? 254 CYS A SG  1 
ATOM   1708 N  N   . GLN A 1 211 ? -1.334  16.791  58.015  1.00 127.17 ? 255 GLN A N   1 
ATOM   1709 C  CA  . GLN A 1 211 ? -2.090  17.343  59.131  1.00 128.40 ? 255 GLN A CA  1 
ATOM   1710 C  C   . GLN A 1 211 ? -3.491  16.732  59.183  1.00 126.89 ? 255 GLN A C   1 
ATOM   1711 O  O   . GLN A 1 211 ? -4.287  17.096  60.047  1.00 128.25 ? 255 GLN A O   1 
ATOM   1712 C  CB  . GLN A 1 211 ? -2.161  18.869  59.025  1.00 133.23 ? 255 GLN A CB  1 
ATOM   1713 C  CG  . GLN A 1 211 ? -0.967  19.588  59.643  1.00 134.63 ? 255 GLN A CG  1 
ATOM   1714 C  CD  . GLN A 1 211 ? 0.354   19.112  59.091  1.00 133.18 ? 255 GLN A CD  1 
ATOM   1715 O  OE1 . GLN A 1 211 ? 0.596   19.149  57.887  1.00 133.56 ? 255 GLN A OE1 1 
ATOM   1716 N  NE2 . GLN A 1 211 ? 1.223   18.649  59.977  1.00 131.76 ? 255 GLN A NE2 1 
ATOM   1717 N  N   . ASP A 1 212 ? -3.785  15.805  58.260  1.00 123.80 ? 256 ASP A N   1 
ATOM   1718 C  CA  . ASP A 1 212 ? -5.049  15.085  58.252  1.00 122.42 ? 256 ASP A CA  1 
ATOM   1719 C  C   . ASP A 1 212 ? -5.202  14.355  59.586  1.00 120.95 ? 256 ASP A C   1 
ATOM   1720 O  O   . ASP A 1 212 ? -4.255  13.725  60.053  1.00 118.89 ? 256 ASP A O   1 
ATOM   1721 C  CB  . ASP A 1 212 ? -5.112  14.127  57.057  1.00 119.61 ? 256 ASP A CB  1 
ATOM   1722 C  CG  . ASP A 1 212 ? -6.484  13.531  56.789  1.00 119.42 ? 256 ASP A CG  1 
ATOM   1723 O  OD1 . ASP A 1 212 ? -6.985  12.788  57.655  1.00 117.84 ? 256 ASP A OD1 1 
ATOM   1724 O  OD2 . ASP A 1 212 ? -7.037  13.807  55.707  1.00 120.65 ? 256 ASP A OD2 1 
ATOM   1725 N  N   . PRO A 1 213 ? -6.383  14.419  60.249  1.00 122.12 ? 257 PRO A N   1 
ATOM   1726 C  CA  . PRO A 1 213 ? -6.550  13.840  61.585  1.00 120.89 ? 257 PRO A CA  1 
ATOM   1727 C  C   . PRO A 1 213 ? -6.392  12.321  61.668  1.00 117.52 ? 257 PRO A C   1 
ATOM   1728 O  O   . PRO A 1 213 ? -6.114  11.794  62.744  1.00 117.28 ? 257 PRO A O   1 
ATOM   1729 C  CB  . PRO A 1 213 ? -7.977  14.255  61.986  1.00 123.58 ? 257 PRO A CB  1 
ATOM   1730 C  CG  . PRO A 1 213 ? -8.682  14.501  60.671  1.00 125.01 ? 257 PRO A CG  1 
ATOM   1731 C  CD  . PRO A 1 213 ? -7.611  15.070  59.765  1.00 124.97 ? 257 PRO A CD  1 
ATOM   1732 N  N   . THR A 1 214 ? -6.569  11.624  60.538  1.00 115.38 ? 258 THR A N   1 
ATOM   1733 C  CA  . THR A 1 214 ? -6.393  10.180  60.486  1.00 111.42 ? 258 THR A CA  1 
ATOM   1734 C  C   . THR A 1 214 ? -4.905  9.829   60.519  1.00 108.61 ? 258 THR A C   1 
ATOM   1735 O  O   . THR A 1 214 ? -4.537  8.762   61.006  1.00 106.13 ? 258 THR A O   1 
ATOM   1736 C  CB  . THR A 1 214 ? -7.100  9.578   59.263  1.00 110.70 ? 258 THR A CB  1 
ATOM   1737 O  OG1 . THR A 1 214 ? -6.566  10.187  58.087  1.00 111.34 ? 258 THR A OG1 1 
ATOM   1738 C  CG2 . THR A 1 214 ? -8.602  9.762   59.299  1.00 112.70 ? 258 THR A CG2 1 
ATOM   1739 N  N   . ILE A 1 215 ? -4.056  10.726  59.997  1.00 109.12 ? 259 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 215 ? -2.610  10.573  60.087  1.00 107.90 ? 259 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 215 ? -2.167  10.870  61.519  1.00 108.64 ? 259 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 215 ? -1.282  10.196  62.044  1.00 106.97 ? 259 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 215 ? -1.882  11.455  59.047  1.00 108.84 ? 259 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 215 ? -1.845  10.793  57.666  1.00 107.82 ? 259 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 215 ? -0.475  11.817  59.505  1.00 108.51 ? 259 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 215 ? -3.202  10.510  57.074  1.00 108.75 ? 259 ILE A CD1 1 
ATOM   1747 N  N   . LYS A 1 216 ? -2.782  11.885  62.141  1.00 111.09 ? 260 LYS A N   1 
ATOM   1748 C  CA  . LYS A 1 216 ? -2.491  12.238  63.523  1.00 111.48 ? 260 LYS A CA  1 
ATOM   1749 C  C   . LYS A 1 216 ? -2.881  11.086  64.447  1.00 109.16 ? 260 LYS A C   1 
ATOM   1750 O  O   . LYS A 1 216 ? -2.240  10.874  65.474  1.00 108.35 ? 260 LYS A O   1 
ATOM   1751 C  CB  . LYS A 1 216 ? -3.222  13.528  63.914  1.00 115.50 ? 260 LYS A CB  1 
ATOM   1752 C  CG  . LYS A 1 216 ? -2.759  14.784  63.187  1.00 118.34 ? 260 LYS A CG  1 
ATOM   1753 C  CD  . LYS A 1 216 ? -1.360  15.230  63.562  1.00 118.98 ? 260 LYS A CD  1 
ATOM   1754 C  CE  . LYS A 1 216 ? -0.846  16.358  62.692  1.00 121.29 ? 260 LYS A CE  1 
ATOM   1755 N  NZ  . LYS A 1 216 ? 0.518   16.781  63.089  1.00 121.63 ? 260 LYS A NZ  1 
ATOM   1756 N  N   . GLU A 1 217 ? -3.938  10.353  64.073  1.00 108.24 ? 261 GLU A N   1 
ATOM   1757 C  CA  . GLU A 1 217 ? -4.338  9.146   64.778  1.00 106.92 ? 261 GLU A CA  1 
ATOM   1758 C  C   . GLU A 1 217 ? -3.258  8.081   64.599  1.00 103.48 ? 261 GLU A C   1 
ATOM   1759 O  O   . GLU A 1 217 ? -2.770  7.523   65.579  1.00 102.33 ? 261 GLU A O   1 
ATOM   1760 C  CB  . GLU A 1 217 ? -5.689  8.649   64.258  1.00 108.16 ? 261 GLU A CB  1 
ATOM   1761 C  CG  . GLU A 1 217 ? -6.266  7.490   65.055  1.00 108.24 ? 261 GLU A CG  1 
ATOM   1762 C  CD  . GLU A 1 217 ? -7.502  6.848   64.448  1.00 109.23 ? 261 GLU A CD  1 
ATOM   1763 O  OE1 . GLU A 1 217 ? -8.055  5.924   65.079  1.00 110.03 ? 261 GLU A OE1 1 
ATOM   1764 O  OE2 . GLU A 1 217 ? -7.908  7.266   63.344  1.00 109.74 ? 261 GLU A OE2 1 
ATOM   1765 N  N   . LEU A 1 218 ? -2.895  7.816   63.336  1.00 101.03 ? 262 LEU A N   1 
ATOM   1766 C  CA  . LEU A 1 218 ? -1.859  6.850   63.000  1.00 97.99  ? 262 LEU A CA  1 
ATOM   1767 C  C   . LEU A 1 218 ? -0.575  7.180   63.759  1.00 97.73  ? 262 LEU A C   1 
ATOM   1768 O  O   . LEU A 1 218 ? 0.071   6.287   64.302  1.00 97.08  ? 262 LEU A O   1 
ATOM   1769 C  CB  . LEU A 1 218 ? -1.633  6.867   61.483  1.00 96.65  ? 262 LEU A CB  1 
ATOM   1770 C  CG  . LEU A 1 218 ? -0.411  6.100   60.978  1.00 94.28  ? 262 LEU A CG  1 
ATOM   1771 C  CD1 . LEU A 1 218 ? -0.505  4.625   61.334  1.00 92.95  ? 262 LEU A CD1 1 
ATOM   1772 C  CD2 . LEU A 1 218 ? -0.250  6.274   59.475  1.00 94.20  ? 262 LEU A CD2 1 
ATOM   1773 N  N   . GLU A 1 219 ? -0.221  8.470   63.786  1.00 98.82  ? 263 GLU A N   1 
ATOM   1774 C  CA  . GLU A 1 219 ? 0.934   8.947   64.529  1.00 99.22  ? 263 GLU A CA  1 
ATOM   1775 C  C   . GLU A 1 219 ? 0.808   8.531   65.993  1.00 99.25  ? 263 GLU A C   1 
ATOM   1776 O  O   . GLU A 1 219 ? 1.752   7.991   66.564  1.00 98.01  ? 263 GLU A O   1 
ATOM   1777 C  CB  . GLU A 1 219 ? 1.057   10.466  64.383  1.00 101.49 ? 263 GLU A CB  1 
ATOM   1778 C  CG  . GLU A 1 219 ? 2.277   11.057  65.067  1.00 102.14 ? 263 GLU A CG  1 
ATOM   1779 C  CD  . GLU A 1 219 ? 2.545   12.510  64.712  1.00 104.28 ? 263 GLU A CD  1 
ATOM   1780 O  OE1 . GLU A 1 219 ? 1.639   13.343  64.916  1.00 106.10 ? 263 GLU A OE1 1 
ATOM   1781 O  OE2 . GLU A 1 219 ? 3.659   12.804  64.233  1.00 103.64 ? 263 GLU A OE2 1 
ATOM   1782 N  N   . SER A 1 220 ? -0.372  8.774   66.580  1.00 100.44 ? 264 SER A N   1 
ATOM   1783 C  CA  . SER A 1 220 ? -0.627  8.484   67.983  1.00 101.19 ? 264 SER A CA  1 
ATOM   1784 C  C   . SER A 1 220 ? -0.558  6.981   68.253  1.00 99.38  ? 264 SER A C   1 
ATOM   1785 O  O   . SER A 1 220 ? -0.062  6.566   69.298  1.00 98.94  ? 264 SER A O   1 
ATOM   1786 C  CB  . SER A 1 220 ? -1.952  9.053   68.420  1.00 103.28 ? 264 SER A CB  1 
ATOM   1787 O  OG  . SER A 1 220 ? -1.976  10.463  68.257  1.00 105.86 ? 264 SER A OG  1 
ATOM   1788 N  N   . ILE A 1 221 ? -1.069  6.178   67.310  1.00 98.51  ? 265 ILE A N   1 
ATOM   1789 C  CA  . ILE A 1 221 ? -1.057  4.728   67.436  1.00 97.48  ? 265 ILE A CA  1 
ATOM   1790 C  C   . ILE A 1 221 ? 0.391   4.239   67.442  1.00 95.97  ? 265 ILE A C   1 
ATOM   1791 O  O   . ILE A 1 221 ? 0.783   3.485   68.329  1.00 95.66  ? 265 ILE A O   1 
ATOM   1792 C  CB  . ILE A 1 221 ? -1.887  4.067   66.314  1.00 97.16  ? 265 ILE A CB  1 
ATOM   1793 C  CG1 . ILE A 1 221 ? -3.377  4.398   66.445  1.00 99.16  ? 265 ILE A CG1 1 
ATOM   1794 C  CG2 . ILE A 1 221 ? -1.651  2.562   66.278  1.00 95.95  ? 265 ILE A CG2 1 
ATOM   1795 C  CD1 . ILE A 1 221 ? -4.215  3.970   65.259  1.00 98.90  ? 265 ILE A CD1 1 
ATOM   1796 N  N   . ILE A 1 222 ? 1.170   4.687   66.450  1.00 94.75  ? 266 ILE A N   1 
ATOM   1797 C  CA  . ILE A 1 222 ? 2.552   4.265   66.279  1.00 93.35  ? 266 ILE A CA  1 
ATOM   1798 C  C   . ILE A 1 222 ? 3.401   4.791   67.438  1.00 94.18  ? 266 ILE A C   1 
ATOM   1799 O  O   . ILE A 1 222 ? 4.307   4.099   67.898  1.00 93.57  ? 266 ILE A O   1 
ATOM   1800 C  CB  . ILE A 1 222 ? 3.091   4.728   64.908  1.00 92.66  ? 266 ILE A CB  1 
ATOM   1801 C  CG1 . ILE A 1 222 ? 2.345   4.061   63.748  1.00 91.97  ? 266 ILE A CG1 1 
ATOM   1802 C  CG2 . ILE A 1 222 ? 4.592   4.504   64.800  1.00 92.12  ? 266 ILE A CG2 1 
ATOM   1803 C  CD1 . ILE A 1 222 ? 2.649   2.588   63.578  1.00 91.56  ? 266 ILE A CD1 1 
ATOM   1804 N  N   . SER A 1 223 ? 3.098   6.010   67.902  1.00 95.22  ? 267 SER A N   1 
ATOM   1805 C  CA  . SER A 1 223 ? 3.847   6.643   68.978  1.00 96.58  ? 267 SER A CA  1 
ATOM   1806 C  C   . SER A 1 223 ? 3.688   5.872   70.288  1.00 96.96  ? 267 SER A C   1 
ATOM   1807 O  O   . SER A 1 223 ? 4.615   5.833   71.094  1.00 98.24  ? 267 SER A O   1 
ATOM   1808 C  CB  . SER A 1 223 ? 3.437   8.084   69.152  1.00 98.39  ? 267 SER A CB  1 
ATOM   1809 O  OG  . SER A 1 223 ? 3.809   8.857   68.021  1.00 99.04  ? 267 SER A OG  1 
ATOM   1810 N  N   . LYS A 1 224 ? 2.512   5.261   70.492  1.00 96.08  ? 268 LYS A N   1 
ATOM   1811 C  CA  . LYS A 1 224 ? 2.220   4.544   71.723  1.00 96.11  ? 268 LYS A CA  1 
ATOM   1812 C  C   . LYS A 1 224 ? 2.881   3.165   71.706  1.00 94.35  ? 268 LYS A C   1 
ATOM   1813 O  O   . LYS A 1 224 ? 2.927   2.496   72.736  1.00 94.33  ? 268 LYS A O   1 
ATOM   1814 C  CB  . LYS A 1 224 ? 0.704   4.448   71.933  1.00 96.86  ? 268 LYS A CB  1 
ATOM   1815 C  CG  . LYS A 1 224 ? 0.276   3.946   73.306  1.00 98.74  ? 268 LYS A CG  1 
ATOM   1816 C  CD  . LYS A 1 224 ? -1.142  4.321   73.690  1.00 100.24 ? 268 LYS A CD  1 
ATOM   1817 C  CE  . LYS A 1 224 ? -2.193  3.698   72.797  1.00 99.39  ? 268 LYS A CE  1 
ATOM   1818 N  NZ  . LYS A 1 224 ? -3.563  3.982   73.288  1.00 100.84 ? 268 LYS A NZ  1 
ATOM   1819 N  N   . ARG A 1 225 ? 3.398   2.751   70.539  1.00 92.75  ? 269 ARG A N   1 
ATOM   1820 C  CA  . ARG A 1 225 ? 4.153   1.513   70.417  1.00 91.85  ? 269 ARG A CA  1 
ATOM   1821 C  C   . ARG A 1 225 ? 5.650   1.783   70.572  1.00 90.80  ? 269 ARG A C   1 
ATOM   1822 O  O   . ARG A 1 225 ? 6.453   0.863   70.442  1.00 89.25  ? 269 ARG A O   1 
ATOM   1823 C  CB  . ARG A 1 225 ? 3.869   0.841   69.069  1.00 91.22  ? 269 ARG A CB  1 
ATOM   1824 C  CG  . ARG A 1 225 ? 2.387   0.716   68.744  1.00 92.29  ? 269 ARG A CG  1 
ATOM   1825 C  CD  . ARG A 1 225 ? 2.062   -0.406  67.776  1.00 91.82  ? 269 ARG A CD  1 
ATOM   1826 N  NE  . ARG A 1 225 ? 2.347   -1.715  68.350  1.00 92.33  ? 269 ARG A NE  1 
ATOM   1827 C  CZ  . ARG A 1 225 ? 2.893   -2.732  67.691  1.00 92.06  ? 269 ARG A CZ  1 
ATOM   1828 N  NH1 . ARG A 1 225 ? 3.108   -2.643  66.390  1.00 91.13  ? 269 ARG A NH1 1 
ATOM   1829 N  NH2 . ARG A 1 225 ? 3.196   -3.848  68.332  1.00 93.26  ? 269 ARG A NH2 1 
ATOM   1830 N  N   . ASN A 1 226 ? 6.009   3.046   70.848  1.00 91.64  ? 270 ASN A N   1 
ATOM   1831 C  CA  . ASN A 1 226 ? 7.386   3.461   71.069  1.00 92.54  ? 270 ASN A CA  1 
ATOM   1832 C  C   . ASN A 1 226 ? 8.150   3.382   69.747  1.00 91.98  ? 270 ASN A C   1 
ATOM   1833 O  O   . ASN A 1 226 ? 9.279   2.895   69.697  1.00 92.16  ? 270 ASN A O   1 
ATOM   1834 C  CB  . ASN A 1 226 ? 8.046   2.655   72.194  1.00 93.29  ? 270 ASN A CB  1 
ATOM   1835 C  CG  . ASN A 1 226 ? 9.219   3.372   72.828  1.00 94.81  ? 270 ASN A CG  1 
ATOM   1836 O  OD1 . ASN A 1 226 ? 10.353  2.905   72.756  1.00 95.64  ? 270 ASN A OD1 1 
ATOM   1837 N  ND2 . ASN A 1 226 ? 8.956   4.507   73.454  1.00 96.22  ? 270 ASN A ND2 1 
ATOM   1838 N  N   . ILE A 1 227 ? 7.510   3.883   68.682  1.00 90.91  ? 271 ILE A N   1 
ATOM   1839 C  CA  . ILE A 1 227 ? 8.059   3.861   67.336  1.00 89.31  ? 271 ILE A CA  1 
ATOM   1840 C  C   . ILE A 1 227 ? 7.924   5.264   66.745  1.00 89.79  ? 271 ILE A C   1 
ATOM   1841 O  O   . ILE A 1 227 ? 6.935   5.951   66.994  1.00 90.21  ? 271 ILE A O   1 
ATOM   1842 C  CB  . ILE A 1 227 ? 7.348   2.791   66.478  1.00 87.80  ? 271 ILE A CB  1 
ATOM   1843 C  CG1 . ILE A 1 227 ? 7.605   1.377   67.006  1.00 87.49  ? 271 ILE A CG1 1 
ATOM   1844 C  CG2 . ILE A 1 227 ? 7.728   2.917   65.009  1.00 87.51  ? 271 ILE A CG2 1 
ATOM   1845 C  CD1 . ILE A 1 227 ? 6.859   0.291   66.260  1.00 86.18  ? 271 ILE A CD1 1 
ATOM   1846 N  N   . GLN A 1 228 ? 8.933   5.674   65.967  1.00 89.60  ? 272 GLN A N   1 
ATOM   1847 C  CA  . GLN A 1 228 ? 8.955   6.983   65.332  1.00 89.69  ? 272 GLN A CA  1 
ATOM   1848 C  C   . GLN A 1 228 ? 7.973   7.000   64.163  1.00 88.44  ? 272 GLN A C   1 
ATOM   1849 O  O   . GLN A 1 228 ? 7.734   5.970   63.536  1.00 87.64  ? 272 GLN A O   1 
ATOM   1850 C  CB  . GLN A 1 228 ? 10.371  7.302   64.850  1.00 90.33  ? 272 GLN A CB  1 
ATOM   1851 C  CG  . GLN A 1 228 ? 10.543  8.720   64.325  1.00 91.58  ? 272 GLN A CG  1 
ATOM   1852 C  CD  . GLN A 1 228 ? 11.994  9.058   64.087  1.00 92.51  ? 272 GLN A CD  1 
ATOM   1853 O  OE1 . GLN A 1 228 ? 12.720  8.319   63.426  1.00 92.08  ? 272 GLN A OE1 1 
ATOM   1854 N  NE2 . GLN A 1 228 ? 12.436  10.177  64.637  1.00 94.62  ? 272 GLN A NE2 1 
ATOM   1855 N  N   . PHE A 1 229 ? 7.419   8.184   63.874  1.00 89.08  ? 273 PHE A N   1 
ATOM   1856 C  CA  . PHE A 1 229 ? 6.502   8.353   62.759  1.00 88.76  ? 273 PHE A CA  1 
ATOM   1857 C  C   . PHE A 1 229 ? 6.922   9.556   61.918  1.00 90.50  ? 273 PHE A C   1 
ATOM   1858 O  O   . PHE A 1 229 ? 6.740   10.699  62.330  1.00 91.79  ? 273 PHE A O   1 
ATOM   1859 C  CB  . PHE A 1 229 ? 5.063   8.525   63.250  1.00 88.49  ? 273 PHE A CB  1 
ATOM   1860 C  CG  . PHE A 1 229 ? 4.063   8.756   62.145  1.00 88.33  ? 273 PHE A CG  1 
ATOM   1861 C  CD1 . PHE A 1 229 ? 3.759   7.748   61.242  1.00 86.88  ? 273 PHE A CD1 1 
ATOM   1862 C  CD2 . PHE A 1 229 ? 3.453   9.991   61.983  1.00 90.21  ? 273 PHE A CD2 1 
ATOM   1863 C  CE1 . PHE A 1 229 ? 2.848   7.963   60.219  1.00 87.10  ? 273 PHE A CE1 1 
ATOM   1864 C  CE2 . PHE A 1 229 ? 2.543   10.205  60.958  1.00 90.56  ? 273 PHE A CE2 1 
ATOM   1865 C  CZ  . PHE A 1 229 ? 2.243   9.191   60.078  1.00 88.94  ? 273 PHE A CZ  1 
ATOM   1866 N  N   . SER A 1 230 ? 7.488   9.273   60.739  1.00 90.93  ? 274 SER A N   1 
ATOM   1867 C  CA  . SER A 1 230 ? 7.712   10.281  59.716  1.00 93.43  ? 274 SER A CA  1 
ATOM   1868 C  C   . SER A 1 230 ? 6.494   10.338  58.797  1.00 93.88  ? 274 SER A C   1 
ATOM   1869 O  O   . SER A 1 230 ? 5.651   9.443   58.824  1.00 92.19  ? 274 SER A O   1 
ATOM   1870 C  CB  . SER A 1 230 ? 8.979   9.994   58.947  1.00 93.83  ? 274 SER A CB  1 
ATOM   1871 O  OG  . SER A 1 230 ? 9.195   10.968  57.937  1.00 95.46  ? 274 SER A OG  1 
ATOM   1872 N  N   . CYS A 1 231 ? 6.410   11.402  57.991  1.00 96.62  ? 275 CYS A N   1 
ATOM   1873 C  CA  . CYS A 1 231 ? 5.319   11.567  57.044  1.00 97.55  ? 275 CYS A CA  1 
ATOM   1874 C  C   . CYS A 1 231 ? 5.728   12.554  55.953  1.00 100.18 ? 275 CYS A C   1 
ATOM   1875 O  O   . CYS A 1 231 ? 6.213   13.642  56.255  1.00 102.51 ? 275 CYS A O   1 
ATOM   1876 C  CB  . CYS A 1 231 ? 4.054   12.051  57.742  1.00 98.38  ? 275 CYS A CB  1 
ATOM   1877 S  SG  . CYS A 1 231 ? 2.585   11.994  56.683  1.00 100.09 ? 275 CYS A SG  1 
ATOM   1878 N  N   . LYS A 1 232 ? 5.525   12.157  54.690  1.00 100.83 ? 276 LYS A N   1 
ATOM   1879 C  CA  . LYS A 1 232 ? 5.891   12.976  53.544  1.00 103.34 ? 276 LYS A CA  1 
ATOM   1880 C  C   . LYS A 1 232 ? 4.719   13.056  52.567  1.00 104.64 ? 276 LYS A C   1 
ATOM   1881 O  O   . LYS A 1 232 ? 3.840   12.196  52.569  1.00 103.22 ? 276 LYS A O   1 
ATOM   1882 C  CB  . LYS A 1 232 ? 7.124   12.401  52.840  1.00 102.45 ? 276 LYS A CB  1 
ATOM   1883 C  CG  . LYS A 1 232 ? 8.442   12.560  53.587  1.00 102.16 ? 276 LYS A CG  1 
ATOM   1884 C  CD  . LYS A 1 232 ? 9.649   12.067  52.808  1.00 102.07 ? 276 LYS A CD  1 
ATOM   1885 C  CE  . LYS A 1 232 ? 9.951   12.892  51.574  1.00 104.34 ? 276 LYS A CE  1 
ATOM   1886 N  NZ  . LYS A 1 232 ? 11.086  12.334  50.803  1.00 104.30 ? 276 LYS A NZ  1 
ATOM   1887 N  N   . ASN A 1 233 ? 4.737   14.102  51.731  1.00 108.00 ? 277 ASN A N   1 
ATOM   1888 C  CA  . ASN A 1 233 ? 3.725   14.318  50.710  1.00 110.11 ? 277 ASN A CA  1 
ATOM   1889 C  C   . ASN A 1 233 ? 4.316   13.994  49.341  1.00 111.85 ? 277 ASN A C   1 
ATOM   1890 O  O   . ASN A 1 233 ? 5.369   14.520  48.983  1.00 113.67 ? 277 ASN A O   1 
ATOM   1891 C  CB  . ASN A 1 233 ? 3.206   15.758  50.727  1.00 112.93 ? 277 ASN A CB  1 
ATOM   1892 C  CG  . ASN A 1 233 ? 2.518   16.126  52.023  1.00 112.55 ? 277 ASN A CG  1 
ATOM   1893 O  OD1 . ASN A 1 233 ? 1.476   15.568  52.359  1.00 110.97 ? 277 ASN A OD1 1 
ATOM   1894 N  ND2 . ASN A 1 233 ? 3.091   17.068  52.754  1.00 113.89 ? 277 ASN A ND2 1 
ATOM   1895 N  N   . ILE A 1 234 ? 3.628   13.127  48.587  1.00 112.13 ? 278 ILE A N   1 
ATOM   1896 C  CA  . ILE A 1 234 ? 3.987   12.836  47.208  1.00 113.87 ? 278 ILE A CA  1 
ATOM   1897 C  C   . ILE A 1 234 ? 3.004   13.571  46.298  1.00 117.59 ? 278 ILE A C   1 
ATOM   1898 O  O   . ILE A 1 234 ? 1.948   13.040  45.957  1.00 116.84 ? 278 ILE A O   1 
ATOM   1899 C  CB  . ILE A 1 234 ? 4.006   11.314  46.947  1.00 111.18 ? 278 ILE A CB  1 
ATOM   1900 C  CG1 . ILE A 1 234 ? 4.892   10.568  47.951  1.00 108.72 ? 278 ILE A CG1 1 
ATOM   1901 C  CG2 . ILE A 1 234 ? 4.410   11.016  45.509  1.00 111.93 ? 278 ILE A CG2 1 
ATOM   1902 C  CD1 . ILE A 1 234 ? 6.338   11.017  47.966  1.00 109.16 ? 278 ILE A CD1 1 
ATOM   1903 N  N   . TYR A 1 235 ? 3.371   14.802  45.919  1.00 121.62 ? 279 TYR A N   1 
ATOM   1904 C  CA  . TYR A 1 235 ? 2.500   15.683  45.156  1.00 125.21 ? 279 TYR A CA  1 
ATOM   1905 C  C   . TYR A 1 235 ? 2.403   15.211  43.707  1.00 126.54 ? 279 TYR A C   1 
ATOM   1906 O  O   . TYR A 1 235 ? 1.328   15.271  43.113  1.00 127.40 ? 279 TYR A O   1 
ATOM   1907 C  CB  . TYR A 1 235 ? 2.997   17.129  45.246  1.00 128.30 ? 279 TYR A CB  1 
ATOM   1908 C  CG  . TYR A 1 235 ? 2.884   17.746  46.618  1.00 128.13 ? 279 TYR A CG  1 
ATOM   1909 C  CD1 . TYR A 1 235 ? 1.650   17.893  47.235  1.00 128.20 ? 279 TYR A CD1 1 
ATOM   1910 C  CD2 . TYR A 1 235 ? 4.006   18.181  47.307  1.00 127.90 ? 279 TYR A CD2 1 
ATOM   1911 C  CE1 . TYR A 1 235 ? 1.533   18.456  48.496  1.00 128.13 ? 279 TYR A CE1 1 
ATOM   1912 C  CE2 . TYR A 1 235 ? 3.906   18.746  48.569  1.00 128.06 ? 279 TYR A CE2 1 
ATOM   1913 C  CZ  . TYR A 1 235 ? 2.665   18.885  49.166  1.00 128.21 ? 279 TYR A CZ  1 
ATOM   1914 O  OH  . TYR A 1 235 ? 2.554   19.443  50.416  1.00 128.71 ? 279 TYR A OH  1 
ATOM   1915 N  N   . ARG A 1 236 ? 3.533   14.755  43.148  1.00 126.90 ? 280 ARG A N   1 
ATOM   1916 C  CA  . ARG A 1 236 ? 3.575   14.212  41.799  1.00 128.46 ? 280 ARG A CA  1 
ATOM   1917 C  C   . ARG A 1 236 ? 3.946   12.731  41.854  1.00 125.83 ? 280 ARG A C   1 
ATOM   1918 O  O   . ARG A 1 236 ? 5.121   12.393  41.988  1.00 124.85 ? 280 ARG A O   1 
ATOM   1919 C  CB  . ARG A 1 236 ? 4.567   14.998  40.933  1.00 131.50 ? 280 ARG A CB  1 
ATOM   1920 C  CG  . ARG A 1 236 ? 4.044   16.335  40.423  1.00 135.32 ? 280 ARG A CG  1 
ATOM   1921 C  CD  . ARG A 1 236 ? 2.686   16.239  39.747  1.00 136.24 ? 280 ARG A CD  1 
ATOM   1922 N  NE  . ARG A 1 236 ? 2.594   15.126  38.809  1.00 134.88 ? 280 ARG A NE  1 
ATOM   1923 C  CZ  . ARG A 1 236 ? 1.457   14.583  38.387  1.00 134.10 ? 280 ARG A CZ  1 
ATOM   1924 N  NH1 . ARG A 1 236 ? 0.296   15.064  38.797  1.00 134.69 ? 280 ARG A NH1 1 
ATOM   1925 N  NH2 . ARG A 1 236 ? 1.484   13.556  37.555  1.00 132.97 ? 280 ARG A NH2 1 
ATOM   1926 N  N   . PRO A 1 237 ? 2.959   11.806  41.764  1.00 125.05 ? 281 PRO A N   1 
ATOM   1927 C  CA  . PRO A 1 237 ? 3.238   10.369  41.708  1.00 122.64 ? 281 PRO A CA  1 
ATOM   1928 C  C   . PRO A 1 237 ? 4.024   9.924   40.475  1.00 124.09 ? 281 PRO A C   1 
ATOM   1929 O  O   . PRO A 1 237 ? 4.906   9.074   40.578  1.00 122.40 ? 281 PRO A O   1 
ATOM   1930 C  CB  . PRO A 1 237 ? 1.844   9.716   41.677  1.00 121.85 ? 281 PRO A CB  1 
ATOM   1931 C  CG  . PRO A 1 237 ? 0.909   10.778  42.215  1.00 122.89 ? 281 PRO A CG  1 
ATOM   1932 C  CD  . PRO A 1 237 ? 1.515   12.090  41.766  1.00 125.89 ? 281 PRO A CD  1 
ATOM   1933 N  N   . ASP A 1 238 ? 3.689   10.501  39.313  1.00 127.96 ? 282 ASP A N   1 
ATOM   1934 C  CA  . ASP A 1 238 ? 4.274   10.098  38.042  1.00 129.44 ? 282 ASP A CA  1 
ATOM   1935 C  C   . ASP A 1 238 ? 5.759   10.454  38.009  1.00 130.46 ? 282 ASP A C   1 
ATOM   1936 O  O   . ASP A 1 238 ? 6.576   9.659   37.549  1.00 129.48 ? 282 ASP A O   1 
ATOM   1937 C  CB  . ASP A 1 238 ? 3.538   10.741  36.863  1.00 132.60 ? 282 ASP A CB  1 
ATOM   1938 C  CG  . ASP A 1 238 ? 2.074   10.347  36.770  1.00 132.44 ? 282 ASP A CG  1 
ATOM   1939 O  OD1 . ASP A 1 238 ? 1.305   10.733  37.674  1.00 131.50 ? 282 ASP A OD1 1 
ATOM   1940 O  OD2 . ASP A 1 238 ? 1.716   9.652   35.799  1.00 133.14 ? 282 ASP A OD2 1 
ATOM   1941 N  N   . LYS A 1 239 ? 6.092   11.657  38.494  1.00 132.36 ? 283 LYS A N   1 
ATOM   1942 C  CA  . LYS A 1 239 ? 7.469   12.124  38.539  1.00 133.68 ? 283 LYS A CA  1 
ATOM   1943 C  C   . LYS A 1 239 ? 8.242   11.384  39.630  1.00 131.00 ? 283 LYS A C   1 
ATOM   1944 O  O   . LYS A 1 239 ? 9.455   11.223  39.522  1.00 131.79 ? 283 LYS A O   1 
ATOM   1945 C  CB  . LYS A 1 239 ? 7.512   13.637  38.773  1.00 136.06 ? 283 LYS A CB  1 
ATOM   1946 C  CG  . LYS A 1 239 ? 6.853   14.475  37.685  1.00 139.47 ? 283 LYS A CG  1 
ATOM   1947 C  CD  . LYS A 1 239 ? 7.049   15.965  37.864  1.00 142.20 ? 283 LYS A CD  1 
ATOM   1948 C  CE  . LYS A 1 239 ? 6.350   16.782  36.799  1.00 146.03 ? 283 LYS A CE  1 
ATOM   1949 N  NZ  . LYS A 1 239 ? 6.563   18.235  36.996  1.00 149.29 ? 283 LYS A NZ  1 
ATOM   1950 N  N   . PHE A 1 240 ? 7.532   10.947  40.680  1.00 128.27 ? 284 PHE A N   1 
ATOM   1951 C  CA  . PHE A 1 240 ? 8.137   10.203  41.774  1.00 125.72 ? 284 PHE A CA  1 
ATOM   1952 C  C   . PHE A 1 240 ? 8.617   8.838   41.281  1.00 125.02 ? 284 PHE A C   1 
ATOM   1953 O  O   . PHE A 1 240 ? 9.692   8.386   41.670  1.00 123.64 ? 284 PHE A O   1 
ATOM   1954 C  CB  . PHE A 1 240 ? 7.150   10.060  42.936  1.00 123.56 ? 284 PHE A CB  1 
ATOM   1955 C  CG  . PHE A 1 240 ? 7.675   9.288   44.121  1.00 121.16 ? 284 PHE A CG  1 
ATOM   1956 C  CD1 . PHE A 1 240 ? 8.798   9.722   44.809  1.00 121.46 ? 284 PHE A CD1 1 
ATOM   1957 C  CD2 . PHE A 1 240 ? 7.048   8.126   44.548  1.00 118.99 ? 284 PHE A CD2 1 
ATOM   1958 C  CE1 . PHE A 1 240 ? 9.283   9.013   45.898  1.00 119.17 ? 284 PHE A CE1 1 
ATOM   1959 C  CE2 . PHE A 1 240 ? 7.534   7.418   45.637  1.00 117.07 ? 284 PHE A CE2 1 
ATOM   1960 C  CZ  . PHE A 1 240 ? 8.649   7.863   46.310  1.00 117.18 ? 284 PHE A CZ  1 
ATOM   1961 N  N   . LEU A 1 241 ? 7.809   8.187   40.434  1.00 126.22 ? 285 LEU A N   1 
ATOM   1962 C  CA  . LEU A 1 241 ? 8.169   6.901   39.852  1.00 126.79 ? 285 LEU A CA  1 
ATOM   1963 C  C   . LEU A 1 241 ? 9.350   7.069   38.898  1.00 129.95 ? 285 LEU A C   1 
ATOM   1964 O  O   . LEU A 1 241 ? 10.228  6.210   38.843  1.00 129.70 ? 285 LEU A O   1 
ATOM   1965 C  CB  . LEU A 1 241 ? 6.957   6.312   39.119  1.00 127.14 ? 285 LEU A CB  1 
ATOM   1966 C  CG  . LEU A 1 241 ? 5.835   5.765   40.003  1.00 125.05 ? 285 LEU A CG  1 
ATOM   1967 C  CD1 . LEU A 1 241 ? 4.746   5.128   39.153  1.00 125.52 ? 285 LEU A CD1 1 
ATOM   1968 C  CD2 . LEU A 1 241 ? 6.368   4.764   41.019  1.00 122.42 ? 285 LEU A CD2 1 
ATOM   1969 N  N   . GLN A 1 242 ? 9.356   8.179   38.148  1.00 133.54 ? 286 GLN A N   1 
ATOM   1970 C  CA  . GLN A 1 242 ? 10.397  8.452   37.169  1.00 136.32 ? 286 GLN A CA  1 
ATOM   1971 C  C   . GLN A 1 242 ? 11.660  8.921   37.893  1.00 136.71 ? 286 GLN A C   1 
ATOM   1972 O  O   . GLN A 1 242 ? 12.766  8.750   37.384  1.00 137.42 ? 286 GLN A O   1 
ATOM   1973 C  CB  . GLN A 1 242 ? 9.889   9.477   36.149  1.00 139.68 ? 286 GLN A CB  1 
ATOM   1974 C  CG  . GLN A 1 242 ? 10.410  9.256   34.735  1.00 143.26 ? 286 GLN A CG  1 
ATOM   1975 C  CD  . GLN A 1 242 ? 11.865  9.623   34.573  1.00 145.92 ? 286 GLN A CD  1 
ATOM   1976 O  OE1 . GLN A 1 242 ? 12.248  10.786  34.689  1.00 148.23 ? 286 GLN A OE1 1 
ATOM   1977 N  NE2 . GLN A 1 242 ? 12.691  8.627   34.291  1.00 146.06 ? 286 GLN A NE2 1 
ATOM   1978 N  N   . CYS A 1 243 ? 11.480  9.506   39.086  1.00 136.13 ? 287 CYS A N   1 
ATOM   1979 C  CA  . CYS A 1 243 ? 12.581  9.947   39.932  1.00 136.44 ? 287 CYS A CA  1 
ATOM   1980 C  C   . CYS A 1 243 ? 13.408  8.756   40.414  1.00 135.09 ? 287 CYS A C   1 
ATOM   1981 O  O   . CYS A 1 243 ? 14.630  8.756   40.273  1.00 135.74 ? 287 CYS A O   1 
ATOM   1982 C  CB  . CYS A 1 243 ? 12.062  10.738  41.130  1.00 135.05 ? 287 CYS A CB  1 
ATOM   1983 S  SG  . CYS A 1 243 ? 13.269  10.927  42.470  1.00 132.74 ? 287 CYS A SG  1 
ATOM   1984 N  N   . VAL A 1 244 ? 12.731  7.751   40.986  1.00 132.33 ? 288 VAL A N   1 
ATOM   1985 C  CA  . VAL A 1 244 ? 13.398  6.594   41.568  1.00 130.21 ? 288 VAL A CA  1 
ATOM   1986 C  C   . VAL A 1 244 ? 14.048  5.757   40.465  1.00 131.40 ? 288 VAL A C   1 
ATOM   1987 O  O   . VAL A 1 244 ? 15.001  5.026   40.730  1.00 130.39 ? 288 VAL A O   1 
ATOM   1988 C  CB  . VAL A 1 244 ? 12.438  5.748   42.431  1.00 126.91 ? 288 VAL A CB  1 
ATOM   1989 C  CG1 . VAL A 1 244 ? 11.951  6.522   43.647  1.00 125.61 ? 288 VAL A CG1 1 
ATOM   1990 C  CG2 . VAL A 1 244 ? 11.257  5.202   41.639  1.00 126.54 ? 288 VAL A CG2 1 
ATOM   1991 N  N   . LYS A 1 245 ? 13.522  5.861   39.238  1.00 133.51 ? 289 LYS A N   1 
ATOM   1992 C  CA  . LYS A 1 245 ? 14.130  5.227   38.078  1.00 135.69 ? 289 LYS A CA  1 
ATOM   1993 C  C   . LYS A 1 245 ? 15.483  5.889   37.820  1.00 139.48 ? 289 LYS A C   1 
ATOM   1994 O  O   . LYS A 1 245 ? 16.505  5.208   37.785  1.00 141.06 ? 289 LYS A O   1 
ATOM   1995 C  CB  . LYS A 1 245 ? 13.179  5.311   36.878  1.00 136.34 ? 289 LYS A CB  1 
ATOM   1996 C  CG  . LYS A 1 245 ? 13.471  4.353   35.729  1.00 137.50 ? 289 LYS A CG  1 
ATOM   1997 C  CD  . LYS A 1 245 ? 14.561  4.821   34.786  1.00 140.73 ? 289 LYS A CD  1 
ATOM   1998 C  CE  . LYS A 1 245 ? 14.675  3.959   33.546  1.00 142.13 ? 289 LYS A CE  1 
ATOM   1999 N  NZ  . LYS A 1 245 ? 15.687  4.489   32.602  1.00 145.54 ? 289 LYS A NZ  1 
ATOM   2000 N  N   . ASN A 1 246 ? 15.471  7.219   37.657  1.00 141.67 ? 290 ASN A N   1 
ATOM   2001 C  CA  . ASN A 1 246 ? 16.684  8.022   37.579  1.00 144.42 ? 290 ASN A CA  1 
ATOM   2002 C  C   . ASN A 1 246 ? 16.321  9.504   37.750  1.00 146.00 ? 290 ASN A C   1 
ATOM   2003 O  O   . ASN A 1 246 ? 15.924  10.119  36.738  1.00 148.43 ? 290 ASN A O   1 
ATOM   2004 C  CB  . ASN A 1 246 ? 17.461  7.790   36.277  1.00 147.51 ? 290 ASN A CB  1 
ATOM   2005 C  CG  . ASN A 1 246 ? 18.484  6.675   36.382  1.00 146.98 ? 290 ASN A CG  1 
ATOM   2006 O  OD1 . ASN A 1 246 ? 19.410  6.751   37.190  1.00 146.50 ? 290 ASN A OD1 1 
ATOM   2007 N  ND2 . ASN A 1 246 ? 18.327  5.638   35.572  1.00 147.11 ? 290 ASN A ND2 1 
ATOM   2008 N  N   . GLN B 2 1   ? 16.773  -40.985 25.059  1.00 101.66 ? 1   GLN H N   1 
ATOM   2009 C  CA  . GLN B 2 1   ? 15.409  -41.509 24.768  1.00 101.05 ? 1   GLN H CA  1 
ATOM   2010 C  C   . GLN B 2 1   ? 14.549  -40.396 24.175  1.00 96.52  ? 1   GLN H C   1 
ATOM   2011 O  O   . GLN B 2 1   ? 13.863  -40.607 23.177  1.00 94.18  ? 1   GLN H O   1 
ATOM   2012 C  CB  . GLN B 2 1   ? 14.754  -42.071 26.035  1.00 103.86 ? 1   GLN H CB  1 
ATOM   2013 C  CG  . GLN B 2 1   ? 15.623  -43.051 26.817  1.00 107.43 ? 1   GLN H CG  1 
ATOM   2014 C  CD  . GLN B 2 1   ? 15.932  -44.324 26.064  1.00 109.96 ? 1   GLN H CD  1 
ATOM   2015 O  OE1 . GLN B 2 1   ? 15.477  -44.543 24.942  1.00 110.00 ? 1   GLN H OE1 1 
ATOM   2016 N  NE2 . GLN B 2 1   ? 16.714  -45.188 26.691  1.00 113.19 ? 1   GLN H NE2 1 
ATOM   2017 N  N   . VAL B 2 2   ? 14.589  -39.218 24.812  1.00 94.45  ? 2   VAL H N   1 
ATOM   2018 C  CA  . VAL B 2 2   ? 13.812  -38.067 24.378  1.00 92.30  ? 2   VAL H CA  1 
ATOM   2019 C  C   . VAL B 2 2   ? 14.437  -37.484 23.110  1.00 90.44  ? 2   VAL H C   1 
ATOM   2020 O  O   . VAL B 2 2   ? 15.659  -37.440 22.977  1.00 90.76  ? 2   VAL H O   1 
ATOM   2021 C  CB  . VAL B 2 2   ? 13.687  -37.007 25.494  1.00 91.78  ? 2   VAL H CB  1 
ATOM   2022 C  CG1 . VAL B 2 2   ? 15.037  -36.463 25.943  1.00 92.20  ? 2   VAL H CG1 1 
ATOM   2023 C  CG2 . VAL B 2 2   ? 12.765  -35.867 25.086  1.00 89.84  ? 2   VAL H CG2 1 
ATOM   2024 N  N   . GLN B 2 3   ? 13.573  -37.042 22.186  1.00 88.42  ? 3   GLN H N   1 
ATOM   2025 C  CA  . GLN B 2 3   ? 13.993  -36.470 20.916  1.00 86.44  ? 3   GLN H CA  1 
ATOM   2026 C  C   . GLN B 2 3   ? 13.040  -35.345 20.525  1.00 83.86  ? 3   GLN H C   1 
ATOM   2027 O  O   . GLN B 2 3   ? 11.828  -35.549 20.476  1.00 84.53  ? 3   GLN H O   1 
ATOM   2028 C  CB  . GLN B 2 3   ? 13.999  -37.532 19.815  1.00 87.99  ? 3   GLN H CB  1 
ATOM   2029 C  CG  . GLN B 2 3   ? 15.131  -38.541 19.934  1.00 90.97  ? 3   GLN H CG  1 
ATOM   2030 C  CD  . GLN B 2 3   ? 15.169  -39.473 18.747  1.00 92.78  ? 3   GLN H CD  1 
ATOM   2031 O  OE1 . GLN B 2 3   ? 15.245  -39.040 17.598  1.00 92.77  ? 3   GLN H OE1 1 
ATOM   2032 N  NE2 . GLN B 2 3   ? 15.106  -40.767 19.017  1.00 95.33  ? 3   GLN H NE2 1 
ATOM   2033 N  N   . LEU B 2 4   ? 13.606  -34.167 20.237  1.00 80.89  ? 4   LEU H N   1 
ATOM   2034 C  CA  . LEU B 2 4   ? 12.838  -33.025 19.768  1.00 78.84  ? 4   LEU H CA  1 
ATOM   2035 C  C   . LEU B 2 4   ? 13.086  -32.845 18.272  1.00 76.88  ? 4   LEU H C   1 
ATOM   2036 O  O   . LEU B 2 4   ? 14.235  -32.768 17.842  1.00 76.23  ? 4   LEU H O   1 
ATOM   2037 C  CB  . LEU B 2 4   ? 13.263  -31.781 20.556  1.00 78.74  ? 4   LEU H CB  1 
ATOM   2038 C  CG  . LEU B 2 4   ? 13.182  -31.894 22.079  1.00 79.66  ? 4   LEU H CG  1 
ATOM   2039 C  CD1 . LEU B 2 4   ? 13.418  -30.542 22.734  1.00 78.69  ? 4   LEU H CD1 1 
ATOM   2040 C  CD2 . LEU B 2 4   ? 11.846  -32.472 22.524  1.00 80.65  ? 4   LEU H CD2 1 
ATOM   2041 N  N   . VAL B 2 5   ? 11.998  -32.786 17.493  1.00 75.67  ? 5   VAL H N   1 
ATOM   2042 C  CA  . VAL B 2 5   ? 12.075  -32.638 16.047  1.00 75.66  ? 5   VAL H CA  1 
ATOM   2043 C  C   . VAL B 2 5   ? 11.309  -31.380 15.646  1.00 75.09  ? 5   VAL H C   1 
ATOM   2044 O  O   . VAL B 2 5   ? 10.087  -31.330 15.775  1.00 75.36  ? 5   VAL H O   1 
ATOM   2045 C  CB  . VAL B 2 5   ? 11.534  -33.889 15.327  1.00 77.04  ? 5   VAL H CB  1 
ATOM   2046 C  CG1 . VAL B 2 5   ? 11.392  -33.673 13.826  1.00 77.07  ? 5   VAL H CG1 1 
ATOM   2047 C  CG2 . VAL B 2 5   ? 12.391  -35.113 15.612  1.00 78.48  ? 5   VAL H CG2 1 
ATOM   2048 N  N   . GLN B 2 6   ? 12.046  -30.378 15.148  1.00 74.46  ? 6   GLN H N   1 
ATOM   2049 C  CA  . GLN B 2 6   ? 11.481  -29.087 14.790  1.00 73.59  ? 6   GLN H CA  1 
ATOM   2050 C  C   . GLN B 2 6   ? 11.047  -29.088 13.326  1.00 73.98  ? 6   GLN H C   1 
ATOM   2051 O  O   . GLN B 2 6   ? 11.384  -29.999 12.572  1.00 74.81  ? 6   GLN H O   1 
ATOM   2052 C  CB  . GLN B 2 6   ? 12.508  -27.978 15.023  1.00 72.24  ? 6   GLN H CB  1 
ATOM   2053 C  CG  . GLN B 2 6   ? 12.899  -27.806 16.482  1.00 71.67  ? 6   GLN H CG  1 
ATOM   2054 C  CD  . GLN B 2 6   ? 13.938  -26.726 16.655  1.00 71.42  ? 6   GLN H CD  1 
ATOM   2055 O  OE1 . GLN B 2 6   ? 15.010  -26.956 17.208  1.00 72.27  ? 6   GLN H OE1 1 
ATOM   2056 N  NE2 . GLN B 2 6   ? 13.628  -25.534 16.173  1.00 71.17  ? 6   GLN H NE2 1 
ATOM   2057 N  N   . SER B 2 7   ? 10.303  -28.044 12.940  1.00 73.05  ? 7   SER H N   1 
ATOM   2058 C  CA  . SER B 2 7   ? 9.883   -27.856 11.560  1.00 73.90  ? 7   SER H CA  1 
ATOM   2059 C  C   . SER B 2 7   ? 11.055  -27.335 10.731  1.00 73.51  ? 7   SER H C   1 
ATOM   2060 O  O   . SER B 2 7   ? 12.081  -26.935 11.279  1.00 71.81  ? 7   SER H O   1 
ATOM   2061 C  CB  . SER B 2 7   ? 8.692   -26.935 11.477  1.00 74.33  ? 7   SER H CB  1 
ATOM   2062 O  OG  . SER B 2 7   ? 8.968   -25.689 12.097  1.00 73.87  ? 7   SER H OG  1 
ATOM   2063 N  N   . GLY B 2 8   ? 10.881  -27.346 9.404   1.00 75.01  ? 8   GLY H N   1 
ATOM   2064 C  CA  . GLY B 2 8   ? 11.943  -26.990 8.476   1.00 75.82  ? 8   GLY H CA  1 
ATOM   2065 C  C   . GLY B 2 8   ? 12.172  -25.483 8.393   1.00 75.28  ? 8   GLY H C   1 
ATOM   2066 O  O   . GLY B 2 8   ? 11.353  -24.693 8.857   1.00 74.76  ? 8   GLY H O   1 
ATOM   2067 N  N   . ALA B 2 9   ? 13.303  -25.106 7.784   1.00 76.84  ? 9   ALA H N   1 
ATOM   2068 C  CA  . ALA B 2 9   ? 13.654  -23.711 7.565   1.00 78.07  ? 9   ALA H CA  1 
ATOM   2069 C  C   . ALA B 2 9   ? 12.734  -23.110 6.505   1.00 80.33  ? 9   ALA H C   1 
ATOM   2070 O  O   . ALA B 2 9   ? 12.198  -23.832 5.667   1.00 82.59  ? 9   ALA H O   1 
ATOM   2071 C  CB  . ALA B 2 9   ? 15.104  -23.608 7.157   1.00 78.07  ? 9   ALA H CB  1 
ATOM   2072 N  N   . GLU B 2 10  ? 12.563  -21.783 6.554   1.00 81.72  ? 10  GLU H N   1 
ATOM   2073 C  CA  . GLU B 2 10  ? 11.690  -21.085 5.622   1.00 83.85  ? 10  GLU H CA  1 
ATOM   2074 C  C   . GLU B 2 10  ? 12.022  -19.594 5.607   1.00 82.76  ? 10  GLU H C   1 
ATOM   2075 O  O   . GLU B 2 10  ? 12.654  -19.078 6.529   1.00 80.00  ? 10  GLU H O   1 
ATOM   2076 C  CB  . GLU B 2 10  ? 10.222  -21.321 5.987   1.00 85.38  ? 10  GLU H CB  1 
ATOM   2077 C  CG  . GLU B 2 10  ? 9.851   -20.871 7.390   1.00 85.23  ? 10  GLU H CG  1 
ATOM   2078 C  CD  . GLU B 2 10  ? 8.459   -21.290 7.833   1.00 88.01  ? 10  GLU H CD  1 
ATOM   2079 O  OE1 . GLU B 2 10  ? 8.342   -21.909 8.911   1.00 88.06  ? 10  GLU H OE1 1 
ATOM   2080 O  OE2 . GLU B 2 10  ? 7.496   -21.008 7.092   1.00 91.14  ? 10  GLU H OE2 1 
ATOM   2081 N  N   . VAL B 2 11  ? 11.580  -18.919 4.537   1.00 83.79  ? 11  VAL H N   1 
ATOM   2082 C  CA  . VAL B 2 11  ? 11.754  -17.484 4.378   1.00 84.55  ? 11  VAL H CA  1 
ATOM   2083 C  C   . VAL B 2 11  ? 10.470  -16.788 4.826   1.00 85.47  ? 11  VAL H C   1 
ATOM   2084 O  O   . VAL B 2 11  ? 9.383   -17.347 4.696   1.00 86.62  ? 11  VAL H O   1 
ATOM   2085 C  CB  . VAL B 2 11  ? 12.122  -17.115 2.926   1.00 86.08  ? 11  VAL H CB  1 
ATOM   2086 C  CG1 . VAL B 2 11  ? 10.982  -17.376 1.950   1.00 88.29  ? 11  VAL H CG1 1 
ATOM   2087 C  CG2 . VAL B 2 11  ? 12.594  -15.673 2.813   1.00 86.57  ? 11  VAL H CG2 1 
ATOM   2088 N  N   . LYS B 2 12  ? 10.612  -15.565 5.352   1.00 85.70  ? 12  LYS H N   1 
ATOM   2089 C  CA  . LYS B 2 12  ? 9.477   -14.768 5.791   1.00 87.30  ? 12  LYS H CA  1 
ATOM   2090 C  C   . LYS B 2 12  ? 9.711   -13.305 5.428   1.00 89.08  ? 12  LYS H C   1 
ATOM   2091 O  O   . LYS B 2 12  ? 10.848  -12.840 5.406   1.00 88.77  ? 12  LYS H O   1 
ATOM   2092 C  CB  . LYS B 2 12  ? 9.260   -14.922 7.301   1.00 85.73  ? 12  LYS H CB  1 
ATOM   2093 C  CG  . LYS B 2 12  ? 8.682   -16.260 7.742   1.00 84.79  ? 12  LYS H CG  1 
ATOM   2094 C  CD  . LYS B 2 12  ? 7.255   -16.488 7.287   1.00 86.99  ? 12  LYS H CD  1 
ATOM   2095 C  CE  . LYS B 2 12  ? 6.736   -17.863 7.649   1.00 87.07  ? 12  LYS H CE  1 
ATOM   2096 N  NZ  . LYS B 2 12  ? 5.369   -18.088 7.125   1.00 90.40  ? 12  LYS H NZ  1 
ATOM   2097 N  N   . LYS B 2 13  ? 8.614   -12.589 5.157   1.00 92.14  ? 13  LYS H N   1 
ATOM   2098 C  CA  . LYS B 2 13  ? 8.678   -11.189 4.769   1.00 94.38  ? 13  LYS H CA  1 
ATOM   2099 C  C   . LYS B 2 13  ? 8.836   -10.346 6.033   1.00 93.15  ? 13  LYS H C   1 
ATOM   2100 O  O   . LYS B 2 13  ? 8.413   -10.767 7.108   1.00 91.91  ? 13  LYS H O   1 
ATOM   2101 C  CB  . LYS B 2 13  ? 7.422   -10.773 3.992   1.00 98.22  ? 13  LYS H CB  1 
ATOM   2102 C  CG  . LYS B 2 13  ? 7.251   -11.388 2.606   1.00 100.25 ? 13  LYS H CG  1 
ATOM   2103 C  CD  . LYS B 2 13  ? 6.986   -12.887 2.580   1.00 99.91  ? 13  LYS H CD  1 
ATOM   2104 C  CE  . LYS B 2 13  ? 5.720   -13.304 3.302   1.00 100.37 ? 13  LYS H CE  1 
ATOM   2105 N  NZ  . LYS B 2 13  ? 5.580   -14.779 3.358   1.00 98.48  ? 13  LYS H NZ  1 
ATOM   2106 N  N   . PRO B 2 14  ? 9.461   -9.147  5.960   1.00 93.28  ? 14  PRO H N   1 
ATOM   2107 C  CA  . PRO B 2 14  ? 9.527   -8.249  7.114   1.00 92.32  ? 14  PRO H CA  1 
ATOM   2108 C  C   . PRO B 2 14  ? 8.131   -7.827  7.569   1.00 93.71  ? 14  PRO H C   1 
ATOM   2109 O  O   . PRO B 2 14  ? 7.345   -7.322  6.770   1.00 96.19  ? 14  PRO H O   1 
ATOM   2110 C  CB  . PRO B 2 14  ? 10.333  -7.041  6.611   1.00 93.65  ? 14  PRO H CB  1 
ATOM   2111 C  CG  . PRO B 2 14  ? 11.072  -7.553  5.390   1.00 93.59  ? 14  PRO H CG  1 
ATOM   2112 C  CD  . PRO B 2 14  ? 10.162  -8.603  4.787   1.00 94.20  ? 14  PRO H CD  1 
ATOM   2113 N  N   . GLY B 2 15  ? 7.827   -8.068  8.851   1.00 92.14  ? 15  GLY H N   1 
ATOM   2114 C  CA  . GLY B 2 15  ? 6.553   -7.679  9.435   1.00 94.60  ? 15  GLY H CA  1 
ATOM   2115 C  C   . GLY B 2 15  ? 5.584   -8.852  9.588   1.00 94.48  ? 15  GLY H C   1 
ATOM   2116 O  O   . GLY B 2 15  ? 4.621   -8.756  10.345  1.00 95.37  ? 15  GLY H O   1 
ATOM   2117 N  N   . SER B 2 16  ? 5.843   -9.951  8.866   1.00 94.24  ? 16  SER H N   1 
ATOM   2118 C  CA  . SER B 2 16  ? 5.009   -11.141 8.933   1.00 94.42  ? 16  SER H CA  1 
ATOM   2119 C  C   . SER B 2 16  ? 5.316   -11.916 10.214  1.00 92.24  ? 16  SER H C   1 
ATOM   2120 O  O   . SER B 2 16  ? 6.145   -11.490 11.015  1.00 90.68  ? 16  SER H O   1 
ATOM   2121 C  CB  . SER B 2 16  ? 5.196   -12.001 7.705   1.00 94.38  ? 16  SER H CB  1 
ATOM   2122 O  OG  . SER B 2 16  ? 6.479   -12.611 7.696   1.00 91.59  ? 16  SER H OG  1 
ATOM   2123 N  N   . SER B 2 17  ? 4.632   -13.054 10.396  1.00 92.37  ? 17  SER H N   1 
ATOM   2124 C  CA  . SER B 2 17  ? 4.803   -13.885 11.576  1.00 90.36  ? 17  SER H CA  1 
ATOM   2125 C  C   . SER B 2 17  ? 5.222   -15.296 11.167  1.00 88.54  ? 17  SER H C   1 
ATOM   2126 O  O   . SER B 2 17  ? 4.897   -15.749 10.070  1.00 88.90  ? 17  SER H O   1 
ATOM   2127 C  CB  . SER B 2 17  ? 3.539   -13.897 12.399  1.00 92.22  ? 17  SER H CB  1 
ATOM   2128 O  OG  . SER B 2 17  ? 3.746   -14.549 13.642  1.00 91.41  ? 17  SER H OG  1 
ATOM   2129 N  N   . VAL B 2 18  ? 5.947   -15.977 12.065  1.00 86.57  ? 18  VAL H N   1 
ATOM   2130 C  CA  . VAL B 2 18  ? 6.423   -17.334 11.834  1.00 85.58  ? 18  VAL H CA  1 
ATOM   2131 C  C   . VAL B 2 18  ? 5.981   -18.210 13.004  1.00 84.76  ? 18  VAL H C   1 
ATOM   2132 O  O   . VAL B 2 18  ? 5.825   -17.719 14.119  1.00 85.29  ? 18  VAL H O   1 
ATOM   2133 C  CB  . VAL B 2 18  ? 7.954   -17.378 11.648  1.00 84.43  ? 18  VAL H CB  1 
ATOM   2134 C  CG1 . VAL B 2 18  ? 8.703   -17.001 12.920  1.00 82.94  ? 18  VAL H CG1 1 
ATOM   2135 C  CG2 . VAL B 2 18  ? 8.425   -18.733 11.139  1.00 83.65  ? 18  VAL H CG2 1 
ATOM   2136 N  N   . LYS B 2 19  ? 5.791   -19.507 12.732  1.00 83.83  ? 19  LYS H N   1 
ATOM   2137 C  CA  . LYS B 2 19  ? 5.375   -20.466 13.743  1.00 82.70  ? 19  LYS H CA  1 
ATOM   2138 C  C   . LYS B 2 19  ? 6.197   -21.744 13.576  1.00 81.22  ? 19  LYS H C   1 
ATOM   2139 O  O   . LYS B 2 19  ? 6.012   -22.480 12.609  1.00 82.22  ? 19  LYS H O   1 
ATOM   2140 C  CB  . LYS B 2 19  ? 3.871   -20.730 13.618  1.00 85.03  ? 19  LYS H CB  1 
ATOM   2141 C  CG  . LYS B 2 19  ? 3.216   -21.393 14.824  1.00 85.09  ? 19  LYS H CG  1 
ATOM   2142 C  CD  . LYS B 2 19  ? 1.742   -21.681 14.617  1.00 87.33  ? 19  LYS H CD  1 
ATOM   2143 C  CE  . LYS B 2 19  ? 1.030   -22.129 15.876  1.00 87.76  ? 19  LYS H CE  1 
ATOM   2144 N  NZ  . LYS B 2 19  ? 0.931   -21.036 16.873  1.00 88.24  ? 19  LYS H NZ  1 
ATOM   2145 N  N   . VAL B 2 20  ? 7.110   -21.988 14.526  1.00 78.88  ? 20  VAL H N   1 
ATOM   2146 C  CA  . VAL B 2 20  ? 8.020   -23.123 14.478  1.00 76.42  ? 20  VAL H CA  1 
ATOM   2147 C  C   . VAL B 2 20  ? 7.535   -24.184 15.466  1.00 76.57  ? 20  VAL H C   1 
ATOM   2148 O  O   . VAL B 2 20  ? 7.307   -23.880 16.636  1.00 76.82  ? 20  VAL H O   1 
ATOM   2149 C  CB  . VAL B 2 20  ? 9.464   -22.682 14.788  1.00 74.50  ? 20  VAL H CB  1 
ATOM   2150 C  CG1 . VAL B 2 20  ? 10.422  -23.864 14.861  1.00 73.55  ? 20  VAL H CG1 1 
ATOM   2151 C  CG2 . VAL B 2 20  ? 9.962   -21.649 13.788  1.00 74.71  ? 20  VAL H CG2 1 
ATOM   2152 N  N   . SER B 2 21  ? 7.394   -25.427 14.984  1.00 76.18  ? 21  SER H N   1 
ATOM   2153 C  CA  . SER B 2 21  ? 6.921   -26.534 15.802  1.00 75.73  ? 21  SER H CA  1 
ATOM   2154 C  C   . SER B 2 21  ? 8.105   -27.268 16.429  1.00 74.57  ? 21  SER H C   1 
ATOM   2155 O  O   . SER B 2 21  ? 9.257   -26.998 16.100  1.00 74.05  ? 21  SER H O   1 
ATOM   2156 C  CB  . SER B 2 21  ? 6.059   -27.476 14.997  1.00 76.78  ? 21  SER H CB  1 
ATOM   2157 O  OG  . SER B 2 21  ? 6.842   -28.251 14.102  1.00 76.39  ? 21  SER H OG  1 
ATOM   2158 N  N   . CYS B 2 22  ? 7.794   -28.200 17.337  1.00 75.69  ? 22  CYS H N   1 
ATOM   2159 C  CA  . CYS B 2 22  ? 8.798   -28.963 18.061  1.00 75.25  ? 22  CYS H CA  1 
ATOM   2160 C  C   . CYS B 2 22  ? 8.148   -30.199 18.677  1.00 77.33  ? 22  CYS H C   1 
ATOM   2161 O  O   . CYS B 2 22  ? 7.637   -30.139 19.794  1.00 79.00  ? 22  CYS H O   1 
ATOM   2162 C  CB  . CYS B 2 22  ? 9.445   -28.115 19.150  1.00 74.50  ? 22  CYS H CB  1 
ATOM   2163 S  SG  . CYS B 2 22  ? 10.353  -29.084 20.384  1.00 73.32  ? 22  CYS H SG  1 
ATOM   2164 N  N   . LYS B 2 23  ? 8.178   -31.313 17.935  1.00 78.45  ? 23  LYS H N   1 
ATOM   2165 C  CA  . LYS B 2 23  ? 7.513   -32.540 18.342  1.00 79.79  ? 23  LYS H CA  1 
ATOM   2166 C  C   . LYS B 2 23  ? 8.436   -33.341 19.256  1.00 80.40  ? 23  LYS H C   1 
ATOM   2167 O  O   . LYS B 2 23  ? 9.415   -33.925 18.798  1.00 80.49  ? 23  LYS H O   1 
ATOM   2168 C  CB  . LYS B 2 23  ? 7.114   -33.361 17.110  1.00 80.79  ? 23  LYS H CB  1 
ATOM   2169 C  CG  . LYS B 2 23  ? 6.377   -34.660 17.407  1.00 83.30  ? 23  LYS H CG  1 
ATOM   2170 C  CD  . LYS B 2 23  ? 5.923   -35.394 16.162  1.00 85.36  ? 23  LYS H CD  1 
ATOM   2171 C  CE  . LYS B 2 23  ? 5.231   -36.706 16.465  1.00 87.64  ? 23  LYS H CE  1 
ATOM   2172 N  NZ  . LYS B 2 23  ? 4.015   -36.511 17.290  1.00 88.61  ? 23  LYS H NZ  1 
ATOM   2173 N  N   . ALA B 2 24  ? 8.107   -33.358 20.553  1.00 82.41  ? 24  ALA H N   1 
ATOM   2174 C  CA  . ALA B 2 24  ? 8.808   -34.184 21.523  1.00 83.82  ? 24  ALA H CA  1 
ATOM   2175 C  C   . ALA B 2 24  ? 8.333   -35.629 21.393  1.00 85.78  ? 24  ALA H C   1 
ATOM   2176 O  O   . ALA B 2 24  ? 7.242   -35.885 20.885  1.00 86.53  ? 24  ALA H O   1 
ATOM   2177 C  CB  . ALA B 2 24  ? 8.579   -33.649 22.915  1.00 84.18  ? 24  ALA H CB  1 
ATOM   2178 N  N   . SER B 2 25  ? 9.166   -36.567 21.859  1.00 86.42  ? 25  SER H N   1 
ATOM   2179 C  CA  . SER B 2 25  ? 8.855   -37.985 21.782  1.00 88.66  ? 25  SER H CA  1 
ATOM   2180 C  C   . SER B 2 25  ? 9.677   -38.755 22.813  1.00 89.98  ? 25  SER H C   1 
ATOM   2181 O  O   . SER B 2 25  ? 10.858  -38.476 22.997  1.00 89.08  ? 25  SER H O   1 
ATOM   2182 C  CB  . SER B 2 25  ? 9.090   -38.513 20.389  1.00 88.82  ? 25  SER H CB  1 
ATOM   2183 O  OG  . SER B 2 25  ? 10.430  -38.282 19.977  1.00 87.77  ? 25  SER H OG  1 
ATOM   2184 N  N   . GLY B 2 26  ? 9.033   -39.724 23.477  1.00 92.02  ? 26  GLY H N   1 
ATOM   2185 C  CA  . GLY B 2 26  ? 9.687   -40.552 24.477  1.00 93.80  ? 26  GLY H CA  1 
ATOM   2186 C  C   . GLY B 2 26  ? 9.920   -39.802 25.788  1.00 93.93  ? 26  GLY H C   1 
ATOM   2187 O  O   . GLY B 2 26  ? 10.927  -40.022 26.458  1.00 94.00  ? 26  GLY H O   1 
ATOM   2188 N  N   . LEU B 2 27  ? 8.972   -38.926 26.145  1.00 94.02  ? 27  LEU H N   1 
ATOM   2189 C  CA  . LEU B 2 27  ? 9.046   -38.157 27.377  1.00 94.83  ? 27  LEU H CA  1 
ATOM   2190 C  C   . LEU B 2 27  ? 8.632   -39.043 28.551  1.00 97.69  ? 27  LEU H C   1 
ATOM   2191 O  O   . LEU B 2 27  ? 7.570   -39.662 28.508  1.00 97.53  ? 27  LEU H O   1 
ATOM   2192 C  CB  . LEU B 2 27  ? 8.132   -36.933 27.260  1.00 93.52  ? 27  LEU H CB  1 
ATOM   2193 C  CG  . LEU B 2 27  ? 8.617   -35.831 26.319  1.00 91.33  ? 27  LEU H CG  1 
ATOM   2194 C  CD1 . LEU B 2 27  ? 7.541   -34.774 26.128  1.00 91.00  ? 27  LEU H CD1 1 
ATOM   2195 C  CD2 . LEU B 2 27  ? 9.897   -35.193 26.841  1.00 90.58  ? 27  LEU H CD2 1 
ATOM   2196 N  N   . PRO B 2 28  ? 9.451   -39.141 29.626  1.00 100.22 ? 28  PRO H N   1 
ATOM   2197 C  CA  . PRO B 2 28  ? 9.113   -39.973 30.783  1.00 104.02 ? 28  PRO H CA  1 
ATOM   2198 C  C   . PRO B 2 28  ? 7.818   -39.593 31.504  1.00 105.37 ? 28  PRO H C   1 
ATOM   2199 O  O   . PRO B 2 28  ? 7.033   -40.470 31.858  1.00 108.09 ? 28  PRO H O   1 
ATOM   2200 C  CB  . PRO B 2 28  ? 10.301  -39.784 31.743  1.00 105.35 ? 28  PRO H CB  1 
ATOM   2201 C  CG  . PRO B 2 28  ? 11.435  -39.306 30.860  1.00 102.99 ? 28  PRO H CG  1 
ATOM   2202 C  CD  . PRO B 2 28  ? 10.766  -38.496 29.770  1.00 99.79  ? 28  PRO H CD  1 
ATOM   2203 N  N   . ASP B 2 29  ? 7.606   -38.286 31.716  1.00 103.94 ? 29  ASP H N   1 
ATOM   2204 C  CA  . ASP B 2 29  ? 6.523   -37.804 32.559  1.00 104.72 ? 29  ASP H CA  1 
ATOM   2205 C  C   . ASP B 2 29  ? 5.680   -36.788 31.787  1.00 102.08 ? 29  ASP H C   1 
ATOM   2206 O  O   . ASP B 2 29  ? 6.095   -36.292 30.742  1.00 99.84  ? 29  ASP H O   1 
ATOM   2207 C  CB  . ASP B 2 29  ? 7.083   -37.215 33.858  1.00 106.35 ? 29  ASP H CB  1 
ATOM   2208 C  CG  . ASP B 2 29  ? 6.083   -37.167 35.002  1.00 109.49 ? 29  ASP H CG  1 
ATOM   2209 O  OD1 . ASP B 2 29  ? 5.623   -38.247 35.423  1.00 112.09 ? 29  ASP H OD1 1 
ATOM   2210 O  OD2 . ASP B 2 29  ? 5.769   -36.051 35.460  1.00 110.26 ? 29  ASP H OD2 1 
ATOM   2211 N  N   . ALA B 2 30  ? 4.487   -36.495 32.322  1.00 102.76 ? 30  ALA H N   1 
ATOM   2212 C  CA  . ALA B 2 30  ? 3.543   -35.577 31.703  1.00 101.05 ? 30  ALA H CA  1 
ATOM   2213 C  C   . ALA B 2 30  ? 3.928   -34.127 31.990  1.00 99.85  ? 30  ALA H C   1 
ATOM   2214 O  O   . ALA B 2 30  ? 3.610   -33.241 31.200  1.00 99.63  ? 30  ALA H O   1 
ATOM   2215 C  CB  . ALA B 2 30  ? 2.147   -35.874 32.195  1.00 103.33 ? 30  ALA H CB  1 
ATOM   2216 N  N   . THR B 2 31  ? 4.584   -33.889 33.135  1.00 100.19 ? 31  THR H N   1 
ATOM   2217 C  CA  . THR B 2 31  ? 5.071   -32.564 33.491  1.00 98.24  ? 31  THR H CA  1 
ATOM   2218 C  C   . THR B 2 31  ? 6.505   -32.398 32.990  1.00 94.40  ? 31  THR H C   1 
ATOM   2219 O  O   . THR B 2 31  ? 7.439   -32.932 33.584  1.00 94.28  ? 31  THR H O   1 
ATOM   2220 C  CB  . THR B 2 31  ? 4.982   -32.318 35.003  1.00 101.48 ? 31  THR H CB  1 
ATOM   2221 O  OG1 . THR B 2 31  ? 5.668   -33.375 35.676  1.00 104.19 ? 31  THR H OG1 1 
ATOM   2222 C  CG2 . THR B 2 31  ? 3.557   -32.240 35.506  1.00 103.65 ? 31  THR H CG2 1 
ATOM   2223 N  N   . TYR B 2 32  ? 6.657   -31.657 31.887  1.00 90.77  ? 32  TYR H N   1 
ATOM   2224 C  CA  . TYR B 2 32  ? 7.958   -31.349 31.315  1.00 88.43  ? 32  TYR H CA  1 
ATOM   2225 C  C   . TYR B 2 32  ? 7.995   -29.867 30.951  1.00 85.89  ? 32  TYR H C   1 
ATOM   2226 O  O   . TYR B 2 32  ? 6.972   -29.187 31.012  1.00 86.97  ? 32  TYR H O   1 
ATOM   2227 C  CB  . TYR B 2 32  ? 8.249   -32.241 30.102  1.00 86.93  ? 32  TYR H CB  1 
ATOM   2228 C  CG  . TYR B 2 32  ? 7.184   -32.238 29.033  1.00 85.58  ? 32  TYR H CG  1 
ATOM   2229 C  CD1 . TYR B 2 32  ? 6.021   -32.977 29.179  1.00 86.57  ? 32  TYR H CD1 1 
ATOM   2230 C  CD2 . TYR B 2 32  ? 7.326   -31.481 27.880  1.00 83.57  ? 32  TYR H CD2 1 
ATOM   2231 C  CE1 . TYR B 2 32  ? 5.033   -32.975 28.207  1.00 85.93  ? 32  TYR H CE1 1 
ATOM   2232 C  CE2 . TYR B 2 32  ? 6.349   -31.468 26.897  1.00 82.96  ? 32  TYR H CE2 1 
ATOM   2233 C  CZ  . TYR B 2 32  ? 5.196   -32.217 27.061  1.00 84.34  ? 32  TYR H CZ  1 
ATOM   2234 O  OH  . TYR B 2 32  ? 4.219   -32.207 26.093  1.00 84.45  ? 32  TYR H OH  1 
ATOM   2235 N  N   . ALA B 2 33  ? 9.186   -29.379 30.583  1.00 83.56  ? 33  ALA H N   1 
ATOM   2236 C  CA  . ALA B 2 33  ? 9.376   -27.988 30.203  1.00 81.28  ? 33  ALA H CA  1 
ATOM   2237 C  C   . ALA B 2 33  ? 10.117  -27.918 28.870  1.00 78.89  ? 33  ALA H C   1 
ATOM   2238 O  O   . ALA B 2 33  ? 11.127  -28.594 28.687  1.00 78.65  ? 33  ALA H O   1 
ATOM   2239 C  CB  . ALA B 2 33  ? 10.129  -27.261 31.290  1.00 82.07  ? 33  ALA H CB  1 
ATOM   2240 N  N   . ILE B 2 34  ? 9.601   -27.092 27.951  1.00 77.36  ? 34  ILE H N   1 
ATOM   2241 C  CA  . ILE B 2 34  ? 10.211  -26.899 26.645  1.00 75.95  ? 34  ILE H CA  1 
ATOM   2242 C  C   . ILE B 2 34  ? 10.690  -25.453 26.544  1.00 75.39  ? 34  ILE H C   1 
ATOM   2243 O  O   . ILE B 2 34  ? 9.883   -24.542 26.375  1.00 75.88  ? 34  ILE H O   1 
ATOM   2244 C  CB  . ILE B 2 34  ? 9.227   -27.258 25.512  1.00 75.64  ? 34  ILE H CB  1 
ATOM   2245 C  CG1 . ILE B 2 34  ? 8.740   -28.708 25.607  1.00 76.57  ? 34  ILE H CG1 1 
ATOM   2246 C  CG2 . ILE B 2 34  ? 9.835   -26.961 24.148  1.00 74.42  ? 34  ILE H CG2 1 
ATOM   2247 C  CD1 . ILE B 2 34  ? 9.826   -29.747 25.432  1.00 76.28  ? 34  ILE H CD1 1 
ATOM   2248 N  N   . GLY B 2 35  ? 12.010  -25.261 26.655  1.00 75.24  ? 35  GLY H N   1 
ATOM   2249 C  CA  . GLY B 2 35  ? 12.623  -23.955 26.477  1.00 74.61  ? 35  GLY H CA  1 
ATOM   2250 C  C   . GLY B 2 35  ? 12.772  -23.600 24.999  1.00 73.03  ? 35  GLY H C   1 
ATOM   2251 O  O   . GLY B 2 35  ? 12.662  -24.468 24.136  1.00 73.55  ? 35  GLY H O   1 
ATOM   2252 N  N   . TRP B 2 36  ? 13.013  -22.312 24.728  1.00 72.32  ? 36  TRP H N   1 
ATOM   2253 C  CA  . TRP B 2 36  ? 13.246  -21.822 23.378  1.00 69.97  ? 36  TRP H CA  1 
ATOM   2254 C  C   . TRP B 2 36  ? 14.437  -20.867 23.383  1.00 68.71  ? 36  TRP H C   1 
ATOM   2255 O  O   . TRP B 2 36  ? 14.476  -19.921 24.166  1.00 68.01  ? 36  TRP H O   1 
ATOM   2256 C  CB  . TRP B 2 36  ? 11.979  -21.162 22.818  1.00 70.17  ? 36  TRP H CB  1 
ATOM   2257 C  CG  . TRP B 2 36  ? 10.948  -22.140 22.344  1.00 70.97  ? 36  TRP H CG  1 
ATOM   2258 C  CD1 . TRP B 2 36  ? 9.922   -22.670 23.072  1.00 72.31  ? 36  TRP H CD1 1 
ATOM   2259 C  CD2 . TRP B 2 36  ? 10.818  -22.687 21.018  1.00 70.53  ? 36  TRP H CD2 1 
ATOM   2260 N  NE1 . TRP B 2 36  ? 9.178   -23.521 22.301  1.00 72.56  ? 36  TRP H NE1 1 
ATOM   2261 C  CE2 . TRP B 2 36  ? 9.700   -23.549 21.035  1.00 71.42  ? 36  TRP H CE2 1 
ATOM   2262 C  CE3 . TRP B 2 36  ? 11.535  -22.539 19.824  1.00 69.44  ? 36  TRP H CE3 1 
ATOM   2263 C  CZ2 . TRP B 2 36  ? 9.287   -24.258 19.906  1.00 70.85  ? 36  TRP H CZ2 1 
ATOM   2264 C  CZ3 . TRP B 2 36  ? 11.127  -23.240 18.709  1.00 69.55  ? 36  TRP H CZ3 1 
ATOM   2265 C  CH2 . TRP B 2 36  ? 10.018  -24.087 18.752  1.00 70.21  ? 36  TRP H CH2 1 
ATOM   2266 N  N   . VAL B 2 37  ? 15.411  -21.155 22.513  1.00 67.94  ? 37  VAL H N   1 
ATOM   2267 C  CA  . VAL B 2 37  ? 16.602  -20.338 22.345  1.00 68.62  ? 37  VAL H CA  1 
ATOM   2268 C  C   . VAL B 2 37  ? 16.794  -20.099 20.851  1.00 67.84  ? 37  VAL H C   1 
ATOM   2269 O  O   . VAL B 2 37  ? 16.572  -21.003 20.050  1.00 68.04  ? 37  VAL H O   1 
ATOM   2270 C  CB  . VAL B 2 37  ? 17.842  -21.016 22.963  1.00 69.41  ? 37  VAL H CB  1 
ATOM   2271 C  CG1 . VAL B 2 37  ? 19.133  -20.290 22.608  1.00 69.73  ? 37  VAL H CG1 1 
ATOM   2272 C  CG2 . VAL B 2 37  ? 17.718  -21.170 24.471  1.00 70.69  ? 37  VAL H CG2 1 
ATOM   2273 N  N   . ARG B 2 38  ? 17.199  -18.879 20.482  1.00 68.28  ? 38  ARG H N   1 
ATOM   2274 C  CA  . ARG B 2 38  ? 17.584  -18.598 19.109  1.00 67.87  ? 38  ARG H CA  1 
ATOM   2275 C  C   . ARG B 2 38  ? 19.064  -18.233 19.083  1.00 67.69  ? 38  ARG H C   1 
ATOM   2276 O  O   . ARG B 2 38  ? 19.603  -17.741 20.073  1.00 67.95  ? 38  ARG H O   1 
ATOM   2277 C  CB  . ARG B 2 38  ? 16.704  -17.502 18.495  1.00 68.84  ? 38  ARG H CB  1 
ATOM   2278 C  CG  . ARG B 2 38  ? 17.063  -16.077 18.894  1.00 69.82  ? 38  ARG H CG  1 
ATOM   2279 C  CD  . ARG B 2 38  ? 16.187  -15.075 18.166  1.00 69.89  ? 38  ARG H CD  1 
ATOM   2280 N  NE  . ARG B 2 38  ? 16.650  -13.702 18.306  1.00 70.58  ? 38  ARG H NE  1 
ATOM   2281 C  CZ  . ARG B 2 38  ? 16.041  -12.648 17.774  1.00 71.40  ? 38  ARG H CZ  1 
ATOM   2282 N  NH1 . ARG B 2 38  ? 14.931  -12.809 17.076  1.00 70.26  ? 38  ARG H NH1 1 
ATOM   2283 N  NH2 . ARG B 2 38  ? 16.535  -11.435 17.954  1.00 73.17  ? 38  ARG H NH2 1 
ATOM   2284 N  N   . GLN B 2 39  ? 19.704  -18.493 17.938  1.00 70.45  ? 39  GLN H N   1 
ATOM   2285 C  CA  . GLN B 2 39  ? 21.108  -18.181 17.741  1.00 71.19  ? 39  GLN H CA  1 
ATOM   2286 C  C   . GLN B 2 39  ? 21.254  -17.338 16.478  1.00 74.57  ? 39  GLN H C   1 
ATOM   2287 O  O   . GLN B 2 39  ? 20.955  -17.806 15.381  1.00 74.92  ? 39  GLN H O   1 
ATOM   2288 C  CB  . GLN B 2 39  ? 21.930  -19.466 17.641  1.00 68.96  ? 39  GLN H CB  1 
ATOM   2289 C  CG  . GLN B 2 39  ? 23.419  -19.243 17.857  1.00 69.29  ? 39  GLN H CG  1 
ATOM   2290 C  CD  . GLN B 2 39  ? 24.196  -20.536 17.863  1.00 68.25  ? 39  GLN H CD  1 
ATOM   2291 O  OE1 . GLN B 2 39  ? 23.758  -21.550 17.324  1.00 66.98  ? 39  GLN H OE1 1 
ATOM   2292 N  NE2 . GLN B 2 39  ? 25.372  -20.501 18.466  1.00 69.09  ? 39  GLN H NE2 1 
ATOM   2293 N  N   . ALA B 2 40  ? 21.701  -16.090 16.658  1.00 77.95  ? 40  ALA H N   1 
ATOM   2294 C  CA  . ALA B 2 40  ? 21.973  -15.187 15.552  1.00 82.07  ? 40  ALA H CA  1 
ATOM   2295 C  C   . ALA B 2 40  ? 23.445  -14.781 15.592  1.00 86.06  ? 40  ALA H C   1 
ATOM   2296 O  O   . ALA B 2 40  ? 24.011  -14.621 16.672  1.00 85.87  ? 40  ALA H O   1 
ATOM   2297 C  CB  . ALA B 2 40  ? 21.065  -13.984 15.639  1.00 83.28  ? 40  ALA H CB  1 
ATOM   2298 N  N   . PRO B 2 41  ? 24.123  -14.631 14.430  1.00 90.68  ? 41  PRO H N   1 
ATOM   2299 C  CA  . PRO B 2 41  ? 25.458  -14.032 14.394  1.00 94.68  ? 41  PRO H CA  1 
ATOM   2300 C  C   . PRO B 2 41  ? 25.420  -12.571 14.840  1.00 98.33  ? 41  PRO H C   1 
ATOM   2301 O  O   . PRO B 2 41  ? 24.636  -11.783 14.315  1.00 99.44  ? 41  PRO H O   1 
ATOM   2302 C  CB  . PRO B 2 41  ? 25.887  -14.150 12.921  1.00 96.64  ? 41  PRO H CB  1 
ATOM   2303 C  CG  . PRO B 2 41  ? 24.980  -15.221 12.346  1.00 93.82  ? 41  PRO H CG  1 
ATOM   2304 C  CD  . PRO B 2 41  ? 23.676  -15.077 13.101  1.00 91.03  ? 41  PRO H CD  1 
ATOM   2305 N  N   . GLY B 2 42  ? 26.266  -12.230 15.821  1.00 100.76 ? 42  GLY H N   1 
ATOM   2306 C  CA  . GLY B 2 42  ? 26.340  -10.881 16.360  1.00 104.79 ? 42  GLY H CA  1 
ATOM   2307 C  C   . GLY B 2 42  ? 25.740  -10.804 17.761  1.00 103.60 ? 42  GLY H C   1 
ATOM   2308 O  O   . GLY B 2 42  ? 26.420  -10.418 18.710  1.00 105.68 ? 42  GLY H O   1 
ATOM   2309 N  N   . GLN B 2 43  ? 24.456  -11.169 17.866  1.00 101.26 ? 43  GLN H N   1 
ATOM   2310 C  CA  . GLN B 2 43  ? 23.759  -11.238 19.141  1.00 99.74  ? 43  GLN H CA  1 
ATOM   2311 C  C   . GLN B 2 43  ? 24.208  -12.488 19.895  1.00 96.38  ? 43  GLN H C   1 
ATOM   2312 O  O   . GLN B 2 43  ? 24.604  -12.405 21.056  1.00 96.78  ? 43  GLN H O   1 
ATOM   2313 C  CB  . GLN B 2 43  ? 22.244  -11.247 18.920  1.00 99.01  ? 43  GLN H CB  1 
ATOM   2314 C  CG  . GLN B 2 43  ? 21.689  -9.913  18.435  1.00 103.08 ? 43  GLN H CG  1 
ATOM   2315 C  CD  . GLN B 2 43  ? 20.248  -9.989  17.988  1.00 102.50 ? 43  GLN H CD  1 
ATOM   2316 O  OE1 . GLN B 2 43  ? 19.708  -11.062 17.724  1.00 101.50 ? 43  GLN H OE1 1 
ATOM   2317 N  NE2 . GLN B 2 43  ? 19.614  -8.833  17.872  1.00 104.68 ? 43  GLN H NE2 1 
ATOM   2318 N  N   . GLY B 2 44  ? 24.141  -13.640 19.216  1.00 93.43  ? 44  GLY H N   1 
ATOM   2319 C  CA  . GLY B 2 44  ? 24.504  -14.920 19.801  1.00 89.72  ? 44  GLY H CA  1 
ATOM   2320 C  C   . GLY B 2 44  ? 23.282  -15.653 20.348  1.00 85.03  ? 44  GLY H C   1 
ATOM   2321 O  O   . GLY B 2 44  ? 22.167  -15.452 19.868  1.00 83.96  ? 44  GLY H O   1 
ATOM   2322 N  N   . LEU B 2 45  ? 23.511  -16.500 21.358  1.00 81.81  ? 45  LEU H N   1 
ATOM   2323 C  CA  . LEU B 2 45  ? 22.451  -17.267 21.993  1.00 77.92  ? 45  LEU H CA  1 
ATOM   2324 C  C   . LEU B 2 45  ? 21.605  -16.343 22.870  1.00 76.44  ? 45  LEU H C   1 
ATOM   2325 O  O   . LEU B 2 45  ? 22.113  -15.756 23.824  1.00 76.87  ? 45  LEU H O   1 
ATOM   2326 C  CB  . LEU B 2 45  ? 23.081  -18.395 22.820  1.00 77.06  ? 45  LEU H CB  1 
ATOM   2327 C  CG  . LEU B 2 45  ? 23.765  -19.507 22.022  1.00 76.00  ? 45  LEU H CG  1 
ATOM   2328 C  CD1 . LEU B 2 45  ? 24.552  -20.428 22.941  1.00 75.61  ? 45  LEU H CD1 1 
ATOM   2329 C  CD2 . LEU B 2 45  ? 22.750  -20.310 21.221  1.00 73.70  ? 45  LEU H CD2 1 
ATOM   2330 N  N   . GLU B 2 46  ? 20.315  -16.223 22.529  1.00 74.14  ? 46  GLU H N   1 
ATOM   2331 C  CA  . GLU B 2 46  ? 19.372  -15.413 23.285  1.00 73.28  ? 46  GLU H CA  1 
ATOM   2332 C  C   . GLU B 2 46  ? 18.258  -16.302 23.832  1.00 70.12  ? 46  GLU H C   1 
ATOM   2333 O  O   . GLU B 2 46  ? 17.627  -17.043 23.081  1.00 67.32  ? 46  GLU H O   1 
ATOM   2334 C  CB  . GLU B 2 46  ? 18.764  -14.316 22.407  1.00 74.58  ? 46  GLU H CB  1 
ATOM   2335 C  CG  . GLU B 2 46  ? 19.745  -13.232 22.005  1.00 78.17  ? 46  GLU H CG  1 
ATOM   2336 C  CD  . GLU B 2 46  ? 19.132  -12.117 21.174  1.00 80.45  ? 46  GLU H CD  1 
ATOM   2337 O  OE1 . GLU B 2 46  ? 18.528  -12.430 20.128  1.00 80.11  ? 46  GLU H OE1 1 
ATOM   2338 O  OE2 . GLU B 2 46  ? 19.262  -10.940 21.572  1.00 82.22  ? 46  GLU H OE2 1 
ATOM   2339 N  N   . TRP B 2 47  ? 18.021  -16.204 25.145  1.00 69.87  ? 47  TRP H N   1 
ATOM   2340 C  CA  . TRP B 2 47  ? 16.899  -16.870 25.786  1.00 68.68  ? 47  TRP H CA  1 
ATOM   2341 C  C   . TRP B 2 47  ? 15.601  -16.174 25.379  1.00 68.53  ? 47  TRP H C   1 
ATOM   2342 O  O   . TRP B 2 47  ? 15.540  -14.946 25.344  1.00 69.66  ? 47  TRP H O   1 
ATOM   2343 C  CB  . TRP B 2 47  ? 17.086  -16.881 27.308  1.00 68.49  ? 47  TRP H CB  1 
ATOM   2344 C  CG  . TRP B 2 47  ? 15.928  -17.446 28.070  1.00 67.39  ? 47  TRP H CG  1 
ATOM   2345 C  CD1 . TRP B 2 47  ? 15.160  -16.793 28.989  1.00 68.52  ? 47  TRP H CD1 1 
ATOM   2346 C  CD2 . TRP B 2 47  ? 15.398  -18.782 27.985  1.00 66.96  ? 47  TRP H CD2 1 
ATOM   2347 N  NE1 . TRP B 2 47  ? 14.194  -17.627 29.482  1.00 67.32  ? 47  TRP H NE1 1 
ATOM   2348 C  CE2 . TRP B 2 47  ? 14.313  -18.853 28.886  1.00 66.72  ? 47  TRP H CE2 1 
ATOM   2349 C  CE3 . TRP B 2 47  ? 15.731  -19.921 27.242  1.00 66.87  ? 47  TRP H CE3 1 
ATOM   2350 C  CZ2 . TRP B 2 47  ? 13.563  -20.016 29.060  1.00 66.34  ? 47  TRP H CZ2 1 
ATOM   2351 C  CZ3 . TRP B 2 47  ? 14.989  -21.069 27.413  1.00 66.51  ? 47  TRP H CZ3 1 
ATOM   2352 C  CH2 . TRP B 2 47  ? 13.921  -21.115 28.312  1.00 66.28  ? 47  TRP H CH2 1 
ATOM   2353 N  N   . MET B 2 48  ? 14.570  -16.975 25.081  1.00 67.62  ? 48  MET H N   1 
ATOM   2354 C  CA  . MET B 2 48  ? 13.299  -16.459 24.596  1.00 68.72  ? 48  MET H CA  1 
ATOM   2355 C  C   . MET B 2 48  ? 12.206  -16.699 25.637  1.00 68.92  ? 48  MET H C   1 
ATOM   2356 O  O   . MET B 2 48  ? 11.538  -15.756 26.056  1.00 69.59  ? 48  MET H O   1 
ATOM   2357 C  CB  . MET B 2 48  ? 12.913  -17.127 23.273  1.00 68.19  ? 48  MET H CB  1 
ATOM   2358 C  CG  . MET B 2 48  ? 13.754  -16.659 22.102  1.00 69.10  ? 48  MET H CG  1 
ATOM   2359 S  SD  . MET B 2 48  ? 13.248  -17.409 20.536  1.00 68.82  ? 48  MET H SD  1 
ATOM   2360 C  CE  . MET B 2 48  ? 11.994  -16.239 20.016  1.00 70.64  ? 48  MET H CE  1 
ATOM   2361 N  N   . GLY B 2 49  ? 12.024  -17.964 26.041  1.00 68.45  ? 49  GLY H N   1 
ATOM   2362 C  CA  . GLY B 2 49  ? 11.030  -18.311 27.045  1.00 68.19  ? 49  GLY H CA  1 
ATOM   2363 C  C   . GLY B 2 49  ? 10.806  -19.818 27.157  1.00 67.31  ? 49  GLY H C   1 
ATOM   2364 O  O   . GLY B 2 49  ? 11.464  -20.599 26.472  1.00 67.27  ? 49  GLY H O   1 
ATOM   2365 N  N   . ARG B 2 50  ? 9.861   -20.203 28.026  1.00 66.92  ? 50  ARG H N   1 
ATOM   2366 C  CA  . ARG B 2 50  ? 9.571   -21.599 28.318  1.00 66.70  ? 50  ARG H CA  1 
ATOM   2367 C  C   . ARG B 2 50  ? 8.075   -21.867 28.170  1.00 67.52  ? 50  ARG H C   1 
ATOM   2368 O  O   . ARG B 2 50  ? 7.291   -20.948 27.938  1.00 66.99  ? 50  ARG H O   1 
ATOM   2369 C  CB  . ARG B 2 50  ? 9.991   -21.947 29.750  1.00 66.75  ? 50  ARG H CB  1 
ATOM   2370 C  CG  . ARG B 2 50  ? 9.194   -21.214 30.821  1.00 67.15  ? 50  ARG H CG  1 
ATOM   2371 C  CD  . ARG B 2 50  ? 9.191   -21.929 32.158  1.00 67.40  ? 50  ARG H CD  1 
ATOM   2372 N  NE  . ARG B 2 50  ? 8.405   -21.225 33.165  1.00 68.11  ? 50  ARG H NE  1 
ATOM   2373 C  CZ  . ARG B 2 50  ? 7.079   -21.133 33.170  1.00 68.90  ? 50  ARG H CZ  1 
ATOM   2374 N  NH1 . ARG B 2 50  ? 6.367   -21.715 32.221  1.00 69.39  ? 50  ARG H NH1 1 
ATOM   2375 N  NH2 . ARG B 2 50  ? 6.467   -20.463 34.131  1.00 69.45  ? 50  ARG H NH2 1 
ATOM   2376 N  N   . ILE B 2 51  ? 7.700   -23.143 28.328  1.00 68.55  ? 51  ILE H N   1 
ATOM   2377 C  CA  . ILE B 2 51  ? 6.307   -23.541 28.465  1.00 70.42  ? 51  ILE H CA  1 
ATOM   2378 C  C   . ILE B 2 51  ? 6.241   -24.828 29.287  1.00 72.18  ? 51  ILE H C   1 
ATOM   2379 O  O   . ILE B 2 51  ? 7.129   -25.672 29.189  1.00 72.03  ? 51  ILE H O   1 
ATOM   2380 C  CB  . ILE B 2 51  ? 5.628   -23.702 27.089  1.00 70.90  ? 51  ILE H CB  1 
ATOM   2381 C  CG1 . ILE B 2 51  ? 4.127   -23.972 27.232  1.00 72.53  ? 51  ILE H CG1 1 
ATOM   2382 C  CG2 . ILE B 2 51  ? 6.316   -24.775 26.256  1.00 71.22  ? 51  ILE H CG2 1 
ATOM   2383 C  CD1 . ILE B 2 51  ? 3.363   -23.926 25.930  1.00 73.79  ? 51  ILE H CD1 1 
ATOM   2384 N  N   . ILE B 2 52  ? 5.184   -24.949 30.104  1.00 74.28  ? 52  ILE H N   1 
ATOM   2385 C  CA  . ILE B 2 52  ? 4.872   -26.175 30.825  1.00 76.98  ? 52  ILE H CA  1 
ATOM   2386 C  C   . ILE B 2 52  ? 3.515   -26.670 30.328  1.00 80.78  ? 52  ILE H C   1 
ATOM   2387 O  O   . ILE B 2 52  ? 2.482   -26.312 30.891  1.00 82.28  ? 52  ILE H O   1 
ATOM   2388 C  CB  . ILE B 2 52  ? 4.870   -25.951 32.353  1.00 77.00  ? 52  ILE H CB  1 
ATOM   2389 C  CG1 . ILE B 2 52  ? 6.129   -25.231 32.847  1.00 74.41  ? 52  ILE H CG1 1 
ATOM   2390 C  CG2 . ILE B 2 52  ? 4.658   -27.269 33.084  1.00 79.44  ? 52  ILE H CG2 1 
ATOM   2391 C  CD1 . ILE B 2 52  ? 7.385   -26.067 32.790  1.00 74.56  ? 52  ILE H CD1 1 
ATOM   2392 N  N   . PRO B 2 53  A 3.470   -27.500 29.258  1.00 83.10  ? 52  PRO H N   1 
ATOM   2393 C  CA  . PRO B 2 53  A 2.213   -27.843 28.585  1.00 86.71  ? 52  PRO H CA  1 
ATOM   2394 C  C   . PRO B 2 53  A 1.031   -28.232 29.474  1.00 90.37  ? 52  PRO H C   1 
ATOM   2395 O  O   . PRO B 2 53  A -0.104  -27.878 29.162  1.00 92.57  ? 52  PRO H O   1 
ATOM   2396 C  CB  . PRO B 2 53  A 2.628   -29.031 27.705  1.00 88.07  ? 52  PRO H CB  1 
ATOM   2397 C  CG  . PRO B 2 53  A 4.059   -28.717 27.343  1.00 84.14  ? 52  PRO H CG  1 
ATOM   2398 C  CD  . PRO B 2 53  A 4.635   -28.131 28.615  1.00 82.00  ? 52  PRO H CD  1 
ATOM   2399 N  N   . ARG B 2 54  ? 1.296   -28.958 30.571  1.00 92.67  ? 53  ARG H N   1 
ATOM   2400 C  CA  . ARG B 2 54  ? 0.240   -29.383 31.480  1.00 96.58  ? 53  ARG H CA  1 
ATOM   2401 C  C   . ARG B 2 54  ? -0.368  -28.166 32.175  1.00 95.14  ? 53  ARG H C   1 
ATOM   2402 O  O   . ARG B 2 54  ? -1.584  -27.989 32.164  1.00 97.70  ? 53  ARG H O   1 
ATOM   2403 C  CB  . ARG B 2 54  ? 0.758   -30.400 32.506  1.00 98.94  ? 53  ARG H CB  1 
ATOM   2404 C  CG  . ARG B 2 54  ? -0.163  -30.592 33.704  1.00 102.81 ? 53  ARG H CG  1 
ATOM   2405 C  CD  . ARG B 2 54  ? 0.057   -31.883 34.470  1.00 106.67 ? 53  ARG H CD  1 
ATOM   2406 N  NE  . ARG B 2 54  ? -0.729  -32.990 33.938  1.00 111.58 ? 53  ARG H NE  1 
ATOM   2407 C  CZ  . ARG B 2 54  ? -0.908  -34.155 34.553  1.00 115.70 ? 53  ARG H CZ  1 
ATOM   2408 N  NH1 . ARG B 2 54  ? -0.341  -34.384 35.725  1.00 116.00 ? 53  ARG H NH1 1 
ATOM   2409 N  NH2 . ARG B 2 54  ? -1.659  -35.089 33.994  1.00 119.62 ? 53  ARG H NH2 1 
ATOM   2410 N  N   . LEU B 2 55  ? 0.494   -27.337 32.777  1.00 91.86  ? 54  LEU H N   1 
ATOM   2411 C  CA  . LEU B 2 55  ? 0.062   -26.149 33.498  1.00 90.98  ? 54  LEU H CA  1 
ATOM   2412 C  C   . LEU B 2 55  ? -0.431  -25.078 32.524  1.00 90.57  ? 54  LEU H C   1 
ATOM   2413 O  O   . LEU B 2 55  ? -1.202  -24.205 32.917  1.00 92.17  ? 54  LEU H O   1 
ATOM   2414 C  CB  . LEU B 2 55  ? 1.227   -25.620 34.341  1.00 88.58  ? 54  LEU H CB  1 
ATOM   2415 C  CG  . LEU B 2 55  ? 1.428   -26.287 35.702  1.00 90.39  ? 54  LEU H CG  1 
ATOM   2416 C  CD1 . LEU B 2 55  ? 1.896   -27.727 35.557  1.00 92.57  ? 54  LEU H CD1 1 
ATOM   2417 C  CD2 . LEU B 2 55  ? 2.416   -25.494 36.544  1.00 88.45  ? 54  LEU H CD2 1 
ATOM   2418 N  N   . ASP B 2 56  ? 0.026   -25.151 31.265  1.00 89.17  ? 55  ASP H N   1 
ATOM   2419 C  CA  . ASP B 2 56  ? -0.225  -24.118 30.271  1.00 87.91  ? 55  ASP H CA  1 
ATOM   2420 C  C   . ASP B 2 56  ? 0.396   -22.814 30.768  1.00 85.24  ? 55  ASP H C   1 
ATOM   2421 O  O   . ASP B 2 56  ? -0.213  -21.750 30.674  1.00 85.43  ? 55  ASP H O   1 
ATOM   2422 C  CB  . ASP B 2 56  ? -1.721  -23.982 29.967  1.00 90.78  ? 55  ASP H CB  1 
ATOM   2423 C  CG  . ASP B 2 56  ? -2.025  -23.311 28.637  1.00 91.88  ? 55  ASP H CG  1 
ATOM   2424 O  OD1 . ASP B 2 56  ? -1.497  -22.205 28.397  1.00 89.06  ? 55  ASP H OD1 1 
ATOM   2425 O  OD2 . ASP B 2 56  ? -2.787  -23.904 27.847  1.00 95.85  ? 55  ASP H OD2 1 
ATOM   2426 N  N   . ALA B 2 57  ? 1.618   -22.921 31.304  1.00 82.79  ? 56  ALA H N   1 
ATOM   2427 C  CA  . ALA B 2 57  ? 2.317   -21.793 31.896  1.00 80.97  ? 56  ALA H CA  1 
ATOM   2428 C  C   . ALA B 2 57  ? 3.457   -21.370 30.975  1.00 78.37  ? 56  ALA H C   1 
ATOM   2429 O  O   . ALA B 2 57  ? 4.256   -22.204 30.557  1.00 76.89  ? 56  ALA H O   1 
ATOM   2430 C  CB  . ALA B 2 57  ? 2.828   -22.169 33.265  1.00 81.17  ? 56  ALA H CB  1 
ATOM   2431 N  N   . GLU B 2 58  ? 3.512   -20.070 30.664  1.00 77.23  ? 57  GLU H N   1 
ATOM   2432 C  CA  . GLU B 2 58  ? 4.562   -19.512 29.829  1.00 75.67  ? 57  GLU H CA  1 
ATOM   2433 C  C   . GLU B 2 58  ? 5.278   -18.407 30.601  1.00 74.16  ? 57  GLU H C   1 
ATOM   2434 O  O   . GLU B 2 58  ? 4.670   -17.718 31.417  1.00 75.55  ? 57  GLU H O   1 
ATOM   2435 C  CB  . GLU B 2 58  ? 3.988   -18.970 28.518  1.00 77.25  ? 57  GLU H CB  1 
ATOM   2436 C  CG  . GLU B 2 58  ? 3.300   -20.023 27.664  1.00 79.11  ? 57  GLU H CG  1 
ATOM   2437 C  CD  . GLU B 2 58  ? 1.933   -20.475 28.152  1.00 81.94  ? 57  GLU H CD  1 
ATOM   2438 O  OE1 . GLU B 2 58  ? 1.375   -19.809 29.047  1.00 83.39  ? 57  GLU H OE1 1 
ATOM   2439 O  OE2 . GLU B 2 58  ? 1.437   -21.503 27.648  1.00 83.97  ? 57  GLU H OE2 1 
ATOM   2440 N  N   . HIS B 2 59  ? 6.578   -18.259 30.330  1.00 72.16  ? 58  HIS H N   1 
ATOM   2441 C  CA  . HIS B 2 59  ? 7.385   -17.201 30.913  1.00 70.83  ? 58  HIS H CA  1 
ATOM   2442 C  C   . HIS B 2 59  ? 8.366   -16.726 29.847  1.00 71.38  ? 58  HIS H C   1 
ATOM   2443 O  O   . HIS B 2 59  ? 9.170   -17.516 29.359  1.00 72.18  ? 58  HIS H O   1 
ATOM   2444 C  CB  . HIS B 2 59  ? 8.091   -17.709 32.175  1.00 68.55  ? 58  HIS H CB  1 
ATOM   2445 C  CG  . HIS B 2 59  ? 8.715   -16.639 33.009  1.00 67.54  ? 58  HIS H CG  1 
ATOM   2446 N  ND1 . HIS B 2 59  ? 9.532   -16.927 34.080  1.00 66.35  ? 58  HIS H ND1 1 
ATOM   2447 C  CD2 . HIS B 2 59  ? 8.657   -15.303 32.936  1.00 67.79  ? 58  HIS H CD2 1 
ATOM   2448 C  CE1 . HIS B 2 59  ? 9.941   -15.795 34.634  1.00 67.03  ? 58  HIS H CE1 1 
ATOM   2449 N  NE2 . HIS B 2 59  ? 9.422   -14.796 33.955  1.00 67.85  ? 58  HIS H NE2 1 
ATOM   2450 N  N   . TYR B 2 60  ? 8.282   -15.440 29.484  1.00 72.93  ? 59  TYR H N   1 
ATOM   2451 C  CA  . TYR B 2 60  ? 9.041   -14.902 28.366  1.00 74.35  ? 59  TYR H CA  1 
ATOM   2452 C  C   . TYR B 2 60  ? 10.110  -13.940 28.873  1.00 75.46  ? 59  TYR H C   1 
ATOM   2453 O  O   . TYR B 2 60  ? 10.004  -13.418 29.979  1.00 76.37  ? 59  TYR H O   1 
ATOM   2454 C  CB  . TYR B 2 60  ? 8.106   -14.193 27.383  1.00 75.96  ? 59  TYR H CB  1 
ATOM   2455 C  CG  . TYR B 2 60  ? 6.933   -15.023 26.928  1.00 76.67  ? 59  TYR H CG  1 
ATOM   2456 C  CD1 . TYR B 2 60  ? 7.120   -16.205 26.230  1.00 75.99  ? 59  TYR H CD1 1 
ATOM   2457 C  CD2 . TYR B 2 60  ? 5.631   -14.633 27.204  1.00 79.18  ? 59  TYR H CD2 1 
ATOM   2458 C  CE1 . TYR B 2 60  ? 6.046   -16.975 25.812  1.00 76.95  ? 59  TYR H CE1 1 
ATOM   2459 C  CE2 . TYR B 2 60  ? 4.546   -15.391 26.792  1.00 79.54  ? 59  TYR H CE2 1 
ATOM   2460 C  CZ  . TYR B 2 60  ? 4.755   -16.566 26.093  1.00 78.69  ? 59  TYR H CZ  1 
ATOM   2461 O  OH  . TYR B 2 60  ? 3.685   -17.323 25.684  1.00 80.40  ? 59  TYR H OH  1 
ATOM   2462 N  N   . ALA B 2 61  ? 11.139  -13.724 28.044  1.00 76.86  ? 60  ALA H N   1 
ATOM   2463 C  CA  . ALA B 2 61  ? 12.136  -12.694 28.286  1.00 79.50  ? 60  ALA H CA  1 
ATOM   2464 C  C   . ALA B 2 61  ? 11.573  -11.346 27.842  1.00 82.50  ? 60  ALA H C   1 
ATOM   2465 O  O   . ALA B 2 61  ? 10.822  -11.279 26.871  1.00 83.02  ? 60  ALA H O   1 
ATOM   2466 C  CB  . ALA B 2 61  ? 13.412  -13.031 27.553  1.00 79.63  ? 60  ALA H CB  1 
ATOM   2467 N  N   . GLN B 2 62  ? 11.954  -10.277 28.554  1.00 99.03  ? 61  GLN H N   1 
ATOM   2468 C  CA  . GLN B 2 62  ? 11.378  -8.957  28.344  1.00 100.65 ? 61  GLN H CA  1 
ATOM   2469 C  C   . GLN B 2 62  ? 11.626  -8.489  26.910  1.00 99.00  ? 61  GLN H C   1 
ATOM   2470 O  O   . GLN B 2 62  ? 10.781  -7.807  26.334  1.00 98.71  ? 61  GLN H O   1 
ATOM   2471 C  CB  . GLN B 2 62  ? 11.915  -7.948  29.369  1.00 105.76 ? 61  GLN H CB  1 
ATOM   2472 C  CG  . GLN B 2 62  ? 13.316  -7.407  29.086  1.00 107.79 ? 61  GLN H CG  1 
ATOM   2473 C  CD  . GLN B 2 62  ? 14.423  -8.411  29.306  1.00 107.93 ? 61  GLN H CD  1 
ATOM   2474 O  OE1 . GLN B 2 62  ? 14.208  -9.500  29.832  1.00 108.76 ? 61  GLN H OE1 1 
ATOM   2475 N  NE2 . GLN B 2 62  ? 15.631  -8.040  28.914  1.00 108.02 ? 61  GLN H NE2 1 
ATOM   2476 N  N   . LYS B 2 63  ? 12.781  -8.867  26.343  1.00 98.49  ? 62  LYS H N   1 
ATOM   2477 C  CA  . LYS B 2 63  ? 13.199  -8.406  25.028  1.00 97.67  ? 62  LYS H CA  1 
ATOM   2478 C  C   . LYS B 2 63  ? 12.197  -8.842  23.960  1.00 93.88  ? 62  LYS H C   1 
ATOM   2479 O  O   . LYS B 2 63  ? 11.871  -8.065  23.066  1.00 93.43  ? 62  LYS H O   1 
ATOM   2480 C  CB  . LYS B 2 63  ? 14.601  -8.936  24.701  1.00 98.99  ? 62  LYS H CB  1 
ATOM   2481 C  CG  . LYS B 2 63  ? 15.191  -8.448  23.383  1.00 99.50  ? 62  LYS H CG  1 
ATOM   2482 C  CD  . LYS B 2 63  ? 16.624  -8.884  23.154  1.00 100.90 ? 62  LYS H CD  1 
ATOM   2483 C  CE  . LYS B 2 63  ? 17.219  -8.331  21.876  1.00 101.16 ? 62  LYS H CE  1 
ATOM   2484 N  NZ  . LYS B 2 63  ? 16.535  -8.857  20.671  1.00 98.16  ? 62  LYS H NZ  1 
ATOM   2485 N  N   . PHE B 2 64  ? 11.719  -10.088 24.057  1.00 92.30  ? 63  PHE H N   1 
ATOM   2486 C  CA  . PHE B 2 64  ? 10.873  -10.673 23.028  1.00 90.76  ? 63  PHE H CA  1 
ATOM   2487 C  C   . PHE B 2 64  ? 9.394   -10.540 23.382  1.00 92.21  ? 63  PHE H C   1 
ATOM   2488 O  O   . PHE B 2 64  ? 8.543   -10.624 22.497  1.00 91.31  ? 63  PHE H O   1 
ATOM   2489 C  CB  . PHE B 2 64  ? 11.221  -12.148 22.824  1.00 88.45  ? 63  PHE H CB  1 
ATOM   2490 C  CG  . PHE B 2 64  ? 12.645  -12.404 22.404  1.00 88.38  ? 63  PHE H CG  1 
ATOM   2491 C  CD1 . PHE B 2 64  ? 13.675  -12.394 23.333  1.00 90.46  ? 63  PHE H CD1 1 
ATOM   2492 C  CD2 . PHE B 2 64  ? 12.957  -12.631 21.072  1.00 86.88  ? 63  PHE H CD2 1 
ATOM   2493 C  CE1 . PHE B 2 64  ? 14.985  -12.623 22.941  1.00 91.60  ? 63  PHE H CE1 1 
ATOM   2494 C  CE2 . PHE B 2 64  ? 14.268  -12.858 20.682  1.00 88.31  ? 63  PHE H CE2 1 
ATOM   2495 C  CZ  . PHE B 2 64  ? 15.279  -12.853 21.616  1.00 90.79  ? 63  PHE H CZ  1 
ATOM   2496 N  N   . GLN B 2 65  ? 9.096   -10.339 24.674  1.00 94.92  ? 64  GLN H N   1 
ATOM   2497 C  CA  . GLN B 2 65  ? 7.728   -10.367 25.166  1.00 95.46  ? 64  GLN H CA  1 
ATOM   2498 C  C   . GLN B 2 65  ? 6.887   -9.349  24.400  1.00 95.51  ? 64  GLN H C   1 
ATOM   2499 O  O   . GLN B 2 65  ? 7.321   -8.220  24.174  1.00 96.50  ? 64  GLN H O   1 
ATOM   2500 C  CB  . GLN B 2 65  ? 7.695   -10.099 26.672  1.00 98.81  ? 64  GLN H CB  1 
ATOM   2501 C  CG  . GLN B 2 65  ? 6.344   -10.389 27.312  1.00 99.61  ? 64  GLN H CG  1 
ATOM   2502 C  CD  . GLN B 2 65  ? 6.412   -10.423 28.819  1.00 102.19 ? 64  GLN H CD  1 
ATOM   2503 O  OE1 . GLN B 2 65  ? 7.427   -10.085 29.425  1.00 103.50 ? 64  GLN H OE1 1 
ATOM   2504 N  NE2 . GLN B 2 65  ? 5.318   -10.834 29.439  1.00 103.75 ? 64  GLN H NE2 1 
ATOM   2505 N  N   . GLY B 2 66  ? 5.682   -9.776  24.002  1.00 93.46  ? 65  GLY H N   1 
ATOM   2506 C  CA  . GLY B 2 66  ? 4.820   -8.993  23.133  1.00 93.20  ? 65  GLY H CA  1 
ATOM   2507 C  C   . GLY B 2 66  ? 4.743   -9.597  21.734  1.00 90.78  ? 65  GLY H C   1 
ATOM   2508 O  O   . GLY B 2 66  ? 3.669   -9.633  21.132  1.00 92.71  ? 65  GLY H O   1 
ATOM   2509 N  N   . ARG B 2 67  ? 5.894   -10.066 21.231  1.00 87.73  ? 66  ARG H N   1 
ATOM   2510 C  CA  . ARG B 2 67  ? 5.984   -10.660 19.907  1.00 85.34  ? 66  ARG H CA  1 
ATOM   2511 C  C   . ARG B 2 67  ? 5.927   -12.184 20.011  1.00 85.69  ? 66  ARG H C   1 
ATOM   2512 O  O   . ARG B 2 67  ? 5.337   -12.836 19.151  1.00 85.83  ? 66  ARG H O   1 
ATOM   2513 C  CB  . ARG B 2 67  ? 7.264   -10.188 19.210  1.00 83.65  ? 66  ARG H CB  1 
ATOM   2514 C  CG  . ARG B 2 67  ? 7.437   -8.675  19.216  1.00 84.49  ? 66  ARG H CG  1 
ATOM   2515 C  CD  . ARG B 2 67  ? 8.372   -8.155  18.141  1.00 83.48  ? 66  ARG H CD  1 
ATOM   2516 N  NE  . ARG B 2 67  ? 9.736   -8.651  18.273  1.00 82.10  ? 66  ARG H NE  1 
ATOM   2517 C  CZ  . ARG B 2 67  ? 10.447  -9.194  17.289  1.00 79.70  ? 66  ARG H CZ  1 
ATOM   2518 N  NH1 . ARG B 2 67  ? 9.925   -9.332  16.084  1.00 78.48  ? 66  ARG H NH1 1 
ATOM   2519 N  NH2 . ARG B 2 67  ? 11.685  -9.598  17.516  1.00 79.06  ? 66  ARG H NH2 1 
ATOM   2520 N  N   . VAL B 2 68  ? 6.538   -12.740 21.067  1.00 86.98  ? 67  VAL H N   1 
ATOM   2521 C  CA  . VAL B 2 68  ? 6.631   -14.181 21.247  1.00 85.48  ? 67  VAL H CA  1 
ATOM   2522 C  C   . VAL B 2 68  ? 5.405   -14.685 22.005  1.00 86.25  ? 67  VAL H C   1 
ATOM   2523 O  O   . VAL B 2 68  ? 5.018   -14.110 23.021  1.00 90.11  ? 67  VAL H O   1 
ATOM   2524 C  CB  . VAL B 2 68  ? 7.935   -14.571 21.971  1.00 85.58  ? 67  VAL H CB  1 
ATOM   2525 C  CG1 . VAL B 2 68  ? 7.877   -15.974 22.560  1.00 85.51  ? 67  VAL H CG1 1 
ATOM   2526 C  CG2 . VAL B 2 68  ? 9.137   -14.429 21.053  1.00 85.81  ? 67  VAL H CG2 1 
ATOM   2527 N  N   . THR B 2 69  ? 4.811   -15.770 21.489  1.00 84.98  ? 68  THR H N   1 
ATOM   2528 C  CA  . THR B 2 69  ? 3.804   -16.538 22.204  1.00 84.69  ? 68  THR H CA  1 
ATOM   2529 C  C   . THR B 2 69  ? 4.077   -18.024 21.983  1.00 82.22  ? 68  THR H C   1 
ATOM   2530 O  O   . THR B 2 69  ? 4.055   -18.497 20.848  1.00 80.44  ? 68  THR H O   1 
ATOM   2531 C  CB  . THR B 2 69  ? 2.383   -16.160 21.765  1.00 85.85  ? 68  THR H CB  1 
ATOM   2532 O  OG1 . THR B 2 69  ? 2.245   -16.450 20.374  1.00 85.75  ? 68  THR H OG1 1 
ATOM   2533 C  CG2 . THR B 2 69  ? 2.051   -14.705 22.019  1.00 87.89  ? 68  THR H CG2 1 
ATOM   2534 N  N   . ILE B 2 70  ? 4.351   -18.742 23.079  1.00 81.58  ? 69  ILE H N   1 
ATOM   2535 C  CA  . ILE B 2 70  ? 4.613   -20.171 23.033  1.00 79.91  ? 69  ILE H CA  1 
ATOM   2536 C  C   . ILE B 2 70  ? 3.328   -20.904 23.412  1.00 80.67  ? 69  ILE H C   1 
ATOM   2537 O  O   . ILE B 2 70  ? 2.773   -20.672 24.484  1.00 81.77  ? 69  ILE H O   1 
ATOM   2538 C  CB  . ILE B 2 70  ? 5.789   -20.544 23.962  1.00 79.69  ? 69  ILE H CB  1 
ATOM   2539 C  CG1 . ILE B 2 70  ? 7.061   -19.767 23.609  1.00 79.56  ? 69  ILE H CG1 1 
ATOM   2540 C  CG2 . ILE B 2 70  ? 6.038   -22.046 23.956  1.00 79.04  ? 69  ILE H CG2 1 
ATOM   2541 C  CD1 . ILE B 2 70  ? 8.127   -19.813 24.681  1.00 80.79  ? 69  ILE H CD1 1 
ATOM   2542 N  N   . THR B 2 71  ? 2.860   -21.775 22.509  1.00 79.69  ? 70  THR H N   1 
ATOM   2543 C  CA  . THR B 2 71  ? 1.717   -22.638 22.763  1.00 80.24  ? 70  THR H CA  1 
ATOM   2544 C  C   . THR B 2 71  ? 2.188   -24.090 22.709  1.00 80.55  ? 70  THR H C   1 
ATOM   2545 O  O   . THR B 2 71  ? 3.352   -24.352 22.412  1.00 80.65  ? 70  THR H O   1 
ATOM   2546 C  CB  . THR B 2 71  ? 0.581   -22.333 21.778  1.00 79.74  ? 70  THR H CB  1 
ATOM   2547 O  OG1 . THR B 2 71  ? 1.057   -22.546 20.449  1.00 78.24  ? 70  THR H OG1 1 
ATOM   2548 C  CG2 . THR B 2 71  ? 0.060   -20.918 21.906  1.00 79.80  ? 70  THR H CG2 1 
ATOM   2549 N  N   . ALA B 2 72  ? 1.284   -25.029 23.016  1.00 82.27  ? 71  ALA H N   1 
ATOM   2550 C  CA  . ALA B 2 72  ? 1.628   -26.442 23.020  1.00 82.93  ? 71  ALA H CA  1 
ATOM   2551 C  C   . ALA B 2 72  ? 0.372   -27.300 22.885  1.00 85.11  ? 71  ALA H C   1 
ATOM   2552 O  O   . ALA B 2 72  ? -0.667  -26.983 23.461  1.00 87.33  ? 71  ALA H O   1 
ATOM   2553 C  CB  . ALA B 2 72  ? 2.385   -26.782 24.281  1.00 83.28  ? 71  ALA H CB  1 
ATOM   2554 N  N   . ASP B 2 73  ? 0.496   -28.384 22.109  1.00 86.22  ? 72  ASP H N   1 
ATOM   2555 C  CA  . ASP B 2 73  ? -0.513  -29.428 22.035  1.00 88.09  ? 72  ASP H CA  1 
ATOM   2556 C  C   . ASP B 2 73  ? -0.035  -30.597 22.895  1.00 88.31  ? 72  ASP H C   1 
ATOM   2557 O  O   . ASP B 2 73  ? 0.958   -31.244 22.568  1.00 87.27  ? 72  ASP H O   1 
ATOM   2558 C  CB  . ASP B 2 73  ? -0.765  -29.836 20.581  1.00 89.56  ? 72  ASP H CB  1 
ATOM   2559 C  CG  . ASP B 2 73  ? -1.909  -30.818 20.398  1.00 93.15  ? 72  ASP H CG  1 
ATOM   2560 O  OD1 . ASP B 2 73  ? -1.806  -31.945 20.923  1.00 95.27  ? 72  ASP H OD1 1 
ATOM   2561 O  OD2 . ASP B 2 73  ? -2.894  -30.450 19.728  1.00 95.87  ? 72  ASP H OD2 1 
ATOM   2562 N  N   . GLU B 2 74  ? -0.755  -30.855 23.994  1.00 89.04  ? 73  GLU H N   1 
ATOM   2563 C  CA  . GLU B 2 74  ? -0.282  -31.749 25.040  1.00 89.43  ? 73  GLU H CA  1 
ATOM   2564 C  C   . GLU B 2 74  ? -0.405  -33.207 24.595  1.00 89.66  ? 73  GLU H C   1 
ATOM   2565 O  O   . GLU B 2 74  ? 0.380   -34.048 25.028  1.00 89.86  ? 73  GLU H O   1 
ATOM   2566 C  CB  . GLU B 2 74  ? -1.056  -31.490 26.334  1.00 91.19  ? 73  GLU H CB  1 
ATOM   2567 C  CG  . GLU B 2 74  ? -0.410  -32.106 27.564  1.00 93.08  ? 73  GLU H CG  1 
ATOM   2568 C  CD  . GLU B 2 74  ? -1.081  -31.766 28.885  1.00 95.45  ? 73  GLU H CD  1 
ATOM   2569 O  OE1 . GLU B 2 74  ? -0.590  -32.238 29.932  1.00 96.69  ? 73  GLU H OE1 1 
ATOM   2570 O  OE2 . GLU B 2 74  ? -2.090  -31.031 28.869  1.00 95.51  ? 73  GLU H OE2 1 
ATOM   2571 N  N   . SER B 2 75  ? -1.388  -33.495 23.730  1.00 89.14  ? 74  SER H N   1 
ATOM   2572 C  CA  . SER B 2 75  ? -1.641  -34.851 23.269  1.00 89.78  ? 74  SER H CA  1 
ATOM   2573 C  C   . SER B 2 75  ? -0.539  -35.313 22.316  1.00 89.28  ? 74  SER H C   1 
ATOM   2574 O  O   . SER B 2 75  ? -0.008  -36.410 22.476  1.00 91.20  ? 74  SER H O   1 
ATOM   2575 C  CB  . SER B 2 75  ? -3.004  -34.963 22.631  1.00 90.03  ? 74  SER H CB  1 
ATOM   2576 O  OG  . SER B 2 75  ? -3.113  -34.106 21.506  1.00 87.68  ? 74  SER H OG  1 
ATOM   2577 N  N   . THR B 2 76  ? -0.196  -34.466 21.334  1.00 87.55  ? 75  THR H N   1 
ATOM   2578 C  CA  . THR B 2 76  ? 0.803   -34.805 20.329  1.00 86.40  ? 75  THR H CA  1 
ATOM   2579 C  C   . THR B 2 76  ? 2.216   -34.543 20.852  1.00 85.29  ? 75  THR H C   1 
ATOM   2580 O  O   . THR B 2 76  ? 3.186   -34.886 20.180  1.00 84.71  ? 75  THR H O   1 
ATOM   2581 C  CB  . THR B 2 76  ? 0.563   -34.044 19.017  1.00 84.91  ? 75  THR H CB  1 
ATOM   2582 O  OG1 . THR B 2 76  ? 0.649   -32.639 19.260  1.00 82.51  ? 75  THR H OG1 1 
ATOM   2583 C  CG2 . THR B 2 76  ? -0.777  -34.361 18.389  1.00 86.15  ? 75  THR H CG2 1 
ATOM   2584 N  N   . SER B 2 77  ? 2.325   -33.930 22.041  1.00 85.93  ? 76  SER H N   1 
ATOM   2585 C  CA  . SER B 2 77  ? 3.607   -33.623 22.660  1.00 87.10  ? 76  SER H CA  1 
ATOM   2586 C  C   . SER B 2 77  ? 4.407   -32.671 21.772  1.00 86.45  ? 76  SER H C   1 
ATOM   2587 O  O   . SER B 2 77  ? 5.611   -32.848 21.593  1.00 86.62  ? 76  SER H O   1 
ATOM   2588 C  CB  . SER B 2 77  ? 4.389   -34.881 22.968  1.00 88.49  ? 76  SER H CB  1 
ATOM   2589 O  OG  . SER B 2 77  ? 3.600   -35.805 23.701  1.00 90.81  ? 76  SER H OG  1 
ATOM   2590 N  N   . THR B 2 78  ? 3.721   -31.654 21.234  1.00 85.77  ? 77  THR H N   1 
ATOM   2591 C  CA  . THR B 2 78  ? 4.316   -30.721 20.292  1.00 84.67  ? 77  THR H CA  1 
ATOM   2592 C  C   . THR B 2 78  ? 4.182   -29.302 20.837  1.00 84.26  ? 77  THR H C   1 
ATOM   2593 O  O   . THR B 2 78  ? 3.071   -28.833 21.073  1.00 83.89  ? 77  THR H O   1 
ATOM   2594 C  CB  . THR B 2 78  ? 3.663   -30.835 18.907  1.00 84.31  ? 77  THR H CB  1 
ATOM   2595 O  OG1 . THR B 2 78  ? 3.681   -32.206 18.508  1.00 85.85  ? 77  THR H OG1 1 
ATOM   2596 C  CG2 . THR B 2 78  ? 4.353   -29.992 17.857  1.00 82.84  ? 77  THR H CG2 1 
ATOM   2597 N  N   . ALA B 2 79  ? 5.326   -28.634 21.032  1.00 84.74  ? 78  ALA H N   1 
ATOM   2598 C  CA  . ALA B 2 79  ? 5.357   -27.233 21.420  1.00 83.84  ? 78  ALA H CA  1 
ATOM   2599 C  C   . ALA B 2 79  ? 5.482   -26.367 20.169  1.00 82.71  ? 78  ALA H C   1 
ATOM   2600 O  O   . ALA B 2 79  ? 6.130   -26.762 19.201  1.00 82.16  ? 78  ALA H O   1 
ATOM   2601 C  CB  . ALA B 2 79  ? 6.496   -26.986 22.379  1.00 84.22  ? 78  ALA H CB  1 
ATOM   2602 N  N   . TYR B 2 80  ? 4.846   -25.190 20.206  1.00 82.35  ? 79  TYR H N   1 
ATOM   2603 C  CA  . TYR B 2 80  ? 4.904   -24.228 19.117  1.00 82.78  ? 79  TYR H CA  1 
ATOM   2604 C  C   . TYR B 2 80  ? 5.374   -22.883 19.662  1.00 84.03  ? 79  TYR H C   1 
ATOM   2605 O  O   . TYR B 2 80  ? 5.073   -22.540 20.803  1.00 86.10  ? 79  TYR H O   1 
ATOM   2606 C  CB  . TYR B 2 80  ? 3.530   -24.073 18.460  1.00 82.48  ? 79  TYR H CB  1 
ATOM   2607 C  CG  . TYR B 2 80  ? 2.927   -25.351 17.936  1.00 82.96  ? 79  TYR H CG  1 
ATOM   2608 C  CD1 . TYR B 2 80  ? 3.419   -25.959 16.792  1.00 83.39  ? 79  TYR H CD1 1 
ATOM   2609 C  CD2 . TYR B 2 80  ? 1.868   -25.962 18.589  1.00 83.92  ? 79  TYR H CD2 1 
ATOM   2610 C  CE1 . TYR B 2 80  ? 2.870   -27.134 16.305  1.00 84.52  ? 79  TYR H CE1 1 
ATOM   2611 C  CE2 . TYR B 2 80  ? 1.309   -27.138 18.118  1.00 84.80  ? 79  TYR H CE2 1 
ATOM   2612 C  CZ  . TYR B 2 80  ? 1.812   -27.727 16.971  1.00 85.06  ? 79  TYR H CZ  1 
ATOM   2613 O  OH  . TYR B 2 80  ? 1.265   -28.893 16.496  1.00 87.18  ? 79  TYR H OH  1 
ATOM   2614 N  N   . MET B 2 81  ? 6.111   -22.130 18.838  1.00 84.50  ? 80  MET H N   1 
ATOM   2615 C  CA  . MET B 2 81  ? 6.469   -20.760 19.165  1.00 85.16  ? 80  MET H CA  1 
ATOM   2616 C  C   . MET B 2 81  ? 6.161   -19.874 17.962  1.00 84.58  ? 80  MET H C   1 
ATOM   2617 O  O   . MET B 2 81  ? 6.639   -20.141 16.862  1.00 84.73  ? 80  MET H O   1 
ATOM   2618 C  CB  . MET B 2 81  ? 7.957   -20.631 19.502  1.00 85.89  ? 80  MET H CB  1 
ATOM   2619 C  CG  . MET B 2 81  ? 8.381   -19.199 19.787  1.00 86.62  ? 80  MET H CG  1 
ATOM   2620 S  SD  . MET B 2 81  ? 9.888   -18.742 18.908  1.00 88.27  ? 80  MET H SD  1 
ATOM   2621 C  CE  . MET B 2 81  ? 9.224   -18.399 17.280  1.00 87.12  ? 80  MET H CE  1 
ATOM   2622 N  N   . GLU B 2 82  ? 5.376   -18.813 18.194  1.00 83.93  ? 81  GLU H N   1 
ATOM   2623 C  CA  . GLU B 2 82  ? 5.033   -17.859 17.153  1.00 83.38  ? 81  GLU H CA  1 
ATOM   2624 C  C   . GLU B 2 82  ? 5.727   -16.529 17.441  1.00 82.65  ? 81  GLU H C   1 
ATOM   2625 O  O   . GLU B 2 82  ? 5.568   -15.972 18.525  1.00 83.10  ? 81  GLU H O   1 
ATOM   2626 C  CB  . GLU B 2 82  ? 3.515   -17.682 17.074  1.00 84.67  ? 81  GLU H CB  1 
ATOM   2627 C  CG  . GLU B 2 82  ? 3.057   -16.931 15.836  1.00 86.06  ? 81  GLU H CG  1 
ATOM   2628 C  CD  . GLU B 2 82  ? 1.555   -16.738 15.716  1.00 87.51  ? 81  GLU H CD  1 
ATOM   2629 O  OE1 . GLU B 2 82  ? 0.831   -17.128 16.654  1.00 88.22  ? 81  GLU H OE1 1 
ATOM   2630 O  OE2 . GLU B 2 82  ? 1.112   -16.201 14.682  1.00 88.84  ? 81  GLU H OE2 1 
ATOM   2631 N  N   . LEU B 2 83  ? 6.496   -16.038 16.459  1.00 80.81  ? 82  LEU H N   1 
ATOM   2632 C  CA  . LEU B 2 83  ? 7.163   -14.748 16.548  1.00 80.50  ? 82  LEU H CA  1 
ATOM   2633 C  C   . LEU B 2 83  ? 6.647   -13.843 15.432  1.00 80.81  ? 82  LEU H C   1 
ATOM   2634 O  O   . LEU B 2 83  ? 6.764   -14.184 14.257  1.00 80.36  ? 82  LEU H O   1 
ATOM   2635 C  CB  . LEU B 2 83  ? 8.677   -14.963 16.438  1.00 80.20  ? 82  LEU H CB  1 
ATOM   2636 C  CG  . LEU B 2 83  ? 9.539   -13.702 16.510  1.00 80.86  ? 82  LEU H CG  1 
ATOM   2637 C  CD1 . LEU B 2 83  ? 9.582   -13.149 17.927  1.00 81.66  ? 82  LEU H CD1 1 
ATOM   2638 C  CD2 . LEU B 2 83  ? 10.948  -13.977 16.010  1.00 81.02  ? 82  LEU H CD2 1 
ATOM   2639 N  N   . SER B 2 84  A 6.089   -12.687 15.818  1.00 81.67  ? 82  SER H N   1 
ATOM   2640 C  CA  . SER B 2 84  A 5.468   -11.759 14.885  1.00 82.42  ? 82  SER H CA  1 
ATOM   2641 C  C   . SER B 2 84  A 6.280   -10.466 14.804  1.00 84.12  ? 82  SER H C   1 
ATOM   2642 O  O   . SER B 2 84  A 7.188   -10.247 15.604  1.00 83.39  ? 82  SER H O   1 
ATOM   2643 C  CB  . SER B 2 84  A 4.038   -11.490 15.279  1.00 81.75  ? 82  SER H CB  1 
ATOM   2644 O  OG  . SER B 2 84  A 3.965   -10.988 16.604  1.00 81.49  ? 82  SER H OG  1 
ATOM   2645 N  N   . SER B 2 85  B 5.933   -9.621  13.823  1.00 85.91  ? 82  SER H N   1 
ATOM   2646 C  CA  . SER B 2 85  B 6.640   -8.378  13.552  1.00 87.33  ? 82  SER H CA  1 
ATOM   2647 C  C   . SER B 2 85  B 8.121   -8.667  13.321  1.00 87.79  ? 82  SER H C   1 
ATOM   2648 O  O   . SER B 2 85  B 8.984   -8.124  14.009  1.00 88.84  ? 82  SER H O   1 
ATOM   2649 C  CB  . SER B 2 85  B 6.427   -7.371  14.655  1.00 87.99  ? 82  SER H CB  1 
ATOM   2650 O  OG  . SER B 2 85  B 5.047   -7.076  14.809  1.00 88.48  ? 82  SER H OG  1 
ATOM   2651 N  N   . LEU B 2 86  C 8.392   -9.526  12.332  1.00 87.78  ? 82  LEU H N   1 
ATOM   2652 C  CA  . LEU B 2 86  C 9.735   -10.006 12.053  1.00 88.01  ? 82  LEU H CA  1 
ATOM   2653 C  C   . LEU B 2 86  C 10.566  -8.897  11.412  1.00 90.38  ? 82  LEU H C   1 
ATOM   2654 O  O   . LEU B 2 86  C 10.118  -8.245  10.470  1.00 90.45  ? 82  LEU H O   1 
ATOM   2655 C  CB  . LEU B 2 86  C 9.643   -11.229 11.133  1.00 87.20  ? 82  LEU H CB  1 
ATOM   2656 C  CG  . LEU B 2 86  C 9.083   -12.501 11.772  1.00 85.15  ? 82  LEU H CG  1 
ATOM   2657 C  CD1 . LEU B 2 86  C 8.934   -13.605 10.736  1.00 84.83  ? 82  LEU H CD1 1 
ATOM   2658 C  CD2 . LEU B 2 86  C 9.963   -12.970 12.921  1.00 84.02  ? 82  LEU H CD2 1 
ATOM   2659 N  N   . ARG B 2 87  ? 11.777  -8.697  11.947  1.00 92.33  ? 83  ARG H N   1 
ATOM   2660 C  CA  . ARG B 2 87  ? 12.751  -7.771  11.393  1.00 96.48  ? 83  ARG H CA  1 
ATOM   2661 C  C   . ARG B 2 87  ? 13.941  -8.562  10.852  1.00 96.35  ? 83  ARG H C   1 
ATOM   2662 O  O   . ARG B 2 87  ? 13.990  -9.782  10.986  1.00 94.45  ? 83  ARG H O   1 
ATOM   2663 C  CB  . ARG B 2 87  ? 13.200  -6.770  12.464  1.00 99.51  ? 83  ARG H CB  1 
ATOM   2664 C  CG  . ARG B 2 87  ? 12.122  -5.789  12.905  1.00 101.19 ? 83  ARG H CG  1 
ATOM   2665 C  CD  . ARG B 2 87  ? 12.719  -4.548  13.543  1.00 104.56 ? 83  ARG H CD  1 
ATOM   2666 N  NE  . ARG B 2 87  ? 13.411  -3.720  12.560  1.00 109.07 ? 83  ARG H NE  1 
ATOM   2667 C  CZ  . ARG B 2 87  ? 14.732  -3.646  12.414  1.00 112.23 ? 83  ARG H CZ  1 
ATOM   2668 N  NH1 . ARG B 2 87  ? 15.532  -4.368  13.180  1.00 112.30 ? 83  ARG H NH1 1 
ATOM   2669 N  NH2 . ARG B 2 87  ? 15.251  -2.859  11.486  1.00 114.52 ? 83  ARG H NH2 1 
ATOM   2670 N  N   . SER B 2 88  ? 14.903  -7.849  10.251  1.00 98.28  ? 84  SER H N   1 
ATOM   2671 C  CA  . SER B 2 88  ? 16.098  -8.462  9.691   1.00 99.39  ? 84  SER H CA  1 
ATOM   2672 C  C   . SER B 2 88  ? 16.969  -9.074  10.788  1.00 98.94  ? 84  SER H C   1 
ATOM   2673 O  O   . SER B 2 88  ? 17.717  -10.012 10.522  1.00 100.04 ? 84  SER H O   1 
ATOM   2674 C  CB  . SER B 2 88  ? 16.883  -7.464  8.879   1.00 102.65 ? 84  SER H CB  1 
ATOM   2675 O  OG  . SER B 2 88  ? 16.137  -7.027  7.753   1.00 104.04 ? 84  SER H OG  1 
ATOM   2676 N  N   . GLU B 2 89  ? 16.868  -8.536  12.011  1.00 98.18  ? 85  GLU H N   1 
ATOM   2677 C  CA  . GLU B 2 89  ? 17.662  -9.006  13.137  1.00 98.37  ? 85  GLU H CA  1 
ATOM   2678 C  C   . GLU B 2 89  ? 17.107  -10.323 13.685  1.00 94.77  ? 85  GLU H C   1 
ATOM   2679 O  O   . GLU B 2 89  ? 17.769  -10.979 14.489  1.00 95.43  ? 85  GLU H O   1 
ATOM   2680 C  CB  . GLU B 2 89  ? 17.720  -7.938  14.233  1.00 100.71 ? 85  GLU H CB  1 
ATOM   2681 C  CG  . GLU B 2 89  ? 16.405  -7.723  14.965  1.00 100.92 ? 85  GLU H CG  1 
ATOM   2682 C  CD  . GLU B 2 89  ? 16.451  -6.650  16.039  1.00 104.02 ? 85  GLU H CD  1 
ATOM   2683 O  OE1 . GLU B 2 89  ? 16.346  -7.004  17.231  1.00 105.14 ? 85  GLU H OE1 1 
ATOM   2684 O  OE2 . GLU B 2 89  ? 16.584  -5.461  15.681  1.00 106.94 ? 85  GLU H OE2 1 
ATOM   2685 N  N   . ASP B 2 90  ? 15.894  -10.703 13.255  1.00 82.21  ? 86  ASP H N   1 
ATOM   2686 C  CA  . ASP B 2 90  ? 15.262  -11.938 13.694  1.00 79.37  ? 86  ASP H CA  1 
ATOM   2687 C  C   . ASP B 2 90  ? 15.665  -13.103 12.790  1.00 77.29  ? 86  ASP H C   1 
ATOM   2688 O  O   . ASP B 2 90  ? 15.218  -14.228 13.005  1.00 76.29  ? 86  ASP H O   1 
ATOM   2689 C  CB  . ASP B 2 90  ? 13.739  -11.790 13.747  1.00 79.70  ? 86  ASP H CB  1 
ATOM   2690 C  CG  . ASP B 2 90  ? 13.268  -10.711 14.706  1.00 80.15  ? 86  ASP H CG  1 
ATOM   2691 O  OD1 . ASP B 2 90  ? 13.718  -10.728 15.868  1.00 79.81  ? 86  ASP H OD1 1 
ATOM   2692 O  OD2 . ASP B 2 90  ? 12.452  -9.867  14.285  1.00 81.01  ? 86  ASP H OD2 1 
ATOM   2693 N  N   . THR B 2 91  ? 16.494  -12.831 11.774  1.00 76.32  ? 87  THR H N   1 
ATOM   2694 C  CA  . THR B 2 91  ? 17.114  -13.885 10.986  1.00 74.54  ? 87  THR H CA  1 
ATOM   2695 C  C   . THR B 2 91  ? 18.094  -14.646 11.876  1.00 72.95  ? 87  THR H C   1 
ATOM   2696 O  O   . THR B 2 91  ? 19.135  -14.110 12.250  1.00 72.79  ? 87  THR H O   1 
ATOM   2697 C  CB  . THR B 2 91  ? 17.804  -13.311 9.742   1.00 75.26  ? 87  THR H CB  1 
ATOM   2698 O  OG1 . THR B 2 91  ? 16.829  -12.597 8.980   1.00 76.07  ? 87  THR H OG1 1 
ATOM   2699 C  CG2 . THR B 2 91  ? 18.451  -14.376 8.885   1.00 74.61  ? 87  THR H CG2 1 
ATOM   2700 N  N   . ALA B 2 92  ? 17.742  -15.892 12.220  1.00 71.59  ? 88  ALA H N   1 
ATOM   2701 C  CA  . ALA B 2 92  ? 18.502  -16.671 13.185  1.00 70.57  ? 88  ALA H CA  1 
ATOM   2702 C  C   . ALA B 2 92  ? 18.062  -18.132 13.147  1.00 70.47  ? 88  ALA H C   1 
ATOM   2703 O  O   . ALA B 2 92  ? 17.077  -18.469 12.491  1.00 72.02  ? 88  ALA H O   1 
ATOM   2704 C  CB  . ALA B 2 92  ? 18.318  -16.083 14.564  1.00 71.01  ? 88  ALA H CB  1 
ATOM   2705 N  N   . VAL B 2 93  ? 18.812  -18.987 13.856  1.00 69.54  ? 89  VAL H N   1 
ATOM   2706 C  CA  . VAL B 2 93  ? 18.467  -20.390 14.020  1.00 69.16  ? 89  VAL H CA  1 
ATOM   2707 C  C   . VAL B 2 93  ? 17.732  -20.541 15.349  1.00 69.43  ? 89  VAL H C   1 
ATOM   2708 O  O   . VAL B 2 93  ? 18.314  -20.302 16.404  1.00 69.65  ? 89  VAL H O   1 
ATOM   2709 C  CB  . VAL B 2 93  ? 19.715  -21.293 13.972  1.00 69.06  ? 89  VAL H CB  1 
ATOM   2710 C  CG1 . VAL B 2 93  ? 19.372  -22.750 14.253  1.00 68.68  ? 89  VAL H CG1 1 
ATOM   2711 C  CG2 . VAL B 2 93  ? 20.456  -21.164 12.650  1.00 69.36  ? 89  VAL H CG2 1 
ATOM   2712 N  N   . TYR B 2 94  ? 16.459  -20.946 15.282  1.00 70.57  ? 90  TYR H N   1 
ATOM   2713 C  CA  . TYR B 2 94  ? 15.615  -21.050 16.462  1.00 70.91  ? 90  TYR H CA  1 
ATOM   2714 C  C   . TYR B 2 94  ? 15.608  -22.492 16.961  1.00 70.21  ? 90  TYR H C   1 
ATOM   2715 O  O   . TYR B 2 94  ? 15.200  -23.399 16.240  1.00 70.26  ? 90  TYR H O   1 
ATOM   2716 C  CB  . TYR B 2 94  ? 14.205  -20.540 16.152  1.00 72.45  ? 90  TYR H CB  1 
ATOM   2717 C  CG  . TYR B 2 94  ? 14.138  -19.057 15.887  1.00 73.74  ? 90  TYR H CG  1 
ATOM   2718 C  CD1 . TYR B 2 94  ? 14.621  -18.518 14.705  1.00 73.81  ? 90  TYR H CD1 1 
ATOM   2719 C  CD2 . TYR B 2 94  ? 13.623  -18.184 16.832  1.00 74.24  ? 90  TYR H CD2 1 
ATOM   2720 C  CE1 . TYR B 2 94  ? 14.575  -17.155 14.459  1.00 74.42  ? 90  TYR H CE1 1 
ATOM   2721 C  CE2 . TYR B 2 94  ? 13.572  -16.818 16.604  1.00 74.50  ? 90  TYR H CE2 1 
ATOM   2722 C  CZ  . TYR B 2 94  ? 14.050  -16.302 15.413  1.00 74.70  ? 90  TYR H CZ  1 
ATOM   2723 O  OH  . TYR B 2 94  ? 14.000  -14.950 15.184  1.00 76.35  ? 90  TYR H OH  1 
ATOM   2724 N  N   . TYR B 2 95  ? 16.071  -22.678 18.204  1.00 70.16  ? 91  TYR H N   1 
ATOM   2725 C  CA  . TYR B 2 95  ? 16.149  -23.983 18.839  1.00 70.17  ? 91  TYR H CA  1 
ATOM   2726 C  C   . TYR B 2 95  ? 15.047  -24.131 19.885  1.00 69.98  ? 91  TYR H C   1 
ATOM   2727 O  O   . TYR B 2 95  ? 14.547  -23.140 20.412  1.00 70.37  ? 91  TYR H O   1 
ATOM   2728 C  CB  . TYR B 2 95  ? 17.501  -24.171 19.533  1.00 70.21  ? 91  TYR H CB  1 
ATOM   2729 C  CG  . TYR B 2 95  ? 18.688  -24.335 18.618  1.00 70.49  ? 91  TYR H CG  1 
ATOM   2730 C  CD1 . TYR B 2 95  ? 18.814  -25.449 17.802  1.00 70.69  ? 91  TYR H CD1 1 
ATOM   2731 C  CD2 . TYR B 2 95  ? 19.698  -23.387 18.580  1.00 70.93  ? 91  TYR H CD2 1 
ATOM   2732 C  CE1 . TYR B 2 95  ? 19.907  -25.613 16.967  1.00 70.51  ? 91  TYR H CE1 1 
ATOM   2733 C  CE2 . TYR B 2 95  ? 20.797  -23.535 17.748  1.00 71.13  ? 91  TYR H CE2 1 
ATOM   2734 C  CZ  . TYR B 2 95  ? 20.903  -24.652 16.938  1.00 70.60  ? 91  TYR H CZ  1 
ATOM   2735 O  OH  . TYR B 2 95  ? 21.988  -24.805 16.110  1.00 71.32  ? 91  TYR H OH  1 
ATOM   2736 N  N   . CYS B 2 96  ? 14.686  -25.388 20.170  1.00 70.22  ? 92  CYS H N   1 
ATOM   2737 C  CA  . CYS B 2 96  ? 13.955  -25.748 21.375  1.00 70.47  ? 92  CYS H CA  1 
ATOM   2738 C  C   . CYS B 2 96  ? 14.776  -26.781 22.141  1.00 69.67  ? 92  CYS H C   1 
ATOM   2739 O  O   . CYS B 2 96  ? 15.693  -27.377 21.581  1.00 70.83  ? 92  CYS H O   1 
ATOM   2740 C  CB  . CYS B 2 96  ? 12.576  -26.308 21.047  1.00 71.41  ? 92  CYS H CB  1 
ATOM   2741 S  SG  . CYS B 2 96  ? 12.638  -27.843 20.087  1.00 73.21  ? 92  CYS H SG  1 
ATOM   2742 N  N   . ALA B 2 97  ? 14.450  -26.981 23.423  1.00 68.59  ? 93  ALA H N   1 
ATOM   2743 C  CA  . ALA B 2 97  ? 15.195  -27.914 24.253  1.00 69.16  ? 93  ALA H CA  1 
ATOM   2744 C  C   . ALA B 2 97  ? 14.385  -28.284 25.493  1.00 70.61  ? 93  ALA H C   1 
ATOM   2745 O  O   . ALA B 2 97  ? 13.528  -27.519 25.931  1.00 69.55  ? 93  ALA H O   1 
ATOM   2746 C  CB  . ALA B 2 97  ? 16.530  -27.316 24.627  1.00 68.32  ? 93  ALA H CB  1 
ATOM   2747 N  N   . ARG B 2 98  ? 14.673  -29.468 26.048  1.00 73.06  ? 94  ARG H N   1 
ATOM   2748 C  CA  . ARG B 2 98  ? 14.030  -29.924 27.268  1.00 75.14  ? 94  ARG H CA  1 
ATOM   2749 C  C   . ARG B 2 98  ? 14.673  -29.218 28.458  1.00 75.37  ? 94  ARG H C   1 
ATOM   2750 O  O   . ARG B 2 98  ? 15.886  -29.286 28.639  1.00 75.55  ? 94  ARG H O   1 
ATOM   2751 C  CB  . ARG B 2 98  ? 14.148  -31.443 27.431  1.00 76.85  ? 94  ARG H CB  1 
ATOM   2752 C  CG  . ARG B 2 98  ? 13.327  -31.995 28.590  1.00 78.78  ? 94  ARG H CG  1 
ATOM   2753 C  CD  . ARG B 2 98  ? 13.506  -33.482 28.822  1.00 80.76  ? 94  ARG H CD  1 
ATOM   2754 N  NE  . ARG B 2 98  ? 14.823  -33.818 29.347  1.00 81.74  ? 94  ARG H NE  1 
ATOM   2755 C  CZ  . ARG B 2 98  ? 15.187  -35.033 29.743  1.00 84.16  ? 94  ARG H CZ  1 
ATOM   2756 N  NH1 . ARG B 2 98  ? 14.320  -36.029 29.717  1.00 85.67  ? 94  ARG H NH1 1 
ATOM   2757 N  NH2 . ARG B 2 98  ? 16.419  -35.246 30.173  1.00 85.08  ? 94  ARG H NH2 1 
ATOM   2758 N  N   . GLY B 2 99  ? 13.841  -28.547 29.262  1.00 75.14  ? 95  GLY H N   1 
ATOM   2759 C  CA  . GLY B 2 99  ? 14.305  -27.868 30.459  1.00 74.73  ? 95  GLY H CA  1 
ATOM   2760 C  C   . GLY B 2 99  ? 14.651  -28.860 31.565  1.00 75.35  ? 95  GLY H C   1 
ATOM   2761 O  O   . GLY B 2 99  ? 13.896  -29.798 31.812  1.00 76.38  ? 95  GLY H O   1 
ATOM   2762 N  N   . LEU B 2 100 ? 15.798  -28.640 32.220  1.00 75.42  ? 96  LEU H N   1 
ATOM   2763 C  CA  . LEU B 2 100 ? 16.239  -29.481 33.321  1.00 76.12  ? 96  LEU H CA  1 
ATOM   2764 C  C   . LEU B 2 100 ? 16.248  -28.678 34.618  1.00 76.01  ? 96  LEU H C   1 
ATOM   2765 O  O   . LEU B 2 100 ? 16.094  -27.458 34.612  1.00 74.76  ? 96  LEU H O   1 
ATOM   2766 C  CB  . LEU B 2 100 ? 17.636  -30.035 33.019  1.00 76.37  ? 96  LEU H CB  1 
ATOM   2767 C  CG  . LEU B 2 100 ? 17.729  -31.106 31.931  1.00 76.80  ? 96  LEU H CG  1 
ATOM   2768 C  CD1 . LEU B 2 100 ? 19.073  -31.820 32.002  1.00 77.53  ? 96  LEU H CD1 1 
ATOM   2769 C  CD2 . LEU B 2 100 ? 16.585  -32.108 32.028  1.00 77.34  ? 96  LEU H CD2 1 
ATOM   2770 N  N   . GLY B 2 101 ? 16.440  -29.404 35.723  1.00 77.52  ? 97  GLY H N   1 
ATOM   2771 C  CA  . GLY B 2 101 ? 16.464  -28.845 37.064  1.00 77.86  ? 97  GLY H CA  1 
ATOM   2772 C  C   . GLY B 2 101 ? 16.117  -29.921 38.087  1.00 78.44  ? 97  GLY H C   1 
ATOM   2773 O  O   . GLY B 2 101 ? 15.961  -31.086 37.728  1.00 78.11  ? 97  GLY H O   1 
ATOM   2774 N  N   . TYR B 2 102 ? 15.989  -29.523 39.356  1.00 79.89  ? 98  TYR H N   1 
ATOM   2775 C  CA  . TYR B 2 102 ? 15.708  -30.475 40.418  1.00 81.44  ? 98  TYR H CA  1 
ATOM   2776 C  C   . TYR B 2 102 ? 14.279  -31.003 40.289  1.00 80.35  ? 98  TYR H C   1 
ATOM   2777 O  O   . TYR B 2 102 ? 14.008  -32.142 40.660  1.00 80.80  ? 98  TYR H O   1 
ATOM   2778 C  CB  . TYR B 2 102 ? 15.946  -29.849 41.794  1.00 83.52  ? 98  TYR H CB  1 
ATOM   2779 C  CG  . TYR B 2 102 ? 15.715  -30.805 42.936  1.00 86.54  ? 98  TYR H CG  1 
ATOM   2780 C  CD1 . TYR B 2 102 ? 16.411  -32.000 43.015  1.00 87.86  ? 98  TYR H CD1 1 
ATOM   2781 C  CD2 . TYR B 2 102 ? 14.780  -30.533 43.922  1.00 88.75  ? 98  TYR H CD2 1 
ATOM   2782 C  CE1 . TYR B 2 102 ? 16.197  -32.894 44.051  1.00 90.21  ? 98  TYR H CE1 1 
ATOM   2783 C  CE2 . TYR B 2 102 ? 14.554  -31.414 44.966  1.00 90.52  ? 98  TYR H CE2 1 
ATOM   2784 C  CZ  . TYR B 2 102 ? 15.266  -32.599 45.030  1.00 91.79  ? 98  TYR H CZ  1 
ATOM   2785 O  OH  . TYR B 2 102 ? 15.052  -33.479 46.058  1.00 96.22  ? 98  TYR H OH  1 
ATOM   2786 N  N   . TYR B 2 103 ? 13.376  -30.165 39.765  1.00 79.14  ? 99  TYR H N   1 
ATOM   2787 C  CA  . TYR B 2 103 ? 11.989  -30.545 39.552  1.00 79.31  ? 99  TYR H CA  1 
ATOM   2788 C  C   . TYR B 2 103 ? 11.743  -30.747 38.059  1.00 79.50  ? 99  TYR H C   1 
ATOM   2789 O  O   . TYR B 2 103 ? 12.573  -30.373 37.232  1.00 79.55  ? 99  TYR H O   1 
ATOM   2790 C  CB  . TYR B 2 103 ? 11.058  -29.491 40.156  1.00 78.44  ? 99  TYR H CB  1 
ATOM   2791 C  CG  . TYR B 2 103 ? 11.284  -29.255 41.628  1.00 78.24  ? 99  TYR H CG  1 
ATOM   2792 C  CD1 . TYR B 2 103 ? 11.004  -30.243 42.559  1.00 78.97  ? 99  TYR H CD1 1 
ATOM   2793 C  CD2 . TYR B 2 103 ? 11.813  -28.060 42.090  1.00 77.34  ? 99  TYR H CD2 1 
ATOM   2794 C  CE1 . TYR B 2 103 ? 11.224  -30.044 43.912  1.00 79.79  ? 99  TYR H CE1 1 
ATOM   2795 C  CE2 . TYR B 2 103 ? 12.037  -27.845 43.441  1.00 78.19  ? 99  TYR H CE2 1 
ATOM   2796 C  CZ  . TYR B 2 103 ? 11.740  -28.840 44.356  1.00 79.49  ? 99  TYR H CZ  1 
ATOM   2797 O  OH  . TYR B 2 103 ? 11.962  -28.638 45.697  1.00 80.63  ? 99  TYR H OH  1 
ATOM   2798 N  N   . LEU B 2 104 ? 10.587  -31.338 37.734  1.00 81.26  ? 100 LEU H N   1 
ATOM   2799 C  CA  . LEU B 2 104 ? 10.249  -31.707 36.368  1.00 81.97  ? 100 LEU H CA  1 
ATOM   2800 C  C   . LEU B 2 104 ? 9.660   -30.513 35.616  1.00 80.98  ? 100 LEU H C   1 
ATOM   2801 O  O   . LEU B 2 104 ? 9.530   -30.559 34.394  1.00 80.07  ? 100 LEU H O   1 
ATOM   2802 C  CB  . LEU B 2 104 ? 9.258   -32.877 36.404  1.00 84.13  ? 100 LEU H CB  1 
ATOM   2803 C  CG  . LEU B 2 104 ? 9.696   -34.104 37.206  1.00 85.54  ? 100 LEU H CG  1 
ATOM   2804 C  CD1 . LEU B 2 104 ? 8.753   -35.272 36.961  1.00 86.53  ? 100 LEU H CD1 1 
ATOM   2805 C  CD2 . LEU B 2 104 ? 11.128  -34.501 36.877  1.00 85.21  ? 100 LEU H CD2 1 
ATOM   2806 N  N   . TYR B 2 105 A 9.300   -29.452 36.352  1.00 80.99  ? 100 TYR H N   1 
ATOM   2807 C  CA  . TYR B 2 105 A 8.774   -28.231 35.761  1.00 80.40  ? 100 TYR H CA  1 
ATOM   2808 C  C   . TYR B 2 105 A 9.898   -27.220 35.528  1.00 79.49  ? 100 TYR H C   1 
ATOM   2809 O  O   . TYR B 2 105 A 9.659   -26.145 34.981  1.00 78.86  ? 100 TYR H O   1 
ATOM   2810 C  CB  . TYR B 2 105 A 7.665   -27.646 36.644  1.00 81.02  ? 100 TYR H CB  1 
ATOM   2811 C  CG  . TYR B 2 105 A 8.038   -27.388 38.084  1.00 81.53  ? 100 TYR H CG  1 
ATOM   2812 C  CD1 . TYR B 2 105 A 8.948   -26.399 38.429  1.00 81.39  ? 100 TYR H CD1 1 
ATOM   2813 C  CD2 . TYR B 2 105 A 7.474   -28.130 39.111  1.00 82.37  ? 100 TYR H CD2 1 
ATOM   2814 C  CE1 . TYR B 2 105 A 9.288   -26.155 39.751  1.00 82.09  ? 100 TYR H CE1 1 
ATOM   2815 C  CE2 . TYR B 2 105 A 7.804   -27.900 40.438  1.00 83.08  ? 100 TYR H CE2 1 
ATOM   2816 C  CZ  . TYR B 2 105 A 8.715   -26.908 40.760  1.00 82.80  ? 100 TYR H CZ  1 
ATOM   2817 O  OH  . TYR B 2 105 A 9.052   -26.668 42.071  1.00 83.13  ? 100 TYR H OH  1 
ATOM   2818 N  N   . SER B 2 106 B 11.120  -27.571 35.948  1.00 79.51  ? 100 SER H N   1 
ATOM   2819 C  CA  . SER B 2 106 B 12.257  -26.668 35.880  1.00 78.67  ? 100 SER H CA  1 
ATOM   2820 C  C   . SER B 2 106 B 12.774  -26.571 34.447  1.00 77.30  ? 100 SER H C   1 
ATOM   2821 O  O   . SER B 2 106 B 12.762  -27.557 33.714  1.00 76.55  ? 100 SER H O   1 
ATOM   2822 C  CB  . SER B 2 106 B 13.345  -27.124 36.814  1.00 79.28  ? 100 SER H CB  1 
ATOM   2823 O  OG  . SER B 2 106 B 12.866  -27.209 38.148  1.00 80.87  ? 100 SER H OG  1 
ATOM   2824 N  N   . SER B 2 107 C 13.225  -25.368 34.066  1.00 77.08  ? 100 SER H N   1 
ATOM   2825 C  CA  . SER B 2 107 C 13.872  -25.143 32.783  1.00 76.34  ? 100 SER H CA  1 
ATOM   2826 C  C   . SER B 2 107 C 14.977  -24.101 32.942  1.00 75.76  ? 100 SER H C   1 
ATOM   2827 O  O   . SER B 2 107 C 14.817  -22.952 32.537  1.00 75.80  ? 100 SER H O   1 
ATOM   2828 C  CB  . SER B 2 107 C 12.874  -24.741 31.721  1.00 75.54  ? 100 SER H CB  1 
ATOM   2829 O  OG  . SER B 2 107 C 12.245  -23.510 32.044  1.00 76.18  ? 100 SER H OG  1 
ATOM   2830 N  N   . TYR B 2 108 D 16.095  -24.527 33.541  1.00 75.85  ? 100 TYR H N   1 
ATOM   2831 C  CA  . TYR B 2 108 D 17.240  -23.663 33.780  1.00 76.10  ? 100 TYR H CA  1 
ATOM   2832 C  C   . TYR B 2 108 D 18.335  -23.965 32.759  1.00 75.31  ? 100 TYR H C   1 
ATOM   2833 O  O   . TYR B 2 108 D 18.855  -23.054 32.117  1.00 74.29  ? 100 TYR H O   1 
ATOM   2834 C  CB  . TYR B 2 108 D 17.752  -23.847 35.211  1.00 77.49  ? 100 TYR H CB  1 
ATOM   2835 C  CG  . TYR B 2 108 D 16.689  -23.810 36.281  1.00 79.21  ? 100 TYR H CG  1 
ATOM   2836 C  CD1 . TYR B 2 108 D 15.703  -22.836 36.280  1.00 79.72  ? 100 TYR H CD1 1 
ATOM   2837 C  CD2 . TYR B 2 108 D 16.680  -24.737 37.312  1.00 80.90  ? 100 TYR H CD2 1 
ATOM   2838 C  CE1 . TYR B 2 108 D 14.725  -22.796 37.261  1.00 80.39  ? 100 TYR H CE1 1 
ATOM   2839 C  CE2 . TYR B 2 108 D 15.714  -24.707 38.305  1.00 81.92  ? 100 TYR H CE2 1 
ATOM   2840 C  CZ  . TYR B 2 108 D 14.732  -23.731 38.281  1.00 81.73  ? 100 TYR H CZ  1 
ATOM   2841 O  OH  . TYR B 2 108 D 13.765  -23.685 39.257  1.00 82.37  ? 100 TYR H OH  1 
ATOM   2842 N  N   . TYR B 2 109 E 18.680  -25.253 32.635  1.00 74.93  ? 100 TYR H N   1 
ATOM   2843 C  CA  . TYR B 2 109 E 19.646  -25.734 31.658  1.00 75.13  ? 100 TYR H CA  1 
ATOM   2844 C  C   . TYR B 2 109 E 18.972  -26.797 30.793  1.00 75.79  ? 100 TYR H C   1 
ATOM   2845 O  O   . TYR B 2 109 E 17.879  -27.258 31.119  1.00 76.43  ? 100 TYR H O   1 
ATOM   2846 C  CB  . TYR B 2 109 E 20.916  -26.252 32.342  1.00 75.15  ? 100 TYR H CB  1 
ATOM   2847 C  CG  . TYR B 2 109 E 20.692  -27.144 33.538  1.00 75.45  ? 100 TYR H CG  1 
ATOM   2848 C  CD1 . TYR B 2 109 E 20.334  -26.613 34.768  1.00 75.70  ? 100 TYR H CD1 1 
ATOM   2849 C  CD2 . TYR B 2 109 E 20.831  -28.520 33.446  1.00 74.92  ? 100 TYR H CD2 1 
ATOM   2850 C  CE1 . TYR B 2 109 E 20.119  -27.422 35.872  1.00 76.06  ? 100 TYR H CE1 1 
ATOM   2851 C  CE2 . TYR B 2 109 E 20.621  -29.344 34.541  1.00 75.74  ? 100 TYR H CE2 1 
ATOM   2852 C  CZ  . TYR B 2 109 E 20.264  -28.793 35.760  1.00 76.04  ? 100 TYR H CZ  1 
ATOM   2853 O  OH  . TYR B 2 109 E 20.054  -29.594 36.857  1.00 76.36  ? 100 TYR H OH  1 
ATOM   2854 N  N   . PHE B 2 110 F 19.623  -27.164 29.681  1.00 75.64  ? 100 PHE H N   1 
ATOM   2855 C  CA  . PHE B 2 110 F 18.998  -27.996 28.664  1.00 75.49  ? 100 PHE H CA  1 
ATOM   2856 C  C   . PHE B 2 110 F 20.005  -29.011 28.130  1.00 74.91  ? 100 PHE H C   1 
ATOM   2857 O  O   . PHE B 2 110 F 21.132  -28.648 27.801  1.00 75.11  ? 100 PHE H O   1 
ATOM   2858 C  CB  . PHE B 2 110 F 18.433  -27.121 27.542  1.00 75.30  ? 100 PHE H CB  1 
ATOM   2859 C  CG  . PHE B 2 110 F 17.728  -25.878 28.025  1.00 76.44  ? 100 PHE H CG  1 
ATOM   2860 C  CD1 . PHE B 2 110 F 18.442  -24.724 28.313  1.00 77.09  ? 100 PHE H CD1 1 
ATOM   2861 C  CD2 . PHE B 2 110 F 16.359  -25.878 28.246  1.00 76.95  ? 100 PHE H CD2 1 
ATOM   2862 C  CE1 . PHE B 2 110 F 17.797  -23.588 28.780  1.00 78.10  ? 100 PHE H CE1 1 
ATOM   2863 C  CE2 . PHE B 2 110 F 15.716  -24.742 28.713  1.00 77.87  ? 100 PHE H CE2 1 
ATOM   2864 C  CZ  . PHE B 2 110 F 16.436  -23.600 28.980  1.00 78.06  ? 100 PHE H CZ  1 
ATOM   2865 N  N   . ASP B 2 111 ? 19.573  -30.277 28.037  1.00 74.49  ? 101 ASP H N   1 
ATOM   2866 C  CA  . ASP B 2 111 ? 20.445  -31.381 27.662  1.00 74.41  ? 101 ASP H CA  1 
ATOM   2867 C  C   . ASP B 2 111 ? 20.115  -31.856 26.247  1.00 73.14  ? 101 ASP H C   1 
ATOM   2868 O  O   . ASP B 2 111 ? 21.021  -32.017 25.431  1.00 72.80  ? 101 ASP H O   1 
ATOM   2869 C  CB  . ASP B 2 111 ? 20.373  -32.530 28.674  1.00 76.34  ? 101 ASP H CB  1 
ATOM   2870 C  CG  . ASP B 2 111 ? 18.982  -33.088 28.935  1.00 77.27  ? 101 ASP H CG  1 
ATOM   2871 O  OD1 . ASP B 2 111 ? 17.993  -32.424 28.556  1.00 76.83  ? 101 ASP H OD1 1 
ATOM   2872 O  OD2 . ASP B 2 111 ? 18.898  -34.197 29.499  1.00 78.44  ? 101 ASP H OD2 1 
ATOM   2873 N  N   . ILE B 2 112 ? 18.824  -32.090 25.973  1.00 72.49  ? 102 ILE H N   1 
ATOM   2874 C  CA  . ILE B 2 112 ? 18.370  -32.524 24.660  1.00 71.77  ? 102 ILE H CA  1 
ATOM   2875 C  C   . ILE B 2 112 ? 17.790  -31.320 23.923  1.00 70.62  ? 102 ILE H C   1 
ATOM   2876 O  O   . ILE B 2 112 ? 16.845  -30.694 24.400  1.00 69.48  ? 102 ILE H O   1 
ATOM   2877 C  CB  . ILE B 2 112 ? 17.356  -33.685 24.768  1.00 72.55  ? 102 ILE H CB  1 
ATOM   2878 C  CG1 . ILE B 2 112 ? 18.050  -35.014 25.083  1.00 73.80  ? 102 ILE H CG1 1 
ATOM   2879 C  CG2 . ILE B 2 112 ? 16.507  -33.794 23.508  1.00 72.12  ? 102 ILE H CG2 1 
ATOM   2880 C  CD1 . ILE B 2 112 ? 18.467  -35.177 26.525  1.00 74.51  ? 102 ILE H CD1 1 
ATOM   2881 N  N   . TRP B 2 113 ? 18.369  -31.025 22.751  1.00 69.79  ? 103 TRP H N   1 
ATOM   2882 C  CA  . TRP B 2 113 ? 17.960  -29.906 21.918  1.00 68.25  ? 103 TRP H CA  1 
ATOM   2883 C  C   . TRP B 2 113 ? 17.266  -30.415 20.659  1.00 69.28  ? 103 TRP H C   1 
ATOM   2884 O  O   . TRP B 2 113 ? 17.360  -31.593 20.323  1.00 70.70  ? 103 TRP H O   1 
ATOM   2885 C  CB  . TRP B 2 113 ? 19.173  -29.046 21.548  1.00 65.97  ? 103 TRP H CB  1 
ATOM   2886 C  CG  . TRP B 2 113 ? 19.788  -28.306 22.695  1.00 64.23  ? 103 TRP H CG  1 
ATOM   2887 C  CD1 . TRP B 2 113 ? 20.372  -28.836 23.809  1.00 63.54  ? 103 TRP H CD1 1 
ATOM   2888 C  CD2 . TRP B 2 113 ? 19.897  -26.879 22.825  1.00 63.37  ? 103 TRP H CD2 1 
ATOM   2889 N  NE1 . TRP B 2 113 ? 20.831  -27.837 24.625  1.00 63.21  ? 103 TRP H NE1 1 
ATOM   2890 C  CE2 . TRP B 2 113 ? 20.555  -26.625 24.047  1.00 63.50  ? 103 TRP H CE2 1 
ATOM   2891 C  CE3 . TRP B 2 113 ? 19.502  -25.796 22.031  1.00 62.97  ? 103 TRP H CE3 1 
ATOM   2892 C  CZ2 . TRP B 2 113 ? 20.824  -25.329 24.488  1.00 63.59  ? 103 TRP H CZ2 1 
ATOM   2893 C  CZ3 . TRP B 2 113 ? 19.769  -24.517 22.468  1.00 63.09  ? 103 TRP H CZ3 1 
ATOM   2894 C  CH2 . TRP B 2 113 ? 20.421  -24.290 23.681  1.00 63.37  ? 103 TRP H CH2 1 
ATOM   2895 N  N   . GLY B 2 114 ? 16.581  -29.501 19.966  1.00 70.14  ? 104 GLY H N   1 
ATOM   2896 C  CA  . GLY B 2 114 ? 16.063  -29.767 18.635  1.00 71.61  ? 104 GLY H CA  1 
ATOM   2897 C  C   . GLY B 2 114 ? 17.142  -29.573 17.572  1.00 72.96  ? 104 GLY H C   1 
ATOM   2898 O  O   . GLY B 2 114 ? 18.254  -29.143 17.874  1.00 71.20  ? 104 GLY H O   1 
ATOM   2899 N  N   . GLN B 2 115 ? 16.788  -29.896 16.324  1.00 75.60  ? 105 GLN H N   1 
ATOM   2900 C  CA  . GLN B 2 115 ? 17.701  -29.799 15.194  1.00 76.60  ? 105 GLN H CA  1 
ATOM   2901 C  C   . GLN B 2 115 ? 17.986  -28.336 14.859  1.00 76.51  ? 105 GLN H C   1 
ATOM   2902 O  O   . GLN B 2 115 ? 19.042  -28.022 14.313  1.00 78.35  ? 105 GLN H O   1 
ATOM   2903 C  CB  . GLN B 2 115 ? 17.126  -30.522 13.973  1.00 78.17  ? 105 GLN H CB  1 
ATOM   2904 C  CG  . GLN B 2 115 ? 15.710  -30.092 13.609  1.00 79.84  ? 105 GLN H CG  1 
ATOM   2905 C  CD  . GLN B 2 115 ? 15.252  -30.644 12.282  1.00 82.39  ? 105 GLN H CD  1 
ATOM   2906 O  OE1 . GLN B 2 115 ? 16.006  -31.292 11.557  1.00 84.77  ? 105 GLN H OE1 1 
ATOM   2907 N  NE2 . GLN B 2 115 ? 13.999  -30.381 11.951  1.00 83.81  ? 105 GLN H NE2 1 
ATOM   2908 N  N   . GLY B 2 116 ? 17.030  -27.452 15.176  1.00 75.63  ? 106 GLY H N   1 
ATOM   2909 C  CA  . GLY B 2 116 ? 17.147  -26.035 14.874  1.00 74.49  ? 106 GLY H CA  1 
ATOM   2910 C  C   . GLY B 2 116 ? 16.427  -25.686 13.575  1.00 74.20  ? 106 GLY H C   1 
ATOM   2911 O  O   . GLY B 2 116 ? 16.333  -26.518 12.676  1.00 74.41  ? 106 GLY H O   1 
ATOM   2912 N  N   . THR B 2 117 ? 15.921  -24.450 13.498  1.00 74.39  ? 107 THR H N   1 
ATOM   2913 C  CA  . THR B 2 117 ? 15.179  -23.975 12.341  1.00 75.29  ? 107 THR H CA  1 
ATOM   2914 C  C   . THR B 2 117 ? 15.694  -22.590 11.956  1.00 76.44  ? 107 THR H C   1 
ATOM   2915 O  O   . THR B 2 117 ? 15.542  -21.640 12.722  1.00 78.22  ? 107 THR H O   1 
ATOM   2916 C  CB  . THR B 2 117 ? 13.672  -23.943 12.630  1.00 75.36  ? 107 THR H CB  1 
ATOM   2917 O  OG1 . THR B 2 117 ? 13.265  -25.235 13.084  1.00 74.48  ? 107 THR H OG1 1 
ATOM   2918 C  CG2 . THR B 2 117 ? 12.850  -23.544 11.424  1.00 75.73  ? 107 THR H CG2 1 
ATOM   2919 N  N   . LEU B 2 118 ? 16.306  -22.490 10.769  1.00 76.36  ? 108 LEU H N   1 
ATOM   2920 C  CA  . LEU B 2 118 ? 16.837  -21.225 10.285  1.00 75.99  ? 108 LEU H CA  1 
ATOM   2921 C  C   . LEU B 2 118 ? 15.717  -20.429 9.621   1.00 76.47  ? 108 LEU H C   1 
ATOM   2922 O  O   . LEU B 2 118 ? 15.355  -20.697 8.476   1.00 77.51  ? 108 LEU H O   1 
ATOM   2923 C  CB  . LEU B 2 118 ? 17.987  -21.490 9.306   1.00 75.59  ? 108 LEU H CB  1 
ATOM   2924 C  CG  . LEU B 2 118 ? 18.572  -20.254 8.621   1.00 75.37  ? 108 LEU H CG  1 
ATOM   2925 C  CD1 . LEU B 2 118 ? 19.115  -19.266 9.642   1.00 75.22  ? 108 LEU H CD1 1 
ATOM   2926 C  CD2 . LEU B 2 118 ? 19.664  -20.646 7.637   1.00 75.64  ? 108 LEU H CD2 1 
ATOM   2927 N  N   . VAL B 2 119 ? 15.177  -19.452 10.358  1.00 76.76  ? 109 VAL H N   1 
ATOM   2928 C  CA  . VAL B 2 119 ? 14.188  -18.532 9.822   1.00 77.79  ? 109 VAL H CA  1 
ATOM   2929 C  C   . VAL B 2 119 ? 14.931  -17.339 9.228   1.00 76.58  ? 109 VAL H C   1 
ATOM   2930 O  O   . VAL B 2 119 ? 15.742  -16.713 9.908   1.00 74.94  ? 109 VAL H O   1 
ATOM   2931 C  CB  . VAL B 2 119 ? 13.178  -18.089 10.900  1.00 78.99  ? 109 VAL H CB  1 
ATOM   2932 C  CG1 . VAL B 2 119 ? 12.141  -17.123 10.340  1.00 79.75  ? 109 VAL H CG1 1 
ATOM   2933 C  CG2 . VAL B 2 119 ? 12.500  -19.281 11.560  1.00 79.50  ? 109 VAL H CG2 1 
ATOM   2934 N  N   . THR B 2 120 ? 14.647  -17.048 7.953   1.00 76.15  ? 110 THR H N   1 
ATOM   2935 C  CA  . THR B 2 120 ? 15.249  -15.926 7.252   1.00 75.90  ? 110 THR H CA  1 
ATOM   2936 C  C   . THR B 2 120 ? 14.173  -14.875 6.995   1.00 76.44  ? 110 THR H C   1 
ATOM   2937 O  O   . THR B 2 120 ? 13.141  -15.181 6.402   1.00 76.25  ? 110 THR H O   1 
ATOM   2938 C  CB  . THR B 2 120 ? 15.910  -16.385 5.945   1.00 75.56  ? 110 THR H CB  1 
ATOM   2939 O  OG1 . THR B 2 120 ? 16.817  -17.446 6.250   1.00 74.89  ? 110 THR H OG1 1 
ATOM   2940 C  CG2 . THR B 2 120 ? 16.648  -15.273 5.233   1.00 76.14  ? 110 THR H CG2 1 
ATOM   2941 N  N   . VAL B 2 121 ? 14.423  -13.644 7.459   1.00 76.69  ? 111 VAL H N   1 
ATOM   2942 C  CA  . VAL B 2 121 ? 13.502  -12.539 7.256   1.00 78.41  ? 111 VAL H CA  1 
ATOM   2943 C  C   . VAL B 2 121 ? 14.016  -11.696 6.091   1.00 79.71  ? 111 VAL H C   1 
ATOM   2944 O  O   . VAL B 2 121 ? 14.981  -10.949 6.241   1.00 78.60  ? 111 VAL H O   1 
ATOM   2945 C  CB  . VAL B 2 121 ? 13.331  -11.703 8.539   1.00 78.36  ? 111 VAL H CB  1 
ATOM   2946 C  CG1 . VAL B 2 121 ? 12.386  -10.528 8.327   1.00 79.60  ? 111 VAL H CG1 1 
ATOM   2947 C  CG2 . VAL B 2 121 ? 12.866  -12.564 9.705   1.00 77.76  ? 111 VAL H CG2 1 
ATOM   2948 N  N   . SER B 2 122 ? 13.360  -11.837 4.932   1.00 82.12  ? 112 SER H N   1 
ATOM   2949 C  CA  . SER B 2 122 ? 13.769  -11.157 3.714   1.00 85.18  ? 112 SER H CA  1 
ATOM   2950 C  C   . SER B 2 122 ? 12.564  -10.954 2.800   1.00 88.17  ? 112 SER H C   1 
ATOM   2951 O  O   . SER B 2 122 ? 11.687  -11.812 2.721   1.00 87.43  ? 112 SER H O   1 
ATOM   2952 C  CB  . SER B 2 122 ? 14.860  -11.926 3.011   1.00 85.12  ? 112 SER H CB  1 
ATOM   2953 O  OG  . SER B 2 122 ? 15.199  -11.314 1.774   1.00 86.40  ? 112 SER H OG  1 
ATOM   2954 N  N   . SER B 2 123 ? 12.548  -9.812  2.103   1.00 92.05  ? 113 SER H N   1 
ATOM   2955 C  CA  . SER B 2 123 ? 11.489  -9.484  1.163   1.00 95.80  ? 113 SER H CA  1 
ATOM   2956 C  C   . SER B 2 123 ? 11.723  -10.189 -0.172  1.00 97.94  ? 113 SER H C   1 
ATOM   2957 O  O   . SER B 2 123 ? 10.794  -10.330 -0.965  1.00 100.11 ? 113 SER H O   1 
ATOM   2958 C  CB  . SER B 2 123 ? 11.375  -7.992  0.983   1.00 97.27  ? 113 SER H CB  1 
ATOM   2959 O  OG  . SER B 2 123 ? 12.612  -7.435  0.562   1.00 97.27  ? 113 SER H OG  1 
ATOM   2960 N  N   . ALA B 2 124 ? 12.969  -10.621 -0.415  1.00 98.44  ? 114 ALA H N   1 
ATOM   2961 C  CA  . ALA B 2 124 ? 13.326  -11.320 -1.639  1.00 99.30  ? 114 ALA H CA  1 
ATOM   2962 C  C   . ALA B 2 124 ? 12.627  -12.677 -1.681  1.00 100.13 ? 114 ALA H C   1 
ATOM   2963 O  O   . ALA B 2 124 ? 12.476  -13.332 -0.652  1.00 99.20  ? 114 ALA H O   1 
ATOM   2964 C  CB  . ALA B 2 124 ? 14.825  -11.470 -1.731  1.00 97.73  ? 114 ALA H CB  1 
ATOM   2965 N  N   . SER B 2 125 ? 12.211  -13.082 -2.888  1.00 102.48 ? 115 SER H N   1 
ATOM   2966 C  CA  . SER B 2 125 ? 11.471  -14.319 -3.083  1.00 102.71 ? 115 SER H CA  1 
ATOM   2967 C  C   . SER B 2 125 ? 12.427  -15.510 -3.028  1.00 101.01 ? 115 SER H C   1 
ATOM   2968 O  O   . SER B 2 125 ? 13.608  -15.378 -3.346  1.00 100.49 ? 115 SER H O   1 
ATOM   2969 C  CB  . SER B 2 125 ? 10.704  -14.284 -4.382  1.00 104.29 ? 115 SER H CB  1 
ATOM   2970 O  OG  . SER B 2 125 ? 9.794   -15.372 -4.464  1.00 104.66 ? 115 SER H OG  1 
ATOM   2971 N  N   . THR B 2 126 ? 11.894  -16.668 -2.617  1.00 99.58  ? 116 THR H N   1 
ATOM   2972 C  CA  . THR B 2 126 ? 12.680  -17.885 -2.478  1.00 96.93  ? 116 THR H CA  1 
ATOM   2973 C  C   . THR B 2 126 ? 13.020  -18.434 -3.863  1.00 96.55  ? 116 THR H C   1 
ATOM   2974 O  O   . THR B 2 126 ? 12.266  -18.237 -4.814  1.00 98.03  ? 116 THR H O   1 
ATOM   2975 C  CB  . THR B 2 126 ? 11.954  -18.918 -1.603  1.00 96.06  ? 116 THR H CB  1 
ATOM   2976 O  OG1 . THR B 2 126 ? 12.766  -20.091 -1.540  1.00 95.23  ? 116 THR H OG1 1 
ATOM   2977 C  CG2 . THR B 2 126 ? 10.574  -19.284 -2.108  1.00 97.47  ? 116 THR H CG2 1 
ATOM   2978 N  N   . LYS B 2 127 ? 14.165  -19.122 -3.954  1.00 94.56  ? 117 LYS H N   1 
ATOM   2979 C  CA  . LYS B 2 127 ? 14.658  -19.665 -5.211  1.00 94.19  ? 117 LYS H CA  1 
ATOM   2980 C  C   . LYS B 2 127 ? 15.280  -21.037 -4.956  1.00 91.54  ? 117 LYS H C   1 
ATOM   2981 O  O   . LYS B 2 127 ? 16.173  -21.170 -4.121  1.00 89.64  ? 117 LYS H O   1 
ATOM   2982 C  CB  . LYS B 2 127 ? 15.670  -18.698 -5.837  1.00 95.33  ? 117 LYS H CB  1 
ATOM   2983 C  CG  . LYS B 2 127 ? 16.307  -19.160 -7.142  1.00 96.94  ? 117 LYS H CG  1 
ATOM   2984 C  CD  . LYS B 2 127 ? 15.317  -19.389 -8.269  1.00 98.97  ? 117 LYS H CD  1 
ATOM   2985 C  CE  . LYS B 2 127 ? 15.970  -19.882 -9.543  1.00 99.11  ? 117 LYS H CE  1 
ATOM   2986 N  NZ  . LYS B 2 127 ? 16.961  -18.911 -10.067 1.00 99.38  ? 117 LYS H NZ  1 
ATOM   2987 N  N   . GLY B 2 128 ? 14.799  -22.048 -5.691  1.00 90.55  ? 118 GLY H N   1 
ATOM   2988 C  CA  . GLY B 2 128 ? 15.294  -23.408 -5.562  1.00 87.85  ? 118 GLY H CA  1 
ATOM   2989 C  C   . GLY B 2 128 ? 16.646  -23.585 -6.249  1.00 85.84  ? 118 GLY H C   1 
ATOM   2990 O  O   . GLY B 2 128 ? 16.921  -22.932 -7.254  1.00 86.54  ? 118 GLY H O   1 
ATOM   2991 N  N   . PRO B 2 129 ? 17.526  -24.476 -5.734  1.00 83.21  ? 119 PRO H N   1 
ATOM   2992 C  CA  . PRO B 2 129 ? 18.865  -24.658 -6.298  1.00 81.83  ? 119 PRO H CA  1 
ATOM   2993 C  C   . PRO B 2 129 ? 18.883  -25.413 -7.624  1.00 81.83  ? 119 PRO H C   1 
ATOM   2994 O  O   . PRO B 2 129 ? 17.916  -26.085 -7.977  1.00 81.09  ? 119 PRO H O   1 
ATOM   2995 C  CB  . PRO B 2 129 ? 19.590  -25.483 -5.223  1.00 80.66  ? 119 PRO H CB  1 
ATOM   2996 C  CG  . PRO B 2 129 ? 18.484  -26.274 -4.559  1.00 81.24  ? 119 PRO H CG  1 
ATOM   2997 C  CD  . PRO B 2 129 ? 17.279  -25.355 -4.580  1.00 82.12  ? 119 PRO H CD  1 
ATOM   2998 N  N   . SER B 2 130 ? 20.002  -25.278 -8.345  1.00 82.54  ? 120 SER H N   1 
ATOM   2999 C  CA  . SER B 2 130 ? 20.272  -26.043 -9.551  1.00 83.27  ? 120 SER H CA  1 
ATOM   3000 C  C   . SER B 2 130 ? 21.510  -26.906 -9.317  1.00 82.09  ? 120 SER H C   1 
ATOM   3001 O  O   . SER B 2 130 ? 22.615  -26.382 -9.197  1.00 82.49  ? 120 SER H O   1 
ATOM   3002 C  CB  . SER B 2 130 ? 20.448  -25.132 -10.739 1.00 84.76  ? 120 SER H CB  1 
ATOM   3003 O  OG  . SER B 2 130 ? 19.305  -24.309 -10.920 1.00 86.02  ? 120 SER H OG  1 
ATOM   3004 N  N   . VAL B 2 131 ? 21.307  -28.228 -9.250  1.00 81.23  ? 121 VAL H N   1 
ATOM   3005 C  CA  . VAL B 2 131 ? 22.354  -29.163 -8.865  1.00 79.04  ? 121 VAL H CA  1 
ATOM   3006 C  C   . VAL B 2 131 ? 23.122  -29.586 -10.116 1.00 78.17  ? 121 VAL H C   1 
ATOM   3007 O  O   . VAL B 2 131 ? 22.516  -29.940 -11.125 1.00 78.10  ? 121 VAL H O   1 
ATOM   3008 C  CB  . VAL B 2 131 ? 21.767  -30.384 -8.131  1.00 78.62  ? 121 VAL H CB  1 
ATOM   3009 C  CG1 . VAL B 2 131 ? 22.859  -31.293 -7.585  1.00 77.94  ? 121 VAL H CG1 1 
ATOM   3010 C  CG2 . VAL B 2 131 ? 20.811  -29.970 -7.021  1.00 78.32  ? 121 VAL H CG2 1 
ATOM   3011 N  N   . PHE B 2 132 ? 24.458  -29.553 -10.027 1.00 77.48  ? 122 PHE H N   1 
ATOM   3012 C  CA  . PHE B 2 132 ? 25.326  -29.934 -11.131 1.00 78.43  ? 122 PHE H CA  1 
ATOM   3013 C  C   . PHE B 2 132 ? 26.393  -30.905 -10.630 1.00 78.68  ? 122 PHE H C   1 
ATOM   3014 O  O   . PHE B 2 132 ? 26.981  -30.690 -9.573  1.00 78.47  ? 122 PHE H O   1 
ATOM   3015 C  CB  . PHE B 2 132 ? 25.964  -28.696 -11.767 1.00 78.15  ? 122 PHE H CB  1 
ATOM   3016 C  CG  . PHE B 2 132 ? 24.976  -27.745 -12.392 1.00 78.41  ? 122 PHE H CG  1 
ATOM   3017 C  CD1 . PHE B 2 132 ? 24.198  -28.140 -13.469 1.00 79.53  ? 122 PHE H CD1 1 
ATOM   3018 C  CD2 . PHE B 2 132 ? 24.813  -26.460 -11.897 1.00 77.70  ? 122 PHE H CD2 1 
ATOM   3019 C  CE1 . PHE B 2 132 ? 23.284  -27.269 -14.041 1.00 80.64  ? 122 PHE H CE1 1 
ATOM   3020 C  CE2 . PHE B 2 132 ? 23.898  -25.591 -12.469 1.00 78.99  ? 122 PHE H CE2 1 
ATOM   3021 C  CZ  . PHE B 2 132 ? 23.135  -25.996 -13.540 1.00 80.24  ? 122 PHE H CZ  1 
ATOM   3022 N  N   . PRO B 2 133 ? 26.680  -31.997 -11.377 1.00 80.05  ? 123 PRO H N   1 
ATOM   3023 C  CA  . PRO B 2 133 ? 27.655  -32.996 -10.940 1.00 79.38  ? 123 PRO H CA  1 
ATOM   3024 C  C   . PRO B 2 133 ? 29.101  -32.563 -11.168 1.00 78.73  ? 123 PRO H C   1 
ATOM   3025 O  O   . PRO B 2 133 ? 29.452  -32.122 -12.260 1.00 79.31  ? 123 PRO H O   1 
ATOM   3026 C  CB  . PRO B 2 133 ? 27.317  -34.203 -11.827 1.00 80.63  ? 123 PRO H CB  1 
ATOM   3027 C  CG  . PRO B 2 133 ? 26.819  -33.581 -13.116 1.00 81.55  ? 123 PRO H CG  1 
ATOM   3028 C  CD  . PRO B 2 133 ? 26.083  -32.330 -12.681 1.00 81.28  ? 123 PRO H CD  1 
ATOM   3029 N  N   . LEU B 2 134 ? 29.923  -32.686 -10.120 1.00 78.23  ? 124 LEU H N   1 
ATOM   3030 C  CA  . LEU B 2 134 ? 31.367  -32.573 -10.252 1.00 79.24  ? 124 LEU H CA  1 
ATOM   3031 C  C   . LEU B 2 134 ? 31.934  -33.968 -10.507 1.00 80.11  ? 124 LEU H C   1 
ATOM   3032 O  O   . LEU B 2 134 ? 32.308  -34.679 -9.574  1.00 78.05  ? 124 LEU H O   1 
ATOM   3033 C  CB  . LEU B 2 134 ? 31.948  -31.940 -8.983  1.00 78.75  ? 124 LEU H CB  1 
ATOM   3034 C  CG  . LEU B 2 134 ? 31.375  -30.575 -8.597  1.00 78.79  ? 124 LEU H CG  1 
ATOM   3035 C  CD1 . LEU B 2 134 ? 32.224  -29.920 -7.517  1.00 78.41  ? 124 LEU H CD1 1 
ATOM   3036 C  CD2 . LEU B 2 134 ? 31.258  -29.660 -9.808  1.00 79.61  ? 124 LEU H CD2 1 
ATOM   3037 N  N   . ALA B 2 135 ? 31.978  -34.345 -11.791 1.00 81.94  ? 125 ALA H N   1 
ATOM   3038 C  CA  . ALA B 2 135 ? 32.309  -35.700 -12.203 1.00 82.53  ? 125 ALA H CA  1 
ATOM   3039 C  C   . ALA B 2 135 ? 33.799  -35.964 -12.001 1.00 82.48  ? 125 ALA H C   1 
ATOM   3040 O  O   . ALA B 2 135 ? 34.628  -35.102 -12.289 1.00 83.63  ? 125 ALA H O   1 
ATOM   3041 C  CB  . ALA B 2 135 ? 31.908  -35.910 -13.644 1.00 83.16  ? 125 ALA H CB  1 
ATOM   3042 N  N   . PRO B 2 136 ? 34.185  -37.163 -11.505 1.00 81.50  ? 126 PRO H N   1 
ATOM   3043 C  CA  . PRO B 2 136 ? 35.596  -37.520 -11.361 1.00 81.39  ? 126 PRO H CA  1 
ATOM   3044 C  C   . PRO B 2 136 ? 36.231  -37.841 -12.712 1.00 81.84  ? 126 PRO H C   1 
ATOM   3045 O  O   . PRO B 2 136 ? 35.575  -38.398 -13.591 1.00 82.32  ? 126 PRO H O   1 
ATOM   3046 C  CB  . PRO B 2 136 ? 35.559  -38.754 -10.449 1.00 81.91  ? 126 PRO H CB  1 
ATOM   3047 C  CG  . PRO B 2 136 ? 34.217  -39.392 -10.745 1.00 82.09  ? 126 PRO H CG  1 
ATOM   3048 C  CD  . PRO B 2 136 ? 33.286  -38.238 -11.057 1.00 81.24  ? 126 PRO H CD  1 
ATOM   3049 N  N   . SER B 2 137 ? 37.512  -37.486 -12.862 1.00 82.06  ? 127 SER H N   1 
ATOM   3050 C  CA  . SER B 2 137 ? 38.208  -37.630 -14.131 1.00 83.38  ? 127 SER H CA  1 
ATOM   3051 C  C   . SER B 2 137 ? 39.703  -37.836 -13.888 1.00 83.17  ? 127 SER H C   1 
ATOM   3052 O  O   . SER B 2 137 ? 40.129  -38.037 -12.751 1.00 81.46  ? 127 SER H O   1 
ATOM   3053 C  CB  . SER B 2 137 ? 37.940  -36.432 -15.017 1.00 84.00  ? 127 SER H CB  1 
ATOM   3054 O  OG  . SER B 2 137 ? 38.509  -35.249 -14.470 1.00 83.94  ? 127 SER H OG  1 
ATOM   3055 N  N   . SER B 2 138 ? 40.481  -37.800 -14.978 1.00 83.07  ? 128 SER H N   1 
ATOM   3056 C  CA  . SER B 2 138 ? 41.935  -37.818 -14.925 1.00 83.04  ? 128 SER H CA  1 
ATOM   3057 C  C   . SER B 2 138 ? 42.468  -36.727 -13.997 1.00 83.49  ? 128 SER H C   1 
ATOM   3058 O  O   . SER B 2 138 ? 43.477  -36.927 -13.324 1.00 82.38  ? 128 SER H O   1 
ATOM   3059 C  CB  . SER B 2 138 ? 42.506  -37.668 -16.313 1.00 82.96  ? 128 SER H CB  1 
ATOM   3060 O  OG  . SER B 2 138 ? 43.923  -37.595 -16.277 1.00 83.60  ? 128 SER H OG  1 
ATOM   3061 N  N   . LYS B 2 139 ? 41.777  -35.580 -13.970 1.00 85.03  ? 129 LYS H N   1 
ATOM   3062 C  CA  . LYS B 2 139 ? 42.271  -34.381 -13.310 1.00 85.89  ? 129 LYS H CA  1 
ATOM   3063 C  C   . LYS B 2 139 ? 42.022  -34.442 -11.802 1.00 85.41  ? 129 LYS H C   1 
ATOM   3064 O  O   . LYS B 2 139 ? 42.746  -33.803 -11.041 1.00 85.49  ? 129 LYS H O   1 
ATOM   3065 C  CB  . LYS B 2 139 ? 41.606  -33.137 -13.909 1.00 86.15  ? 129 LYS H CB  1 
ATOM   3066 C  CG  . LYS B 2 139 ? 41.622  -33.048 -15.431 1.00 87.08  ? 129 LYS H CG  1 
ATOM   3067 C  CD  . LYS B 2 139 ? 42.991  -33.239 -16.051 1.00 88.30  ? 129 LYS H CD  1 
ATOM   3068 C  CE  . LYS B 2 139 ? 42.985  -33.068 -17.555 1.00 89.52  ? 129 LYS H CE  1 
ATOM   3069 N  NZ  . LYS B 2 139 ? 44.325  -33.309 -18.141 1.00 91.31  ? 129 LYS H NZ  1 
ATOM   3070 N  N   . SER B 2 140 ? 41.000  -35.198 -11.377 1.00 85.47  ? 130 SER H N   1 
ATOM   3071 C  CA  . SER B 2 140 ? 40.631  -35.267 -9.971  1.00 85.51  ? 130 SER H CA  1 
ATOM   3072 C  C   . SER B 2 140 ? 41.000  -36.626 -9.378  1.00 87.12  ? 130 SER H C   1 
ATOM   3073 O  O   . SER B 2 140 ? 40.163  -37.272 -8.751  1.00 86.22  ? 130 SER H O   1 
ATOM   3074 C  CB  . SER B 2 140 ? 39.164  -34.970 -9.779  1.00 83.74  ? 130 SER H CB  1 
ATOM   3075 O  OG  . SER B 2 140 ? 38.360  -36.024 -10.285 1.00 83.36  ? 130 SER H OG  1 
ATOM   3076 N  N   . THR B 2 141 ? 42.261  -37.039 -9.571  1.00 89.44  ? 131 THR H N   1 
ATOM   3077 C  CA  . THR B 2 141 ? 42.801  -38.236 -8.941  1.00 90.47  ? 131 THR H CA  1 
ATOM   3078 C  C   . THR B 2 141 ? 44.138  -37.896 -8.287  1.00 91.56  ? 131 THR H C   1 
ATOM   3079 O  O   . THR B 2 141 ? 45.013  -37.320 -8.930  1.00 92.97  ? 131 THR H O   1 
ATOM   3080 C  CB  . THR B 2 141 ? 42.968  -39.386 -9.943  1.00 90.70  ? 131 THR H CB  1 
ATOM   3081 O  OG1 . THR B 2 141 ? 43.731  -38.900 -11.048 1.00 91.83  ? 131 THR H OG1 1 
ATOM   3082 C  CG2 . THR B 2 141 ? 41.651  -39.948 -10.434 1.00 90.06  ? 131 THR H CG2 1 
ATOM   3083 N  N   . SER B 2 142 ? 44.281  -38.265 -7.008  1.00 92.37  ? 132 SER H N   1 
ATOM   3084 C  CA  . SER B 2 142 ? 45.473  -37.955 -6.234  1.00 93.46  ? 132 SER H CA  1 
ATOM   3085 C  C   . SER B 2 142 ? 46.066  -39.238 -5.655  1.00 94.63  ? 132 SER H C   1 
ATOM   3086 O  O   . SER B 2 142 ? 46.013  -39.464 -4.448  1.00 94.94  ? 132 SER H O   1 
ATOM   3087 C  CB  . SER B 2 142 ? 45.162  -36.945 -5.156  1.00 92.55  ? 132 SER H CB  1 
ATOM   3088 O  OG  . SER B 2 142 ? 46.325  -36.623 -4.408  1.00 93.28  ? 132 SER H OG  1 
ATOM   3089 N  N   . GLY B 2 143 ? 46.621  -40.074 -6.541  1.00 95.25  ? 133 GLY H N   1 
ATOM   3090 C  CA  . GLY B 2 143 ? 47.380  -41.248 -6.140  1.00 95.64  ? 133 GLY H CA  1 
ATOM   3091 C  C   . GLY B 2 143 ? 46.489  -42.363 -5.598  1.00 94.75  ? 133 GLY H C   1 
ATOM   3092 O  O   . GLY B 2 143 ? 46.619  -42.755 -4.439  1.00 94.56  ? 133 GLY H O   1 
ATOM   3093 N  N   . GLY B 2 144 ? 45.583  -42.856 -6.450  1.00 93.23  ? 134 GLY H N   1 
ATOM   3094 C  CA  . GLY B 2 144 ? 44.761  -44.013 -6.132  1.00 91.83  ? 134 GLY H CA  1 
ATOM   3095 C  C   . GLY B 2 144 ? 43.394  -43.640 -5.560  1.00 89.50  ? 134 GLY H C   1 
ATOM   3096 O  O   . GLY B 2 144 ? 42.539  -44.510 -5.404  1.00 88.89  ? 134 GLY H O   1 
ATOM   3097 N  N   . THR B 2 145 ? 43.198  -42.352 -5.246  1.00 87.65  ? 135 THR H N   1 
ATOM   3098 C  CA  . THR B 2 145 ? 41.933  -41.869 -4.714  1.00 86.09  ? 135 THR H CA  1 
ATOM   3099 C  C   . THR B 2 145 ? 41.353  -40.833 -5.673  1.00 84.52  ? 135 THR H C   1 
ATOM   3100 O  O   . THR B 2 145 ? 42.028  -39.867 -6.020  1.00 86.02  ? 135 THR H O   1 
ATOM   3101 C  CB  . THR B 2 145 ? 42.101  -41.276 -3.309  1.00 85.44  ? 135 THR H CB  1 
ATOM   3102 O  OG1 . THR B 2 145 ? 42.866  -40.075 -3.414  1.00 86.62  ? 135 THR H OG1 1 
ATOM   3103 C  CG2 . THR B 2 145 ? 42.772  -42.226 -2.342  1.00 86.35  ? 135 THR H CG2 1 
ATOM   3104 N  N   . ALA B 2 146 ? 40.104  -41.056 -6.096  1.00 82.74  ? 136 ALA H N   1 
ATOM   3105 C  CA  . ALA B 2 146 ? 39.388  -40.114 -6.940  1.00 80.99  ? 136 ALA H CA  1 
ATOM   3106 C  C   . ALA B 2 146 ? 38.564  -39.179 -6.060  1.00 79.63  ? 136 ALA H C   1 
ATOM   3107 O  O   . ALA B 2 146 ? 38.183  -39.542 -4.950  1.00 79.84  ? 136 ALA H O   1 
ATOM   3108 C  CB  . ALA B 2 146 ? 38.514  -40.854 -7.922  1.00 80.76  ? 136 ALA H CB  1 
ATOM   3109 N  N   . ALA B 2 147 ? 38.309  -37.971 -6.574  1.00 78.46  ? 137 ALA H N   1 
ATOM   3110 C  CA  . ALA B 2 147 ? 37.459  -37.001 -5.908  1.00 76.45  ? 137 ALA H CA  1 
ATOM   3111 C  C   . ALA B 2 147 ? 36.294  -36.649 -6.828  1.00 76.06  ? 137 ALA H C   1 
ATOM   3112 O  O   . ALA B 2 147 ? 36.482  -36.471 -8.030  1.00 75.49  ? 137 ALA H O   1 
ATOM   3113 C  CB  . ALA B 2 147 ? 38.260  -35.778 -5.536  1.00 76.27  ? 137 ALA H CB  1 
ATOM   3114 N  N   . LEU B 2 148 ? 35.095  -36.572 -6.243  1.00 76.31  ? 138 LEU H N   1 
ATOM   3115 C  CA  . LEU B 2 148 ? 33.891  -36.177 -6.955  1.00 76.49  ? 138 LEU H CA  1 
ATOM   3116 C  C   . LEU B 2 148 ? 32.991  -35.405 -5.997  1.00 75.73  ? 138 LEU H C   1 
ATOM   3117 O  O   . LEU B 2 148 ? 33.229  -35.402 -4.791  1.00 75.24  ? 138 LEU H O   1 
ATOM   3118 C  CB  . LEU B 2 148 ? 33.195  -37.422 -7.520  1.00 77.70  ? 138 LEU H CB  1 
ATOM   3119 C  CG  . LEU B 2 148 ? 32.900  -38.553 -6.532  1.00 78.14  ? 138 LEU H CG  1 
ATOM   3120 C  CD1 . LEU B 2 148 ? 31.555  -38.358 -5.845  1.00 77.98  ? 138 LEU H CD1 1 
ATOM   3121 C  CD2 . LEU B 2 148 ? 32.943  -39.904 -7.233  1.00 78.62  ? 138 LEU H CD2 1 
ATOM   3122 N  N   . GLY B 2 149 ? 31.964  -34.745 -6.543  1.00 76.15  ? 139 GLY H N   1 
ATOM   3123 C  CA  . GLY B 2 149 ? 31.093  -33.914 -5.731  1.00 76.54  ? 139 GLY H CA  1 
ATOM   3124 C  C   . GLY B 2 149 ? 29.880  -33.401 -6.499  1.00 77.29  ? 139 GLY H C   1 
ATOM   3125 O  O   . GLY B 2 149 ? 29.516  -33.948 -7.538  1.00 76.10  ? 139 GLY H O   1 
ATOM   3126 N  N   . CYS B 2 150 ? 29.262  -32.346 -5.954  1.00 79.10  ? 140 CYS H N   1 
ATOM   3127 C  CA  . CYS B 2 150 ? 28.130  -31.686 -6.584  1.00 81.10  ? 140 CYS H CA  1 
ATOM   3128 C  C   . CYS B 2 150 ? 28.186  -30.185 -6.324  1.00 79.98  ? 140 CYS H C   1 
ATOM   3129 O  O   . CYS B 2 150 ? 28.790  -29.735 -5.353  1.00 79.42  ? 140 CYS H O   1 
ATOM   3130 C  CB  . CYS B 2 150 ? 26.807  -32.251 -6.085  1.00 82.96  ? 140 CYS H CB  1 
ATOM   3131 S  SG  . CYS B 2 150 ? 26.325  -33.770 -6.944  1.00 89.76  ? 140 CYS H SG  1 
ATOM   3132 N  N   . LEU B 2 151 ? 27.536  -29.431 -7.217  1.00 79.86  ? 141 LEU H N   1 
ATOM   3133 C  CA  . LEU B 2 151 ? 27.508  -27.981 -7.155  1.00 79.88  ? 141 LEU H CA  1 
ATOM   3134 C  C   . LEU B 2 151 ? 26.054  -27.519 -7.163  1.00 79.99  ? 141 LEU H C   1 
ATOM   3135 O  O   . LEU B 2 151 ? 25.393  -27.570 -8.198  1.00 80.32  ? 141 LEU H O   1 
ATOM   3136 C  CB  . LEU B 2 151 ? 28.283  -27.429 -8.356  1.00 80.43  ? 141 LEU H CB  1 
ATOM   3137 C  CG  . LEU B 2 151 ? 28.386  -25.907 -8.440  1.00 80.53  ? 141 LEU H CG  1 
ATOM   3138 C  CD1 . LEU B 2 151 ? 29.294  -25.363 -7.348  1.00 80.10  ? 141 LEU H CD1 1 
ATOM   3139 C  CD2 . LEU B 2 151 ? 28.884  -25.476 -9.811  1.00 81.33  ? 141 LEU H CD2 1 
ATOM   3140 N  N   . VAL B 2 152 ? 25.564  -27.093 -5.993  1.00 79.84  ? 142 VAL H N   1 
ATOM   3141 C  CA  . VAL B 2 152 ? 24.230  -26.527 -5.873  1.00 80.69  ? 142 VAL H CA  1 
ATOM   3142 C  C   . VAL B 2 152 ? 24.362  -25.008 -5.957  1.00 79.88  ? 142 VAL H C   1 
ATOM   3143 O  O   . VAL B 2 152 ? 25.074  -24.396 -5.163  1.00 78.58  ? 142 VAL H O   1 
ATOM   3144 C  CB  . VAL B 2 152 ? 23.522  -26.992 -4.583  1.00 81.34  ? 142 VAL H CB  1 
ATOM   3145 C  CG1 . VAL B 2 152 ? 23.537  -28.507 -4.461  1.00 81.45  ? 142 VAL H CG1 1 
ATOM   3146 C  CG2 . VAL B 2 152 ? 24.109  -26.365 -3.330  1.00 80.61  ? 142 VAL H CG2 1 
ATOM   3147 N  N   . LYS B 2 153 ? 23.679  -24.417 -6.943  1.00 80.10  ? 143 LYS H N   1 
ATOM   3148 C  CA  . LYS B 2 153 ? 23.956  -23.055 -7.364  1.00 80.56  ? 143 LYS H CA  1 
ATOM   3149 C  C   . LYS B 2 153 ? 22.639  -22.308 -7.566  1.00 80.37  ? 143 LYS H C   1 
ATOM   3150 O  O   . LYS B 2 153 ? 21.628  -22.913 -7.915  1.00 80.10  ? 143 LYS H O   1 
ATOM   3151 C  CB  . LYS B 2 153 ? 24.797  -23.089 -8.645  1.00 81.60  ? 143 LYS H CB  1 
ATOM   3152 C  CG  . LYS B 2 153 ? 25.470  -21.777 -9.028  1.00 83.03  ? 143 LYS H CG  1 
ATOM   3153 C  CD  . LYS B 2 153 ? 26.409  -21.909 -10.213 1.00 83.54  ? 143 LYS H CD  1 
ATOM   3154 C  CE  . LYS B 2 153 ? 27.142  -20.626 -10.547 1.00 83.54  ? 143 LYS H CE  1 
ATOM   3155 N  NZ  . LYS B 2 153 ? 26.214  -19.559 -10.991 1.00 84.40  ? 143 LYS H NZ  1 
ATOM   3156 N  N   . ASP B 2 154 ? 22.678  -20.990 -7.335  1.00 80.31  ? 144 ASP H N   1 
ATOM   3157 C  CA  . ASP B 2 154 ? 21.533  -20.112 -7.521  1.00 81.05  ? 144 ASP H CA  1 
ATOM   3158 C  C   . ASP B 2 154 ? 20.377  -20.576 -6.637  1.00 80.90  ? 144 ASP H C   1 
ATOM   3159 O  O   . ASP B 2 154 ? 19.377  -21.086 -7.140  1.00 82.47  ? 144 ASP H O   1 
ATOM   3160 C  CB  . ASP B 2 154 ? 21.113  -20.037 -8.993  1.00 81.91  ? 144 ASP H CB  1 
ATOM   3161 C  CG  . ASP B 2 154 ? 22.164  -19.451 -9.922  1.00 82.23  ? 144 ASP H CG  1 
ATOM   3162 O  OD1 . ASP B 2 154 ? 23.246  -19.072 -9.429  1.00 81.06  ? 144 ASP H OD1 1 
ATOM   3163 O  OD2 . ASP B 2 154 ? 21.888  -19.373 -11.135 1.00 83.21  ? 144 ASP H OD2 1 
ATOM   3164 N  N   . TYR B 2 155 ? 20.522  -20.389 -5.318  1.00 79.25  ? 145 TYR H N   1 
ATOM   3165 C  CA  . TYR B 2 155 ? 19.459  -20.715 -4.379  1.00 79.13  ? 145 TYR H CA  1 
ATOM   3166 C  C   . TYR B 2 155 ? 19.358  -19.626 -3.314  1.00 78.97  ? 145 TYR H C   1 
ATOM   3167 O  O   . TYR B 2 155 ? 20.341  -18.956 -3.004  1.00 78.33  ? 145 TYR H O   1 
ATOM   3168 C  CB  . TYR B 2 155 ? 19.671  -22.114 -3.790  1.00 77.53  ? 145 TYR H CB  1 
ATOM   3169 C  CG  . TYR B 2 155 ? 20.749  -22.248 -2.742  1.00 75.47  ? 145 TYR H CG  1 
ATOM   3170 C  CD1 . TYR B 2 155 ? 20.533  -21.849 -1.432  1.00 75.12  ? 145 TYR H CD1 1 
ATOM   3171 C  CD2 . TYR B 2 155 ? 21.982  -22.800 -3.051  1.00 74.61  ? 145 TYR H CD2 1 
ATOM   3172 C  CE1 . TYR B 2 155 ? 21.514  -21.981 -0.462  1.00 73.79  ? 145 TYR H CE1 1 
ATOM   3173 C  CE2 . TYR B 2 155 ? 22.974  -22.939 -2.094  1.00 73.31  ? 145 TYR H CE2 1 
ATOM   3174 C  CZ  . TYR B 2 155 ? 22.741  -22.527 -0.794  1.00 72.72  ? 145 TYR H CZ  1 
ATOM   3175 O  OH  . TYR B 2 155 ? 23.721  -22.660 0.160   1.00 71.62  ? 145 TYR H OH  1 
ATOM   3176 N  N   . PHE B 2 156 ? 18.145  -19.462 -2.769  1.00 79.60  ? 146 PHE H N   1 
ATOM   3177 C  CA  . PHE B 2 156 ? 17.881  -18.494 -1.717  1.00 79.89  ? 146 PHE H CA  1 
ATOM   3178 C  C   . PHE B 2 156 ? 16.585  -18.865 -0.996  1.00 79.29  ? 146 PHE H C   1 
ATOM   3179 O  O   . PHE B 2 156 ? 15.615  -19.256 -1.642  1.00 79.68  ? 146 PHE H O   1 
ATOM   3180 C  CB  . PHE B 2 156 ? 17.778  -17.079 -2.295  1.00 81.55  ? 146 PHE H CB  1 
ATOM   3181 C  CG  . PHE B 2 156 ? 17.574  -15.994 -1.266  1.00 82.08  ? 146 PHE H CG  1 
ATOM   3182 C  CD1 . PHE B 2 156 ? 18.638  -15.518 -0.514  1.00 81.72  ? 146 PHE H CD1 1 
ATOM   3183 C  CD2 . PHE B 2 156 ? 16.311  -15.473 -1.025  1.00 83.40  ? 146 PHE H CD2 1 
ATOM   3184 C  CE1 . PHE B 2 156 ? 18.447  -14.532 0.443   1.00 82.01  ? 146 PHE H CE1 1 
ATOM   3185 C  CE2 . PHE B 2 156 ? 16.121  -14.489 -0.067  1.00 83.93  ? 146 PHE H CE2 1 
ATOM   3186 C  CZ  . PHE B 2 156 ? 17.189  -14.020 0.665   1.00 83.22  ? 146 PHE H CZ  1 
ATOM   3187 N  N   . PRO B 2 157 ? 16.508  -18.767 0.353   1.00 78.32  ? 147 PRO H N   1 
ATOM   3188 C  CA  . PRO B 2 157 ? 17.660  -18.478 1.209   1.00 77.38  ? 147 PRO H CA  1 
ATOM   3189 C  C   . PRO B 2 157 ? 18.426  -19.746 1.580   1.00 76.06  ? 147 PRO H C   1 
ATOM   3190 O  O   . PRO B 2 157 ? 18.273  -20.779 0.933   1.00 74.96  ? 147 PRO H O   1 
ATOM   3191 C  CB  . PRO B 2 157 ? 16.979  -17.843 2.430   1.00 76.94  ? 147 PRO H CB  1 
ATOM   3192 C  CG  . PRO B 2 157 ? 15.696  -18.629 2.562   1.00 77.35  ? 147 PRO H CG  1 
ATOM   3193 C  CD  . PRO B 2 157 ? 15.266  -18.899 1.133   1.00 78.40  ? 147 PRO H CD  1 
ATOM   3194 N  N   . GLU B 2 158 ? 19.263  -19.644 2.617   1.00 75.94  ? 148 GLU H N   1 
ATOM   3195 C  CA  . GLU B 2 158 ? 19.847  -20.808 3.261   1.00 75.79  ? 148 GLU H CA  1 
ATOM   3196 C  C   . GLU B 2 158 ? 18.787  -21.459 4.151   1.00 76.17  ? 148 GLU H C   1 
ATOM   3197 O  O   . GLU B 2 158 ? 17.782  -20.826 4.472   1.00 76.91  ? 148 GLU H O   1 
ATOM   3198 C  CB  . GLU B 2 158 ? 21.090  -20.385 4.049   1.00 75.52  ? 148 GLU H CB  1 
ATOM   3199 C  CG  . GLU B 2 158 ? 22.229  -19.915 3.162   1.00 76.00  ? 148 GLU H CG  1 
ATOM   3200 C  CD  . GLU B 2 158 ? 23.560  -19.752 3.875   1.00 76.45  ? 148 GLU H CD  1 
ATOM   3201 O  OE1 . GLU B 2 158 ? 24.057  -20.754 4.425   1.00 76.52  ? 148 GLU H OE1 1 
ATOM   3202 O  OE2 . GLU B 2 158 ? 24.097  -18.626 3.877   1.00 77.87  ? 148 GLU H OE2 1 
ATOM   3203 N  N   . PRO B 2 159 ? 18.953  -22.735 4.579   1.00 76.02  ? 149 PRO H N   1 
ATOM   3204 C  CA  . PRO B 2 159 ? 20.081  -23.582 4.194   1.00 74.84  ? 149 PRO H CA  1 
ATOM   3205 C  C   . PRO B 2 159 ? 19.773  -24.589 3.089   1.00 74.01  ? 149 PRO H C   1 
ATOM   3206 O  O   . PRO B 2 159 ? 18.614  -24.812 2.747   1.00 73.19  ? 149 PRO H O   1 
ATOM   3207 C  CB  . PRO B 2 159 ? 20.327  -24.319 5.517   1.00 74.43  ? 149 PRO H CB  1 
ATOM   3208 C  CG  . PRO B 2 159 ? 18.927  -24.569 6.056   1.00 75.42  ? 149 PRO H CG  1 
ATOM   3209 C  CD  . PRO B 2 159 ? 18.071  -23.432 5.527   1.00 76.31  ? 149 PRO H CD  1 
ATOM   3210 N  N   . VAL B 2 160 ? 20.841  -25.185 2.547   1.00 73.88  ? 150 VAL H N   1 
ATOM   3211 C  CA  . VAL B 2 160 ? 20.752  -26.338 1.667   1.00 74.11  ? 150 VAL H CA  1 
ATOM   3212 C  C   . VAL B 2 160 ? 21.559  -27.465 2.307   1.00 73.79  ? 150 VAL H C   1 
ATOM   3213 O  O   . VAL B 2 160 ? 22.748  -27.295 2.569   1.00 75.53  ? 150 VAL H O   1 
ATOM   3214 C  CB  . VAL B 2 160 ? 21.259  -26.005 0.249   1.00 74.31  ? 150 VAL H CB  1 
ATOM   3215 C  CG1 . VAL B 2 160 ? 21.554  -27.252 -0.572  1.00 74.12  ? 150 VAL H CG1 1 
ATOM   3216 C  CG2 . VAL B 2 160 ? 20.291  -25.096 -0.493  1.00 75.41  ? 150 VAL H CG2 1 
ATOM   3217 N  N   . THR B 2 161 ? 20.896  -28.600 2.567   1.00 73.27  ? 151 THR H N   1 
ATOM   3218 C  CA  . THR B 2 161 ? 21.546  -29.771 3.135   1.00 72.23  ? 151 THR H CA  1 
ATOM   3219 C  C   . THR B 2 161 ? 21.884  -30.750 2.013   1.00 72.61  ? 151 THR H C   1 
ATOM   3220 O  O   . THR B 2 161 ? 21.123  -30.890 1.056   1.00 72.50  ? 151 THR H O   1 
ATOM   3221 C  CB  . THR B 2 161 ? 20.667  -30.428 4.207   1.00 71.56  ? 151 THR H CB  1 
ATOM   3222 O  OG1 . THR B 2 161 ? 19.486  -30.927 3.578   1.00 71.35  ? 151 THR H OG1 1 
ATOM   3223 C  CG2 . THR B 2 161 ? 20.289  -29.478 5.322   1.00 71.05  ? 151 THR H CG2 1 
ATOM   3224 N  N   . VAL B 2 162 ? 23.037  -31.418 2.148   1.00 72.46  ? 152 VAL H N   1 
ATOM   3225 C  CA  . VAL B 2 162 ? 23.505  -32.384 1.166   1.00 72.90  ? 152 VAL H CA  1 
ATOM   3226 C  C   . VAL B 2 162 ? 23.943  -33.649 1.901   1.00 72.38  ? 152 VAL H C   1 
ATOM   3227 O  O   . VAL B 2 162 ? 24.735  -33.578 2.838   1.00 71.99  ? 152 VAL H O   1 
ATOM   3228 C  CB  . VAL B 2 162 ? 24.655  -31.815 0.309   1.00 73.26  ? 152 VAL H CB  1 
ATOM   3229 C  CG1 . VAL B 2 162 ? 25.208  -32.854 -0.657  1.00 73.42  ? 152 VAL H CG1 1 
ATOM   3230 C  CG2 . VAL B 2 162 ? 24.238  -30.556 -0.439  1.00 73.41  ? 152 VAL H CG2 1 
ATOM   3231 N  N   . SER B 2 163 ? 23.410  -34.797 1.464   1.00 72.63  ? 153 SER H N   1 
ATOM   3232 C  CA  . SER B 2 163 ? 23.868  -36.099 1.920   1.00 73.11  ? 153 SER H CA  1 
ATOM   3233 C  C   . SER B 2 163 ? 24.237  -36.950 0.708   1.00 73.72  ? 153 SER H C   1 
ATOM   3234 O  O   . SER B 2 163 ? 23.929  -36.580 -0.423  1.00 74.28  ? 153 SER H O   1 
ATOM   3235 C  CB  . SER B 2 163 ? 22.829  -36.776 2.779   1.00 73.66  ? 153 SER H CB  1 
ATOM   3236 O  OG  . SER B 2 163 ? 21.661  -37.070 2.028   1.00 74.59  ? 153 SER H OG  1 
ATOM   3237 N  N   . TRP B 2 164 ? 24.897  -38.087 0.960   1.00 73.58  ? 154 TRP H N   1 
ATOM   3238 C  CA  . TRP B 2 164 ? 25.409  -38.942 -0.100  1.00 73.45  ? 154 TRP H CA  1 
ATOM   3239 C  C   . TRP B 2 164 ? 24.893  -40.367 0.076   1.00 73.60  ? 154 TRP H C   1 
ATOM   3240 O  O   . TRP B 2 164 ? 24.989  -40.929 1.164   1.00 72.98  ? 154 TRP H O   1 
ATOM   3241 C  CB  . TRP B 2 164 ? 26.941  -38.900 -0.117  1.00 73.23  ? 154 TRP H CB  1 
ATOM   3242 C  CG  . TRP B 2 164 ? 27.507  -37.656 -0.728  1.00 72.30  ? 154 TRP H CG  1 
ATOM   3243 C  CD1 . TRP B 2 164 ? 27.921  -36.533 -0.074  1.00 71.46  ? 154 TRP H CD1 1 
ATOM   3244 C  CD2 . TRP B 2 164 ? 27.755  -37.421 -2.125  1.00 72.68  ? 154 TRP H CD2 1 
ATOM   3245 N  NE1 . TRP B 2 164 ? 28.390  -35.608 -0.967  1.00 71.39  ? 154 TRP H NE1 1 
ATOM   3246 C  CE2 . TRP B 2 164 ? 28.304  -36.125 -2.232  1.00 72.16  ? 154 TRP H CE2 1 
ATOM   3247 C  CE3 . TRP B 2 164 ? 27.563  -38.170 -3.292  1.00 73.73  ? 154 TRP H CE3 1 
ATOM   3248 C  CZ2 . TRP B 2 164 ? 28.663  -35.569 -3.459  1.00 72.37  ? 154 TRP H CZ2 1 
ATOM   3249 C  CZ3 . TRP B 2 164 ? 27.917  -37.620 -4.505  1.00 73.35  ? 154 TRP H CZ3 1 
ATOM   3250 C  CH2 . TRP B 2 164 ? 28.460  -36.337 -4.584  1.00 72.86  ? 154 TRP H CH2 1 
ATOM   3251 N  N   . ASN B 2 165 ? 24.353  -40.932 -1.013  1.00 74.20  ? 155 ASN H N   1 
ATOM   3252 C  CA  . ASN B 2 165 ? 23.853  -42.299 -1.038  1.00 75.55  ? 155 ASN H CA  1 
ATOM   3253 C  C   . ASN B 2 165 ? 22.824  -42.489 0.076   1.00 75.95  ? 155 ASN H C   1 
ATOM   3254 O  O   . ASN B 2 165 ? 22.798  -43.527 0.736   1.00 76.70  ? 155 ASN H O   1 
ATOM   3255 C  CB  . ASN B 2 165 ? 25.000  -43.312 -0.963  1.00 76.22  ? 155 ASN H CB  1 
ATOM   3256 C  CG  . ASN B 2 165 ? 25.928  -43.233 -2.158  1.00 76.08  ? 155 ASN H CG  1 
ATOM   3257 O  OD1 . ASN B 2 165 ? 25.515  -43.488 -3.287  1.00 76.72  ? 155 ASN H OD1 1 
ATOM   3258 N  ND2 . ASN B 2 165 ? 27.181  -42.882 -1.922  1.00 75.45  ? 155 ASN H ND2 1 
ATOM   3259 N  N   . SER B 2 166 ? 21.975  -41.468 0.254   1.00 75.37  ? 156 SER H N   1 
ATOM   3260 C  CA  . SER B 2 166 ? 20.941  -41.436 1.277   1.00 75.03  ? 156 SER H CA  1 
ATOM   3261 C  C   . SER B 2 166 ? 21.535  -41.665 2.668   1.00 74.81  ? 156 SER H C   1 
ATOM   3262 O  O   . SER B 2 166 ? 20.981  -42.421 3.464   1.00 76.75  ? 156 SER H O   1 
ATOM   3263 C  CB  . SER B 2 166 ? 19.850  -42.430 0.962   1.00 76.47  ? 156 SER H CB  1 
ATOM   3264 O  OG  . SER B 2 166 ? 19.367  -42.244 -0.361  1.00 76.63  ? 156 SER H OG  1 
ATOM   3265 N  N   . GLY B 2 167 ? 22.665  -41.001 2.949   1.00 72.98  ? 157 GLY H N   1 
ATOM   3266 C  CA  . GLY B 2 167 ? 23.282  -41.026 4.267   1.00 71.69  ? 157 GLY H CA  1 
ATOM   3267 C  C   . GLY B 2 167 ? 24.168  -42.250 4.498   1.00 72.42  ? 157 GLY H C   1 
ATOM   3268 O  O   . GLY B 2 167 ? 24.686  -42.430 5.598   1.00 72.95  ? 157 GLY H O   1 
ATOM   3269 N  N   . ALA B 2 168 ? 24.347  -43.078 3.461   1.00 73.33  ? 158 ALA H N   1 
ATOM   3270 C  CA  . ALA B 2 168 ? 25.142  -44.293 3.563   1.00 74.30  ? 158 ALA H CA  1 
ATOM   3271 C  C   . ALA B 2 168 ? 26.629  -43.964 3.439   1.00 74.88  ? 158 ALA H C   1 
ATOM   3272 O  O   . ALA B 2 168 ? 27.467  -44.691 3.970   1.00 75.91  ? 158 ALA H O   1 
ATOM   3273 C  CB  . ALA B 2 168 ? 24.707  -45.282 2.508   1.00 74.80  ? 158 ALA H CB  1 
ATOM   3274 N  N   . LEU B 2 169 ? 26.942  -42.873 2.724   1.00 74.43  ? 159 LEU H N   1 
ATOM   3275 C  CA  . LEU B 2 169 ? 28.310  -42.406 2.558   1.00 74.20  ? 159 LEU H CA  1 
ATOM   3276 C  C   . LEU B 2 169 ? 28.499  -41.107 3.339   1.00 73.37  ? 159 LEU H C   1 
ATOM   3277 O  O   . LEU B 2 169 ? 27.814  -40.120 3.076   1.00 72.30  ? 159 LEU H O   1 
ATOM   3278 C  CB  . LEU B 2 169 ? 28.584  -42.203 1.063   1.00 74.05  ? 159 LEU H CB  1 
ATOM   3279 C  CG  . LEU B 2 169 ? 29.971  -41.671 0.704   1.00 73.40  ? 159 LEU H CG  1 
ATOM   3280 C  CD1 . LEU B 2 169 ? 31.057  -42.651 1.124   1.00 74.61  ? 159 LEU H CD1 1 
ATOM   3281 C  CD2 . LEU B 2 169 ? 30.067  -41.382 -0.787  1.00 73.59  ? 159 LEU H CD2 1 
ATOM   3282 N  N   . THR B 2 170 ? 29.428  -41.132 4.305   1.00 73.53  ? 160 THR H N   1 
ATOM   3283 C  CA  . THR B 2 170 ? 29.751  -39.968 5.120   1.00 72.33  ? 160 THR H CA  1 
ATOM   3284 C  C   . THR B 2 170 ? 31.264  -39.740 5.163   1.00 72.37  ? 160 THR H C   1 
ATOM   3285 O  O   . THR B 2 170 ? 31.704  -38.595 5.237   1.00 71.13  ? 160 THR H O   1 
ATOM   3286 C  CB  . THR B 2 170 ? 29.172  -40.103 6.536   1.00 72.06  ? 160 THR H CB  1 
ATOM   3287 O  OG1 . THR B 2 170 ? 29.862  -41.148 7.224   1.00 73.52  ? 160 THR H OG1 1 
ATOM   3288 C  CG2 . THR B 2 170 ? 27.686  -40.389 6.540   1.00 71.67  ? 160 THR H CG2 1 
ATOM   3289 N  N   . SER B 2 171 ? 32.052  -40.825 5.139   1.00 73.87  ? 161 SER H N   1 
ATOM   3290 C  CA  . SER B 2 171 ? 33.504  -40.733 5.188   1.00 75.16  ? 161 SER H CA  1 
ATOM   3291 C  C   . SER B 2 171 ? 34.038  -40.058 3.927   1.00 75.36  ? 161 SER H C   1 
ATOM   3292 O  O   . SER B 2 171 ? 33.679  -40.444 2.816   1.00 75.09  ? 161 SER H O   1 
ATOM   3293 C  CB  . SER B 2 171 ? 34.133  -42.092 5.376   1.00 76.75  ? 161 SER H CB  1 
ATOM   3294 O  OG  . SER B 2 171 ? 33.851  -42.611 6.667   1.00 78.09  ? 161 SER H OG  1 
ATOM   3295 N  N   . GLY B 2 172 ? 34.895  -39.046 4.125   1.00 75.93  ? 162 GLY H N   1 
ATOM   3296 C  CA  . GLY B 2 172 ? 35.568  -38.353 3.037   1.00 75.67  ? 162 GLY H CA  1 
ATOM   3297 C  C   . GLY B 2 172 ? 34.822  -37.102 2.574   1.00 74.89  ? 162 GLY H C   1 
ATOM   3298 O  O   . GLY B 2 172 ? 35.353  -36.337 1.770   1.00 75.15  ? 162 GLY H O   1 
ATOM   3299 N  N   . VAL B 2 173 ? 33.605  -36.894 3.096   1.00 73.69  ? 163 VAL H N   1 
ATOM   3300 C  CA  . VAL B 2 173 ? 32.725  -35.840 2.617   1.00 72.23  ? 163 VAL H CA  1 
ATOM   3301 C  C   . VAL B 2 173 ? 33.163  -34.508 3.221   1.00 72.32  ? 163 VAL H C   1 
ATOM   3302 O  O   . VAL B 2 173 ? 33.497  -34.440 4.403   1.00 72.27  ? 163 VAL H O   1 
ATOM   3303 C  CB  . VAL B 2 173 ? 31.247  -36.140 2.943   1.00 70.67  ? 163 VAL H CB  1 
ATOM   3304 C  CG1 . VAL B 2 173 ? 30.332  -34.988 2.553   1.00 69.23  ? 163 VAL H CG1 1 
ATOM   3305 C  CG2 . VAL B 2 173 ? 30.777  -37.434 2.295   1.00 71.50  ? 163 VAL H CG2 1 
ATOM   3306 N  N   . HIS B 2 174 ? 33.160  -33.463 2.382   1.00 72.71  ? 164 HIS H N   1 
ATOM   3307 C  CA  . HIS B 2 174 ? 33.362  -32.090 2.815   1.00 72.35  ? 164 HIS H CA  1 
ATOM   3308 C  C   . HIS B 2 174 ? 32.310  -31.207 2.151   1.00 70.51  ? 164 HIS H C   1 
ATOM   3309 O  O   . HIS B 2 174 ? 32.326  -31.039 0.934   1.00 68.52  ? 164 HIS H O   1 
ATOM   3310 C  CB  . HIS B 2 174 ? 34.769  -31.597 2.457   1.00 74.59  ? 164 HIS H CB  1 
ATOM   3311 C  CG  . HIS B 2 174 ? 35.869  -32.215 3.256   1.00 77.26  ? 164 HIS H CG  1 
ATOM   3312 N  ND1 . HIS B 2 174 ? 35.962  -32.087 4.625   1.00 78.19  ? 164 HIS H ND1 1 
ATOM   3313 C  CD2 . HIS B 2 174 ? 36.927  -32.946 2.878   1.00 78.95  ? 164 HIS H CD2 1 
ATOM   3314 C  CE1 . HIS B 2 174 ? 37.040  -32.731 5.051   1.00 79.84  ? 164 HIS H CE1 1 
ATOM   3315 N  NE2 . HIS B 2 174 ? 37.641  -33.261 4.006   1.00 80.20  ? 164 HIS H NE2 1 
ATOM   3316 N  N   . THR B 2 175 ? 31.391  -30.665 2.961   1.00 70.31  ? 165 THR H N   1 
ATOM   3317 C  CA  . THR B 2 175 ? 30.394  -29.715 2.492   1.00 69.39  ? 165 THR H CA  1 
ATOM   3318 C  C   . THR B 2 175 ? 30.832  -28.309 2.895   1.00 69.43  ? 165 THR H C   1 
ATOM   3319 O  O   . THR B 2 175 ? 30.943  -28.007 4.082   1.00 70.27  ? 165 THR H O   1 
ATOM   3320 C  CB  . THR B 2 175 ? 28.999  -30.065 3.027   1.00 68.37  ? 165 THR H CB  1 
ATOM   3321 O  OG1 . THR B 2 175 ? 28.688  -31.397 2.616   1.00 68.27  ? 165 THR H OG1 1 
ATOM   3322 C  CG2 . THR B 2 175 ? 27.925  -29.119 2.537   1.00 67.87  ? 165 THR H CG2 1 
ATOM   3323 N  N   . PHE B 2 176 ? 31.082  -27.461 1.889   1.00 68.55  ? 166 PHE H N   1 
ATOM   3324 C  CA  . PHE B 2 176 ? 31.669  -26.146 2.098   1.00 66.80  ? 166 PHE H CA  1 
ATOM   3325 C  C   . PHE B 2 176 ? 30.582  -25.151 2.490   1.00 65.57  ? 166 PHE H C   1 
ATOM   3326 O  O   . PHE B 2 176 ? 29.446  -25.268 2.037   1.00 64.07  ? 166 PHE H O   1 
ATOM   3327 C  CB  . PHE B 2 176 ? 32.391  -25.688 0.828   1.00 66.57  ? 166 PHE H CB  1 
ATOM   3328 C  CG  . PHE B 2 176 ? 33.561  -26.555 0.442   1.00 66.37  ? 166 PHE H CG  1 
ATOM   3329 C  CD1 . PHE B 2 176 ? 34.799  -26.379 1.038   1.00 66.36  ? 166 PHE H CD1 1 
ATOM   3330 C  CD2 . PHE B 2 176 ? 33.413  -27.576 -0.485  1.00 66.51  ? 166 PHE H CD2 1 
ATOM   3331 C  CE1 . PHE B 2 176 ? 35.872  -27.187 0.693   1.00 66.92  ? 166 PHE H CE1 1 
ATOM   3332 C  CE2 . PHE B 2 176 ? 34.486  -28.387 -0.824  1.00 67.03  ? 166 PHE H CE2 1 
ATOM   3333 C  CZ  . PHE B 2 176 ? 35.713  -28.191 -0.234  1.00 67.27  ? 166 PHE H CZ  1 
ATOM   3334 N  N   . PRO B 2 177 ? 30.888  -24.152 3.352   1.00 65.38  ? 167 PRO H N   1 
ATOM   3335 C  CA  . PRO B 2 177 ? 29.987  -23.019 3.566   1.00 65.07  ? 167 PRO H CA  1 
ATOM   3336 C  C   . PRO B 2 177 ? 29.628  -22.332 2.251   1.00 65.09  ? 167 PRO H C   1 
ATOM   3337 O  O   . PRO B 2 177 ? 30.460  -22.234 1.351   1.00 66.79  ? 167 PRO H O   1 
ATOM   3338 C  CB  . PRO B 2 177 ? 30.791  -22.074 4.474   1.00 65.49  ? 167 PRO H CB  1 
ATOM   3339 C  CG  . PRO B 2 177 ? 31.764  -22.986 5.193   1.00 65.61  ? 167 PRO H CG  1 
ATOM   3340 C  CD  . PRO B 2 177 ? 32.092  -24.078 4.194   1.00 65.89  ? 167 PRO H CD  1 
ATOM   3341 N  N   . ALA B 2 178 ? 28.380  -21.866 2.150   1.00 64.57  ? 168 ALA H N   1 
ATOM   3342 C  CA  . ALA B 2 178 ? 27.897  -21.224 0.940   1.00 64.98  ? 168 ALA H CA  1 
ATOM   3343 C  C   . ALA B 2 178 ? 28.550  -19.853 0.790   1.00 65.88  ? 168 ALA H C   1 
ATOM   3344 O  O   . ALA B 2 178 ? 28.905  -19.219 1.782   1.00 65.94  ? 168 ALA H O   1 
ATOM   3345 C  CB  . ALA B 2 178 ? 26.392  -21.118 0.976   1.00 64.95  ? 168 ALA H CB  1 
ATOM   3346 N  N   . VAL B 2 179 ? 28.715  -19.422 -0.467  1.00 66.00  ? 169 VAL H N   1 
ATOM   3347 C  CA  . VAL B 2 179 ? 29.189  -18.084 -0.782  1.00 66.72  ? 169 VAL H CA  1 
ATOM   3348 C  C   . VAL B 2 179 ? 27.994  -17.257 -1.246  1.00 68.38  ? 169 VAL H C   1 
ATOM   3349 O  O   . VAL B 2 179 ? 27.055  -17.798 -1.829  1.00 68.63  ? 169 VAL H O   1 
ATOM   3350 C  CB  . VAL B 2 179 ? 30.309  -18.098 -1.843  1.00 66.62  ? 169 VAL H CB  1 
ATOM   3351 C  CG1 . VAL B 2 179 ? 31.537  -18.851 -1.357  1.00 66.22  ? 169 VAL H CG1 1 
ATOM   3352 C  CG2 . VAL B 2 179 ? 29.843  -18.651 -3.183  1.00 66.54  ? 169 VAL H CG2 1 
ATOM   3353 N  N   . LEU B 2 180 ? 28.039  -15.949 -0.968  1.00 69.61  ? 170 LEU H N   1 
ATOM   3354 C  CA  . LEU B 2 180 ? 27.041  -15.014 -1.460  1.00 70.33  ? 170 LEU H CA  1 
ATOM   3355 C  C   . LEU B 2 180 ? 27.492  -14.499 -2.825  1.00 72.29  ? 170 LEU H C   1 
ATOM   3356 O  O   . LEU B 2 180 ? 28.474  -13.766 -2.917  1.00 72.30  ? 170 LEU H O   1 
ATOM   3357 C  CB  . LEU B 2 180 ? 26.884  -13.870 -0.451  1.00 70.36  ? 170 LEU H CB  1 
ATOM   3358 C  CG  . LEU B 2 180 ? 25.881  -12.780 -0.827  1.00 70.68  ? 170 LEU H CG  1 
ATOM   3359 C  CD1 . LEU B 2 180 ? 24.457  -13.310 -0.770  1.00 70.60  ? 170 LEU H CD1 1 
ATOM   3360 C  CD2 . LEU B 2 180 ? 26.036  -11.569 0.078   1.00 70.52  ? 170 LEU H CD2 1 
ATOM   3361 N  N   . GLN B 2 181 ? 26.767  -14.898 -3.877  1.00 74.36  ? 171 GLN H N   1 
ATOM   3362 C  CA  . GLN B 2 181 ? 27.068  -14.464 -5.232  1.00 76.73  ? 171 GLN H CA  1 
ATOM   3363 C  C   . GLN B 2 181 ? 26.661  -13.001 -5.385  1.00 79.19  ? 171 GLN H C   1 
ATOM   3364 O  O   . GLN B 2 181 ? 25.976  -12.449 -4.525  1.00 80.70  ? 171 GLN H O   1 
ATOM   3365 C  CB  . GLN B 2 181 ? 26.342  -15.336 -6.260  1.00 76.89  ? 171 GLN H CB  1 
ATOM   3366 C  CG  . GLN B 2 181 ? 26.669  -16.820 -6.154  1.00 75.91  ? 171 GLN H CG  1 
ATOM   3367 C  CD  . GLN B 2 181 ? 25.885  -17.647 -7.144  1.00 76.81  ? 171 GLN H CD  1 
ATOM   3368 O  OE1 . GLN B 2 181 ? 25.122  -18.537 -6.776  1.00 76.00  ? 171 GLN H OE1 1 
ATOM   3369 N  NE2 . GLN B 2 181 ? 26.066  -17.352 -8.421  1.00 78.43  ? 171 GLN H NE2 1 
ATOM   3370 N  N   . SER B 2 182 ? 27.082  -12.385 -6.495  1.00 82.20  ? 172 SER H N   1 
ATOM   3371 C  CA  . SER B 2 182 ? 26.776  -10.990 -6.771  1.00 83.94  ? 172 SER H CA  1 
ATOM   3372 C  C   . SER B 2 182 ? 25.269  -10.785 -6.937  1.00 82.61  ? 172 SER H C   1 
ATOM   3373 O  O   . SER B 2 182 ? 24.761  -9.699  -6.662  1.00 81.74  ? 172 SER H O   1 
ATOM   3374 C  CB  . SER B 2 182 ? 27.532  -10.509 -7.984  1.00 87.16  ? 172 SER H CB  1 
ATOM   3375 O  OG  . SER B 2 182 ? 27.237  -11.314 -9.116  1.00 88.32  ? 172 SER H OG  1 
ATOM   3376 N  N   . SER B 2 183 ? 24.565  -11.837 -7.378  1.00 81.93  ? 173 SER H N   1 
ATOM   3377 C  CA  . SER B 2 183 ? 23.133  -11.776 -7.634  1.00 81.45  ? 173 SER H CA  1 
ATOM   3378 C  C   . SER B 2 183 ? 22.326  -11.842 -6.337  1.00 80.18  ? 173 SER H C   1 
ATOM   3379 O  O   . SER B 2 183 ? 21.115  -11.625 -6.360  1.00 80.81  ? 173 SER H O   1 
ATOM   3380 C  CB  . SER B 2 183 ? 22.717  -12.877 -8.576  1.00 81.14  ? 173 SER H CB  1 
ATOM   3381 O  OG  . SER B 2 183 ? 22.981  -14.153 -8.010  1.00 78.77  ? 173 SER H OG  1 
ATOM   3382 N  N   . GLY B 2 184 ? 22.988  -12.167 -5.218  1.00 78.98  ? 174 GLY H N   1 
ATOM   3383 C  CA  . GLY B 2 184 ? 22.318  -12.308 -3.935  1.00 77.40  ? 174 GLY H CA  1 
ATOM   3384 C  C   . GLY B 2 184 ? 21.922  -13.756 -3.650  1.00 76.15  ? 174 GLY H C   1 
ATOM   3385 O  O   . GLY B 2 184 ? 21.496  -14.077 -2.542  1.00 74.24  ? 174 GLY H O   1 
ATOM   3386 N  N   . LEU B 2 185 ? 22.066  -14.617 -4.667  1.00 76.14  ? 175 LEU H N   1 
ATOM   3387 C  CA  . LEU B 2 185 ? 21.817  -16.041 -4.534  1.00 74.59  ? 175 LEU H CA  1 
ATOM   3388 C  C   . LEU B 2 185 ? 23.072  -16.712 -3.983  1.00 74.05  ? 175 LEU H C   1 
ATOM   3389 O  O   . LEU B 2 185 ? 24.176  -16.193 -4.139  1.00 73.77  ? 175 LEU H O   1 
ATOM   3390 C  CB  . LEU B 2 185 ? 21.442  -16.610 -5.907  1.00 75.41  ? 175 LEU H CB  1 
ATOM   3391 C  CG  . LEU B 2 185 ? 20.258  -15.941 -6.607  1.00 76.09  ? 175 LEU H CG  1 
ATOM   3392 C  CD1 . LEU B 2 185 ? 19.927  -16.653 -7.910  1.00 77.51  ? 175 LEU H CD1 1 
ATOM   3393 C  CD2 . LEU B 2 185 ? 19.036  -15.898 -5.702  1.00 74.80  ? 175 LEU H CD2 1 
ATOM   3394 N  N   . TYR B 2 186 ? 22.883  -17.872 -3.345  1.00 73.52  ? 176 TYR H N   1 
ATOM   3395 C  CA  . TYR B 2 186 ? 23.967  -18.601 -2.705  1.00 72.42  ? 176 TYR H CA  1 
ATOM   3396 C  C   . TYR B 2 186 ? 24.423  -19.752 -3.598  1.00 72.51  ? 176 TYR H C   1 
ATOM   3397 O  O   . TYR B 2 186 ? 23.672  -20.219 -4.452  1.00 73.26  ? 176 TYR H O   1 
ATOM   3398 C  CB  . TYR B 2 186 ? 23.513  -19.130 -1.344  1.00 71.74  ? 176 TYR H CB  1 
ATOM   3399 C  CG  . TYR B 2 186 ? 23.253  -18.074 -0.299  1.00 70.95  ? 176 TYR H CG  1 
ATOM   3400 C  CD1 . TYR B 2 186 ? 24.299  -17.429 0.341   1.00 71.23  ? 176 TYR H CD1 1 
ATOM   3401 C  CD2 . TYR B 2 186 ? 21.960  -17.720 0.053   1.00 70.17  ? 176 TYR H CD2 1 
ATOM   3402 C  CE1 . TYR B 2 186 ? 24.069  -16.464 1.309   1.00 71.59  ? 176 TYR H CE1 1 
ATOM   3403 C  CE2 . TYR B 2 186 ? 21.713  -16.757 1.018   1.00 70.66  ? 176 TYR H CE2 1 
ATOM   3404 C  CZ  . TYR B 2 186 ? 22.771  -16.126 1.648   1.00 71.44  ? 176 TYR H CZ  1 
ATOM   3405 O  OH  . TYR B 2 186 ? 22.534  -15.168 2.606   1.00 72.19  ? 176 TYR H OH  1 
ATOM   3406 N  N   . SER B 2 187 ? 25.662  -20.204 -3.372  1.00 72.45  ? 177 SER H N   1 
ATOM   3407 C  CA  . SER B 2 187 ? 26.245  -21.315 -4.108  1.00 73.11  ? 177 SER H CA  1 
ATOM   3408 C  C   . SER B 2 187 ? 27.087  -22.160 -3.155  1.00 72.71  ? 177 SER H C   1 
ATOM   3409 O  O   . SER B 2 187 ? 27.844  -21.621 -2.352  1.00 72.23  ? 177 SER H O   1 
ATOM   3410 C  CB  . SER B 2 187 ? 27.060  -20.820 -5.277  1.00 75.04  ? 177 SER H CB  1 
ATOM   3411 O  OG  . SER B 2 187 ? 27.515  -21.899 -6.080  1.00 75.60  ? 177 SER H OG  1 
ATOM   3412 N  N   . LEU B 2 188 ? 26.950  -23.486 -3.264  1.00 74.27  ? 178 LEU H N   1 
ATOM   3413 C  CA  . LEU B 2 188 ? 27.547  -24.410 -2.313  1.00 75.63  ? 178 LEU H CA  1 
ATOM   3414 C  C   . LEU B 2 188 ? 28.163  -25.585 -3.069  1.00 75.89  ? 178 LEU H C   1 
ATOM   3415 O  O   . LEU B 2 188 ? 27.656  -25.982 -4.117  1.00 76.11  ? 178 LEU H O   1 
ATOM   3416 C  CB  . LEU B 2 188 ? 26.451  -24.883 -1.352  1.00 76.23  ? 178 LEU H CB  1 
ATOM   3417 C  CG  . LEU B 2 188 ? 26.897  -25.784 -0.201  1.00 77.10  ? 178 LEU H CG  1 
ATOM   3418 C  CD1 . LEU B 2 188 ? 26.635  -25.116 1.141   1.00 78.06  ? 178 LEU H CD1 1 
ATOM   3419 C  CD2 . LEU B 2 188 ? 26.208  -27.140 -0.270  1.00 77.73  ? 178 LEU H CD2 1 
ATOM   3420 N  N   . SER B 2 189 ? 29.262  -26.121 -2.523  1.00 75.83  ? 179 SER H N   1 
ATOM   3421 C  CA  . SER B 2 189 ? 29.891  -27.325 -3.044  1.00 75.32  ? 179 SER H CA  1 
ATOM   3422 C  C   . SER B 2 189 ? 29.923  -28.402 -1.964  1.00 73.85  ? 179 SER H C   1 
ATOM   3423 O  O   . SER B 2 189 ? 30.050  -28.098 -0.779  1.00 73.37  ? 179 SER H O   1 
ATOM   3424 C  CB  . SER B 2 189 ? 31.276  -27.037 -3.565  1.00 76.69  ? 179 SER H CB  1 
ATOM   3425 O  OG  . SER B 2 189 ? 31.217  -26.381 -4.822  1.00 78.34  ? 179 SER H OG  1 
ATOM   3426 N  N   . SER B 2 190 ? 29.795  -29.661 -2.400  1.00 73.18  ? 180 SER H N   1 
ATOM   3427 C  CA  . SER B 2 190 ? 29.960  -30.817 -1.534  1.00 72.58  ? 180 SER H CA  1 
ATOM   3428 C  C   . SER B 2 190 ? 30.735  -31.891 -2.292  1.00 72.30  ? 180 SER H C   1 
ATOM   3429 O  O   . SER B 2 190 ? 30.274  -32.364 -3.327  1.00 71.88  ? 180 SER H O   1 
ATOM   3430 C  CB  . SER B 2 190 ? 28.628  -31.337 -1.053  1.00 71.92  ? 180 SER H CB  1 
ATOM   3431 O  OG  . SER B 2 190 ? 28.805  -32.378 -0.103  1.00 70.87  ? 180 SER H OG  1 
ATOM   3432 N  N   . VAL B 2 191 ? 31.911  -32.256 -1.769  1.00 73.09  ? 181 VAL H N   1 
ATOM   3433 C  CA  . VAL B 2 191 ? 32.805  -33.186 -2.442  1.00 74.03  ? 181 VAL H CA  1 
ATOM   3434 C  C   . VAL B 2 191 ? 33.094  -34.360 -1.513  1.00 74.46  ? 181 VAL H C   1 
ATOM   3435 O  O   . VAL B 2 191 ? 32.935  -34.251 -0.299  1.00 75.82  ? 181 VAL H O   1 
ATOM   3436 C  CB  . VAL B 2 191 ? 34.112  -32.500 -2.888  1.00 75.20  ? 181 VAL H CB  1 
ATOM   3437 C  CG1 . VAL B 2 191 ? 33.839  -31.324 -3.814  1.00 76.37  ? 181 VAL H CG1 1 
ATOM   3438 C  CG2 . VAL B 2 191 ? 34.969  -32.070 -1.705  1.00 75.37  ? 181 VAL H CG2 1 
ATOM   3439 N  N   . VAL B 2 192 ? 33.530  -35.474 -2.112  1.00 74.55  ? 182 VAL H N   1 
ATOM   3440 C  CA  . VAL B 2 192 ? 33.904  -36.669 -1.374  1.00 74.27  ? 182 VAL H CA  1 
ATOM   3441 C  C   . VAL B 2 192 ? 35.052  -37.351 -2.113  1.00 74.58  ? 182 VAL H C   1 
ATOM   3442 O  O   . VAL B 2 192 ? 35.087  -37.353 -3.342  1.00 73.30  ? 182 VAL H O   1 
ATOM   3443 C  CB  . VAL B 2 192 ? 32.699  -37.615 -1.184  1.00 73.84  ? 182 VAL H CB  1 
ATOM   3444 C  CG1 . VAL B 2 192 ? 32.005  -37.938 -2.500  1.00 73.79  ? 182 VAL H CG1 1 
ATOM   3445 C  CG2 . VAL B 2 192 ? 33.088  -38.896 -0.459  1.00 73.75  ? 182 VAL H CG2 1 
ATOM   3446 N  N   . THR B 2 193 ? 35.996  -37.910 -1.345  1.00 75.74  ? 183 THR H N   1 
ATOM   3447 C  CA  . THR B 2 193 ? 37.077  -38.711 -1.897  1.00 76.62  ? 183 THR H CA  1 
ATOM   3448 C  C   . THR B 2 193 ? 36.733  -40.190 -1.734  1.00 76.54  ? 183 THR H C   1 
ATOM   3449 O  O   . THR B 2 193 ? 36.354  -40.630 -0.648  1.00 76.65  ? 183 THR H O   1 
ATOM   3450 C  CB  . THR B 2 193 ? 38.421  -38.355 -1.247  1.00 78.19  ? 183 THR H CB  1 
ATOM   3451 O  OG1 . THR B 2 193 ? 38.265  -38.400 0.172   1.00 79.13  ? 183 THR H OG1 1 
ATOM   3452 C  CG2 . THR B 2 193 ? 38.926  -36.989 -1.656  1.00 79.42  ? 183 THR H CG2 1 
ATOM   3453 N  N   . VAL B 2 194 ? 36.865  -40.943 -2.834  1.00 76.34  ? 184 VAL H N   1 
ATOM   3454 C  CA  . VAL B 2 194 ? 36.565  -42.366 -2.861  1.00 75.48  ? 184 VAL H CA  1 
ATOM   3455 C  C   . VAL B 2 194 ? 37.713  -43.081 -3.569  1.00 76.49  ? 184 VAL H C   1 
ATOM   3456 O  O   . VAL B 2 194 ? 38.521  -42.436 -4.234  1.00 77.78  ? 184 VAL H O   1 
ATOM   3457 C  CB  . VAL B 2 194 ? 35.215  -42.635 -3.554  1.00 74.66  ? 184 VAL H CB  1 
ATOM   3458 C  CG1 . VAL B 2 194 ? 34.087  -41.848 -2.904  1.00 74.53  ? 184 VAL H CG1 1 
ATOM   3459 C  CG2 . VAL B 2 194 ? 35.271  -42.354 -5.050  1.00 74.54  ? 184 VAL H CG2 1 
ATOM   3460 N  N   . PRO B 2 195 ? 37.836  -44.425 -3.449  1.00 76.73  ? 185 PRO H N   1 
ATOM   3461 C  CA  . PRO B 2 195 ? 38.851  -45.171 -4.195  1.00 76.66  ? 185 PRO H CA  1 
ATOM   3462 C  C   . PRO B 2 195 ? 38.695  -45.003 -5.705  1.00 76.84  ? 185 PRO H C   1 
ATOM   3463 O  O   . PRO B 2 195 ? 37.580  -45.011 -6.226  1.00 75.87  ? 185 PRO H O   1 
ATOM   3464 C  CB  . PRO B 2 195 ? 38.625  -46.637 -3.790  1.00 76.50  ? 185 PRO H CB  1 
ATOM   3465 C  CG  . PRO B 2 195 ? 37.862  -46.560 -2.483  1.00 76.30  ? 185 PRO H CG  1 
ATOM   3466 C  CD  . PRO B 2 195 ? 37.035  -45.295 -2.575  1.00 76.31  ? 185 PRO H CD  1 
ATOM   3467 N  N   . SER B 2 196 ? 39.834  -44.854 -6.392  1.00 78.27  ? 186 SER H N   1 
ATOM   3468 C  CA  . SER B 2 196 ? 39.863  -44.647 -7.831  1.00 78.67  ? 186 SER H CA  1 
ATOM   3469 C  C   . SER B 2 196 ? 39.493  -45.936 -8.562  1.00 78.31  ? 186 SER H C   1 
ATOM   3470 O  O   . SER B 2 196 ? 38.929  -45.891 -9.653  1.00 79.51  ? 186 SER H O   1 
ATOM   3471 C  CB  . SER B 2 196 ? 41.217  -44.142 -8.259  1.00 80.65  ? 186 SER H CB  1 
ATOM   3472 O  OG  . SER B 2 196 ? 41.209  -43.755 -9.624  1.00 83.88  ? 186 SER H OG  1 
ATOM   3473 N  N   . SER B 2 197 ? 39.812  -47.079 -7.942  1.00 77.64  ? 187 SER H N   1 
ATOM   3474 C  CA  . SER B 2 197 ? 39.597  -48.388 -8.538  1.00 77.47  ? 187 SER H CA  1 
ATOM   3475 C  C   . SER B 2 197 ? 38.109  -48.723 -8.630  1.00 78.07  ? 187 SER H C   1 
ATOM   3476 O  O   . SER B 2 197 ? 37.688  -49.392 -9.571  1.00 79.31  ? 187 SER H O   1 
ATOM   3477 C  CB  . SER B 2 197 ? 40.337  -49.447 -7.763  1.00 76.60  ? 187 SER H CB  1 
ATOM   3478 O  OG  . SER B 2 197 ? 39.931  -49.454 -6.402  1.00 74.59  ? 187 SER H OG  1 
ATOM   3479 N  N   . SER B 2 198 ? 37.322  -48.252 -7.655  1.00 79.18  ? 188 SER H N   1 
ATOM   3480 C  CA  . SER B 2 198 ? 35.943  -48.688 -7.495  1.00 79.69  ? 188 SER H CA  1 
ATOM   3481 C  C   . SER B 2 198 ? 34.960  -47.675 -8.086  1.00 80.11  ? 188 SER H C   1 
ATOM   3482 O  O   . SER B 2 198 ? 33.825  -47.582 -7.626  1.00 81.41  ? 188 SER H O   1 
ATOM   3483 C  CB  . SER B 2 198 ? 35.648  -48.951 -6.038  1.00 79.54  ? 188 SER H CB  1 
ATOM   3484 O  OG  . SER B 2 198 ? 35.681  -47.745 -5.286  1.00 79.63  ? 188 SER H OG  1 
ATOM   3485 N  N   . LEU B 2 199 ? 35.385  -46.934 -9.118  1.00 80.05  ? 189 LEU H N   1 
ATOM   3486 C  CA  . LEU B 2 199 ? 34.518  -45.961 -9.767  1.00 80.20  ? 189 LEU H CA  1 
ATOM   3487 C  C   . LEU B 2 199 ? 33.530  -46.668 -10.693 1.00 80.47  ? 189 LEU H C   1 
ATOM   3488 O  O   . LEU B 2 199 ? 32.452  -46.142 -10.959 1.00 81.38  ? 189 LEU H O   1 
ATOM   3489 C  CB  . LEU B 2 199 ? 35.371  -44.952 -10.544 1.00 81.07  ? 189 LEU H CB  1 
ATOM   3490 C  CG  . LEU B 2 199 ? 36.168  -43.958 -9.698  1.00 80.91  ? 189 LEU H CG  1 
ATOM   3491 C  CD1 . LEU B 2 199 ? 36.890  -42.955 -10.584 1.00 82.24  ? 189 LEU H CD1 1 
ATOM   3492 C  CD2 . LEU B 2 199 ? 35.272  -43.233 -8.704  1.00 80.32  ? 189 LEU H CD2 1 
ATOM   3493 N  N   . GLY B 2 200 ? 33.908  -47.856 -11.182 1.00 80.96  ? 190 GLY H N   1 
ATOM   3494 C  CA  . GLY B 2 200 ? 33.089  -48.610 -12.117 1.00 81.93  ? 190 GLY H CA  1 
ATOM   3495 C  C   . GLY B 2 200 ? 31.946  -49.357 -11.432 1.00 82.35  ? 190 GLY H C   1 
ATOM   3496 O  O   . GLY B 2 200 ? 30.866  -49.489 -12.007 1.00 83.34  ? 190 GLY H O   1 
ATOM   3497 N  N   . THR B 2 201 ? 32.194  -49.840 -10.207 1.00 81.63  ? 191 THR H N   1 
ATOM   3498 C  CA  . THR B 2 201 ? 31.270  -50.724 -9.511  1.00 81.63  ? 191 THR H CA  1 
ATOM   3499 C  C   . THR B 2 201 ? 30.303  -49.931 -8.629  1.00 81.16  ? 191 THR H C   1 
ATOM   3500 O  O   . THR B 2 201 ? 29.129  -50.285 -8.535  1.00 80.84  ? 191 THR H O   1 
ATOM   3501 C  CB  . THR B 2 201 ? 32.036  -51.766 -8.685  1.00 80.95  ? 191 THR H CB  1 
ATOM   3502 O  OG1 . THR B 2 201 ? 32.773  -51.095 -7.662  1.00 80.05  ? 191 THR H OG1 1 
ATOM   3503 C  CG2 . THR B 2 201 ? 32.981  -52.599 -9.524  1.00 80.79  ? 191 THR H CG2 1 
ATOM   3504 N  N   . GLN B 2 202 ? 30.807  -48.869 -7.984  1.00 80.37  ? 192 GLN H N   1 
ATOM   3505 C  CA  . GLN B 2 202 ? 30.053  -48.127 -6.983  1.00 79.32  ? 192 GLN H CA  1 
ATOM   3506 C  C   . GLN B 2 202 ? 29.228  -47.027 -7.647  1.00 78.63  ? 192 GLN H C   1 
ATOM   3507 O  O   . GLN B 2 202 ? 29.631  -46.473 -8.667  1.00 78.47  ? 192 GLN H O   1 
ATOM   3508 C  CB  . GLN B 2 202 ? 30.999  -47.502 -5.954  1.00 78.56  ? 192 GLN H CB  1 
ATOM   3509 C  CG  . GLN B 2 202 ? 31.951  -48.497 -5.304  1.00 78.97  ? 192 GLN H CG  1 
ATOM   3510 C  CD  . GLN B 2 202 ? 31.226  -49.638 -4.637  1.00 80.47  ? 192 GLN H CD  1 
ATOM   3511 O  OE1 . GLN B 2 202 ? 31.417  -50.804 -4.978  1.00 79.76  ? 192 GLN H OE1 1 
ATOM   3512 N  NE2 . GLN B 2 202 ? 30.377  -49.304 -3.678  1.00 81.89  ? 192 GLN H NE2 1 
ATOM   3513 N  N   . THR B 2 203 ? 28.076  -46.715 -7.037  1.00 78.55  ? 193 THR H N   1 
ATOM   3514 C  CA  . THR B 2 203 ? 27.230  -45.611 -7.464  1.00 78.88  ? 193 THR H CA  1 
ATOM   3515 C  C   . THR B 2 203 ? 27.274  -44.514 -6.403  1.00 77.51  ? 193 THR H C   1 
ATOM   3516 O  O   . THR B 2 203 ? 27.341  -44.808 -5.210  1.00 76.72  ? 193 THR H O   1 
ATOM   3517 C  CB  . THR B 2 203 ? 25.791  -46.078 -7.720  1.00 80.59  ? 193 THR H CB  1 
ATOM   3518 O  OG1 . THR B 2 203 ? 25.839  -47.242 -8.547  1.00 82.37  ? 193 THR H OG1 1 
ATOM   3519 C  CG2 . THR B 2 203 ? 24.935  -45.023 -8.386  1.00 81.18  ? 193 THR H CG2 1 
ATOM   3520 N  N   . TYR B 2 204 ? 27.227  -43.254 -6.856  1.00 76.59  ? 194 TYR H N   1 
ATOM   3521 C  CA  . TYR B 2 204 ? 27.346  -42.101 -5.977  1.00 75.13  ? 194 TYR H CA  1 
ATOM   3522 C  C   . TYR B 2 204 ? 26.268  -41.075 -6.323  1.00 75.88  ? 194 TYR H C   1 
ATOM   3523 O  O   . TYR B 2 204 ? 26.350  -40.415 -7.358  1.00 74.61  ? 194 TYR H O   1 
ATOM   3524 C  CB  . TYR B 2 204 ? 28.748  -41.497 -6.092  1.00 73.26  ? 194 TYR H CB  1 
ATOM   3525 C  CG  . TYR B 2 204 ? 29.864  -42.423 -5.676  1.00 72.20  ? 194 TYR H CG  1 
ATOM   3526 C  CD1 . TYR B 2 204 ? 30.033  -42.788 -4.349  1.00 71.17  ? 194 TYR H CD1 1 
ATOM   3527 C  CD2 . TYR B 2 204 ? 30.744  -42.948 -6.610  1.00 71.94  ? 194 TYR H CD2 1 
ATOM   3528 C  CE1 . TYR B 2 204 ? 31.055  -43.640 -3.959  1.00 70.69  ? 194 TYR H CE1 1 
ATOM   3529 C  CE2 . TYR B 2 204 ? 31.770  -43.801 -6.236  1.00 71.38  ? 194 TYR H CE2 1 
ATOM   3530 C  CZ  . TYR B 2 204 ? 31.927  -44.149 -4.906  1.00 70.97  ? 194 TYR H CZ  1 
ATOM   3531 O  OH  . TYR B 2 204 ? 32.943  -44.995 -4.533  1.00 71.12  ? 194 TYR H OH  1 
ATOM   3532 N  N   . ILE B 2 205 ? 25.263  -40.954 -5.445  1.00 77.57  ? 195 ILE H N   1 
ATOM   3533 C  CA  . ILE B 2 205 ? 24.185  -39.992 -5.611  1.00 79.18  ? 195 ILE H CA  1 
ATOM   3534 C  C   . ILE B 2 205 ? 24.259  -38.979 -4.471  1.00 79.07  ? 195 ILE H C   1 
ATOM   3535 O  O   . ILE B 2 205 ? 24.311  -39.364 -3.305  1.00 78.33  ? 195 ILE H O   1 
ATOM   3536 C  CB  . ILE B 2 205 ? 22.804  -40.682 -5.648  1.00 80.73  ? 195 ILE H CB  1 
ATOM   3537 C  CG1 . ILE B 2 205 ? 22.772  -41.888 -6.593  1.00 82.14  ? 195 ILE H CG1 1 
ATOM   3538 C  CG2 . ILE B 2 205 ? 21.711  -39.676 -5.983  1.00 81.72  ? 195 ILE H CG2 1 
ATOM   3539 C  CD1 . ILE B 2 205 ? 23.126  -43.204 -5.933  1.00 82.46  ? 195 ILE H CD1 1 
ATOM   3540 N  N   . CYS B 2 206 ? 24.258  -37.687 -4.826  1.00 79.86  ? 196 CYS H N   1 
ATOM   3541 C  CA  . CYS B 2 206 ? 24.145  -36.617 -3.849  1.00 80.60  ? 196 CYS H CA  1 
ATOM   3542 C  C   . CYS B 2 206 ? 22.672  -36.258 -3.671  1.00 81.79  ? 196 CYS H C   1 
ATOM   3543 O  O   . CYS B 2 206 ? 21.936  -36.167 -4.652  1.00 82.84  ? 196 CYS H O   1 
ATOM   3544 C  CB  . CYS B 2 206 ? 24.925  -35.380 -4.280  1.00 80.71  ? 196 CYS H CB  1 
ATOM   3545 S  SG  . CYS B 2 206 ? 24.127  -34.456 -5.618  1.00 82.55  ? 196 CYS H SG  1 
ATOM   3546 N  N   . ASN B 2 207 ? 22.260  -36.049 -2.415  1.00 81.63  ? 197 ASN H N   1 
ATOM   3547 C  CA  . ASN B 2 207 ? 20.877  -35.742 -2.088  1.00 81.85  ? 197 ASN H CA  1 
ATOM   3548 C  C   . ASN B 2 207 ? 20.796  -34.300 -1.595  1.00 81.77  ? 197 ASN H C   1 
ATOM   3549 O  O   . ASN B 2 207 ? 21.162  -34.007 -0.459  1.00 80.43  ? 197 ASN H O   1 
ATOM   3550 C  CB  . ASN B 2 207 ? 20.315  -36.711 -1.045  1.00 81.49  ? 197 ASN H CB  1 
ATOM   3551 C  CG  . ASN B 2 207 ? 20.778  -38.135 -1.261  1.00 80.14  ? 197 ASN H CG  1 
ATOM   3552 O  OD1 . ASN B 2 207 ? 20.365  -38.794 -2.212  1.00 80.15  ? 197 ASN H OD1 1 
ATOM   3553 N  ND2 . ASN B 2 207 ? 21.642  -38.612 -0.381  1.00 78.63  ? 197 ASN H ND2 1 
ATOM   3554 N  N   . VAL B 2 208 ? 20.322  -33.409 -2.472  1.00 82.93  ? 198 VAL H N   1 
ATOM   3555 C  CA  . VAL B 2 208 ? 20.172  -32.001 -2.147  1.00 82.79  ? 198 VAL H CA  1 
ATOM   3556 C  C   . VAL B 2 208 ? 18.760  -31.780 -1.614  1.00 84.38  ? 198 VAL H C   1 
ATOM   3557 O  O   . VAL B 2 208 ? 17.810  -32.388 -2.103  1.00 86.63  ? 198 VAL H O   1 
ATOM   3558 C  CB  . VAL B 2 208 ? 20.464  -31.121 -3.376  1.00 82.95  ? 198 VAL H CB  1 
ATOM   3559 C  CG1 . VAL B 2 208 ? 20.181  -29.650 -3.106  1.00 82.74  ? 198 VAL H CG1 1 
ATOM   3560 C  CG2 . VAL B 2 208 ? 21.890  -31.319 -3.867  1.00 82.42  ? 198 VAL H CG2 1 
ATOM   3561 N  N   . ASN B 2 209 ? 18.642  -30.907 -0.608  1.00 83.96  ? 199 ASN H N   1 
ATOM   3562 C  CA  . ASN B 2 209 ? 17.363  -30.617 0.018   1.00 85.11  ? 199 ASN H CA  1 
ATOM   3563 C  C   . ASN B 2 209 ? 17.322  -29.135 0.382   1.00 82.92  ? 199 ASN H C   1 
ATOM   3564 O  O   . ASN B 2 209 ? 18.185  -28.651 1.110   1.00 81.70  ? 199 ASN H O   1 
ATOM   3565 C  CB  . ASN B 2 209 ? 17.124  -31.514 1.237   1.00 86.78  ? 199 ASN H CB  1 
ATOM   3566 C  CG  . ASN B 2 209 ? 15.686  -31.504 1.715   1.00 89.20  ? 199 ASN H CG  1 
ATOM   3567 O  OD1 . ASN B 2 209 ? 14.777  -31.864 0.970   1.00 91.75  ? 199 ASN H OD1 1 
ATOM   3568 N  ND2 . ASN B 2 209 ? 15.472  -31.105 2.958   1.00 89.55  ? 199 ASN H ND2 1 
ATOM   3569 N  N   . HIS B 2 210 ? 16.318  -28.429 -0.155  1.00 82.28  ? 200 HIS H N   1 
ATOM   3570 C  CA  . HIS B 2 210 ? 16.106  -27.017 0.116   1.00 80.57  ? 200 HIS H CA  1 
ATOM   3571 C  C   . HIS B 2 210 ? 14.665  -26.841 0.590   1.00 81.24  ? 200 HIS H C   1 
ATOM   3572 O  O   . HIS B 2 210 ? 13.751  -26.731 -0.224  1.00 81.36  ? 200 HIS H O   1 
ATOM   3573 C  CB  . HIS B 2 210 ? 16.447  -26.189 -1.130  1.00 79.71  ? 200 HIS H CB  1 
ATOM   3574 C  CG  . HIS B 2 210 ? 16.424  -24.709 -0.930  1.00 78.05  ? 200 HIS H CG  1 
ATOM   3575 N  ND1 . HIS B 2 210 ? 15.600  -23.878 -1.658  1.00 78.10  ? 200 HIS H ND1 1 
ATOM   3576 C  CD2 . HIS B 2 210 ? 17.124  -23.910 -0.116  1.00 76.27  ? 200 HIS H CD2 1 
ATOM   3577 C  CE1 . HIS B 2 210 ? 15.796  -22.624 -1.279  1.00 77.08  ? 200 HIS H CE1 1 
ATOM   3578 N  NE2 . HIS B 2 210 ? 16.717  -22.621 -0.343  1.00 75.87  ? 200 HIS H NE2 1 
ATOM   3579 N  N   . LYS B 2 211 ? 14.483  -26.834 1.918   1.00 81.81  ? 201 LYS H N   1 
ATOM   3580 C  CA  . LYS B 2 211 ? 13.162  -26.844 2.530   1.00 83.91  ? 201 LYS H CA  1 
ATOM   3581 C  C   . LYS B 2 211 ? 12.424  -25.532 2.265   1.00 83.19  ? 201 LYS H C   1 
ATOM   3582 O  O   . LYS B 2 211 ? 11.211  -25.555 2.069   1.00 84.55  ? 201 LYS H O   1 
ATOM   3583 C  CB  . LYS B 2 211 ? 13.264  -27.133 4.032   1.00 84.88  ? 201 LYS H CB  1 
ATOM   3584 C  CG  . LYS B 2 211 ? 13.762  -28.530 4.382   1.00 86.03  ? 201 LYS H CG  1 
ATOM   3585 C  CD  . LYS B 2 211 ? 13.623  -28.887 5.848   1.00 86.93  ? 201 LYS H CD  1 
ATOM   3586 C  CE  . LYS B 2 211 ? 14.070  -30.302 6.152   1.00 87.76  ? 201 LYS H CE  1 
ATOM   3587 N  NZ  . LYS B 2 211 ? 13.826  -30.666 7.569   1.00 89.42  ? 201 LYS H NZ  1 
ATOM   3588 N  N   . PRO B 2 212 ? 13.098  -24.355 2.264   1.00 81.53  ? 202 PRO H N   1 
ATOM   3589 C  CA  . PRO B 2 212 ? 12.443  -23.094 1.900   1.00 81.58  ? 202 PRO H CA  1 
ATOM   3590 C  C   . PRO B 2 212 ? 11.692  -23.086 0.566   1.00 83.44  ? 202 PRO H C   1 
ATOM   3591 O  O   . PRO B 2 212 ? 10.726  -22.341 0.418   1.00 84.95  ? 202 PRO H O   1 
ATOM   3592 C  CB  . PRO B 2 212 ? 13.614  -22.101 1.844   1.00 78.98  ? 202 PRO H CB  1 
ATOM   3593 C  CG  . PRO B 2 212 ? 14.600  -22.649 2.849   1.00 78.12  ? 202 PRO H CG  1 
ATOM   3594 C  CD  . PRO B 2 212 ? 14.496  -24.150 2.683   1.00 79.66  ? 202 PRO H CD  1 
ATOM   3595 N  N   . SER B 2 213 ? 12.141  -23.905 -0.398  1.00 84.40  ? 203 SER H N   1 
ATOM   3596 C  CA  . SER B 2 213 ? 11.498  -23.992 -1.702  1.00 86.30  ? 203 SER H CA  1 
ATOM   3597 C  C   . SER B 2 213 ? 10.878  -25.372 -1.934  1.00 89.43  ? 203 SER H C   1 
ATOM   3598 O  O   . SER B 2 213 ? 10.348  -25.625 -3.014  1.00 91.52  ? 203 SER H O   1 
ATOM   3599 C  CB  . SER B 2 213 ? 12.476  -23.656 -2.802  1.00 84.67  ? 203 SER H CB  1 
ATOM   3600 O  OG  . SER B 2 213 ? 13.459  -24.672 -2.940  1.00 82.11  ? 203 SER H OG  1 
ATOM   3601 N  N   . ASN B 2 214 ? 10.938  -26.250 -0.922  1.00 90.75  ? 204 ASN H N   1 
ATOM   3602 C  CA  . ASN B 2 214 ? 10.484  -27.630 -1.037  1.00 93.71  ? 204 ASN H CA  1 
ATOM   3603 C  C   . ASN B 2 214 ? 11.148  -28.305 -2.236  1.00 94.67  ? 204 ASN H C   1 
ATOM   3604 O  O   . ASN B 2 214 ? 10.487  -29.014 -2.994  1.00 97.54  ? 204 ASN H O   1 
ATOM   3605 C  CB  . ASN B 2 214 ? 8.958   -27.734 -1.145  1.00 96.26  ? 204 ASN H CB  1 
ATOM   3606 C  CG  . ASN B 2 214 ? 8.234   -27.221 0.080   1.00 97.01  ? 204 ASN H CG  1 
ATOM   3607 O  OD1 . ASN B 2 214 ? 7.371   -26.352 -0.022  1.00 98.32  ? 204 ASN H OD1 1 
ATOM   3608 N  ND2 . ASN B 2 214 ? 8.564   -27.766 1.240   1.00 96.54  ? 204 ASN H ND2 1 
ATOM   3609 N  N   . THR B 2 215 ? 12.460  -28.089 -2.393  1.00 93.22  ? 205 THR H N   1 
ATOM   3610 C  CA  . THR B 2 215 ? 13.196  -28.616 -3.530  1.00 94.06  ? 205 THR H CA  1 
ATOM   3611 C  C   . THR B 2 215 ? 14.140  -29.718 -3.058  1.00 94.20  ? 205 THR H C   1 
ATOM   3612 O  O   . THR B 2 215 ? 15.160  -29.438 -2.430  1.00 92.65  ? 205 THR H O   1 
ATOM   3613 C  CB  . THR B 2 215 ? 13.961  -27.506 -4.262  1.00 92.98  ? 205 THR H CB  1 
ATOM   3614 O  OG1 . THR B 2 215 ? 13.018  -26.506 -4.652  1.00 94.57  ? 205 THR H OG1 1 
ATOM   3615 C  CG2 . THR B 2 215 ? 14.709  -28.008 -5.478  1.00 92.55  ? 205 THR H CG2 1 
ATOM   3616 N  N   . LYS B 2 216 ? 13.773  -30.969 -3.361  1.00 96.72  ? 206 LYS H N   1 
ATOM   3617 C  CA  . LYS B 2 216 ? 14.646  -32.111 -3.155  1.00 96.35  ? 206 LYS H CA  1 
ATOM   3618 C  C   . LYS B 2 216 ? 15.131  -32.596 -4.520  1.00 95.47  ? 206 LYS H C   1 
ATOM   3619 O  O   . LYS B 2 216 ? 14.330  -32.760 -5.438  1.00 96.59  ? 206 LYS H O   1 
ATOM   3620 C  CB  . LYS B 2 216 ? 13.912  -33.218 -2.392  1.00 99.61  ? 206 LYS H CB  1 
ATOM   3621 C  CG  . LYS B 2 216 ? 14.777  -34.404 -1.985  1.00 101.02 ? 206 LYS H CG  1 
ATOM   3622 C  CD  . LYS B 2 216 ? 14.042  -35.438 -1.161  1.00 104.13 ? 206 LYS H CD  1 
ATOM   3623 C  CE  . LYS B 2 216 ? 14.911  -36.622 -0.792  1.00 104.02 ? 206 LYS H CE  1 
ATOM   3624 N  NZ  . LYS B 2 216 ? 14.171  -37.604 0.036   1.00 106.74 ? 206 LYS H NZ  1 
ATOM   3625 N  N   . VAL B 2 217 ? 16.448  -32.805 -4.641  1.00 92.85  ? 207 VAL H N   1 
ATOM   3626 C  CA  . VAL B 2 217 ? 17.056  -33.228 -5.893  1.00 92.73  ? 207 VAL H CA  1 
ATOM   3627 C  C   . VAL B 2 217 ? 18.104  -34.298 -5.597  1.00 90.72  ? 207 VAL H C   1 
ATOM   3628 O  O   . VAL B 2 217 ? 18.906  -34.147 -4.678  1.00 87.92  ? 207 VAL H O   1 
ATOM   3629 C  CB  . VAL B 2 217 ? 17.676  -32.035 -6.650  1.00 92.80  ? 207 VAL H CB  1 
ATOM   3630 C  CG1 . VAL B 2 217 ? 18.395  -32.481 -7.915  1.00 93.72  ? 207 VAL H CG1 1 
ATOM   3631 C  CG2 . VAL B 2 217 ? 16.640  -30.967 -6.970  1.00 94.26  ? 207 VAL H CG2 1 
ATOM   3632 N  N   . ASP B 2 218 ? 18.076  -35.376 -6.391  1.00 91.84  ? 208 ASP H N   1 
ATOM   3633 C  CA  . ASP B 2 218 ? 19.084  -36.423 -6.337  1.00 91.03  ? 208 ASP H CA  1 
ATOM   3634 C  C   . ASP B 2 218 ? 19.810  -36.461 -7.680  1.00 91.16  ? 208 ASP H C   1 
ATOM   3635 O  O   . ASP B 2 218 ? 19.166  -36.515 -8.726  1.00 93.42  ? 208 ASP H O   1 
ATOM   3636 C  CB  . ASP B 2 218 ? 18.463  -37.781 -6.003  1.00 92.47  ? 208 ASP H CB  1 
ATOM   3637 C  CG  . ASP B 2 218 ? 17.711  -37.805 -4.683  1.00 93.63  ? 208 ASP H CG  1 
ATOM   3638 O  OD1 . ASP B 2 218 ? 18.291  -37.368 -3.669  1.00 93.06  ? 208 ASP H OD1 1 
ATOM   3639 O  OD2 . ASP B 2 218 ? 16.555  -38.273 -4.676  1.00 96.21  ? 208 ASP H OD2 1 
ATOM   3640 N  N   . LYS B 2 219 ? 21.149  -36.430 -7.636  1.00 88.99  ? 209 LYS H N   1 
ATOM   3641 C  CA  . LYS B 2 219 ? 21.962  -36.373 -8.841  1.00 89.42  ? 209 LYS H CA  1 
ATOM   3642 C  C   . LYS B 2 219 ? 23.084  -37.403 -8.745  1.00 88.30  ? 209 LYS H C   1 
ATOM   3643 O  O   . LYS B 2 219 ? 23.934  -37.315 -7.861  1.00 86.58  ? 209 LYS H O   1 
ATOM   3644 C  CB  . LYS B 2 219 ? 22.536  -34.964 -9.030  1.00 89.52  ? 209 LYS H CB  1 
ATOM   3645 C  CG  . LYS B 2 219 ? 23.032  -34.649 -10.436 1.00 91.21  ? 209 LYS H CG  1 
ATOM   3646 C  CD  . LYS B 2 219 ? 21.910  -34.393 -11.425 1.00 94.38  ? 209 LYS H CD  1 
ATOM   3647 C  CE  . LYS B 2 219 ? 22.377  -34.323 -12.865 1.00 96.70  ? 209 LYS H CE  1 
ATOM   3648 N  NZ  . LYS B 2 219 ? 22.839  -35.642 -13.364 1.00 97.26  ? 209 LYS H NZ  1 
ATOM   3649 N  N   . LYS B 2 220 ? 23.072  -38.375 -9.668  1.00 88.72  ? 210 LYS H N   1 
ATOM   3650 C  CA  . LYS B 2 220 ? 24.116  -39.383 -9.751  1.00 87.64  ? 210 LYS H CA  1 
ATOM   3651 C  C   . LYS B 2 220 ? 25.329  -38.784 -10.457 1.00 85.18  ? 210 LYS H C   1 
ATOM   3652 O  O   . LYS B 2 220 ? 25.206  -38.251 -11.557 1.00 85.54  ? 210 LYS H O   1 
ATOM   3653 C  CB  . LYS B 2 220 ? 23.614  -40.627 -10.492 1.00 91.18  ? 210 LYS H CB  1 
ATOM   3654 C  CG  . LYS B 2 220 ? 24.628  -41.758 -10.620 1.00 91.85  ? 210 LYS H CG  1 
ATOM   3655 C  CD  . LYS B 2 220 ? 24.054  -43.048 -11.171 1.00 94.04  ? 210 LYS H CD  1 
ATOM   3656 C  CE  . LYS B 2 220 ? 23.502  -42.911 -12.574 1.00 97.26  ? 210 LYS H CE  1 
ATOM   3657 N  NZ  . LYS B 2 220 ? 23.066  -44.218 -13.119 1.00 99.55  ? 210 LYS H NZ  1 
ATOM   3658 N  N   . VAL B 2 221 ? 26.497  -38.894 -9.811  1.00 82.79  ? 211 VAL H N   1 
ATOM   3659 C  CA  . VAL B 2 221 ? 27.733  -38.317 -10.314 1.00 82.11  ? 211 VAL H CA  1 
ATOM   3660 C  C   . VAL B 2 221 ? 28.516  -39.404 -11.049 1.00 82.06  ? 211 VAL H C   1 
ATOM   3661 O  O   . VAL B 2 221 ? 29.263  -40.159 -10.431 1.00 81.08  ? 211 VAL H O   1 
ATOM   3662 C  CB  . VAL B 2 221 ? 28.554  -37.695 -9.166  1.00 80.27  ? 211 VAL H CB  1 
ATOM   3663 C  CG1 . VAL B 2 221 ? 29.874  -37.119 -9.657  1.00 81.04  ? 211 VAL H CG1 1 
ATOM   3664 C  CG2 . VAL B 2 221 ? 27.758  -36.640 -8.412  1.00 79.43  ? 211 VAL H CG2 1 
ATOM   3665 N  N   . GLU B 2 222 ? 28.336  -39.468 -12.374 1.00 83.46  ? 212 GLU H N   1 
ATOM   3666 C  CA  . GLU B 2 222 ? 28.985  -40.474 -13.200 1.00 84.21  ? 212 GLU H CA  1 
ATOM   3667 C  C   . GLU B 2 222 ? 30.385  -39.998 -13.579 1.00 83.81  ? 212 GLU H C   1 
ATOM   3668 O  O   . GLU B 2 222 ? 30.600  -38.804 -13.778 1.00 83.27  ? 212 GLU H O   1 
ATOM   3669 C  CB  . GLU B 2 222 ? 28.155  -40.754 -14.455 1.00 87.16  ? 212 GLU H CB  1 
ATOM   3670 C  CG  . GLU B 2 222 ? 26.715  -41.132 -14.159 1.00 88.80  ? 212 GLU H CG  1 
ATOM   3671 C  CD  . GLU B 2 222 ? 25.965  -41.726 -15.339 1.00 92.32  ? 212 GLU H CD  1 
ATOM   3672 O  OE1 . GLU B 2 222 ? 25.011  -41.081 -15.820 1.00 93.80  ? 212 GLU H OE1 1 
ATOM   3673 O  OE2 . GLU B 2 222 ? 26.332  -42.838 -15.769 1.00 94.15  ? 212 GLU H OE2 1 
ATOM   3674 N  N   . PRO B 2 223 ? 31.375  -40.914 -13.702 1.00 84.03  ? 213 PRO H N   1 
ATOM   3675 C  CA  . PRO B 2 223 ? 32.751  -40.534 -14.036 1.00 84.52  ? 213 PRO H CA  1 
ATOM   3676 C  C   . PRO B 2 223 ? 32.945  -40.111 -15.492 1.00 86.55  ? 213 PRO H C   1 
ATOM   3677 O  O   . PRO B 2 223 ? 32.121  -40.421 -16.350 1.00 86.98  ? 213 PRO H O   1 
ATOM   3678 C  CB  . PRO B 2 223 ? 33.548  -41.814 -13.734 1.00 83.55  ? 213 PRO H CB  1 
ATOM   3679 C  CG  . PRO B 2 223 ? 32.555  -42.931 -13.968 1.00 83.83  ? 213 PRO H CG  1 
ATOM   3680 C  CD  . PRO B 2 223 ? 31.223  -42.367 -13.518 1.00 83.56  ? 213 PRO H CD  1 
ATOM   3681 N  N   . LYS B 2 224 ? 34.047  -39.391 -15.746 1.00 88.18  ? 214 LYS H N   1 
ATOM   3682 C  CA  . LYS B 2 224 ? 34.413  -38.950 -17.083 1.00 92.43  ? 214 LYS H CA  1 
ATOM   3683 C  C   . LYS B 2 224 ? 35.918  -39.163 -17.288 1.00 92.85  ? 214 LYS H C   1 
ATOM   3684 O  O   . LYS B 2 224 ? 36.273  -40.225 -17.838 1.00 92.74  ? 214 LYS H O   1 
ATOM   3685 C  CB  . LYS B 2 224 ? 34.050  -37.476 -17.290 1.00 94.40  ? 214 LYS H CB  1 
ATOM   3686 C  CG  . LYS B 2 224 ? 32.561  -37.157 -17.246 1.00 95.41  ? 214 LYS H CG  1 
ATOM   3687 C  CD  . LYS B 2 224 ? 32.251  -35.693 -17.489 1.00 97.53  ? 214 LYS H CD  1 
ATOM   3688 C  CE  . LYS B 2 224 ? 30.782  -35.358 -17.325 1.00 98.04  ? 214 LYS H CE  1 
ATOM   3689 N  NZ  . LYS B 2 224 ? 30.523  -33.912 -17.521 1.00 98.74  ? 214 LYS H NZ  1 
ATOM   3690 N  N   . GLU C 3 1   ? 19.517  -7.515  32.609  1.00 84.72  ? 1   GLU L N   1 
ATOM   3691 C  CA  . GLU C 3 1   ? 19.996  -8.924  32.589  1.00 82.15  ? 1   GLU L CA  1 
ATOM   3692 C  C   . GLU C 3 1   ? 21.508  -8.949  32.791  1.00 80.03  ? 1   GLU L C   1 
ATOM   3693 O  O   . GLU C 3 1   ? 22.183  -7.943  32.587  1.00 79.66  ? 1   GLU L O   1 
ATOM   3694 C  CB  . GLU C 3 1   ? 19.596  -9.611  31.281  1.00 81.91  ? 1   GLU L CB  1 
ATOM   3695 C  CG  . GLU C 3 1   ? 20.130  -8.927  30.035  1.00 82.69  ? 1   GLU L CG  1 
ATOM   3696 C  CD  . GLU C 3 1   ? 19.643  -9.544  28.735  1.00 83.60  ? 1   GLU L CD  1 
ATOM   3697 O  OE1 . GLU C 3 1   ? 18.414  -9.558  28.516  1.00 85.79  ? 1   GLU L OE1 1 
ATOM   3698 O  OE2 . GLU C 3 1   ? 20.492  -10.012 27.949  1.00 83.16  ? 1   GLU L OE2 1 
ATOM   3699 N  N   . ILE C 3 2   ? 22.021  -10.121 33.184  1.00 78.71  ? 2   ILE L N   1 
ATOM   3700 C  CA  . ILE C 3 2   ? 23.424  -10.290 33.528  1.00 77.60  ? 2   ILE L CA  1 
ATOM   3701 C  C   . ILE C 3 2   ? 24.208  -10.577 32.248  1.00 75.95  ? 2   ILE L C   1 
ATOM   3702 O  O   . ILE C 3 2   ? 23.756  -11.342 31.398  1.00 73.69  ? 2   ILE L O   1 
ATOM   3703 C  CB  . ILE C 3 2   ? 23.591  -11.399 34.590  1.00 77.38  ? 2   ILE L CB  1 
ATOM   3704 C  CG1 . ILE C 3 2   ? 22.653  -11.182 35.782  1.00 78.60  ? 2   ILE L CG1 1 
ATOM   3705 C  CG2 . ILE C 3 2   ? 25.039  -11.519 35.039  1.00 77.20  ? 2   ILE L CG2 1 
ATOM   3706 C  CD1 . ILE C 3 2   ? 22.916  -12.099 36.955  1.00 79.02  ? 2   ILE L CD1 1 
ATOM   3707 N  N   . VAL C 3 3   ? 25.386  -9.950  32.126  1.00 75.88  ? 3   VAL L N   1 
ATOM   3708 C  CA  . VAL C 3 3   ? 26.206  -10.051 30.929  1.00 75.79  ? 3   VAL L CA  1 
ATOM   3709 C  C   . VAL C 3 3   ? 27.321  -11.065 31.175  1.00 75.26  ? 3   VAL L C   1 
ATOM   3710 O  O   . VAL C 3 3   ? 28.236  -10.806 31.954  1.00 76.21  ? 3   VAL L O   1 
ATOM   3711 C  CB  . VAL C 3 3   ? 26.781  -8.679  30.526  1.00 76.04  ? 3   VAL L CB  1 
ATOM   3712 C  CG1 . VAL C 3 3   ? 27.698  -8.786  29.315  1.00 75.52  ? 3   VAL L CG1 1 
ATOM   3713 C  CG2 . VAL C 3 3   ? 25.682  -7.655  30.279  1.00 76.91  ? 3   VAL L CG2 1 
ATOM   3714 N  N   . MET C 3 4   ? 27.230  -12.216 30.498  1.00 74.25  ? 4   MET L N   1 
ATOM   3715 C  CA  . MET C 3 4   ? 28.265  -13.234 30.559  1.00 73.57  ? 4   MET L CA  1 
ATOM   3716 C  C   . MET C 3 4   ? 29.395  -12.834 29.615  1.00 74.31  ? 4   MET L C   1 
ATOM   3717 O  O   . MET C 3 4   ? 29.152  -12.586 28.436  1.00 74.10  ? 4   MET L O   1 
ATOM   3718 C  CB  . MET C 3 4   ? 27.721  -14.601 30.128  1.00 72.41  ? 4   MET L CB  1 
ATOM   3719 C  CG  . MET C 3 4   ? 26.695  -15.202 31.078  1.00 71.85  ? 4   MET L CG  1 
ATOM   3720 S  SD  . MET C 3 4   ? 27.290  -15.427 32.776  1.00 71.37  ? 4   MET L SD  1 
ATOM   3721 C  CE  . MET C 3 4   ? 26.463  -14.063 33.590  1.00 72.00  ? 4   MET L CE  1 
ATOM   3722 N  N   . THR C 3 5   ? 30.625  -12.776 30.143  1.00 75.60  ? 5   THR L N   1 
ATOM   3723 C  CA  . THR C 3 5   ? 31.792  -12.410 29.356  1.00 76.51  ? 5   THR L CA  1 
ATOM   3724 C  C   . THR C 3 5   ? 32.843  -13.512 29.467  1.00 76.30  ? 5   THR L C   1 
ATOM   3725 O  O   . THR C 3 5   ? 33.435  -13.699 30.528  1.00 76.18  ? 5   THR L O   1 
ATOM   3726 C  CB  . THR C 3 5   ? 32.360  -11.057 29.803  1.00 77.80  ? 5   THR L CB  1 
ATOM   3727 O  OG1 . THR C 3 5   ? 31.290  -10.111 29.814  1.00 78.15  ? 5   THR L OG1 1 
ATOM   3728 C  CG2 . THR C 3 5   ? 33.475  -10.562 28.908  1.00 78.93  ? 5   THR L CG2 1 
ATOM   3729 N  N   . GLN C 3 6   ? 33.064  -14.229 28.357  1.00 76.12  ? 6   GLN L N   1 
ATOM   3730 C  CA  . GLN C 3 6   ? 34.023  -15.321 28.308  1.00 76.39  ? 6   GLN L CA  1 
ATOM   3731 C  C   . GLN C 3 6   ? 35.354  -14.812 27.762  1.00 77.53  ? 6   GLN L C   1 
ATOM   3732 O  O   . GLN C 3 6   ? 35.407  -13.771 27.111  1.00 77.74  ? 6   GLN L O   1 
ATOM   3733 C  CB  . GLN C 3 6   ? 33.499  -16.459 27.429  1.00 75.25  ? 6   GLN L CB  1 
ATOM   3734 C  CG  . GLN C 3 6   ? 32.150  -17.005 27.870  1.00 73.64  ? 6   GLN L CG  1 
ATOM   3735 C  CD  . GLN C 3 6   ? 31.682  -18.128 26.978  1.00 72.80  ? 6   GLN L CD  1 
ATOM   3736 O  OE1 . GLN C 3 6   ? 30.696  -18.002 26.256  1.00 71.35  ? 6   GLN L OE1 1 
ATOM   3737 N  NE2 . GLN C 3 6   ? 32.403  -19.237 27.010  1.00 73.72  ? 6   GLN L NE2 1 
ATOM   3738 N  N   . SER C 3 7   ? 36.422  -15.572 28.030  1.00 78.96  ? 7   SER L N   1 
ATOM   3739 C  CA  . SER C 3 7   ? 37.754  -15.236 27.553  1.00 80.74  ? 7   SER L CA  1 
ATOM   3740 C  C   . SER C 3 7   ? 38.650  -16.475 27.577  1.00 81.41  ? 7   SER L C   1 
ATOM   3741 O  O   . SER C 3 7   ? 38.487  -17.338 28.437  1.00 81.45  ? 7   SER L O   1 
ATOM   3742 C  CB  . SER C 3 7   ? 38.345  -14.111 28.366  1.00 81.57  ? 7   SER L CB  1 
ATOM   3743 O  OG  . SER C 3 7   ? 38.309  -14.412 29.753  1.00 81.54  ? 7   SER L OG  1 
ATOM   3744 N  N   . PRO C 3 8   ? 39.620  -16.618 26.641  1.00 81.96  ? 8   PRO L N   1 
ATOM   3745 C  CA  . PRO C 3 8   ? 39.799  -15.689 25.525  1.00 81.66  ? 8   PRO L CA  1 
ATOM   3746 C  C   . PRO C 3 8   ? 38.758  -15.894 24.426  1.00 79.34  ? 8   PRO L C   1 
ATOM   3747 O  O   . PRO C 3 8   ? 37.923  -16.793 24.514  1.00 77.60  ? 8   PRO L O   1 
ATOM   3748 C  CB  . PRO C 3 8   ? 41.208  -16.000 24.986  1.00 84.10  ? 8   PRO L CB  1 
ATOM   3749 C  CG  . PRO C 3 8   ? 41.816  -16.973 25.985  1.00 85.10  ? 8   PRO L CG  1 
ATOM   3750 C  CD  . PRO C 3 8   ? 40.642  -17.673 26.636  1.00 83.40  ? 8   PRO L CD  1 
ATOM   3751 N  N   . ALA C 3 9   ? 38.820  -15.040 23.397  1.00 78.95  ? 9   ALA L N   1 
ATOM   3752 C  CA  . ALA C 3 9   ? 37.903  -15.107 22.271  1.00 77.84  ? 9   ALA L CA  1 
ATOM   3753 C  C   . ALA C 3 9   ? 38.097  -16.426 21.527  1.00 77.75  ? 9   ALA L C   1 
ATOM   3754 O  O   . ALA C 3 9   ? 37.142  -17.174 21.332  1.00 75.71  ? 9   ALA L O   1 
ATOM   3755 C  CB  . ALA C 3 9   ? 38.116  -13.920 21.364  1.00 79.00  ? 9   ALA L CB  1 
ATOM   3756 N  N   . THR C 3 10  ? 39.344  -16.686 21.113  1.00 79.97  ? 10  THR L N   1 
ATOM   3757 C  CA  . THR C 3 10  ? 39.732  -17.954 20.512  1.00 80.69  ? 10  THR L CA  1 
ATOM   3758 C  C   . THR C 3 10  ? 40.889  -18.547 21.311  1.00 81.97  ? 10  THR L C   1 
ATOM   3759 O  O   . THR C 3 10  ? 41.578  -17.832 22.036  1.00 83.10  ? 10  THR L O   1 
ATOM   3760 C  CB  . THR C 3 10  ? 40.106  -17.791 19.033  1.00 81.83  ? 10  THR L CB  1 
ATOM   3761 O  OG1 . THR C 3 10  ? 41.067  -16.740 18.935  1.00 84.14  ? 10  THR L OG1 1 
ATOM   3762 C  CG2 . THR C 3 10  ? 38.921  -17.477 18.146  1.00 80.93  ? 10  THR L CG2 1 
ATOM   3763 N  N   . LEU C 3 11  ? 41.091  -19.862 21.163  1.00 82.33  ? 11  LEU L N   1 
ATOM   3764 C  CA  . LEU C 3 11  ? 42.111  -20.584 21.906  1.00 83.39  ? 11  LEU L CA  1 
ATOM   3765 C  C   . LEU C 3 11  ? 42.678  -21.682 21.009  1.00 84.38  ? 11  LEU L C   1 
ATOM   3766 O  O   . LEU C 3 11  ? 41.923  -22.439 20.404  1.00 83.36  ? 11  LEU L O   1 
ATOM   3767 C  CB  . LEU C 3 11  ? 41.474  -21.153 23.180  1.00 82.47  ? 11  LEU L CB  1 
ATOM   3768 C  CG  . LEU C 3 11  ? 42.420  -21.392 24.358  1.00 84.17  ? 11  LEU L CG  1 
ATOM   3769 C  CD1 . LEU C 3 11  ? 41.640  -21.805 25.596  1.00 83.08  ? 11  LEU L CD1 1 
ATOM   3770 C  CD2 . LEU C 3 11  ? 43.471  -22.440 24.025  1.00 86.80  ? 11  LEU L CD2 1 
ATOM   3771 N  N   . SER C 3 12  ? 44.012  -21.747 20.924  1.00 87.00  ? 12  SER L N   1 
ATOM   3772 C  CA  . SER C 3 12  ? 44.693  -22.661 20.021  1.00 88.97  ? 12  SER L CA  1 
ATOM   3773 C  C   . SER C 3 12  ? 45.637  -23.563 20.814  1.00 90.99  ? 12  SER L C   1 
ATOM   3774 O  O   . SER C 3 12  ? 46.640  -23.092 21.349  1.00 92.87  ? 12  SER L O   1 
ATOM   3775 C  CB  . SER C 3 12  ? 45.423  -21.892 18.951  1.00 90.72  ? 12  SER L CB  1 
ATOM   3776 O  OG  . SER C 3 12  ? 45.863  -22.755 17.916  1.00 93.45  ? 12  SER L OG  1 
ATOM   3777 N  N   . VAL C 3 13  ? 45.302  -24.860 20.881  1.00 90.50  ? 13  VAL L N   1 
ATOM   3778 C  CA  . VAL C 3 13  ? 46.039  -25.820 21.690  1.00 91.89  ? 13  VAL L CA  1 
ATOM   3779 C  C   . VAL C 3 13  ? 46.215  -27.119 20.904  1.00 92.67  ? 13  VAL L C   1 
ATOM   3780 O  O   . VAL C 3 13  ? 45.432  -27.416 20.004  1.00 90.60  ? 13  VAL L O   1 
ATOM   3781 C  CB  . VAL C 3 13  ? 45.335  -26.077 23.038  1.00 90.19  ? 13  VAL L CB  1 
ATOM   3782 C  CG1 . VAL C 3 13  ? 45.655  -24.998 24.064  1.00 90.01  ? 13  VAL L CG1 1 
ATOM   3783 C  CG2 . VAL C 3 13  ? 43.830  -26.235 22.872  1.00 86.73  ? 13  VAL L CG2 1 
ATOM   3784 N  N   . SER C 3 14  ? 47.253  -27.883 21.267  1.00 95.22  ? 14  SER L N   1 
ATOM   3785 C  CA  . SER C 3 14  ? 47.527  -29.179 20.666  1.00 97.16  ? 14  SER L CA  1 
ATOM   3786 C  C   . SER C 3 14  ? 46.831  -30.277 21.467  1.00 96.62  ? 14  SER L C   1 
ATOM   3787 O  O   . SER C 3 14  ? 46.612  -30.116 22.666  1.00 96.36  ? 14  SER L O   1 
ATOM   3788 C  CB  . SER C 3 14  ? 49.011  -29.430 20.586  1.00 100.77 ? 14  SER L CB  1 
ATOM   3789 O  OG  . SER C 3 14  ? 49.660  -28.407 19.848  1.00 101.71 ? 14  SER L OG  1 
ATOM   3790 N  N   . PRO C 3 15  ? 46.458  -31.420 20.842  1.00 96.98  ? 15  PRO L N   1 
ATOM   3791 C  CA  . PRO C 3 15  ? 45.892  -32.553 21.579  1.00 96.68  ? 15  PRO L CA  1 
ATOM   3792 C  C   . PRO C 3 15  ? 46.822  -33.053 22.683  1.00 99.75  ? 15  PRO L C   1 
ATOM   3793 O  O   . PRO C 3 15  ? 47.982  -33.363 22.422  1.00 102.86 ? 15  PRO L O   1 
ATOM   3794 C  CB  . PRO C 3 15  ? 45.699  -33.636 20.505  1.00 97.23  ? 15  PRO L CB  1 
ATOM   3795 C  CG  . PRO C 3 15  ? 45.606  -32.865 19.206  1.00 96.34  ? 15  PRO L CG  1 
ATOM   3796 C  CD  . PRO C 3 15  ? 46.525  -31.676 19.394  1.00 97.58  ? 15  PRO L CD  1 
ATOM   3797 N  N   . GLY C 3 16  ? 46.298  -33.113 23.914  1.00 99.36  ? 16  GLY L N   1 
ATOM   3798 C  CA  . GLY C 3 16  ? 47.065  -33.548 25.071  1.00 102.73 ? 16  GLY L CA  1 
ATOM   3799 C  C   . GLY C 3 16  ? 47.294  -32.423 26.079  1.00 103.08 ? 16  GLY L C   1 
ATOM   3800 O  O   . GLY C 3 16  ? 47.629  -32.690 27.231  1.00 104.82 ? 16  GLY L O   1 
ATOM   3801 N  N   . GLU C 3 17  ? 47.121  -31.170 25.632  1.00 102.10 ? 17  GLU L N   1 
ATOM   3802 C  CA  . GLU C 3 17  ? 47.289  -30.001 26.482  1.00 101.79 ? 17  GLU L CA  1 
ATOM   3803 C  C   . GLU C 3 17  ? 45.967  -29.681 27.179  1.00 98.52  ? 17  GLU L C   1 
ATOM   3804 O  O   . GLU C 3 17  ? 44.923  -30.214 26.809  1.00 95.86  ? 17  GLU L O   1 
ATOM   3805 C  CB  . GLU C 3 17  ? 47.771  -28.807 25.655  1.00 101.82 ? 17  GLU L CB  1 
ATOM   3806 C  CG  . GLU C 3 17  ? 49.138  -29.012 25.022  1.00 105.65 ? 17  GLU L CG  1 
ATOM   3807 C  CD  . GLU C 3 17  ? 49.639  -27.849 24.180  1.00 105.94 ? 17  GLU L CD  1 
ATOM   3808 O  OE1 . GLU C 3 17  ? 48.924  -26.829 24.088  1.00 102.82 ? 17  GLU L OE1 1 
ATOM   3809 O  OE2 . GLU C 3 17  ? 50.744  -27.965 23.614  1.00 108.96 ? 17  GLU L OE2 1 
ATOM   3810 N  N   . ARG C 3 18  ? 46.032  -28.789 28.177  1.00 98.97  ? 18  ARG L N   1 
ATOM   3811 C  CA  . ARG C 3 18  ? 44.893  -28.449 29.016  1.00 96.72  ? 18  ARG L CA  1 
ATOM   3812 C  C   . ARG C 3 18  ? 44.342  -27.082 28.615  1.00 94.51  ? 18  ARG L C   1 
ATOM   3813 O  O   . ARG C 3 18  ? 44.962  -26.056 28.890  1.00 95.53  ? 18  ARG L O   1 
ATOM   3814 C  CB  . ARG C 3 18  ? 45.316  -28.445 30.489  1.00 98.69  ? 18  ARG L CB  1 
ATOM   3815 C  CG  . ARG C 3 18  ? 44.173  -28.272 31.479  1.00 96.79  ? 18  ARG L CG  1 
ATOM   3816 C  CD  . ARG C 3 18  ? 44.666  -28.114 32.907  1.00 99.11  ? 18  ARG L CD  1 
ATOM   3817 N  NE  . ARG C 3 18  ? 45.649  -29.122 33.289  1.00 103.47 ? 18  ARG L NE  1 
ATOM   3818 C  CZ  . ARG C 3 18  ? 45.403  -30.424 33.397  1.00 105.02 ? 18  ARG L CZ  1 
ATOM   3819 N  NH1 . ARG C 3 18  ? 44.179  -30.889 33.215  1.00 103.08 ? 18  ARG L NH1 1 
ATOM   3820 N  NH2 . ARG C 3 18  ? 46.383  -31.258 33.701  1.00 108.29 ? 18  ARG L NH2 1 
ATOM   3821 N  N   . ALA C 3 19  ? 43.165  -27.080 27.975  1.00 92.29  ? 19  ALA L N   1 
ATOM   3822 C  CA  . ALA C 3 19  ? 42.482  -25.849 27.607  1.00 89.75  ? 19  ALA L CA  1 
ATOM   3823 C  C   . ALA C 3 19  ? 41.728  -25.302 28.818  1.00 87.64  ? 19  ALA L C   1 
ATOM   3824 O  O   . ALA C 3 19  ? 40.996  -26.039 29.475  1.00 86.36  ? 19  ALA L O   1 
ATOM   3825 C  CB  . ALA C 3 19  ? 41.549  -26.107 26.448  1.00 88.35  ? 19  ALA L CB  1 
ATOM   3826 N  N   . THR C 3 20  ? 41.911  -24.003 29.092  1.00 86.81  ? 20  THR L N   1 
ATOM   3827 C  CA  . THR C 3 20  ? 41.312  -23.349 30.246  1.00 85.71  ? 20  THR L CA  1 
ATOM   3828 C  C   . THR C 3 20  ? 40.447  -22.180 29.777  1.00 83.77  ? 20  THR L C   1 
ATOM   3829 O  O   . THR C 3 20  ? 40.968  -21.121 29.430  1.00 83.15  ? 20  THR L O   1 
ATOM   3830 C  CB  . THR C 3 20  ? 42.396  -22.896 31.235  1.00 87.02  ? 20  THR L CB  1 
ATOM   3831 O  OG1 . THR C 3 20  ? 43.105  -24.057 31.666  1.00 88.93  ? 20  THR L OG1 1 
ATOM   3832 C  CG2 . THR C 3 20  ? 41.841  -22.165 32.438  1.00 85.96  ? 20  THR L CG2 1 
ATOM   3833 N  N   . LEU C 3 21  ? 39.123  -22.388 29.776  1.00 82.45  ? 21  LEU L N   1 
ATOM   3834 C  CA  . LEU C 3 21  ? 38.169  -21.376 29.349  1.00 81.50  ? 21  LEU L CA  1 
ATOM   3835 C  C   . LEU C 3 21  ? 37.636  -20.632 30.572  1.00 81.55  ? 21  LEU L C   1 
ATOM   3836 O  O   . LEU C 3 21  ? 37.326  -21.251 31.588  1.00 81.25  ? 21  LEU L O   1 
ATOM   3837 C  CB  . LEU C 3 21  ? 37.026  -22.050 28.580  1.00 79.85  ? 21  LEU L CB  1 
ATOM   3838 C  CG  . LEU C 3 21  ? 37.437  -23.020 27.471  1.00 80.02  ? 21  LEU L CG  1 
ATOM   3839 C  CD1 . LEU C 3 21  ? 36.251  -23.348 26.577  1.00 78.47  ? 21  LEU L CD1 1 
ATOM   3840 C  CD2 . LEU C 3 21  ? 38.586  -22.466 26.643  1.00 81.22  ? 21  LEU L CD2 1 
ATOM   3841 N  N   . SER C 3 22  ? 37.524  -19.302 30.452  1.00 81.43  ? 22  SER L N   1 
ATOM   3842 C  CA  . SER C 3 22  ? 37.068  -18.449 31.537  1.00 80.60  ? 22  SER L CA  1 
ATOM   3843 C  C   . SER C 3 22  ? 35.664  -17.929 31.239  1.00 79.69  ? 22  SER L C   1 
ATOM   3844 O  O   . SER C 3 22  ? 35.251  -17.869 30.082  1.00 79.10  ? 22  SER L O   1 
ATOM   3845 C  CB  . SER C 3 22  ? 38.027  -17.309 31.770  1.00 81.19  ? 22  SER L CB  1 
ATOM   3846 O  OG  . SER C 3 22  ? 39.328  -17.792 32.066  1.00 82.81  ? 22  SER L OG  1 
ATOM   3847 N  N   . CYS C 3 23  ? 34.950  -17.556 32.308  1.00 80.18  ? 23  CYS L N   1 
ATOM   3848 C  CA  . CYS C 3 23  ? 33.607  -17.009 32.217  1.00 79.54  ? 23  CYS L CA  1 
ATOM   3849 C  C   . CYS C 3 23  ? 33.385  -16.034 33.371  1.00 80.49  ? 23  CYS L C   1 
ATOM   3850 O  O   . CYS C 3 23  ? 33.531  -16.409 34.532  1.00 81.12  ? 23  CYS L O   1 
ATOM   3851 C  CB  . CYS C 3 23  ? 32.562  -18.119 32.254  1.00 79.04  ? 23  CYS L CB  1 
ATOM   3852 S  SG  . CYS C 3 23  ? 30.865  -17.518 32.460  1.00 77.83  ? 23  CYS L SG  1 
ATOM   3853 N  N   . ARG C 3 24  ? 33.040  -14.784 33.034  1.00 81.22  ? 24  ARG L N   1 
ATOM   3854 C  CA  . ARG C 3 24  ? 32.814  -13.744 34.024  1.00 81.86  ? 24  ARG L CA  1 
ATOM   3855 C  C   . ARG C 3 24  ? 31.363  -13.279 33.947  1.00 80.17  ? 24  ARG L C   1 
ATOM   3856 O  O   . ARG C 3 24  ? 30.879  -12.930 32.872  1.00 78.54  ? 24  ARG L O   1 
ATOM   3857 C  CB  . ARG C 3 24  ? 33.749  -12.553 33.788  1.00 83.95  ? 24  ARG L CB  1 
ATOM   3858 C  CG  . ARG C 3 24  ? 33.784  -11.554 34.937  1.00 85.57  ? 24  ARG L CG  1 
ATOM   3859 C  CD  . ARG C 3 24  ? 34.274  -10.183 34.510  1.00 87.60  ? 24  ARG L CD  1 
ATOM   3860 N  NE  . ARG C 3 24  ? 35.537  -10.237 33.783  1.00 89.76  ? 24  ARG L NE  1 
ATOM   3861 C  CZ  . ARG C 3 24  ? 36.693  -9.744  34.220  1.00 92.71  ? 24  ARG L CZ  1 
ATOM   3862 N  NH1 . ARG C 3 24  ? 36.770  -9.173  35.411  1.00 93.77  ? 24  ARG L NH1 1 
ATOM   3863 N  NH2 . ARG C 3 24  ? 37.774  -9.829  33.462  1.00 94.34  ? 24  ARG L NH2 1 
ATOM   3864 N  N   . ALA C 3 25  ? 30.690  -13.271 35.103  1.00 80.40  ? 25  ALA L N   1 
ATOM   3865 C  CA  . ALA C 3 25  ? 29.346  -12.729 35.220  1.00 80.23  ? 25  ALA L CA  1 
ATOM   3866 C  C   . ALA C 3 25  ? 29.424  -11.298 35.745  1.00 81.11  ? 25  ALA L C   1 
ATOM   3867 O  O   . ALA C 3 25  ? 30.195  -11.016 36.660  1.00 83.01  ? 25  ALA L O   1 
ATOM   3868 C  CB  . ALA C 3 25  ? 28.521  -13.605 36.129  1.00 80.25  ? 25  ALA L CB  1 
ATOM   3869 N  N   . SER C 3 26  ? 28.616  -10.405 35.159  1.00 80.98  ? 26  SER L N   1 
ATOM   3870 C  CA  . SER C 3 26  ? 28.595  -9.003  35.550  1.00 81.82  ? 26  SER L CA  1 
ATOM   3871 C  C   . SER C 3 26  ? 28.186  -8.870  37.017  1.00 82.50  ? 26  SER L C   1 
ATOM   3872 O  O   . SER C 3 26  ? 28.707  -8.017  37.733  1.00 82.11  ? 26  SER L O   1 
ATOM   3873 C  CB  . SER C 3 26  ? 27.689  -8.202  34.647  1.00 81.73  ? 26  SER L CB  1 
ATOM   3874 O  OG  . SER C 3 26  ? 26.350  -8.670  34.720  1.00 81.29  ? 26  SER L OG  1 
ATOM   3875 N  N   . GLN C 3 27  ? 27.251  -9.728  37.444  1.00 86.46  ? 27  GLN L N   1 
ATOM   3876 C  CA  . GLN C 3 27  ? 26.821  -9.814  38.830  1.00 88.56  ? 27  GLN L CA  1 
ATOM   3877 C  C   . GLN C 3 27  ? 26.882  -11.275 39.268  1.00 85.96  ? 27  GLN L C   1 
ATOM   3878 O  O   . GLN C 3 27  ? 26.900  -12.173 38.430  1.00 82.93  ? 27  GLN L O   1 
ATOM   3879 C  CB  . GLN C 3 27  ? 25.406  -9.255  38.986  1.00 90.10  ? 27  GLN L CB  1 
ATOM   3880 C  CG  . GLN C 3 27  ? 25.307  -7.761  38.710  1.00 93.42  ? 27  GLN L CG  1 
ATOM   3881 C  CD  . GLN C 3 27  ? 23.877  -7.277  38.687  1.00 94.72  ? 27  GLN L CD  1 
ATOM   3882 O  OE1 . GLN C 3 27  ? 23.456  -6.487  39.531  1.00 98.44  ? 27  GLN L OE1 1 
ATOM   3883 N  NE2 . GLN C 3 27  ? 23.115  -7.753  37.712  1.00 93.18  ? 27  GLN L NE2 1 
ATOM   3884 N  N   . SER C 3 28  ? 26.912  -11.496 40.588  1.00 86.62  ? 28  SER L N   1 
ATOM   3885 C  CA  . SER C 3 28  ? 27.012  -12.835 41.148  1.00 84.90  ? 28  SER L CA  1 
ATOM   3886 C  C   . SER C 3 28  ? 25.823  -13.681 40.698  1.00 81.93  ? 28  SER L C   1 
ATOM   3887 O  O   . SER C 3 28  ? 24.687  -13.212 40.708  1.00 82.08  ? 28  SER L O   1 
ATOM   3888 C  CB  . SER C 3 28  ? 27.111  -12.784 42.651  1.00 86.94  ? 28  SER L CB  1 
ATOM   3889 O  OG  . SER C 3 28  ? 27.273  -14.087 43.193  1.00 85.99  ? 28  SER L OG  1 
ATOM   3890 N  N   . VAL C 3 29  ? 26.105  -14.928 40.300  1.00 80.32  ? 29  VAL L N   1 
ATOM   3891 C  CA  . VAL C 3 29  ? 25.080  -15.855 39.844  1.00 78.46  ? 29  VAL L CA  1 
ATOM   3892 C  C   . VAL C 3 29  ? 25.153  -17.134 40.679  1.00 78.96  ? 29  VAL L C   1 
ATOM   3893 O  O   . VAL C 3 29  ? 24.753  -18.199 40.211  1.00 77.83  ? 29  VAL L O   1 
ATOM   3894 C  CB  . VAL C 3 29  ? 25.220  -16.148 38.334  1.00 76.18  ? 29  VAL L CB  1 
ATOM   3895 C  CG1 . VAL C 3 29  ? 25.182  -14.869 37.511  1.00 76.50  ? 29  VAL L CG1 1 
ATOM   3896 C  CG2 . VAL C 3 29  ? 26.472  -16.953 38.008  1.00 75.34  ? 29  VAL L CG2 1 
ATOM   3897 N  N   . SER C 3 30  ? 25.643  -17.006 41.922  1.00 80.98  ? 30  SER L N   1 
ATOM   3898 C  CA  A SER C 3 30  ? 25.805  -18.135 42.824  0.55 81.64  ? 30  SER L CA  1 
ATOM   3899 C  CA  B SER C 3 30  ? 25.802  -18.137 42.822  0.45 81.73  ? 30  SER L CA  1 
ATOM   3900 C  C   . SER C 3 30  ? 26.569  -19.251 42.109  1.00 80.53  ? 30  SER L C   1 
ATOM   3901 O  O   . SER C 3 30  ? 27.650  -19.005 41.574  1.00 80.92  ? 30  SER L O   1 
ATOM   3902 C  CB  A SER C 3 30  ? 24.464  -18.579 43.364  0.55 81.58  ? 30  SER L CB  1 
ATOM   3903 C  CB  B SER C 3 30  ? 24.461  -18.593 43.351  0.45 81.74  ? 30  SER L CB  1 
ATOM   3904 O  OG  A SER C 3 30  ? 23.787  -17.496 43.985  0.55 82.81  ? 30  SER L OG  1 
ATOM   3905 O  OG  B SER C 3 30  ? 24.610  -19.688 44.244  0.45 82.96  ? 30  SER L OG  1 
ATOM   3906 N  N   . SER C 3 31  ? 26.015  -20.476 42.105  1.00 79.47  ? 31  SER L N   1 
ATOM   3907 C  CA  A SER C 3 31  ? 26.589  -21.587 41.362  0.38 77.87  ? 31  SER L CA  1 
ATOM   3908 C  CA  B SER C 3 31  ? 26.586  -21.590 41.366  0.62 78.16  ? 31  SER L CA  1 
ATOM   3909 C  C   . SER C 3 31  ? 25.610  -22.050 40.284  1.00 75.32  ? 31  SER L C   1 
ATOM   3910 O  O   . SER C 3 31  ? 25.663  -23.195 39.840  1.00 74.44  ? 31  SER L O   1 
ATOM   3911 C  CB  A SER C 3 31  ? 26.970  -22.713 42.290  0.38 79.62  ? 31  SER L CB  1 
ATOM   3912 C  CB  B SER C 3 31  ? 26.955  -22.718 42.301  0.62 80.24  ? 31  SER L CB  1 
ATOM   3913 O  OG  A SER C 3 31  ? 27.983  -22.300 43.196  0.38 81.74  ? 31  SER L OG  1 
ATOM   3914 O  OG  B SER C 3 31  ? 25.815  -23.191 43.004  0.62 81.45  ? 31  SER L OG  1 
ATOM   3915 N  N   . ASN C 3 32  ? 24.721  -21.139 39.859  1.00 73.52  ? 32  ASN L N   1 
ATOM   3916 C  CA  . ASN C 3 32  ? 23.744  -21.424 38.821  1.00 71.65  ? 32  ASN L CA  1 
ATOM   3917 C  C   . ASN C 3 32  ? 24.351  -21.077 37.464  1.00 71.04  ? 32  ASN L C   1 
ATOM   3918 O  O   . ASN C 3 32  ? 23.991  -20.069 36.856  1.00 70.13  ? 32  ASN L O   1 
ATOM   3919 C  CB  . ASN C 3 32  ? 22.434  -20.669 39.061  1.00 70.93  ? 32  ASN L CB  1 
ATOM   3920 C  CG  . ASN C 3 32  ? 21.695  -21.132 40.299  1.00 72.00  ? 32  ASN L CG  1 
ATOM   3921 O  OD1 . ASN C 3 32  ? 21.351  -20.326 41.159  1.00 73.88  ? 32  ASN L OD1 1 
ATOM   3922 N  ND2 . ASN C 3 32  ? 21.434  -22.425 40.393  1.00 71.48  ? 32  ASN L ND2 1 
ATOM   3923 N  N   . LEU C 3 33  ? 25.270  -21.934 37.004  1.00 71.71  ? 33  LEU L N   1 
ATOM   3924 C  CA  . LEU C 3 33  ? 26.057  -21.689 35.806  1.00 70.75  ? 33  LEU L CA  1 
ATOM   3925 C  C   . LEU C 3 33  ? 26.231  -23.011 35.060  1.00 70.29  ? 33  LEU L C   1 
ATOM   3926 O  O   . LEU C 3 33  ? 26.661  -24.002 35.648  1.00 71.55  ? 33  LEU L O   1 
ATOM   3927 C  CB  . LEU C 3 33  ? 27.401  -21.082 36.232  1.00 72.16  ? 33  LEU L CB  1 
ATOM   3928 C  CG  . LEU C 3 33  ? 28.282  -20.475 35.135  1.00 71.53  ? 33  LEU L CG  1 
ATOM   3929 C  CD1 . LEU C 3 33  ? 28.815  -21.536 34.181  1.00 70.53  ? 33  LEU L CD1 1 
ATOM   3930 C  CD2 . LEU C 3 33  ? 27.541  -19.388 34.370  1.00 71.30  ? 33  LEU L CD2 1 
ATOM   3931 N  N   . ALA C 3 34  ? 25.879  -23.010 33.766  1.00 68.32  ? 34  ALA L N   1 
ATOM   3932 C  CA  . ALA C 3 34  ? 25.992  -24.187 32.918  1.00 66.89  ? 34  ALA L CA  1 
ATOM   3933 C  C   . ALA C 3 34  ? 27.026  -23.937 31.821  1.00 65.61  ? 34  ALA L C   1 
ATOM   3934 O  O   . ALA C 3 34  ? 27.250  -22.796 31.426  1.00 64.27  ? 34  ALA L O   1 
ATOM   3935 C  CB  . ALA C 3 34  ? 24.640  -24.524 32.335  1.00 65.46  ? 34  ALA L CB  1 
ATOM   3936 N  N   . TRP C 3 35  ? 27.648  -25.023 31.343  1.00 65.69  ? 35  TRP L N   1 
ATOM   3937 C  CA  . TRP C 3 35  ? 28.592  -24.975 30.236  1.00 65.11  ? 35  TRP L CA  1 
ATOM   3938 C  C   . TRP C 3 35  ? 28.047  -25.793 29.067  1.00 63.93  ? 35  TRP L C   1 
ATOM   3939 O  O   . TRP C 3 35  ? 27.413  -26.825 29.277  1.00 64.00  ? 35  TRP L O   1 
ATOM   3940 C  CB  . TRP C 3 35  ? 29.968  -25.486 30.678  1.00 66.05  ? 35  TRP L CB  1 
ATOM   3941 C  CG  . TRP C 3 35  ? 30.766  -24.512 31.490  1.00 67.09  ? 35  TRP L CG  1 
ATOM   3942 C  CD1 . TRP C 3 35  ? 30.886  -24.476 32.849  1.00 68.29  ? 35  TRP L CD1 1 
ATOM   3943 C  CD2 . TRP C 3 35  ? 31.608  -23.458 30.987  1.00 67.25  ? 35  TRP L CD2 1 
ATOM   3944 N  NE1 . TRP C 3 35  ? 31.722  -23.460 33.227  1.00 69.01  ? 35  TRP L NE1 1 
ATOM   3945 C  CE2 . TRP C 3 35  ? 32.183  -22.819 32.108  1.00 68.63  ? 35  TRP L CE2 1 
ATOM   3946 C  CE3 . TRP C 3 35  ? 31.927  -22.989 29.707  1.00 66.68  ? 35  TRP L CE3 1 
ATOM   3947 C  CZ2 . TRP C 3 35  ? 33.056  -21.738 31.982  1.00 68.90  ? 35  TRP L CZ2 1 
ATOM   3948 C  CZ3 . TRP C 3 35  ? 32.788  -21.919 29.584  1.00 67.35  ? 35  TRP L CZ3 1 
ATOM   3949 C  CH2 . TRP C 3 35  ? 33.344  -21.305 30.708  1.00 68.26  ? 35  TRP L CH2 1 
ATOM   3950 N  N   . TYR C 3 36  ? 28.306  -25.318 27.842  1.00 63.44  ? 36  TYR L N   1 
ATOM   3951 C  CA  . TYR C 3 36  ? 27.833  -25.975 26.633  1.00 64.11  ? 36  TYR L CA  1 
ATOM   3952 C  C   . TYR C 3 36  ? 28.986  -26.153 25.647  1.00 65.12  ? 36  TYR L C   1 
ATOM   3953 O  O   . TYR C 3 36  ? 30.009  -25.479 25.748  1.00 66.02  ? 36  TYR L O   1 
ATOM   3954 C  CB  . TYR C 3 36  ? 26.695  -25.178 25.988  1.00 63.60  ? 36  TYR L CB  1 
ATOM   3955 C  CG  . TYR C 3 36  ? 25.413  -25.142 26.781  1.00 63.86  ? 36  TYR L CG  1 
ATOM   3956 C  CD1 . TYR C 3 36  ? 25.283  -24.335 27.900  1.00 64.51  ? 36  TYR L CD1 1 
ATOM   3957 C  CD2 . TYR C 3 36  ? 24.328  -25.926 26.422  1.00 64.33  ? 36  TYR L CD2 1 
ATOM   3958 C  CE1 . TYR C 3 36  ? 24.108  -24.298 28.634  1.00 64.61  ? 36  TYR L CE1 1 
ATOM   3959 C  CE2 . TYR C 3 36  ? 23.147  -25.904 27.146  1.00 64.44  ? 36  TYR L CE2 1 
ATOM   3960 C  CZ  . TYR C 3 36  ? 23.035  -25.086 28.256  1.00 64.83  ? 36  TYR L CZ  1 
ATOM   3961 O  OH  . TYR C 3 36  ? 21.868  -25.058 28.983  1.00 65.34  ? 36  TYR L OH  1 
ATOM   3962 N  N   . GLN C 3 37  ? 28.793  -27.078 24.697  1.00 65.65  ? 37  GLN L N   1 
ATOM   3963 C  CA  . GLN C 3 37  ? 29.729  -27.323 23.610  1.00 65.70  ? 37  GLN L CA  1 
ATOM   3964 C  C   . GLN C 3 37  ? 28.951  -27.382 22.297  1.00 65.37  ? 37  GLN L C   1 
ATOM   3965 O  O   . GLN C 3 37  ? 28.129  -28.276 22.109  1.00 65.76  ? 37  GLN L O   1 
ATOM   3966 C  CB  . GLN C 3 37  ? 30.473  -28.642 23.830  1.00 66.95  ? 37  GLN L CB  1 
ATOM   3967 C  CG  . GLN C 3 37  ? 31.448  -28.994 22.712  1.00 68.73  ? 37  GLN L CG  1 
ATOM   3968 C  CD  . GLN C 3 37  ? 31.856  -30.447 22.722  1.00 69.88  ? 37  GLN L CD  1 
ATOM   3969 O  OE1 . GLN C 3 37  ? 33.018  -30.785 22.937  1.00 71.79  ? 37  GLN L OE1 1 
ATOM   3970 N  NE2 . GLN C 3 37  ? 30.897  -31.324 22.477  1.00 69.32  ? 37  GLN L NE2 1 
ATOM   3971 N  N   . GLN C 3 38  ? 29.223  -26.433 21.393  1.00 65.13  ? 38  GLN L N   1 
ATOM   3972 C  CA  . GLN C 3 38  ? 28.574  -26.418 20.091  1.00 65.78  ? 38  GLN L CA  1 
ATOM   3973 C  C   . GLN C 3 38  ? 29.596  -26.751 19.006  1.00 67.48  ? 38  GLN L C   1 
ATOM   3974 O  O   . GLN C 3 38  ? 30.489  -25.958 18.714  1.00 67.47  ? 38  GLN L O   1 
ATOM   3975 C  CB  . GLN C 3 38  ? 27.909  -25.067 19.823  1.00 64.86  ? 38  GLN L CB  1 
ATOM   3976 C  CG  . GLN C 3 38  ? 26.937  -25.109 18.652  1.00 65.23  ? 38  GLN L CG  1 
ATOM   3977 C  CD  . GLN C 3 38  ? 26.124  -23.846 18.514  1.00 65.31  ? 38  GLN L CD  1 
ATOM   3978 O  OE1 . GLN C 3 38  ? 26.453  -22.804 19.075  1.00 64.47  ? 38  GLN L OE1 1 
ATOM   3979 N  NE2 . GLN C 3 38  ? 25.051  -23.931 17.746  1.00 66.40  ? 38  GLN L NE2 1 
ATOM   3980 N  N   . LYS C 3 39  ? 29.446  -27.943 18.418  1.00 68.69  ? 39  LYS L N   1 
ATOM   3981 C  CA  . LYS C 3 39  ? 30.238  -28.346 17.269  1.00 69.95  ? 39  LYS L CA  1 
ATOM   3982 C  C   . LYS C 3 39  ? 29.561  -27.821 16.005  1.00 69.90  ? 39  LYS L C   1 
ATOM   3983 O  O   . LYS C 3 39  ? 28.366  -27.538 16.017  1.00 69.03  ? 39  LYS L O   1 
ATOM   3984 C  CB  . LYS C 3 39  ? 30.392  -29.870 17.241  1.00 71.51  ? 39  LYS L CB  1 
ATOM   3985 C  CG  . LYS C 3 39  ? 31.165  -30.460 18.413  1.00 71.37  ? 39  LYS L CG  1 
ATOM   3986 C  CD  . LYS C 3 39  ? 31.311  -31.963 18.346  1.00 73.11  ? 39  LYS L CD  1 
ATOM   3987 C  CE  . LYS C 3 39  ? 32.076  -32.531 19.521  1.00 73.57  ? 39  LYS L CE  1 
ATOM   3988 N  NZ  . LYS C 3 39  ? 32.326  -33.982 19.361  1.00 76.10  ? 39  LYS L NZ  1 
ATOM   3989 N  N   . PRO C 3 40  ? 30.300  -27.670 14.881  1.00 71.75  ? 40  PRO L N   1 
ATOM   3990 C  CA  . PRO C 3 40  ? 29.737  -27.108 13.651  1.00 73.07  ? 40  PRO L CA  1 
ATOM   3991 C  C   . PRO C 3 40  ? 28.463  -27.803 13.170  1.00 73.43  ? 40  PRO L C   1 
ATOM   3992 O  O   . PRO C 3 40  ? 28.418  -29.026 13.072  1.00 74.11  ? 40  PRO L O   1 
ATOM   3993 C  CB  . PRO C 3 40  ? 30.865  -27.300 12.624  1.00 74.94  ? 40  PRO L CB  1 
ATOM   3994 C  CG  . PRO C 3 40  ? 32.126  -27.314 13.460  1.00 74.64  ? 40  PRO L CG  1 
ATOM   3995 C  CD  . PRO C 3 40  ? 31.726  -28.006 14.745  1.00 72.97  ? 40  PRO L CD  1 
ATOM   3996 N  N   . GLY C 3 41  ? 27.430  -26.999 12.885  1.00 74.03  ? 41  GLY L N   1 
ATOM   3997 C  CA  . GLY C 3 41  ? 26.189  -27.484 12.301  1.00 75.68  ? 41  GLY L CA  1 
ATOM   3998 C  C   . GLY C 3 41  ? 25.356  -28.324 13.269  1.00 75.42  ? 41  GLY L C   1 
ATOM   3999 O  O   . GLY C 3 41  ? 24.547  -29.140 12.832  1.00 77.13  ? 41  GLY L O   1 
ATOM   4000 N  N   . GLN C 3 42  ? 25.545  -28.104 14.577  1.00 73.58  ? 42  GLN L N   1 
ATOM   4001 C  CA  . GLN C 3 42  ? 24.872  -28.889 15.601  1.00 73.00  ? 42  GLN L CA  1 
ATOM   4002 C  C   . GLN C 3 42  ? 24.293  -27.964 16.668  1.00 71.42  ? 42  GLN L C   1 
ATOM   4003 O  O   . GLN C 3 42  ? 24.656  -26.792 16.750  1.00 70.23  ? 42  GLN L O   1 
ATOM   4004 C  CB  . GLN C 3 42  ? 25.842  -29.879 16.250  1.00 72.86  ? 42  GLN L CB  1 
ATOM   4005 C  CG  . GLN C 3 42  ? 26.318  -30.982 15.315  1.00 74.54  ? 42  GLN L CG  1 
ATOM   4006 C  CD  . GLN C 3 42  ? 27.171  -32.009 16.019  1.00 74.78  ? 42  GLN L CD  1 
ATOM   4007 O  OE1 . GLN C 3 42  ? 27.448  -31.912 17.213  1.00 72.90  ? 42  GLN L OE1 1 
ATOM   4008 N  NE2 . GLN C 3 42  ? 27.598  -33.015 15.274  1.00 77.41  ? 42  GLN L NE2 1 
ATOM   4009 N  N   . ALA C 3 43  ? 23.386  -28.518 17.481  1.00 71.38  ? 43  ALA L N   1 
ATOM   4010 C  CA  . ALA C 3 43  ? 22.864  -27.826 18.647  1.00 70.16  ? 43  ALA L CA  1 
ATOM   4011 C  C   . ALA C 3 43  ? 23.891  -27.902 19.774  1.00 69.11  ? 43  ALA L C   1 
ATOM   4012 O  O   . ALA C 3 43  ? 24.754  -28.779 19.767  1.00 69.06  ? 43  ALA L O   1 
ATOM   4013 C  CB  . ALA C 3 43  ? 21.544  -28.432 19.061  1.00 70.27  ? 43  ALA L CB  1 
ATOM   4014 N  N   . PRO C 3 44  ? 23.854  -26.975 20.760  1.00 67.95  ? 44  PRO L N   1 
ATOM   4015 C  CA  . PRO C 3 44  ? 24.722  -27.063 21.937  1.00 67.14  ? 44  PRO L CA  1 
ATOM   4016 C  C   . PRO C 3 44  ? 24.582  -28.374 22.713  1.00 66.51  ? 44  PRO L C   1 
ATOM   4017 O  O   . PRO C 3 44  ? 23.507  -28.970 22.753  1.00 65.78  ? 44  PRO L O   1 
ATOM   4018 C  CB  . PRO C 3 44  ? 24.272  -25.874 22.803  1.00 66.19  ? 44  PRO L CB  1 
ATOM   4019 C  CG  . PRO C 3 44  ? 23.697  -24.890 21.809  1.00 66.17  ? 44  PRO L CG  1 
ATOM   4020 C  CD  . PRO C 3 44  ? 23.028  -25.756 20.763  1.00 67.00  ? 44  PRO L CD  1 
ATOM   4021 N  N   . ARG C 3 45  ? 25.695  -28.802 23.323  1.00 65.80  ? 45  ARG L N   1 
ATOM   4022 C  CA  . ARG C 3 45  ? 25.759  -30.011 24.127  1.00 66.99  ? 45  ARG L CA  1 
ATOM   4023 C  C   . ARG C 3 45  ? 26.109  -29.625 25.562  1.00 66.47  ? 45  ARG L C   1 
ATOM   4024 O  O   . ARG C 3 45  ? 27.158  -29.031 25.800  1.00 65.71  ? 45  ARG L O   1 
ATOM   4025 C  CB  . ARG C 3 45  ? 26.806  -30.961 23.536  1.00 68.74  ? 45  ARG L CB  1 
ATOM   4026 C  CG  . ARG C 3 45  ? 27.053  -32.235 24.333  1.00 70.76  ? 45  ARG L CG  1 
ATOM   4027 C  CD  . ARG C 3 45  ? 28.188  -33.027 23.711  1.00 73.08  ? 45  ARG L CD  1 
ATOM   4028 N  NE  . ARG C 3 45  ? 28.500  -34.274 24.400  1.00 75.67  ? 45  ARG L NE  1 
ATOM   4029 C  CZ  . ARG C 3 45  ? 29.716  -34.638 24.799  1.00 77.42  ? 45  ARG L CZ  1 
ATOM   4030 N  NH1 . ARG C 3 45  ? 30.736  -33.807 24.674  1.00 76.48  ? 45  ARG L NH1 1 
ATOM   4031 N  NH2 . ARG C 3 45  ? 29.910  -35.833 25.333  1.00 79.99  ? 45  ARG L NH2 1 
ATOM   4032 N  N   . LEU C 3 46  ? 25.227  -29.974 26.508  1.00 66.41  ? 46  LEU L N   1 
ATOM   4033 C  CA  . LEU C 3 46  ? 25.413  -29.630 27.910  1.00 65.90  ? 46  LEU L CA  1 
ATOM   4034 C  C   . LEU C 3 46  ? 26.565  -30.446 28.491  1.00 66.63  ? 46  LEU L C   1 
ATOM   4035 O  O   . LEU C 3 46  ? 26.493  -31.672 28.544  1.00 68.33  ? 46  LEU L O   1 
ATOM   4036 C  CB  . LEU C 3 46  ? 24.113  -29.902 28.674  1.00 66.47  ? 46  LEU L CB  1 
ATOM   4037 C  CG  . LEU C 3 46  ? 24.153  -29.623 30.177  1.00 66.28  ? 46  LEU L CG  1 
ATOM   4038 C  CD1 . LEU C 3 46  ? 24.138  -28.127 30.454  1.00 64.96  ? 46  LEU L CD1 1 
ATOM   4039 C  CD2 . LEU C 3 46  ? 22.992  -30.304 30.883  1.00 67.57  ? 46  LEU L CD2 1 
ATOM   4040 N  N   . LEU C 3 47  ? 27.615  -29.745 28.933  1.00 66.45  ? 47  LEU L N   1 
ATOM   4041 C  CA  . LEU C 3 47  ? 28.754  -30.373 29.580  1.00 68.08  ? 47  LEU L CA  1 
ATOM   4042 C  C   . LEU C 3 47  ? 28.545  -30.355 31.091  1.00 68.35  ? 47  LEU L C   1 
ATOM   4043 O  O   . LEU C 3 47  ? 28.513  -31.407 31.726  1.00 68.82  ? 47  LEU L O   1 
ATOM   4044 C  CB  . LEU C 3 47  ? 30.034  -29.619 29.199  1.00 68.34  ? 47  LEU L CB  1 
ATOM   4045 C  CG  . LEU C 3 47  ? 30.399  -29.611 27.714  1.00 67.85  ? 47  LEU L CG  1 
ATOM   4046 C  CD1 . LEU C 3 47  ? 31.746  -28.936 27.503  1.00 68.49  ? 47  LEU L CD1 1 
ATOM   4047 C  CD2 . LEU C 3 47  ? 30.413  -31.021 27.140  1.00 69.07  ? 47  LEU L CD2 1 
ATOM   4048 N  N   . ILE C 3 48  ? 28.391  -29.145 31.644  1.00 68.16  ? 48  ILE L N   1 
ATOM   4049 C  CA  . ILE C 3 48  ? 28.345  -28.936 33.082  1.00 69.16  ? 48  ILE L CA  1 
ATOM   4050 C  C   . ILE C 3 48  ? 27.048  -28.214 33.438  1.00 68.28  ? 48  ILE L C   1 
ATOM   4051 O  O   . ILE C 3 48  ? 26.509  -27.462 32.630  1.00 66.15  ? 48  ILE L O   1 
ATOM   4052 C  CB  . ILE C 3 48  ? 29.580  -28.139 33.556  1.00 69.59  ? 48  ILE L CB  1 
ATOM   4053 C  CG1 . ILE C 3 48  ? 30.890  -28.702 32.994  1.00 69.91  ? 48  ILE L CG1 1 
ATOM   4054 C  CG2 . ILE C 3 48  ? 29.616  -28.042 35.074  1.00 71.21  ? 48  ILE L CG2 1 
ATOM   4055 C  CD1 . ILE C 3 48  ? 31.167  -30.138 33.374  1.00 71.26  ? 48  ILE L CD1 1 
ATOM   4056 N  N   . TYR C 3 49  ? 26.556  -28.468 34.656  1.00 71.50  ? 49  TYR L N   1 
ATOM   4057 C  CA  . TYR C 3 49  ? 25.498  -27.674 35.262  1.00 72.02  ? 49  TYR L CA  1 
ATOM   4058 C  C   . TYR C 3 49  ? 25.775  -27.562 36.759  1.00 73.67  ? 49  TYR L C   1 
ATOM   4059 O  O   . TYR C 3 49  ? 26.466  -28.403 37.329  1.00 75.57  ? 49  TYR L O   1 
ATOM   4060 C  CB  . TYR C 3 49  ? 24.119  -28.271 34.962  1.00 71.77  ? 49  TYR L CB  1 
ATOM   4061 C  CG  . TYR C 3 49  ? 23.840  -29.624 35.571  1.00 73.31  ? 49  TYR L CG  1 
ATOM   4062 C  CD1 . TYR C 3 49  ? 23.514  -29.758 36.913  1.00 74.50  ? 49  TYR L CD1 1 
ATOM   4063 C  CD2 . TYR C 3 49  ? 23.889  -30.776 34.802  1.00 73.87  ? 49  TYR L CD2 1 
ATOM   4064 C  CE1 . TYR C 3 49  ? 23.249  -30.998 37.473  1.00 76.13  ? 49  TYR L CE1 1 
ATOM   4065 C  CE2 . TYR C 3 49  ? 23.628  -32.023 35.346  1.00 75.64  ? 49  TYR L CE2 1 
ATOM   4066 C  CZ  . TYR C 3 49  ? 23.306  -32.135 36.687  1.00 76.52  ? 49  TYR L CZ  1 
ATOM   4067 O  OH  . TYR C 3 49  ? 23.048  -33.370 37.231  1.00 78.15  ? 49  TYR L OH  1 
ATOM   4068 N  N   . GLY C 3 50  ? 25.241  -26.508 37.383  1.00 74.34  ? 50  GLY L N   1 
ATOM   4069 C  CA  . GLY C 3 50  ? 25.487  -26.248 38.792  1.00 76.97  ? 50  GLY L CA  1 
ATOM   4070 C  C   . GLY C 3 50  ? 26.958  -25.950 39.074  1.00 79.05  ? 50  GLY L C   1 
ATOM   4071 O  O   . GLY C 3 50  ? 27.449  -26.253 40.160  1.00 80.92  ? 50  GLY L O   1 
ATOM   4072 N  N   . ALA C 3 51  ? 27.644  -25.370 38.076  1.00 79.16  ? 51  ALA L N   1 
ATOM   4073 C  CA  . ALA C 3 51  ? 29.032  -24.934 38.174  1.00 80.23  ? 51  ALA L CA  1 
ATOM   4074 C  C   . ALA C 3 51  ? 30.000  -26.089 37.915  1.00 81.41  ? 51  ALA L C   1 
ATOM   4075 O  O   . ALA C 3 51  ? 30.873  -25.962 37.059  1.00 81.03  ? 51  ALA L O   1 
ATOM   4076 C  CB  . ALA C 3 51  ? 29.302  -24.272 39.507  1.00 82.45  ? 51  ALA L CB  1 
ATOM   4077 N  N   . SER C 3 52  ? 29.858  -27.197 38.660  1.00 83.09  ? 52  SER L N   1 
ATOM   4078 C  CA  . SER C 3 52  ? 30.868  -28.248 38.673  1.00 84.49  ? 52  SER L CA  1 
ATOM   4079 C  C   . SER C 3 52  ? 30.326  -29.617 38.252  1.00 84.14  ? 52  SER L C   1 
ATOM   4080 O  O   . SER C 3 52  ? 31.116  -30.490 37.896  1.00 85.31  ? 52  SER L O   1 
ATOM   4081 C  CB  . SER C 3 52  ? 31.521  -28.329 40.031  1.00 87.12  ? 52  SER L CB  1 
ATOM   4082 O  OG  . SER C 3 52  ? 30.564  -28.614 41.040  1.00 88.38  ? 52  SER L OG  1 
ATOM   4083 N  N   . THR C 3 53  ? 28.999  -29.815 38.287  1.00 82.56  ? 53  THR L N   1 
ATOM   4084 C  CA  . THR C 3 53  ? 28.418  -31.138 38.105  1.00 82.80  ? 53  THR L CA  1 
ATOM   4085 C  C   . THR C 3 53  ? 28.290  -31.468 36.618  1.00 81.34  ? 53  THR L C   1 
ATOM   4086 O  O   . THR C 3 53  ? 27.636  -30.740 35.875  1.00 78.67  ? 53  THR L O   1 
ATOM   4087 C  CB  . THR C 3 53  ? 27.054  -31.246 38.800  1.00 82.65  ? 53  THR L CB  1 
ATOM   4088 O  OG1 . THR C 3 53  ? 27.216  -30.843 40.160  1.00 84.40  ? 53  THR L OG1 1 
ATOM   4089 C  CG2 . THR C 3 53  ? 26.471  -32.641 38.744  1.00 83.82  ? 53  THR L CG2 1 
ATOM   4090 N  N   . ARG C 3 54  ? 28.894  -32.593 36.206  1.00 82.98  ? 54  ARG L N   1 
ATOM   4091 C  CA  . ARG C 3 54  ? 28.855  -33.042 34.822  1.00 82.66  ? 54  ARG L CA  1 
ATOM   4092 C  C   . ARG C 3 54  ? 27.489  -33.644 34.505  1.00 82.04  ? 54  ARG L C   1 
ATOM   4093 O  O   . ARG C 3 54  ? 26.789  -34.116 35.398  1.00 83.22  ? 54  ARG L O   1 
ATOM   4094 C  CB  . ARG C 3 54  ? 29.942  -34.088 34.549  1.00 85.19  ? 54  ARG L CB  1 
ATOM   4095 C  CG  . ARG C 3 54  ? 31.365  -33.570 34.690  1.00 86.43  ? 54  ARG L CG  1 
ATOM   4096 C  CD  . ARG C 3 54  ? 32.368  -34.449 33.967  1.00 87.80  ? 54  ARG L CD  1 
ATOM   4097 N  NE  . ARG C 3 54  ? 32.424  -35.803 34.498  1.00 91.36  ? 54  ARG L NE  1 
ATOM   4098 C  CZ  . ARG C 3 54  ? 32.951  -36.132 35.673  1.00 94.61  ? 54  ARG L CZ  1 
ATOM   4099 N  NH1 . ARG C 3 54  ? 33.492  -35.203 36.443  1.00 94.39  ? 54  ARG L NH1 1 
ATOM   4100 N  NH2 . ARG C 3 54  ? 32.944  -37.393 36.070  1.00 97.64  ? 54  ARG L NH2 1 
ATOM   4101 N  N   . ALA C 3 55  ? 27.138  -33.637 33.213  1.00 81.05  ? 55  ALA L N   1 
ATOM   4102 C  CA  . ALA C 3 55  ? 25.891  -34.212 32.733  1.00 81.90  ? 55  ALA L CA  1 
ATOM   4103 C  C   . ALA C 3 55  ? 26.096  -35.692 32.417  1.00 84.30  ? 55  ALA L C   1 
ATOM   4104 O  O   . ALA C 3 55  ? 27.199  -36.213 32.566  1.00 86.22  ? 55  ALA L O   1 
ATOM   4105 C  CB  . ALA C 3 55  ? 25.410  -33.444 31.525  1.00 80.21  ? 55  ALA L CB  1 
ATOM   4106 N  N   . THR C 3 56  ? 25.018  -36.355 31.977  1.00 85.06  ? 56  THR L N   1 
ATOM   4107 C  CA  . THR C 3 56  ? 25.040  -37.778 31.674  1.00 87.32  ? 56  THR L CA  1 
ATOM   4108 C  C   . THR C 3 56  ? 25.844  -38.029 30.400  1.00 87.25  ? 56  THR L C   1 
ATOM   4109 O  O   . THR C 3 56  ? 25.579  -37.418 29.366  1.00 85.61  ? 56  THR L O   1 
ATOM   4110 C  CB  . THR C 3 56  ? 23.617  -38.332 31.521  1.00 88.28  ? 56  THR L CB  1 
ATOM   4111 O  OG1 . THR C 3 56  ? 22.905  -38.058 32.727  1.00 89.14  ? 56  THR L OG1 1 
ATOM   4112 C  CG2 . THR C 3 56  ? 23.586  -39.818 31.234  1.00 91.30  ? 56  THR L CG2 1 
ATOM   4113 N  N   . GLY C 3 57  ? 26.819  -38.941 30.490  1.00 88.92  ? 57  GLY L N   1 
ATOM   4114 C  CA  . GLY C 3 57  ? 27.605  -39.359 29.340  1.00 89.66  ? 57  GLY L CA  1 
ATOM   4115 C  C   . GLY C 3 57  ? 28.581  -38.281 28.872  1.00 87.66  ? 57  GLY L C   1 
ATOM   4116 O  O   . GLY C 3 57  ? 28.883  -38.198 27.683  1.00 87.47  ? 57  GLY L O   1 
ATOM   4117 N  N   . ILE C 3 58  ? 29.061  -37.462 29.817  1.00 86.69  ? 58  ILE L N   1 
ATOM   4118 C  CA  . ILE C 3 58  ? 30.080  -36.460 29.546  1.00 84.69  ? 58  ILE L CA  1 
ATOM   4119 C  C   . ILE C 3 58  ? 31.392  -36.940 30.161  1.00 86.65  ? 58  ILE L C   1 
ATOM   4120 O  O   . ILE C 3 58  ? 31.437  -37.236 31.354  1.00 88.57  ? 58  ILE L O   1 
ATOM   4121 C  CB  . ILE C 3 58  ? 29.659  -35.080 30.095  1.00 81.50  ? 58  ILE L CB  1 
ATOM   4122 C  CG1 . ILE C 3 58  ? 28.353  -34.585 29.464  1.00 79.62  ? 58  ILE L CG1 1 
ATOM   4123 C  CG2 . ILE C 3 58  ? 30.783  -34.067 29.936  1.00 80.47  ? 58  ILE L CG2 1 
ATOM   4124 C  CD1 . ILE C 3 58  ? 28.398  -34.439 27.957  1.00 78.13  ? 58  ILE L CD1 1 
ATOM   4125 N  N   . PRO C 3 59  ? 32.494  -37.042 29.378  1.00 86.82  ? 59  PRO L N   1 
ATOM   4126 C  CA  . PRO C 3 59  ? 33.777  -37.512 29.906  1.00 88.59  ? 59  PRO L CA  1 
ATOM   4127 C  C   . PRO C 3 59  ? 34.255  -36.742 31.136  1.00 88.34  ? 59  PRO L C   1 
ATOM   4128 O  O   . PRO C 3 59  ? 33.847  -35.603 31.359  1.00 86.80  ? 59  PRO L O   1 
ATOM   4129 C  CB  . PRO C 3 59  ? 34.755  -37.293 28.740  1.00 88.69  ? 59  PRO L CB  1 
ATOM   4130 C  CG  . PRO C 3 59  ? 33.883  -37.328 27.503  1.00 87.59  ? 59  PRO L CG  1 
ATOM   4131 C  CD  . PRO C 3 59  ? 32.559  -36.735 27.939  1.00 85.58  ? 59  PRO L CD  1 
ATOM   4132 N  N   . ALA C 3 60  ? 35.137  -37.378 31.917  1.00 90.60  ? 60  ALA L N   1 
ATOM   4133 C  CA  . ALA C 3 60  ? 35.718  -36.768 33.104  1.00 90.91  ? 60  ALA L CA  1 
ATOM   4134 C  C   . ALA C 3 60  ? 36.771  -35.731 32.711  1.00 89.89  ? 60  ALA L C   1 
ATOM   4135 O  O   . ALA C 3 60  ? 37.232  -34.968 33.558  1.00 89.57  ? 60  ALA L O   1 
ATOM   4136 C  CB  . ALA C 3 60  ? 36.305  -37.838 33.992  1.00 93.91  ? 60  ALA L CB  1 
ATOM   4137 N  N   . ARG C 3 61  ? 37.155  -35.730 31.427  1.00 89.56  ? 61  ARG L N   1 
ATOM   4138 C  CA  . ARG C 3 61  ? 38.050  -34.735 30.857  1.00 89.14  ? 61  ARG L CA  1 
ATOM   4139 C  C   . ARG C 3 61  ? 37.528  -33.327 31.147  1.00 85.99  ? 61  ARG L C   1 
ATOM   4140 O  O   . ARG C 3 61  ? 38.262  -32.488 31.668  1.00 85.43  ? 61  ARG L O   1 
ATOM   4141 C  CB  . ARG C 3 61  ? 38.185  -34.995 29.352  1.00 89.86  ? 61  ARG L CB  1 
ATOM   4142 C  CG  . ARG C 3 61  ? 39.081  -34.012 28.613  1.00 90.28  ? 61  ARG L CG  1 
ATOM   4143 C  CD  . ARG C 3 61  ? 39.394  -34.474 27.202  1.00 91.00  ? 61  ARG L CD  1 
ATOM   4144 N  NE  . ARG C 3 61  ? 38.203  -34.673 26.384  1.00 89.66  ? 61  ARG L NE  1 
ATOM   4145 C  CZ  . ARG C 3 61  ? 37.771  -35.851 25.942  1.00 90.84  ? 61  ARG L CZ  1 
ATOM   4146 N  NH1 . ARG C 3 61  ? 38.382  -36.965 26.304  1.00 93.33  ? 61  ARG L NH1 1 
ATOM   4147 N  NH2 . ARG C 3 61  ? 36.713  -35.912 25.151  1.00 90.10  ? 61  ARG L NH2 1 
ATOM   4148 N  N   . PHE C 3 62  ? 36.255  -33.085 30.810  1.00 83.10  ? 62  PHE L N   1 
ATOM   4149 C  CA  . PHE C 3 62  ? 35.615  -31.795 31.019  1.00 80.65  ? 62  PHE L CA  1 
ATOM   4150 C  C   . PHE C 3 62  ? 35.354  -31.587 32.510  1.00 80.95  ? 62  PHE L C   1 
ATOM   4151 O  O   . PHE C 3 62  ? 34.754  -32.443 33.156  1.00 82.03  ? 62  PHE L O   1 
ATOM   4152 C  CB  . PHE C 3 62  ? 34.311  -31.717 30.220  1.00 78.61  ? 62  PHE L CB  1 
ATOM   4153 C  CG  . PHE C 3 62  ? 34.471  -31.931 28.736  1.00 78.32  ? 62  PHE L CG  1 
ATOM   4154 C  CD1 . PHE C 3 62  ? 35.000  -30.937 27.927  1.00 77.35  ? 62  PHE L CD1 1 
ATOM   4155 C  CD2 . PHE C 3 62  ? 34.113  -33.136 28.150  1.00 79.10  ? 62  PHE L CD2 1 
ATOM   4156 C  CE1 . PHE C 3 62  ? 35.151  -31.137 26.563  1.00 76.94  ? 62  PHE L CE1 1 
ATOM   4157 C  CE2 . PHE C 3 62  ? 34.268  -33.336 26.786  1.00 78.96  ? 62  PHE L CE2 1 
ATOM   4158 C  CZ  . PHE C 3 62  ? 34.786  -32.336 25.995  1.00 77.98  ? 62  PHE L CZ  1 
ATOM   4159 N  N   . SER C 3 63  ? 35.795  -30.439 33.041  1.00 80.02  ? 63  SER L N   1 
ATOM   4160 C  CA  . SER C 3 63  ? 35.761  -30.176 34.472  1.00 80.12  ? 63  SER L CA  1 
ATOM   4161 C  C   . SER C 3 63  ? 35.397  -28.716 34.737  1.00 78.56  ? 63  SER L C   1 
ATOM   4162 O  O   . SER C 3 63  ? 36.184  -27.819 34.443  1.00 78.44  ? 63  SER L O   1 
ATOM   4163 C  CB  . SER C 3 63  ? 37.085  -30.533 35.101  1.00 82.31  ? 63  SER L CB  1 
ATOM   4164 O  OG  . SER C 3 63  ? 37.086  -30.244 36.491  1.00 83.50  ? 63  SER L OG  1 
ATOM   4165 N  N   . GLY C 3 64  ? 34.205  -28.495 35.308  1.00 77.82  ? 64  GLY L N   1 
ATOM   4166 C  CA  . GLY C 3 64  ? 33.741  -27.162 35.663  1.00 76.74  ? 64  GLY L CA  1 
ATOM   4167 C  C   . GLY C 3 64  ? 34.053  -26.815 37.119  1.00 78.05  ? 64  GLY L C   1 
ATOM   4168 O  O   . GLY C 3 64  ? 34.108  -27.700 37.971  1.00 79.74  ? 64  GLY L O   1 
ATOM   4169 N  N   . SER C 3 65  ? 34.253  -25.519 37.391  1.00 77.94  ? 65  SER L N   1 
ATOM   4170 C  CA  . SER C 3 65  ? 34.561  -25.042 38.731  1.00 80.43  ? 65  SER L CA  1 
ATOM   4171 C  C   . SER C 3 65  ? 34.317  -23.537 38.829  1.00 80.70  ? 65  SER L C   1 
ATOM   4172 O  O   . SER C 3 65  ? 34.101  -22.871 37.818  1.00 78.43  ? 65  SER L O   1 
ATOM   4173 C  CB  . SER C 3 65  ? 35.976  -25.390 39.121  1.00 82.20  ? 65  SER L CB  1 
ATOM   4174 O  OG  . SER C 3 65  ? 36.906  -24.817 38.215  1.00 82.01  ? 65  SER L OG  1 
ATOM   4175 N  N   . GLY C 3 66  ? 34.354  -23.019 40.064  1.00 83.52  ? 66  GLY L N   1 
ATOM   4176 C  CA  . GLY C 3 66  ? 34.183  -21.599 40.327  1.00 85.08  ? 66  GLY L CA  1 
ATOM   4177 C  C   . GLY C 3 66  ? 32.751  -21.261 40.736  1.00 85.55  ? 66  GLY L C   1 
ATOM   4178 O  O   . GLY C 3 66  ? 31.839  -22.060 40.532  1.00 85.12  ? 66  GLY L O   1 
ATOM   4179 N  N   . SER C 3 67  ? 32.575  -20.067 41.315  1.00 87.77  ? 67  SER L N   1 
ATOM   4180 C  CA  . SER C 3 67  ? 31.272  -19.600 41.764  1.00 88.35  ? 67  SER L CA  1 
ATOM   4181 C  C   . SER C 3 67  ? 31.273  -18.078 41.879  1.00 90.42  ? 67  SER L C   1 
ATOM   4182 O  O   . SER C 3 67  ? 32.329  -17.460 42.007  1.00 93.41  ? 67  SER L O   1 
ATOM   4183 C  CB  . SER C 3 67  ? 30.885  -20.247 43.070  1.00 89.86  ? 67  SER L CB  1 
ATOM   4184 O  OG  . SER C 3 67  ? 31.837  -19.957 44.083  1.00 92.87  ? 67  SER L OG  1 
ATOM   4185 N  N   . GLY C 3 68  ? 30.073  -17.488 41.833  1.00 89.91  ? 68  GLY L N   1 
ATOM   4186 C  CA  . GLY C 3 68  ? 29.909  -16.047 41.938  1.00 91.33  ? 68  GLY L CA  1 
ATOM   4187 C  C   . GLY C 3 68  ? 30.015  -15.366 40.576  1.00 90.93  ? 68  GLY L C   1 
ATOM   4188 O  O   . GLY C 3 68  ? 29.071  -15.411 39.790  1.00 89.59  ? 68  GLY L O   1 
ATOM   4189 N  N   . THR C 3 69  ? 31.172  -14.743 40.311  1.00 92.74  ? 69  THR L N   1 
ATOM   4190 C  CA  . THR C 3 69  ? 31.389  -13.988 39.086  1.00 91.61  ? 69  THR L CA  1 
ATOM   4191 C  C   . THR C 3 69  ? 32.580  -14.536 38.298  1.00 91.65  ? 69  THR L C   1 
ATOM   4192 O  O   . THR C 3 69  ? 32.998  -13.916 37.323  1.00 91.13  ? 69  THR L O   1 
ATOM   4193 C  CB  . THR C 3 69  ? 31.603  -12.499 39.392  1.00 93.59  ? 69  THR L CB  1 
ATOM   4194 O  OG1 . THR C 3 69  ? 32.762  -12.375 40.218  1.00 95.72  ? 69  THR L OG1 1 
ATOM   4195 C  CG2 . THR C 3 69  ? 30.416  -11.861 40.079  1.00 94.14  ? 69  THR L CG2 1 
ATOM   4196 N  N   . GLU C 3 70  ? 33.121  -15.690 38.713  1.00 92.19  ? 70  GLU L N   1 
ATOM   4197 C  CA  . GLU C 3 70  ? 34.296  -16.263 38.074  1.00 92.09  ? 70  GLU L CA  1 
ATOM   4198 C  C   . GLU C 3 70  ? 34.158  -17.782 38.001  1.00 90.39  ? 70  GLU L C   1 
ATOM   4199 O  O   . GLU C 3 70  ? 34.201  -18.459 39.027  1.00 91.47  ? 70  GLU L O   1 
ATOM   4200 C  CB  . GLU C 3 70  ? 35.569  -15.879 38.834  1.00 95.47  ? 70  GLU L CB  1 
ATOM   4201 C  CG  . GLU C 3 70  ? 35.901  -14.395 38.781  1.00 97.91  ? 70  GLU L CG  1 
ATOM   4202 C  CD  . GLU C 3 70  ? 36.247  -13.843 37.406  1.00 97.93  ? 70  GLU L CD  1 
ATOM   4203 O  OE1 . GLU C 3 70  ? 36.357  -14.639 36.451  1.00 95.69  ? 70  GLU L OE1 1 
ATOM   4204 O  OE2 . GLU C 3 70  ? 36.403  -12.610 37.293  1.00 100.70 ? 70  GLU L OE2 1 
ATOM   4205 N  N   . PHE C 3 71  ? 34.005  -18.296 36.773  1.00 87.74  ? 71  PHE L N   1 
ATOM   4206 C  CA  . PHE C 3 71  ? 33.889  -19.724 36.521  1.00 86.34  ? 71  PHE L CA  1 
ATOM   4207 C  C   . PHE C 3 71  ? 34.955  -20.154 35.517  1.00 85.66  ? 71  PHE L C   1 
ATOM   4208 O  O   . PHE C 3 71  ? 35.566  -19.314 34.859  1.00 85.74  ? 71  PHE L O   1 
ATOM   4209 C  CB  . PHE C 3 71  ? 32.489  -20.072 36.008  1.00 84.32  ? 71  PHE L CB  1 
ATOM   4210 C  CG  . PHE C 3 71  ? 31.356  -19.634 36.903  1.00 84.39  ? 71  PHE L CG  1 
ATOM   4211 C  CD1 . PHE C 3 71  ? 30.923  -18.317 36.910  1.00 84.63  ? 71  PHE L CD1 1 
ATOM   4212 C  CD2 . PHE C 3 71  ? 30.729  -20.538 37.747  1.00 83.86  ? 71  PHE L CD2 1 
ATOM   4213 C  CE1 . PHE C 3 71  ? 29.882  -17.916 37.734  1.00 84.66  ? 71  PHE L CE1 1 
ATOM   4214 C  CE2 . PHE C 3 71  ? 29.689  -20.136 38.570  1.00 84.11  ? 71  PHE L CE2 1 
ATOM   4215 C  CZ  . PHE C 3 71  ? 29.269  -18.826 38.564  1.00 84.58  ? 71  PHE L CZ  1 
ATOM   4216 N  N   . THR C 3 72  ? 35.163  -21.473 35.410  1.00 84.34  ? 72  THR L N   1 
ATOM   4217 C  CA  . THR C 3 72  ? 36.193  -22.034 34.551  1.00 83.38  ? 72  THR L CA  1 
ATOM   4218 C  C   . THR C 3 72  ? 35.749  -23.396 34.021  1.00 81.93  ? 72  THR L C   1 
ATOM   4219 O  O   . THR C 3 72  ? 35.104  -24.160 34.734  1.00 82.43  ? 72  THR L O   1 
ATOM   4220 C  CB  . THR C 3 72  ? 37.527  -22.161 35.300  1.00 85.21  ? 72  THR L CB  1 
ATOM   4221 O  OG1 . THR C 3 72  ? 37.947  -20.853 35.688  1.00 87.28  ? 72  THR L OG1 1 
ATOM   4222 C  CG2 . THR C 3 72  ? 38.617  -22.812 34.476  1.00 85.70  ? 72  THR L CG2 1 
ATOM   4223 N  N   . LEU C 3 73  ? 36.105  -23.676 32.761  1.00 80.99  ? 73  LEU L N   1 
ATOM   4224 C  CA  . LEU C 3 73  ? 35.984  -25.004 32.181  1.00 79.67  ? 73  LEU L CA  1 
ATOM   4225 C  C   . LEU C 3 73  ? 37.383  -25.510 31.840  1.00 81.71  ? 73  LEU L C   1 
ATOM   4226 O  O   . LEU C 3 73  ? 38.166  -24.793 31.219  1.00 82.85  ? 73  LEU L O   1 
ATOM   4227 C  CB  . LEU C 3 73  ? 35.095  -24.932 30.936  1.00 76.93  ? 73  LEU L CB  1 
ATOM   4228 C  CG  . LEU C 3 73  ? 34.840  -26.259 30.220  1.00 76.28  ? 73  LEU L CG  1 
ATOM   4229 C  CD1 . LEU C 3 73  ? 34.028  -27.204 31.093  1.00 76.35  ? 73  LEU L CD1 1 
ATOM   4230 C  CD2 . LEU C 3 73  ? 34.136  -26.029 28.891  1.00 74.57  ? 73  LEU L CD2 1 
ATOM   4231 N  N   . THR C 3 74  ? 37.683  -26.746 32.257  1.00 82.96  ? 74  THR L N   1 
ATOM   4232 C  CA  . THR C 3 74  ? 38.999  -27.338 32.074  1.00 84.73  ? 74  THR L CA  1 
ATOM   4233 C  C   . THR C 3 74  ? 38.863  -28.636 31.284  1.00 85.82  ? 74  THR L C   1 
ATOM   4234 O  O   . THR C 3 74  ? 38.185  -29.561 31.726  1.00 86.82  ? 74  THR L O   1 
ATOM   4235 C  CB  . THR C 3 74  ? 39.681  -27.581 33.427  1.00 86.17  ? 74  THR L CB  1 
ATOM   4236 O  OG1 . THR C 3 74  ? 39.782  -26.326 34.099  1.00 86.40  ? 74  THR L OG1 1 
ATOM   4237 C  CG2 . THR C 3 74  ? 41.053  -28.205 33.297  1.00 88.13  ? 74  THR L CG2 1 
ATOM   4238 N  N   . ILE C 3 75  ? 39.517  -28.687 30.117  1.00 87.47  ? 75  ILE L N   1 
ATOM   4239 C  CA  . ILE C 3 75  ? 39.530  -29.873 29.274  1.00 89.25  ? 75  ILE L CA  1 
ATOM   4240 C  C   . ILE C 3 75  ? 40.921  -30.499 29.373  1.00 92.71  ? 75  ILE L C   1 
ATOM   4241 O  O   . ILE C 3 75  ? 41.877  -29.972 28.811  1.00 93.75  ? 75  ILE L O   1 
ATOM   4242 C  CB  . ILE C 3 75  ? 39.143  -29.519 27.821  1.00 87.73  ? 75  ILE L CB  1 
ATOM   4243 C  CG1 . ILE C 3 75  ? 37.983  -28.519 27.762  1.00 85.02  ? 75  ILE L CG1 1 
ATOM   4244 C  CG2 . ILE C 3 75  ? 38.840  -30.780 27.024  1.00 88.14  ? 75  ILE L CG2 1 
ATOM   4245 C  CD1 . ILE C 3 75  ? 37.606  -28.088 26.363  1.00 83.64  ? 75  ILE L CD1 1 
ATOM   4246 N  N   . SER C 3 76  ? 41.017  -31.623 30.097  1.00 95.03  ? 76  SER L N   1 
ATOM   4247 C  CA  . SER C 3 76  ? 42.295  -32.175 30.520  1.00 99.79  ? 76  SER L CA  1 
ATOM   4248 C  C   . SER C 3 76  ? 43.097  -32.701 29.328  1.00 102.71 ? 76  SER L C   1 
ATOM   4249 O  O   . SER C 3 76  ? 43.988  -32.010 28.839  1.00 106.62 ? 76  SER L O   1 
ATOM   4250 C  CB  . SER C 3 76  ? 42.101  -33.230 31.581  1.00 101.74 ? 76  SER L CB  1 
ATOM   4251 O  OG  . SER C 3 76  ? 41.617  -32.648 32.783  1.00 102.07 ? 76  SER L OG  1 
ATOM   4252 N  N   . SER C 3 77  ? 42.798  -33.927 28.879  1.00 103.20 ? 77  SER L N   1 
ATOM   4253 C  CA  . SER C 3 77  ? 43.525  -34.539 27.777  1.00 103.95 ? 77  SER L CA  1 
ATOM   4254 C  C   . SER C 3 77  ? 42.820  -34.216 26.463  1.00 100.75 ? 77  SER L C   1 
ATOM   4255 O  O   . SER C 3 77  ? 42.124  -35.062 25.904  1.00 100.78 ? 77  SER L O   1 
ATOM   4256 C  CB  . SER C 3 77  ? 43.672  -36.027 27.982  1.00 106.72 ? 77  SER L CB  1 
ATOM   4257 O  OG  . SER C 3 77  ? 42.403  -36.656 28.089  1.00 106.59 ? 77  SER L OG  1 
ATOM   4258 N  N   . LEU C 3 78  ? 43.026  -32.984 25.979  1.00 97.61  ? 78  LEU L N   1 
ATOM   4259 C  CA  . LEU C 3 78  ? 42.304  -32.452 24.834  1.00 94.29  ? 78  LEU L CA  1 
ATOM   4260 C  C   . LEU C 3 78  ? 42.499  -33.359 23.620  1.00 93.35  ? 78  LEU L C   1 
ATOM   4261 O  O   . LEU C 3 78  ? 43.571  -33.928 23.429  1.00 95.95  ? 78  LEU L O   1 
ATOM   4262 C  CB  . LEU C 3 78  ? 42.810  -31.036 24.539  1.00 94.84  ? 78  LEU L CB  1 
ATOM   4263 C  CG  . LEU C 3 78  ? 42.005  -30.245 23.507  1.00 93.89  ? 78  LEU L CG  1 
ATOM   4264 C  CD1 . LEU C 3 78  ? 40.981  -29.347 24.187  1.00 91.54  ? 78  LEU L CD1 1 
ATOM   4265 C  CD2 . LEU C 3 78  ? 42.922  -29.431 22.605  1.00 95.19  ? 78  LEU L CD2 1 
ATOM   4266 N  N   . GLN C 3 79  ? 41.442  -33.472 22.807  1.00 89.58  ? 79  GLN L N   1 
ATOM   4267 C  CA  . GLN C 3 79  ? 41.458  -34.268 21.591  1.00 89.28  ? 79  GLN L CA  1 
ATOM   4268 C  C   . GLN C 3 79  ? 41.058  -33.384 20.413  1.00 87.58  ? 79  GLN L C   1 
ATOM   4269 O  O   . GLN C 3 79  ? 40.614  -32.254 20.605  1.00 85.43  ? 79  GLN L O   1 
ATOM   4270 C  CB  . GLN C 3 79  ? 40.506  -35.456 21.732  1.00 89.02  ? 79  GLN L CB  1 
ATOM   4271 C  CG  . GLN C 3 79  ? 40.848  -36.373 22.898  1.00 90.30  ? 79  GLN L CG  1 
ATOM   4272 C  CD  . GLN C 3 79  ? 39.844  -37.485 23.080  1.00 90.29  ? 79  GLN L CD  1 
ATOM   4273 O  OE1 . GLN C 3 79  ? 38.846  -37.574 22.369  1.00 89.20  ? 79  GLN L OE1 1 
ATOM   4274 N  NE2 . GLN C 3 79  ? 40.103  -38.345 24.051  1.00 91.89  ? 79  GLN L NE2 1 
ATOM   4275 N  N   . SER C 3 80  ? 41.214  -33.919 19.196  1.00 88.60  ? 80  SER L N   1 
ATOM   4276 C  CA  . SER C 3 80  ? 40.869  -33.199 17.979  1.00 87.58  ? 80  SER L CA  1 
ATOM   4277 C  C   . SER C 3 80  ? 39.353  -33.041 17.862  1.00 85.55  ? 80  SER L C   1 
ATOM   4278 O  O   . SER C 3 80  ? 38.878  -32.092 17.241  1.00 84.14  ? 80  SER L O   1 
ATOM   4279 C  CB  . SER C 3 80  ? 41.442  -33.882 16.763  1.00 89.58  ? 80  SER L CB  1 
ATOM   4280 O  OG  . SER C 3 80  ? 40.887  -35.179 16.598  1.00 90.99  ? 80  SER L OG  1 
ATOM   4281 N  N   . GLU C 3 81  ? 38.605  -33.971 18.472  1.00 85.13  ? 81  GLU L N   1 
ATOM   4282 C  CA  . GLU C 3 81  ? 37.151  -33.950 18.429  1.00 83.50  ? 81  GLU L CA  1 
ATOM   4283 C  C   . GLU C 3 81  ? 36.604  -32.854 19.344  1.00 80.39  ? 81  GLU L C   1 
ATOM   4284 O  O   . GLU C 3 81  ? 35.415  -32.549 19.289  1.00 78.15  ? 81  GLU L O   1 
ATOM   4285 C  CB  . GLU C 3 81  ? 36.569  -35.308 18.832  1.00 84.57  ? 81  GLU L CB  1 
ATOM   4286 C  CG  . GLU C 3 81  ? 36.860  -36.427 17.844  1.00 86.92  ? 81  GLU L CG  1 
ATOM   4287 C  CD  . GLU C 3 81  ? 38.243  -37.051 17.934  1.00 89.63  ? 81  GLU L CD  1 
ATOM   4288 O  OE1 . GLU C 3 81  ? 39.023  -36.643 18.817  1.00 89.19  ? 81  GLU L OE1 1 
ATOM   4289 O  OE2 . GLU C 3 81  ? 38.537  -37.948 17.117  1.00 92.15  ? 81  GLU L OE2 1 
ATOM   4290 N  N   . ASP C 3 82  ? 37.474  -32.262 20.176  1.00 80.34  ? 82  ASP L N   1 
ATOM   4291 C  CA  . ASP C 3 82  ? 37.083  -31.202 21.092  1.00 79.61  ? 82  ASP L CA  1 
ATOM   4292 C  C   . ASP C 3 82  ? 37.135  -29.838 20.397  1.00 78.23  ? 82  ASP L C   1 
ATOM   4293 O  O   . ASP C 3 82  ? 37.059  -28.807 21.064  1.00 76.76  ? 82  ASP L O   1 
ATOM   4294 C  CB  . ASP C 3 82  ? 37.964  -31.218 22.346  1.00 81.26  ? 82  ASP L CB  1 
ATOM   4295 C  CG  . ASP C 3 82  ? 37.931  -32.531 23.113  1.00 82.80  ? 82  ASP L CG  1 
ATOM   4296 O  OD1 . ASP C 3 82  ? 37.105  -33.397 22.763  1.00 83.59  ? 82  ASP L OD1 1 
ATOM   4297 O  OD2 . ASP C 3 82  ? 38.741  -32.682 24.050  1.00 83.94  ? 82  ASP L OD2 1 
ATOM   4298 N  N   . PHE C 3 83  ? 37.272  -29.831 19.064  1.00 78.57  ? 83  PHE L N   1 
ATOM   4299 C  CA  . PHE C 3 83  ? 37.101  -28.621 18.276  1.00 76.60  ? 83  PHE L CA  1 
ATOM   4300 C  C   . PHE C 3 83  ? 35.637  -28.191 18.332  1.00 74.26  ? 83  PHE L C   1 
ATOM   4301 O  O   . PHE C 3 83  ? 34.773  -28.872 17.783  1.00 74.18  ? 83  PHE L O   1 
ATOM   4302 C  CB  . PHE C 3 83  ? 37.529  -28.848 16.822  1.00 77.52  ? 83  PHE L CB  1 
ATOM   4303 C  CG  . PHE C 3 83  ? 37.190  -27.709 15.892  1.00 76.65  ? 83  PHE L CG  1 
ATOM   4304 C  CD1 . PHE C 3 83  ? 37.931  -26.537 15.905  1.00 76.46  ? 83  PHE L CD1 1 
ATOM   4305 C  CD2 . PHE C 3 83  ? 36.106  -27.793 15.030  1.00 75.89  ? 83  PHE L CD2 1 
ATOM   4306 C  CE1 . PHE C 3 83  ? 37.609  -25.485 15.061  1.00 76.38  ? 83  PHE L CE1 1 
ATOM   4307 C  CE2 . PHE C 3 83  ? 35.784  -26.739 14.189  1.00 75.31  ? 83  PHE L CE2 1 
ATOM   4308 C  CZ  . PHE C 3 83  ? 36.536  -25.587 14.205  1.00 75.70  ? 83  PHE L CZ  1 
ATOM   4309 N  N   . ALA C 3 84  ? 35.373  -27.060 18.995  1.00 73.12  ? 84  ALA L N   1 
ATOM   4310 C  CA  . ALA C 3 84  ? 34.015  -26.567 19.170  1.00 71.83  ? 84  ALA L CA  1 
ATOM   4311 C  C   . ALA C 3 84  ? 34.038  -25.143 19.718  1.00 70.63  ? 84  ALA L C   1 
ATOM   4312 O  O   . ALA C 3 84  ? 35.086  -24.642 20.122  1.00 70.89  ? 84  ALA L O   1 
ATOM   4313 C  CB  . ALA C 3 84  ? 33.250  -27.487 20.092  1.00 70.86  ? 84  ALA L CB  1 
ATOM   4314 N  N   . VAL C 3 85  ? 32.862  -24.504 19.713  1.00 69.35  ? 85  VAL L N   1 
ATOM   4315 C  CA  . VAL C 3 85  ? 32.655  -23.240 20.401  1.00 68.51  ? 85  VAL L CA  1 
ATOM   4316 C  C   . VAL C 3 85  ? 31.971  -23.539 21.733  1.00 65.88  ? 85  VAL L C   1 
ATOM   4317 O  O   . VAL C 3 85  ? 30.931  -24.193 21.765  1.00 62.96  ? 85  VAL L O   1 
ATOM   4318 C  CB  . VAL C 3 85  ? 31.829  -22.254 19.551  1.00 68.78  ? 85  VAL L CB  1 
ATOM   4319 C  CG1 . VAL C 3 85  ? 31.753  -20.882 20.205  1.00 68.72  ? 85  VAL L CG1 1 
ATOM   4320 C  CG2 . VAL C 3 85  ? 32.367  -22.141 18.132  1.00 70.26  ? 85  VAL L CG2 1 
ATOM   4321 N  N   . TYR C 3 86  ? 32.572  -23.054 22.825  1.00 65.75  ? 86  TYR L N   1 
ATOM   4322 C  CA  . TYR C 3 86  ? 32.095  -23.348 24.165  1.00 65.68  ? 86  TYR L CA  1 
ATOM   4323 C  C   . TYR C 3 86  ? 31.424  -22.106 24.745  1.00 65.64  ? 86  TYR L C   1 
ATOM   4324 O  O   . TYR C 3 86  ? 31.993  -21.016 24.713  1.00 64.61  ? 86  TYR L O   1 
ATOM   4325 C  CB  . TYR C 3 86  ? 33.245  -23.857 25.037  1.00 66.49  ? 86  TYR L CB  1 
ATOM   4326 C  CG  . TYR C 3 86  ? 33.840  -25.159 24.564  1.00 67.37  ? 86  TYR L CG  1 
ATOM   4327 C  CD1 . TYR C 3 86  ? 34.687  -25.204 23.467  1.00 68.95  ? 86  TYR L CD1 1 
ATOM   4328 C  CD2 . TYR C 3 86  ? 33.529  -26.357 25.189  1.00 67.37  ? 86  TYR L CD2 1 
ATOM   4329 C  CE1 . TYR C 3 86  ? 35.227  -26.398 23.017  1.00 69.86  ? 86  TYR L CE1 1 
ATOM   4330 C  CE2 . TYR C 3 86  ? 34.060  -27.560 24.752  1.00 68.72  ? 86  TYR L CE2 1 
ATOM   4331 C  CZ  . TYR C 3 86  ? 34.912  -27.582 23.661  1.00 69.83  ? 86  TYR L CZ  1 
ATOM   4332 O  OH  . TYR C 3 86  ? 35.441  -28.770 23.221  1.00 70.92  ? 86  TYR L OH  1 
ATOM   4333 N  N   . TYR C 3 87  ? 30.206  -22.301 25.267  1.00 66.74  ? 87  TYR L N   1 
ATOM   4334 C  CA  . TYR C 3 87  ? 29.390  -21.231 25.818  1.00 67.00  ? 87  TYR L CA  1 
ATOM   4335 C  C   . TYR C 3 87  ? 29.090  -21.519 27.286  1.00 66.55  ? 87  TYR L C   1 
ATOM   4336 O  O   . TYR C 3 87  ? 29.027  -22.676 27.694  1.00 67.28  ? 87  TYR L O   1 
ATOM   4337 C  CB  . TYR C 3 87  ? 28.077  -21.107 25.040  1.00 66.43  ? 87  TYR L CB  1 
ATOM   4338 C  CG  . TYR C 3 87  ? 28.238  -20.767 23.580  1.00 67.49  ? 87  TYR L CG  1 
ATOM   4339 C  CD1 . TYR C 3 87  ? 28.431  -19.459 23.166  1.00 68.69  ? 87  TYR L CD1 1 
ATOM   4340 C  CD2 . TYR C 3 87  ? 28.221  -21.757 22.611  1.00 67.57  ? 87  TYR L CD2 1 
ATOM   4341 C  CE1 . TYR C 3 87  ? 28.582  -19.140 21.826  1.00 68.98  ? 87  TYR L CE1 1 
ATOM   4342 C  CE2 . TYR C 3 87  ? 28.376  -21.456 21.267  1.00 68.06  ? 87  TYR L CE2 1 
ATOM   4343 C  CZ  . TYR C 3 87  ? 28.554  -20.142 20.873  1.00 68.41  ? 87  TYR L CZ  1 
ATOM   4344 O  OH  . TYR C 3 87  ? 28.709  -19.836 19.544  1.00 69.68  ? 87  TYR L OH  1 
ATOM   4345 N  N   . CYS C 3 88  ? 28.910  -20.450 28.068  1.00 66.68  ? 88  CYS L N   1 
ATOM   4346 C  CA  . CYS C 3 88  ? 28.381  -20.560 29.417  1.00 67.11  ? 88  CYS L CA  1 
ATOM   4347 C  C   . CYS C 3 88  ? 26.980  -19.956 29.454  1.00 66.99  ? 88  CYS L C   1 
ATOM   4348 O  O   . CYS C 3 88  ? 26.574  -19.263 28.523  1.00 66.25  ? 88  CYS L O   1 
ATOM   4349 C  CB  . CYS C 3 88  ? 29.296  -19.877 30.427  1.00 68.02  ? 88  CYS L CB  1 
ATOM   4350 S  SG  . CYS C 3 88  ? 29.687  -18.162 29.998  1.00 69.40  ? 88  CYS L SG  1 
ATOM   4351 N  N   . GLN C 3 89  ? 26.246  -20.244 30.533  1.00 67.55  ? 89  GLN L N   1 
ATOM   4352 C  CA  . GLN C 3 89  ? 24.883  -19.767 30.697  1.00 67.64  ? 89  GLN L CA  1 
ATOM   4353 C  C   . GLN C 3 89  ? 24.563  -19.656 32.184  1.00 68.88  ? 89  GLN L C   1 
ATOM   4354 O  O   . GLN C 3 89  ? 24.619  -20.652 32.903  1.00 69.93  ? 89  GLN L O   1 
ATOM   4355 C  CB  . GLN C 3 89  ? 23.891  -20.728 30.038  1.00 67.42  ? 89  GLN L CB  1 
ATOM   4356 C  CG  . GLN C 3 89  ? 22.442  -20.260 30.129  1.00 68.72  ? 89  GLN L CG  1 
ATOM   4357 C  CD  . GLN C 3 89  ? 21.456  -21.386 30.333  1.00 69.71  ? 89  GLN L CD  1 
ATOM   4358 O  OE1 . GLN C 3 89  ? 21.754  -22.557 30.107  1.00 70.78  ? 89  GLN L OE1 1 
ATOM   4359 N  NE2 . GLN C 3 89  ? 20.257  -21.031 30.764  1.00 70.63  ? 89  GLN L NE2 1 
ATOM   4360 N  N   . GLN C 3 90  ? 24.217  -18.445 32.632  1.00 69.60  ? 90  GLN L N   1 
ATOM   4361 C  CA  . GLN C 3 90  ? 23.728  -18.246 33.986  1.00 71.38  ? 90  GLN L CA  1 
ATOM   4362 C  C   . GLN C 3 90  ? 22.240  -18.585 34.021  1.00 70.85  ? 90  GLN L C   1 
ATOM   4363 O  O   . GLN C 3 90  ? 21.534  -18.397 33.032  1.00 69.12  ? 90  GLN L O   1 
ATOM   4364 C  CB  . GLN C 3 90  ? 24.002  -16.815 34.458  1.00 73.61  ? 90  GLN L CB  1 
ATOM   4365 C  CG  . GLN C 3 90  ? 23.155  -15.747 33.773  1.00 74.20  ? 90  GLN L CG  1 
ATOM   4366 C  CD  . GLN C 3 90  ? 21.808  -15.521 34.420  1.00 74.71  ? 90  GLN L CD  1 
ATOM   4367 O  OE1 . GLN C 3 90  ? 21.481  -16.103 35.453  1.00 75.53  ? 90  GLN L OE1 1 
ATOM   4368 N  NE2 . GLN C 3 90  ? 21.014  -14.655 33.814  1.00 75.00  ? 90  GLN L NE2 1 
ATOM   4369 N  N   . TYR C 3 91  ? 21.779  -19.093 35.170  1.00 72.04  ? 91  TYR L N   1 
ATOM   4370 C  CA  . TYR C 3 91  ? 20.361  -19.320 35.394  1.00 72.57  ? 91  TYR L CA  1 
ATOM   4371 C  C   . TYR C 3 91  ? 20.012  -18.975 36.841  1.00 73.65  ? 91  TYR L C   1 
ATOM   4372 O  O   . TYR C 3 91  ? 19.167  -19.624 37.455  1.00 75.20  ? 91  TYR L O   1 
ATOM   4373 C  CB  . TYR C 3 91  ? 19.978  -20.746 34.978  1.00 72.92  ? 91  TYR L CB  1 
ATOM   4374 C  CG  . TYR C 3 91  ? 20.806  -21.852 35.584  1.00 73.87  ? 91  TYR L CG  1 
ATOM   4375 C  CD1 . TYR C 3 91  ? 20.482  -22.403 36.814  1.00 74.81  ? 91  TYR L CD1 1 
ATOM   4376 C  CD2 . TYR C 3 91  ? 21.885  -22.392 34.901  1.00 74.04  ? 91  TYR L CD2 1 
ATOM   4377 C  CE1 . TYR C 3 91  ? 21.228  -23.432 37.366  1.00 75.79  ? 91  TYR L CE1 1 
ATOM   4378 C  CE2 . TYR C 3 91  ? 22.645  -23.418 35.441  1.00 74.32  ? 91  TYR L CE2 1 
ATOM   4379 C  CZ  . TYR C 3 91  ? 22.314  -23.942 36.678  1.00 75.28  ? 91  TYR L CZ  1 
ATOM   4380 O  OH  . TYR C 3 91  ? 23.053  -24.961 37.226  1.00 76.22  ? 91  TYR L OH  1 
ATOM   4381 N  N   . ASN C 3 92  ? 20.660  -17.923 37.361  1.00 73.42  ? 92  ASN L N   1 
ATOM   4382 C  CA  . ASN C 3 92  ? 20.382  -17.398 38.689  1.00 74.56  ? 92  ASN L CA  1 
ATOM   4383 C  C   . ASN C 3 92  ? 19.391  -16.239 38.587  1.00 74.16  ? 92  ASN L C   1 
ATOM   4384 O  O   . ASN C 3 92  ? 18.645  -15.978 39.528  1.00 75.27  ? 92  ASN L O   1 
ATOM   4385 C  CB  . ASN C 3 92  ? 21.665  -16.935 39.386  1.00 75.78  ? 92  ASN L CB  1 
ATOM   4386 C  CG  . ASN C 3 92  ? 21.488  -16.703 40.871  1.00 77.40  ? 92  ASN L CG  1 
ATOM   4387 O  OD1 . ASN C 3 92  ? 21.633  -15.580 41.349  1.00 80.02  ? 92  ASN L OD1 1 
ATOM   4388 N  ND2 . ASN C 3 92  ? 21.180  -17.755 41.611  1.00 77.11  ? 92  ASN L ND2 1 
ATOM   4389 N  N   . ASN C 3 93  ? 19.404  -15.548 37.439  1.00 72.71  ? 93  ASN L N   1 
ATOM   4390 C  CA  . ASN C 3 93  ? 18.624  -14.339 37.230  1.00 73.34  ? 93  ASN L CA  1 
ATOM   4391 C  C   . ASN C 3 93  ? 17.893  -14.456 35.895  1.00 71.91  ? 93  ASN L C   1 
ATOM   4392 O  O   . ASN C 3 93  ? 18.508  -14.778 34.882  1.00 71.75  ? 93  ASN L O   1 
ATOM   4393 C  CB  . ASN C 3 93  ? 19.527  -13.102 37.296  1.00 74.42  ? 93  ASN L CB  1 
ATOM   4394 C  CG  . ASN C 3 93  ? 18.855  -11.821 36.845  1.00 75.35  ? 93  ASN L CG  1 
ATOM   4395 O  OD1 . ASN C 3 93  ? 18.642  -11.612 35.653  1.00 75.35  ? 93  ASN L OD1 1 
ATOM   4396 N  ND2 . ASN C 3 93  ? 18.554  -10.940 37.784  1.00 77.10  ? 93  ASN L ND2 1 
ATOM   4397 N  N   . TRP C 3 94  ? 16.581  -14.193 35.908  1.00 71.99  ? 94  TRP L N   1 
ATOM   4398 C  CA  . TRP C 3 94  ? 15.773  -14.216 34.698  1.00 70.39  ? 94  TRP L CA  1 
ATOM   4399 C  C   . TRP C 3 94  ? 15.838  -12.850 34.017  1.00 71.87  ? 94  TRP L C   1 
ATOM   4400 O  O   . TRP C 3 94  ? 15.744  -11.827 34.690  1.00 73.90  ? 94  TRP L O   1 
ATOM   4401 C  CB  . TRP C 3 94  ? 14.328  -14.618 35.026  1.00 70.01  ? 94  TRP L CB  1 
ATOM   4402 C  CG  . TRP C 3 94  ? 13.424  -14.668 33.832  1.00 68.21  ? 94  TRP L CG  1 
ATOM   4403 C  CD1 . TRP C 3 94  ? 12.931  -13.609 33.127  1.00 68.41  ? 94  TRP L CD1 1 
ATOM   4404 C  CD2 . TRP C 3 94  ? 12.924  -15.849 33.180  1.00 66.16  ? 94  TRP L CD2 1 
ATOM   4405 N  NE1 . TRP C 3 94  ? 12.150  -14.047 32.092  1.00 67.37  ? 94  TRP L NE1 1 
ATOM   4406 C  CE2 . TRP C 3 94  ? 12.127  -15.416 32.098  1.00 66.14  ? 94  TRP L CE2 1 
ATOM   4407 C  CE3 . TRP C 3 94  ? 13.063  -17.223 33.407  1.00 65.21  ? 94  TRP L CE3 1 
ATOM   4408 C  CZ2 . TRP C 3 94  ? 11.475  -16.310 31.251  1.00 65.68  ? 94  TRP L CZ2 1 
ATOM   4409 C  CZ3 . TRP C 3 94  ? 12.419  -18.107 32.567  1.00 64.91  ? 94  TRP L CZ3 1 
ATOM   4410 C  CH2 . TRP C 3 94  ? 11.634  -17.654 31.506  1.00 65.09  ? 94  TRP L CH2 1 
ATOM   4411 N  N   . PRO C 3 95  ? 15.984  -12.770 32.671  1.00 72.12  ? 95  PRO L N   1 
ATOM   4412 C  CA  . PRO C 3 95  ? 16.108  -13.945 31.804  1.00 70.77  ? 95  PRO L CA  1 
ATOM   4413 C  C   . PRO C 3 95  ? 17.509  -14.552 31.818  1.00 70.40  ? 95  PRO L C   1 
ATOM   4414 O  O   . PRO C 3 95  ? 18.461  -13.910 32.260  1.00 71.00  ? 95  PRO L O   1 
ATOM   4415 C  CB  . PRO C 3 95  ? 15.800  -13.369 30.416  1.00 70.31  ? 95  PRO L CB  1 
ATOM   4416 C  CG  . PRO C 3 95  ? 16.343  -11.962 30.491  1.00 71.73  ? 95  PRO L CG  1 
ATOM   4417 C  CD  . PRO C 3 95  ? 16.032  -11.514 31.905  1.00 73.18  ? 95  PRO L CD  1 
ATOM   4418 N  N   . TRP C 3 96  ? 17.613  -15.793 31.323  1.00 69.24  ? 96  TRP L N   1 
ATOM   4419 C  CA  . TRP C 3 96  ? 18.894  -16.467 31.193  1.00 67.89  ? 96  TRP L CA  1 
ATOM   4420 C  C   . TRP C 3 96  ? 19.712  -15.765 30.113  1.00 66.88  ? 96  TRP L C   1 
ATOM   4421 O  O   . TRP C 3 96  ? 19.161  -15.302 29.117  1.00 65.86  ? 96  TRP L O   1 
ATOM   4422 C  CB  . TRP C 3 96  ? 18.730  -17.960 30.870  1.00 68.02  ? 96  TRP L CB  1 
ATOM   4423 C  CG  . TRP C 3 96  ? 17.639  -18.676 31.607  1.00 69.58  ? 96  TRP L CG  1 
ATOM   4424 C  CD1 . TRP C 3 96  ? 16.792  -19.612 31.087  1.00 69.84  ? 96  TRP L CD1 1 
ATOM   4425 C  CD2 . TRP C 3 96  ? 17.257  -18.517 32.987  1.00 71.36  ? 96  TRP L CD2 1 
ATOM   4426 N  NE1 . TRP C 3 96  ? 15.919  -20.052 32.045  1.00 71.07  ? 96  TRP L NE1 1 
ATOM   4427 C  CE2 . TRP C 3 96  ? 16.178  -19.398 33.220  1.00 71.74  ? 96  TRP L CE2 1 
ATOM   4428 C  CE3 . TRP C 3 96  ? 17.713  -17.721 34.045  1.00 72.41  ? 96  TRP L CE3 1 
ATOM   4429 C  CZ2 . TRP C 3 96  ? 15.558  -19.504 34.465  1.00 72.93  ? 96  TRP L CZ2 1 
ATOM   4430 C  CZ3 . TRP C 3 96  ? 17.102  -17.829 35.275  1.00 73.21  ? 96  TRP L CZ3 1 
ATOM   4431 C  CH2 . TRP C 3 96  ? 16.038  -18.708 35.480  1.00 73.46  ? 96  TRP L CH2 1 
ATOM   4432 N  N   . THR C 3 97  ? 21.029  -15.697 30.328  1.00 66.58  ? 97  THR L N   1 
ATOM   4433 C  CA  . THR C 3 97  ? 21.939  -15.074 29.383  1.00 67.01  ? 97  THR L CA  1 
ATOM   4434 C  C   . THR C 3 97  ? 23.125  -16.005 29.143  1.00 67.17  ? 97  THR L C   1 
ATOM   4435 O  O   . THR C 3 97  ? 23.561  -16.704 30.056  1.00 66.39  ? 97  THR L O   1 
ATOM   4436 C  CB  . THR C 3 97  ? 22.380  -13.693 29.884  1.00 67.99  ? 97  THR L CB  1 
ATOM   4437 O  OG1 . THR C 3 97  ? 22.934  -13.849 31.190  1.00 67.73  ? 97  THR L OG1 1 
ATOM   4438 C  CG2 . THR C 3 97  ? 21.244  -12.695 29.931  1.00 68.76  ? 97  THR L CG2 1 
ATOM   4439 N  N   . PHE C 3 98  ? 23.626  -16.007 27.901  1.00 68.44  ? 98  PHE L N   1 
ATOM   4440 C  CA  . PHE C 3 98  ? 24.770  -16.819 27.520  1.00 68.34  ? 98  PHE L CA  1 
ATOM   4441 C  C   . PHE C 3 98  ? 25.972  -15.916 27.268  1.00 68.69  ? 98  PHE L C   1 
ATOM   4442 O  O   . PHE C 3 98  ? 25.815  -14.715 27.060  1.00 69.97  ? 98  PHE L O   1 
ATOM   4443 C  CB  . PHE C 3 98  ? 24.470  -17.640 26.262  1.00 68.43  ? 98  PHE L CB  1 
ATOM   4444 C  CG  . PHE C 3 98  ? 23.260  -18.538 26.347  1.00 68.90  ? 98  PHE L CG  1 
ATOM   4445 C  CD1 . PHE C 3 98  ? 21.978  -18.015 26.268  1.00 69.75  ? 98  PHE L CD1 1 
ATOM   4446 C  CD2 . PHE C 3 98  ? 23.404  -19.908 26.504  1.00 69.27  ? 98  PHE L CD2 1 
ATOM   4447 C  CE1 . PHE C 3 98  ? 20.867  -18.843 26.341  1.00 70.05  ? 98  PHE L CE1 1 
ATOM   4448 C  CE2 . PHE C 3 98  ? 22.293  -20.734 26.579  1.00 69.68  ? 98  PHE L CE2 1 
ATOM   4449 C  CZ  . PHE C 3 98  ? 21.027  -20.201 26.497  1.00 69.69  ? 98  PHE L CZ  1 
ATOM   4450 N  N   . GLY C 3 99  ? 27.170  -16.511 27.289  1.00 68.90  ? 99  GLY L N   1 
ATOM   4451 C  CA  . GLY C 3 99  ? 28.383  -15.825 26.876  1.00 70.59  ? 99  GLY L CA  1 
ATOM   4452 C  C   . GLY C 3 99  ? 28.471  -15.726 25.354  1.00 71.18  ? 99  GLY L C   1 
ATOM   4453 O  O   . GLY C 3 99  ? 27.697  -16.367 24.645  1.00 68.77  ? 99  GLY L O   1 
ATOM   4454 N  N   . GLN C 3 100 ? 29.417  -14.915 24.866  1.00 74.66  ? 100 GLN L N   1 
ATOM   4455 C  CA  . GLN C 3 100 ? 29.575  -14.687 23.437  1.00 76.70  ? 100 GLN L CA  1 
ATOM   4456 C  C   . GLN C 3 100 ? 30.233  -15.904 22.785  1.00 76.10  ? 100 GLN L C   1 
ATOM   4457 O  O   . GLN C 3 100 ? 30.064  -16.125 21.588  1.00 76.52  ? 100 GLN L O   1 
ATOM   4458 C  CB  . GLN C 3 100 ? 30.346  -13.389 23.164  1.00 80.00  ? 100 GLN L CB  1 
ATOM   4459 C  CG  . GLN C 3 100 ? 31.859  -13.478 23.346  1.00 82.72  ? 100 GLN L CG  1 
ATOM   4460 C  CD  . GLN C 3 100 ? 32.317  -13.435 24.785  1.00 84.32  ? 100 GLN L CD  1 
ATOM   4461 O  OE1 . GLN C 3 100 ? 31.531  -13.228 25.708  1.00 85.47  ? 100 GLN L OE1 1 
ATOM   4462 N  NE2 . GLN C 3 100 ? 33.613  -13.619 24.984  1.00 85.48  ? 100 GLN L NE2 1 
ATOM   4463 N  N   . GLY C 3 101 ? 30.990  -16.677 23.576  1.00 75.32  ? 101 GLY L N   1 
ATOM   4464 C  CA  . GLY C 3 101 ? 31.563  -17.934 23.123  1.00 74.99  ? 101 GLY L CA  1 
ATOM   4465 C  C   . GLY C 3 101 ? 33.088  -17.930 23.191  1.00 76.89  ? 101 GLY L C   1 
ATOM   4466 O  O   . GLY C 3 101 ? 33.711  -16.870 23.200  1.00 78.48  ? 101 GLY L O   1 
ATOM   4467 N  N   . THR C 3 102 ? 33.670  -19.136 23.242  1.00 77.61  ? 102 THR L N   1 
ATOM   4468 C  CA  . THR C 3 102 ? 35.113  -19.325 23.225  1.00 78.71  ? 102 THR L CA  1 
ATOM   4469 C  C   . THR C 3 102 ? 35.447  -20.484 22.288  1.00 77.58  ? 102 THR L C   1 
ATOM   4470 O  O   . THR C 3 102 ? 35.258  -21.644 22.645  1.00 76.30  ? 102 THR L O   1 
ATOM   4471 C  CB  . THR C 3 102 ? 35.660  -19.564 24.639  1.00 79.38  ? 102 THR L CB  1 
ATOM   4472 O  OG1 . THR C 3 102 ? 35.425  -18.391 25.419  1.00 79.48  ? 102 THR L OG1 1 
ATOM   4473 C  CG2 . THR C 3 102 ? 37.137  -19.891 24.655  1.00 80.86  ? 102 THR L CG2 1 
ATOM   4474 N  N   . LYS C 3 103 ? 35.941  -20.153 21.089  1.00 79.06  ? 103 LYS L N   1 
ATOM   4475 C  CA  . LYS C 3 103 ? 36.226  -21.145 20.065  1.00 80.09  ? 103 LYS L CA  1 
ATOM   4476 C  C   . LYS C 3 103 ? 37.587  -21.779 20.337  1.00 80.44  ? 103 LYS L C   1 
ATOM   4477 O  O   . LYS C 3 103 ? 38.586  -21.074 20.455  1.00 81.45  ? 103 LYS L O   1 
ATOM   4478 C  CB  . LYS C 3 103 ? 36.192  -20.498 18.676  1.00 81.77  ? 103 LYS L CB  1 
ATOM   4479 C  CG  . LYS C 3 103 ? 36.320  -21.466 17.507  1.00 83.50  ? 103 LYS L CG  1 
ATOM   4480 C  CD  . LYS C 3 103 ? 36.184  -20.799 16.157  1.00 85.61  ? 103 LYS L CD  1 
ATOM   4481 C  CE  . LYS C 3 103 ? 36.330  -21.768 15.004  1.00 87.46  ? 103 LYS L CE  1 
ATOM   4482 N  NZ  . LYS C 3 103 ? 36.252  -21.076 13.695  1.00 89.43  ? 103 LYS L NZ  1 
ATOM   4483 N  N   . VAL C 3 104 ? 37.607  -23.115 20.431  1.00 80.02  ? 104 VAL L N   1 
ATOM   4484 C  CA  . VAL C 3 104 ? 38.832  -23.865 20.655  1.00 81.59  ? 104 VAL L CA  1 
ATOM   4485 C  C   . VAL C 3 104 ? 39.300  -24.427 19.315  1.00 83.13  ? 104 VAL L C   1 
ATOM   4486 O  O   . VAL C 3 104 ? 38.559  -25.155 18.660  1.00 83.31  ? 104 VAL L O   1 
ATOM   4487 C  CB  . VAL C 3 104 ? 38.629  -24.987 21.692  1.00 80.71  ? 104 VAL L CB  1 
ATOM   4488 C  CG1 . VAL C 3 104 ? 39.891  -25.816 21.884  1.00 82.32  ? 104 VAL L CG1 1 
ATOM   4489 C  CG2 . VAL C 3 104 ? 38.137  -24.443 23.026  1.00 79.76  ? 104 VAL L CG2 1 
ATOM   4490 N  N   . GLU C 3 105 ? 40.530  -24.074 18.923  1.00 85.98  ? 105 GLU L N   1 
ATOM   4491 C  CA  . GLU C 3 105 ? 41.125  -24.541 17.681  1.00 88.15  ? 105 GLU L CA  1 
ATOM   4492 C  C   . GLU C 3 105 ? 42.247  -25.525 18.005  1.00 90.45  ? 105 GLU L C   1 
ATOM   4493 O  O   . GLU C 3 105 ? 42.898  -25.411 19.043  1.00 90.08  ? 105 GLU L O   1 
ATOM   4494 C  CB  . GLU C 3 105 ? 41.629  -23.351 16.861  1.00 89.27  ? 105 GLU L CB  1 
ATOM   4495 C  CG  . GLU C 3 105 ? 40.511  -22.455 16.354  1.00 88.50  ? 105 GLU L CG  1 
ATOM   4496 C  CD  . GLU C 3 105 ? 40.957  -21.206 15.612  1.00 90.26  ? 105 GLU L CD  1 
ATOM   4497 O  OE1 . GLU C 3 105 ? 40.077  -20.444 15.163  1.00 89.77  ? 105 GLU L OE1 1 
ATOM   4498 O  OE2 . GLU C 3 105 ? 42.180  -20.995 15.486  1.00 92.65  ? 105 GLU L OE2 1 
ATOM   4499 N  N   . ILE C 3 106 ? 42.458  -26.489 17.100  1.00 82.73  ? 106 ILE L N   1 
ATOM   4500 C  CA  . ILE C 3 106 ? 43.400  -27.577 17.313  1.00 83.14  ? 106 ILE L CA  1 
ATOM   4501 C  C   . ILE C 3 106 ? 44.660  -27.317 16.488  1.00 81.12  ? 106 ILE L C   1 
ATOM   4502 O  O   . ILE C 3 106 ? 44.574  -27.054 15.291  1.00 79.30  ? 106 ILE L O   1 
ATOM   4503 C  CB  . ILE C 3 106 ? 42.754  -28.933 16.956  1.00 83.87  ? 106 ILE L CB  1 
ATOM   4504 C  CG1 . ILE C 3 106 ? 41.408  -29.135 17.660  1.00 86.62  ? 106 ILE L CG1 1 
ATOM   4505 C  CG2 . ILE C 3 106 ? 43.715  -30.081 17.234  1.00 84.43  ? 106 ILE L CG2 1 
ATOM   4506 C  CD1 . ILE C 3 106 ? 41.472  -29.054 19.170  1.00 89.29  ? 106 ILE L CD1 1 
ATOM   4507 N  N   . LYS C 3 107 ? 45.825  -27.401 17.143  1.00 81.82  ? 107 LYS L N   1 
ATOM   4508 C  CA  . LYS C 3 107 ? 47.106  -27.267 16.467  1.00 81.68  ? 107 LYS L CA  1 
ATOM   4509 C  C   . LYS C 3 107 ? 47.608  -28.649 16.054  1.00 81.05  ? 107 LYS L C   1 
ATOM   4510 O  O   . LYS C 3 107 ? 47.650  -29.568 16.870  1.00 81.61  ? 107 LYS L O   1 
ATOM   4511 C  CB  . LYS C 3 107 ? 48.129  -26.569 17.370  1.00 83.54  ? 107 LYS L CB  1 
ATOM   4512 C  CG  . LYS C 3 107 ? 47.862  -25.093 17.629  1.00 85.48  ? 107 LYS L CG  1 
ATOM   4513 C  CD  . LYS C 3 107 ? 49.035  -24.349 18.241  1.00 86.85  ? 107 LYS L CD  1 
ATOM   4514 C  CE  . LYS C 3 107 ? 49.401  -24.837 19.626  1.00 87.64  ? 107 LYS L CE  1 
ATOM   4515 N  NZ  . LYS C 3 107 ? 50.494  -24.029 20.218  1.00 89.26  ? 107 LYS L NZ  1 
ATOM   4516 N  N   . ARG C 3 108 ? 47.986  -28.772 14.776  1.00 79.88  ? 108 ARG L N   1 
ATOM   4517 C  CA  . ARG C 3 108 ? 48.565  -29.992 14.235  1.00 79.65  ? 108 ARG L CA  1 
ATOM   4518 C  C   . ARG C 3 108 ? 49.809  -29.630 13.426  1.00 79.74  ? 108 ARG L C   1 
ATOM   4519 O  O   . ARG C 3 108 ? 50.148  -28.454 13.299  1.00 80.31  ? 108 ARG L O   1 
ATOM   4520 C  CB  . ARG C 3 108 ? 47.537  -30.728 13.369  1.00 79.21  ? 108 ARG L CB  1 
ATOM   4521 C  CG  . ARG C 3 108 ? 46.950  -29.885 12.245  1.00 78.26  ? 108 ARG L CG  1 
ATOM   4522 C  CD  . ARG C 3 108 ? 46.484  -30.716 11.063  1.00 78.36  ? 108 ARG L CD  1 
ATOM   4523 N  NE  . ARG C 3 108 ? 47.598  -31.385 10.399  1.00 79.13  ? 108 ARG L NE  1 
ATOM   4524 C  CZ  . ARG C 3 108 ? 47.636  -32.675 10.080  1.00 78.47  ? 108 ARG L CZ  1 
ATOM   4525 N  NH1 . ARG C 3 108 ? 46.589  -33.451 10.297  1.00 78.65  ? 108 ARG L NH1 1 
ATOM   4526 N  NH2 . ARG C 3 108 ? 48.723  -33.182 9.525   1.00 78.70  ? 108 ARG L NH2 1 
ATOM   4527 N  N   . THR C 3 109 ? 50.480  -30.654 12.883  1.00 79.95  ? 109 THR L N   1 
ATOM   4528 C  CA  . THR C 3 109 ? 51.634  -30.456 12.019  1.00 78.61  ? 109 THR L CA  1 
ATOM   4529 C  C   . THR C 3 109 ? 51.167  -29.980 10.644  1.00 76.51  ? 109 THR L C   1 
ATOM   4530 O  O   . THR C 3 109 ? 50.008  -30.164 10.276  1.00 73.93  ? 109 THR L O   1 
ATOM   4531 C  CB  . THR C 3 109 ? 52.483  -31.732 11.923  1.00 79.26  ? 109 THR L CB  1 
ATOM   4532 O  OG1 . THR C 3 109 ? 51.654  -32.800 11.462  1.00 78.59  ? 109 THR L OG1 1 
ATOM   4533 C  CG2 . THR C 3 109 ? 53.117  -32.119 13.241  1.00 79.82  ? 109 THR L CG2 1 
ATOM   4534 N  N   . VAL C 3 110 ? 52.093  -29.365 9.899   1.00 76.50  ? 110 VAL L N   1 
ATOM   4535 C  CA  . VAL C 3 110 ? 51.812  -28.825 8.576   1.00 75.86  ? 110 VAL L CA  1 
ATOM   4536 C  C   . VAL C 3 110 ? 51.479  -29.976 7.626   1.00 74.56  ? 110 VAL L C   1 
ATOM   4537 O  O   . VAL C 3 110 ? 52.058  -31.057 7.727   1.00 75.64  ? 110 VAL L O   1 
ATOM   4538 C  CB  . VAL C 3 110 ? 52.988  -27.964 8.063   1.00 77.91  ? 110 VAL L CB  1 
ATOM   4539 C  CG1 . VAL C 3 110 ? 54.331  -28.673 8.192   1.00 80.61  ? 110 VAL L CG1 1 
ATOM   4540 C  CG2 . VAL C 3 110 ? 52.772  -27.482 6.634   1.00 77.62  ? 110 VAL L CG2 1 
ATOM   4541 N  N   . ALA C 3 111 ? 50.530  -29.732 6.712   1.00 72.04  ? 111 ALA L N   1 
ATOM   4542 C  CA  . ALA C 3 111 ? 50.077  -30.739 5.765   1.00 71.66  ? 111 ALA L CA  1 
ATOM   4543 C  C   . ALA C 3 111 ? 49.727  -30.076 4.435   1.00 70.62  ? 111 ALA L C   1 
ATOM   4544 O  O   . ALA C 3 111 ? 48.903  -29.165 4.398   1.00 69.11  ? 111 ALA L O   1 
ATOM   4545 C  CB  . ALA C 3 111 ? 48.891  -31.480 6.331   1.00 70.86  ? 111 ALA L CB  1 
ATOM   4546 N  N   . ALA C 3 112 ? 50.352  -30.557 3.352   1.00 71.11  ? 112 ALA L N   1 
ATOM   4547 C  CA  . ALA C 3 112 ? 50.167  -29.994 2.024   1.00 70.80  ? 112 ALA L CA  1 
ATOM   4548 C  C   . ALA C 3 112 ? 48.811  -30.415 1.459   1.00 68.71  ? 112 ALA L C   1 
ATOM   4549 O  O   . ALA C 3 112 ? 48.349  -31.523 1.720   1.00 69.02  ? 112 ALA L O   1 
ATOM   4550 C  CB  . ALA C 3 112 ? 51.293  -30.436 1.123   1.00 73.77  ? 112 ALA L CB  1 
ATOM   4551 N  N   . PRO C 3 113 ? 48.137  -29.555 0.660   1.00 67.76  ? 113 PRO L N   1 
ATOM   4552 C  CA  . PRO C 3 113 ? 46.831  -29.887 0.091   1.00 67.37  ? 113 PRO L CA  1 
ATOM   4553 C  C   . PRO C 3 113 ? 46.911  -30.762 -1.156  1.00 68.60  ? 113 PRO L C   1 
ATOM   4554 O  O   . PRO C 3 113 ? 47.779  -30.561 -2.002  1.00 72.06  ? 113 PRO L O   1 
ATOM   4555 C  CB  . PRO C 3 113 ? 46.267  -28.509 -0.288  1.00 66.60  ? 113 PRO L CB  1 
ATOM   4556 C  CG  . PRO C 3 113 ? 47.495  -27.709 -0.659  1.00 68.39  ? 113 PRO L CG  1 
ATOM   4557 C  CD  . PRO C 3 113 ? 48.587  -28.211 0.266   1.00 69.07  ? 113 PRO L CD  1 
ATOM   4558 N  N   . SER C 3 114 ? 45.998  -31.734 -1.248  1.00 68.32  ? 114 SER L N   1 
ATOM   4559 C  CA  . SER C 3 114 ? 45.752  -32.451 -2.488  1.00 69.71  ? 114 SER L CA  1 
ATOM   4560 C  C   . SER C 3 114 ? 44.854  -31.593 -3.374  1.00 68.38  ? 114 SER L C   1 
ATOM   4561 O  O   . SER C 3 114 ? 43.783  -31.173 -2.941  1.00 65.94  ? 114 SER L O   1 
ATOM   4562 C  CB  . SER C 3 114 ? 45.139  -33.803 -2.222  1.00 71.27  ? 114 SER L CB  1 
ATOM   4563 O  OG  . SER C 3 114 ? 45.996  -34.599 -1.416  1.00 73.27  ? 114 SER L OG  1 
ATOM   4564 N  N   . VAL C 3 115 ? 45.303  -31.332 -4.607  1.00 70.00  ? 115 VAL L N   1 
ATOM   4565 C  CA  . VAL C 3 115 ? 44.625  -30.396 -5.489  1.00 70.09  ? 115 VAL L CA  1 
ATOM   4566 C  C   . VAL C 3 115 ? 43.901  -31.176 -6.585  1.00 71.61  ? 115 VAL L C   1 
ATOM   4567 O  O   . VAL C 3 115 ? 44.505  -32.000 -7.268  1.00 73.91  ? 115 VAL L O   1 
ATOM   4568 C  CB  . VAL C 3 115 ? 45.613  -29.368 -6.074  1.00 71.15  ? 115 VAL L CB  1 
ATOM   4569 C  CG1 . VAL C 3 115 ? 44.924  -28.397 -7.022  1.00 71.18  ? 115 VAL L CG1 1 
ATOM   4570 C  CG2 . VAL C 3 115 ? 46.350  -28.617 -4.975  1.00 70.47  ? 115 VAL L CG2 1 
ATOM   4571 N  N   . PHE C 3 116 ? 42.598  -30.902 -6.731  1.00 71.27  ? 116 PHE L N   1 
ATOM   4572 C  CA  . PHE C 3 116 ? 41.767  -31.506 -7.760  1.00 73.03  ? 116 PHE L CA  1 
ATOM   4573 C  C   . PHE C 3 116 ? 41.027  -30.394 -8.499  1.00 72.54  ? 116 PHE L C   1 
ATOM   4574 O  O   . PHE C 3 116 ? 40.726  -29.359 -7.909  1.00 73.78  ? 116 PHE L O   1 
ATOM   4575 C  CB  . PHE C 3 116 ? 40.761  -32.491 -7.151  1.00 74.65  ? 116 PHE L CB  1 
ATOM   4576 C  CG  . PHE C 3 116 ? 41.308  -33.434 -6.107  1.00 76.96  ? 116 PHE L CG  1 
ATOM   4577 C  CD1 . PHE C 3 116 ? 41.581  -32.993 -4.820  1.00 76.80  ? 116 PHE L CD1 1 
ATOM   4578 C  CD2 . PHE C 3 116 ? 41.539  -34.769 -6.403  1.00 79.77  ? 116 PHE L CD2 1 
ATOM   4579 C  CE1 . PHE C 3 116 ? 42.078  -33.862 -3.859  1.00 77.94  ? 116 PHE L CE1 1 
ATOM   4580 C  CE2 . PHE C 3 116 ? 42.037  -35.637 -5.442  1.00 81.46  ? 116 PHE L CE2 1 
ATOM   4581 C  CZ  . PHE C 3 116 ? 42.305  -35.182 -4.172  1.00 80.24  ? 116 PHE L CZ  1 
ATOM   4582 N  N   . ILE C 3 117 ? 40.733  -30.616 -9.786  1.00 72.93  ? 117 ILE L N   1 
ATOM   4583 C  CA  . ILE C 3 117 ? 39.993  -29.645 -10.577 1.00 72.88  ? 117 ILE L CA  1 
ATOM   4584 C  C   . ILE C 3 117 ? 38.884  -30.366 -11.340 1.00 73.05  ? 117 ILE L C   1 
ATOM   4585 O  O   . ILE C 3 117 ? 39.044  -31.520 -11.734 1.00 74.41  ? 117 ILE L O   1 
ATOM   4586 C  CB  . ILE C 3 117 ? 40.926  -28.852 -11.517 1.00 74.62  ? 117 ILE L CB  1 
ATOM   4587 C  CG1 . ILE C 3 117 ? 40.216  -27.639 -12.127 1.00 74.50  ? 117 ILE L CG1 1 
ATOM   4588 C  CG2 . ILE C 3 117 ? 41.524  -29.752 -12.589 1.00 77.57  ? 117 ILE L CG2 1 
ATOM   4589 C  CD1 . ILE C 3 117 ? 41.115  -26.735 -12.939 1.00 76.56  ? 117 ILE L CD1 1 
ATOM   4590 N  N   . PHE C 3 118 ? 37.765  -29.659 -11.541 1.00 72.26  ? 118 PHE L N   1 
ATOM   4591 C  CA  . PHE C 3 118 ? 36.598  -30.206 -12.213 1.00 72.91  ? 118 PHE L CA  1 
ATOM   4592 C  C   . PHE C 3 118 ? 36.134  -29.240 -13.298 1.00 73.19  ? 118 PHE L C   1 
ATOM   4593 O  O   . PHE C 3 118 ? 35.854  -28.080 -13.006 1.00 71.51  ? 118 PHE L O   1 
ATOM   4594 C  CB  . PHE C 3 118 ? 35.455  -30.445 -11.220 1.00 72.12  ? 118 PHE L CB  1 
ATOM   4595 C  CG  . PHE C 3 118 ? 35.813  -31.291 -10.025 1.00 71.53  ? 118 PHE L CG  1 
ATOM   4596 C  CD1 . PHE C 3 118 ? 36.510  -30.753 -8.952  1.00 70.47  ? 118 PHE L CD1 1 
ATOM   4597 C  CD2 . PHE C 3 118 ? 35.463  -32.631 -9.977  1.00 72.49  ? 118 PHE L CD2 1 
ATOM   4598 C  CE1 . PHE C 3 118 ? 36.839  -31.534 -7.855  1.00 70.33  ? 118 PHE L CE1 1 
ATOM   4599 C  CE2 . PHE C 3 118 ? 35.794  -33.410 -8.880  1.00 73.43  ? 118 PHE L CE2 1 
ATOM   4600 C  CZ  . PHE C 3 118 ? 36.482  -32.861 -7.821  1.00 71.79  ? 118 PHE L CZ  1 
ATOM   4601 N  N   . PRO C 3 119 ? 36.023  -29.678 -14.575 1.00 76.39  ? 119 PRO L N   1 
ATOM   4602 C  CA  . PRO C 3 119 ? 35.471  -28.824 -15.629 1.00 77.55  ? 119 PRO L CA  1 
ATOM   4603 C  C   . PRO C 3 119 ? 33.973  -28.580 -15.443 1.00 76.90  ? 119 PRO L C   1 
ATOM   4604 O  O   . PRO C 3 119 ? 33.342  -29.208 -14.596 1.00 75.79  ? 119 PRO L O   1 
ATOM   4605 C  CB  . PRO C 3 119 ? 35.758  -29.605 -16.922 1.00 79.08  ? 119 PRO L CB  1 
ATOM   4606 C  CG  . PRO C 3 119 ? 35.857  -31.050 -16.480 1.00 79.44  ? 119 PRO L CG  1 
ATOM   4607 C  CD  . PRO C 3 119 ? 36.432  -31.000 -15.078 1.00 78.15  ? 119 PRO L CD  1 
ATOM   4608 N  N   . PRO C 3 120 ? 33.361  -27.646 -16.210 1.00 78.64  ? 120 PRO L N   1 
ATOM   4609 C  CA  . PRO C 3 120 ? 31.918  -27.406 -16.136 1.00 79.41  ? 120 PRO L CA  1 
ATOM   4610 C  C   . PRO C 3 120 ? 31.084  -28.597 -16.603 1.00 80.78  ? 120 PRO L C   1 
ATOM   4611 O  O   . PRO C 3 120 ? 31.484  -29.322 -17.511 1.00 80.41  ? 120 PRO L O   1 
ATOM   4612 C  CB  . PRO C 3 120 ? 31.681  -26.215 -17.082 1.00 80.29  ? 120 PRO L CB  1 
ATOM   4613 C  CG  . PRO C 3 120 ? 33.049  -25.588 -17.259 1.00 80.54  ? 120 PRO L CG  1 
ATOM   4614 C  CD  . PRO C 3 120 ? 34.024  -26.742 -17.161 1.00 80.31  ? 120 PRO L CD  1 
ATOM   4615 N  N   . SER C 3 121 ? 29.917  -28.772 -15.971 1.00 82.42  ? 121 SER L N   1 
ATOM   4616 C  CA  . SER C 3 121 ? 28.977  -29.818 -16.339 1.00 84.70  ? 121 SER L CA  1 
ATOM   4617 C  C   . SER C 3 121 ? 28.366  -29.510 -17.704 1.00 87.40  ? 121 SER L C   1 
ATOM   4618 O  O   . SER C 3 121 ? 28.206  -28.346 -18.064 1.00 87.96  ? 121 SER L O   1 
ATOM   4619 C  CB  . SER C 3 121 ? 27.912  -29.968 -15.286 1.00 85.12  ? 121 SER L CB  1 
ATOM   4620 O  OG  . SER C 3 121 ? 26.935  -30.916 -15.687 1.00 88.35  ? 121 SER L OG  1 
ATOM   4621 N  N   . ASP C 3 122 ? 28.018  -30.568 -18.447 1.00 90.72  ? 122 ASP L N   1 
ATOM   4622 C  CA  . ASP C 3 122 ? 27.419  -30.430 -19.767 1.00 93.33  ? 122 ASP L CA  1 
ATOM   4623 C  C   . ASP C 3 122 ? 25.978  -29.942 -19.629 1.00 94.38  ? 122 ASP L C   1 
ATOM   4624 O  O   . ASP C 3 122 ? 25.454  -29.297 -20.534 1.00 94.35  ? 122 ASP L O   1 
ATOM   4625 C  CB  . ASP C 3 122 ? 27.481  -31.746 -20.546 1.00 96.01  ? 122 ASP L CB  1 
ATOM   4626 C  CG  . ASP C 3 122 ? 28.895  -32.259 -20.758 1.00 96.54  ? 122 ASP L CG  1 
ATOM   4627 O  OD1 . ASP C 3 122 ? 29.688  -31.541 -21.400 1.00 95.71  ? 122 ASP L OD1 1 
ATOM   4628 O  OD2 . ASP C 3 122 ? 29.193  -33.368 -20.271 1.00 97.94  ? 122 ASP L OD2 1 
ATOM   4629 N  N   . GLU C 3 123 ? 25.348  -30.269 -18.493 1.00 96.45  ? 123 GLU L N   1 
ATOM   4630 C  CA  . GLU C 3 123 ? 24.021  -29.773 -18.167 1.00 99.06  ? 123 GLU L CA  1 
ATOM   4631 C  C   . GLU C 3 123 ? 24.087  -28.260 -17.960 1.00 97.38  ? 123 GLU L C   1 
ATOM   4632 O  O   . GLU C 3 123 ? 23.207  -27.529 -18.411 1.00 98.55  ? 123 GLU L O   1 
ATOM   4633 C  CB  . GLU C 3 123 ? 23.470  -30.453 -16.909 1.00 101.80 ? 123 GLU L CB  1 
ATOM   4634 C  CG  . GLU C 3 123 ? 23.205  -31.945 -17.057 1.00 104.76 ? 123 GLU L CG  1 
ATOM   4635 C  CD  . GLU C 3 123 ? 24.407  -32.855 -16.856 1.00 104.61 ? 123 GLU L CD  1 
ATOM   4636 O  OE1 . GLU C 3 123 ? 24.449  -33.561 -15.826 1.00 104.02 ? 123 GLU L OE1 1 
ATOM   4637 O  OE2 . GLU C 3 123 ? 25.293  -32.870 -17.735 1.00 103.43 ? 123 GLU L OE2 1 
ATOM   4638 N  N   . GLN C 3 124 ? 25.146  -27.810 -17.275 1.00 94.54  ? 124 GLN L N   1 
ATOM   4639 C  CA  . GLN C 3 124 ? 25.327  -26.408 -16.936 1.00 92.74  ? 124 GLN L CA  1 
ATOM   4640 C  C   . GLN C 3 124 ? 25.608  -25.587 -18.193 1.00 93.99  ? 124 GLN L C   1 
ATOM   4641 O  O   . GLN C 3 124 ? 25.146  -24.455 -18.303 1.00 95.86  ? 124 GLN L O   1 
ATOM   4642 C  CB  . GLN C 3 124 ? 26.470  -26.250 -15.931 1.00 89.07  ? 124 GLN L CB  1 
ATOM   4643 C  CG  . GLN C 3 124 ? 26.564  -24.855 -15.328 1.00 87.70  ? 124 GLN L CG  1 
ATOM   4644 C  CD  . GLN C 3 124 ? 27.760  -24.679 -14.423 1.00 85.16  ? 124 GLN L CD  1 
ATOM   4645 O  OE1 . GLN C 3 124 ? 27.986  -23.607 -13.867 1.00 83.42  ? 124 GLN L OE1 1 
ATOM   4646 N  NE2 . GLN C 3 124 ? 28.543  -25.735 -14.270 1.00 84.07  ? 124 GLN L NE2 1 
ATOM   4647 N  N   . LEU C 3 125 ? 26.375  -26.154 -19.132 1.00 94.84  ? 125 LEU L N   1 
ATOM   4648 C  CA  . LEU C 3 125 ? 26.774  -25.433 -20.332 1.00 96.22  ? 125 LEU L CA  1 
ATOM   4649 C  C   . LEU C 3 125 ? 25.555  -25.118 -21.198 1.00 98.13  ? 125 LEU L C   1 
ATOM   4650 O  O   . LEU C 3 125 ? 25.495  -24.052 -21.807 1.00 99.68  ? 125 LEU L O   1 
ATOM   4651 C  CB  . LEU C 3 125 ? 27.812  -26.257 -21.102 1.00 96.41  ? 125 LEU L CB  1 
ATOM   4652 C  CG  . LEU C 3 125 ? 29.212  -26.292 -20.487 1.00 95.94  ? 125 LEU L CG  1 
ATOM   4653 C  CD1 . LEU C 3 125 ? 30.159  -27.122 -21.340 1.00 96.98  ? 125 LEU L CD1 1 
ATOM   4654 C  CD2 . LEU C 3 125 ? 29.764  -24.886 -20.298 1.00 95.93  ? 125 LEU L CD2 1 
ATOM   4655 N  N   . LYS C 3 126 ? 24.582  -26.037 -21.239 1.00 98.98  ? 126 LYS L N   1 
ATOM   4656 C  CA  . LYS C 3 126 ? 23.358  -25.820 -21.996 1.00 100.43 ? 126 LYS L CA  1 
ATOM   4657 C  C   . LYS C 3 126 ? 22.514  -24.727 -21.341 1.00 99.58  ? 126 LYS L C   1 
ATOM   4658 O  O   . LYS C 3 126 ? 21.685  -24.113 -22.009 1.00 102.14 ? 126 LYS L O   1 
ATOM   4659 C  CB  . LYS C 3 126 ? 22.561  -27.121 -22.151 1.00 102.80 ? 126 LYS L CB  1 
ATOM   4660 C  CG  . LYS C 3 126 ? 22.887  -27.929 -23.402 1.00 104.75 ? 126 LYS L CG  1 
ATOM   4661 C  CD  . LYS C 3 126 ? 22.404  -27.276 -24.688 1.00 106.92 ? 126 LYS L CD  1 
ATOM   4662 C  CE  . LYS C 3 126 ? 22.894  -27.965 -25.945 1.00 107.55 ? 126 LYS L CE  1 
ATOM   4663 N  NZ  . LYS C 3 126 ? 22.315  -29.322 -26.096 1.00 109.42 ? 126 LYS L NZ  1 
ATOM   4664 N  N   . SER C 3 127 ? 22.722  -24.494 -20.038 1.00 96.76  ? 127 SER L N   1 
ATOM   4665 C  CA  . SER C 3 127 ? 22.081  -23.387 -19.345 1.00 97.55  ? 127 SER L CA  1 
ATOM   4666 C  C   . SER C 3 127 ? 22.609  -22.058 -19.883 1.00 96.50  ? 127 SER L C   1 
ATOM   4667 O  O   . SER C 3 127 ? 21.828  -21.202 -20.292 1.00 100.51 ? 127 SER L O   1 
ATOM   4668 C  CB  . SER C 3 127 ? 22.272  -23.487 -17.852 1.00 97.11  ? 127 SER L CB  1 
ATOM   4669 O  OG  . SER C 3 127 ? 21.610  -22.423 -17.184 1.00 99.77  ? 127 SER L OG  1 
ATOM   4670 N  N   . GLY C 3 128 ? 23.940  -21.904 -19.883 1.00 91.87  ? 128 GLY L N   1 
ATOM   4671 C  CA  . GLY C 3 128 ? 24.580  -20.673 -20.318 1.00 90.42  ? 128 GLY L CA  1 
ATOM   4672 C  C   . GLY C 3 128 ? 25.822  -20.343 -19.491 1.00 87.56  ? 128 GLY L C   1 
ATOM   4673 O  O   . GLY C 3 128 ? 26.765  -19.742 -20.002 1.00 87.99  ? 128 GLY L O   1 
ATOM   4674 N  N   . THR C 3 129 ? 25.799  -20.731 -18.210 1.00 84.77  ? 129 THR L N   1 
ATOM   4675 C  CA  . THR C 3 129 ? 26.915  -20.514 -17.303 1.00 82.13  ? 129 THR L CA  1 
ATOM   4676 C  C   . THR C 3 129 ? 27.914  -21.661 -17.452 1.00 78.27  ? 129 THR L C   1 
ATOM   4677 O  O   . THR C 3 129 ? 27.581  -22.713 -17.994 1.00 77.16  ? 129 THR L O   1 
ATOM   4678 C  CB  . THR C 3 129 ? 26.408  -20.370 -15.860 1.00 82.65  ? 129 THR L CB  1 
ATOM   4679 O  OG1 . THR C 3 129 ? 25.367  -19.392 -15.854 1.00 85.15  ? 129 THR L OG1 1 
ATOM   4680 C  CG2 . THR C 3 129 ? 27.486  -19.965 -14.877 1.00 81.52  ? 129 THR L CG2 1 
ATOM   4681 N  N   . ALA C 3 130 ? 29.147  -21.433 -16.985 1.00 76.15  ? 130 ALA L N   1 
ATOM   4682 C  CA  . ALA C 3 130 ? 30.167  -22.467 -16.933 1.00 74.36  ? 130 ALA L CA  1 
ATOM   4683 C  C   . ALA C 3 130 ? 31.042  -22.249 -15.701 1.00 73.45  ? 130 ALA L C   1 
ATOM   4684 O  O   . ALA C 3 130 ? 31.771  -21.262 -15.626 1.00 74.73  ? 130 ALA L O   1 
ATOM   4685 C  CB  . ALA C 3 130 ? 30.981  -22.451 -18.204 1.00 74.31  ? 130 ALA L CB  1 
ATOM   4686 N  N   . SER C 3 131 ? 30.959  -23.181 -14.742 1.00 72.08  ? 131 SER L N   1 
ATOM   4687 C  CA  . SER C 3 131 ? 31.679  -23.074 -13.483 1.00 71.22  ? 131 SER L CA  1 
ATOM   4688 C  C   . SER C 3 131 ? 32.813  -24.094 -13.440 1.00 69.37  ? 131 SER L C   1 
ATOM   4689 O  O   . SER C 3 131 ? 32.584  -25.291 -13.601 1.00 68.98  ? 131 SER L O   1 
ATOM   4690 C  CB  . SER C 3 131 ? 30.748  -23.246 -12.311 1.00 72.17  ? 131 SER L CB  1 
ATOM   4691 O  OG  . SER C 3 131 ? 29.815  -22.178 -12.245 1.00 74.91  ? 131 SER L OG  1 
ATOM   4692 N  N   . VAL C 3 132 ? 34.036  -23.599 -13.218 1.00 68.78  ? 132 VAL L N   1 
ATOM   4693 C  CA  . VAL C 3 132 ? 35.203  -24.447 -13.048 1.00 68.96  ? 132 VAL L CA  1 
ATOM   4694 C  C   . VAL C 3 132 ? 35.550  -24.466 -11.562 1.00 68.46  ? 132 VAL L C   1 
ATOM   4695 O  O   . VAL C 3 132 ? 35.694  -23.411 -10.949 1.00 69.62  ? 132 VAL L O   1 
ATOM   4696 C  CB  . VAL C 3 132 ? 36.382  -23.950 -13.908 1.00 69.93  ? 132 VAL L CB  1 
ATOM   4697 C  CG1 . VAL C 3 132 ? 37.580  -24.886 -13.835 1.00 70.23  ? 132 VAL L CG1 1 
ATOM   4698 C  CG2 . VAL C 3 132 ? 35.965  -23.733 -15.355 1.00 70.98  ? 132 VAL L CG2 1 
ATOM   4699 N  N   . VAL C 3 133 ? 35.678  -25.671 -10.995 1.00 68.26  ? 133 VAL L N   1 
ATOM   4700 C  CA  . VAL C 3 133 ? 35.862  -25.838 -9.563  1.00 67.91  ? 133 VAL L CA  1 
ATOM   4701 C  C   . VAL C 3 133 ? 37.270  -26.359 -9.294  1.00 68.35  ? 133 VAL L C   1 
ATOM   4702 O  O   . VAL C 3 133 ? 37.678  -27.371 -9.857  1.00 68.57  ? 133 VAL L O   1 
ATOM   4703 C  CB  . VAL C 3 133 ? 34.802  -26.786 -8.971  1.00 68.04  ? 133 VAL L CB  1 
ATOM   4704 C  CG1 . VAL C 3 133 ? 35.032  -27.034 -7.486  1.00 67.78  ? 133 VAL L CG1 1 
ATOM   4705 C  CG2 . VAL C 3 133 ? 33.390  -26.276 -9.221  1.00 68.87  ? 133 VAL L CG2 1 
ATOM   4706 N  N   . CYS C 3 134 ? 37.997  -25.645 -8.427  1.00 69.33  ? 134 CYS L N   1 
ATOM   4707 C  CA  . CYS C 3 134 ? 39.241  -26.128 -7.850  1.00 70.68  ? 134 CYS L CA  1 
ATOM   4708 C  C   . CYS C 3 134 ? 38.947  -26.652 -6.445  1.00 71.18  ? 134 CYS L C   1 
ATOM   4709 O  O   . CYS C 3 134 ? 37.999  -26.199 -5.803  1.00 71.60  ? 134 CYS L O   1 
ATOM   4710 C  CB  . CYS C 3 134 ? 40.284  -25.017 -7.814  1.00 71.20  ? 134 CYS L CB  1 
ATOM   4711 S  SG  . CYS C 3 134 ? 41.942  -25.574 -7.338  1.00 72.79  ? 134 CYS L SG  1 
ATOM   4712 N  N   . LEU C 3 135 ? 39.754  -27.614 -5.982  1.00 70.92  ? 135 LEU L N   1 
ATOM   4713 C  CA  . LEU C 3 135 ? 39.548  -28.232 -4.681  1.00 70.49  ? 135 LEU L CA  1 
ATOM   4714 C  C   . LEU C 3 135 ? 40.894  -28.491 -4.012  1.00 70.52  ? 135 LEU L C   1 
ATOM   4715 O  O   . LEU C 3 135 ? 41.669  -29.320 -4.480  1.00 71.05  ? 135 LEU L O   1 
ATOM   4716 C  CB  . LEU C 3 135 ? 38.764  -29.536 -4.868  1.00 72.11  ? 135 LEU L CB  1 
ATOM   4717 C  CG  . LEU C 3 135 ? 38.678  -30.444 -3.639  1.00 73.99  ? 135 LEU L CG  1 
ATOM   4718 C  CD1 . LEU C 3 135 ? 37.972  -29.743 -2.489  1.00 73.67  ? 135 LEU L CD1 1 
ATOM   4719 C  CD2 . LEU C 3 135 ? 37.973  -31.750 -3.975  1.00 75.41  ? 135 LEU L CD2 1 
ATOM   4720 N  N   . LEU C 3 136 ? 41.151  -27.769 -2.915  1.00 70.94  ? 136 LEU L N   1 
ATOM   4721 C  CA  . LEU C 3 136 ? 42.243  -28.085 -2.008  1.00 73.01  ? 136 LEU L CA  1 
ATOM   4722 C  C   . LEU C 3 136 ? 41.674  -28.925 -0.869  1.00 74.20  ? 136 LEU L C   1 
ATOM   4723 O  O   . LEU C 3 136 ? 40.759  -28.481 -0.179  1.00 74.96  ? 136 LEU L O   1 
ATOM   4724 C  CB  . LEU C 3 136 ? 42.866  -26.791 -1.473  1.00 72.74  ? 136 LEU L CB  1 
ATOM   4725 C  CG  . LEU C 3 136 ? 43.672  -25.966 -2.477  1.00 73.58  ? 136 LEU L CG  1 
ATOM   4726 C  CD1 . LEU C 3 136 ? 42.775  -25.371 -3.556  1.00 72.93  ? 136 LEU L CD1 1 
ATOM   4727 C  CD2 . LEU C 3 136 ? 44.447  -24.870 -1.759  1.00 74.22  ? 136 LEU L CD2 1 
ATOM   4728 N  N   . ASN C 3 137 ? 42.219  -30.132 -0.684  1.00 76.07  ? 137 ASN L N   1 
ATOM   4729 C  CA  . ASN C 3 137 ? 41.625  -31.109 0.214   1.00 77.23  ? 137 ASN L CA  1 
ATOM   4730 C  C   . ASN C 3 137 ? 42.609  -31.429 1.337   1.00 77.72  ? 137 ASN L C   1 
ATOM   4731 O  O   . ASN C 3 137 ? 43.743  -31.823 1.073   1.00 77.89  ? 137 ASN L O   1 
ATOM   4732 C  CB  . ASN C 3 137 ? 41.198  -32.367 -0.548  1.00 79.21  ? 137 ASN L CB  1 
ATOM   4733 C  CG  . ASN C 3 137 ? 40.047  -33.100 0.111   1.00 81.29  ? 137 ASN L CG  1 
ATOM   4734 O  OD1 . ASN C 3 137 ? 40.178  -33.610 1.222   1.00 82.91  ? 137 ASN L OD1 1 
ATOM   4735 N  ND2 . ASN C 3 137 ? 38.914  -33.160 -0.570  1.00 81.32  ? 137 ASN L ND2 1 
ATOM   4736 N  N   . ASN C 3 138 ? 42.156  -31.228 2.583   1.00 77.88  ? 138 ASN L N   1 
ATOM   4737 C  CA  . ASN C 3 138 ? 42.850  -31.675 3.782   1.00 79.04  ? 138 ASN L CA  1 
ATOM   4738 C  C   . ASN C 3 138 ? 44.254  -31.077 3.839   1.00 77.81  ? 138 ASN L C   1 
ATOM   4739 O  O   . ASN C 3 138 ? 45.224  -31.722 3.446   1.00 80.31  ? 138 ASN L O   1 
ATOM   4740 C  CB  . ASN C 3 138 ? 42.886  -33.205 3.877   1.00 82.11  ? 138 ASN L CB  1 
ATOM   4741 C  CG  . ASN C 3 138 ? 41.513  -33.828 4.026   1.00 83.99  ? 138 ASN L CG  1 
ATOM   4742 O  OD1 . ASN C 3 138 ? 40.513  -33.127 4.167   1.00 84.13  ? 138 ASN L OD1 1 
ATOM   4743 N  ND2 . ASN C 3 138 ? 41.454  -35.150 4.001   1.00 86.92  ? 138 ASN L ND2 1 
ATOM   4744 N  N   . PHE C 3 139 ? 44.347  -29.842 4.348   1.00 75.70  ? 139 PHE L N   1 
ATOM   4745 C  CA  . PHE C 3 139 ? 45.626  -29.175 4.534   1.00 75.03  ? 139 PHE L CA  1 
ATOM   4746 C  C   . PHE C 3 139 ? 45.622  -28.396 5.847   1.00 74.75  ? 139 PHE L C   1 
ATOM   4747 O  O   . PHE C 3 139 ? 44.579  -28.224 6.475   1.00 72.77  ? 139 PHE L O   1 
ATOM   4748 C  CB  . PHE C 3 139 ? 45.937  -28.246 3.357   1.00 72.87  ? 139 PHE L CB  1 
ATOM   4749 C  CG  . PHE C 3 139 ? 44.907  -27.175 3.101   1.00 70.78  ? 139 PHE L CG  1 
ATOM   4750 C  CD1 . PHE C 3 139 ? 43.814  -27.416 2.281   1.00 70.00  ? 139 PHE L CD1 1 
ATOM   4751 C  CD2 . PHE C 3 139 ? 45.047  -25.913 3.658   1.00 69.80  ? 139 PHE L CD2 1 
ATOM   4752 C  CE1 . PHE C 3 139 ? 42.873  -26.424 2.044   1.00 68.76  ? 139 PHE L CE1 1 
ATOM   4753 C  CE2 . PHE C 3 139 ? 44.102  -24.925 3.425   1.00 68.78  ? 139 PHE L CE2 1 
ATOM   4754 C  CZ  . PHE C 3 139 ? 43.019  -25.181 2.616   1.00 68.37  ? 139 PHE L CZ  1 
ATOM   4755 N  N   . TYR C 3 140 ? 46.813  -27.936 6.242   1.00 76.77  ? 140 TYR L N   1 
ATOM   4756 C  CA  . TYR C 3 140 ? 46.995  -27.118 7.430   1.00 78.46  ? 140 TYR L CA  1 
ATOM   4757 C  C   . TYR C 3 140 ? 48.349  -26.418 7.329   1.00 80.11  ? 140 TYR L C   1 
ATOM   4758 O  O   . TYR C 3 140 ? 49.336  -27.061 6.981   1.00 82.43  ? 140 TYR L O   1 
ATOM   4759 C  CB  . TYR C 3 140 ? 46.891  -27.982 8.692   1.00 79.92  ? 140 TYR L CB  1 
ATOM   4760 C  CG  . TYR C 3 140 ? 47.063  -27.236 9.992   1.00 80.86  ? 140 TYR L CG  1 
ATOM   4761 C  CD1 . TYR C 3 140 ? 48.317  -26.856 10.445  1.00 81.15  ? 140 TYR L CD1 1 
ATOM   4762 C  CD2 . TYR C 3 140 ? 45.965  -26.891 10.765  1.00 81.14  ? 140 TYR L CD2 1 
ATOM   4763 C  CE1 . TYR C 3 140 ? 48.478  -26.165 11.636  1.00 81.26  ? 140 TYR L CE1 1 
ATOM   4764 C  CE2 . TYR C 3 140 ? 46.107  -26.198 11.956  1.00 81.69  ? 140 TYR L CE2 1 
ATOM   4765 C  CZ  . TYR C 3 140 ? 47.369  -25.833 12.393  1.00 81.92  ? 140 TYR L CZ  1 
ATOM   4766 O  OH  . TYR C 3 140 ? 47.518  -25.149 13.574  1.00 84.00  ? 140 TYR L OH  1 
ATOM   4767 N  N   . PRO C 3 141 ? 48.469  -25.105 7.642   1.00 80.75  ? 141 PRO L N   1 
ATOM   4768 C  CA  . PRO C 3 141 ? 47.374  -24.301 8.192   1.00 80.50  ? 141 PRO L CA  1 
ATOM   4769 C  C   . PRO C 3 141 ? 46.412  -23.744 7.143   1.00 79.95  ? 141 PRO L C   1 
ATOM   4770 O  O   . PRO C 3 141 ? 46.529  -24.049 5.958   1.00 79.74  ? 141 PRO L O   1 
ATOM   4771 C  CB  . PRO C 3 141 ? 48.144  -23.177 8.904   1.00 81.47  ? 141 PRO L CB  1 
ATOM   4772 C  CG  . PRO C 3 141 ? 49.354  -22.952 8.029   1.00 82.21  ? 141 PRO L CG  1 
ATOM   4773 C  CD  . PRO C 3 141 ? 49.705  -24.322 7.485   1.00 81.98  ? 141 PRO L CD  1 
ATOM   4774 N  N   . ARG C 3 142 ? 45.465  -22.921 7.612   1.00 80.57  ? 142 ARG L N   1 
ATOM   4775 C  CA  . ARG C 3 142 ? 44.362  -22.410 6.812   1.00 80.83  ? 142 ARG L CA  1 
ATOM   4776 C  C   . ARG C 3 142 ? 44.866  -21.582 5.630   1.00 79.45  ? 142 ARG L C   1 
ATOM   4777 O  O   . ARG C 3 142 ? 44.262  -21.610 4.560   1.00 78.44  ? 142 ARG L O   1 
ATOM   4778 C  CB  . ARG C 3 142 ? 43.454  -21.559 7.706   1.00 83.52  ? 142 ARG L CB  1 
ATOM   4779 C  CG  . ARG C 3 142 ? 42.151  -21.110 7.058   1.00 85.93  ? 142 ARG L CG  1 
ATOM   4780 C  CD  . ARG C 3 142 ? 41.425  -20.109 7.937   1.00 89.87  ? 142 ARG L CD  1 
ATOM   4781 N  NE  . ARG C 3 142 ? 41.145  -20.642 9.265   1.00 92.41  ? 142 ARG L NE  1 
ATOM   4782 C  CZ  . ARG C 3 142 ? 40.871  -19.904 10.336  1.00 95.50  ? 142 ARG L CZ  1 
ATOM   4783 N  NH1 . ARG C 3 142 ? 40.853  -18.585 10.250  1.00 98.59  ? 142 ARG L NH1 1 
ATOM   4784 N  NH2 . ARG C 3 142 ? 40.629  -20.490 11.497  1.00 97.42  ? 142 ARG L NH2 1 
ATOM   4785 N  N   . GLU C 3 143 ? 45.963  -20.842 5.833   1.00 79.57  ? 143 GLU L N   1 
ATOM   4786 C  CA  . GLU C 3 143 ? 46.445  -19.880 4.854   1.00 80.14  ? 143 GLU L CA  1 
ATOM   4787 C  C   . GLU C 3 143 ? 46.855  -20.609 3.575   1.00 79.57  ? 143 GLU L C   1 
ATOM   4788 O  O   . GLU C 3 143 ? 47.865  -21.309 3.561   1.00 81.38  ? 143 GLU L O   1 
ATOM   4789 C  CB  . GLU C 3 143 ? 47.625  -19.082 5.414   1.00 81.90  ? 143 GLU L CB  1 
ATOM   4790 C  CG  . GLU C 3 143 ? 47.275  -18.203 6.605   1.00 83.41  ? 143 GLU L CG  1 
ATOM   4791 C  CD  . GLU C 3 143 ? 47.156  -18.927 7.936   1.00 83.76  ? 143 GLU L CD  1 
ATOM   4792 O  OE1 . GLU C 3 143 ? 48.135  -19.592 8.337   1.00 83.76  ? 143 GLU L OE1 1 
ATOM   4793 O  OE2 . GLU C 3 143 ? 46.087  -18.825 8.570   1.00 84.29  ? 143 GLU L OE2 1 
ATOM   4794 N  N   . ALA C 3 144 ? 46.062  -20.432 2.509   1.00 78.26  ? 144 ALA L N   1 
ATOM   4795 C  CA  . ALA C 3 144 ? 46.302  -21.095 1.236   1.00 78.10  ? 144 ALA L CA  1 
ATOM   4796 C  C   . ALA C 3 144 ? 45.897  -20.174 0.088   1.00 80.90  ? 144 ALA L C   1 
ATOM   4797 O  O   . ALA C 3 144 ? 44.793  -19.634 0.088   1.00 82.71  ? 144 ALA L O   1 
ATOM   4798 C  CB  . ALA C 3 144 ? 45.542  -22.397 1.185   1.00 75.96  ? 144 ALA L CB  1 
ATOM   4799 N  N   . LYS C 3 145 ? 46.799  -20.017 -0.891  1.00 83.39  ? 145 LYS L N   1 
ATOM   4800 C  CA  . LYS C 3 145 ? 46.590  -19.124 -2.019  1.00 84.61  ? 145 LYS L CA  1 
ATOM   4801 C  C   . LYS C 3 145 ? 46.098  -19.931 -3.219  1.00 82.24  ? 145 LYS L C   1 
ATOM   4802 O  O   . LYS C 3 145 ? 46.548  -21.053 -3.438  1.00 81.34  ? 145 LYS L O   1 
ATOM   4803 C  CB  . LYS C 3 145 ? 47.893  -18.394 -2.362  1.00 88.85  ? 145 LYS L CB  1 
ATOM   4804 C  CG  . LYS C 3 145 ? 47.754  -17.179 -3.273  1.00 92.25  ? 145 LYS L CG  1 
ATOM   4805 C  CD  . LYS C 3 145 ? 47.129  -15.974 -2.592  1.00 94.06  ? 145 LYS L CD  1 
ATOM   4806 C  CE  . LYS C 3 145 ? 47.156  -14.722 -3.445  1.00 96.71  ? 145 LYS L CE  1 
ATOM   4807 N  NZ  . LYS C 3 145 ? 46.325  -14.862 -4.665  1.00 96.27  ? 145 LYS L NZ  1 
ATOM   4808 N  N   . VAL C 3 146 ? 45.173  -19.341 -3.985  1.00 82.18  ? 146 VAL L N   1 
ATOM   4809 C  CA  . VAL C 3 146 ? 44.674  -19.932 -5.217  1.00 82.36  ? 146 VAL L CA  1 
ATOM   4810 C  C   . VAL C 3 146 ? 44.694  -18.858 -6.301  1.00 85.50  ? 146 VAL L C   1 
ATOM   4811 O  O   . VAL C 3 146 ? 44.313  -17.716 -6.048  1.00 87.70  ? 146 VAL L O   1 
ATOM   4812 C  CB  . VAL C 3 146 ? 43.258  -20.514 -5.035  1.00 80.47  ? 146 VAL L CB  1 
ATOM   4813 C  CG1 . VAL C 3 146 ? 42.666  -20.995 -6.354  1.00 79.49  ? 146 VAL L CG1 1 
ATOM   4814 C  CG2 . VAL C 3 146 ? 43.235  -21.624 -3.996  1.00 79.84  ? 146 VAL L CG2 1 
ATOM   4815 N  N   . GLN C 3 147 ? 45.138  -19.239 -7.505  1.00 86.40  ? 147 GLN L N   1 
ATOM   4816 C  CA  . GLN C 3 147 ? 45.150  -18.338 -8.645  1.00 87.98  ? 147 GLN L CA  1 
ATOM   4817 C  C   . GLN C 3 147 ? 44.641  -19.077 -9.877  1.00 85.10  ? 147 GLN L C   1 
ATOM   4818 O  O   . GLN C 3 147 ? 45.199  -20.102 -10.257 1.00 85.21  ? 147 GLN L O   1 
ATOM   4819 C  CB  . GLN C 3 147 ? 46.559  -17.800 -8.902  1.00 92.98  ? 147 GLN L CB  1 
ATOM   4820 C  CG  . GLN C 3 147 ? 47.122  -16.987 -7.746  1.00 95.38  ? 147 GLN L CG  1 
ATOM   4821 C  CD  . GLN C 3 147 ? 48.435  -16.326 -8.087  1.00 99.82  ? 147 GLN L CD  1 
ATOM   4822 O  OE1 . GLN C 3 147 ? 48.904  -16.372 -9.223  1.00 102.62 ? 147 GLN L OE1 1 
ATOM   4823 N  NE2 . GLN C 3 147 ? 49.039  -15.693 -7.095  1.00 101.95 ? 147 GLN L NE2 1 
ATOM   4824 N  N   . TRP C 3 148 ? 43.578  -18.539 -10.486 1.00 83.84  ? 148 TRP L N   1 
ATOM   4825 C  CA  . TRP C 3 148 ? 43.040  -19.064 -11.729 1.00 82.99  ? 148 TRP L CA  1 
ATOM   4826 C  C   . TRP C 3 148 ? 43.817  -18.480 -12.905 1.00 83.14  ? 148 TRP L C   1 
ATOM   4827 O  O   . TRP C 3 148 ? 44.059  -17.276 -12.949 1.00 85.02  ? 148 TRP L O   1 
ATOM   4828 C  CB  . TRP C 3 148 ? 41.543  -18.750 -11.836 1.00 83.26  ? 148 TRP L CB  1 
ATOM   4829 C  CG  . TRP C 3 148 ? 40.690  -19.560 -10.910 1.00 82.67  ? 148 TRP L CG  1 
ATOM   4830 C  CD1 . TRP C 3 148 ? 40.177  -19.168 -9.707  1.00 82.47  ? 148 TRP L CD1 1 
ATOM   4831 C  CD2 . TRP C 3 148 ? 40.227  -20.906 -11.122 1.00 81.95  ? 148 TRP L CD2 1 
ATOM   4832 N  NE1 . TRP C 3 148 ? 39.440  -20.179 -9.152  1.00 81.58  ? 148 TRP L NE1 1 
ATOM   4833 C  CE2 . TRP C 3 148 ? 39.449  -21.256 -9.998  1.00 81.32  ? 148 TRP L CE2 1 
ATOM   4834 C  CE3 . TRP C 3 148 ? 40.393  -21.846 -12.147 1.00 81.77  ? 148 TRP L CE3 1 
ATOM   4835 C  CZ2 . TRP C 3 148 ? 38.842  -22.506 -9.874  1.00 80.77  ? 148 TRP L CZ2 1 
ATOM   4836 C  CZ3 . TRP C 3 148 ? 39.794  -23.081 -12.022 1.00 80.94  ? 148 TRP L CZ3 1 
ATOM   4837 C  CH2 . TRP C 3 148 ? 39.029  -23.404 -10.900 1.00 80.13  ? 148 TRP L CH2 1 
ATOM   4838 N  N   . LYS C 3 149 ? 44.203  -19.350 -13.847 1.00 82.27  ? 149 LYS L N   1 
ATOM   4839 C  CA  . LYS C 3 149 ? 44.855  -18.932 -15.078 1.00 83.25  ? 149 LYS L CA  1 
ATOM   4840 C  C   . LYS C 3 149 ? 44.090  -19.506 -16.268 1.00 81.79  ? 149 LYS L C   1 
ATOM   4841 O  O   . LYS C 3 149 ? 43.805  -20.700 -16.303 1.00 81.44  ? 149 LYS L O   1 
ATOM   4842 C  CB  . LYS C 3 149 ? 46.316  -19.394 -15.105 1.00 84.66  ? 149 LYS L CB  1 
ATOM   4843 C  CG  . LYS C 3 149 ? 47.223  -18.746 -14.067 1.00 86.00  ? 149 LYS L CG  1 
ATOM   4844 C  CD  . LYS C 3 149 ? 48.698  -18.962 -14.346 1.00 88.70  ? 149 LYS L CD  1 
ATOM   4845 C  CE  . LYS C 3 149 ? 49.602  -18.293 -13.331 1.00 90.46  ? 149 LYS L CE  1 
ATOM   4846 N  NZ  . LYS C 3 149 ? 49.461  -18.902 -11.984 1.00 89.70  ? 149 LYS L NZ  1 
ATOM   4847 N  N   . VAL C 3 150 ? 43.766  -18.638 -17.234 1.00 82.19  ? 150 VAL L N   1 
ATOM   4848 C  CA  . VAL C 3 150 ? 43.078  -19.041 -18.449 1.00 82.72  ? 150 VAL L CA  1 
ATOM   4849 C  C   . VAL C 3 150 ? 43.980  -18.718 -19.639 1.00 84.92  ? 150 VAL L C   1 
ATOM   4850 O  O   . VAL C 3 150 ? 44.116  -17.554 -20.014 1.00 86.00  ? 150 VAL L O   1 
ATOM   4851 C  CB  . VAL C 3 150 ? 41.702  -18.357 -18.561 1.00 82.79  ? 150 VAL L CB  1 
ATOM   4852 C  CG1 . VAL C 3 150 ? 41.024  -18.652 -19.890 1.00 83.90  ? 150 VAL L CG1 1 
ATOM   4853 C  CG2 . VAL C 3 150 ? 40.792  -18.739 -17.403 1.00 81.20  ? 150 VAL L CG2 1 
ATOM   4854 N  N   . ASP C 3 151 ? 44.579  -19.768 -20.220 1.00 85.30  ? 151 ASP L N   1 
ATOM   4855 C  CA  . ASP C 3 151 ? 45.641  -19.653 -21.210 1.00 87.49  ? 151 ASP L CA  1 
ATOM   4856 C  C   . ASP C 3 151 ? 46.854  -18.969 -20.579 1.00 88.32  ? 151 ASP L C   1 
ATOM   4857 O  O   . ASP C 3 151 ? 47.513  -18.154 -21.221 1.00 89.19  ? 151 ASP L O   1 
ATOM   4858 C  CB  . ASP C 3 151 ? 45.175  -18.934 -22.482 1.00 88.51  ? 151 ASP L CB  1 
ATOM   4859 C  CG  . ASP C 3 151 ? 44.039  -19.636 -23.206 1.00 88.12  ? 151 ASP L CG  1 
ATOM   4860 O  OD1 . ASP C 3 151 ? 44.193  -20.834 -23.514 1.00 88.25  ? 151 ASP L OD1 1 
ATOM   4861 O  OD2 . ASP C 3 151 ? 43.019  -18.974 -23.472 1.00 88.02  ? 151 ASP L OD2 1 
ATOM   4862 N  N   . ASN C 3 152 ? 47.131  -19.319 -19.315 1.00 87.76  ? 152 ASN L N   1 
ATOM   4863 C  CA  . ASN C 3 152 ? 48.270  -18.801 -18.569 1.00 89.25  ? 152 ASN L CA  1 
ATOM   4864 C  C   . ASN C 3 152 ? 48.071  -17.312 -18.274 1.00 89.55  ? 152 ASN L C   1 
ATOM   4865 O  O   . ASN C 3 152 ? 49.038  -16.602 -18.003 1.00 91.00  ? 152 ASN L O   1 
ATOM   4866 C  CB  . ASN C 3 152 ? 49.587  -19.075 -19.307 1.00 92.35  ? 152 ASN L CB  1 
ATOM   4867 C  CG  . ASN C 3 152 ? 50.805  -19.091 -18.405 1.00 93.93  ? 152 ASN L CG  1 
ATOM   4868 O  OD1 . ASN C 3 152 ? 50.689  -19.025 -17.183 1.00 93.28  ? 152 ASN L OD1 1 
ATOM   4869 N  ND2 . ASN C 3 152 ? 51.982  -19.190 -19.001 1.00 96.13  ? 152 ASN L ND2 1 
ATOM   4870 N  N   . ALA C 3 153 ? 46.811  -16.854 -18.302 1.00 88.45  ? 153 ALA L N   1 
ATOM   4871 C  CA  . ALA C 3 153 ? 46.475  -15.456 -18.079 1.00 89.33  ? 153 ALA L CA  1 
ATOM   4872 C  C   . ALA C 3 153 ? 45.738  -15.325 -16.747 1.00 87.82  ? 153 ALA L C   1 
ATOM   4873 O  O   . ALA C 3 153 ? 44.624  -15.826 -16.602 1.00 85.87  ? 153 ALA L O   1 
ATOM   4874 C  CB  . ALA C 3 153 ? 45.647  -14.933 -19.229 1.00 89.57  ? 153 ALA L CB  1 
ATOM   4875 N  N   . LEU C 3 154 ? 46.370  -14.633 -15.791 1.00 88.39  ? 154 LEU L N   1 
ATOM   4876 C  CA  . LEU C 3 154 ? 45.923  -14.622 -14.406 1.00 86.95  ? 154 LEU L CA  1 
ATOM   4877 C  C   . LEU C 3 154 ? 44.580  -13.897 -14.314 1.00 86.64  ? 154 LEU L C   1 
ATOM   4878 O  O   . LEU C 3 154 ? 44.492  -12.705 -14.601 1.00 88.33  ? 154 LEU L O   1 
ATOM   4879 C  CB  . LEU C 3 154 ? 46.998  -13.948 -13.544 1.00 88.74  ? 154 LEU L CB  1 
ATOM   4880 C  CG  . LEU C 3 154 ? 47.126  -14.457 -12.107 1.00 88.90  ? 154 LEU L CG  1 
ATOM   4881 C  CD1 . LEU C 3 154 ? 48.161  -13.645 -11.342 1.00 91.30  ? 154 LEU L CD1 1 
ATOM   4882 C  CD2 . LEU C 3 154 ? 45.790  -14.430 -11.378 1.00 87.03  ? 154 LEU L CD2 1 
ATOM   4883 N  N   . GLN C 3 155 ? 43.537  -14.640 -13.919 1.00 85.21  ? 155 GLN L N   1 
ATOM   4884 C  CA  . GLN C 3 155 ? 42.184  -14.111 -13.835 1.00 85.35  ? 155 GLN L CA  1 
ATOM   4885 C  C   . GLN C 3 155 ? 42.031  -13.289 -12.558 1.00 86.31  ? 155 GLN L C   1 
ATOM   4886 O  O   . GLN C 3 155 ? 42.810  -13.440 -11.618 1.00 84.99  ? 155 GLN L O   1 
ATOM   4887 C  CB  . GLN C 3 155 ? 41.160  -15.248 -13.866 1.00 83.41  ? 155 GLN L CB  1 
ATOM   4888 C  CG  . GLN C 3 155 ? 41.114  -15.993 -15.191 1.00 83.54  ? 155 GLN L CG  1 
ATOM   4889 C  CD  . GLN C 3 155 ? 40.634  -15.116 -16.322 1.00 85.84  ? 155 GLN L CD  1 
ATOM   4890 O  OE1 . GLN C 3 155 ? 39.503  -14.635 -16.322 1.00 86.35  ? 155 GLN L OE1 1 
ATOM   4891 N  NE2 . GLN C 3 155 ? 41.499  -14.898 -17.299 1.00 87.47  ? 155 GLN L NE2 1 
ATOM   4892 N  N   . SER C 3 156 ? 41.006  -12.429 -12.540 1.00 88.22  ? 156 SER L N   1 
ATOM   4893 C  CA  . SER C 3 156 ? 40.810  -11.486 -11.453 1.00 90.10  ? 156 SER L CA  1 
ATOM   4894 C  C   . SER C 3 156 ? 39.356  -11.018 -11.407 1.00 91.26  ? 156 SER L C   1 
ATOM   4895 O  O   . SER C 3 156 ? 38.919  -10.259 -12.271 1.00 93.49  ? 156 SER L O   1 
ATOM   4896 C  CB  . SER C 3 156 ? 41.754  -10.319 -11.593 1.00 92.91  ? 156 SER L CB  1 
ATOM   4897 O  OG  . SER C 3 156 ? 41.574  -9.390  -10.535 1.00 95.58  ? 156 SER L OG  1 
ATOM   4898 N  N   . GLY C 3 157 ? 38.620  -11.492 -10.394 1.00 90.57  ? 157 GLY L N   1 
ATOM   4899 C  CA  . GLY C 3 157 ? 37.317  -10.947 -10.043 1.00 91.29  ? 157 GLY L CA  1 
ATOM   4900 C  C   . GLY C 3 157 ? 36.149  -11.700 -10.680 1.00 90.01  ? 157 GLY L C   1 
ATOM   4901 O  O   . GLY C 3 157 ? 35.125  -11.091 -10.988 1.00 92.07  ? 157 GLY L O   1 
ATOM   4902 N  N   . ASN C 3 158 ? 36.300  -13.021 -10.853 1.00 86.72  ? 158 ASN L N   1 
ATOM   4903 C  CA  . ASN C 3 158 ? 35.250  -13.854 -11.422 1.00 84.43  ? 158 ASN L CA  1 
ATOM   4904 C  C   . ASN C 3 158 ? 35.240  -15.222 -10.736 1.00 80.24  ? 158 ASN L C   1 
ATOM   4905 O  O   . ASN C 3 158 ? 34.899  -16.226 -11.359 1.00 77.70  ? 158 ASN L O   1 
ATOM   4906 C  CB  . ASN C 3 158 ? 35.399  -13.974 -12.943 1.00 85.45  ? 158 ASN L CB  1 
ATOM   4907 C  CG  . ASN C 3 158 ? 36.771  -14.444 -13.386 1.00 85.36  ? 158 ASN L CG  1 
ATOM   4908 O  OD1 . ASN C 3 158 ? 37.652  -14.690 -12.564 1.00 84.91  ? 158 ASN L OD1 1 
ATOM   4909 N  ND2 . ASN C 3 158 ? 36.965  -14.565 -14.689 1.00 85.00  ? 158 ASN L ND2 1 
ATOM   4910 N  N   . SER C 3 159 ? 35.589  -15.243 -9.442  1.00 78.41  ? 159 SER L N   1 
ATOM   4911 C  CA  . SER C 3 159 ? 35.675  -16.480 -8.680  1.00 75.43  ? 159 SER L CA  1 
ATOM   4912 C  C   . SER C 3 159 ? 35.433  -16.205 -7.198  1.00 75.44  ? 159 SER L C   1 
ATOM   4913 O  O   . SER C 3 159 ? 35.589  -15.075 -6.739  1.00 76.56  ? 159 SER L O   1 
ATOM   4914 C  CB  . SER C 3 159 ? 37.003  -17.158 -8.899  1.00 73.60  ? 159 SER L CB  1 
ATOM   4915 O  OG  . SER C 3 159 ? 38.072  -16.351 -8.427  1.00 73.57  ? 159 SER L OG  1 
ATOM   4916 N  N   . GLN C 3 160 ? 35.052  -17.260 -6.464  1.00 73.75  ? 160 GLN L N   1 
ATOM   4917 C  CA  . GLN C 3 160 ? 34.751  -17.165 -5.043  1.00 73.73  ? 160 GLN L CA  1 
ATOM   4918 C  C   . GLN C 3 160 ? 35.343  -18.371 -4.318  1.00 71.19  ? 160 GLN L C   1 
ATOM   4919 O  O   . GLN C 3 160 ? 35.255  -19.492 -4.811  1.00 69.15  ? 160 GLN L O   1 
ATOM   4920 C  CB  . GLN C 3 160 ? 33.238  -17.109 -4.814  1.00 74.82  ? 160 GLN L CB  1 
ATOM   4921 C  CG  . GLN C 3 160 ? 32.525  -16.057 -5.653  1.00 76.71  ? 160 GLN L CG  1 
ATOM   4922 C  CD  . GLN C 3 160 ? 31.069  -15.918 -5.283  1.00 77.68  ? 160 GLN L CD  1 
ATOM   4923 O  OE1 . GLN C 3 160 ? 30.179  -16.372 -6.000  1.00 77.72  ? 160 GLN L OE1 1 
ATOM   4924 N  NE2 . GLN C 3 160 ? 30.814  -15.294 -4.145  1.00 78.83  ? 160 GLN L NE2 1 
ATOM   4925 N  N   . GLU C 3 161 ? 35.936  -18.124 -3.142  1.00 71.64  ? 161 GLU L N   1 
ATOM   4926 C  CA  . GLU C 3 161 ? 36.498  -19.177 -2.310  1.00 70.82  ? 161 GLU L CA  1 
ATOM   4927 C  C   . GLU C 3 161 ? 35.529  -19.526 -1.186  1.00 69.92  ? 161 GLU L C   1 
ATOM   4928 O  O   . GLU C 3 161 ? 34.615  -18.762 -0.889  1.00 71.60  ? 161 GLU L O   1 
ATOM   4929 C  CB  . GLU C 3 161 ? 37.827  -18.741 -1.690  1.00 71.98  ? 161 GLU L CB  1 
ATOM   4930 C  CG  . GLU C 3 161 ? 38.993  -18.755 -2.656  1.00 72.94  ? 161 GLU L CG  1 
ATOM   4931 C  CD  . GLU C 3 161 ? 40.342  -18.522 -1.996  1.00 74.93  ? 161 GLU L CD  1 
ATOM   4932 O  OE1 . GLU C 3 161 ? 41.367  -18.625 -2.701  1.00 76.67  ? 161 GLU L OE1 1 
ATOM   4933 O  OE2 . GLU C 3 161 ? 40.366  -18.243 -0.779  1.00 75.11  ? 161 GLU L OE2 1 
ATOM   4934 N  N   . SER C 3 162 ? 35.763  -20.686 -0.561  1.00 69.12  ? 162 SER L N   1 
ATOM   4935 C  CA  . SER C 3 162 ? 35.061  -21.086 0.648   1.00 69.32  ? 162 SER L CA  1 
ATOM   4936 C  C   . SER C 3 162 ? 35.868  -22.159 1.374   1.00 67.74  ? 162 SER L C   1 
ATOM   4937 O  O   . SER C 3 162 ? 36.089  -23.237 0.829   1.00 67.25  ? 162 SER L O   1 
ATOM   4938 C  CB  . SER C 3 162 ? 33.671  -21.570 0.337   1.00 69.87  ? 162 SER L CB  1 
ATOM   4939 O  OG  . SER C 3 162 ? 32.997  -21.951 1.528   1.00 70.63  ? 162 SER L OG  1 
ATOM   4940 N  N   . VAL C 3 163 ? 36.305  -21.848 2.601   1.00 68.43  ? 163 VAL L N   1 
ATOM   4941 C  CA  . VAL C 3 163 ? 37.054  -22.787 3.422   1.00 69.18  ? 163 VAL L CA  1 
ATOM   4942 C  C   . VAL C 3 163 ? 36.079  -23.506 4.353   1.00 71.58  ? 163 VAL L C   1 
ATOM   4943 O  O   . VAL C 3 163 ? 35.082  -22.926 4.780   1.00 73.69  ? 163 VAL L O   1 
ATOM   4944 C  CB  . VAL C 3 163 ? 38.177  -22.085 4.214   1.00 69.27  ? 163 VAL L CB  1 
ATOM   4945 C  CG1 . VAL C 3 163 ? 37.639  -21.219 5.345   1.00 71.17  ? 163 VAL L CG1 1 
ATOM   4946 C  CG2 . VAL C 3 163 ? 39.193  -23.081 4.753   1.00 68.20  ? 163 VAL L CG2 1 
ATOM   4947 N  N   . THR C 3 164 ? 36.382  -24.773 4.661   1.00 72.27  ? 164 THR L N   1 
ATOM   4948 C  CA  . THR C 3 164 ? 35.605  -25.545 5.616   1.00 72.94  ? 164 THR L CA  1 
ATOM   4949 C  C   . THR C 3 164 ? 36.050  -25.209 7.035   1.00 74.20  ? 164 THR L C   1 
ATOM   4950 O  O   . THR C 3 164 ? 37.102  -24.606 7.243   1.00 73.91  ? 164 THR L O   1 
ATOM   4951 C  CB  . THR C 3 164 ? 35.751  -27.054 5.378   1.00 72.23  ? 164 THR L CB  1 
ATOM   4952 O  OG1 . THR C 3 164 ? 37.138  -27.389 5.458   1.00 70.32  ? 164 THR L OG1 1 
ATOM   4953 C  CG2 . THR C 3 164 ? 35.193  -27.500 4.045   1.00 71.79  ? 164 THR L CG2 1 
ATOM   4954 N  N   . GLU C 3 165 ? 35.228  -25.615 8.006   1.00 76.45  ? 165 GLU L N   1 
ATOM   4955 C  CA  . GLU C 3 165 ? 35.617  -25.601 9.406   1.00 78.74  ? 165 GLU L CA  1 
ATOM   4956 C  C   . GLU C 3 165 ? 36.701  -26.658 9.614   1.00 77.15  ? 165 GLU L C   1 
ATOM   4957 O  O   . GLU C 3 165 ? 36.963  -27.466 8.725   1.00 78.06  ? 165 GLU L O   1 
ATOM   4958 C  CB  . GLU C 3 165 ? 34.401  -25.824 10.313  1.00 82.01  ? 165 GLU L CB  1 
ATOM   4959 C  CG  . GLU C 3 165 ? 33.775  -27.211 10.212  1.00 84.07  ? 165 GLU L CG  1 
ATOM   4960 C  CD  . GLU C 3 165 ? 32.938  -27.503 8.976   1.00 85.28  ? 165 GLU L CD  1 
ATOM   4961 O  OE1 . GLU C 3 165 ? 32.817  -26.612 8.108   1.00 85.76  ? 165 GLU L OE1 1 
ATOM   4962 O  OE2 . GLU C 3 165 ? 32.401  -28.628 8.886   1.00 86.01  ? 165 GLU L OE2 1 
ATOM   4963 N  N   . GLN C 3 166 ? 37.330  -26.635 10.793  1.00 76.25  ? 166 GLN L N   1 
ATOM   4964 C  CA  . GLN C 3 166 ? 38.423  -27.543 11.099  1.00 75.19  ? 166 GLN L CA  1 
ATOM   4965 C  C   . GLN C 3 166 ? 37.858  -28.950 11.291  1.00 75.99  ? 166 GLN L C   1 
ATOM   4966 O  O   . GLN C 3 166 ? 36.827  -29.119 11.939  1.00 77.26  ? 166 GLN L O   1 
ATOM   4967 C  CB  . GLN C 3 166 ? 39.176  -27.054 12.337  1.00 75.12  ? 166 GLN L CB  1 
ATOM   4968 C  CG  . GLN C 3 166 ? 40.563  -27.660 12.484  1.00 74.86  ? 166 GLN L CG  1 
ATOM   4969 C  CD  . GLN C 3 166 ? 41.368  -26.995 13.573  1.00 75.91  ? 166 GLN L CD  1 
ATOM   4970 O  OE1 . GLN C 3 166 ? 40.852  -26.213 14.368  1.00 77.09  ? 166 GLN L OE1 1 
ATOM   4971 N  NE2 . GLN C 3 166 ? 42.652  -27.307 13.619  1.00 76.47  ? 166 GLN L NE2 1 
ATOM   4972 N  N   . ASP C 3 167 ? 38.540  -29.948 10.712  1.00 75.62  ? 167 ASP L N   1 
ATOM   4973 C  CA  . ASP C 3 167 ? 38.060  -31.321 10.717  1.00 75.86  ? 167 ASP L CA  1 
ATOM   4974 C  C   . ASP C 3 167 ? 38.156  -31.881 12.136  1.00 77.10  ? 167 ASP L C   1 
ATOM   4975 O  O   . ASP C 3 167 ? 39.042  -31.501 12.899  1.00 76.66  ? 167 ASP L O   1 
ATOM   4976 C  CB  . ASP C 3 167 ? 38.833  -32.182 9.714   1.00 75.62  ? 167 ASP L CB  1 
ATOM   4977 C  CG  . ASP C 3 167 ? 38.116  -33.464 9.322   1.00 76.59  ? 167 ASP L CG  1 
ATOM   4978 O  OD1 . ASP C 3 167 ? 37.054  -33.363 8.676   1.00 76.66  ? 167 ASP L OD1 1 
ATOM   4979 O  OD2 . ASP C 3 167 ? 38.625  -34.551 9.665   1.00 77.58  ? 167 ASP L OD2 1 
ATOM   4980 N  N   . SER C 3 168 ? 37.234  -32.794 12.466  1.00 78.31  ? 168 SER L N   1 
ATOM   4981 C  CA  A SER C 3 168 ? 37.128  -33.343 13.808  0.84 80.37  ? 168 SER L CA  1 
ATOM   4982 C  CA  B SER C 3 168 ? 37.121  -33.350 13.805  0.16 80.05  ? 168 SER L CA  1 
ATOM   4983 C  C   . SER C 3 168 ? 38.212  -34.392 14.045  1.00 80.74  ? 168 SER L C   1 
ATOM   4984 O  O   . SER C 3 168 ? 38.645  -34.589 15.177  1.00 80.98  ? 168 SER L O   1 
ATOM   4985 C  CB  A SER C 3 168 ? 35.756  -33.917 14.046  0.84 82.12  ? 168 SER L CB  1 
ATOM   4986 C  CB  B SER C 3 168 ? 35.748  -33.936 14.018  0.16 81.14  ? 168 SER L CB  1 
ATOM   4987 O  OG  A SER C 3 168 ? 35.477  -34.960 13.124  0.84 83.32  ? 168 SER L OG  1 
ATOM   4988 O  OG  B SER C 3 168 ? 35.589  -34.396 15.351  0.16 82.96  ? 168 SER L OG  1 
ATOM   4989 N  N   . LYS C 3 169 ? 38.641  -35.060 12.966  1.00 81.49  ? 169 LYS L N   1 
ATOM   4990 C  CA  . LYS C 3 169 ? 39.608  -36.143 13.053  1.00 82.57  ? 169 LYS L CA  1 
ATOM   4991 C  C   . LYS C 3 169 ? 40.997  -35.650 12.652  1.00 81.00  ? 169 LYS L C   1 
ATOM   4992 O  O   . LYS C 3 169 ? 41.941  -35.769 13.429  1.00 81.01  ? 169 LYS L O   1 
ATOM   4993 C  CB  . LYS C 3 169 ? 39.153  -37.309 12.170  1.00 83.88  ? 169 LYS L CB  1 
ATOM   4994 C  CG  . LYS C 3 169 ? 37.833  -37.943 12.588  1.00 86.15  ? 169 LYS L CG  1 
ATOM   4995 C  CD  . LYS C 3 169 ? 37.296  -38.960 11.605  1.00 87.58  ? 169 LYS L CD  1 
ATOM   4996 C  CE  . LYS C 3 169 ? 35.978  -39.559 12.047  1.00 89.80  ? 169 LYS L CE  1 
ATOM   4997 N  NZ  . LYS C 3 169 ? 35.426  -40.484 11.029  1.00 91.26  ? 169 LYS L NZ  1 
ATOM   4998 N  N   . ASP C 3 170 ? 41.103  -35.097 11.437  1.00 79.58  ? 170 ASP L N   1 
ATOM   4999 C  CA  . ASP C 3 170 ? 42.384  -34.733 10.848  1.00 79.20  ? 170 ASP L CA  1 
ATOM   5000 C  C   . ASP C 3 170 ? 42.916  -33.434 11.451  1.00 77.59  ? 170 ASP L C   1 
ATOM   5001 O  O   . ASP C 3 170 ? 44.128  -33.271 11.563  1.00 78.53  ? 170 ASP L O   1 
ATOM   5002 C  CB  . ASP C 3 170 ? 42.273  -34.589 9.327   1.00 79.36  ? 170 ASP L CB  1 
ATOM   5003 C  CG  . ASP C 3 170 ? 41.891  -35.868 8.600   1.00 81.81  ? 170 ASP L CG  1 
ATOM   5004 O  OD1 . ASP C 3 170 ? 41.746  -36.912 9.273   1.00 83.84  ? 170 ASP L OD1 1 
ATOM   5005 O  OD2 . ASP C 3 170 ? 41.737  -35.808 7.362   1.00 82.09  ? 170 ASP L OD2 1 
ATOM   5006 N  N   . SER C 3 171 ? 42.004  -32.521 11.820  1.00 75.55  ? 171 SER L N   1 
ATOM   5007 C  CA  . SER C 3 171 ? 42.336  -31.164 12.240  1.00 74.74  ? 171 SER L CA  1 
ATOM   5008 C  C   . SER C 3 171 ? 42.779  -30.326 11.040  1.00 73.82  ? 171 SER L C   1 
ATOM   5009 O  O   . SER C 3 171 ? 43.484  -29.331 11.204  1.00 73.30  ? 171 SER L O   1 
ATOM   5010 C  CB  . SER C 3 171 ? 43.376  -31.145 13.342  1.00 75.25  ? 171 SER L CB  1 
ATOM   5011 O  OG  . SER C 3 171 ? 43.017  -32.014 14.404  1.00 75.98  ? 171 SER L OG  1 
ATOM   5012 N  N   . THR C 3 172 ? 42.330  -30.719 9.841   1.00 73.46  ? 172 THR L N   1 
ATOM   5013 C  CA  . THR C 3 172 ? 42.743  -30.087 8.598   1.00 73.44  ? 172 THR L CA  1 
ATOM   5014 C  C   . THR C 3 172 ? 41.592  -29.256 8.035   1.00 72.67  ? 172 THR L C   1 
ATOM   5015 O  O   . THR C 3 172 ? 40.466  -29.336 8.524   1.00 72.49  ? 172 THR L O   1 
ATOM   5016 C  CB  . THR C 3 172 ? 43.219  -31.130 7.576   1.00 73.58  ? 172 THR L CB  1 
ATOM   5017 O  OG1 . THR C 3 172 ? 42.144  -32.033 7.310   1.00 73.37  ? 172 THR L OG1 1 
ATOM   5018 C  CG2 . THR C 3 172 ? 44.432  -31.904 8.044   1.00 74.71  ? 172 THR L CG2 1 
ATOM   5019 N  N   . TYR C 3 173 ? 41.903  -28.456 7.006   1.00 72.41  ? 173 TYR L N   1 
ATOM   5020 C  CA  . TYR C 3 173 ? 40.919  -27.638 6.316   1.00 71.15  ? 173 TYR L CA  1 
ATOM   5021 C  C   . TYR C 3 173 ? 40.833  -28.065 4.854   1.00 69.42  ? 173 TYR L C   1 
ATOM   5022 O  O   . TYR C 3 173 ? 41.733  -28.728 4.344   1.00 69.59  ? 173 TYR L O   1 
ATOM   5023 C  CB  . TYR C 3 173 ? 41.283  -26.153 6.393   1.00 71.90  ? 173 TYR L CB  1 
ATOM   5024 C  CG  . TYR C 3 173 ? 41.460  -25.602 7.786   1.00 73.55  ? 173 TYR L CG  1 
ATOM   5025 C  CD1 . TYR C 3 173 ? 42.638  -25.796 8.490   1.00 74.33  ? 173 TYR L CD1 1 
ATOM   5026 C  CD2 . TYR C 3 173 ? 40.446  -24.889 8.406   1.00 74.20  ? 173 TYR L CD2 1 
ATOM   5027 C  CE1 . TYR C 3 173 ? 42.808  -25.290 9.769   1.00 75.84  ? 173 TYR L CE1 1 
ATOM   5028 C  CE2 . TYR C 3 173 ? 40.598  -24.378 9.685   1.00 75.88  ? 173 TYR L CE2 1 
ATOM   5029 C  CZ  . TYR C 3 173 ? 41.784  -24.579 10.369  1.00 76.79  ? 173 TYR L CZ  1 
ATOM   5030 O  OH  . TYR C 3 173 ? 41.947  -24.079 11.638  1.00 79.27  ? 173 TYR L OH  1 
ATOM   5031 N  N   . SER C 3 174 ? 39.734  -27.673 4.200   1.00 68.03  ? 174 SER L N   1 
ATOM   5032 C  CA  . SER C 3 174 ? 39.575  -27.822 2.763   1.00 67.20  ? 174 SER L CA  1 
ATOM   5033 C  C   . SER C 3 174 ? 39.072  -26.504 2.182   1.00 67.55  ? 174 SER L C   1 
ATOM   5034 O  O   . SER C 3 174 ? 38.390  -25.749 2.870   1.00 68.85  ? 174 SER L O   1 
ATOM   5035 C  CB  . SER C 3 174 ? 38.644  -28.959 2.426   1.00 66.62  ? 174 SER L CB  1 
ATOM   5036 O  OG  . SER C 3 174 ? 39.207  -30.208 2.799   1.00 67.67  ? 174 SER L OG  1 
ATOM   5037 N  N   . LEU C 3 175 ? 39.411  -26.246 0.913   1.00 67.25  ? 175 LEU L N   1 
ATOM   5038 C  CA  . LEU C 3 175 ? 39.011  -25.026 0.229   1.00 67.35  ? 175 LEU L CA  1 
ATOM   5039 C  C   . LEU C 3 175 ? 38.319  -25.393 -1.081  1.00 66.54  ? 175 LEU L C   1 
ATOM   5040 O  O   . LEU C 3 175 ? 38.599  -26.442 -1.657  1.00 65.41  ? 175 LEU L O   1 
ATOM   5041 C  CB  . LEU C 3 175 ? 40.257  -24.171 -0.028  1.00 68.50  ? 175 LEU L CB  1 
ATOM   5042 C  CG  . LEU C 3 175 ? 40.000  -22.699 -0.352  1.00 68.97  ? 175 LEU L CG  1 
ATOM   5043 C  CD1 . LEU C 3 175 ? 40.042  -21.850 0.910   1.00 69.77  ? 175 LEU L CD1 1 
ATOM   5044 C  CD2 . LEU C 3 175 ? 40.998  -22.187 -1.379  1.00 69.32  ? 175 LEU L CD2 1 
ATOM   5045 N  N   . SER C 3 176 ? 37.419  -24.515 -1.540  1.00 67.05  ? 176 SER L N   1 
ATOM   5046 C  CA  . SER C 3 176 ? 36.732  -24.697 -2.808  1.00 67.79  ? 176 SER L CA  1 
ATOM   5047 C  C   . SER C 3 176 ? 36.613  -23.358 -3.530  1.00 69.67  ? 176 SER L C   1 
ATOM   5048 O  O   . SER C 3 176 ? 35.721  -22.567 -3.230  1.00 71.03  ? 176 SER L O   1 
ATOM   5049 C  CB  . SER C 3 176 ? 35.382  -25.336 -2.604  1.00 67.70  ? 176 SER L CB  1 
ATOM   5050 O  OG  . SER C 3 176 ? 34.735  -25.572 -3.847  1.00 67.12  ? 176 SER L OG  1 
ATOM   5051 N  N   . SER C 3 177 ? 37.532  -23.120 -4.475  1.00 70.91  ? 177 SER L N   1 
ATOM   5052 C  CA  . SER C 3 177 ? 37.468  -21.965 -5.356  1.00 71.47  ? 177 SER L CA  1 
ATOM   5053 C  C   . SER C 3 177 ? 36.667  -22.334 -6.603  1.00 70.93  ? 177 SER L C   1 
ATOM   5054 O  O   . SER C 3 177 ? 36.726  -23.474 -7.059  1.00 70.58  ? 177 SER L O   1 
ATOM   5055 C  CB  . SER C 3 177 ? 38.852  -21.477 -5.704  1.00 72.35  ? 177 SER L CB  1 
ATOM   5056 O  OG  . SER C 3 177 ? 38.822  -20.124 -6.133  1.00 73.60  ? 177 SER L OG  1 
ATOM   5057 N  N   . THR C 3 178 ? 35.916  -21.365 -7.142  1.00 71.73  ? 178 THR L N   1 
ATOM   5058 C  CA  . THR C 3 178 ? 34.991  -21.619 -8.236  1.00 72.19  ? 178 THR L CA  1 
ATOM   5059 C  C   . THR C 3 178 ? 35.028  -20.461 -9.230  1.00 73.60  ? 178 THR L C   1 
ATOM   5060 O  O   . THR C 3 178 ? 34.474  -19.398 -8.961  1.00 76.56  ? 178 THR L O   1 
ATOM   5061 C  CB  . THR C 3 178 ? 33.559  -21.817 -7.720  1.00 72.61  ? 178 THR L CB  1 
ATOM   5062 O  OG1 . THR C 3 178 ? 33.584  -22.769 -6.656  1.00 72.20  ? 178 THR L OG1 1 
ATOM   5063 C  CG2 . THR C 3 178 ? 32.603  -22.273 -8.801  1.00 72.75  ? 178 THR L CG2 1 
ATOM   5064 N  N   . LEU C 3 179 ? 35.674  -20.683 -10.381 1.00 73.79  ? 179 LEU L N   1 
ATOM   5065 C  CA  . LEU C 3 179 ? 35.689  -19.712 -11.464 1.00 75.14  ? 179 LEU L CA  1 
ATOM   5066 C  C   . LEU C 3 179 ? 34.391  -19.835 -12.257 1.00 75.75  ? 179 LEU L C   1 
ATOM   5067 O  O   . LEU C 3 179 ? 34.093  -20.903 -12.786 1.00 75.74  ? 179 LEU L O   1 
ATOM   5068 C  CB  . LEU C 3 179 ? 36.901  -19.983 -12.361 1.00 75.22  ? 179 LEU L CB  1 
ATOM   5069 C  CG  . LEU C 3 179 ? 37.123  -18.983 -13.495 1.00 77.07  ? 179 LEU L CG  1 
ATOM   5070 C  CD1 . LEU C 3 179 ? 38.001  -17.829 -13.033 1.00 78.27  ? 179 LEU L CD1 1 
ATOM   5071 C  CD2 . LEU C 3 179 ? 37.729  -19.665 -14.713 1.00 77.50  ? 179 LEU L CD2 1 
ATOM   5072 N  N   . THR C 3 180 ? 33.635  -18.733 -12.343 1.00 77.30  ? 180 THR L N   1 
ATOM   5073 C  CA  . THR C 3 180 ? 32.343  -18.734 -13.011 1.00 78.61  ? 180 THR L CA  1 
ATOM   5074 C  C   . THR C 3 180 ? 32.381  -17.769 -14.194 1.00 80.57  ? 180 THR L C   1 
ATOM   5075 O  O   . THR C 3 180 ? 32.618  -16.576 -14.016 1.00 81.06  ? 180 THR L O   1 
ATOM   5076 C  CB  . THR C 3 180 ? 31.215  -18.376 -12.036 1.00 79.06  ? 180 THR L CB  1 
ATOM   5077 O  OG1 . THR C 3 180 ? 31.375  -19.162 -10.854 1.00 77.06  ? 180 THR L OG1 1 
ATOM   5078 C  CG2 . THR C 3 180 ? 29.839  -18.606 -12.621 1.00 80.40  ? 180 THR L CG2 1 
ATOM   5079 N  N   . LEU C 3 181 ? 32.142  -18.313 -15.395 1.00 82.30  ? 181 LEU L N   1 
ATOM   5080 C  CA  . LEU C 3 181 ? 32.101  -17.541 -16.626 1.00 85.11  ? 181 LEU L CA  1 
ATOM   5081 C  C   . LEU C 3 181 ? 30.840  -17.903 -17.407 1.00 87.23  ? 181 LEU L C   1 
ATOM   5082 O  O   . LEU C 3 181 ? 30.186  -18.900 -17.109 1.00 87.83  ? 181 LEU L O   1 
ATOM   5083 C  CB  . LEU C 3 181 ? 33.351  -17.860 -17.452 1.00 85.15  ? 181 LEU L CB  1 
ATOM   5084 C  CG  . LEU C 3 181 ? 34.687  -17.466 -16.824 1.00 85.29  ? 181 LEU L CG  1 
ATOM   5085 C  CD1 . LEU C 3 181 ? 35.843  -17.877 -17.723 1.00 85.53  ? 181 LEU L CD1 1 
ATOM   5086 C  CD2 . LEU C 3 181 ? 34.742  -15.969 -16.542 1.00 87.39  ? 181 LEU L CD2 1 
ATOM   5087 N  N   . SER C 3 182 ? 30.514  -17.081 -18.411 1.00 90.16  ? 182 SER L N   1 
ATOM   5088 C  CA  . SER C 3 182 ? 29.481  -17.418 -19.377 1.00 92.72  ? 182 SER L CA  1 
ATOM   5089 C  C   . SER C 3 182 ? 30.045  -18.419 -20.382 1.00 92.76  ? 182 SER L C   1 
ATOM   5090 O  O   . SER C 3 182 ? 31.257  -18.617 -20.443 1.00 91.13  ? 182 SER L O   1 
ATOM   5091 C  CB  . SER C 3 182 ? 28.957  -16.183 -20.065 1.00 95.21  ? 182 SER L CB  1 
ATOM   5092 O  OG  . SER C 3 182 ? 29.992  -15.526 -20.782 1.00 95.28  ? 182 SER L OG  1 
ATOM   5093 N  N   . LYS C 3 183 ? 29.157  -19.044 -21.165 1.00 95.01  ? 183 LYS L N   1 
ATOM   5094 C  CA  . LYS C 3 183 ? 29.575  -19.979 -22.198 1.00 95.96  ? 183 LYS L CA  1 
ATOM   5095 C  C   . LYS C 3 183 ? 30.316  -19.220 -23.296 1.00 97.46  ? 183 LYS L C   1 
ATOM   5096 O  O   . LYS C 3 183 ? 31.318  -19.706 -23.813 1.00 97.23  ? 183 LYS L O   1 
ATOM   5097 C  CB  . LYS C 3 183 ? 28.380  -20.747 -22.773 1.00 97.85  ? 183 LYS L CB  1 
ATOM   5098 C  CG  . LYS C 3 183 ? 28.743  -21.806 -23.808 1.00 98.56  ? 183 LYS L CG  1 
ATOM   5099 C  CD  . LYS C 3 183 ? 27.609  -22.743 -24.165 1.00 99.87  ? 183 LYS L CD  1 
ATOM   5100 C  CE  . LYS C 3 183 ? 26.444  -22.047 -24.837 1.00 102.61 ? 183 LYS L CE  1 
ATOM   5101 N  NZ  . LYS C 3 183 ? 25.388  -23.010 -25.228 1.00 104.68 ? 183 LYS L NZ  1 
ATOM   5102 N  N   . ALA C 3 184 ? 29.818  -18.024 -23.635 1.00 99.93  ? 184 ALA L N   1 
ATOM   5103 C  CA  . ALA C 3 184 ? 30.454  -17.165 -24.622 1.00 101.19 ? 184 ALA L CA  1 
ATOM   5104 C  C   . ALA C 3 184 ? 31.925  -16.952 -24.270 1.00 100.36 ? 184 ALA L C   1 
ATOM   5105 O  O   . ALA C 3 184 ? 32.789  -17.066 -25.136 1.00 101.43 ? 184 ALA L O   1 
ATOM   5106 C  CB  . ALA C 3 184 ? 29.716  -15.851 -24.712 1.00 103.07 ? 184 ALA L CB  1 
ATOM   5107 N  N   . ASP C 3 185 ? 32.195  -16.651 -22.993 1.00 99.44  ? 185 ASP L N   1 
ATOM   5108 C  CA  . ASP C 3 185 ? 33.546  -16.396 -22.516 1.00 98.61  ? 185 ASP L CA  1 
ATOM   5109 C  C   . ASP C 3 185 ? 34.316  -17.707 -22.357 1.00 95.96  ? 185 ASP L C   1 
ATOM   5110 O  O   . ASP C 3 185 ? 35.534  -17.727 -22.527 1.00 95.52  ? 185 ASP L O   1 
ATOM   5111 C  CB  . ASP C 3 185 ? 33.532  -15.602 -21.206 1.00 99.00  ? 185 ASP L CB  1 
ATOM   5112 C  CG  . ASP C 3 185 ? 33.340  -14.107 -21.400 1.00 101.75 ? 185 ASP L CG  1 
ATOM   5113 O  OD1 . ASP C 3 185 ? 32.384  -13.723 -22.103 1.00 104.21 ? 185 ASP L OD1 1 
ATOM   5114 O  OD2 . ASP C 3 185 ? 34.149  -13.338 -20.845 1.00 102.21 ? 185 ASP L OD2 1 
ATOM   5115 N  N   . TYR C 3 186 ? 33.605  -18.792 -22.021 1.00 94.14  ? 186 TYR L N   1 
ATOM   5116 C  CA  . TYR C 3 186 ? 34.228  -20.086 -21.788 1.00 91.80  ? 186 TYR L CA  1 
ATOM   5117 C  C   . TYR C 3 186 ? 34.731  -20.692 -23.099 1.00 92.60  ? 186 TYR L C   1 
ATOM   5118 O  O   . TYR C 3 186 ? 35.788  -21.319 -23.122 1.00 91.14  ? 186 TYR L O   1 
ATOM   5119 C  CB  . TYR C 3 186 ? 33.254  -21.045 -21.094 1.00 89.83  ? 186 TYR L CB  1 
ATOM   5120 C  CG  . TYR C 3 186 ? 33.823  -22.414 -20.818 1.00 87.39  ? 186 TYR L CG  1 
ATOM   5121 C  CD1 . TYR C 3 186 ? 34.890  -22.580 -19.949 1.00 85.15  ? 186 TYR L CD1 1 
ATOM   5122 C  CD2 . TYR C 3 186 ? 33.314  -23.544 -21.439 1.00 87.35  ? 186 TYR L CD2 1 
ATOM   5123 C  CE1 . TYR C 3 186 ? 35.431  -23.830 -19.696 1.00 84.04  ? 186 TYR L CE1 1 
ATOM   5124 C  CE2 . TYR C 3 186 ? 33.840  -24.803 -21.194 1.00 86.31  ? 186 TYR L CE2 1 
ATOM   5125 C  CZ  . TYR C 3 186 ? 34.906  -24.947 -20.322 1.00 84.80  ? 186 TYR L CZ  1 
ATOM   5126 O  OH  . TYR C 3 186 ? 35.440  -26.189 -20.075 1.00 84.00  ? 186 TYR L OH  1 
ATOM   5127 N  N   . GLU C 3 187 ? 33.967  -20.507 -24.183 1.00 94.85  ? 187 GLU L N   1 
ATOM   5128 C  CA  . GLU C 3 187 ? 34.272  -21.127 -25.464 1.00 97.50  ? 187 GLU L CA  1 
ATOM   5129 C  C   . GLU C 3 187 ? 35.424  -20.398 -26.162 1.00 99.61  ? 187 GLU L C   1 
ATOM   5130 O  O   . GLU C 3 187 ? 36.025  -20.948 -27.083 1.00 101.47 ? 187 GLU L O   1 
ATOM   5131 C  CB  . GLU C 3 187 ? 33.023  -21.148 -26.350 1.00 99.52  ? 187 GLU L CB  1 
ATOM   5132 C  CG  . GLU C 3 187 ? 31.880  -21.981 -25.788 1.00 99.64  ? 187 GLU L CG  1 
ATOM   5133 C  CD  . GLU C 3 187 ? 32.027  -23.486 -25.936 1.00 100.48 ? 187 GLU L CD  1 
ATOM   5134 O  OE1 . GLU C 3 187 ? 32.215  -24.167 -24.906 1.00 98.54  ? 187 GLU L OE1 1 
ATOM   5135 O  OE2 . GLU C 3 187 ? 31.929  -23.978 -27.077 1.00 104.18 ? 187 GLU L OE2 1 
ATOM   5136 N  N   . LYS C 3 188 ? 35.726  -19.167 -25.724 1.00 99.81  ? 188 LYS L N   1 
ATOM   5137 C  CA  . LYS C 3 188 ? 36.788  -18.363 -26.314 1.00 101.03 ? 188 LYS L CA  1 
ATOM   5138 C  C   . LYS C 3 188 ? 38.165  -18.934 -25.974 1.00 100.87 ? 188 LYS L C   1 
ATOM   5139 O  O   . LYS C 3 188 ? 39.078  -18.856 -26.793 1.00 103.11 ? 188 LYS L O   1 
ATOM   5140 C  CB  . LYS C 3 188 ? 36.701  -16.910 -25.833 1.00 101.38 ? 188 LYS L CB  1 
ATOM   5141 C  CG  . LYS C 3 188 ? 35.649  -16.055 -26.527 1.00 103.62 ? 188 LYS L CG  1 
ATOM   5142 C  CD  . LYS C 3 188 ? 35.382  -14.724 -25.844 1.00 104.38 ? 188 LYS L CD  1 
ATOM   5143 C  CE  . LYS C 3 188 ? 36.591  -13.813 -25.774 1.00 105.48 ? 188 LYS L CE  1 
ATOM   5144 N  NZ  . LYS C 3 188 ? 37.100  -13.455 -27.119 1.00 108.01 ? 188 LYS L NZ  1 
ATOM   5145 N  N   . HIS C 3 189 ? 38.310  -19.494 -24.766 1.00 99.66  ? 189 HIS L N   1 
ATOM   5146 C  CA  . HIS C 3 189 ? 39.611  -19.901 -24.254 1.00 99.69  ? 189 HIS L CA  1 
ATOM   5147 C  C   . HIS C 3 189 ? 39.693  -21.425 -24.191 1.00 98.81  ? 189 HIS L C   1 
ATOM   5148 O  O   . HIS C 3 189 ? 38.669  -22.105 -24.157 1.00 98.36  ? 189 HIS L O   1 
ATOM   5149 C  CB  . HIS C 3 189 ? 39.875  -19.228 -22.902 1.00 98.80  ? 189 HIS L CB  1 
ATOM   5150 C  CG  . HIS C 3 189 ? 39.817  -17.735 -22.958 1.00 100.48 ? 189 HIS L CG  1 
ATOM   5151 N  ND1 . HIS C 3 189 ? 38.642  -17.048 -23.174 1.00 101.15 ? 189 HIS L ND1 1 
ATOM   5152 C  CD2 . HIS C 3 189 ? 40.770  -16.802 -22.823 1.00 101.60 ? 189 HIS L CD2 1 
ATOM   5153 C  CE1 . HIS C 3 189 ? 38.889  -15.746 -23.171 1.00 102.81 ? 189 HIS L CE1 1 
ATOM   5154 N  NE2 . HIS C 3 189 ? 40.175  -15.574 -22.959 1.00 103.14 ? 189 HIS L NE2 1 
ATOM   5155 N  N   . LYS C 3 190 ? 40.929  -21.943 -24.164 1.00 98.12  ? 190 LYS L N   1 
ATOM   5156 C  CA  . LYS C 3 190 ? 41.191  -23.368 -24.294 1.00 96.84  ? 190 LYS L CA  1 
ATOM   5157 C  C   . LYS C 3 190 ? 41.654  -23.939 -22.954 1.00 92.67  ? 190 LYS L C   1 
ATOM   5158 O  O   . LYS C 3 190 ? 41.000  -24.818 -22.399 1.00 90.38  ? 190 LYS L O   1 
ATOM   5159 C  CB  . LYS C 3 190 ? 42.244  -23.610 -25.381 1.00 100.50 ? 190 LYS L CB  1 
ATOM   5160 C  CG  . LYS C 3 190 ? 42.322  -25.034 -25.918 1.00 102.75 ? 190 LYS L CG  1 
ATOM   5161 C  CD  . LYS C 3 190 ? 41.190  -25.383 -26.864 1.00 105.13 ? 190 LYS L CD  1 
ATOM   5162 C  CE  . LYS C 3 190 ? 41.398  -26.698 -27.587 1.00 107.39 ? 190 LYS L CE  1 
ATOM   5163 N  NZ  . LYS C 3 190 ? 40.392  -26.898 -28.658 1.00 108.76 ? 190 LYS L NZ  1 
ATOM   5164 N  N   . VAL C 3 191 ? 42.787  -23.430 -22.451 1.00 91.12  ? 191 VAL L N   1 
ATOM   5165 C  CA  . VAL C 3 191 ? 43.443  -23.982 -21.275 1.00 89.13  ? 191 VAL L CA  1 
ATOM   5166 C  C   . VAL C 3 191 ? 42.874  -23.315 -20.025 1.00 86.23  ? 191 VAL L C   1 
ATOM   5167 O  O   . VAL C 3 191 ? 42.861  -22.090 -19.932 1.00 87.82  ? 191 VAL L O   1 
ATOM   5168 C  CB  . VAL C 3 191 ? 44.972  -23.796 -21.349 1.00 90.61  ? 191 VAL L CB  1 
ATOM   5169 C  CG1 . VAL C 3 191 ? 45.660  -24.202 -20.052 1.00 89.32  ? 191 VAL L CG1 1 
ATOM   5170 C  CG2 . VAL C 3 191 ? 45.573  -24.539 -22.532 1.00 93.30  ? 191 VAL L CG2 1 
ATOM   5171 N  N   . TYR C 3 192 ? 42.423  -24.139 -19.070 1.00 82.64  ? 192 TYR L N   1 
ATOM   5172 C  CA  . TYR C 3 192 ? 41.979  -23.667 -17.768 1.00 79.14  ? 192 TYR L CA  1 
ATOM   5173 C  C   . TYR C 3 192 ? 42.805  -24.354 -16.687 1.00 77.83  ? 192 TYR L C   1 
ATOM   5174 O  O   . TYR C 3 192 ? 42.994  -25.566 -16.734 1.00 79.10  ? 192 TYR L O   1 
ATOM   5175 C  CB  . TYR C 3 192 ? 40.484  -23.928 -17.579 1.00 77.48  ? 192 TYR L CB  1 
ATOM   5176 C  CG  . TYR C 3 192 ? 39.604  -23.139 -18.512 1.00 78.11  ? 192 TYR L CG  1 
ATOM   5177 C  CD1 . TYR C 3 192 ? 39.500  -23.479 -19.851 1.00 79.29  ? 192 TYR L CD1 1 
ATOM   5178 C  CD2 . TYR C 3 192 ? 38.906  -22.028 -18.068 1.00 78.21  ? 192 TYR L CD2 1 
ATOM   5179 C  CE1 . TYR C 3 192 ? 38.706  -22.750 -20.721 1.00 80.72  ? 192 TYR L CE1 1 
ATOM   5180 C  CE2 . TYR C 3 192 ? 38.109  -21.286 -18.925 1.00 79.39  ? 192 TYR L CE2 1 
ATOM   5181 C  CZ  . TYR C 3 192 ? 38.011  -21.648 -20.257 1.00 80.74  ? 192 TYR L CZ  1 
ATOM   5182 O  OH  . TYR C 3 192 ? 37.223  -20.917 -21.109 1.00 82.06  ? 192 TYR L OH  1 
ATOM   5183 N  N   . ALA C 3 193 ? 43.291  -23.567 -15.722 1.00 77.09  ? 193 ALA L N   1 
ATOM   5184 C  CA  . ALA C 3 193 ? 44.191  -24.068 -14.697 1.00 78.04  ? 193 ALA L CA  1 
ATOM   5185 C  C   . ALA C 3 193 ? 43.982  -23.296 -13.397 1.00 77.96  ? 193 ALA L C   1 
ATOM   5186 O  O   . ALA C 3 193 ? 43.415  -22.206 -13.406 1.00 78.63  ? 193 ALA L O   1 
ATOM   5187 C  CB  . ALA C 3 193 ? 45.617  -23.951 -15.176 1.00 79.30  ? 193 ALA L CB  1 
ATOM   5188 N  N   . CYS C 3 194 ? 44.446  -23.881 -12.285 1.00 77.72  ? 194 CYS L N   1 
ATOM   5189 C  CA  . CYS C 3 194 ? 44.479  -23.191 -11.005 1.00 78.11  ? 194 CYS L CA  1 
ATOM   5190 C  C   . CYS C 3 194 ? 45.776  -23.535 -10.274 1.00 78.34  ? 194 CYS L C   1 
ATOM   5191 O  O   . CYS C 3 194 ? 46.070  -24.705 -10.040 1.00 77.36  ? 194 CYS L O   1 
ATOM   5192 C  CB  . CYS C 3 194 ? 43.265  -23.532 -10.147 1.00 77.53  ? 194 CYS L CB  1 
ATOM   5193 S  SG  . CYS C 3 194 ? 43.148  -25.283 -9.699  1.00 78.77  ? 194 CYS L SG  1 
ATOM   5194 N  N   . GLU C 3 195 ? 46.545  -22.493 -9.933  1.00 79.93  ? 195 GLU L N   1 
ATOM   5195 C  CA  . GLU C 3 195 ? 47.812  -22.642 -9.237  1.00 80.96  ? 195 GLU L CA  1 
ATOM   5196 C  C   . GLU C 3 195 ? 47.569  -22.481 -7.738  1.00 79.26  ? 195 GLU L C   1 
ATOM   5197 O  O   . GLU C 3 195 ? 46.797  -21.617 -7.326  1.00 78.86  ? 195 GLU L O   1 
ATOM   5198 C  CB  . GLU C 3 195 ? 48.816  -21.616 -9.766  1.00 83.57  ? 195 GLU L CB  1 
ATOM   5199 C  CG  . GLU C 3 195 ? 50.225  -21.813 -9.241  1.00 86.35  ? 195 GLU L CG  1 
ATOM   5200 C  CD  . GLU C 3 195 ? 51.259  -20.895 -9.870  1.00 90.31  ? 195 GLU L CD  1 
ATOM   5201 O  OE1 . GLU C 3 195 ? 51.432  -20.960 -11.104 1.00 91.79  ? 195 GLU L OE1 1 
ATOM   5202 O  OE2 . GLU C 3 195 ? 51.888  -20.116 -9.125  1.00 93.07  ? 195 GLU L OE2 1 
ATOM   5203 N  N   . VAL C 3 196 ? 48.244  -23.314 -6.938  1.00 78.72  ? 196 VAL L N   1 
ATOM   5204 C  CA  . VAL C 3 196 ? 47.984  -23.412 -5.510  1.00 77.86  ? 196 VAL L CA  1 
ATOM   5205 C  C   . VAL C 3 196 ? 49.303  -23.295 -4.751  1.00 79.80  ? 196 VAL L C   1 
ATOM   5206 O  O   . VAL C 3 196 ? 50.174  -24.150 -4.894  1.00 81.01  ? 196 VAL L O   1 
ATOM   5207 C  CB  . VAL C 3 196 ? 47.262  -24.732 -5.174  1.00 76.24  ? 196 VAL L CB  1 
ATOM   5208 C  CG1 . VAL C 3 196 ? 47.155  -24.959 -3.673  1.00 75.60  ? 196 VAL L CG1 1 
ATOM   5209 C  CG2 . VAL C 3 196 ? 45.890  -24.807 -5.830  1.00 74.63  ? 196 VAL L CG2 1 
ATOM   5210 N  N   . THR C 3 197 ? 49.426  -22.241 -3.933  1.00 81.29  ? 197 THR L N   1 
ATOM   5211 C  CA  . THR C 3 197 ? 50.580  -22.049 -3.069  1.00 83.86  ? 197 THR L CA  1 
ATOM   5212 C  C   . THR C 3 197 ? 50.194  -22.382 -1.629  1.00 83.97  ? 197 THR L C   1 
ATOM   5213 O  O   . THR C 3 197 ? 49.080  -22.087 -1.199  1.00 82.24  ? 197 THR L O   1 
ATOM   5214 C  CB  . THR C 3 197 ? 51.126  -20.619 -3.181  1.00 85.65  ? 197 THR L CB  1 
ATOM   5215 O  OG1 . THR C 3 197 ? 51.366  -20.343 -4.562  1.00 86.24  ? 197 THR L OG1 1 
ATOM   5216 C  CG2 . THR C 3 197 ? 52.395  -20.407 -2.385  1.00 88.05  ? 197 THR L CG2 1 
ATOM   5217 N  N   . HIS C 3 198 ? 51.132  -22.997 -0.896  1.00 86.51  ? 198 HIS L N   1 
ATOM   5218 C  CA  . HIS C 3 198 ? 50.906  -23.415 0.479   1.00 87.03  ? 198 HIS L CA  1 
ATOM   5219 C  C   . HIS C 3 198 ? 52.254  -23.689 1.145   1.00 89.98  ? 198 HIS L C   1 
ATOM   5220 O  O   . HIS C 3 198 ? 53.248  -23.906 0.456   1.00 93.47  ? 198 HIS L O   1 
ATOM   5221 C  CB  . HIS C 3 198 ? 50.001  -24.652 0.518   1.00 86.17  ? 198 HIS L CB  1 
ATOM   5222 C  CG  . HIS C 3 198 ? 49.418  -24.929 1.863   1.00 86.30  ? 198 HIS L CG  1 
ATOM   5223 N  ND1 . HIS C 3 198 ? 49.851  -25.956 2.673   1.00 87.18  ? 198 HIS L ND1 1 
ATOM   5224 C  CD2 . HIS C 3 198 ? 48.457  -24.298 2.548   1.00 85.85  ? 198 HIS L CD2 1 
ATOM   5225 C  CE1 . HIS C 3 198 ? 49.158  -25.944 3.801   1.00 87.07  ? 198 HIS L CE1 1 
ATOM   5226 N  NE2 . HIS C 3 198 ? 48.305  -24.946 3.747   1.00 86.33  ? 198 HIS L NE2 1 
ATOM   5227 N  N   . GLN C 3 199 ? 52.274  -23.678 2.486   1.00 90.74  ? 199 GLN L N   1 
ATOM   5228 C  CA  . GLN C 3 199 ? 53.488  -23.920 3.253   1.00 93.27  ? 199 GLN L CA  1 
ATOM   5229 C  C   . GLN C 3 199 ? 54.046  -25.310 2.953   1.00 93.25  ? 199 GLN L C   1 
ATOM   5230 O  O   . GLN C 3 199 ? 55.241  -25.456 2.704   1.00 95.50  ? 199 GLN L O   1 
ATOM   5231 C  CB  . GLN C 3 199 ? 53.227  -23.802 4.757   1.00 94.07  ? 199 GLN L CB  1 
ATOM   5232 C  CG  . GLN C 3 199 ? 53.156  -22.370 5.262   1.00 95.67  ? 199 GLN L CG  1 
ATOM   5233 C  CD  . GLN C 3 199 ? 53.254  -22.302 6.768   1.00 97.25  ? 199 GLN L CD  1 
ATOM   5234 O  OE1 . GLN C 3 199 ? 54.204  -22.801 7.367   1.00 98.16  ? 199 GLN L OE1 1 
ATOM   5235 N  NE2 . GLN C 3 199 ? 52.267  -21.683 7.398   1.00 96.93  ? 199 GLN L NE2 1 
ATOM   5236 N  N   . GLY C 3 200 ? 53.168  -26.320 3.001   1.00 90.51  ? 200 GLY L N   1 
ATOM   5237 C  CA  . GLY C 3 200 ? 53.552  -27.708 2.802   1.00 90.43  ? 200 GLY L CA  1 
ATOM   5238 C  C   . GLY C 3 200 ? 54.176  -27.965 1.430   1.00 90.28  ? 200 GLY L C   1 
ATOM   5239 O  O   . GLY C 3 200 ? 55.011  -28.856 1.292   1.00 92.46  ? 200 GLY L O   1 
ATOM   5240 N  N   . LEU C 3 201 ? 53.755  -27.186 0.425   1.00 88.61  ? 201 LEU L N   1 
ATOM   5241 C  CA  . LEU C 3 201 ? 54.270  -27.316 -0.930  1.00 89.61  ? 201 LEU L CA  1 
ATOM   5242 C  C   . LEU C 3 201 ? 55.650  -26.670 -1.028  1.00 92.48  ? 201 LEU L C   1 
ATOM   5243 O  O   . LEU C 3 201 ? 55.854  -25.557 -0.544  1.00 92.57  ? 201 LEU L O   1 
ATOM   5244 C  CB  . LEU C 3 201 ? 53.290  -26.649 -1.901  1.00 87.15  ? 201 LEU L CB  1 
ATOM   5245 C  CG  . LEU C 3 201 ? 51.892  -27.264 -1.968  1.00 84.71  ? 201 LEU L CG  1 
ATOM   5246 C  CD1 . LEU C 3 201 ? 51.027  -26.525 -2.976  1.00 83.46  ? 201 LEU L CD1 1 
ATOM   5247 C  CD2 . LEU C 3 201 ? 51.959  -28.743 -2.317  1.00 85.45  ? 201 LEU L CD2 1 
ATOM   5248 N  N   . SER C 3 202 ? 56.588  -27.385 -1.665  1.00 94.65  ? 202 SER L N   1 
ATOM   5249 C  CA  A SER C 3 202 ? 57.920  -26.868 -1.932  0.57 97.98  ? 202 SER L CA  1 
ATOM   5250 C  CA  B SER C 3 202 ? 57.920  -26.867 -1.931  0.43 98.07  ? 202 SER L CA  1 
ATOM   5251 C  C   . SER C 3 202 ? 57.869  -25.883 -3.099  1.00 98.16  ? 202 SER L C   1 
ATOM   5252 O  O   . SER C 3 202 ? 58.722  -25.004 -3.211  1.00 100.39 ? 202 SER L O   1 
ATOM   5253 C  CB  A SER C 3 202 ? 58.891  -27.989 -2.202  0.57 100.56 ? 202 SER L CB  1 
ATOM   5254 C  CB  B SER C 3 202 ? 58.894  -27.987 -2.197  0.43 100.80 ? 202 SER L CB  1 
ATOM   5255 O  OG  A SER C 3 202 ? 58.990  -28.855 -1.081  0.57 100.70 ? 202 SER L OG  1 
ATOM   5256 O  OG  B SER C 3 202 ? 58.469  -28.782 -3.294  0.43 100.28 ? 202 SER L OG  1 
ATOM   5257 N  N   . SER C 3 203 ? 56.860  -26.050 -3.966  1.00 95.61  ? 203 SER L N   1 
ATOM   5258 C  CA  . SER C 3 203 ? 56.625  -25.153 -5.086  1.00 95.03  ? 203 SER L CA  1 
ATOM   5259 C  C   . SER C 3 203 ? 55.154  -25.227 -5.496  1.00 91.22  ? 203 SER L C   1 
ATOM   5260 O  O   . SER C 3 203 ? 54.485  -26.217 -5.207  1.00 89.13  ? 203 SER L O   1 
ATOM   5261 C  CB  . SER C 3 203 ? 57.543  -25.476 -6.240  1.00 97.74  ? 203 SER L CB  1 
ATOM   5262 O  OG  . SER C 3 203 ? 57.357  -26.813 -6.682  1.00 97.17  ? 203 SER L OG  1 
ATOM   5263 N  N   . PRO C 3 204 ? 54.600  -24.187 -6.165  1.00 90.07  ? 204 PRO L N   1 
ATOM   5264 C  CA  . PRO C 3 204 ? 53.191  -24.185 -6.570  1.00 86.94  ? 204 PRO L CA  1 
ATOM   5265 C  C   . PRO C 3 204 ? 52.756  -25.414 -7.369  1.00 86.08  ? 204 PRO L C   1 
ATOM   5266 O  O   . PRO C 3 204 ? 53.498  -25.898 -8.221  1.00 87.55  ? 204 PRO L O   1 
ATOM   5267 C  CB  . PRO C 3 204 ? 53.074  -22.929 -7.448  1.00 87.12  ? 204 PRO L CB  1 
ATOM   5268 C  CG  . PRO C 3 204 ? 54.160  -22.012 -6.931  1.00 89.57  ? 204 PRO L CG  1 
ATOM   5269 C  CD  . PRO C 3 204 ? 55.289  -22.939 -6.535  1.00 91.79  ? 204 PRO L CD  1 
ATOM   5270 N  N   . VAL C 3 205 ? 51.541  -25.899 -7.079  1.00 84.34  ? 205 VAL L N   1 
ATOM   5271 C  CA  . VAL C 3 205 ? 50.961  -27.052 -7.751  1.00 84.13  ? 205 VAL L CA  1 
ATOM   5272 C  C   . VAL C 3 205 ? 49.876  -26.562 -8.708  1.00 83.09  ? 205 VAL L C   1 
ATOM   5273 O  O   . VAL C 3 205 ? 49.076  -25.702 -8.348  1.00 82.06  ? 205 VAL L O   1 
ATOM   5274 C  CB  . VAL C 3 205 ? 50.394  -28.066 -6.736  1.00 82.72  ? 205 VAL L CB  1 
ATOM   5275 C  CG1 . VAL C 3 205 ? 49.571  -29.154 -7.411  1.00 81.97  ? 205 VAL L CG1 1 
ATOM   5276 C  CG2 . VAL C 3 205 ? 51.490  -28.681 -5.878  1.00 84.46  ? 205 VAL L CG2 1 
ATOM   5277 N  N   . THR C 3 206 ? 49.850  -27.135 -9.918  1.00 84.37  ? 206 THR L N   1 
ATOM   5278 C  CA  . THR C 3 206 ? 48.910  -26.730 -10.951 1.00 84.31  ? 206 THR L CA  1 
ATOM   5279 C  C   . THR C 3 206 ? 48.151  -27.951 -11.465 1.00 84.37  ? 206 THR L C   1 
ATOM   5280 O  O   . THR C 3 206 ? 48.757  -28.896 -11.966 1.00 88.65  ? 206 THR L O   1 
ATOM   5281 C  CB  . THR C 3 206 ? 49.626  -26.019 -12.109 1.00 86.36  ? 206 THR L CB  1 
ATOM   5282 O  OG1 . THR C 3 206 ? 50.410  -24.949 -11.579 1.00 87.57  ? 206 THR L OG1 1 
ATOM   5283 C  CG2 . THR C 3 206 ? 48.672  -25.475 -13.151 1.00 85.10  ? 206 THR L CG2 1 
ATOM   5284 N  N   . LYS C 3 207 ? 46.822  -27.919 -11.313 1.00 81.96  ? 207 LYS L N   1 
ATOM   5285 C  CA  . LYS C 3 207 ? 45.922  -28.807 -12.033 1.00 81.35  ? 207 LYS L CA  1 
ATOM   5286 C  C   . LYS C 3 207 ? 45.278  -28.012 -13.166 1.00 79.29  ? 207 LYS L C   1 
ATOM   5287 O  O   . LYS C 3 207 ? 44.960  -26.838 -12.993 1.00 78.25  ? 207 LYS L O   1 
ATOM   5288 C  CB  . LYS C 3 207 ? 44.874  -29.403 -11.086 1.00 81.38  ? 207 LYS L CB  1 
ATOM   5289 C  CG  . LYS C 3 207 ? 45.120  -30.846 -10.661 1.00 83.68  ? 207 LYS L CG  1 
ATOM   5290 C  CD  . LYS C 3 207 ? 46.418  -31.076 -9.914  1.00 85.91  ? 207 LYS L CD  1 
ATOM   5291 C  CE  . LYS C 3 207 ? 46.707  -32.548 -9.699  1.00 88.11  ? 207 LYS L CE  1 
ATOM   5292 N  NZ  . LYS C 3 207 ? 47.945  -32.761 -8.912  1.00 89.92  ? 207 LYS L NZ  1 
ATOM   5293 N  N   . SER C 3 208 ? 45.097  -28.658 -14.325 1.00 79.49  ? 208 SER L N   1 
ATOM   5294 C  CA  . SER C 3 208 ? 44.626  -27.966 -15.515 1.00 79.29  ? 208 SER L CA  1 
ATOM   5295 C  C   . SER C 3 208 ? 43.971  -28.939 -16.493 1.00 79.33  ? 208 SER L C   1 
ATOM   5296 O  O   . SER C 3 208 ? 44.102  -30.154 -16.359 1.00 78.46  ? 208 SER L O   1 
ATOM   5297 C  CB  . SER C 3 208 ? 45.755  -27.213 -16.175 1.00 80.68  ? 208 SER L CB  1 
ATOM   5298 O  OG  . SER C 3 208 ? 46.755  -28.103 -16.648 1.00 82.77  ? 208 SER L OG  1 
ATOM   5299 N  N   . PHE C 3 209 ? 43.272  -28.371 -17.483 1.00 79.72  ? 209 PHE L N   1 
ATOM   5300 C  CA  . PHE C 3 209 ? 42.618  -29.143 -18.526 1.00 80.80  ? 209 PHE L CA  1 
ATOM   5301 C  C   . PHE C 3 209 ? 42.376  -28.267 -19.754 1.00 80.93  ? 209 PHE L C   1 
ATOM   5302 O  O   . PHE C 3 209 ? 42.554  -27.051 -19.708 1.00 79.08  ? 209 PHE L O   1 
ATOM   5303 C  CB  . PHE C 3 209 ? 41.292  -29.724 -18.025 1.00 80.18  ? 209 PHE L CB  1 
ATOM   5304 C  CG  . PHE C 3 209 ? 40.234  -28.701 -17.692 1.00 79.33  ? 209 PHE L CG  1 
ATOM   5305 C  CD1 . PHE C 3 209 ? 40.271  -28.000 -16.496 1.00 78.24  ? 209 PHE L CD1 1 
ATOM   5306 C  CD2 . PHE C 3 209 ? 39.208  -28.426 -18.585 1.00 80.11  ? 209 PHE L CD2 1 
ATOM   5307 C  CE1 . PHE C 3 209 ? 39.297  -27.059 -16.194 1.00 77.65  ? 209 PHE L CE1 1 
ATOM   5308 C  CE2 . PHE C 3 209 ? 38.239  -27.480 -18.285 1.00 79.32  ? 209 PHE L CE2 1 
ATOM   5309 C  CZ  . PHE C 3 209 ? 38.283  -26.801 -17.089 1.00 78.11  ? 209 PHE L CZ  1 
ATOM   5310 N  N   . ASN C 3 210 ? 41.976  -28.918 -20.851 1.00 82.90  ? 210 ASN L N   1 
ATOM   5311 C  CA  . ASN C 3 210 ? 41.531  -28.248 -22.061 1.00 84.62  ? 210 ASN L CA  1 
ATOM   5312 C  C   . ASN C 3 210 ? 40.064  -28.601 -22.290 1.00 85.06  ? 210 ASN L C   1 
ATOM   5313 O  O   . ASN C 3 210 ? 39.554  -29.542 -21.686 1.00 86.85  ? 210 ASN L O   1 
ATOM   5314 C  CB  . ASN C 3 210 ? 42.370  -28.660 -23.276 1.00 87.45  ? 210 ASN L CB  1 
ATOM   5315 C  CG  . ASN C 3 210 ? 43.863  -28.516 -23.063 1.00 87.78  ? 210 ASN L CG  1 
ATOM   5316 O  OD1 . ASN C 3 210 ? 44.310  -28.012 -22.035 1.00 87.11  ? 210 ASN L OD1 1 
ATOM   5317 N  ND2 . ASN C 3 210 ? 44.645  -28.957 -24.034 1.00 89.72  ? 210 ASN L ND2 1 
ATOM   5318 N  N   . ARG C 3 211 ? 39.391  -27.855 -23.174 1.00 86.04  ? 211 ARG L N   1 
ATOM   5319 C  CA  . ARG C 3 211 ? 38.047  -28.215 -23.598 1.00 86.79  ? 211 ARG L CA  1 
ATOM   5320 C  C   . ARG C 3 211 ? 38.152  -29.318 -24.651 1.00 89.92  ? 211 ARG L C   1 
ATOM   5321 O  O   . ARG C 3 211 ? 38.592  -29.065 -25.772 1.00 92.44  ? 211 ARG L O   1 
ATOM   5322 C  CB  . ARG C 3 211 ? 37.293  -27.008 -24.165 1.00 87.13  ? 211 ARG L CB  1 
ATOM   5323 C  CG  . ARG C 3 211 ? 37.390  -25.739 -23.328 1.00 85.49  ? 211 ARG L CG  1 
ATOM   5324 C  CD  . ARG C 3 211 ? 36.307  -24.731 -23.675 1.00 86.16  ? 211 ARG L CD  1 
ATOM   5325 N  NE  . ARG C 3 211 ? 35.956  -24.692 -25.091 1.00 88.90  ? 211 ARG L NE  1 
ATOM   5326 C  CZ  . ARG C 3 211 ? 36.772  -24.325 -26.075 1.00 90.37  ? 211 ARG L CZ  1 
ATOM   5327 N  NH1 . ARG C 3 211 ? 38.009  -23.943 -25.812 1.00 90.26  ? 211 ARG L NH1 1 
ATOM   5328 N  NH2 . ARG C 3 211 ? 36.344  -24.345 -27.326 1.00 92.37  ? 211 ARG L NH2 1 
ATOM   5329 N  N   . GLY C 3 212 ? 37.761  -30.543 -24.275 1.00 89.89  ? 212 GLY L N   1 
ATOM   5330 C  CA  . GLY C 3 212 ? 37.839  -31.690 -25.167 1.00 91.64  ? 212 GLY L CA  1 
ATOM   5331 C  C   . GLY C 3 212 ? 37.772  -33.004 -24.407 1.00 91.52  ? 212 GLY L C   1 
ATOM   5332 O  O   . GLY C 3 212 ? 38.617  -33.185 -23.508 1.00 89.11  ? 212 GLY L O   1 
HETATM 5333 K  K   . K   D 4 .   ? -5.796  -2.441  52.881  1.00 62.47  ? 401 K   A K   1 
HETATM 5334 K  K   . K   E 4 .   ? -13.057 -18.921 63.716  1.00 91.40  ? 402 K   A K   1 
HETATM 5335 CL CL  . CL  F 5 .   ? -1.501  -14.406 36.426  1.00 64.14  ? 403 CL  A CL  1 
HETATM 5336 CL CL  . CL  G 5 .   ? 33.338  -36.811 23.675  1.00 64.83  ? 301 CL  L CL  1 
HETATM 5337 O  O   . HOH H 6 .   ? 10.219  -21.408 51.903  1.00 69.68  ? 501 HOH A O   1 
HETATM 5338 O  O   . HOH H 6 .   ? -22.567 -26.723 45.963  1.00 78.97  ? 502 HOH A O   1 
HETATM 5339 O  O   . HOH H 6 .   ? -2.836  -27.675 54.168  1.00 80.66  ? 503 HOH A O   1 
HETATM 5340 O  O   . HOH H 6 .   ? 6.035   -14.984 54.920  1.00 58.23  ? 504 HOH A O   1 
HETATM 5341 O  O   . HOH H 6 .   ? -29.411 -28.675 53.875  1.00 53.23  ? 505 HOH A O   1 
HETATM 5342 O  O   . HOH H 6 .   ? -16.764 -16.160 60.088  1.00 48.73  ? 506 HOH A O   1 
HETATM 5343 O  O   . HOH H 6 .   ? -11.041 -9.503  53.414  1.00 58.65  ? 507 HOH A O   1 
HETATM 5344 O  O   . HOH H 6 .   ? 16.080  -8.551  38.727  1.00 43.49  ? 508 HOH A O   1 
HETATM 5345 O  O   . HOH H 6 .   ? -18.443 -23.113 49.995  1.00 79.43  ? 509 HOH A O   1 
HETATM 5346 O  O   . HOH H 6 .   ? -5.335  -5.416  40.580  1.00 78.46  ? 510 HOH A O   1 
HETATM 5347 O  O   . HOH H 6 .   ? 1.275   -4.033  52.752  1.00 57.21  ? 511 HOH A O   1 
HETATM 5348 O  O   . HOH H 6 .   ? -15.703 -35.317 48.344  1.00 64.06  ? 512 HOH A O   1 
HETATM 5349 O  O   . HOH H 6 .   ? 12.060  -12.252 64.698  1.00 61.55  ? 513 HOH A O   1 
HETATM 5350 O  O   . HOH H 6 .   ? 6.123   17.054  52.877  1.00 64.05  ? 514 HOH A O   1 
HETATM 5351 O  O   . HOH H 6 .   ? 1.817   14.058  61.223  1.00 80.36  ? 515 HOH A O   1 
HETATM 5352 O  O   . HOH H 6 .   ? 17.158  -22.435 47.682  1.00 52.42  ? 516 HOH A O   1 
HETATM 5353 O  O   . HOH H 6 .   ? -5.121  -31.015 42.492  1.00 62.62  ? 517 HOH A O   1 
HETATM 5354 O  O   . HOH H 6 .   ? -1.610  20.730  43.790  1.00 78.26  ? 518 HOH A O   1 
HETATM 5355 O  O   . HOH H 6 .   ? 6.902   -11.501 33.906  1.00 43.71  ? 519 HOH A O   1 
HETATM 5356 O  O   . HOH H 6 .   ? -11.065 -17.499 29.754  1.00 80.28  ? 520 HOH A O   1 
HETATM 5357 O  O   . HOH H 6 .   ? -2.804  -10.233 64.862  1.00 63.58  ? 521 HOH A O   1 
HETATM 5358 O  O   . HOH H 6 .   ? -0.566  -17.183 36.774  1.00 70.04  ? 522 HOH A O   1 
HETATM 5359 O  O   . HOH H 6 .   ? 4.260   22.012  48.042  1.00 67.70  ? 523 HOH A O   1 
HETATM 5360 O  O   . HOH H 6 .   ? -3.818  -28.987 38.439  1.00 59.33  ? 524 HOH A O   1 
HETATM 5361 O  O   . HOH H 6 .   ? -11.433 -6.676  54.681  1.00 73.23  ? 525 HOH A O   1 
HETATM 5362 O  O   . HOH H 6 .   ? -7.718  -0.938  47.053  1.00 70.22  ? 526 HOH A O   1 
HETATM 5363 O  O   . HOH H 6 .   ? -8.905  -9.626  51.684  1.00 63.79  ? 527 HOH A O   1 
HETATM 5364 O  O   . HOH H 6 .   ? 11.028  16.190  48.525  1.00 89.01  ? 528 HOH A O   1 
HETATM 5365 O  O   . HOH H 6 .   ? 12.650  11.750  46.011  1.00 58.87  ? 529 HOH A O   1 
HETATM 5366 O  O   . HOH I 6 .   ? 27.584  -47.033 5.322   1.00 60.06  ? 301 HOH H O   1 
HETATM 5367 O  O   . HOH I 6 .   ? 36.676  -40.338 -20.520 1.00 54.56  ? 302 HOH H O   1 
HETATM 5368 O  O   . HOH I 6 .   ? 16.992  -22.910 -11.300 1.00 66.93  ? 303 HOH H O   1 
HETATM 5369 O  O   . HOH I 6 .   ? 2.130   -20.253 19.400  1.00 50.50  ? 304 HOH H O   1 
HETATM 5370 O  O   . HOH I 6 .   ? 26.785  -13.019 22.710  1.00 62.93  ? 305 HOH H O   1 
HETATM 5371 O  O   . HOH I 6 .   ? 26.356  -14.008 -9.653  1.00 43.96  ? 306 HOH H O   1 
HETATM 5372 O  O   . HOH I 6 .   ? 19.269  -32.330 36.228  1.00 50.47  ? 307 HOH H O   1 
HETATM 5373 O  O   . HOH I 6 .   ? 11.118  -23.570 37.984  1.00 61.49  ? 308 HOH H O   1 
HETATM 5374 O  O   . HOH I 6 .   ? 6.402   -40.888 22.870  1.00 63.41  ? 309 HOH H O   1 
HETATM 5375 O  O   . HOH I 6 .   ? 20.949  -32.355 22.159  1.00 59.51  ? 310 HOH H O   1 
HETATM 5376 O  O   . HOH I 6 .   ? 15.842  -35.436 -8.417  1.00 70.31  ? 311 HOH H O   1 
HETATM 5377 O  O   . HOH I 6 .   ? 34.595  -30.682 6.930   1.00 50.68  ? 312 HOH H O   1 
HETATM 5378 O  O   . HOH I 6 .   ? 18.422  -30.290 9.839   1.00 67.24  ? 313 HOH H O   1 
HETATM 5379 O  O   . HOH I 6 .   ? 6.040   -13.362 31.243  1.00 40.78  ? 314 HOH H O   1 
HETATM 5380 O  O   . HOH I 6 .   ? 27.491  -47.580 -3.547  1.00 53.52  ? 315 HOH H O   1 
HETATM 5381 O  O   . HOH I 6 .   ? 40.056  -37.731 -18.221 1.00 60.86  ? 316 HOH H O   1 
HETATM 5382 O  O   . HOH I 6 .   ? -3.943  -30.916 23.240  1.00 57.61  ? 317 HOH H O   1 
HETATM 5383 O  O   . HOH I 6 .   ? -2.002  -21.148 34.267  1.00 74.59  ? 318 HOH H O   1 
HETATM 5384 O  O   . HOH I 6 .   ? 18.245  -26.940 39.691  1.00 59.17  ? 319 HOH H O   1 
HETATM 5385 O  O   . HOH I 6 .   ? 7.982   -28.912 8.365   1.00 43.49  ? 320 HOH H O   1 
HETATM 5386 O  O   . HOH I 6 .   ? 18.928  -33.369 39.466  1.00 66.68  ? 321 HOH H O   1 
HETATM 5387 O  O   . HOH I 6 .   ? 12.302  -35.914 39.543  1.00 44.70  ? 322 HOH H O   1 
HETATM 5388 O  O   . HOH I 6 .   ? 14.066  -34.113 34.691  1.00 46.76  ? 323 HOH H O   1 
HETATM 5389 O  O   . HOH J 6 .   ? 27.720  -33.648 -17.824 1.00 49.16  ? 401 HOH L O   1 
HETATM 5390 O  O   . HOH J 6 .   ? 40.397  -30.776 14.993  1.00 62.09  ? 402 HOH L O   1 
HETATM 5391 O  O   . HOH J 6 .   ? 34.508  -33.291 22.463  1.00 61.34  ? 403 HOH L O   1 
HETATM 5392 O  O   . HOH J 6 .   ? 31.998  -23.602 36.405  1.00 62.12  ? 404 HOH L O   1 
HETATM 5393 O  O   . HOH J 6 .   ? 43.364  -21.931 12.497  1.00 73.03  ? 405 HOH L O   1 
HETATM 5394 O  O   . HOH J 6 .   ? 49.665  -32.742 -6.814  1.00 110.63 ? 406 HOH L O   1 
HETATM 5395 O  O   . HOH J 6 .   ? 21.985  -5.491  31.436  1.00 60.38  ? 407 HOH L O   1 
HETATM 5396 O  O   . HOH J 6 .   ? 27.201  -29.941 19.079  1.00 43.93  ? 408 HOH L O   1 
HETATM 5397 O  O   . HOH J 6 .   ? 34.081  -15.476 42.680  1.00 58.48  ? 409 HOH L O   1 
HETATM 5398 O  O   . HOH J 6 .   ? 33.704  -16.203 20.549  1.00 56.31  ? 410 HOH L O   1 
HETATM 5399 O  O   . HOH J 6 .   ? 51.053  -29.553 17.751  1.00 56.86  ? 411 HOH L O   1 
HETATM 5400 O  O   . HOH J 6 .   ? 34.762  -31.574 16.781  1.00 54.07  ? 412 HOH L O   1 
HETATM 5401 O  O   . HOH J 6 .   ? 32.663  -27.873 -12.148 1.00 53.13  ? 413 HOH L O   1 
HETATM 5402 O  O   . HOH J 6 .   ? 36.017  -11.806 -29.330 1.00 69.76  ? 414 HOH L O   1 
HETATM 5403 O  O   . HOH J 6 .   ? 37.845  -19.290 11.890  1.00 54.99  ? 415 HOH L O   1 
HETATM 5404 O  O   . HOH J 6 .   ? 28.671  -31.580 20.476  1.00 42.39  ? 416 HOH L O   1 
HETATM 5405 O  O   . HOH J 6 .   ? 37.461  -24.966 -30.058 1.00 48.07  ? 417 HOH L O   1 
HETATM 5406 O  O   . HOH J 6 .   ? 35.387  -23.459 42.893  1.00 47.13  ? 418 HOH L O   1 
HETATM 5407 O  O   . HOH J 6 .   ? 29.479  -35.035 19.756  1.00 46.44  ? 419 HOH L O   1 
HETATM 5408 O  O   . HOH J 6 .   ? 45.264  -22.620 10.677  1.00 63.55  ? 420 HOH L O   1 
HETATM 5409 O  O   . HOH J 6 .   ? 35.613  -15.100 -2.303  1.00 52.95  ? 421 HOH L O   1 
HETATM 5410 O  O   . HOH J 6 .   ? 47.382  -33.592 -5.866  1.00 72.91  ? 422 HOH L O   1 
HETATM 5411 O  O   . HOH J 6 .   ? 41.556  -13.410 22.350  1.00 42.41  ? 423 HOH L O   1 
HETATM 5412 O  O   . HOH J 6 .   ? 47.962  -36.429 9.168   1.00 48.76  ? 424 HOH L O   1 
HETATM 5413 O  O   . HOH J 6 .   ? 43.685  -15.100 17.345  1.00 61.13  ? 425 HOH L O   1 
HETATM 5414 O  O   . HOH J 6 .   ? 43.241  -35.917 0.394   1.00 46.08  ? 426 HOH L O   1 
HETATM 5415 O  O   . HOH J 6 .   ? 31.979  -13.915 43.908  1.00 64.04  ? 427 HOH L O   1 
HETATM 5416 O  O   . HOH J 6 .   ? 37.548  -12.376 -23.018 1.00 71.96  ? 428 HOH L O   1 
HETATM 5417 O  O   . HOH J 6 .   ? 34.979  -41.296 30.081  1.00 64.02  ? 429 HOH L 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   . TRP A 2   ? 0.9945 1.2431 1.2198 0.0257  -0.0861 -0.0471 46  TRP A N   
2    C CA  . TRP A 2   ? 0.9892 1.2246 1.2083 0.0323  -0.0836 -0.0364 46  TRP A CA  
3    C C   . TRP A 2   ? 0.9642 1.1859 1.1832 0.0254  -0.0756 -0.0306 46  TRP A C   
4    O O   . TRP A 2   ? 0.9529 1.1669 1.1614 0.0270  -0.0724 -0.0257 46  TRP A O   
5    C CB  . TRP A 2   ? 1.0068 1.2579 1.2395 0.0358  -0.0842 -0.0383 46  TRP A CB  
6    C CG  . TRP A 2   ? 1.0353 1.2793 1.2671 0.0438  -0.0803 -0.0340 46  TRP A CG  
7    C CD1 . TRP A 2   ? 1.0446 1.2817 1.2757 0.0390  -0.0717 -0.0355 46  TRP A CD1 
8    C CD2 . TRP A 2   ? 1.0794 1.3270 1.3177 0.0568  -0.0816 -0.0281 46  TRP A CD2 
9    N NE1 . TRP A 2   ? 1.0700 1.3020 1.3089 0.0460  -0.0653 -0.0376 46  TRP A NE1 
10   C CE2 . TRP A 2   ? 1.0906 1.3250 1.3371 0.0588  -0.0704 -0.0300 46  TRP A CE2 
11   C CE3 . TRP A 2   ? 1.0974 1.3650 1.3398 0.0665  -0.0895 -0.0199 46  TRP A CE3 
12   C CZ2 . TRP A 2   ? 1.1077 1.3384 1.3733 0.0715  -0.0639 -0.0236 46  TRP A CZ2 
13   C CZ3 . TRP A 2   ? 1.1109 1.3810 1.3689 0.0813  -0.0858 -0.0065 46  TRP A CZ3 
14   C CH2 . TRP A 2   ? 1.1142 1.3610 1.3870 0.0845  -0.0717 -0.0080 46  TRP A CH2 
15   N N   . ARG A 3   ? 0.9525 1.1763 1.1883 0.0172  -0.0703 -0.0305 47  ARG A N   
16   C CA  . ARG A 3   ? 0.9450 1.1630 1.1868 0.0124  -0.0620 -0.0176 47  ARG A CA  
17   C C   . ARG A 3   ? 0.9511 1.1508 1.1775 0.0133  -0.0622 -0.0162 47  ARG A C   
18   O O   . ARG A 3   ? 0.9577 1.1513 1.1860 0.0116  -0.0632 -0.0265 47  ARG A O   
19   C CB  . ARG A 3   ? 0.9417 1.1659 1.2182 0.0056  -0.0524 -0.0138 47  ARG A CB  
20   C CG  . ARG A 3   ? 0.9346 1.1593 1.2284 0.0028  -0.0414 0.0082  47  ARG A CG  
21   C CD  . ARG A 3   ? 0.9260 1.1746 1.2091 0.0031  -0.0417 0.0256  47  ARG A CD  
22   N NE  . ARG A 3   ? 0.9314 1.2042 1.2243 0.0013  -0.0417 0.0263  47  ARG A NE  
23   C CZ  . ARG A 3   ? 0.9288 1.2154 1.2560 -0.0016 -0.0330 0.0390  47  ARG A CZ  
24   N NH1 . ARG A 3   ? 0.9396 1.2163 1.3011 -0.0027 -0.0209 0.0526  47  ARG A NH1 
25   N NH2 . ARG A 3   ? 0.9134 1.2236 1.2458 -0.0034 -0.0339 0.0382  47  ARG A NH2 
26   N N   . GLN A 4   ? 0.9511 1.1478 1.1628 0.0140  -0.0605 -0.0061 48  GLN A N   
27   C CA  . GLN A 4   ? 0.9608 1.1411 1.1559 0.0150  -0.0606 -0.0040 48  GLN A CA  
28   C C   . GLN A 4   ? 0.9705 1.1394 1.1467 0.0213  -0.0682 -0.0140 48  GLN A C   
29   O O   . GLN A 4   ? 0.9716 1.1291 1.1380 0.0214  -0.0692 -0.0155 48  GLN A O   
30   C CB  . GLN A 4   ? 0.9654 1.1381 1.1790 0.0107  -0.0533 0.0014  48  GLN A CB  
31   C CG  . GLN A 4   ? 0.9722 1.1599 1.2077 0.0076  -0.0438 0.0231  48  GLN A CG  
32   C CD  . GLN A 4   ? 0.9853 1.1619 1.2436 0.0059  -0.0335 0.0332  48  GLN A CD  
33   O OE1 . GLN A 4   ? 1.0063 1.1699 1.2894 0.0029  -0.0266 0.0220  48  GLN A OE1 
34   N NE2 . GLN A 4   ? 0.9796 1.1653 1.2334 0.0065  -0.0304 0.0523  48  GLN A NE2 
35   N N   . GLN A 5   ? 0.9804 1.1563 1.1550 0.0270  -0.0722 -0.0179 49  GLN A N   
36   C CA  . GLN A 5   ? 0.9859 1.1565 1.1488 0.0359  -0.0767 -0.0176 49  GLN A CA  
37   C C   . GLN A 5   ? 0.9914 1.1480 1.1466 0.0378  -0.0700 -0.0146 49  GLN A C   
38   O O   . GLN A 5   ? 1.0028 1.1656 1.1656 0.0346  -0.0637 -0.0186 49  GLN A O   
39   C CB  . GLN A 5   ? 0.9875 1.1752 1.1616 0.0426  -0.0811 -0.0191 49  GLN A CB  
40   C CG  . GLN A 5   ? 1.0066 1.1956 1.1786 0.0549  -0.0833 -0.0097 49  GLN A CG  
41   C CD  . GLN A 5   ? 1.0234 1.2352 1.2117 0.0632  -0.0869 -0.0062 49  GLN A CD  
42   O OE1 . GLN A 5   ? 1.0180 1.2457 1.2153 0.0583  -0.0897 -0.0147 49  GLN A OE1 
43   N NE2 . GLN A 5   ? 1.0467 1.2619 1.2436 0.0766  -0.0853 0.0089  49  GLN A NE2 
44   N N   . TRP A 6   ? 0.9872 1.1290 1.1293 0.0411  -0.0698 -0.0102 50  TRP A N   
45   C CA  . TRP A 6   ? 0.9836 1.1112 1.1219 0.0409  -0.0607 -0.0107 50  TRP A CA  
46   C C   . TRP A 6   ? 0.9803 1.0972 1.1237 0.0528  -0.0582 -0.0027 50  TRP A C   
47   O O   . TRP A 6   ? 0.9796 1.1067 1.1230 0.0609  -0.0663 0.0069  50  TRP A O   
48   C CB  . TRP A 6   ? 0.9838 1.1037 1.1071 0.0334  -0.0591 -0.0097 50  TRP A CB  
49   C CG  . TRP A 6   ? 0.9796 1.1141 1.1063 0.0246  -0.0594 -0.0083 50  TRP A CG  
50   C CD1 . TRP A 6   ? 0.9843 1.1169 1.1114 0.0216  -0.0614 -0.0029 50  TRP A CD1 
51   C CD2 . TRP A 6   ? 0.9756 1.1333 1.1125 0.0178  -0.0550 -0.0094 50  TRP A CD2 
52   N NE1 . TRP A 6   ? 0.9758 1.1258 1.1171 0.0157  -0.0575 0.0041  50  TRP A NE1 
53   C CE2 . TRP A 6   ? 0.9721 1.1416 1.1167 0.0131  -0.0550 0.0017  50  TRP A CE2 
54   C CE3 . TRP A 6   ? 0.9746 1.1480 1.1189 0.0146  -0.0492 -0.0187 50  TRP A CE3 
55   C CZ2 . TRP A 6   ? 0.9553 1.1560 1.1126 0.0068  -0.0510 0.0097  50  TRP A CZ2 
56   C CZ3 . TRP A 6   ? 0.9625 1.1690 1.1145 0.0059  -0.0463 -0.0167 50  TRP A CZ3 
57   C CH2 . TRP A 6   ? 0.9562 1.1783 1.1136 0.0027  -0.0480 0.0002  50  TRP A CH2 
58   N N   . SER A 7   ? 0.9803 1.0824 1.1325 0.0527  -0.0449 -0.0064 51  SER A N   
59   C CA  . SER A 7   ? 1.0119 1.1013 1.1825 0.0652  -0.0362 0.0046  51  SER A CA  
60   C C   . SER A 7   ? 1.0311 1.1058 1.1878 0.0675  -0.0357 0.0149  51  SER A C   
61   O O   . SER A 7   ? 1.0488 1.1266 1.2103 0.0798  -0.0384 0.0352  51  SER A O   
62   C CB  . SER A 7   ? 1.0197 1.0998 1.2195 0.0627  -0.0164 -0.0089 51  SER A CB  
63   O OG  . SER A 7   ? 1.0078 1.1054 1.2179 0.0579  -0.0166 -0.0212 51  SER A OG  
64   N N   . GLY A 8   ? 1.0338 1.0989 1.1746 0.0556  -0.0320 0.0030  52  GLY A N   
65   C CA  . GLY A 8   ? 1.0418 1.0921 1.1691 0.0560  -0.0303 0.0100  52  GLY A CA  
66   C C   . GLY A 8   ? 1.0472 1.1080 1.1526 0.0592  -0.0463 0.0219  52  GLY A C   
67   O O   . GLY A 8   ? 1.0289 1.1075 1.1291 0.0572  -0.0572 0.0192  52  GLY A O   
68   N N   . PRO A 9   ? 1.0620 1.1150 1.1568 0.0625  -0.0460 0.0326  53  PRO A N   
69   C CA  . PRO A 9   ? 1.0524 1.1226 1.1276 0.0625  -0.0589 0.0389  53  PRO A CA  
70   C C   . PRO A 9   ? 1.0316 1.1022 1.0917 0.0497  -0.0641 0.0231  53  PRO A C   
71   O O   . PRO A 9   ? 1.0292 1.0865 1.0882 0.0424  -0.0581 0.0147  53  PRO A O   
72   C CB  . PRO A 9   ? 1.0712 1.1320 1.1405 0.0673  -0.0540 0.0531  53  PRO A CB  
73   C CG  . PRO A 9   ? 1.0872 1.1253 1.1829 0.0738  -0.0368 0.0589  53  PRO A CG  
74   C CD  . PRO A 9   ? 1.0796 1.1100 1.1838 0.0646  -0.0312 0.0368  53  PRO A CD  
75   N N   . GLY A 10  ? 1.0157 1.1071 1.0692 0.0466  -0.0731 0.0194  54  GLY A N   
76   C CA  . GLY A 10  ? 1.0012 1.0919 1.0531 0.0355  -0.0736 0.0056  54  GLY A CA  
77   C C   . GLY A 10  ? 1.0057 1.0803 1.0455 0.0308  -0.0694 0.0051  54  GLY A C   
78   O O   . GLY A 10  ? 1.0169 1.0814 1.0463 0.0353  -0.0670 0.0138  54  GLY A O   
79   N N   . THR A 11  ? 0.9909 1.0633 1.0375 0.0224  -0.0664 -0.0036 55  THR A N   
80   C CA  . THR A 11  ? 0.9833 1.0430 1.0231 0.0180  -0.0616 -0.0038 55  THR A CA  
81   C C   . THR A 11  ? 0.9925 1.0595 1.0160 0.0183  -0.0649 -0.0053 55  THR A C   
82   O O   . THR A 11  ? 0.9970 1.0889 1.0203 0.0172  -0.0699 -0.0114 55  THR A O   
83   C CB  . THR A 11  ? 0.9735 1.0332 1.0354 0.0107  -0.0550 -0.0099 55  THR A CB  
84   O OG1 . THR A 11  ? 0.9579 1.0199 1.0356 0.0114  -0.0523 -0.0020 55  THR A OG1 
85   C CG2 . THR A 11  ? 0.9700 1.0183 1.0305 0.0072  -0.0487 -0.0078 55  THR A CG2 
86   N N   . THR A 12  ? 0.9998 1.0519 1.0097 0.0188  -0.0617 0.0003  56  THR A N   
87   C CA  . THR A 12  ? 1.0169 1.0781 1.0106 0.0191  -0.0639 0.0024  56  THR A CA  
88   C C   . THR A 12  ? 1.0217 1.1031 1.0199 0.0089  -0.0636 -0.0155 56  THR A C   
89   O O   . THR A 12  ? 1.0117 1.0834 1.0276 0.0020  -0.0568 -0.0268 56  THR A O   
90   C CB  . THR A 12  ? 1.0165 1.0553 0.9983 0.0199  -0.0584 0.0099  56  THR A CB  
91   O OG1 . THR A 12  ? 0.9988 1.0216 0.9846 0.0252  -0.0542 0.0181  56  THR A OG1 
92   C CG2 . THR A 12  ? 1.0286 1.0779 0.9946 0.0218  -0.0600 0.0172  56  THR A CG2 
93   N N   . LYS A 13  ? 1.0371 1.1524 1.0243 0.0072  -0.0689 -0.0178 57  LYS A N   
94   C CA  . LYS A 13  ? 1.0570 1.2026 1.0498 -0.0065 -0.0664 -0.0424 57  LYS A CA  
95   C C   . LYS A 13  ? 1.0614 1.1868 1.0548 -0.0135 -0.0575 -0.0515 57  LYS A C   
96   O O   . LYS A 13  ? 1.0720 1.1833 1.0469 -0.0083 -0.0584 -0.0367 57  LYS A O   
97   C CB  . LYS A 13  ? 1.0772 1.2782 1.0541 -0.0080 -0.0746 -0.0399 57  LYS A CB  
98   C CG  . LYS A 13  ? 1.0914 1.3227 1.0720 -0.0013 -0.0830 -0.0299 57  LYS A CG  
99   C CD  . LYS A 13  ? 1.1137 1.4108 1.0798 -0.0001 -0.0915 -0.0170 57  LYS A CD  
100  C CE  . LYS A 13  ? 1.1207 1.4501 1.0943 0.0090  -0.0995 -0.0013 57  LYS A CE  
101  N NZ  . LYS A 13  ? 1.1433 1.5472 1.1058 0.0125  -0.1078 0.0206  57  LYS A NZ  
102  N N   . ARG A 14  ? 1.0634 1.1871 1.0836 -0.0251 -0.0466 -0.0756 58  ARG A N   
103  C CA  . ARG A 14  ? 1.0683 1.1719 1.1001 -0.0311 -0.0349 -0.0841 58  ARG A CA  
104  C C   . ARG A 14  ? 1.0280 1.0933 1.0539 -0.0201 -0.0351 -0.0588 58  ARG A C   
105  O O   . ARG A 14  ? 1.0192 1.0745 1.0277 -0.0187 -0.0349 -0.0516 58  ARG A O   
106  C CB  . ARG A 14  ? 1.1076 1.2399 1.1201 -0.0399 -0.0352 -0.0968 58  ARG A CB  
107  C CG  . ARG A 14  ? 1.1440 1.3229 1.1724 -0.0581 -0.0286 -0.1331 58  ARG A CG  
108  C CD  . ARG A 14  ? 1.1854 1.4137 1.1855 -0.0664 -0.0337 -0.1407 58  ARG A CD  
109  N NE  . ARG A 14  ? 1.2155 1.4828 1.1866 -0.0578 -0.0504 -0.1176 58  ARG A NE  
110  C CZ  . ARG A 14  ? 1.2365 1.5065 1.1784 -0.0454 -0.0600 -0.0849 58  ARG A CZ  
111  N NH1 . ARG A 14  ? 1.2408 1.4764 1.1730 -0.0417 -0.0560 -0.0749 58  ARG A NH1 
112  N NH2 . ARG A 14  ? 1.2468 1.5553 1.1743 -0.0363 -0.0717 -0.0604 58  ARG A NH2 
113  N N   . PHE A 15  ? 0.9983 1.0489 1.0391 -0.0139 -0.0348 -0.0469 59  PHE A N   
114  C CA  . PHE A 15  ? 0.9858 1.0151 1.0236 -0.0069 -0.0341 -0.0263 59  PHE A CA  
115  C C   . PHE A 15  ? 0.9798 0.9988 1.0416 -0.0102 -0.0218 -0.0250 59  PHE A C   
116  O O   . PHE A 15  ? 0.9718 0.9825 1.0209 -0.0079 -0.0215 -0.0135 59  PHE A O   
117  C CB  . PHE A 15  ? 0.9678 0.9974 1.0153 -0.0017 -0.0369 -0.0156 59  PHE A CB  
118  C CG  . PHE A 15  ? 0.9407 0.9645 0.9881 0.0017  -0.0349 0.0019  59  PHE A CG  
119  C CD1 . PHE A 15  ? 0.9360 0.9540 0.9576 0.0035  -0.0378 0.0076  59  PHE A CD1 
120  C CD2 . PHE A 15  ? 0.9225 0.9538 0.9993 0.0018  -0.0284 0.0132  59  PHE A CD2 
121  C CE1 . PHE A 15  ? 0.9312 0.9557 0.9531 0.0027  -0.0348 0.0179  59  PHE A CE1 
122  C CE2 . PHE A 15  ? 0.9154 0.9582 0.9907 0.0029  -0.0271 0.0300  59  PHE A CE2 
123  C CZ  . PHE A 15  ? 0.9192 0.9609 0.9655 0.0019  -0.0306 0.0294  59  PHE A CZ  
124  N N   . PRO A 16  ? 0.9794 0.9999 1.0824 -0.0157 -0.0091 -0.0358 60  PRO A N   
125  C CA  . PRO A 16  ? 0.9772 0.9883 1.1143 -0.0170 0.0063  -0.0307 60  PRO A CA  
126  C C   . PRO A 16  ? 0.9845 0.9921 1.1061 -0.0219 0.0088  -0.0419 60  PRO A C   
127  O O   . PRO A 16  ? 0.9724 0.9722 1.0974 -0.0185 0.0132  -0.0270 60  PRO A O   
128  C CB  . PRO A 16  ? 0.9815 0.9940 1.1728 -0.0235 0.0233  -0.0469 60  PRO A CB  
129  C CG  . PRO A 16  ? 0.9789 1.0018 1.1629 -0.0229 0.0142  -0.0507 60  PRO A CG  
130  C CD  . PRO A 16  ? 0.9793 1.0113 1.1058 -0.0209 -0.0056 -0.0529 60  PRO A CD  
131  N N   . GLU A 17  ? 0.9986 1.0193 1.1034 -0.0306 0.0059  -0.0676 61  GLU A N   
132  C CA  . GLU A 17  ? 1.0162 1.0411 1.1052 -0.0372 0.0084  -0.0807 61  GLU A CA  
133  C C   . GLU A 17  ? 1.0062 1.0225 1.0517 -0.0292 -0.0039 -0.0593 61  GLU A C   
134  O O   . GLU A 17  ? 1.0156 1.0248 1.0561 -0.0306 0.0005  -0.0580 61  GLU A O   
135  C CB  . GLU A 17  ? 1.0441 1.1014 1.1208 -0.0494 0.0062  -0.1104 61  GLU A CB  
136  C CG  . GLU A 17  ? 1.0662 1.1369 1.1910 -0.0636 0.0243  -0.1439 61  GLU A CG  
137  C CD  . GLU A 17  ? 1.0837 1.1591 1.2305 -0.0630 0.0244  -0.1465 61  GLU A CD  
138  O OE1 . GLU A 17  ? 1.0857 1.1531 1.2099 -0.0504 0.0095  -0.1202 61  GLU A OE1 
139  O OE2 . GLU A 17  ? 1.1130 1.2011 1.3026 -0.0766 0.0414  -0.1777 61  GLU A OE2 
140  N N   . THR A 18  ? 0.9807 0.9977 1.0001 -0.0215 -0.0170 -0.0445 62  THR A N   
141  C CA  . THR A 18  ? 0.9628 0.9710 0.9489 -0.0154 -0.0246 -0.0281 62  THR A CA  
142  C C   . THR A 18  ? 0.9486 0.9423 0.9419 -0.0125 -0.0197 -0.0137 62  THR A C   
143  O O   . THR A 18  ? 0.9700 0.9574 0.9469 -0.0131 -0.0187 -0.0095 62  THR A O   
144  C CB  . THR A 18  ? 0.9535 0.9655 0.9234 -0.0085 -0.0345 -0.0181 62  THR A CB  
145  O OG1 . THR A 18  ? 0.9587 0.9957 0.9206 -0.0110 -0.0398 -0.0271 62  THR A OG1 
146  C CG2 . THR A 18  ? 0.9563 0.9554 0.9047 -0.0030 -0.0364 -0.0033 62  THR A CG2 
147  N N   . VAL A 19  ? 0.9285 0.9241 0.9472 -0.0100 -0.0164 -0.0048 63  VAL A N   
148  C CA  . VAL A 19  ? 0.9150 0.9143 0.9412 -0.0078 -0.0129 0.0126  63  VAL A CA  
149  C C   . VAL A 19  ? 0.9142 0.9117 0.9573 -0.0100 -0.0030 0.0145  63  VAL A C   
150  O O   . VAL A 19  ? 0.9120 0.9134 0.9432 -0.0102 -0.0026 0.0236  63  VAL A O   
151  C CB  . VAL A 19  ? 0.8993 0.9125 0.9525 -0.0046 -0.0110 0.0261  63  VAL A CB  
152  C CG1 . VAL A 19  ? 0.8883 0.9227 0.9547 -0.0034 -0.0064 0.0481  63  VAL A CG1 
153  C CG2 . VAL A 19  ? 0.9010 0.9170 0.9372 -0.0029 -0.0201 0.0235  63  VAL A CG2 
154  N N   . LEU A 20  ? 0.9170 0.9104 0.9917 -0.0128 0.0068  0.0032  64  LEU A N   
155  C CA  . LEU A 20  ? 0.9225 0.9123 1.0232 -0.0149 0.0200  0.0023  64  LEU A CA  
156  C C   . LEU A 20  ? 0.9223 0.9064 0.9866 -0.0195 0.0157  -0.0097 64  LEU A C   
157  O O   . LEU A 20  ? 0.9183 0.9022 0.9822 -0.0188 0.0195  -0.0001 64  LEU A O   
158  C CB  . LEU A 20  ? 0.9376 0.9234 1.0859 -0.0198 0.0356  -0.0157 64  LEU A CB  
159  C CG  . LEU A 20  ? 0.9340 0.9231 1.1347 -0.0145 0.0467  0.0008  64  LEU A CG  
160  C CD1 . LEU A 20  ? 0.9429 0.9254 1.1945 -0.0225 0.0659  -0.0254 64  LEU A CD1 
161  C CD2 . LEU A 20  ? 0.9286 0.9270 1.1611 -0.0058 0.0556  0.0360  64  LEU A CD2 
162  N N   . ALA A 21  ? 0.9126 0.8978 0.9485 -0.0241 0.0080  -0.0279 65  ALA A N   
163  C CA  . ALA A 21  ? 0.9077 0.8936 0.9105 -0.0283 0.0043  -0.0362 65  ALA A CA  
164  C C   . ALA A 21  ? 0.9097 0.8876 0.8854 -0.0237 -0.0011 -0.0183 65  ALA A C   
165  O O   . ALA A 21  ? 0.9307 0.9052 0.8955 -0.0264 0.0019  -0.0191 65  ALA A O   
166  C CB  . ALA A 21  ? 0.9109 0.9118 0.8899 -0.0315 -0.0043 -0.0481 65  ALA A CB  
167  N N   . ARG A 22  ? 0.8982 0.8754 0.8659 -0.0186 -0.0075 -0.0059 66  ARG A N   
168  C CA  . ARG A 22  ? 0.8895 0.8639 0.8381 -0.0177 -0.0090 0.0041  66  ARG A CA  
169  C C   . ARG A 22  ? 0.8740 0.8586 0.8387 -0.0190 -0.0025 0.0138  66  ARG A C   
170  O O   . ARG A 22  ? 0.8763 0.8616 0.8265 -0.0222 -0.0005 0.0151  66  ARG A O   
171  C CB  . ARG A 22  ? 0.8830 0.8598 0.8272 -0.0146 -0.0138 0.0092  66  ARG A CB  
172  C CG  . ARG A 22  ? 0.8890 0.8586 0.8181 -0.0113 -0.0192 0.0063  66  ARG A CG  
173  C CD  . ARG A 22  ? 0.8847 0.8546 0.8157 -0.0084 -0.0205 0.0101  66  ARG A CD  
174  N NE  . ARG A 22  ? 0.8931 0.8584 0.8178 -0.0028 -0.0241 0.0127  66  ARG A NE  
175  C CZ  . ARG A 22  ? 0.8836 0.8447 0.8130 0.0005  -0.0221 0.0156  66  ARG A CZ  
176  N NH1 . ARG A 22  ? 0.8591 0.8228 0.7960 -0.0040 -0.0165 0.0110  66  ARG A NH1 
177  N NH2 . ARG A 22  ? 0.8924 0.8529 0.8220 0.0078  -0.0243 0.0234  66  ARG A NH2 
178  N N   . CYS A 23  ? 0.8633 0.8598 0.8616 -0.0162 0.0018  0.0230  67  CYS A N   
179  C CA  . CYS A 23  ? 0.8657 0.8834 0.8867 -0.0151 0.0084  0.0411  67  CYS A CA  
180  C C   . CYS A 23  ? 0.8681 0.8786 0.8964 -0.0169 0.0161  0.0377  67  CYS A C   
181  O O   . CYS A 23  ? 0.8499 0.8766 0.8761 -0.0181 0.0185  0.0483  67  CYS A O   
182  C CB  . CYS A 23  ? 0.8635 0.8967 0.9281 -0.0096 0.0142  0.0581  67  CYS A CB  
183  S SG  . CYS A 23  ? 0.8720 0.9518 0.9652 -0.0060 0.0203  0.0931  67  CYS A SG  
184  N N   . VAL A 24  ? 0.8819 0.8738 0.9197 -0.0188 0.0209  0.0205  68  VAL A N   
185  C CA  . VAL A 24  ? 0.8866 0.8718 0.9319 -0.0224 0.0296  0.0111  68  VAL A CA  
186  C C   . VAL A 24  ? 0.8877 0.8681 0.8875 -0.0267 0.0225  0.0056  68  VAL A C   
187  O O   . VAL A 24  ? 0.8912 0.8759 0.8911 -0.0281 0.0271  0.0105  68  VAL A O   
188  C CB  . VAL A 24  ? 0.8975 0.8729 0.9612 -0.0279 0.0374  -0.0139 68  VAL A CB  
189  C CG1 . VAL A 24  ? 0.9059 0.8780 0.9714 -0.0346 0.0464  -0.0299 68  VAL A CG1 
190  C CG2 . VAL A 24  ? 0.8946 0.8712 1.0150 -0.0251 0.0505  -0.0110 68  VAL A CG2 
191  N N   . LYS A 25  ? 0.8781 0.8510 0.8443 -0.0280 0.0129  -0.0021 69  LYS A N   
192  C CA  . LYS A 25  ? 0.8775 0.8432 0.8081 -0.0311 0.0092  -0.0052 69  LYS A CA  
193  C C   . LYS A 25  ? 0.8611 0.8326 0.7833 -0.0320 0.0100  0.0049  69  LYS A C   
194  O O   . LYS A 25  ? 0.8626 0.8304 0.7690 -0.0361 0.0129  0.0027  69  LYS A O   
195  C CB  . LYS A 25  ? 0.8903 0.8515 0.7998 -0.0295 0.0016  -0.0084 69  LYS A CB  
196  C CG  . LYS A 25  ? 0.9066 0.8608 0.7881 -0.0305 0.0008  -0.0055 69  LYS A CG  
197  C CD  . LYS A 25  ? 0.9221 0.8800 0.7918 -0.0266 -0.0050 -0.0014 69  LYS A CD  
198  C CE  . LYS A 25  ? 0.9463 0.8973 0.7991 -0.0248 -0.0023 0.0099  69  LYS A CE  
199  N NZ  . LYS A 25  ? 0.9606 0.9239 0.8084 -0.0187 -0.0070 0.0217  69  LYS A NZ  
200  N N   . TYR A 26  ? 0.8519 0.8381 0.7854 -0.0301 0.0084  0.0139  70  TYR A N   
201  C CA  . TYR A 26  ? 0.8444 0.8494 0.7708 -0.0350 0.0101  0.0179  70  TYR A CA  
202  C C   . TYR A 26  ? 0.8447 0.8734 0.7845 -0.0371 0.0155  0.0272  70  TYR A C   
203  O O   . TYR A 26  ? 0.8285 0.8686 0.7550 -0.0443 0.0186  0.0233  70  TYR A O   
204  C CB  . TYR A 26  ? 0.8226 0.8479 0.7577 -0.0344 0.0072  0.0230  70  TYR A CB  
205  C CG  . TYR A 26  ? 0.8053 0.8614 0.7339 -0.0438 0.0108  0.0199  70  TYR A CG  
206  C CD1 . TYR A 26  ? 0.7886 0.8901 0.7296 -0.0477 0.0132  0.0319  70  TYR A CD1 
207  C CD2 . TYR A 26  ? 0.8047 0.8503 0.7195 -0.0501 0.0141  0.0040  70  TYR A CD2 
208  C CE1 . TYR A 26  ? 0.7807 0.9241 0.7152 -0.0602 0.0173  0.0242  70  TYR A CE1 
209  C CE2 . TYR A 26  ? 0.7974 0.8755 0.7110 -0.0629 0.0214  -0.0074 70  TYR A CE2 
210  C CZ  . TYR A 26  ? 0.7836 0.9146 0.7042 -0.0695 0.0221  0.0004  70  TYR A CZ  
211  O OH  . TYR A 26  ? 0.7800 0.9565 0.6988 -0.0859 0.0299  -0.0152 70  TYR A OH  
212  N N   . THR A 27  ? 0.8502 0.8881 0.8221 -0.0310 0.0186  0.0402  71  THR A N   
213  C CA  . THR A 27  ? 0.8523 0.9167 0.8475 -0.0299 0.0255  0.0561  71  THR A CA  
214  C C   . THR A 27  ? 0.8661 0.9116 0.8489 -0.0336 0.0297  0.0443  71  THR A C   
215  O O   . THR A 27  ? 0.8629 0.9312 0.8496 -0.0360 0.0337  0.0525  71  THR A O   
216  C CB  . THR A 27  ? 0.8439 0.9177 0.8889 -0.0205 0.0327  0.0758  71  THR A CB  
217  O OG1 . THR A 27  ? 0.8521 0.8885 0.9060 -0.0192 0.0360  0.0582  71  THR A OG1 
218  C CG2 . THR A 27  ? 0.8388 0.9438 0.9000 -0.0167 0.0296  0.0952  71  THR A CG2 
219  N N   . GLU A 28  ? 0.8740 0.8851 0.8420 -0.0347 0.0287  0.0260  72  GLU A N   
220  C CA  . GLU A 28  ? 0.8816 0.8780 0.8337 -0.0394 0.0322  0.0137  72  GLU A CA  
221  C C   . GLU A 28  ? 0.8956 0.8936 0.8152 -0.0460 0.0301  0.0103  72  GLU A C   
222  O O   . GLU A 28  ? 0.9275 0.9300 0.8424 -0.0502 0.0347  0.0089  72  GLU A O   
223  C CB  . GLU A 28  ? 0.8796 0.8542 0.8215 -0.0408 0.0308  -0.0036 72  GLU A CB  
224  C CG  . GLU A 28  ? 0.8723 0.8466 0.8529 -0.0395 0.0395  -0.0103 72  GLU A CG  
225  C CD  . GLU A 28  ? 0.8747 0.8429 0.8477 -0.0443 0.0385  -0.0320 72  GLU A CD  
226  O OE1 . GLU A 28  ? 0.8581 0.8246 0.7951 -0.0458 0.0287  -0.0346 72  GLU A OE1 
227  O OE2 . GLU A 28  ? 0.8806 0.8506 0.8886 -0.0474 0.0496  -0.0462 72  GLU A OE2 
228  N N   . ILE A 29  ? 0.8896 0.8835 0.7920 -0.0475 0.0255  0.0073  73  ILE A N   
229  C CA  . ILE A 29  ? 0.8928 0.8838 0.7740 -0.0551 0.0287  0.0000  73  ILE A CA  
230  C C   . ILE A 29  ? 0.8953 0.9247 0.7840 -0.0623 0.0324  0.0024  73  ILE A C   
231  O O   . ILE A 29  ? 0.8975 0.9341 0.7769 -0.0709 0.0385  -0.0049 73  ILE A O   
232  C CB  . ILE A 29  ? 0.8866 0.8593 0.7577 -0.0540 0.0271  -0.0047 73  ILE A CB  
233  C CG1 . ILE A 29  ? 0.8897 0.8393 0.7527 -0.0475 0.0227  -0.0035 73  ILE A CG1 
234  C CG2 . ILE A 29  ? 0.9006 0.8688 0.7633 -0.0628 0.0366  -0.0142 73  ILE A CG2 
235  C CD1 . ILE A 29  ? 0.8929 0.8308 0.7533 -0.0430 0.0204  -0.0013 73  ILE A CD1 
236  N N   . HIS A 30  ? 0.9128 0.9735 0.8191 -0.0597 0.0291  0.0135  74  HIS A N   
237  C CA  . HIS A 30  ? 0.9283 1.0435 0.8419 -0.0678 0.0315  0.0184  74  HIS A CA  
238  C C   . HIS A 30  ? 0.9284 1.0777 0.8689 -0.0610 0.0319  0.0430  74  HIS A C   
239  O O   . HIS A 30  ? 0.9067 1.0677 0.8728 -0.0514 0.0298  0.0624  74  HIS A O   
240  C CB  . HIS A 30  ? 0.9333 1.0723 0.8491 -0.0713 0.0293  0.0157  74  HIS A CB  
241  C CG  . HIS A 30  ? 0.9587 1.0687 0.8581 -0.0788 0.0339  -0.0081 74  HIS A CG  
242  N ND1 . HIS A 30  ? 0.9712 1.1094 0.8671 -0.0951 0.0433  -0.0286 74  HIS A ND1 
243  C CD2 . HIS A 30  ? 0.9735 1.0328 0.8653 -0.0725 0.0332  -0.0140 74  HIS A CD2 
244  C CE1 . HIS A 30  ? 0.9979 1.0957 0.8901 -0.0972 0.0504  -0.0455 74  HIS A CE1 
245  N NE2 . HIS A 30  ? 0.9894 1.0410 0.8781 -0.0822 0.0432  -0.0333 74  HIS A NE2 
246  N N   . PRO A 31  ? 0.9796 1.1436 0.9966 0.0308  0.0781  0.1147  75  PRO A N   
247  C CA  . PRO A 31  ? 0.9836 1.1680 0.9902 0.0413  0.0788  0.1174  75  PRO A CA  
248  C C   . PRO A 31  ? 0.9944 1.1918 0.9968 0.0464  0.0793  0.1127  75  PRO A C   
249  O O   . PRO A 31  ? 0.9887 1.1977 0.9837 0.0593  0.0824  0.1184  75  PRO A O   
250  C CB  . PRO A 31  ? 0.9838 1.1935 0.9947 0.0352  0.0788  0.1217  75  PRO A CB  
251  C CG  . PRO A 31  ? 0.9877 1.1941 1.0125 0.0184  0.0790  0.1158  75  PRO A CG  
252  C CD  . PRO A 31  ? 0.9874 1.1602 1.0167 0.0178  0.0795  0.1157  75  PRO A CD  
253  N N   . GLU A 32  ? 1.0139 1.2110 1.0222 0.0367  0.0780  0.1030  76  GLU A N   
254  C CA  . GLU A 32  ? 1.0253 1.2423 1.0293 0.0400  0.0781  0.0985  76  GLU A CA  
255  C C   . GLU A 32  ? 1.0324 1.2265 1.0292 0.0514  0.0802  0.1000  76  GLU A C   
256  O O   . GLU A 32  ? 1.0310 1.2411 1.0222 0.0593  0.0819  0.1019  76  GLU A O   
257  C CB  . GLU A 32  ? 1.0308 1.2613 1.0443 0.0227  0.0774  0.0836  76  GLU A CB  
258  C CG  . GLU A 32  ? 1.0393 1.2356 1.0606 0.0145  0.0790  0.0739  76  GLU A CG  
259  C CD  . GLU A 32  ? 1.0399 1.2077 1.0732 0.0072  0.0811  0.0764  76  GLU A CD  
260  O OE1 . GLU A 32  ? 1.0357 1.2090 1.0694 0.0079  0.0806  0.0859  76  GLU A OE1 
261  O OE2 . GLU A 32  ? 1.0469 1.1890 1.0899 0.0018  0.0841  0.0704  76  GLU A OE2 
262  N N   . MET A 33  ? 1.0426 1.2033 1.0400 0.0520  0.0807  0.1001  77  MET A N   
263  C CA  . MET A 33  ? 1.0456 1.1842 1.0380 0.0596  0.0833  0.0990  77  MET A CA  
264  C C   . MET A 33  ? 1.0420 1.1697 1.0280 0.0706  0.0883  0.1057  77  MET A C   
265  O O   . MET A 33  ? 1.0288 1.1354 1.0125 0.0738  0.0916  0.1029  77  MET A O   
266  C CB  . MET A 33  ? 1.0586 1.1727 1.0584 0.0515  0.0812  0.0923  77  MET A CB  
267  C CG  . MET A 33  ? 1.0813 1.1979 1.0882 0.0421  0.0804  0.0817  77  MET A CG  
268  S SD  . MET A 33  ? 1.1013 1.2285 1.0996 0.0487  0.0826  0.0777  77  MET A SD  
269  C CE  . MET A 33  ? 1.1042 1.2779 1.1006 0.0456  0.0814  0.0774  77  MET A CE  
270  N N   . ARG A 34  ? 1.0452 1.1885 1.0293 0.0755  0.0905  0.1125  78  ARG A N   
271  C CA  . ARG A 34  ? 1.0422 1.1757 1.0223 0.0839  0.0978  0.1153  78  ARG A CA  
272  C C   . ARG A 34  ? 1.0368 1.1642 1.0135 0.0978  0.1086  0.1194  78  ARG A C   
273  O O   . ARG A 34  ? 1.0410 1.1521 1.0165 0.1036  0.1186  0.1180  78  ARG A O   
274  C CB  . ARG A 34  ? 1.0451 1.1977 1.0256 0.0848  0.0982  0.1208  78  ARG A CB  
275  C CG  . ARG A 34  ? 1.0338 1.1893 1.0181 0.0726  0.0910  0.1198  78  ARG A CG  
276  C CD  . ARG A 34  ? 1.0476 1.2196 1.0308 0.0744  0.0933  0.1246  78  ARG A CD  
277  N NE  . ARG A 34  ? 1.0448 1.2289 1.0336 0.0633  0.0870  0.1280  78  ARG A NE  
278  C CZ  . ARG A 34  ? 1.0367 1.2178 1.0265 0.0576  0.0851  0.1302  78  ARG A CZ  
279  N NH1 . ARG A 34  ? 1.0372 1.2082 1.0219 0.0603  0.0873  0.1267  78  ARG A NH1 
280  N NH2 . ARG A 34  ? 1.0380 1.2296 1.0348 0.0487  0.0818  0.1364  78  ARG A NH2 
281  N N   . HIS A 35  ? 1.0265 1.1694 1.0030 0.1025  0.1081  0.1245  79  HIS A N   
282  C CA  . HIS A 35  ? 1.0331 1.1731 1.0080 0.1175  0.1195  0.1333  79  HIS A CA  
283  C C   . HIS A 35  ? 1.0310 1.1384 1.0050 0.1160  0.1246  0.1261  79  HIS A C   
284  O O   . HIS A 35  ? 1.0314 1.1247 1.0060 0.1273  0.1383  0.1319  79  HIS A O   
285  C CB  . HIS A 35  ? 1.0262 1.2015 1.0004 0.1220  0.1161  0.1416  79  HIS A CB  
286  C CG  . HIS A 35  ? 1.0033 1.1809 0.9767 0.1096  0.1072  0.1310  79  HIS A CG  
287  N ND1 . HIS A 35  ? 1.0000 1.1605 0.9713 0.1119  0.1111  0.1292  79  HIS A ND1 
288  C CD2 . HIS A 35  ? 0.9849 1.1789 0.9608 0.0945  0.0969  0.1206  79  HIS A CD2 
289  C CE1 . HIS A 35  ? 0.9897 1.1576 0.9618 0.0992  0.1026  0.1178  79  HIS A CE1 
290  N NE2 . HIS A 35  ? 0.9817 1.1682 0.9574 0.0882  0.0949  0.1118  79  HIS A NE2 
291  N N   . VAL A 36  ? 1.0276 1.1239 1.0021 0.1024  0.1152  0.1144  80  VAL A N   
292  C CA  . VAL A 36  ? 1.0293 1.1008 1.0038 0.0993  0.1181  0.1065  80  VAL A CA  
293  C C   . VAL A 36  ? 1.0328 1.0832 1.0076 0.0994  0.1276  0.1007  80  VAL A C   
294  O O   . VAL A 36  ? 1.0262 1.0797 1.0013 0.0933  0.1238  0.0962  80  VAL A O   
295  C CB  . VAL A 36  ? 1.0212 1.0905 0.9985 0.0864  0.1063  0.0973  80  VAL A CB  
296  C CG1 . VAL A 36  ? 1.0224 1.0697 1.0008 0.0829  0.1086  0.0891  80  VAL A CG1 
297  C CG2 . VAL A 36  ? 1.0197 1.1085 0.9980 0.0834  0.1003  0.0975  80  VAL A CG2 
298  N N   . ASP A 37  ? 1.0430 1.0744 1.0186 0.1053  0.1412  0.1001  81  ASP A N   
299  C CA  . ASP A 37  ? 1.0490 1.0600 1.0268 0.1012  0.1525  0.0887  81  ASP A CA  
300  C C   . ASP A 37  ? 1.0498 1.0547 1.0278 0.0888  0.1446  0.0762  81  ASP A C   
301  O O   . ASP A 37  ? 1.0649 1.0635 1.0434 0.0887  0.1434  0.0765  81  ASP A O   
302  C CB  . ASP A 37  ? 1.0648 1.0555 1.0466 0.1120  0.1741  0.0932  81  ASP A CB  
303  C CG  . ASP A 37  ? 1.0845 1.0533 1.0710 0.1055  0.1904  0.0773  81  ASP A CG  
304  O OD1 . ASP A 37  ? 1.0852 1.0607 1.0700 0.0921  0.1828  0.0623  81  ASP A OD1 
305  O OD2 . ASP A 37  ? 1.1078 1.0554 1.1009 0.1138  0.2122  0.0803  81  ASP A OD2 
306  N N   . CYS A 38  ? 1.0431 1.0545 1.0212 0.0791  0.1397  0.0665  82  CYS A N   
307  C CA  . CYS A 38  ? 1.0358 1.0512 1.0155 0.0692  0.1301  0.0586  82  CYS A CA  
308  C C   . CYS A 38  ? 1.0369 1.0379 1.0190 0.0645  0.1410  0.0461  82  CYS A C   
309  O O   . CYS A 38  ? 1.0337 1.0365 1.0181 0.0592  0.1347  0.0419  82  CYS A O   
310  C CB  . CYS A 38  ? 1.0413 1.0766 1.0206 0.0621  0.1221  0.0558  82  CYS A CB  
311  S SG  . CYS A 38  ? 1.0599 1.1114 1.0390 0.0650  0.1097  0.0706  82  CYS A SG  
312  N N   . GLN A 39  ? 1.0480 1.0341 1.0314 0.0662  0.1592  0.0400  83  GLN A N   
313  C CA  . GLN A 39  ? 1.0562 1.0248 1.0440 0.0606  0.1739  0.0274  83  GLN A CA  
314  C C   . GLN A 39  ? 1.0387 0.9926 1.0275 0.0682  0.1763  0.0375  83  GLN A C   
315  O O   . GLN A 39  ? 1.0174 0.9656 1.0089 0.0618  0.1778  0.0297  83  GLN A O   
316  C CB  . GLN A 39  ? 1.0874 1.0396 1.0797 0.0602  0.1971  0.0178  83  GLN A CB  
317  C CG  . GLN A 39  ? 1.1050 1.0717 1.0985 0.0444  0.2006  -0.0048 83  GLN A CG  
318  C CD  . GLN A 39  ? 1.1131 1.0857 1.1094 0.0305  0.1996  -0.0206 83  GLN A CD  
319  O OE1 . GLN A 39  ? 1.1235 1.0736 1.1254 0.0292  0.2132  -0.0250 83  GLN A OE1 
320  N NE2 . GLN A 39  ? 1.1061 1.1125 1.0994 0.0209  0.1838  -0.0272 83  GLN A NE2 
321  N N   . SER A 40  ? 1.0280 0.9811 1.0146 0.0816  0.1767  0.0550  84  SER A N   
322  C CA  . SER A 40  ? 1.0281 0.9763 1.0143 0.0897  0.1786  0.0665  84  SER A CA  
323  C C   . SER A 40  ? 1.0143 0.9754 0.9982 0.0835  0.1605  0.0639  84  SER A C   
324  O O   . SER A 40  ? 1.0049 0.9602 0.9897 0.0833  0.1629  0.0636  84  SER A O   
325  C CB  . SER A 40  ? 1.0206 0.9774 1.0048 0.1050  0.1816  0.0859  84  SER A CB  
326  O OG  . SER A 40  ? 1.0326 0.9736 1.0221 0.1136  0.2024  0.0905  84  SER A OG  
327  N N   . VAL A 41  ? 1.0082 0.9859 0.9907 0.0789  0.1444  0.0625  85  VAL A N   
328  C CA  . VAL A 41  ? 1.0053 0.9922 0.9894 0.0735  0.1300  0.0601  85  VAL A CA  
329  C C   . VAL A 41  ? 1.0051 0.9863 0.9936 0.0654  0.1310  0.0484  85  VAL A C   
330  O O   . VAL A 41  ? 1.0074 0.9875 0.9983 0.0643  0.1278  0.0466  85  VAL A O   
331  C CB  . VAL A 41  ? 1.0040 1.0061 0.9892 0.0706  0.1170  0.0627  85  VAL A CB  
332  C CG1 . VAL A 41  ? 1.0050 1.0113 0.9966 0.0646  0.1066  0.0591  85  VAL A CG1 
333  C CG2 . VAL A 41  ? 1.0016 1.0150 0.9839 0.0762  0.1141  0.0725  85  VAL A CG2 
334  N N   . TRP A 42  ? 1.0078 0.9898 0.9977 0.0591  0.1356  0.0391  86  TRP A N   
335  C CA  . TRP A 42  ? 1.0125 0.9980 1.0071 0.0500  0.1365  0.0267  86  TRP A CA  
336  C C   . TRP A 42  ? 1.0248 0.9921 1.0212 0.0494  0.1502  0.0217  86  TRP A C   
337  O O   . TRP A 42  ? 1.0316 1.0019 1.0320 0.0445  0.1481  0.0154  86  TRP A O   
338  C CB  . TRP A 42  ? 1.0227 1.0218 1.0177 0.0414  0.1394  0.0155  86  TRP A CB  
339  C CG  . TRP A 42  ? 1.0394 1.0492 1.0394 0.0303  0.1425  0.0004  86  TRP A CG  
340  C CD1 . TRP A 42  ? 1.0620 1.0700 1.0641 0.0197  0.1576  -0.0173 86  TRP A CD1 
341  C CD2 . TRP A 42  ? 1.0357 1.0617 1.0411 0.0281  0.1318  0.0005  86  TRP A CD2 
342  N NE1 . TRP A 42  ? 1.0640 1.0907 1.0713 0.0097  0.1555  -0.0291 86  TRP A NE1 
343  C CE2 . TRP A 42  ? 1.0475 1.0861 1.0569 0.0161  0.1393  -0.0168 86  TRP A CE2 
344  C CE3 . TRP A 42  ? 1.0186 1.0501 1.0277 0.0349  0.1185  0.0126  86  TRP A CE3 
345  C CZ2 . TRP A 42  ? 1.0359 1.0966 1.0520 0.0123  0.1322  -0.0199 86  TRP A CZ2 
346  C CZ3 . TRP A 42  ? 1.0143 1.0623 1.0313 0.0323  0.1131  0.0101  86  TRP A CZ3 
347  C CH2 . TRP A 42  ? 1.0216 1.0861 1.0415 0.0220  0.1189  -0.0047 86  TRP A CH2 
348  N N   . ASP A 43  ? 1.0429 0.9921 1.0375 0.0555  0.1655  0.0264  87  ASP A N   
349  C CA  . ASP A 43  ? 1.0597 0.9893 1.0575 0.0567  0.1819  0.0259  87  ASP A CA  
350  C C   . ASP A 43  ? 1.0396 0.9730 1.0352 0.0623  0.1741  0.0352  87  ASP A C   
351  O O   . ASP A 43  ? 1.0410 0.9694 1.0400 0.0578  0.1787  0.0296  87  ASP A O   
352  C CB  . ASP A 43  ? 1.0954 1.0053 1.0943 0.0658  0.2018  0.0345  87  ASP A CB  
353  C CG  . ASP A 43  ? 1.1130 1.0143 1.1166 0.0585  0.2157  0.0206  87  ASP A CG  
354  O OD1 . ASP A 43  ? 1.1170 1.0337 1.1211 0.0451  0.2083  0.0035  87  ASP A OD1 
355  O OD2 . ASP A 43  ? 1.1198 1.0018 1.1274 0.0667  0.2350  0.0271  87  ASP A OD2 
356  N N   . ALA A 44  ? 1.0195 0.9648 1.0100 0.0706  0.1631  0.0475  88  ALA A N   
357  C CA  . ALA A 44  ? 1.0147 0.9693 1.0030 0.0743  0.1562  0.0534  88  ALA A CA  
358  C C   . ALA A 44  ? 1.0159 0.9784 1.0087 0.0660  0.1436  0.0426  88  ALA A C   
359  O O   . ALA A 44  ? 1.0193 0.9846 1.0129 0.0658  0.1423  0.0413  88  ALA A O   
360  C CB  . ALA A 44  ? 1.0037 0.9744 0.9867 0.0821  0.1489  0.0651  88  ALA A CB  
361  N N   . PHE A 45  ? 1.0202 0.9885 1.0165 0.0604  0.1353  0.0366  89  PHE A N   
362  C CA  . PHE A 45  ? 1.0156 0.9933 1.0192 0.0553  0.1251  0.0304  89  PHE A CA  
363  C C   . PHE A 45  ? 1.0267 1.0024 1.0350 0.0491  0.1317  0.0202  89  PHE A C   
364  O O   . PHE A 45  ? 1.0167 0.9948 1.0298 0.0484  0.1296  0.0171  89  PHE A O   
365  C CB  . PHE A 45  ? 1.0115 1.0011 1.0181 0.0534  0.1159  0.0319  89  PHE A CB  
366  C CG  . PHE A 45  ? 1.0069 1.0060 1.0229 0.0535  0.1055  0.0339  89  PHE A CG  
367  C CD1 . PHE A 45  ? 1.0076 1.0115 1.0322 0.0517  0.1047  0.0289  89  PHE A CD1 
368  C CD2 . PHE A 45  ? 1.0018 1.0044 1.0205 0.0558  0.0986  0.0415  89  PHE A CD2 
369  C CE1 . PHE A 45  ? 1.0053 1.0160 1.0418 0.0543  0.0982  0.0331  89  PHE A CE1 
370  C CE2 . PHE A 45  ? 0.9977 1.0041 1.0288 0.0567  0.0932  0.0447  89  PHE A CE2 
371  C CZ  . PHE A 45  ? 1.0035 1.0132 1.0440 0.0570  0.0934  0.0414  89  PHE A CZ  
372  N N   . LYS A 46  ? 1.0507 1.0233 1.0587 0.0435  0.1411  0.0131  90  LYS A N   
373  C CA  . LYS A 46  ? 1.0708 1.0452 1.0843 0.0342  0.1490  0.0001  90  LYS A CA  
374  C C   . LYS A 46  ? 1.0836 1.0424 1.0973 0.0359  0.1595  0.0010  90  LYS A C   
375  O O   . LYS A 46  ? 1.0835 1.0490 1.1027 0.0316  0.1585  -0.0052 90  LYS A O   
376  C CB  . LYS A 46  ? 1.0949 1.0678 1.1086 0.0256  0.1608  -0.0110 90  LYS A CB  
377  C CG  . LYS A 46  ? 1.1255 1.1055 1.1463 0.0118  0.1704  -0.0290 90  LYS A CG  
378  C CD  . LYS A 46  ? 1.1501 1.1374 1.1725 -0.0004 0.1809  -0.0456 90  LYS A CD  
379  C CE  . LYS A 46  ? 1.1712 1.1739 1.2018 -0.0173 0.1898  -0.0670 90  LYS A CE  
380  N NZ  . LYS A 46  ? 1.1974 1.2156 1.2299 -0.0324 0.1995  -0.0876 90  LYS A NZ  
381  N N   . GLY A 47  ? 1.0940 1.0355 1.1022 0.0434  0.1699  0.0111  91  GLY A N   
382  C CA  . GLY A 47  ? 1.1028 1.0317 1.1107 0.0466  0.1824  0.0162  91  GLY A CA  
383  C C   . GLY A 47  ? 1.1013 1.0421 1.1084 0.0496  0.1721  0.0190  91  GLY A C   
384  O O   . GLY A 47  ? 1.1170 1.0534 1.1249 0.0498  0.1810  0.0202  91  GLY A O   
385  N N   . ALA A 48  ? 1.0969 1.0521 1.1037 0.0516  0.1555  0.0195  92  ALA A N   
386  C CA  . ALA A 48  ? 1.0938 1.0593 1.1018 0.0535  0.1476  0.0191  92  ALA A CA  
387  C C   . ALA A 48  ? 1.0980 1.0677 1.1149 0.0473  0.1475  0.0084  92  ALA A C   
388  O O   . ALA A 48  ? 1.0946 1.0663 1.1118 0.0478  0.1512  0.0071  92  ALA A O   
389  C CB  . ALA A 48  ? 1.0805 1.0556 1.0897 0.0555  0.1341  0.0206  92  ALA A CB  
390  N N   . PHE A 49  ? 1.1014 1.0778 1.1257 0.0418  0.1433  0.0013  93  PHE A N   
391  C CA  . PHE A 49  ? 1.0967 1.0857 1.1316 0.0377  0.1405  -0.0070 93  PHE A CA  
392  C C   . PHE A 49  ? 1.1075 1.0993 1.1458 0.0277  0.1504  -0.0172 93  PHE A C   
393  O O   . PHE A 49  ? 1.1257 1.1310 1.1726 0.0233  0.1503  -0.0247 93  PHE A O   
394  C CB  . PHE A 49  ? 1.0793 1.0839 1.1231 0.0403  0.1277  -0.0051 93  PHE A CB  
395  C CG  . PHE A 49  ? 1.0651 1.0802 1.1085 0.0374  0.1242  -0.0042 93  PHE A CG  
396  C CD1 . PHE A 49  ? 1.0606 1.0682 1.0963 0.0402  0.1218  0.0026  93  PHE A CD1 
397  C CD2 . PHE A 49  ? 1.0617 1.1000 1.1123 0.0311  0.1233  -0.0111 93  PHE A CD2 
398  C CE1 . PHE A 49  ? 1.0607 1.0809 1.0955 0.0370  0.1190  0.0025  93  PHE A CE1 
399  C CE2 . PHE A 49  ? 1.0603 1.1156 1.1096 0.0272  0.1202  -0.0116 93  PHE A CE2 
400  C CZ  . PHE A 49  ? 1.0593 1.1041 1.1004 0.0302  0.1182  -0.0049 93  PHE A CZ  
401  N N   . ILE A 50  ? 1.1073 1.0873 1.1405 0.0233  0.1605  -0.0190 94  ILE A N   
402  C CA  . ILE A 50  ? 1.1131 1.0959 1.1515 0.0103  0.1725  -0.0331 94  ILE A CA  
403  C C   . ILE A 50  ? 1.1179 1.0835 1.1576 0.0072  0.1889  -0.0349 94  ILE A C   
404  O O   . ILE A 50  ? 1.1116 1.0592 1.1449 0.0161  0.1947  -0.0223 94  ILE A O   
405  C CB  . ILE A 50  ? 1.1237 1.0994 1.1588 0.0056  0.1797  -0.0372 94  ILE A CB  
406  C CG1 . ILE A 50  ? 1.1374 1.1294 1.1800 -0.0114 0.1882  -0.0578 94  ILE A CG1 
407  C CG2 . ILE A 50  ? 1.1392 1.0831 1.1685 0.0118  0.1952  -0.0278 94  ILE A CG2 
408  C CD1 . ILE A 50  ? 1.1280 1.1620 1.1758 -0.0154 0.1719  -0.0633 94  ILE A CD1 
409  N N   . SER A 51  ? 1.1120 1.0881 1.1606 -0.0056 0.1965  -0.0499 95  SER A N   
410  C CA  . SER A 51  ? 1.1152 1.0769 1.1677 -0.0114 0.2140  -0.0533 95  SER A CA  
411  C C   . SER A 51  ? 1.0902 1.0518 1.1396 -0.0008 0.2086  -0.0417 95  SER A C   
412  O O   . SER A 51  ? 1.0996 1.0451 1.1477 0.0003  0.2229  -0.0357 95  SER A O   
413  C CB  . SER A 51  ? 1.1366 1.0656 1.1876 -0.0129 0.2364  -0.0502 95  SER A CB  
414  O OG  . SER A 51  ? 1.1471 1.0767 1.2029 -0.0258 0.2446  -0.0664 95  SER A OG  
415  N N   . LYS A 52  ? 1.0482 1.0290 1.0979 0.0064  0.1897  -0.0388 96  LYS A N   
416  C CA  . LYS A 52  ? 1.0247 1.0088 1.0728 0.0149  0.1845  -0.0322 96  LYS A CA  
417  C C   . LYS A 52  ? 1.0034 1.0123 1.0624 0.0149  0.1720  -0.0392 96  LYS A C   
418  O O   . LYS A 52  ? 0.9871 1.0110 1.0516 0.0144  0.1624  -0.0415 96  LYS A O   
419  C CB  . LYS A 52  ? 1.0136 0.9900 1.0514 0.0266  0.1776  -0.0190 96  LYS A CB  
420  C CG  . LYS A 52  ? 1.0329 0.9905 1.0609 0.0308  0.1904  -0.0071 96  LYS A CG  
421  C CD  . LYS A 52  ? 1.0282 0.9868 1.0469 0.0411  0.1821  0.0046  96  LYS A CD  
422  C CE  . LYS A 52  ? 1.0467 0.9912 1.0580 0.0476  0.1954  0.0193  96  LYS A CE  
423  N NZ  . LYS A 52  ? 1.0439 0.9952 1.0473 0.0565  0.1861  0.0294  96  LYS A NZ  
424  N N   . HIS A 53  ? 0.9949 1.0102 1.0580 0.0167  0.1734  -0.0411 97  HIS A N   
425  C CA  . HIS A 53  ? 0.9824 1.0209 1.0592 0.0178  0.1655  -0.0473 97  HIS A CA  
426  C C   . HIS A 53  ? 0.9741 1.0162 1.0547 0.0285  0.1523  -0.0409 97  HIS A C   
427  O O   . HIS A 53  ? 0.9715 1.0004 1.0449 0.0345  0.1505  -0.0358 97  HIS A O   
428  C CB  . HIS A 53  ? 0.9810 1.0245 1.0618 0.0173  0.1720  -0.0517 97  HIS A CB  
429  C CG  . HIS A 53  ? 0.9646 1.0345 1.0620 0.0170  0.1676  -0.0588 97  HIS A CG  
430  N ND1 . HIS A 53  ? 0.9511 1.0299 1.0587 0.0272  0.1607  -0.0576 97  HIS A ND1 
431  C CD2 . HIS A 53  ? 0.9632 1.0556 1.0706 0.0081  0.1698  -0.0671 97  HIS A CD2 
432  C CE1 . HIS A 53  ? 0.9475 1.0531 1.0712 0.0270  0.1590  -0.0619 97  HIS A CE1 
433  N NE2 . HIS A 53  ? 0.9515 1.0691 1.0745 0.0150  0.1634  -0.0680 97  HIS A NE2 
434  N N   . PRO A 54  ? 0.9700 1.0330 1.0635 0.0311  0.1440  -0.0406 98  PRO A N   
435  C CA  . PRO A 54  ? 0.9675 1.0309 1.0674 0.0416  0.1345  -0.0318 98  PRO A CA  
436  C C   . PRO A 54  ? 0.9694 1.0248 1.0771 0.0498  0.1349  -0.0318 98  PRO A C   
437  O O   . PRO A 54  ? 0.9734 1.0222 1.0872 0.0570  0.1306  -0.0258 98  PRO A O   
438  C CB  . PRO A 54  ? 0.9738 1.0687 1.0888 0.0438  0.1286  -0.0289 98  PRO A CB  
439  C CG  . PRO A 54  ? 0.9745 1.0865 1.0862 0.0305  0.1336  -0.0392 98  PRO A CG  
440  C CD  . PRO A 54  ? 0.9722 1.0638 1.0760 0.0241  0.1446  -0.0474 98  PRO A CD  
441  N N   . CYS A 55  ? 0.9711 1.0276 1.0799 0.0476  0.1417  -0.0399 99  CYS A N   
442  C CA  . CYS A 55  ? 0.9674 1.0206 1.0857 0.0536  0.1443  -0.0444 99  CYS A CA  
443  C C   . CYS A 55  ? 0.9587 1.0001 1.0615 0.0497  0.1494  -0.0496 99  CYS A C   
444  O O   . CYS A 55  ? 0.9467 0.9890 1.0547 0.0515  0.1534  -0.0576 99  CYS A O   
445  C CB  . CYS A 55  ? 0.9772 1.0490 1.1110 0.0552  0.1483  -0.0500 99  CYS A CB  
446  S SG  . CYS A 55  ? 0.9858 1.0871 1.1372 0.0595  0.1423  -0.0423 99  CYS A SG  
447  N N   . ASP A 56  ? 0.9610 0.9945 1.0457 0.0450  0.1505  -0.0447 100 ASP A N   
448  C CA  . ASP A 56  ? 0.9816 1.0124 1.0512 0.0430  0.1561  -0.0451 100 ASP A CA  
449  C C   . ASP A 56  ? 0.9839 1.0051 1.0392 0.0437  0.1535  -0.0356 100 ASP A C   
450  O O   . ASP A 56  ? 0.9904 1.0085 1.0329 0.0425  0.1598  -0.0285 100 ASP A O   
451  C CB  . ASP A 56  ? 0.9958 1.0312 1.0609 0.0381  0.1658  -0.0460 100 ASP A CB  
452  C CG  . ASP A 56  ? 1.0077 1.0506 1.0619 0.0380  0.1727  -0.0462 100 ASP A CG  
453  O OD1 . ASP A 56  ? 1.0083 1.0574 1.0590 0.0403  0.1694  -0.0497 100 ASP A OD1 
454  O OD2 . ASP A 56  ? 1.0215 1.0667 1.0712 0.0347  0.1823  -0.0433 100 ASP A OD2 
455  N N   . ILE A 57  ? 0.9789 0.9958 1.0383 0.0466  0.1457  -0.0342 101 ILE A N   
456  C CA  . ILE A 57  ? 0.9710 0.9818 1.0188 0.0476  0.1423  -0.0260 101 ILE A CA  
457  C C   . ILE A 57  ? 0.9746 0.9943 1.0161 0.0474  0.1426  -0.0299 101 ILE A C   
458  O O   . ILE A 57  ? 0.9758 1.0010 1.0268 0.0460  0.1433  -0.0415 101 ILE A O   
459  C CB  . ILE A 57  ? 0.9655 0.9704 1.0214 0.0496  0.1344  -0.0219 101 ILE A CB  
460  C CG1 . ILE A 57  ? 0.9612 0.9693 1.0250 0.0486  0.1336  -0.0207 101 ILE A CG1 
461  C CG2 . ILE A 57  ? 0.9644 0.9641 1.0084 0.0504  0.1314  -0.0136 101 ILE A CG2 
462  C CD1 . ILE A 57  ? 0.9679 0.9726 1.0215 0.0436  0.1400  -0.0191 101 ILE A CD1 
463  N N   . THR A 58  ? 0.9891 1.0130 1.0155 0.0486  0.1432  -0.0210 102 THR A N   
464  C CA  . THR A 58  ? 1.0085 1.0513 1.0270 0.0474  0.1429  -0.0242 102 THR A CA  
465  C C   . THR A 58  ? 1.0229 1.0650 1.0383 0.0479  0.1366  -0.0193 102 THR A C   
466  O O   . THR A 58  ? 1.0164 1.0422 1.0346 0.0501  0.1330  -0.0122 102 THR A O   
467  C CB  . THR A 58  ? 1.0153 1.0755 1.0192 0.0499  0.1503  -0.0150 102 THR A CB  
468  O OG1 . THR A 58  ? 1.0194 1.0687 1.0154 0.0556  0.1534  0.0025  102 THR A OG1 
469  C CG2 . THR A 58  ? 1.0179 1.0801 1.0249 0.0485  0.1575  -0.0196 102 THR A CG2 
470  N N   . GLU A 59  ? 1.0542 1.1186 1.0639 0.0447  0.1356  -0.0245 103 GLU A N   
471  C CA  . GLU A 59  ? 1.0670 1.1372 1.0736 0.0439  0.1303  -0.0209 103 GLU A CA  
472  C C   . GLU A 59  ? 1.0884 1.1657 1.0803 0.0519  0.1314  -0.0008 103 GLU A C   
473  O O   . GLU A 59  ? 1.0975 1.1724 1.0874 0.0539  0.1273  0.0064  103 GLU A O   
474  C CB  . GLU A 59  ? 1.0749 1.1727 1.0820 0.0352  0.1302  -0.0368 103 GLU A CB  
475  C CG  . GLU A 59  ? 1.0811 1.1672 1.1067 0.0271  0.1328  -0.0581 103 GLU A CG  
476  C CD  . GLU A 59  ? 1.0912 1.1819 1.1211 0.0253  0.1393  -0.0700 103 GLU A CD  
477  O OE1 . GLU A 59  ? 1.0866 1.1873 1.1049 0.0304  0.1412  -0.0603 103 GLU A OE1 
478  O OE2 . GLU A 59  ? 1.0960 1.1797 1.1425 0.0191  0.1441  -0.0888 103 GLU A OE2 
479  N N   . GLU A 60  ? 1.1079 1.1932 1.0913 0.0572  0.1387  0.0089  104 GLU A N   
480  C CA  . GLU A 60  ? 1.1283 1.2178 1.1011 0.0671  0.1443  0.0306  104 GLU A CA  
481  C C   . GLU A 60  ? 1.1098 1.1639 1.0871 0.0704  0.1476  0.0381  104 GLU A C   
482  O O   . GLU A 60  ? 1.1176 1.1675 1.0900 0.0783  0.1532  0.0541  104 GLU A O   
483  C CB  . GLU A 60  ? 1.1723 1.2808 1.1372 0.0722  0.1541  0.0408  104 GLU A CB  
484  C CG  . GLU A 60  ? 1.2157 1.3714 1.1730 0.0696  0.1517  0.0357  104 GLU A CG  
485  C CD  . GLU A 60  ? 1.2601 1.4437 1.2079 0.0767  0.1616  0.0510  104 GLU A CD  
486  O OE1 . GLU A 60  ? 1.2783 1.5090 1.2187 0.0739  0.1598  0.0465  104 GLU A OE1 
487  O OE2 . GLU A 60  ? 1.2993 1.4598 1.2478 0.0844  0.1723  0.0672  104 GLU A OE2 
488  N N   . ASP A 61  ? 1.0897 1.1222 1.0772 0.0644  0.1452  0.0261  105 ASP A N   
489  C CA  . ASP A 61  ? 1.0864 1.0940 1.0787 0.0643  0.1471  0.0285  105 ASP A CA  
490  C C   . ASP A 61  ? 1.0817 1.0869 1.0739 0.0651  0.1394  0.0311  105 ASP A C   
491  O O   . ASP A 61  ? 1.0962 1.0887 1.0871 0.0676  0.1433  0.0378  105 ASP A O   
492  C CB  . ASP A 61  ? 1.0811 1.0782 1.0847 0.0580  0.1452  0.0158  105 ASP A CB  
493  C CG  . ASP A 61  ? 1.0894 1.0870 1.0941 0.0563  0.1542  0.0131  105 ASP A CG  
494  O OD1 . ASP A 61  ? 1.0936 1.0830 1.0939 0.0584  0.1660  0.0221  105 ASP A OD1 
495  O OD2 . ASP A 61  ? 1.0968 1.1017 1.1082 0.0531  0.1512  0.0024  105 ASP A OD2 
496  N N   . TYR A 62  ? 1.0823 1.0996 1.0772 0.0620  0.1303  0.0243  106 TYR A N   
497  C CA  . TYR A 62  ? 1.0777 1.0943 1.0741 0.0615  0.1232  0.0263  106 TYR A CA  
498  C C   . TYR A 62  ? 1.0838 1.1216 1.0708 0.0652  0.1228  0.0345  106 TYR A C   
499  O O   . TYR A 62  ? 1.0802 1.1206 1.0673 0.0648  0.1178  0.0372  106 TYR A O   
500  C CB  . TYR A 62  ? 1.0624 1.0766 1.0713 0.0553  0.1163  0.0147  106 TYR A CB  
501  C CG  . TYR A 62  ? 1.0490 1.0483 1.0690 0.0545  0.1154  0.0115  106 TYR A CG  
502  C CD1 . TYR A 62  ? 1.0429 1.0344 1.0631 0.0559  0.1139  0.0177  106 TYR A CD1 
503  C CD2 . TYR A 62  ? 1.0436 1.0418 1.0746 0.0524  0.1165  0.0020  106 TYR A CD2 
504  C CE1 . TYR A 62  ? 1.0365 1.0251 1.0666 0.0549  0.1124  0.0153  106 TYR A CE1 
505  C CE2 . TYR A 62  ? 1.0351 1.0271 1.0776 0.0533  0.1155  0.0015  106 TYR A CE2 
506  C CZ  . TYR A 62  ? 1.0298 1.0199 1.0713 0.0544  0.1128  0.0086  106 TYR A CZ  
507  O OH  . TYR A 62  ? 1.0225 1.0167 1.0749 0.0550  0.1112  0.0086  106 TYR A OH  
508  N N   . GLN A 63  ? 1.0916 1.1488 1.0704 0.0691  0.1284  0.0400  107 GLN A N   
509  C CA  . GLN A 63  ? 1.0947 1.1829 1.0646 0.0742  0.1284  0.0503  107 GLN A CA  
510  C C   . GLN A 63  ? 1.0808 1.1610 1.0479 0.0829  0.1308  0.0661  107 GLN A C   
511  O O   . GLN A 63  ? 1.0675 1.1670 1.0326 0.0833  0.1256  0.0689  107 GLN A O   
512  C CB  . GLN A 63  ? 1.1197 1.2320 1.0816 0.0799  0.1360  0.0588  107 GLN A CB  
513  C CG  . GLN A 63  ? 1.1378 1.2911 1.0903 0.0885  0.1374  0.0750  107 GLN A CG  
514  C CD  . GLN A 63  ? 1.1447 1.3352 1.0963 0.0788  0.1276  0.0614  107 GLN A CD  
515  O OE1 . GLN A 63  ? 1.1425 1.3224 1.1021 0.0656  0.1214  0.0398  107 GLN A OE1 
516  N NE2 . GLN A 63  ? 1.1554 1.3923 1.0988 0.0853  0.1279  0.0745  107 GLN A NE2 
517  N N   . PRO A 64  ? 1.0758 1.1291 1.0438 0.0892  0.1404  0.0752  108 PRO A N   
518  C CA  . PRO A 64  ? 1.0746 1.1185 1.0418 0.0972  0.1454  0.0877  108 PRO A CA  
519  C C   . PRO A 64  ? 1.0514 1.0882 1.0224 0.0909  0.1355  0.0796  108 PRO A C   
520  O O   . PRO A 64  ? 1.0563 1.1002 1.0253 0.0965  0.1358  0.0886  108 PRO A O   
521  C CB  . PRO A 64  ? 1.0930 1.1055 1.0638 0.1000  0.1600  0.0912  108 PRO A CB  
522  C CG  . PRO A 64  ? 1.0857 1.0886 1.0606 0.0899  0.1571  0.0758  108 PRO A CG  
523  C CD  . PRO A 64  ? 1.0851 1.1167 1.0563 0.0878  0.1489  0.0720  108 PRO A CD  
524  N N   . LEU A 65  ? 1.0236 1.0485 1.0010 0.0806  0.1278  0.0645  109 LEU A N   
525  C CA  . LEU A 65  ? 1.0010 1.0214 0.9832 0.0751  0.1191  0.0593  109 LEU A CA  
526  C C   . LEU A 65  ? 0.9986 1.0417 0.9812 0.0715  0.1111  0.0570  109 LEU A C   
527  O O   . LEU A 65  ? 0.9922 1.0382 0.9763 0.0701  0.1066  0.0592  109 LEU A O   
528  C CB  . LEU A 65  ? 0.9871 0.9927 0.9782 0.0679  0.1153  0.0481  109 LEU A CB  
529  C CG  . LEU A 65  ? 0.9725 0.9756 0.9704 0.0636  0.1074  0.0461  109 LEU A CG  
530  C CD1 . LEU A 65  ? 0.9708 0.9689 0.9653 0.0659  0.1098  0.0514  109 LEU A CD1 
531  C CD2 . LEU A 65  ? 0.9680 0.9647 0.9769 0.0593  0.1041  0.0388  109 LEU A CD2 
532  N N   . MET A 66  ? 1.0112 1.0725 0.9929 0.0682  0.1104  0.0509  110 MET A N   
533  C CA  . MET A 66  ? 1.0127 1.0996 0.9959 0.0611  0.1050  0.0437  110 MET A CA  
534  C C   . MET A 66  ? 1.0022 1.1156 0.9776 0.0676  0.1050  0.0565  110 MET A C   
535  O O   . MET A 66  ? 0.9958 1.1264 0.9737 0.0612  0.1001  0.0521  110 MET A O   
536  C CB  . MET A 66  ? 1.0324 1.1401 1.0151 0.0554  0.1064  0.0322  110 MET A CB  
537  C CG  . MET A 66  ? 1.0347 1.1215 1.0285 0.0478  0.1068  0.0168  110 MET A CG  
538  S SD  . MET A 66  ? 1.0450 1.1091 1.0559 0.0392  0.1031  0.0077  110 MET A SD  
539  C CE  . MET A 66  ? 1.0431 1.0755 1.0574 0.0470  0.1028  0.0175  110 MET A CE  
540  N N   . LYS A 67  ? 1.0054 1.1225 0.9730 0.0806  0.1123  0.0728  111 LYS A N   
541  C CA  . LYS A 67  ? 1.0145 1.1584 0.9764 0.0910  0.1147  0.0893  111 LYS A CA  
542  C C   . LYS A 67  ? 1.0059 1.1322 0.9707 0.0934  0.1138  0.0940  111 LYS A C   
543  O O   . LYS A 67  ? 1.0037 1.1543 0.9680 0.0938  0.1099  0.0980  111 LYS A O   
544  C CB  . LYS A 67  ? 1.0310 1.1792 0.9875 0.1066  0.1266  0.1084  111 LYS A CB  
545  C CG  . LYS A 67  ? 1.0436 1.2202 0.9952 0.1063  0.1280  0.1081  111 LYS A CG  
546  C CD  . LYS A 67  ? 1.0626 1.2378 1.0109 0.1224  0.1422  0.1301  111 LYS A CD  
547  C CE  . LYS A 67  ? 1.0676 1.2723 1.0105 0.1215  0.1436  0.1299  111 LYS A CE  
548  N NZ  . LYS A 67  ? 1.0855 1.2835 1.0271 0.1374  0.1598  0.1537  111 LYS A NZ  
549  N N   . LEU A 68  ? 0.9945 1.0832 0.9624 0.0940  0.1178  0.0925  112 LEU A N   
550  C CA  . LEU A 68  ? 0.9909 1.0650 0.9611 0.0953  0.1182  0.0951  112 LEU A CA  
551  C C   . LEU A 68  ? 0.9763 1.0569 0.9510 0.0841  0.1068  0.0858  112 LEU A C   
552  O O   . LEU A 68  ? 0.9801 1.0675 0.9549 0.0856  0.1052  0.0908  112 LEU A O   
553  C CB  . LEU A 68  ? 1.0001 1.0401 0.9730 0.0945  0.1248  0.0905  112 LEU A CB  
554  C CG  . LEU A 68  ? 1.0213 1.0472 0.9929 0.1045  0.1406  0.0994  112 LEU A CG  
555  C CD1 . LEU A 68  ? 1.0296 1.0258 1.0054 0.0995  0.1480  0.0900  112 LEU A CD1 
556  C CD2 . LEU A 68  ? 1.0305 1.0689 1.0004 0.1190  0.1500  0.1174  112 LEU A CD2 
557  N N   . GLY A 69  ? 0.9628 1.0401 0.9428 0.0735  0.1010  0.0731  113 GLY A N   
558  C CA  . GLY A 69  ? 0.9575 1.0342 0.9458 0.0630  0.0940  0.0654  113 GLY A CA  
559  C C   . GLY A 69  ? 0.9606 1.0629 0.9521 0.0538  0.0911  0.0564  113 GLY A C   
560  O O   . GLY A 69  ? 0.9753 1.0696 0.9773 0.0432  0.0896  0.0447  113 GLY A O   
561  N N   . THR A 70  ? 0.9622 1.0977 0.9462 0.0580  0.0919  0.0618  114 THR A N   
562  C CA  . THR A 70  ? 0.9691 1.1398 0.9555 0.0471  0.0894  0.0510  114 THR A CA  
563  C C   . THR A 70  ? 0.9730 1.1492 0.9660 0.0393  0.0861  0.0495  114 THR A C   
564  O O   . THR A 70  ? 0.9555 1.1306 0.9449 0.0478  0.0856  0.0628  114 THR A O   
565  C CB  . THR A 70  ? 0.9730 1.1879 0.9490 0.0552  0.0909  0.0597  114 THR A CB  
566  O OG1 . THR A 70  ? 0.9820 1.1868 0.9523 0.0644  0.0958  0.0656  114 THR A OG1 
567  C CG2 . THR A 70  ? 0.9776 1.2383 0.9555 0.0411  0.0885  0.0442  114 THR A CG2 
568  N N   . GLN A 71  ? 0.9933 1.1747 0.9973 0.0226  0.0860  0.0323  115 GLN A N   
569  C CA  . GLN A 71  ? 1.0085 1.1891 1.0220 0.0129  0.0852  0.0299  115 GLN A CA  
570  C C   . GLN A 71  ? 1.0288 1.2386 1.0513 -0.0063 0.0877  0.0091  115 GLN A C   
571  O O   . GLN A 71  ? 1.0341 1.2452 1.0615 -0.0153 0.0915  -0.0077 115 GLN A O   
572  C CB  . GLN A 71  ? 1.0097 1.1453 1.0340 0.0122  0.0866  0.0323  115 GLN A CB  
573  C CG  . GLN A 71  ? 1.0085 1.1402 1.0414 0.0063  0.0865  0.0370  115 GLN A CG  
574  C CD  . GLN A 71  ? 1.0028 1.0981 1.0440 0.0101  0.0875  0.0460  115 GLN A CD  
575  O OE1 . GLN A 71  ? 0.9835 1.0575 1.0258 0.0158  0.0882  0.0468  115 GLN A OE1 
576  N NE2 . GLN A 71  ? 1.0116 1.1047 1.0591 0.0071  0.0878  0.0540  115 GLN A NE2 
577  N N   . THR A 72  ? 1.0622 1.2971 1.0878 -0.0139 0.0867  0.0086  116 THR A N   
578  C CA  . THR A 72  ? 1.1135 1.3819 1.1489 -0.0353 0.0904  -0.0135 116 THR A CA  
579  C C   . THR A 72  ? 1.1384 1.3803 1.1920 -0.0493 0.0960  -0.0194 116 THR A C   
580  O O   . THR A 72  ? 1.1410 1.4000 1.1954 -0.0518 0.0943  -0.0130 116 THR A O   
581  C CB  . THR A 72  ? 1.1286 1.4615 1.1530 -0.0339 0.0857  -0.0101 116 THR A CB  
582  O OG1 . THR A 72  ? 1.1251 1.4791 1.1345 -0.0186 0.0828  -0.0003 116 THR A OG1 
583  C CG2 . THR A 72  ? 1.1402 1.5182 1.1743 -0.0589 0.0894  -0.0364 116 THR A CG2 
584  N N   . VAL A 73  ? 1.0574 1.3120 1.3153 0.0819  0.1073  0.0804  117 VAL A N   
585  C CA  . VAL A 73  ? 1.0460 1.3175 1.2843 0.0486  0.0912  0.0689  117 VAL A CA  
586  C C   . VAL A 73  ? 1.0324 1.3615 1.2629 0.0272  0.0758  0.0832  117 VAL A C   
587  O O   . VAL A 73  ? 1.0276 1.3705 1.2617 0.0345  0.0734  0.0963  117 VAL A O   
588  C CB  . VAL A 73  ? 1.0458 1.2521 1.2667 0.0270  0.0806  0.0473  117 VAL A CB  
589  C CG1 . VAL A 73  ? 1.0598 1.2224 1.2854 0.0396  0.0921  0.0288  117 VAL A CG1 
590  C CG2 . VAL A 73  ? 1.0387 1.2120 1.2572 0.0221  0.0735  0.0488  117 VAL A CG2 
591  N N   . PRO A 74  ? 1.0360 1.4014 1.2532 -0.0021 0.0653  0.0811  118 PRO A N   
592  C CA  . PRO A 74  ? 1.0340 1.4441 1.2390 -0.0332 0.0488  0.0890  118 PRO A CA  
593  C C   . PRO A 74  ? 1.0320 1.3817 1.2119 -0.0526 0.0358  0.0778  118 PRO A C   
594  O O   . PRO A 74  ? 1.0319 1.3199 1.1930 -0.0667 0.0311  0.0627  118 PRO A O   
595  C CB  . PRO A 74  ? 1.0405 1.4819 1.2352 -0.0640 0.0443  0.0865  118 PRO A CB  
596  C CG  . PRO A 74  ? 1.0451 1.4338 1.2343 -0.0533 0.0537  0.0725  118 PRO A CG  
597  C CD  . PRO A 74  ? 1.0386 1.4042 1.2494 -0.0097 0.0699  0.0712  118 PRO A CD  
598  N N   . CYS A 75  ? 1.0304 1.4026 1.2090 -0.0499 0.0308  0.0867  119 CYS A N   
599  C CA  . CYS A 75  ? 1.0327 1.3500 1.1896 -0.0569 0.0241  0.0770  119 CYS A CA  
600  C C   . CYS A 75  ? 1.0584 1.3551 1.1790 -0.0997 0.0077  0.0632  119 CYS A C   
601  O O   . CYS A 75  ? 1.0727 1.3081 1.1703 -0.1055 0.0040  0.0504  119 CYS A O   
602  C CB  . CYS A 75  ? 1.0293 1.3798 1.1930 -0.0362 0.0268  0.0923  119 CYS A CB  
603  S SG  . CYS A 75  ? 1.0285 1.4954 1.2028 -0.0397 0.0196  0.1140  119 CYS A SG  
604  N N   . ASN A 76  ? 1.0636 1.4102 1.1794 -0.1294 0.0000  0.0663  120 ASN A N   
605  C CA  . ASN A 76  ? 1.0861 1.4050 1.1656 -0.1752 -0.0132 0.0535  120 ASN A CA  
606  C C   . ASN A 76  ? 1.0885 1.3431 1.1549 -0.1843 -0.0108 0.0454  120 ASN A C   
607  O O   . ASN A 76  ? 1.1227 1.3232 1.1542 -0.2144 -0.0182 0.0351  120 ASN A O   
608  C CB  . ASN A 76  ? 1.0944 1.4969 1.1748 -0.2104 -0.0227 0.0609  120 ASN A CB  
609  C CG  . ASN A 76  ? 1.0729 1.5389 1.1830 -0.2079 -0.0150 0.0748  120 ASN A CG  
610  O OD1 . ASN A 76  ? 1.0355 1.5428 1.1792 -0.1678 -0.0029 0.0878  120 ASN A OD1 
611  N ND2 . ASN A 76  ? 1.0965 1.5678 1.1924 -0.2501 -0.0195 0.0728  120 ASN A ND2 
612  N N   . LYS A 77  ? 1.0651 1.3235 1.1557 -0.1575 0.0001  0.0502  121 LYS A N   
613  C CA  . LYS A 77  ? 1.0819 1.2923 1.1599 -0.1623 0.0018  0.0447  121 LYS A CA  
614  C C   . LYS A 77  ? 1.0661 1.2195 1.1505 -0.1308 0.0065  0.0359  121 LYS A C   
615  O O   . LYS A 77  ? 1.0484 1.2024 1.1476 -0.1123 0.0140  0.0344  121 LYS A O   
616  C CB  . LYS A 77  ? 1.0793 1.3464 1.1750 -0.1610 0.0103  0.0539  121 LYS A CB  
617  C CG  . LYS A 77  ? 1.0980 1.4384 1.1954 -0.1938 0.0071  0.0651  121 LYS A CG  
618  C CD  . LYS A 77  ? 1.1484 1.4533 1.2097 -0.2417 -0.0020 0.0628  121 LYS A CD  
619  C CE  . LYS A 77  ? 1.1656 1.5506 1.2332 -0.2802 -0.0037 0.0742  121 LYS A CE  
620  N NZ  . LYS A 77  ? 1.2237 1.5611 1.2534 -0.3310 -0.0100 0.0728  121 LYS A NZ  
621  N N   . ILE A 78  ? 1.0660 1.1740 1.1386 -0.1264 0.0024  0.0287  122 ILE A N   
622  C CA  . ILE A 78  ? 1.0453 1.1079 1.1274 -0.1006 0.0062  0.0212  122 ILE A CA  
623  C C   . ILE A 78  ? 1.0654 1.0638 1.1166 -0.1105 -0.0016 0.0135  122 ILE A C   
624  O O   . ILE A 78  ? 1.1020 1.0763 1.1226 -0.1317 -0.0074 0.0110  122 ILE A O   
625  C CB  . ILE A 78  ? 1.0309 1.1021 1.1313 -0.0792 0.0127  0.0233  122 ILE A CB  
626  C CG1 . ILE A 78  ? 1.0127 1.1364 1.1451 -0.0599 0.0237  0.0346  122 ILE A CG1 
627  C CG2 . ILE A 78  ? 1.0174 1.0420 1.1252 -0.0607 0.0159  0.0153  122 ILE A CG2 
628  C CD1 . ILE A 78  ? 1.0058 1.1340 1.1558 -0.0365 0.0329  0.0419  122 ILE A CD1 
629  N N   . LEU A 79  ? 1.0424 1.0135 1.1008 -0.0942 -0.0013 0.0093  123 LEU A N   
630  C CA  . LEU A 79  ? 1.0530 0.9686 1.0874 -0.0932 -0.0077 0.0058  123 LEU A CA  
631  C C   . LEU A 79  ? 1.0262 0.9296 1.0841 -0.0659 -0.0050 0.0000  123 LEU A C   
632  O O   . LEU A 79  ? 0.9835 0.9073 1.0691 -0.0533 -0.0025 -0.0028 123 LEU A O   
633  C CB  . LEU A 79  ? 1.0644 0.9730 1.0839 -0.1014 -0.0126 0.0106  123 LEU A CB  
634  C CG  . LEU A 79  ? 1.0961 0.9521 1.0927 -0.0927 -0.0193 0.0122  123 LEU A CG  
635  C CD1 . LEU A 79  ? 1.1526 0.9537 1.1092 -0.1086 -0.0210 0.0148  123 LEU A CD1 
636  C CD2 . LEU A 79  ? 1.1059 0.9693 1.0929 -0.0941 -0.0238 0.0188  123 LEU A CD2 
637  N N   . LEU A 80  ? 1.0435 0.9142 1.0888 -0.0588 -0.0043 -0.0033 124 LEU A N   
638  C CA  . LEU A 80  ? 1.0276 0.8891 1.0936 -0.0341 -0.0012 -0.0070 124 LEU A CA  
639  C C   . LEU A 80  ? 1.0539 0.8810 1.1030 -0.0256 -0.0091 -0.0055 124 LEU A C   
640  O O   . LEU A 80  ? 1.0872 0.8878 1.1036 -0.0393 -0.0151 -0.0005 124 LEU A O   
641  C CB  . LEU A 80  ? 1.0346 0.8846 1.0937 -0.0268 0.0063  -0.0102 124 LEU A CB  
642  C CG  . LEU A 80  ? 1.0135 0.8992 1.0812 -0.0338 0.0128  -0.0074 124 LEU A CG  
643  C CD1 . LEU A 80  ? 1.0291 0.9065 1.0869 -0.0236 0.0208  -0.0106 124 LEU A CD1 
644  C CD2 . LEU A 80  ? 0.9719 0.8977 1.0820 -0.0252 0.0191  -0.0021 124 LEU A CD2 
645  N N   . TRP A 81  ? 1.0535 0.8852 1.1262 -0.0026 -0.0085 -0.0072 125 TRP A N   
646  C CA  . TRP A 81  ? 1.0931 0.9022 1.1543 0.0131  -0.0163 -0.0024 125 TRP A CA  
647  C C   . TRP A 81  ? 1.0979 0.9207 1.1885 0.0398  -0.0118 -0.0044 125 TRP A C   
648  O O   . TRP A 81  ? 1.0704 0.9273 1.1967 0.0413  -0.0039 -0.0092 125 TRP A O   
649  C CB  . TRP A 81  ? 1.0767 0.9090 1.1423 0.0076  -0.0273 0.0009  125 TRP A CB  
650  C CG  . TRP A 81  ? 1.0300 0.9131 1.1380 0.0057  -0.0267 -0.0080 125 TRP A CG  
651  C CD1 . TRP A 81  ? 1.0092 0.9142 1.1259 -0.0100 -0.0223 -0.0133 125 TRP A CD1 
652  C CD2 . TRP A 81  ? 1.0133 0.9290 1.1599 0.0191  -0.0293 -0.0136 125 TRP A CD2 
653  N NE1 . TRP A 81  ? 0.9891 0.9255 1.1425 -0.0074 -0.0206 -0.0234 125 TRP A NE1 
654  C CE2 . TRP A 81  ? 0.9829 0.9288 1.1563 0.0065  -0.0258 -0.0245 125 TRP A CE2 
655  C CE3 . TRP A 81  ? 1.0195 0.9448 1.1821 0.0403  -0.0333 -0.0105 125 TRP A CE3 
656  C CZ2 . TRP A 81  ? 0.9621 0.9411 1.1751 0.0078  -0.0269 -0.0344 125 TRP A CZ2 
657  C CZ3 . TRP A 81  ? 0.9894 0.9617 1.1966 0.0424  -0.0357 -0.0182 125 TRP A CZ3 
658  C CH2 . TRP A 81  ? 0.9642 0.9602 1.1953 0.0231  -0.0329 -0.0311 125 TRP A CH2 
659  N N   . SER A 82  ? 1.1471 0.9442 1.2228 0.0621  -0.0153 0.0019  126 SER A N   
660  C CA  . SER A 82  ? 1.1570 0.9789 1.2643 0.0911  -0.0115 0.0027  126 SER A CA  
661  C C   . SER A 82  ? 1.1958 1.0219 1.3009 0.1133  -0.0238 0.0141  126 SER A C   
662  O O   . SER A 82  ? 1.2491 1.0210 1.3134 0.1279  -0.0242 0.0235  126 SER A O   
663  C CB  . SER A 82  ? 1.1820 0.9705 1.2727 0.1065  0.0036  -0.0009 126 SER A CB  
664  O OG  . SER A 82  ? 1.1680 0.9981 1.2996 0.1315  0.0114  -0.0004 126 SER A OG  
665  N N   . ARG A 83  ? 1.1855 1.0753 1.3324 0.1143  -0.0340 0.0134  127 ARG A N   
666  C CA  . ARG A 83  ? 1.2261 1.1428 1.3781 0.1351  -0.0492 0.0248  127 ARG A CA  
667  C C   . ARG A 83  ? 1.2582 1.1406 1.3637 0.1258  -0.0605 0.0350  127 ARG A C   
668  O O   . ARG A 83  ? 1.3012 1.1790 1.3893 0.1489  -0.0704 0.0517  127 ARG A O   
669  C CB  . ARG A 83  ? 1.2855 1.1949 1.4407 0.1764  -0.0431 0.0357  127 ARG A CB  
670  C CG  . ARG A 83  ? 1.2745 1.2445 1.4863 0.1869  -0.0340 0.0291  127 ARG A CG  
671  C CD  . ARG A 83  ? 1.3250 1.2858 1.5371 0.2310  -0.0223 0.0387  127 ARG A CD  
672  N NE  . ARG A 83  ? 1.3054 1.3513 1.5810 0.2443  -0.0190 0.0385  127 ARG A NE  
673  C CZ  . ARG A 83  ? 1.2804 1.3617 1.5941 0.2250  -0.0064 0.0275  127 ARG A CZ  
674  N NH1 . ARG A 83  ? 1.2638 1.3030 1.5571 0.1970  0.0036  0.0167  127 ARG A NH1 
675  N NH2 . ARG A 83  ? 1.2697 1.4322 1.6428 0.2339  -0.0035 0.0297  127 ARG A NH2 
676  N N   . ILE A 84  ? 1.2500 1.1138 1.3367 0.0935  -0.0579 0.0275  128 ILE A N   
677  C CA  . ILE A 84  ? 1.2815 1.1272 1.3302 0.0780  -0.0664 0.0361  128 ILE A CA  
678  C C   . ILE A 84  ? 1.2412 1.1224 1.3054 0.0480  -0.0662 0.0211  128 ILE A C   
679  O O   . ILE A 84  ? 1.2382 1.0960 1.2824 0.0263  -0.0586 0.0192  128 ILE A O   
680  C CB  . ILE A 84  ? 1.3371 1.1041 1.3332 0.0717  -0.0582 0.0468  128 ILE A CB  
681  C CG1 . ILE A 84  ? 1.4041 1.1210 1.3765 0.1055  -0.0560 0.0620  128 ILE A CG1 
682  C CG2 . ILE A 84  ? 1.3641 1.1196 1.3252 0.0475  -0.0632 0.0559  128 ILE A CG2 
683  C CD1 . ILE A 84  ? 1.4410 1.1679 1.3999 0.1290  -0.0696 0.0838  128 ILE A CD1 
684  N N   . LYS A 85  ? 1.2118 1.1507 1.3126 0.0471  -0.0737 0.0094  129 LYS A N   
685  C CA  . LYS A 85  ? 1.1890 1.1544 1.3032 0.0233  -0.0712 -0.0072 129 LYS A CA  
686  C C   . LYS A 85  ? 1.2198 1.1862 1.2967 0.0123  -0.0788 -0.0025 129 LYS A C   
687  O O   . LYS A 85  ? 1.2274 1.1877 1.2922 -0.0056 -0.0703 -0.0074 129 LYS A O   
688  C CB  . LYS A 85  ? 1.1635 1.1808 1.3242 0.0215  -0.0756 -0.0242 129 LYS A CB  
689  C CG  . LYS A 85  ? 1.1459 1.1784 1.3173 -0.0006 -0.0701 -0.0444 129 LYS A CG  
690  C CD  . LYS A 85  ? 1.1396 1.2146 1.3504 -0.0090 -0.0753 -0.0641 129 LYS A CD  
691  C CE  . LYS A 85  ? 1.1280 1.2069 1.3836 -0.0083 -0.0628 -0.0669 129 LYS A CE  
692  N NZ  . LYS A 85  ? 1.1291 1.2445 1.4230 -0.0254 -0.0656 -0.0876 129 LYS A NZ  
693  N N   . ASP A 86  ? 1.2499 1.2296 1.3089 0.0255  -0.0941 0.0091  130 ASP A N   
694  C CA  . ASP A 86  ? 1.2684 1.2614 1.2925 0.0169  -0.1025 0.0137  130 ASP A CA  
695  C C   . ASP A 86  ? 1.2932 1.2388 1.2744 0.0049  -0.0926 0.0304  130 ASP A C   
696  O O   . ASP A 86  ? 1.3065 1.2638 1.2722 -0.0135 -0.0874 0.0254  130 ASP A O   
697  C CB  . ASP A 86  ? 1.3018 1.3231 1.3142 0.0375  -0.1220 0.0277  130 ASP A CB  
698  C CG  . ASP A 86  ? 1.2879 1.3730 1.3440 0.0421  -0.1349 0.0095  130 ASP A CG  
699  O OD1 . ASP A 86  ? 1.2376 1.3350 1.3324 0.0280  -0.1264 -0.0137 130 ASP A OD1 
700  O OD2 . ASP A 86  ? 1.3294 1.4534 1.3806 0.0589  -0.1534 0.0202  130 ASP A OD2 
701  N N   . LEU A 87  ? 1.3119 1.2043 1.2740 0.0144  -0.0886 0.0489  131 LEU A N   
702  C CA  . LEU A 87  ? 1.3427 1.1854 1.2620 -0.0020 -0.0801 0.0656  131 LEU A CA  
703  C C   . LEU A 87  ? 1.3013 1.1420 1.2326 -0.0275 -0.0662 0.0521  131 LEU A C   
704  O O   . LEU A 87  ? 1.3295 1.1650 1.2371 -0.0506 -0.0599 0.0590  131 LEU A O   
705  C CB  . LEU A 87  ? 1.3980 1.1747 1.2916 0.0152  -0.0786 0.0852  131 LEU A CB  
706  C CG  . LEU A 87  ? 1.4720 1.1875 1.3128 -0.0022 -0.0719 0.1072  131 LEU A CG  
707  C CD1 . LEU A 87  ? 1.5164 1.2428 1.3245 0.0047  -0.0809 0.1306  131 LEU A CD1 
708  C CD2 . LEU A 87  ? 1.5321 1.1660 1.3497 0.0093  -0.0645 0.1165  131 LEU A CD2 
709  N N   . ALA A 88  ? 1.2484 1.0991 1.2172 -0.0227 -0.0611 0.0355  132 ALA A N   
710  C CA  . ALA A 88  ? 1.2118 1.0690 1.1945 -0.0412 -0.0492 0.0253  132 ALA A CA  
711  C C   . ALA A 88  ? 1.1834 1.0876 1.1771 -0.0531 -0.0457 0.0159  132 ALA A C   
712  O O   . ALA A 88  ? 1.1823 1.0958 1.1717 -0.0707 -0.0367 0.0171  132 ALA A O   
713  C CB  . ALA A 88  ? 1.1787 1.0390 1.1964 -0.0292 -0.0442 0.0133  132 ALA A CB  
714  N N   . HIS A 89  ? 1.1716 1.1079 1.1791 -0.0432 -0.0525 0.0054  133 HIS A N   
715  C CA  . HIS A 89  ? 1.1559 1.1295 1.1681 -0.0508 -0.0477 -0.0078 133 HIS A CA  
716  C C   . HIS A 89  ? 1.1963 1.1754 1.1678 -0.0625 -0.0478 0.0054  133 HIS A C   
717  O O   . HIS A 89  ? 1.2079 1.2101 1.1768 -0.0730 -0.0365 0.0017  133 HIS A O   
718  C CB  . HIS A 89  ? 1.1378 1.1389 1.1720 -0.0415 -0.0556 -0.0274 133 HIS A CB  
719  C CG  . HIS A 89  ? 1.0988 1.1005 1.1768 -0.0361 -0.0503 -0.0411 133 HIS A CG  
720  N ND1 . HIS A 89  ? 1.0867 1.1109 1.1912 -0.0344 -0.0554 -0.0605 133 HIS A ND1 
721  C CD2 . HIS A 89  ? 1.0736 1.0580 1.1717 -0.0343 -0.0398 -0.0375 133 HIS A CD2 
722  C CE1 . HIS A 89  ? 1.0646 1.0819 1.2055 -0.0322 -0.0462 -0.0658 133 HIS A CE1 
723  N NE2 . HIS A 89  ? 1.0506 1.0450 1.1868 -0.0299 -0.0368 -0.0513 133 HIS A NE2 
724  N N   . GLN A 90  ? 1.2326 1.1923 1.1727 -0.0580 -0.0589 0.0234  134 GLN A N   
725  C CA  . GLN A 90  ? 1.2725 1.2317 1.1695 -0.0697 -0.0579 0.0422  134 GLN A CA  
726  C C   . GLN A 90  ? 1.2841 1.2260 1.1708 -0.0933 -0.0444 0.0542  134 GLN A C   
727  O O   . GLN A 90  ? 1.2995 1.2646 1.1671 -0.1093 -0.0362 0.0619  134 GLN A O   
728  C CB  . GLN A 90  ? 1.3213 1.2517 1.1862 -0.0568 -0.0708 0.0652  134 GLN A CB  
729  C CG  . GLN A 90  ? 1.3232 1.2912 1.1918 -0.0370 -0.0871 0.0571  134 GLN A CG  
730  C CD  . GLN A 90  ? 1.3717 1.3159 1.2151 -0.0162 -0.1003 0.0835  134 GLN A CD  
731  O OE1 . GLN A 90  ? 1.4070 1.2954 1.2226 -0.0166 -0.0951 0.1088  134 GLN A OE1 
732  N NE2 . GLN A 90  ? 1.3796 1.3662 1.2317 0.0024  -0.1175 0.0779  134 GLN A NE2 
733  N N   . PHE A 91  ? 1.2864 1.1928 1.1852 -0.0966 -0.0422 0.0551  135 PHE A N   
734  C CA  . PHE A 91  ? 1.3018 1.1958 1.1924 -0.1232 -0.0324 0.0632  135 PHE A CA  
735  C C   . PHE A 91  ? 1.2612 1.2133 1.1800 -0.1314 -0.0216 0.0511  135 PHE A C   
736  O O   . PHE A 91  ? 1.2718 1.2487 1.1801 -0.1537 -0.0132 0.0609  135 PHE A O   
737  C CB  . PHE A 91  ? 1.3122 1.1568 1.2058 -0.1227 -0.0337 0.0614  135 PHE A CB  
738  C CG  . PHE A 91  ? 1.3397 1.1744 1.2242 -0.1543 -0.0264 0.0650  135 PHE A CG  
739  C CD1 . PHE A 91  ? 1.3013 1.1846 1.2167 -0.1622 -0.0205 0.0538  135 PHE A CD1 
740  C CD2 . PHE A 91  ? 1.4116 1.1894 1.2556 -0.1773 -0.0256 0.0802  135 PHE A CD2 
741  C CE1 . PHE A 91  ? 1.3204 1.2081 1.2289 -0.1933 -0.0168 0.0569  135 PHE A CE1 
742  C CE2 . PHE A 91  ? 1.4331 1.2061 1.2687 -0.2133 -0.0206 0.0803  135 PHE A CE2 
743  C CZ  . PHE A 91  ? 1.3843 1.2187 1.2533 -0.2219 -0.0176 0.0682  135 PHE A CZ  
744  N N   . THR A 92  ? 1.2226 1.1964 1.1780 -0.1126 -0.0203 0.0318  136 THR A N   
745  C CA  . THR A 92  ? 1.1975 1.2183 1.1810 -0.1120 -0.0081 0.0220  136 THR A CA  
746  C C   . THR A 92  ? 1.2296 1.2896 1.2058 -0.1082 -0.0012 0.0167  136 THR A C   
747  O O   . THR A 92  ? 1.2092 1.3110 1.1985 -0.1092 0.0121  0.0148  136 THR A O   
748  C CB  . THR A 92  ? 1.1459 1.1655 1.1665 -0.0927 -0.0063 0.0063  136 THR A CB  
749  O OG1 . THR A 92  ? 1.1339 1.1434 1.1595 -0.0769 -0.0136 -0.0061 136 THR A OG1 
750  C CG2 . THR A 92  ? 1.1380 1.1283 1.1640 -0.0955 -0.0095 0.0106  136 THR A CG2 
751  N N   . GLN A 93  ? 1.2861 1.3367 1.2403 -0.1012 -0.0101 0.0142  137 GLN A N   
752  C CA  . GLN A 93  ? 1.3261 1.4117 1.2631 -0.0984 -0.0044 0.0073  137 GLN A CA  
753  C C   . GLN A 93  ? 1.3726 1.4764 1.2794 -0.1190 0.0031  0.0300  137 GLN A C   
754  O O   . GLN A 93  ? 1.3920 1.5398 1.2941 -0.1195 0.0168  0.0268  137 GLN A O   
755  C CB  . GLN A 93  ? 1.3531 1.4302 1.2731 -0.0868 -0.0192 -0.0017 137 GLN A CB  
756  C CG  . GLN A 93  ? 1.3936 1.5069 1.2907 -0.0832 -0.0145 -0.0153 137 GLN A CG  
757  C CD  . GLN A 93  ? 1.3899 1.5229 1.3124 -0.0732 0.0003  -0.0440 137 GLN A CD  
758  O OE1 . GLN A 93  ? 1.3818 1.5332 1.3181 -0.0733 0.0182  -0.0415 137 GLN A OE1 
759  N NE2 . GLN A 93  ? 1.3990 1.5289 1.3271 -0.0645 -0.0065 -0.0712 137 GLN A NE2 
760  N N   . VAL A 94  ? 1.4049 1.4723 1.2905 -0.1360 -0.0036 0.0529  138 VAL A N   
761  C CA  . VAL A 94  ? 1.4392 1.5156 1.2972 -0.1630 0.0043  0.0772  138 VAL A CA  
762  C C   . VAL A 94  ? 1.4176 1.5283 1.3032 -0.1811 0.0161  0.0784  138 VAL A C   
763  O O   . VAL A 94  ? 1.4151 1.5844 1.3068 -0.1867 0.0303  0.0805  138 VAL A O   
764  C CB  . VAL A 94  ? 1.4898 1.5023 1.3126 -0.1757 -0.0053 0.1008  138 VAL A CB  
765  C CG1 . VAL A 94  ? 1.5414 1.5522 1.3391 -0.2124 0.0048  0.1264  138 VAL A CG1 
766  C CG2 . VAL A 94  ? 1.5190 1.5135 1.3124 -0.1550 -0.0170 0.1064  138 VAL A CG2 
767  N N   . GLN A 95  ? 1.4102 1.4899 1.3117 -0.1883 0.0102  0.0770  139 GLN A N   
768  C CA  . GLN A 95  ? 1.3950 1.5121 1.3225 -0.2052 0.0172  0.0778  139 GLN A CA  
769  C C   . GLN A 95  ? 1.3339 1.4841 1.3026 -0.1758 0.0216  0.0586  139 GLN A C   
770  O O   . GLN A 95  ? 1.3274 1.4436 1.3100 -0.1602 0.0143  0.0476  139 GLN A O   
771  C CB  . GLN A 95  ? 1.4380 1.5036 1.3537 -0.2295 0.0086  0.0840  139 GLN A CB  
772  C CG  . GLN A 95  ? 1.4363 1.5460 1.3772 -0.2492 0.0116  0.0828  139 GLN A CG  
773  C CD  . GLN A 95  ? 1.5030 1.5646 1.4204 -0.2853 0.0047  0.0878  139 GLN A CD  
774  O OE1 . GLN A 95  ? 1.5823 1.5678 1.4632 -0.2939 0.0000  0.0937  139 GLN A OE1 
775  N NE2 . GLN A 95  ? 1.5037 1.6092 1.4400 -0.3061 0.0041  0.0851  139 GLN A NE2 
776  N N   . ARG A 96  ? 1.2989 1.5146 1.2863 -0.1675 0.0360  0.0569  140 ARG A N   
777  C CA  . ARG A 96  ? 1.2549 1.4908 1.2722 -0.1332 0.0446  0.0391  140 ARG A CA  
778  C C   . ARG A 96  ? 1.2106 1.4666 1.2629 -0.1261 0.0465  0.0398  140 ARG A C   
779  O O   . ARG A 96  ? 1.1898 1.4437 1.2659 -0.0972 0.0529  0.0277  140 ARG A O   
780  C CB  . ARG A 96  ? 1.2606 1.5522 1.2780 -0.1211 0.0624  0.0366  140 ARG A CB  
781  C CG  . ARG A 96  ? 1.2841 1.5595 1.2651 -0.1195 0.0615  0.0306  140 ARG A CG  
782  C CD  . ARG A 96  ? 1.2783 1.5066 1.2574 -0.0977 0.0526  0.0071  140 ARG A CD  
783  N NE  . ARG A 96  ? 1.3021 1.5313 1.2476 -0.0927 0.0523  -0.0029 140 ARG A NE  
784  C CZ  . ARG A 96  ? 1.3160 1.5812 1.2535 -0.0787 0.0691  -0.0165 140 ARG A CZ  
785  N NH1 . ARG A 96  ? 1.2948 1.5972 1.2592 -0.0644 0.0890  -0.0196 140 ARG A NH1 
786  N NH2 . ARG A 96  ? 1.3539 1.6197 1.2543 -0.0765 0.0665  -0.0269 140 ARG A NH2 
787  N N   . ASP A 97  ? 1.2043 1.4788 1.2573 -0.1538 0.0413  0.0540  141 ASP A N   
788  C CA  . ASP A 97  ? 1.1747 1.4824 1.2573 -0.1481 0.0418  0.0568  141 ASP A CA  
789  C C   . ASP A 97  ? 1.1567 1.4041 1.2375 -0.1429 0.0301  0.0486  141 ASP A C   
790  O O   . ASP A 97  ? 1.1325 1.3990 1.2356 -0.1299 0.0311  0.0495  141 ASP A O   
791  C CB  . ASP A 97  ? 1.1846 1.5547 1.2709 -0.1820 0.0407  0.0730  141 ASP A CB  
792  C CG  . ASP A 97  ? 1.2263 1.5543 1.2784 -0.2275 0.0284  0.0784  141 ASP A CG  
793  O OD1 . ASP A 97  ? 1.2655 1.5182 1.2886 -0.2280 0.0224  0.0734  141 ASP A OD1 
794  O OD2 . ASP A 97  ? 1.2314 1.6026 1.2861 -0.2620 0.0250  0.0878  141 ASP A OD2 
795  N N   . MET A 98  ? 1.1701 1.3496 1.2240 -0.1500 0.0202  0.0430  142 MET A N   
796  C CA  . MET A 98  ? 1.1661 1.2910 1.2193 -0.1398 0.0119  0.0345  142 MET A CA  
797  C C   . MET A 98  ? 1.1337 1.2434 1.2069 -0.1068 0.0165  0.0218  142 MET A C   
798  O O   . MET A 98  ? 1.1312 1.2431 1.2005 -0.0984 0.0199  0.0157  142 MET A O   
799  C CB  . MET A 98  ? 1.2196 1.2804 1.2366 -0.1575 0.0010  0.0360  142 MET A CB  
800  C CG  . MET A 98  ? 1.2429 1.2686 1.2478 -0.1700 -0.0057 0.0341  142 MET A CG  
801  S SD  . MET A 98  ? 1.2715 1.3342 1.2649 -0.2131 -0.0074 0.0420  142 MET A SD  
802  C CE  . MET A 98  ? 1.3403 1.3280 1.2831 -0.2465 -0.0127 0.0478  142 MET A CE  
803  N N   . PHE A 99  ? 1.1049 1.1993 1.1968 -0.0913 0.0169  0.0171  143 PHE A N   
804  C CA  . PHE A 99  ? 1.0811 1.1596 1.1955 -0.0659 0.0226  0.0056  143 PHE A CA  
805  C C   . PHE A 99  ? 1.0543 1.0884 1.1681 -0.0619 0.0148  0.0007  143 PHE A C   
806  O O   . PHE A 99  ? 1.0465 1.0706 1.1542 -0.0674 0.0117  0.0059  143 PHE A O   
807  C CB  . PHE A 99  ? 1.0785 1.1872 1.2227 -0.0464 0.0366  0.0089  143 PHE A CB  
808  C CG  . PHE A 99  ? 1.0983 1.2509 1.2505 -0.0377 0.0492  0.0114  143 PHE A CG  
809  C CD1 . PHE A 99  ? 1.1051 1.3081 1.2506 -0.0523 0.0491  0.0244  143 PHE A CD1 
810  C CD2 . PHE A 99  ? 1.1112 1.2553 1.2773 -0.0154 0.0628  -0.0003 143 PHE A CD2 
811  C CE1 . PHE A 99  ? 1.1111 1.3627 1.2666 -0.0402 0.0632  0.0279  143 PHE A CE1 
812  C CE2 . PHE A 99  ? 1.1202 1.3014 1.2907 -0.0021 0.0776  0.0003  143 PHE A CE2 
813  C CZ  . PHE A 99  ? 1.1198 1.3587 1.2865 -0.0122 0.0782  0.0157  143 PHE A CZ  
814  N N   . THR A 100 ? 1.0318 1.0451 1.1516 -0.0522 0.0119  -0.0104 144 THR A N   
815  C CA  . THR A 100 ? 1.0034 0.9901 1.1357 -0.0429 0.0083  -0.0152 144 THR A CA  
816  C C   . THR A 100 ? 0.9773 0.9708 1.1445 -0.0290 0.0207  -0.0217 144 THR A C   
817  O O   . THR A 100 ? 0.9672 0.9784 1.1444 -0.0237 0.0320  -0.0218 144 THR A O   
818  C CB  . THR A 100 ? 1.0043 0.9738 1.1248 -0.0424 -0.0041 -0.0207 144 THR A CB  
819  O OG1 . THR A 100 ? 0.9850 0.9709 1.1114 -0.0409 -0.0035 -0.0326 144 THR A OG1 
820  C CG2 . THR A 100 ? 1.0296 0.9803 1.1121 -0.0537 -0.0137 -0.0099 144 THR A CG2 
821  N N   . LEU A 101 ? 0.9260 1.0866 0.9906 -0.0682 0.0858  -0.0122 145 LEU A N   
822  C CA  . LEU A 101 ? 0.9043 1.0754 0.9499 -0.0476 0.0772  -0.0100 145 LEU A CA  
823  C C   . LEU A 101 ? 0.8936 1.0580 0.9239 -0.0336 0.0796  0.0068  145 LEU A C   
824  O O   . LEU A 101 ? 0.8828 1.0659 0.9063 -0.0191 0.0759  0.0085  145 LEU A O   
825  C CB  . LEU A 101 ? 0.9063 1.0509 0.9438 -0.0425 0.0733  -0.0163 145 LEU A CB  
826  C CG  . LEU A 101 ? 0.8878 1.0391 0.9066 -0.0249 0.0660  -0.0124 145 LEU A CG  
827  C CD1 . LEU A 101 ? 0.8822 1.0760 0.9010 -0.0238 0.0591  -0.0199 145 LEU A CD1 
828  C CD2 . LEU A 101 ? 0.8962 1.0206 0.9092 -0.0213 0.0655  -0.0163 145 LEU A CD2 
829  N N   . GLU A 102 ? 0.9040 1.0425 0.9297 -0.0381 0.0859  0.0193  146 GLU A N   
830  C CA  . GLU A 102 ? 0.9020 1.0353 0.9087 -0.0272 0.0878  0.0319  146 GLU A CA  
831  C C   . GLU A 102 ? 0.8933 1.0587 0.9031 -0.0300 0.0964  0.0338  146 GLU A C   
832  O O   . GLU A 102 ? 0.8876 1.0566 0.8816 -0.0216 0.1000  0.0385  146 GLU A O   
833  C CB  . GLU A 102 ? 0.9299 1.0308 0.9278 -0.0304 0.0890  0.0470  146 GLU A CB  
834  C CG  . GLU A 102 ? 0.9332 1.0067 0.9304 -0.0230 0.0812  0.0450  146 GLU A CG  
835  C CD  . GLU A 102 ? 0.9477 1.0116 0.9656 -0.0309 0.0810  0.0316  146 GLU A CD  
836  O OE1 . GLU A 102 ? 0.9680 1.0243 1.0032 -0.0456 0.0873  0.0322  146 GLU A OE1 
837  O OE2 . GLU A 102 ? 0.9531 1.0175 0.9700 -0.0240 0.0758  0.0195  146 GLU A OE2 
838  N N   . ASP A 103 ? 0.8857 1.0780 0.9173 -0.0429 0.1005  0.0273  147 ASP A N   
839  C CA  . ASP A 103 ? 0.8827 1.1142 0.9240 -0.0457 0.1098  0.0268  147 ASP A CA  
840  C C   . ASP A 103 ? 0.8443 1.1099 0.8951 -0.0281 0.1041  0.0163  147 ASP A C   
841  O O   . ASP A 103 ? 0.8405 1.1430 0.9039 -0.0243 0.1113  0.0136  147 ASP A O   
842  C CB  . ASP A 103 ? 0.9050 1.1525 0.9698 -0.0708 0.1181  0.0263  147 ASP A CB  
843  C CG  . ASP A 103 ? 0.9329 1.1456 0.9913 -0.0872 0.1264  0.0434  147 ASP A CG  
844  O OD1 . ASP A 103 ? 0.9379 1.1444 0.9745 -0.0828 0.1322  0.0586  147 ASP A OD1 
845  O OD2 . ASP A 103 ? 0.9432 1.1359 1.0191 -0.1045 0.1271  0.0415  147 ASP A OD2 
846  N N   . THR A 104 ? 0.8101 1.0653 0.8567 -0.0168 0.0919  0.0122  148 THR A N   
847  C CA  . THR A 104 ? 0.7871 1.0642 0.8386 0.0038  0.0853  0.0099  148 THR A CA  
848  C C   . THR A 104 ? 0.7933 1.0435 0.8267 0.0213  0.0878  0.0141  148 THR A C   
849  O O   . THR A 104 ? 0.7957 1.0143 0.8099 0.0163  0.0909  0.0177  148 THR A O   
850  C CB  . THR A 104 ? 0.7679 1.0492 0.8198 0.0059  0.0720  0.0069  148 THR A CB  
851  O OG1 . THR A 104 ? 0.7553 0.9936 0.7857 0.0082  0.0689  0.0100  148 THR A OG1 
852  C CG2 . THR A 104 ? 0.7668 1.0729 0.8344 -0.0151 0.0694  -0.0036 148 THR A CG2 
853  N N   . LEU A 105 ? 0.7949 1.0584 0.8370 0.0417  0.0858  0.0136  149 LEU A N   
854  C CA  . LEU A 105 ? 0.8030 1.0406 0.8337 0.0572  0.0898  0.0127  149 LEU A CA  
855  C C   . LEU A 105 ? 0.7975 0.9927 0.8062 0.0554  0.0830  0.0167  149 LEU A C   
856  O O   . LEU A 105 ? 0.7903 0.9618 0.7814 0.0507  0.0869  0.0148  149 LEU A O   
857  C CB  . LEU A 105 ? 0.8129 1.0676 0.8648 0.0807  0.0883  0.0131  149 LEU A CB  
858  C CG  . LEU A 105 ? 0.8296 1.0510 0.8761 0.0974  0.0928  0.0096  149 LEU A CG  
859  C CD1 . LEU A 105 ? 0.8361 1.0547 0.8733 0.0936  0.1072  -0.0045 149 LEU A CD1 
860  C CD2 . LEU A 105 ? 0.8459 1.0790 0.9198 0.1227  0.0906  0.0145  149 LEU A CD2 
861  N N   . LEU A 106 ? 0.7985 0.9909 0.8085 0.0583  0.0728  0.0223  150 LEU A N   
862  C CA  . LEU A 106 ? 0.8038 0.9626 0.7974 0.0579  0.0678  0.0260  150 LEU A CA  
863  C C   . LEU A 106 ? 0.7968 0.9371 0.7775 0.0422  0.0688  0.0237  150 LEU A C   
864  O O   . LEU A 106 ? 0.7855 0.9000 0.7538 0.0422  0.0686  0.0240  150 LEU A O   
865  C CB  . LEU A 106 ? 0.8071 0.9778 0.8030 0.0606  0.0584  0.0330  150 LEU A CB  
866  C CG  . LEU A 106 ? 0.8268 1.0160 0.8366 0.0790  0.0547  0.0427  150 LEU A CG  
867  C CD1 . LEU A 106 ? 0.8342 1.0358 0.8380 0.0799  0.0446  0.0541  150 LEU A CD1 
868  C CD2 . LEU A 106 ? 0.8419 1.0008 0.8543 0.0942  0.0608  0.0446  150 LEU A CD2 
869  N N   . GLY A 107 ? 0.7949 0.9492 0.7824 0.0290  0.0696  0.0217  151 GLY A N   
870  C CA  . GLY A 107 ? 0.8024 0.9369 0.7842 0.0163  0.0712  0.0228  151 GLY A CA  
871  C C   . GLY A 107 ? 0.8216 0.9467 0.7920 0.0153  0.0770  0.0278  151 GLY A C   
872  O O   . GLY A 107 ? 0.8310 0.9348 0.7905 0.0134  0.0747  0.0326  151 GLY A O   
873  N N   . TYR A 108 ? 0.8292 0.9763 0.8027 0.0166  0.0846  0.0261  152 TYR A N   
874  C CA  . TYR A 108 ? 0.8422 0.9907 0.8012 0.0140  0.0921  0.0288  152 TYR A CA  
875  C C   . TYR A 108 ? 0.8389 0.9692 0.7808 0.0231  0.0888  0.0244  152 TYR A C   
876  O O   . TYR A 108 ? 0.8536 0.9764 0.7780 0.0179  0.0880  0.0292  152 TYR A O   
877  C CB  . TYR A 108 ? 0.8621 1.0446 0.8313 0.0154  0.1030  0.0232  152 TYR A CB  
878  C CG  . TYR A 108 ? 0.8890 1.0840 0.8419 0.0098  0.1141  0.0242  152 TYR A CG  
879  C CD1 . TYR A 108 ? 0.9075 1.0985 0.8428 0.0185  0.1168  0.0145  152 TYR A CD1 
880  C CD2 . TYR A 108 ? 0.9091 1.1228 0.8638 -0.0061 0.1232  0.0338  152 TYR A CD2 
881  C CE1 . TYR A 108 ? 0.9362 1.1462 0.8520 0.0120  0.1275  0.0126  152 TYR A CE1 
882  C CE2 . TYR A 108 ? 0.9431 1.1744 0.8787 -0.0127 0.1346  0.0371  152 TYR A CE2 
883  C CZ  . TYR A 108 ? 0.9555 1.1877 0.8695 -0.0032 0.1365  0.0256  152 TYR A CZ  
884  O OH  . TYR A 108 ? 0.9747 1.2313 0.8652 -0.0112 0.1482  0.0264  152 TYR A OH  
885  N N   . LEU A 109 ? 0.8266 0.9514 0.7752 0.0358  0.0864  0.0166  153 LEU A N   
886  C CA  . LEU A 109 ? 0.8414 0.9476 0.7795 0.0424  0.0853  0.0090  153 LEU A CA  
887  C C   . LEU A 109 ? 0.8442 0.9310 0.7708 0.0354  0.0767  0.0143  153 LEU A C   
888  O O   . LEU A 109 ? 0.8412 0.9243 0.7530 0.0322  0.0758  0.0099  153 LEU A O   
889  C CB  . LEU A 109 ? 0.8351 0.9328 0.7880 0.0561  0.0842  0.0057  153 LEU A CB  
890  C CG  . LEU A 109 ? 0.8423 0.9592 0.8126 0.0690  0.0922  -0.0002 153 LEU A CG  
891  C CD1 . LEU A 109 ? 0.8502 0.9511 0.8357 0.0849  0.0899  0.0018  153 LEU A CD1 
892  C CD2 . LEU A 109 ? 0.8587 0.9849 0.8213 0.0689  0.1038  -0.0152 153 LEU A CD2 
893  N N   . ALA A 110 ? 0.8453 0.9249 0.7802 0.0330  0.0705  0.0217  154 ALA A N   
894  C CA  . ALA A 110 ? 0.8471 0.9106 0.7792 0.0305  0.0634  0.0241  154 ALA A CA  
895  C C   . ALA A 110 ? 0.8551 0.9173 0.7873 0.0233  0.0601  0.0333  154 ALA A C   
896  O O   . ALA A 110 ? 0.8848 0.9380 0.8202 0.0230  0.0544  0.0355  154 ALA A O   
897  C CB  . ALA A 110 ? 0.8397 0.8981 0.7816 0.0339  0.0610  0.0242  154 ALA A CB  
898  N N   . ASP A 111 ? 0.8554 0.9263 0.7874 0.0179  0.0645  0.0399  155 ASP A N   
899  C CA  . ASP A 111 ? 0.8582 0.9213 0.7949 0.0118  0.0626  0.0526  155 ASP A CA  
900  C C   . ASP A 111 ? 0.8662 0.9281 0.7892 0.0128  0.0562  0.0620  155 ASP A C   
901  O O   . ASP A 111 ? 0.8797 0.9553 0.7838 0.0117  0.0575  0.0610  155 ASP A O   
902  C CB  . ASP A 111 ? 0.8745 0.9461 0.8154 0.0028  0.0706  0.0598  155 ASP A CB  
903  C CG  . ASP A 111 ? 0.8945 0.9497 0.8454 -0.0041 0.0702  0.0755  155 ASP A CG  
904  O OD1 . ASP A 111 ? 0.8916 0.9298 0.8600 -0.0028 0.0672  0.0716  155 ASP A OD1 
905  O OD2 . ASP A 111 ? 0.9229 0.9823 0.8650 -0.0107 0.0742  0.0918  155 ASP A OD2 
906  N N   . ASP A 112 ? 0.8702 0.9202 0.8047 0.0153  0.0493  0.0693  156 ASP A N   
907  C CA  . ASP A 112 ? 0.8832 0.9378 0.8109 0.0179  0.0400  0.0814  156 ASP A CA  
908  C C   . ASP A 112 ? 0.8534 0.9201 0.7687 0.0195  0.0348  0.0679  156 ASP A C   
909  O O   . ASP A 112 ? 0.8566 0.9389 0.7581 0.0184  0.0272  0.0734  156 ASP A O   
910  C CB  . ASP A 112 ? 0.9313 0.9950 0.8433 0.0129  0.0407  0.1020  156 ASP A CB  
911  C CG  . ASP A 112 ? 0.9578 1.0040 0.8861 0.0087  0.0465  0.1187  156 ASP A CG  
912  O OD1 . ASP A 112 ? 0.9536 0.9815 0.9061 0.0095  0.0498  0.1096  156 ASP A OD1 
913  O OD2 . ASP A 112 ? 0.9898 1.0417 0.9060 0.0031  0.0485  0.1403  156 ASP A OD2 
914  N N   . LEU A 113 ? 0.8343 0.8948 0.7555 0.0208  0.0385  0.0511  157 LEU A N   
915  C CA  . LEU A 113 ? 0.8466 0.9111 0.7616 0.0199  0.0359  0.0373  157 LEU A CA  
916  C C   . LEU A 113 ? 0.8512 0.9083 0.7844 0.0215  0.0336  0.0328  157 LEU A C   
917  O O   . LEU A 113 ? 0.8183 0.8673 0.7640 0.0239  0.0377  0.0336  157 LEU A O   
918  C CB  . LEU A 113 ? 0.8437 0.9053 0.7504 0.0201  0.0449  0.0243  157 LEU A CB  
919  C CG  . LEU A 113 ? 0.8584 0.9344 0.7463 0.0177  0.0498  0.0223  157 LEU A CG  
920  C CD1 . LEU A 113 ? 0.8575 0.9300 0.7454 0.0214  0.0596  0.0054  157 LEU A CD1 
921  C CD2 . LEU A 113 ? 0.8731 0.9670 0.7428 0.0120  0.0423  0.0224  157 LEU A CD2 
922  N N   . THR A 114 ? 0.8766 0.9417 0.8109 0.0182  0.0277  0.0262  158 THR A N   
923  C CA  . THR A 114 ? 0.8801 0.9434 0.8315 0.0167  0.0275  0.0208  158 THR A CA  
924  C C   . THR A 114 ? 0.8955 0.9514 0.8422 0.0097  0.0314  0.0073  158 THR A C   
925  O O   . THR A 114 ? 0.9253 0.9841 0.8588 0.0057  0.0303  -0.0016 158 THR A O   
926  C CB  . THR A 114 ? 0.8876 0.9698 0.8537 0.0176  0.0175  0.0255  158 THR A CB  
927  O OG1 . THR A 114 ? 0.9049 0.9867 0.8783 0.0260  0.0148  0.0401  158 THR A OG1 
928  C CG2 . THR A 114 ? 0.8768 0.9633 0.8642 0.0153  0.0198  0.0193  158 THR A CG2 
929  N N   . TRP A 115 ? 0.8951 0.9410 0.8531 0.0076  0.0371  0.0057  159 TRP A N   
930  C CA  . TRP A 115 ? 0.9153 0.9461 0.8737 0.0008  0.0425  -0.0031 159 TRP A CA  
931  C C   . TRP A 115 ? 0.9337 0.9618 0.9065 -0.0044 0.0474  0.0009  159 TRP A C   
932  O O   . TRP A 115 ? 0.9280 0.9621 0.9045 0.0000  0.0499  0.0093  159 TRP A O   
933  C CB  . TRP A 115 ? 0.9048 0.9168 0.8539 0.0074  0.0497  -0.0036 159 TRP A CB  
934  C CG  . TRP A 115 ? 0.8846 0.8933 0.8351 0.0156  0.0538  0.0088  159 TRP A CG  
935  C CD1 . TRP A 115 ? 0.8911 0.8892 0.8467 0.0164  0.0590  0.0167  159 TRP A CD1 
936  C CD2 . TRP A 115 ? 0.8631 0.8826 0.8094 0.0222  0.0527  0.0148  159 TRP A CD2 
937  N NE1 . TRP A 115 ? 0.8700 0.8774 0.8228 0.0235  0.0595  0.0257  159 TRP A NE1 
938  C CE2 . TRP A 115 ? 0.8557 0.8749 0.8048 0.0262  0.0561  0.0225  159 TRP A CE2 
939  C CE3 . TRP A 115 ? 0.8541 0.8843 0.7950 0.0235  0.0493  0.0157  159 TRP A CE3 
940  C CZ2 . TRP A 115 ? 0.8388 0.8702 0.7873 0.0299  0.0558  0.0259  159 TRP A CZ2 
941  C CZ3 . TRP A 115 ? 0.8401 0.8759 0.7825 0.0269  0.0509  0.0215  159 TRP A CZ3 
942  C CH2 . TRP A 115 ? 0.8367 0.8739 0.7837 0.0293  0.0539  0.0240  159 TRP A CH2 
943  N N   . CYS A 116 ? 0.9699 0.9907 0.9507 -0.0162 0.0499  -0.0066 160 CYS A N   
944  C CA  . CYS A 116 ? 0.9951 1.0087 0.9873 -0.0241 0.0580  -0.0001 160 CYS A CA  
945  C C   . CYS A 116 ? 1.0357 1.0304 1.0366 -0.0387 0.0622  -0.0102 160 CYS A C   
946  O O   . CYS A 116 ? 1.0345 1.0293 1.0333 -0.0435 0.0573  -0.0270 160 CYS A O   
947  C CB  . CYS A 116 ? 0.9783 1.0209 0.9848 -0.0277 0.0569  0.0019  160 CYS A CB  
948  S SG  . CYS A 116 ? 0.9742 1.0452 1.0002 -0.0403 0.0482  -0.0121 160 CYS A SG  
949  N N   . GLY A 117 ? 1.0747 1.0538 1.0849 -0.0472 0.0720  -0.0002 161 GLY A N   
950  C CA  . GLY A 117 ? 1.1307 1.0837 1.1540 -0.0633 0.0787  -0.0077 161 GLY A CA  
951  C C   . GLY A 117 ? 1.1572 1.1184 1.1973 -0.0809 0.0865  0.0009  161 GLY A C   
952  O O   . GLY A 117 ? 1.1614 1.1418 1.1985 -0.0773 0.0899  0.0167  161 GLY A O   
953  N N   . GLU A 118 ? 1.2036 1.1522 1.2619 -0.1018 0.0907  -0.0117 162 GLU A N   
954  C CA  . GLU A 118 ? 1.2313 1.1904 1.3097 -0.1234 0.0997  -0.0054 162 GLU A CA  
955  C C   . GLU A 118 ? 1.2713 1.1920 1.3484 -0.1257 0.1144  0.0217  162 GLU A C   
956  O O   . GLU A 118 ? 1.3093 1.1904 1.3772 -0.1124 0.1163  0.0303  162 GLU A O   
957  C CB  . GLU A 118 ? 1.2569 1.2191 1.3579 -0.1480 0.0981  -0.0313 162 GLU A CB  
958  C CG  . GLU A 118 ? 1.2389 1.2443 1.3389 -0.1453 0.0810  -0.0550 162 GLU A CG  
959  C CD  . GLU A 118 ? 1.2710 1.2878 1.3905 -0.1707 0.0766  -0.0843 162 GLU A CD  
960  O OE1 . GLU A 118 ? 1.3104 1.2999 1.4497 -0.1939 0.0888  -0.0884 162 GLU A OE1 
961  O OE2 . GLU A 118 ? 1.2603 1.3142 1.3750 -0.1684 0.0609  -0.1023 162 GLU A OE2 
962  N N   . PHE A 119 ? 1.2862 1.2226 1.3740 -0.1421 0.1249  0.0368  163 PHE A N   
963  C CA  . PHE A 119 ? 1.3321 1.2399 1.4153 -0.1456 0.1388  0.0695  163 PHE A CA  
964  C C   . PHE A 119 ? 1.3964 1.2482 1.4997 -0.1624 0.1483  0.0705  163 PHE A C   
965  O O   . PHE A 119 ? 1.4290 1.2335 1.5274 -0.1501 0.1519  0.0881  163 PHE A O   
966  C CB  . PHE A 119 ? 1.3251 1.2731 1.4111 -0.1601 0.1494  0.0850  163 PHE A CB  
967  C CG  . PHE A 119 ? 1.3589 1.2850 1.4349 -0.1654 0.1636  0.1237  163 PHE A CG  
968  C CD1 . PHE A 119 ? 1.3495 1.2847 1.3960 -0.1454 0.1619  0.1476  163 PHE A CD1 
969  C CD2 . PHE A 119 ? 1.4031 1.2992 1.4993 -0.1914 0.1783  0.1377  163 PHE A CD2 
970  C CE1 . PHE A 119 ? 1.3893 1.3101 1.4234 -0.1496 0.1730  0.1874  163 PHE A CE1 
971  C CE2 . PHE A 119 ? 1.4411 1.3158 1.5268 -0.1958 0.1912  0.1799  163 PHE A CE2 
972  C CZ  . PHE A 119 ? 1.4315 1.3208 1.4845 -0.1739 0.1877  0.2061  163 PHE A CZ  
973  N N   . ALA A 120 ? 1.4082 1.2669 1.5381 -0.1907 0.1526  0.0509  164 ALA A N   
974  C CA  . ALA A 120 ? 1.4657 1.2715 1.6209 -0.2138 0.1647  0.0494  164 ALA A CA  
975  C C   . ALA A 120 ? 1.4890 1.2456 1.6452 -0.2009 0.1599  0.0285  164 ALA A C   
976  O O   . ALA A 120 ? 1.5347 1.2322 1.6964 -0.1942 0.1692  0.0465  164 ALA A O   
977  C CB  . ALA A 120 ? 1.4698 1.3050 1.6546 -0.2480 0.1677  0.0255  164 ALA A CB  
978  N N   . THR A 121 ? 1.4535 1.2376 1.6052 -0.1964 0.1458  -0.0083 165 THR A N   
979  C CA  . THR A 121 ? 1.4523 1.2014 1.6033 -0.1867 0.1424  -0.0353 165 THR A CA  
980  C C   . THR A 121 ? 1.4133 1.1537 1.5386 -0.1503 0.1373  -0.0191 165 THR A C   
981  O O   . THR A 121 ? 1.3520 1.1215 1.4584 -0.1347 0.1330  0.0068  165 THR A O   
982  C CB  . THR A 121 ? 1.4321 1.2226 1.5836 -0.1981 0.1292  -0.0789 165 THR A CB  
983  O OG1 . THR A 121 ? 1.3572 1.2063 1.4863 -0.1809 0.1144  -0.0736 165 THR A OG1 
984  C CG2 . THR A 121 ? 1.4580 1.2649 1.6388 -0.2357 0.1323  -0.0989 165 THR A CG2 
985  N N   . SER A 122 ? 1.4374 1.1406 1.5649 -0.1384 0.1388  -0.0382 166 SER A N   
986  C CA  . SER A 122 ? 1.4182 1.1201 1.5262 -0.1055 0.1337  -0.0307 166 SER A CA  
987  C C   . SER A 122 ? 1.3779 1.1147 1.4699 -0.1007 0.1224  -0.0667 166 SER A C   
988  O O   . SER A 122 ? 1.3857 1.1085 1.4718 -0.0824 0.1233  -0.0790 166 SER A O   
989  C CB  . SER A 122 ? 1.4697 1.1081 1.5949 -0.0912 0.1456  -0.0210 166 SER A CB  
990  O OG  . SER A 122 ? 1.5185 1.1203 1.6652 -0.1046 0.1533  -0.0599 166 SER A OG  
991  N N   . LYS A 123 ? 1.3372 1.1232 1.4230 -0.1167 0.1121  -0.0811 167 LYS A N   
992  C CA  . LYS A 123 ? 1.3055 1.1304 1.3747 -0.1156 0.0999  -0.1106 167 LYS A CA  
993  C C   . LYS A 123 ? 1.2374 1.1122 1.2857 -0.1011 0.0871  -0.0921 167 LYS A C   
994  O O   . LYS A 123 ? 1.2125 1.1040 1.2650 -0.1026 0.0865  -0.0693 167 LYS A O   
995  C CB  . LYS A 123 ? 1.3243 1.1685 1.4072 -0.1457 0.0961  -0.1433 167 LYS A CB  
996  C CG  . LYS A 123 ? 1.3904 1.1847 1.4957 -0.1637 0.1090  -0.1718 167 LYS A CG  
997  C CD  . LYS A 123 ? 1.4214 1.2416 1.5414 -0.1975 0.1042  -0.2077 167 LYS A CD  
998  C CE  . LYS A 123 ? 1.4217 1.2600 1.5645 -0.2196 0.1047  -0.1910 167 LYS A CE  
999  N NZ  . LYS A 123 ? 1.4478 1.3138 1.6107 -0.2548 0.1001  -0.2284 167 LYS A NZ  
1000 N N   . ILE A 124 ? 1.1979 1.0955 1.2249 -0.0879 0.0787  -0.1033 168 ILE A N   
1001 C CA  . ILE A 124 ? 1.1362 1.0746 1.1459 -0.0744 0.0673  -0.0875 168 ILE A CA  
1002 C C   . ILE A 124 ? 1.0965 1.0806 1.1116 -0.0889 0.0551  -0.0949 168 ILE A C   
1003 O O   . ILE A 124 ? 1.1184 1.1139 1.1400 -0.1073 0.0515  -0.1201 168 ILE A O   
1004 C CB  . ILE A 124 ? 1.1416 1.0872 1.1287 -0.0580 0.0644  -0.0942 168 ILE A CB  
1005 C CG1 . ILE A 124 ? 1.1605 1.0687 1.1488 -0.0408 0.0759  -0.0853 168 ILE A CG1 
1006 C CG2 . ILE A 124 ? 1.1081 1.0930 1.0801 -0.0478 0.0528  -0.0788 168 ILE A CG2 
1007 C CD1 . ILE A 124 ? 1.1615 1.0789 1.1325 -0.0271 0.0765  -0.0957 168 ILE A CD1 
1008 N N   . ASN A 125 ? 1.0272 1.0393 1.0422 -0.0800 0.0489  -0.0745 169 ASN A N   
1009 C CA  . ASN A 125 ? 0.9834 1.0418 1.0103 -0.0879 0.0372  -0.0767 169 ASN A CA  
1010 C C   . ASN A 125 ? 0.9442 1.0348 0.9531 -0.0752 0.0228  -0.0752 169 ASN A C   
1011 O O   . ASN A 125 ? 0.9052 0.9960 0.9051 -0.0574 0.0219  -0.0570 169 ASN A O   
1012 C CB  . ASN A 125 ? 0.9541 1.0227 0.9978 -0.0855 0.0420  -0.0572 169 ASN A CB  
1013 C CG  . ASN A 125 ? 0.9354 1.0536 1.0009 -0.0924 0.0321  -0.0605 169 ASN A CG  
1014 O OD1 . ASN A 125 ? 0.9370 1.0856 1.0049 -0.0991 0.0190  -0.0747 169 ASN A OD1 
1015 N ND2 . ASN A 125 ? 0.9216 1.0536 1.0041 -0.0902 0.0384  -0.0481 169 ASN A ND2 
1016 N N   . TYR A 126 ? 0.9496 1.0690 0.9534 -0.0861 0.0116  -0.0942 170 TYR A N   
1017 C CA  . TYR A 126 ? 0.9563 1.1100 0.9401 -0.0761 -0.0027 -0.0892 170 TYR A CA  
1018 C C   . TYR A 126 ? 0.9476 1.1510 0.9496 -0.0751 -0.0187 -0.0791 170 TYR A C   
1019 O O   . TYR A 126 ? 0.9559 1.1891 0.9457 -0.0644 -0.0322 -0.0667 170 TYR A O   
1020 C CB  . TYR A 126 ? 0.9910 1.1534 0.9521 -0.0871 -0.0058 -0.1150 170 TYR A CB  
1021 C CG  . TYR A 126 ? 1.0061 1.1255 0.9504 -0.0818 0.0095  -0.1243 170 TYR A CG  
1022 C CD1 . TYR A 126 ? 1.0210 1.0966 0.9800 -0.0899 0.0245  -0.1393 170 TYR A CD1 
1023 C CD2 . TYR A 126 ? 1.0117 1.1348 0.9296 -0.0676 0.0099  -0.1157 170 TYR A CD2 
1024 C CE1 . TYR A 126 ? 1.0380 1.0759 0.9882 -0.0810 0.0383  -0.1468 170 TYR A CE1 
1025 C CE2 . TYR A 126 ? 1.0218 1.1123 0.9298 -0.0611 0.0246  -0.1251 170 TYR A CE2 
1026 C CZ  . TYR A 126 ? 1.0378 1.0860 0.9632 -0.0660 0.0383  -0.1411 170 TYR A CZ  
1027 O OH  . TYR A 126 ? 1.0559 1.0734 0.9777 -0.0558 0.0526  -0.1496 170 TYR A OH  
1028 N N   . GLN A 127 ? 0.9542 1.1682 0.9876 -0.0856 -0.0166 -0.0821 171 GLN A N   
1029 C CA  . GLN A 127 ? 0.9443 1.2108 1.0034 -0.0836 -0.0309 -0.0750 171 GLN A CA  
1030 C C   . GLN A 127 ? 0.9121 1.1763 0.9810 -0.0595 -0.0294 -0.0490 171 GLN A C   
1031 O O   . GLN A 127 ? 0.9156 1.2086 0.9865 -0.0445 -0.0435 -0.0342 171 GLN A O   
1032 C CB  . GLN A 127 ? 0.9599 1.2432 1.0529 -0.1052 -0.0267 -0.0897 171 GLN A CB  
1033 C CG  . GLN A 127 ? 0.9744 1.3255 1.0970 -0.1066 -0.0446 -0.0894 171 GLN A CG  
1034 C CD  . GLN A 127 ? 0.9941 1.3655 1.1577 -0.1242 -0.0368 -0.0982 171 GLN A CD  
1035 O OE1 . GLN A 127 ? 1.0167 1.3497 1.1857 -0.1336 -0.0168 -0.0987 171 GLN A OE1 
1036 N NE2 . GLN A 127 ? 1.0013 1.4384 1.1954 -0.1288 -0.0529 -0.1027 171 GLN A NE2 
1037 N N   . SER A 128 ? 0.8924 1.1226 0.9679 -0.0565 -0.0122 -0.0435 172 SER A N   
1038 C CA  . SER A 128 ? 0.8779 1.1052 0.9644 -0.0370 -0.0079 -0.0262 172 SER A CA  
1039 C C   . SER A 128 ? 0.8787 1.0627 0.9529 -0.0354 0.0101  -0.0225 172 SER A C   
1040 O O   . SER A 128 ? 0.8838 1.0430 0.9494 -0.0489 0.0197  -0.0297 172 SER A O   
1041 C CB  . SER A 128 ? 0.8645 1.1327 0.9909 -0.0358 -0.0103 -0.0261 172 SER A CB  
1042 O OG  . SER A 128 ? 0.8581 1.1279 1.0003 -0.0556 0.0019  -0.0375 172 SER A OG  
1043 N N   . CYS A 129 ? 0.8748 1.0506 0.9498 -0.0187 0.0141  -0.0109 173 CYS A N   
1044 C CA  . CYS A 129 ? 0.8732 1.0197 0.9373 -0.0165 0.0289  -0.0071 173 CYS A CA  
1045 C C   . CYS A 129 ? 0.8627 1.0229 0.9468 -0.0059 0.0349  -0.0044 173 CYS A C   
1046 O O   . CYS A 129 ? 0.8447 1.0246 0.9484 0.0059  0.0270  -0.0020 173 CYS A O   
1047 C CB  . CYS A 129 ? 0.8796 0.9968 0.9154 -0.0087 0.0288  -0.0014 173 CYS A CB  
1048 S SG  . CYS A 129 ? 0.9179 1.0178 0.9312 -0.0189 0.0261  -0.0101 173 CYS A SG  
1049 N N   . PRO A 130 ? 0.8736 1.0253 0.9539 -0.0092 0.0494  -0.0049 174 PRO A N   
1050 C CA  . PRO A 130 ? 0.8734 1.0433 0.9728 -0.0019 0.0580  -0.0091 174 PRO A CA  
1051 C C   . PRO A 130 ? 0.8785 1.0374 0.9786 0.0149  0.0550  -0.0081 174 PRO A C   
1052 O O   . PRO A 130 ? 0.8782 1.0120 0.9546 0.0168  0.0550  -0.0039 174 PRO A O   
1053 C CB  . PRO A 130 ? 0.8759 1.0395 0.9594 -0.0120 0.0732  -0.0082 174 PRO A CB  
1054 C CG  . PRO A 130 ? 0.8845 1.0267 0.9505 -0.0252 0.0722  -0.0010 174 PRO A CG  
1055 C CD  . PRO A 130 ? 0.8833 1.0101 0.9412 -0.0192 0.0582  -0.0010 174 PRO A CD  
1056 N N   . ASP A 131 ? 0.8835 1.0617 1.0156 0.0270  0.0530  -0.0120 175 ASP A N   
1057 C CA  . ASP A 131 ? 0.8874 1.0520 1.0296 0.0422  0.0539  -0.0131 175 ASP A CA  
1058 C C   . ASP A 131 ? 0.8970 1.0592 1.0334 0.0388  0.0704  -0.0272 175 ASP A C   
1059 O O   . ASP A 131 ? 0.9000 1.0853 1.0407 0.0307  0.0815  -0.0361 175 ASP A O   
1060 C CB  . ASP A 131 ? 0.8844 1.0693 1.0688 0.0583  0.0479  -0.0123 175 ASP A CB  
1061 C CG  . ASP A 131 ? 0.8937 1.0560 1.0947 0.0753  0.0481  -0.0102 175 ASP A CG  
1062 O OD1 . ASP A 131 ? 0.9109 1.0426 1.0882 0.0718  0.0514  -0.0093 175 ASP A OD1 
1063 O OD2 . ASP A 131 ? 0.8988 1.0742 1.1400 0.0918  0.0453  -0.0091 175 ASP A OD2 
1064 N N   . TRP A 132 ? 0.9174 1.0556 1.0431 0.0430  0.0723  -0.0293 176 TRP A N   
1065 C CA  . TRP A 132 ? 0.9420 1.0822 1.0585 0.0381  0.0857  -0.0453 176 TRP A CA  
1066 C C   . TRP A 132 ? 0.9551 1.1198 1.1038 0.0438  0.0984  -0.0656 176 TRP A C   
1067 O O   . TRP A 132 ? 0.9609 1.1493 1.1007 0.0345  0.1113  -0.0778 176 TRP A O   
1068 C CB  . TRP A 132 ? 0.9730 1.0861 1.0804 0.0404  0.0841  -0.0470 176 TRP A CB  
1069 C CG  . TRP A 132 ? 1.0066 1.1274 1.1066 0.0341  0.0963  -0.0679 176 TRP A CG  
1070 C CD1 . TRP A 132 ? 1.0135 1.1478 1.0817 0.0220  0.0999  -0.0694 176 TRP A CD1 
1071 C CD2 . TRP A 132 ? 1.0382 1.1571 1.1641 0.0392  0.1065  -0.0921 176 TRP A CD2 
1072 N NE1 . TRP A 132 ? 1.0307 1.1776 1.0989 0.0177  0.1103  -0.0933 176 TRP A NE1 
1073 C CE2 . TRP A 132 ? 1.0465 1.1823 1.1505 0.0272  0.1157  -0.1107 176 TRP A CE2 
1074 C CE3 . TRP A 132 ? 1.0497 1.1538 1.2170 0.0536  0.1087  -0.0998 176 TRP A CE3 
1075 C CZ2 . TRP A 132 ? 1.0686 1.2082 1.1891 0.0263  0.1279  -0.1423 176 TRP A CZ2 
1076 C CZ3 . TRP A 132 ? 1.0768 1.1774 1.2650 0.0550  0.1221  -0.1294 176 TRP A CZ3 
1077 C CH2 . TRP A 132 ? 1.0841 1.2028 1.2483 0.0402  0.1321  -0.1532 176 TRP A CH2 
1078 N N   . ARG A 133 ? 0.9659 1.1265 1.1529 0.0600  0.0953  -0.0678 177 ARG A N   
1079 C CA  . ARG A 133 ? 0.9710 1.1505 1.1969 0.0702  0.1086  -0.0903 177 ARG A CA  
1080 C C   . ARG A 133 ? 0.9400 1.1611 1.1880 0.0701  0.1115  -0.0912 177 ARG A C   
1081 O O   . ARG A 133 ? 0.9308 1.1827 1.1853 0.0643  0.1282  -0.1105 177 ARG A O   
1082 C CB  . ARG A 133 ? 1.0037 1.1572 1.2676 0.0904  0.1042  -0.0893 177 ARG A CB  
1083 C CG  . ARG A 133 ? 1.0513 1.2200 1.3646 0.1054  0.1190  -0.1149 177 ARG A CG  
1084 C CD  . ARG A 133 ? 1.1010 1.2298 1.4474 0.1218  0.1207  -0.1202 177 ARG A CD  
1085 N NE  . ARG A 133 ? 1.1257 1.2265 1.4462 0.1082  0.1288  -0.1367 177 ARG A NE  
1086 C CZ  . ARG A 133 ? 1.1573 1.2572 1.4922 0.1063  0.1473  -0.1737 177 ARG A CZ  
1087 N NH1 . ARG A 133 ? 1.1774 1.3015 1.5526 0.1187  0.1620  -0.1993 177 ARG A NH1 
1088 N NH2 . ARG A 133 ? 1.1644 1.2437 1.4745 0.0911  0.1515  -0.1879 177 ARG A NH2 
1089 N N   . LYS A 134 ? 0.9116 1.1384 1.1708 0.0746  0.0955  -0.0711 178 LYS A N   
1090 C CA  . LYS A 134 ? 0.8951 1.1652 1.1877 0.0766  0.0955  -0.0727 178 LYS A CA  
1091 C C   . LYS A 134 ? 0.8773 1.1702 1.1450 0.0526  0.1023  -0.0724 178 LYS A C   
1092 O O   . LYS A 134 ? 0.8647 1.1981 1.1564 0.0479  0.1140  -0.0836 178 LYS A O   
1093 C CB  . LYS A 134 ? 0.8911 1.1652 1.2046 0.0889  0.0737  -0.0520 178 LYS A CB  
1094 C CG  . LYS A 134 ? 0.9149 1.1723 1.2646 0.1154  0.0676  -0.0468 178 LYS A CG  
1095 C CD  . LYS A 134 ? 0.9265 1.2063 1.3054 0.1302  0.0465  -0.0253 178 LYS A CD  
1096 C CE  . LYS A 134 ? 0.9303 1.1953 1.2691 0.1208  0.0267  -0.0011 178 LYS A CE  
1097 N NZ  . LYS A 134 ? 0.9398 1.2373 1.3038 0.1336  0.0047  0.0192  178 LYS A NZ  
1098 N N   . ASP A 135 ? 0.8690 1.1356 1.0920 0.0379  0.0961  -0.0589 179 ASP A N   
1099 C CA  . ASP A 135 ? 0.8655 1.1438 1.0680 0.0160  0.1011  -0.0534 179 ASP A CA  
1100 C C   . ASP A 135 ? 0.8897 1.1599 1.0574 0.0044  0.1159  -0.0562 179 ASP A C   
1101 O O   . ASP A 135 ? 0.8993 1.2001 1.0725 -0.0033 0.1328  -0.0665 179 ASP A O   
1102 C CB  . ASP A 135 ? 0.8482 1.1060 1.0316 0.0083  0.0846  -0.0372 179 ASP A CB  
1103 C CG  . ASP A 135 ? 0.8353 1.1106 1.0476 0.0173  0.0677  -0.0334 179 ASP A CG  
1104 O OD1 . ASP A 135 ? 0.8363 1.1524 1.0868 0.0190  0.0698  -0.0405 179 ASP A OD1 
1105 O OD2 . ASP A 135 ? 0.8361 1.0896 1.0323 0.0221  0.0526  -0.0228 179 ASP A OD2 
1106 N N   . CYS A 136 ? 0.9009 1.1357 1.0331 0.0033  0.1093  -0.0464 180 CYS A N   
1107 C CA  . CYS A 136 ? 0.9133 1.1427 1.0091 -0.0084 0.1180  -0.0412 180 CYS A CA  
1108 C C   . CYS A 136 ? 0.8869 1.0904 0.9606 -0.0010 0.1123  -0.0418 180 CYS A C   
1109 O O   . CYS A 136 ? 0.8804 1.0566 0.9502 0.0055  0.0993  -0.0334 180 CYS A O   
1110 C CB  . CYS A 136 ? 0.9377 1.1539 1.0148 -0.0227 0.1149  -0.0218 180 CYS A CB  
1111 S SG  . CYS A 136 ? 0.9911 1.2356 1.0978 -0.0370 0.1202  -0.0216 180 CYS A SG  
1112 N N   . SER A 137 ? 0.8770 1.0943 0.9351 -0.0043 0.1227  -0.0525 181 SER A N   
1113 C CA  . SER A 137 ? 0.8700 1.0715 0.9109 -0.0005 0.1184  -0.0576 181 SER A CA  
1114 C C   . SER A 137 ? 0.8535 1.0382 0.8620 -0.0056 0.1099  -0.0359 181 SER A C   
1115 O O   . SER A 137 ? 0.8634 1.0281 0.8647 -0.0006 0.1011  -0.0337 181 SER A O   
1116 C CB  . SER A 137 ? 0.8894 1.1183 0.9254 -0.0043 0.1317  -0.0809 181 SER A CB  
1117 O OG  . SER A 137 ? 0.9122 1.1724 0.9252 -0.0173 0.1419  -0.0746 181 SER A OG  
1118 N N   . ASN A 138 ? 0.8410 1.0338 0.8338 -0.0153 0.1136  -0.0192 182 ASN A N   
1119 C CA  . ASN A 138 ? 0.8330 1.0110 0.7994 -0.0177 0.1075  0.0026  182 ASN A CA  
1120 C C   . ASN A 138 ? 0.8151 0.9619 0.7890 -0.0161 0.0995  0.0162  182 ASN A C   
1121 O O   . ASN A 138 ? 0.8071 0.9456 0.7750 -0.0235 0.1021  0.0328  182 ASN A O   
1122 C CB  . ASN A 138 ? 0.8520 1.0540 0.7962 -0.0288 0.1169  0.0165  182 ASN A CB  
1123 C CG  . ASN A 138 ? 0.8576 1.0991 0.7906 -0.0329 0.1260  -0.0014 182 ASN A CG  
1124 O OD1 . ASN A 138 ? 0.8431 1.0902 0.7671 -0.0289 0.1210  -0.0133 182 ASN A OD1 
1125 N ND2 . ASN A 138 ? 0.8710 1.1433 0.8052 -0.0428 0.1406  -0.0059 182 ASN A ND2 
1126 N N   . ASN A 139 ? 0.8061 0.9355 0.7926 -0.0073 0.0904  0.0088  183 ASN A N   
1127 C CA  . ASN A 139 ? 0.7980 0.9040 0.7894 -0.0064 0.0826  0.0158  183 ASN A CA  
1128 C C   . ASN A 139 ? 0.8052 0.8900 0.7806 -0.0001 0.0758  0.0238  183 ASN A C   
1129 O O   . ASN A 139 ? 0.8039 0.8938 0.7715 0.0048  0.0744  0.0211  183 ASN A O   
1130 C CB  . ASN A 139 ? 0.7765 0.8854 0.7905 -0.0017 0.0766  0.0058  183 ASN A CB  
1131 C CG  . ASN A 139 ? 0.7669 0.8735 0.7868 0.0089  0.0727  -0.0016 183 ASN A CG  
1132 O OD1 . ASN A 139 ? 0.7816 0.8717 0.7959 0.0140  0.0647  0.0027  183 ASN A OD1 
1133 N ND2 . ASN A 139 ? 0.7603 0.8828 0.7926 0.0112  0.0799  -0.0138 183 ASN A ND2 
1134 N N   . PRO A 140 ? 0.8225 0.8857 0.7955 -0.0008 0.0725  0.0308  184 PRO A N   
1135 C CA  . PRO A 140 ? 0.8244 0.8706 0.7866 0.0067  0.0683  0.0365  184 PRO A CA  
1136 C C   . PRO A 140 ? 0.8036 0.8548 0.7636 0.0143  0.0634  0.0301  184 PRO A C   
1137 O O   . PRO A 140 ? 0.8106 0.8658 0.7627 0.0190  0.0627  0.0344  184 PRO A O   
1138 C CB  . PRO A 140 ? 0.8283 0.8543 0.7956 0.0040  0.0663  0.0333  184 PRO A CB  
1139 C CG  . PRO A 140 ? 0.8377 0.8655 0.8150 -0.0083 0.0715  0.0344  184 PRO A CG  
1140 C CD  . PRO A 140 ? 0.8264 0.8825 0.8102 -0.0101 0.0739  0.0303  184 PRO A CD  
1141 N N   . VAL A 141 ? 0.7827 0.8359 0.7520 0.0149  0.0597  0.0220  185 VAL A N   
1142 C CA  . VAL A 141 ? 0.7659 0.8192 0.7355 0.0198  0.0564  0.0192  185 VAL A CA  
1143 C C   . VAL A 141 ? 0.7632 0.8289 0.7352 0.0192  0.0601  0.0137  185 VAL A C   
1144 O O   . VAL A 141 ? 0.7478 0.8163 0.7145 0.0200  0.0595  0.0135  185 VAL A O   
1145 C CB  . VAL A 141 ? 0.7535 0.8058 0.7335 0.0214  0.0512  0.0176  185 VAL A CB  
1146 C CG1 . VAL A 141 ? 0.7466 0.7950 0.7288 0.0247  0.0496  0.0194  185 VAL A CG1 
1147 C CG2 . VAL A 141 ? 0.7534 0.8013 0.7276 0.0194  0.0464  0.0190  185 VAL A CG2 
1148 N N   . SER A 142 ? 0.7654 0.8425 0.7467 0.0165  0.0646  0.0063  186 SER A N   
1149 C CA  . SER A 142 ? 0.7628 0.8544 0.7472 0.0143  0.0698  -0.0059 186 SER A CA  
1150 C C   . SER A 142 ? 0.7675 0.8742 0.7327 0.0107  0.0707  -0.0024 186 SER A C   
1151 O O   . SER A 142 ? 0.7635 0.8806 0.7269 0.0085  0.0703  -0.0111 186 SER A O   
1152 C CB  . SER A 142 ? 0.7632 0.8686 0.7616 0.0128  0.0769  -0.0166 186 SER A CB  
1153 O OG  . SER A 142 ? 0.7629 0.8592 0.7847 0.0193  0.0744  -0.0191 186 SER A OG  
1154 N N   . VAL A 143 ? 0.7733 0.8824 0.7265 0.0096  0.0713  0.0115  187 VAL A N   
1155 C CA  . VAL A 143 ? 0.7939 0.9206 0.7294 0.0085  0.0707  0.0217  187 VAL A CA  
1156 C C   . VAL A 143 ? 0.7948 0.9165 0.7279 0.0152  0.0633  0.0284  187 VAL A C   
1157 O O   . VAL A 143 ? 0.7928 0.9381 0.7174 0.0152  0.0600  0.0302  187 VAL A O   
1158 C CB  . VAL A 143 ? 0.8128 0.9370 0.7398 0.0059  0.0744  0.0401  187 VAL A CB  
1159 C CG1 . VAL A 143 ? 0.8326 0.9744 0.7414 0.0075  0.0719  0.0584  187 VAL A CG1 
1160 C CG2 . VAL A 143 ? 0.8174 0.9545 0.7493 -0.0028 0.0837  0.0326  187 VAL A CG2 
1161 N N   . PHE A 144 ? 0.7946 0.8918 0.7356 0.0204  0.0609  0.0308  188 PHE A N   
1162 C CA  . PHE A 144 ? 0.7956 0.8914 0.7378 0.0267  0.0567  0.0340  188 PHE A CA  
1163 C C   . PHE A 144 ? 0.7886 0.9004 0.7361 0.0222  0.0555  0.0212  188 PHE A C   
1164 O O   . PHE A 144 ? 0.7834 0.9170 0.7295 0.0228  0.0522  0.0222  188 PHE A O   
1165 C CB  . PHE A 144 ? 0.8020 0.8734 0.7491 0.0306  0.0567  0.0344  188 PHE A CB  
1166 C CG  . PHE A 144 ? 0.8062 0.8806 0.7562 0.0356  0.0554  0.0338  188 PHE A CG  
1167 C CD1 . PHE A 144 ? 0.8233 0.9050 0.7746 0.0446  0.0545  0.0419  188 PHE A CD1 
1168 C CD2 . PHE A 144 ? 0.8041 0.8766 0.7580 0.0318  0.0558  0.0271  188 PHE A CD2 
1169 C CE1 . PHE A 144 ? 0.8228 0.9139 0.7808 0.0495  0.0551  0.0394  188 PHE A CE1 
1170 C CE2 . PHE A 144 ? 0.8047 0.8849 0.7612 0.0340  0.0570  0.0270  188 PHE A CE2 
1171 C CZ  . PHE A 144 ? 0.8111 0.9027 0.7705 0.0427  0.0571  0.0312  188 PHE A CZ  
1172 N N   . TRP A 145 ? 0.7946 0.8957 0.7514 0.0174  0.0581  0.0098  189 TRP A N   
1173 C CA  . TRP A 145 ? 0.8108 0.9164 0.7779 0.0114  0.0589  -0.0022 189 TRP A CA  
1174 C C   . TRP A 145 ? 0.8361 0.9692 0.8009 0.0037  0.0598  -0.0159 189 TRP A C   
1175 O O   . TRP A 145 ? 0.8588 1.0050 0.8301 -0.0032 0.0589  -0.0256 189 TRP A O   
1176 C CB  . TRP A 145 ? 0.8104 0.8935 0.7915 0.0106  0.0617  -0.0070 189 TRP A CB  
1177 C CG  . TRP A 145 ? 0.8178 0.8833 0.7986 0.0150  0.0592  0.0054  189 TRP A CG  
1178 C CD1 . TRP A 145 ? 0.8218 0.8752 0.8028 0.0195  0.0570  0.0119  189 TRP A CD1 
1179 C CD2 . TRP A 145 ? 0.8143 0.8797 0.7932 0.0137  0.0589  0.0115  189 TRP A CD2 
1180 N NE1 . TRP A 145 ? 0.8262 0.8726 0.8017 0.0209  0.0547  0.0212  189 TRP A NE1 
1181 C CE2 . TRP A 145 ? 0.8235 0.8763 0.7974 0.0175  0.0571  0.0214  189 TRP A CE2 
1182 C CE3 . TRP A 145 ? 0.8176 0.8980 0.7994 0.0085  0.0603  0.0086  189 TRP A CE3 
1183 C CZ2 . TRP A 145 ? 0.8300 0.8842 0.7982 0.0163  0.0584  0.0285  189 TRP A CZ2 
1184 C CZ3 . TRP A 145 ? 0.8232 0.9042 0.8042 0.0076  0.0621  0.0161  189 TRP A CZ3 
1185 C CH2 . TRP A 145 ? 0.8243 0.8920 0.7970 0.0115  0.0621  0.0259  189 TRP A CH2 
1186 N N   . LYS A 146 ? 0.8594 1.0052 0.8145 0.0028  0.0621  -0.0178 190 LYS A N   
1187 C CA  . LYS A 146 ? 0.8816 1.0614 0.8284 -0.0055 0.0632  -0.0321 190 LYS A CA  
1188 C C   . LYS A 146 ? 0.8952 1.1054 0.8291 -0.0043 0.0547  -0.0201 190 LYS A C   
1189 O O   . LYS A 146 ? 0.9119 1.1540 0.8444 -0.0129 0.0518  -0.0342 190 LYS A O   
1190 C CB  . LYS A 146 ? 0.9004 1.0906 0.8377 -0.0073 0.0698  -0.0346 190 LYS A CB  
1191 C CG  . LYS A 146 ? 0.9315 1.1638 0.8541 -0.0174 0.0724  -0.0510 190 LYS A CG  
1192 C CD  . LYS A 146 ? 0.9583 1.2008 0.8789 -0.0215 0.0840  -0.0641 190 LYS A CD  
1193 C CE  . LYS A 146 ? 0.9688 1.1896 0.9177 -0.0215 0.0927  -0.0906 190 LYS A CE  
1194 N NZ  . LYS A 146 ? 0.9930 1.2336 0.9435 -0.0250 0.1058  -0.1091 190 LYS A NZ  
1195 N N   . THR A 147 ? 0.8943 1.0956 0.8223 0.0068  0.0507  0.0047  191 THR A N   
1196 C CA  . THR A 147 ? 0.9111 1.1400 0.8319 0.0132  0.0422  0.0212  191 THR A CA  
1197 C C   . THR A 147 ? 0.9216 1.1614 0.8578 0.0136  0.0375  0.0151  191 THR A C   
1198 O O   . THR A 147 ? 0.9416 1.2228 0.8772 0.0110  0.0301  0.0132  191 THR A O   
1199 C CB  . THR A 147 ? 0.9118 1.1196 0.8289 0.0265  0.0415  0.0482  191 THR A CB  
1200 O OG1 . THR A 147 ? 0.9095 1.1047 0.8164 0.0221  0.0480  0.0523  191 THR A OG1 
1201 C CG2 . THR A 147 ? 0.9318 1.1677 0.8440 0.0367  0.0326  0.0704  191 THR A CG2 
1202 N N   . VAL A 148 ? 0.9115 1.1195 0.8611 0.0158  0.0418  0.0127  192 VAL A N   
1203 C CA  . VAL A 148 ? 0.9082 1.1261 0.8732 0.0152  0.0405  0.0093  192 VAL A CA  
1204 C C   . VAL A 148 ? 0.9148 1.1493 0.8894 -0.0022 0.0418  -0.0131 192 VAL A C   
1205 O O   . VAL A 148 ? 0.9206 1.1861 0.9066 -0.0075 0.0381  -0.0182 192 VAL A O   
1206 C CB  . VAL A 148 ? 0.8975 1.0810 0.8692 0.0208  0.0461  0.0144  192 VAL A CB  
1207 C CG1 . VAL A 148 ? 0.9034 1.0699 0.8693 0.0360  0.0460  0.0305  192 VAL A CG1 
1208 C CG2 . VAL A 148 ? 0.8927 1.0450 0.8655 0.0128  0.0519  0.0058  192 VAL A CG2 
1209 N N   . SER A 149 ? 0.9080 1.1222 0.8823 -0.0111 0.0477  -0.0279 193 SER A N   
1210 C CA  . SER A 149 ? 0.9058 1.1257 0.8937 -0.0281 0.0514  -0.0525 193 SER A CA  
1211 C C   . SER A 149 ? 0.9179 1.1872 0.8982 -0.0380 0.0457  -0.0682 193 SER A C   
1212 O O   . SER A 149 ? 0.9209 1.2084 0.9145 -0.0542 0.0462  -0.0902 193 SER A O   
1213 C CB  . SER A 149 ? 0.9016 1.0849 0.8964 -0.0309 0.0599  -0.0638 193 SER A CB  
1214 O OG  . SER A 149 ? 0.8854 1.0308 0.8870 -0.0232 0.0628  -0.0482 193 SER A OG  
1215 N N   . ARG A 150 ? 0.9197 1.2118 0.8781 -0.0298 0.0405  -0.0565 194 ARG A N   
1216 C CA  . ARG A 150 ? 0.9384 1.2863 0.8828 -0.0377 0.0329  -0.0656 194 ARG A CA  
1217 C C   . ARG A 150 ? 0.9083 1.2974 0.8613 -0.0361 0.0212  -0.0568 194 ARG A C   
1218 O O   . ARG A 150 ? 0.9126 1.3441 0.8716 -0.0518 0.0163  -0.0782 194 ARG A O   
1219 C CB  . ARG A 150 ? 0.9842 1.3442 0.9015 -0.0289 0.0312  -0.0475 194 ARG A CB  
1220 C CG  . ARG A 150 ? 1.0455 1.4679 0.9409 -0.0385 0.0240  -0.0559 194 ARG A CG  
1221 C CD  . ARG A 150 ? 1.0908 1.5224 0.9577 -0.0340 0.0265  -0.0386 194 ARG A CD  
1222 N NE  . ARG A 150 ? 1.1224 1.5384 0.9846 -0.0151 0.0212  0.0034  194 ARG A NE  
1223 C CZ  . ARG A 150 ? 1.1425 1.5188 1.0008 -0.0073 0.0293  0.0215  194 ARG A CZ  
1224 N NH1 . ARG A 150 ? 1.1434 1.4969 1.0021 -0.0151 0.0421  0.0031  194 ARG A NH1 
1225 N NH2 . ARG A 150 ? 1.1596 1.5197 1.0175 0.0082  0.0248  0.0568  194 ARG A NH2 
1226 N N   A ARG A 151 ? 1.1595 1.1280 1.1239 -0.0087 0.0500  -0.0211 195 ARG A N   
1227 N N   B ARG A 151 ? 1.1609 1.1294 1.1253 -0.0087 0.0500  -0.0211 195 ARG A N   
1228 C CA  A ARG A 151 ? 1.1664 1.1240 1.1309 0.0115  0.0483  -0.0189 195 ARG A CA  
1229 C CA  B ARG A 151 ? 1.1693 1.1265 1.1337 0.0115  0.0484  -0.0190 195 ARG A CA  
1230 C C   A ARG A 151 ? 1.1349 1.1231 1.1172 0.0219  0.0500  -0.0269 195 ARG A C   
1231 C C   B ARG A 151 ? 1.1365 1.1245 1.1187 0.0219  0.0500  -0.0269 195 ARG A C   
1232 O O   A ARG A 151 ? 1.1229 1.1265 1.1144 0.0358  0.0481  -0.0242 195 ARG A O   
1233 O O   B ARG A 151 ? 1.1239 1.1273 1.1153 0.0357  0.0481  -0.0241 195 ARG A O   
1234 C CB  A ARG A 151 ? 1.2012 1.1154 1.1511 0.0162  0.0497  -0.0221 195 ARG A CB  
1235 C CB  B ARG A 151 ? 1.2060 1.1199 1.1558 0.0158  0.0498  -0.0225 195 ARG A CB  
1236 C CG  A ARG A 151 ? 1.2388 1.1132 1.1678 0.0070  0.0479  -0.0114 195 ARG A CG  
1237 C CG  B ARG A 151 ? 1.2452 1.1192 1.1739 0.0054  0.0483  -0.0125 195 ARG A CG  
1238 C CD  A ARG A 151 ? 1.2791 1.1027 1.1927 0.0137  0.0494  -0.0158 195 ARG A CD  
1239 C CD  B ARG A 151 ? 1.2627 1.1257 1.1849 0.0188  0.0428  0.0035  195 ARG A CD  
1240 N NE  A ARG A 151 ? 1.2821 1.1005 1.2029 0.0424  0.0482  -0.0169 195 ARG A NE  
1241 N NE  B ARG A 151 ? 1.3030 1.1197 1.2002 0.0084  0.0415  0.0155  195 ARG A NE  
1242 C CZ  A ARG A 151 ? 1.2828 1.0944 1.2076 0.0548  0.0531  -0.0320 195 ARG A CZ  
1243 C CZ  B ARG A 151 ? 1.3284 1.1238 1.2118 0.0182  0.0355  0.0331  195 ARG A CZ  
1244 N NH1 A ARG A 151 ? 1.2784 1.0843 1.1968 0.0397  0.0581  -0.0464 195 ARG A NH1 
1245 N NH1 B ARG A 151 ? 1.3095 1.1313 1.2047 0.0396  0.0291  0.0392  195 ARG A NH1 
1246 N NH2 A ARG A 151 ? 1.2915 1.1058 1.2269 0.0821  0.0528  -0.0334 195 ARG A NH2 
1247 N NH2 B ARG A 151 ? 1.3770 1.1251 1.2340 0.0053  0.0352  0.0455  195 ARG A NH2 
1248 N N   . PHE A 152 ? 1.1195 1.1175 1.1058 0.0140  0.0530  -0.0359 196 PHE A N   
1249 C CA  . PHE A 152 ? 1.0974 1.1195 1.0958 0.0199  0.0557  -0.0419 196 PHE A CA  
1250 C C   . PHE A 152 ? 1.0749 1.1266 1.0869 0.0183  0.0542  -0.0383 196 PHE A C   
1251 O O   . PHE A 152 ? 1.0633 1.1337 1.0857 0.0256  0.0555  -0.0398 196 PHE A O   
1252 C CB  . PHE A 152 ? 1.0920 1.1139 1.0859 0.0104  0.0574  -0.0492 196 PHE A CB  
1253 C CG  . PHE A 152 ? 1.0800 1.1197 1.0793 0.0144  0.0611  -0.0538 196 PHE A CG  
1254 C CD1 . PHE A 152 ? 1.0949 1.1343 1.0940 0.0258  0.0663  -0.0593 196 PHE A CD1 
1255 C CD2 . PHE A 152 ? 1.0639 1.1203 1.0682 0.0069  0.0599  -0.0524 196 PHE A CD2 
1256 C CE1 . PHE A 152 ? 1.0863 1.1447 1.0885 0.0260  0.0716  -0.0631 196 PHE A CE1 
1257 C CE2 . PHE A 152 ? 1.0599 1.1284 1.0649 0.0077  0.0637  -0.0542 196 PHE A CE2 
1258 C CZ  . PHE A 152 ? 1.0680 1.1390 1.0712 0.0155  0.0701  -0.0594 196 PHE A CZ  
1259 N N   . ALA A 153 ? 1.0709 1.1279 1.0830 0.0077  0.0524  -0.0354 197 ALA A N   
1260 C CA  . ALA A 153 ? 1.0488 1.1295 1.0715 0.0049  0.0519  -0.0352 197 ALA A CA  
1261 C C   . ALA A 153 ? 1.0680 1.1577 1.0910 0.0109  0.0489  -0.0301 197 ALA A C   
1262 O O   . ALA A 153 ? 1.0690 1.1802 1.1017 0.0116  0.0485  -0.0324 197 ALA A O   
1263 C CB  . ALA A 153 ? 1.0372 1.1223 1.0604 -0.0061 0.0522  -0.0361 197 ALA A CB  
1264 N N   . GLU A 154 ? 1.1032 1.1753 1.1140 0.0141  0.0461  -0.0225 198 GLU A N   
1265 C CA  . GLU A 154 ? 1.1186 1.1981 1.1267 0.0219  0.0406  -0.0145 198 GLU A CA  
1266 C C   . GLU A 154 ? 1.1257 1.2195 1.1468 0.0374  0.0390  -0.0168 198 GLU A C   
1267 O O   . GLU A 154 ? 1.1279 1.2478 1.1568 0.0413  0.0344  -0.0151 198 GLU A O   
1268 C CB  . GLU A 154 ? 1.1490 1.1982 1.1378 0.0230  0.0374  -0.0032 198 GLU A CB  
1269 C CG  . GLU A 154 ? 1.1567 1.2018 1.1325 0.0054  0.0393  0.0007  198 GLU A CG  
1270 C CD  . GLU A 154 ? 1.1997 1.2090 1.1530 0.0014  0.0377  0.0130  198 GLU A CD  
1271 O OE1 . GLU A 154 ? 1.2223 1.2003 1.1705 0.0039  0.0391  0.0118  198 GLU A OE1 
1272 O OE2 . GLU A 154 ? 1.2210 1.2319 1.1595 -0.0057 0.0355  0.0235  198 GLU A OE2 
1273 N N   . ALA A 155 ? 1.1337 1.2147 1.1575 0.0449  0.0431  -0.0222 199 ALA A N   
1274 C CA  . ALA A 155 ? 1.1435 1.2390 1.1803 0.0610  0.0437  -0.0256 199 ALA A CA  
1275 C C   . ALA A 155 ? 1.1220 1.2550 1.1764 0.0557  0.0468  -0.0325 199 ALA A C   
1276 O O   . ALA A 155 ? 1.1300 1.2892 1.1995 0.0661  0.0462  -0.0346 199 ALA A O   
1277 C CB  . ALA A 155 ? 1.1669 1.2377 1.1985 0.0681  0.0495  -0.0321 199 ALA A CB  
1278 N N   . ALA A 156 ? 1.0961 1.2314 1.1493 0.0397  0.0499  -0.0360 200 ALA A N   
1279 C CA  . ALA A 156 ? 1.0620 1.2213 1.1273 0.0316  0.0540  -0.0420 200 ALA A CA  
1280 C C   . ALA A 156 ? 1.0470 1.2367 1.1234 0.0297  0.0493  -0.0418 200 ALA A C   
1281 O O   . ALA A 156 ? 1.0525 1.2430 1.1230 0.0304  0.0426  -0.0368 200 ALA A O   
1282 C CB  . ALA A 156 ? 1.0486 1.1956 1.1082 0.0182  0.0567  -0.0439 200 ALA A CB  
1283 N N   . CYS A 157 ? 1.0323 1.2480 1.1228 0.0246  0.0531  -0.0476 201 CYS A N   
1284 C CA  . CYS A 157 ? 1.0219 1.2714 1.1246 0.0193  0.0487  -0.0500 201 CYS A CA  
1285 C C   . CYS A 157 ? 1.0028 1.2664 1.1144 0.0029  0.0556  -0.0573 201 CYS A C   
1286 O O   . CYS A 157 ? 0.9829 1.2317 1.0909 -0.0014 0.0635  -0.0583 201 CYS A O   
1287 C CB  . CYS A 157 ? 1.0337 1.3122 1.1502 0.0358  0.0433  -0.0478 201 CYS A CB  
1288 S SG  . CYS A 157 ? 1.0438 1.3501 1.1806 0.0408  0.0532  -0.0553 201 CYS A SG  
1289 N N   . ASP A 158 ? 1.0014 1.2930 1.1224 -0.0076 0.0521  -0.0620 202 ASP A N   
1290 C CA  . ASP A 158 ? 1.0003 1.3051 1.1295 -0.0269 0.0582  -0.0693 202 ASP A CA  
1291 C C   . ASP A 158 ? 0.9998 1.2645 1.1146 -0.0383 0.0637  -0.0697 202 ASP A C   
1292 O O   . ASP A 158 ? 0.9970 1.2431 1.1022 -0.0403 0.0603  -0.0711 202 ASP A O   
1293 C CB  . ASP A 158 ? 1.0012 1.3343 1.1462 -0.0256 0.0652  -0.0710 202 ASP A CB  
1294 C CG  . ASP A 158 ? 0.9915 1.3705 1.1565 -0.0114 0.0589  -0.0718 202 ASP A CG  
1295 O OD1 . ASP A 158 ? 0.9940 1.3791 1.1571 -0.0020 0.0474  -0.0683 202 ASP A OD1 
1296 O OD2 . ASP A 158 ? 0.9907 1.4009 1.1728 -0.0093 0.0655  -0.0755 202 ASP A OD2 
1297 N N   . VAL A 159 ? 1.0101 1.2630 1.1229 -0.0447 0.0722  -0.0683 203 VAL A N   
1298 C CA  . VAL A 159 ? 1.0252 1.2407 1.1250 -0.0538 0.0758  -0.0664 203 VAL A CA  
1299 C C   . VAL A 159 ? 1.0219 1.2134 1.1101 -0.0413 0.0765  -0.0592 203 VAL A C   
1300 O O   . VAL A 159 ? 1.0256 1.2202 1.1112 -0.0398 0.0818  -0.0562 203 VAL A O   
1301 C CB  . VAL A 159 ? 1.0459 1.2615 1.1468 -0.0735 0.0837  -0.0676 203 VAL A CB  
1302 C CG1 . VAL A 159 ? 1.0615 1.2327 1.1467 -0.0794 0.0861  -0.0622 203 VAL A CG1 
1303 C CG2 . VAL A 159 ? 1.0513 1.2911 1.1636 -0.0901 0.0828  -0.0769 203 VAL A CG2 
1304 N N   . VAL A 160 ? 1.0111 1.1821 1.0922 -0.0338 0.0714  -0.0578 204 VAL A N   
1305 C CA  . VAL A 160 ? 1.0071 1.1568 1.0777 -0.0253 0.0706  -0.0523 204 VAL A CA  
1306 C C   . VAL A 160 ? 1.0182 1.1428 1.0814 -0.0319 0.0719  -0.0490 204 VAL A C   
1307 O O   . VAL A 160 ? 1.0314 1.1470 1.0972 -0.0392 0.0720  -0.0522 204 VAL A O   
1308 C CB  . VAL A 160 ? 0.9970 1.1416 1.0653 -0.0163 0.0651  -0.0522 204 VAL A CB  
1309 C CG1 . VAL A 160 ? 1.0010 1.1286 1.0600 -0.0103 0.0639  -0.0480 204 VAL A CG1 
1310 C CG2 . VAL A 160 ? 0.9885 1.1526 1.0614 -0.0097 0.0621  -0.0528 204 VAL A CG2 
1311 N N   . HIS A 161 ? 1.0220 1.1341 1.0745 -0.0288 0.0721  -0.0426 205 HIS A N   
1312 C CA  . HIS A 161 ? 1.0427 1.1306 1.0861 -0.0320 0.0708  -0.0360 205 HIS A CA  
1313 C C   . HIS A 161 ? 1.0297 1.1079 1.0699 -0.0217 0.0639  -0.0335 205 HIS A C   
1314 O O   . HIS A 161 ? 1.0190 1.1066 1.0588 -0.0159 0.0622  -0.0356 205 HIS A O   
1315 C CB  . HIS A 161 ? 1.0749 1.1604 1.1058 -0.0402 0.0762  -0.0291 205 HIS A CB  
1316 C CG  . HIS A 161 ? 1.0978 1.1974 1.1339 -0.0537 0.0841  -0.0319 205 HIS A CG  
1317 N ND1 . HIS A 161 ? 1.1309 1.2130 1.1609 -0.0683 0.0877  -0.0270 205 HIS A ND1 
1318 C CD2 . HIS A 161 ? 1.0912 1.2220 1.1395 -0.0554 0.0888  -0.0390 205 HIS A CD2 
1319 C CE1 . HIS A 161 ? 1.1327 1.2378 1.1712 -0.0816 0.0951  -0.0321 205 HIS A CE1 
1320 N NE2 . HIS A 161 ? 1.1126 1.2508 1.1640 -0.0726 0.0954  -0.0396 205 HIS A NE2 
1321 N N   . VAL A 162 ? 1.0331 1.0923 1.0720 -0.0195 0.0597  -0.0291 206 VAL A N   
1322 C CA  . VAL A 162 ? 1.0306 1.0868 1.0695 -0.0099 0.0522  -0.0262 206 VAL A CA  
1323 C C   . VAL A 162 ? 1.0559 1.0911 1.0853 -0.0080 0.0473  -0.0151 206 VAL A C   
1324 O O   . VAL A 162 ? 1.0725 1.0875 1.1023 -0.0102 0.0487  -0.0127 206 VAL A O   
1325 C CB  . VAL A 162 ? 1.0168 1.0799 1.0712 -0.0035 0.0504  -0.0347 206 VAL A CB  
1326 C CG1 . VAL A 162 ? 1.0296 1.0786 1.0916 -0.0034 0.0526  -0.0392 206 VAL A CG1 
1327 C CG2 . VAL A 162 ? 1.0148 1.0846 1.0735 0.0047  0.0433  -0.0331 206 VAL A CG2 
1328 N N   . MET A 163 ? 1.0716 1.1098 1.0905 -0.0046 0.0409  -0.0081 207 MET A N   
1329 C CA  . MET A 163 ? 1.1153 1.1359 1.1210 -0.0019 0.0336  0.0055  207 MET A CA  
1330 C C   . MET A 163 ? 1.1229 1.1490 1.1411 0.0123  0.0222  0.0065  207 MET A C   
1331 O O   . MET A 163 ? 1.1138 1.1612 1.1342 0.0142  0.0172  0.0031  207 MET A O   
1332 C CB  . MET A 163 ? 1.1350 1.1605 1.1170 -0.0095 0.0338  0.0124  207 MET A CB  
1333 C CG  . MET A 163 ? 1.1758 1.1865 1.1388 -0.0071 0.0239  0.0290  207 MET A CG  
1334 S SD  . MET A 163 ? 1.2029 1.2173 1.1306 -0.0209 0.0279  0.0369  207 MET A SD  
1335 C CE  . MET A 163 ? 1.1895 1.2046 1.1187 -0.0354 0.0465  0.0301  207 MET A CE  
1336 N N   . LEU A 164 ? 1.1551 1.1623 1.1825 0.0220  0.0186  0.0100  208 LEU A N   
1337 C CA  . LEU A 164 ? 1.1626 1.1794 1.2086 0.0389  0.0089  0.0089  208 LEU A CA  
1338 C C   . LEU A 164 ? 1.1954 1.1970 1.2299 0.0489  -0.0042 0.0267  208 LEU A C   
1339 O O   . LEU A 164 ? 1.2171 1.1941 1.2271 0.0412  -0.0041 0.0404  208 LEU A O   
1340 C CB  . LEU A 164 ? 1.1676 1.1742 1.2337 0.0465  0.0146  -0.0022 208 LEU A CB  
1341 C CG  . LEU A 164 ? 1.1375 1.1613 1.2133 0.0374  0.0258  -0.0188 208 LEU A CG  
1342 C CD1 . LEU A 164 ? 1.1469 1.1602 1.2382 0.0440  0.0313  -0.0310 208 LEU A CD1 
1343 C CD2 . LEU A 164 ? 1.1126 1.1721 1.1974 0.0368  0.0242  -0.0252 208 LEU A CD2 
1344 N N   . ASP A 165 ? 1.2026 1.2221 1.2554 0.0658  -0.0157 0.0270  209 ASP A N   
1345 C CA  . ASP A 165 ? 1.2517 1.2624 1.2974 0.0798  -0.0317 0.0448  209 ASP A CA  
1346 C C   . ASP A 165 ? 1.2951 1.2855 1.3620 0.1021  -0.0354 0.0450  209 ASP A C   
1347 O O   . ASP A 165 ? 1.2832 1.2992 1.3811 0.1146  -0.0346 0.0306  209 ASP A O   
1348 C CB  . ASP A 165 ? 1.2389 1.2922 1.2901 0.0829  -0.0447 0.0453  209 ASP A CB  
1349 C CG  . ASP A 165 ? 1.2763 1.3255 1.3096 0.0917  -0.0631 0.0665  209 ASP A CG  
1350 O OD1 . ASP A 165 ? 1.3180 1.3270 1.3354 0.0983  -0.0664 0.0831  209 ASP A OD1 
1351 O OD2 . ASP A 165 ? 1.2719 1.3573 1.3052 0.0905  -0.0746 0.0667  209 ASP A OD2 
1352 N N   . GLY A 166 ? 1.3581 1.3014 1.4072 0.1065  -0.0385 0.0611  210 GLY A N   
1353 C CA  . GLY A 166 ? 1.4073 1.3186 1.4723 0.1285  -0.0413 0.0617  210 GLY A CA  
1354 C C   . GLY A 166 ? 1.4387 1.3709 1.5246 0.1576  -0.0598 0.0691  210 GLY A C   
1355 O O   . GLY A 166 ? 1.4452 1.3782 1.5612 0.1801  -0.0599 0.0582  210 GLY A O   
1356 N N   . SER A 167 ? 1.4634 1.4161 1.5338 0.1573  -0.0753 0.0862  211 SER A N   
1357 C CA  . SER A 167 ? 1.5061 1.4790 1.5922 0.1846  -0.0967 0.0980  211 SER A CA  
1358 C C   . SER A 167 ? 1.4814 1.5196 1.6095 0.1944  -0.0985 0.0776  211 SER A C   
1359 O O   . SER A 167 ? 1.4966 1.5500 1.6575 0.2230  -0.1072 0.0749  211 SER A O   
1360 C CB  . SER A 167 ? 1.5314 1.5073 1.5833 0.1779  -0.1132 0.1224  211 SER A CB  
1361 O OG  . SER A 167 ? 1.4980 1.5148 1.5391 0.1532  -0.1090 0.1132  211 SER A OG  
1362 N N   . ARG A 168 ? 1.4648 1.5410 1.5921 0.1706  -0.0897 0.0635  212 ARG A N   
1363 C CA  . ARG A 168 ? 1.4542 1.5934 1.6151 0.1727  -0.0915 0.0467  212 ARG A CA  
1364 C C   . ARG A 168 ? 1.4372 1.5853 1.6351 0.1860  -0.0786 0.0260  212 ARG A C   
1365 O O   . ARG A 168 ? 1.4057 1.5557 1.6050 0.1690  -0.0606 0.0091  212 ARG A O   
1366 C CB  . ARG A 168 ? 1.4329 1.5970 1.5788 0.1420  -0.0832 0.0371  212 ARG A CB  
1367 C CG  . ARG A 168 ? 1.4638 1.6393 1.5808 0.1303  -0.0975 0.0512  212 ARG A CG  
1368 C CD  . ARG A 168 ? 1.4413 1.6364 1.5448 0.1019  -0.0882 0.0385  212 ARG A CD  
1369 N NE  . ARG A 168 ? 1.4227 1.6682 1.5574 0.0982  -0.0876 0.0215  212 ARG A NE  
1370 C CZ  . ARG A 168 ? 1.4275 1.7107 1.5598 0.0839  -0.0959 0.0169  212 ARG A CZ  
1371 N NH1 . ARG A 168 ? 1.4493 1.7274 1.5487 0.0738  -0.1063 0.0271  212 ARG A NH1 
1372 N NH2 . ARG A 168 ? 1.4074 1.7340 1.5688 0.0776  -0.0930 0.0012  212 ARG A NH2 
1373 N N   . SER A 169 ? 1.4574 1.6118 1.6844 0.2178  -0.0884 0.0274  213 SER A N   
1374 C CA  . SER A 169 ? 1.4432 1.6179 1.7099 0.2344  -0.0774 0.0054  213 SER A CA  
1375 C C   . SER A 169 ? 1.4222 1.5609 1.6777 0.2186  -0.0544 -0.0100 213 SER A C   
1376 O O   . SER A 169 ? 1.4467 1.5257 1.6756 0.2150  -0.0507 -0.0014 213 SER A O   
1377 C CB  . SER A 169 ? 1.4072 1.6592 1.7070 0.2311  -0.0786 -0.0090 213 SER A CB  
1378 O OG  . SER A 169 ? 1.4010 1.6788 1.7397 0.2469  -0.0664 -0.0311 213 SER A OG  
1379 N N   . LYS A 170 ? 1.3720 1.5492 1.6469 0.2078  -0.0394 -0.0325 214 LYS A N   
1380 C CA  . LYS A 170 ? 1.3409 1.4944 1.6033 0.1897  -0.0193 -0.0472 214 LYS A CA  
1381 C C   . LYS A 170 ? 1.3122 1.4431 1.5364 0.1604  -0.0170 -0.0364 214 LYS A C   
1382 O O   . LYS A 170 ? 1.2888 1.4490 1.5056 0.1452  -0.0216 -0.0318 214 LYS A O   
1383 C CB  . LYS A 170 ? 1.3067 1.5116 1.5953 0.1841  -0.0057 -0.0704 214 LYS A CB  
1384 C CG  . LYS A 170 ? 1.2664 1.5228 1.5571 0.1636  -0.0077 -0.0704 214 LYS A CG  
1385 C CD  . LYS A 170 ? 1.2439 1.5576 1.5665 0.1625  0.0029  -0.0904 214 LYS A CD  
1386 C CE  . LYS A 170 ? 1.2358 1.5390 1.5532 0.1522  0.0235  -0.1081 214 LYS A CE  
1387 N NZ  . LYS A 170 ? 1.2189 1.5806 1.5630 0.1475  0.0351  -0.1262 214 LYS A NZ  
1388 N N   . ILE A 171 ? 1.3090 1.3885 1.5101 0.1526  -0.0093 -0.0342 215 ILE A N   
1389 C CA  . ILE A 171 ? 1.2881 1.3444 1.4552 0.1291  -0.0077 -0.0227 215 ILE A CA  
1390 C C   . ILE A 171 ? 1.2328 1.3177 1.3968 0.1070  0.0033  -0.0347 215 ILE A C   
1391 O O   . ILE A 171 ? 1.2189 1.3211 1.3707 0.0938  -0.0004 -0.0283 215 ILE A O   
1392 C CB  . ILE A 171 ? 1.3247 1.3233 1.4721 0.1256  -0.0019 -0.0182 215 ILE A CB  
1393 C CG1 . ILE A 171 ? 1.3787 1.3399 1.5254 0.1479  -0.0137 -0.0034 215 ILE A CG1 
1394 C CG2 . ILE A 171 ? 1.3146 1.2989 1.4312 0.1003  0.0020  -0.0090 215 ILE A CG2 
1395 C CD1 . ILE A 171 ? 1.4205 1.3194 1.5482 0.1429  -0.0072 0.0000  215 ILE A CD1 
1396 N N   . PHE A 172 ? 1.2087 1.2958 1.3817 0.1034  0.0166  -0.0520 216 PHE A N   
1397 C CA  . PHE A 172 ? 1.1634 1.2784 1.3350 0.0857  0.0261  -0.0624 216 PHE A CA  
1398 C C   . PHE A 172 ? 1.1451 1.3076 1.3426 0.0917  0.0263  -0.0723 216 PHE A C   
1399 O O   . PHE A 172 ? 1.1730 1.3469 1.3947 0.1104  0.0262  -0.0806 216 PHE A O   
1400 C CB  . PHE A 172 ? 1.1576 1.2559 1.3227 0.0768  0.0392  -0.0750 216 PHE A CB  
1401 C CG  . PHE A 172 ? 1.1245 1.2506 1.2871 0.0611  0.0479  -0.0843 216 PHE A CG  
1402 C CD1 . PHE A 172 ? 1.0996 1.2295 1.2451 0.0454  0.0468  -0.0759 216 PHE A CD1 
1403 C CD2 . PHE A 172 ? 1.1260 1.2732 1.3019 0.0627  0.0575  -0.1011 216 PHE A CD2 
1404 C CE1 . PHE A 172 ? 1.0821 1.2315 1.2230 0.0326  0.0535  -0.0816 216 PHE A CE1 
1405 C CE2 . PHE A 172 ? 1.1063 1.2764 1.2752 0.0470  0.0649  -0.1065 216 PHE A CE2 
1406 C CZ  . PHE A 172 ? 1.0847 1.2536 1.2358 0.0325  0.0620  -0.0954 216 PHE A CZ  
1407 N N   . ASP A 173 ? 1.1039 1.2935 1.2967 0.0753  0.0271  -0.0718 217 ASP A N   
1408 C CA  . ASP A 173 ? 1.0746 1.3117 1.2894 0.0740  0.0284  -0.0804 217 ASP A CA  
1409 C C   . ASP A 173 ? 1.0533 1.3007 1.2564 0.0522  0.0399  -0.0867 217 ASP A C   
1410 O O   . ASP A 173 ? 1.0461 1.2800 1.2272 0.0371  0.0385  -0.0787 217 ASP A O   
1411 C CB  . ASP A 173 ? 1.0676 1.3271 1.2876 0.0749  0.0141  -0.0706 217 ASP A CB  
1412 C CG  . ASP A 173 ? 1.0518 1.3666 1.3004 0.0741  0.0138  -0.0798 217 ASP A CG  
1413 O OD1 . ASP A 173 ? 1.0399 1.3766 1.3040 0.0728  0.0265  -0.0938 217 ASP A OD1 
1414 O OD2 . ASP A 173 ? 1.0472 1.3859 1.3017 0.0731  0.0012  -0.0736 217 ASP A OD2 
1415 N N   . LYS A 174 ? 1.0549 1.3254 1.2717 0.0516  0.0513  -0.1010 218 LYS A N   
1416 C CA  . LYS A 174 ? 1.0495 1.3286 1.2526 0.0314  0.0622  -0.1053 218 LYS A CA  
1417 C C   . LYS A 174 ? 1.0396 1.3447 1.2426 0.0149  0.0599  -0.1008 218 LYS A C   
1418 O O   . LYS A 174 ? 1.0368 1.3327 1.2187 -0.0033 0.0641  -0.0965 218 LYS A O   
1419 C CB  . LYS A 174 ? 1.0640 1.3634 1.2789 0.0341  0.0757  -0.1223 218 LYS A CB  
1420 C CG  . LYS A 174 ? 1.0805 1.4221 1.3305 0.0482  0.0780  -0.1342 218 LYS A CG  
1421 C CD  . LYS A 174 ? 1.0921 1.4639 1.3510 0.0447  0.0947  -0.1526 218 LYS A CD  
1422 C CE  . LYS A 174 ? 1.0905 1.4888 1.3371 0.0177  0.1029  -0.1509 218 LYS A CE  
1423 N NZ  . LYS A 174 ? 1.1028 1.5391 1.3595 0.0137  0.1201  -0.1690 218 LYS A NZ  
1424 N N   . ASP A 175 ? 1.0414 1.3777 1.2675 0.0213  0.0525  -0.1015 219 ASP A N   
1425 C CA  . ASP A 175 ? 1.0366 1.4022 1.2659 0.0032  0.0503  -0.1000 219 ASP A CA  
1426 C C   . ASP A 175 ? 1.0298 1.3681 1.2360 -0.0058 0.0394  -0.0877 219 ASP A C   
1427 O O   . ASP A 175 ? 1.0385 1.3899 1.2402 -0.0242 0.0374  -0.0866 219 ASP A O   
1428 C CB  . ASP A 175 ? 1.0433 1.4616 1.3098 0.0129  0.0460  -0.1075 219 ASP A CB  
1429 C CG  . ASP A 175 ? 1.0478 1.5025 1.3399 0.0197  0.0597  -0.1233 219 ASP A CG  
1430 O OD1 . ASP A 175 ? 1.0407 1.4788 1.3175 0.0138  0.0728  -0.1284 219 ASP A OD1 
1431 O OD2 . ASP A 175 ? 1.0570 1.5596 1.3844 0.0313  0.0571  -0.1312 219 ASP A OD2 
1432 N N   . SER A 176 ? 1.0204 1.3209 1.2110 0.0054  0.0334  -0.0796 220 SER A N   
1433 C CA  . SER A 176 ? 1.0132 1.2878 1.1799 -0.0019 0.0255  -0.0699 220 SER A CA  
1434 C C   . SER A 176 ? 1.0040 1.2520 1.1453 -0.0179 0.0336  -0.0682 220 SER A C   
1435 O O   . SER A 176 ? 1.0022 1.2480 1.1417 -0.0212 0.0436  -0.0717 220 SER A O   
1436 C CB  . SER A 176 ? 1.0211 1.2692 1.1803 0.0140  0.0180  -0.0618 220 SER A CB  
1437 O OG  . SER A 176 ? 1.0146 1.2320 1.1615 0.0167  0.0260  -0.0613 220 SER A OG  
1438 N N   . THR A 177 ? 0.9974 1.2255 1.1182 -0.0266 0.0288  -0.0630 221 THR A N   
1439 C CA  . THR A 177 ? 0.9828 1.1825 1.0803 -0.0378 0.0348  -0.0608 221 THR A CA  
1440 C C   . THR A 177 ? 0.9757 1.1525 1.0649 -0.0281 0.0398  -0.0578 221 THR A C   
1441 O O   . THR A 177 ? 0.9829 1.1471 1.0611 -0.0335 0.0460  -0.0568 221 THR A O   
1442 C CB  . THR A 177 ? 0.9800 1.1613 1.0582 -0.0452 0.0292  -0.0587 221 THR A CB  
1443 O OG1 . THR A 177 ? 0.9895 1.1968 1.0771 -0.0525 0.0212  -0.0620 221 THR A OG1 
1444 C CG2 . THR A 177 ? 0.9870 1.1415 1.0451 -0.0573 0.0352  -0.0583 221 THR A CG2 
1445 N N   . PHE A 178 ? 0.9629 1.1343 1.0563 -0.0148 0.0361  -0.0555 222 PHE A N   
1446 C CA  . PHE A 178 ? 0.9497 1.1031 1.0376 -0.0084 0.0406  -0.0541 222 PHE A CA  
1447 C C   . PHE A 178 ? 0.9411 1.1060 1.0397 -0.0075 0.0477  -0.0607 222 PHE A C   
1448 O O   . PHE A 178 ? 0.9362 1.0936 1.0255 -0.0115 0.0528  -0.0610 222 PHE A O   
1449 C CB  . PHE A 178 ? 0.9538 1.0964 1.0425 0.0020  0.0358  -0.0497 222 PHE A CB  
1450 C CG  . PHE A 178 ? 0.9509 1.0783 1.0379 0.0058  0.0409  -0.0502 222 PHE A CG  
1451 C CD1 . PHE A 178 ? 0.9479 1.0642 1.0223 0.0005  0.0452  -0.0489 222 PHE A CD1 
1452 C CD2 . PHE A 178 ? 0.9538 1.0788 1.0530 0.0146  0.0413  -0.0533 222 PHE A CD2 
1453 C CE1 . PHE A 178 ? 0.9443 1.0524 1.0188 0.0009  0.0492  -0.0506 222 PHE A CE1 
1454 C CE2 . PHE A 178 ? 0.9565 1.0657 1.0526 0.0143  0.0462  -0.0557 222 PHE A CE2 
1455 C CZ  . PHE A 178 ? 0.9489 1.0521 1.0329 0.0060  0.0499  -0.0543 222 PHE A CZ  
1456 N N   . GLY A 179 ? 0.9380 1.1238 1.0562 -0.0013 0.0475  -0.0665 223 GLY A N   
1457 C CA  . GLY A 179 ? 0.9382 1.1369 1.0671 0.0011  0.0555  -0.0761 223 GLY A CA  
1458 C C   . GLY A 179 ? 0.9380 1.1504 1.0598 -0.0131 0.0630  -0.0788 223 GLY A C   
1459 O O   . GLY A 179 ? 0.9518 1.1656 1.0688 -0.0152 0.0701  -0.0840 223 GLY A O   
1460 N N   . SER A 180 ? 0.9399 1.1610 1.0584 -0.0246 0.0614  -0.0749 224 SER A N   
1461 C CA  . SER A 180 ? 0.9560 1.1879 1.0662 -0.0407 0.0687  -0.0752 224 SER A CA  
1462 C C   . SER A 180 ? 0.9734 1.1751 1.0569 -0.0480 0.0683  -0.0656 224 SER A C   
1463 O O   . SER A 180 ? 0.9834 1.1839 1.0549 -0.0532 0.0737  -0.0643 224 SER A O   
1464 C CB  . SER A 180 ? 0.9590 1.2144 1.0794 -0.0523 0.0678  -0.0765 224 SER A CB  
1465 O OG  . SER A 180 ? 0.9648 1.2036 1.0778 -0.0545 0.0586  -0.0706 224 SER A OG  
1466 N N   . VAL A 181 ? 0.9790 1.1577 1.0528 -0.0471 0.0617  -0.0592 225 VAL A N   
1467 C CA  . VAL A 181 ? 0.9828 1.1330 1.0342 -0.0516 0.0610  -0.0509 225 VAL A CA  
1468 C C   . VAL A 181 ? 0.9780 1.1139 1.0248 -0.0389 0.0590  -0.0487 225 VAL A C   
1469 O O   . VAL A 181 ? 0.9807 1.1127 1.0181 -0.0387 0.0608  -0.0454 225 VAL A O   
1470 C CB  . VAL A 181 ? 0.9866 1.1199 1.0296 -0.0584 0.0568  -0.0487 225 VAL A CB  
1471 C CG1 . VAL A 181 ? 1.0072 1.1067 1.0276 -0.0608 0.0569  -0.0412 225 VAL A CG1 
1472 C CG2 . VAL A 181 ? 0.9907 1.1445 1.0418 -0.0737 0.0578  -0.0526 225 VAL A CG2 
1473 N N   . GLU A 182 ? 0.9754 1.1066 1.0282 -0.0299 0.0551  -0.0500 226 GLU A N   
1474 C CA  . GLU A 182 ? 0.9851 1.1037 1.0330 -0.0214 0.0540  -0.0477 226 GLU A CA  
1475 C C   . GLU A 182 ? 0.9962 1.1243 1.0486 -0.0187 0.0566  -0.0505 226 GLU A C   
1476 O O   . GLU A 182 ? 0.9929 1.1171 1.0382 -0.0169 0.0564  -0.0475 226 GLU A O   
1477 C CB  . GLU A 182 ? 0.9822 1.0970 1.0340 -0.0157 0.0507  -0.0482 226 GLU A CB  
1478 C CG  . GLU A 182 ? 0.9940 1.0994 1.0368 -0.0193 0.0475  -0.0471 226 GLU A CG  
1479 C CD  . GLU A 182 ? 0.9917 1.0961 1.0338 -0.0153 0.0435  -0.0464 226 GLU A CD  
1480 O OE1 . GLU A 182 ? 0.9959 1.0947 1.0356 -0.0102 0.0452  -0.0445 226 GLU A OE1 
1481 O OE2 . GLU A 182 ? 0.9884 1.0994 1.0311 -0.0190 0.0385  -0.0473 226 GLU A OE2 
1482 N N   . VAL A 183 ? 1.0214 1.1628 1.0861 -0.0178 0.0588  -0.0573 227 VAL A N   
1483 C CA  . VAL A 183 ? 1.0404 1.1879 1.1086 -0.0163 0.0619  -0.0636 227 VAL A CA  
1484 C C   . VAL A 183 ? 1.0682 1.2247 1.1254 -0.0231 0.0645  -0.0633 227 VAL A C   
1485 O O   . VAL A 183 ? 1.0654 1.2246 1.1179 -0.0235 0.0642  -0.0651 227 VAL A O   
1486 C CB  . VAL A 183 ? 1.0368 1.1925 1.1205 -0.0115 0.0644  -0.0729 227 VAL A CB  
1487 C CG1 . VAL A 183 ? 1.0422 1.2029 1.1272 -0.0123 0.0694  -0.0834 227 VAL A CG1 
1488 C CG2 . VAL A 183 ? 1.0395 1.1822 1.1303 -0.0034 0.0598  -0.0700 227 VAL A CG2 
1489 N N   . HIS A 184 ? 1.1044 1.2668 1.1560 -0.0303 0.0667  -0.0604 228 HIS A N   
1490 C CA  . HIS A 184 ? 1.1400 1.3111 1.1775 -0.0389 0.0698  -0.0583 228 HIS A CA  
1491 C C   . HIS A 184 ? 1.1403 1.2955 1.1601 -0.0385 0.0642  -0.0456 228 HIS A C   
1492 O O   . HIS A 184 ? 1.1410 1.3011 1.1456 -0.0434 0.0640  -0.0408 228 HIS A O   
1493 C CB  . HIS A 184 ? 1.1743 1.3589 1.2122 -0.0494 0.0758  -0.0596 228 HIS A CB  
1494 C CG  . HIS A 184 ? 1.2024 1.4105 1.2599 -0.0471 0.0821  -0.0739 228 HIS A CG  
1495 N ND1 . HIS A 184 ? 1.2436 1.4762 1.3003 -0.0551 0.0913  -0.0820 228 HIS A ND1 
1496 C CD2 . HIS A 184 ? 1.2088 1.4194 1.2869 -0.0360 0.0806  -0.0814 228 HIS A CD2 
1497 C CE1 . HIS A 184 ? 1.2370 1.4873 1.3165 -0.0470 0.0957  -0.0959 228 HIS A CE1 
1498 N NE2 . HIS A 184 ? 1.2226 1.4579 1.3151 -0.0347 0.0883  -0.0945 228 HIS A NE2 
1499 N N   . ASN A 185 ? 1.1409 1.2780 1.1621 -0.0314 0.0596  -0.0403 229 ASN A N   
1500 C CA  . ASN A 185 ? 1.1522 1.2728 1.1603 -0.0266 0.0545  -0.0296 229 ASN A CA  
1501 C C   . ASN A 185 ? 1.1381 1.2643 1.1535 -0.0160 0.0507  -0.0311 229 ASN A C   
1502 O O   . ASN A 185 ? 1.1519 1.2701 1.1620 -0.0079 0.0462  -0.0238 229 ASN A O   
1503 C CB  . ASN A 185 ? 1.1639 1.2601 1.1666 -0.0268 0.0537  -0.0249 229 ASN A CB  
1504 C CG  . ASN A 185 ? 1.1814 1.2722 1.1746 -0.0412 0.0572  -0.0219 229 ASN A CG  
1505 O OD1 . ASN A 185 ? 1.2039 1.2915 1.1816 -0.0483 0.0578  -0.0138 229 ASN A OD1 
1506 N ND2 . ASN A 185 ? 1.1791 1.2710 1.1807 -0.0473 0.0590  -0.0276 229 ASN A ND2 
1507 N N   . LEU A 186 ? 1.1169 1.2569 1.1453 -0.0163 0.0528  -0.0408 230 LEU A N   
1508 C CA  . LEU A 186 ? 1.1088 1.2585 1.1447 -0.0115 0.0505  -0.0434 230 LEU A CA  
1509 C C   . LEU A 186 ? 1.1234 1.2905 1.1524 -0.0135 0.0465  -0.0420 230 LEU A C   
1510 O O   . LEU A 186 ? 1.1206 1.3004 1.1485 -0.0212 0.0486  -0.0500 230 LEU A O   
1511 C CB  . LEU A 186 ? 1.0959 1.2482 1.1438 -0.0144 0.0543  -0.0532 230 LEU A CB  
1512 C CG  . LEU A 186 ? 1.0905 1.2287 1.1438 -0.0111 0.0558  -0.0524 230 LEU A CG  
1513 C CD1 . LEU A 186 ? 1.0880 1.2234 1.1499 -0.0132 0.0584  -0.0593 230 LEU A CD1 
1514 C CD2 . LEU A 186 ? 1.0862 1.2224 1.1401 -0.0060 0.0548  -0.0486 230 LEU A CD2 
1515 N N   . GLN A 187 ? 1.1519 1.3198 1.1759 -0.0054 0.0402  -0.0324 231 GLN A N   
1516 C CA  . GLN A 187 ? 1.1728 1.3589 1.1879 -0.0055 0.0332  -0.0276 231 GLN A CA  
1517 C C   . GLN A 187 ? 1.1470 1.3604 1.1747 -0.0089 0.0314  -0.0377 231 GLN A C   
1518 O O   . GLN A 187 ? 1.1332 1.3534 1.1761 -0.0036 0.0312  -0.0400 231 GLN A O   
1519 C CB  . GLN A 187 ? 1.2121 1.3895 1.2205 0.0080  0.0254  -0.0132 231 GLN A CB  
1520 C CG  . GLN A 187 ? 1.2463 1.3899 1.2393 0.0085  0.0272  -0.0034 231 GLN A CG  
1521 C CD  . GLN A 187 ? 1.2983 1.4257 1.2821 0.0235  0.0190  0.0111  231 GLN A CD  
1522 O OE1 . GLN A 187 ? 1.3183 1.4227 1.3058 0.0341  0.0203  0.0124  231 GLN A OE1 
1523 N NE2 . GLN A 187 ? 1.3340 1.4727 1.3046 0.0254  0.0101  0.0220  231 GLN A NE2 
1524 N N   . PRO A 188 ? 1.1370 1.3680 1.1578 -0.0199 0.0308  -0.0451 232 PRO A N   
1525 C CA  . PRO A 188 ? 1.1314 1.3856 1.1627 -0.0276 0.0297  -0.0574 232 PRO A CA  
1526 C C   . PRO A 188 ? 1.1395 1.4236 1.1769 -0.0223 0.0189  -0.0523 232 PRO A C   
1527 O O   . PRO A 188 ? 1.1325 1.4387 1.1827 -0.0300 0.0180  -0.0624 232 PRO A O   
1528 C CB  . PRO A 188 ? 1.1347 1.3961 1.1524 -0.0408 0.0326  -0.0683 232 PRO A CB  
1529 C CG  . PRO A 188 ? 1.1473 1.4032 1.1441 -0.0389 0.0309  -0.0562 232 PRO A CG  
1530 C CD  . PRO A 188 ? 1.1415 1.3714 1.1426 -0.0280 0.0325  -0.0439 232 PRO A CD  
1531 N N   . GLU A 189 ? 1.1619 1.4466 1.1908 -0.0094 0.0103  -0.0366 233 GLU A N   
1532 C CA  . GLU A 189 ? 1.1759 1.4904 1.2145 0.0015  -0.0013 -0.0298 233 GLU A CA  
1533 C C   . GLU A 189 ? 1.1680 1.4902 1.2329 0.0085  0.0028  -0.0349 233 GLU A C   
1534 O O   . GLU A 189 ? 1.1596 1.5189 1.2419 0.0062  -0.0013 -0.0410 233 GLU A O   
1535 C CB  . GLU A 189 ? 1.1993 1.5013 1.2232 0.0182  -0.0107 -0.0100 233 GLU A CB  
1536 C CG  . GLU A 189 ? 1.2262 1.5306 1.2212 0.0106  -0.0176 -0.0015 233 GLU A CG  
1537 C CD  . GLU A 189 ? 1.2308 1.5025 1.2046 -0.0006 -0.0073 -0.0004 233 GLU A CD  
1538 O OE1 . GLU A 189 ? 1.2086 1.4749 1.1890 -0.0126 0.0044  -0.0159 233 GLU A OE1 
1539 O OE2 . GLU A 189 ? 1.2550 1.5072 1.2059 0.0026  -0.0112 0.0162  233 GLU A OE2 
1540 N N   . LYS A 190 ? 1.1752 1.4653 1.2420 0.0150  0.0115  -0.0331 234 LYS A N   
1541 C CA  . LYS A 190 ? 1.1755 1.4701 1.2620 0.0221  0.0171  -0.0369 234 LYS A CA  
1542 C C   . LYS A 190 ? 1.1613 1.4486 1.2535 0.0057  0.0279  -0.0487 234 LYS A C   
1543 O O   . LYS A 190 ? 1.1583 1.4673 1.2668 0.0003  0.0314  -0.0554 234 LYS A O   
1544 C CB  . LYS A 190 ? 1.1928 1.4560 1.2741 0.0389  0.0192  -0.0283 234 LYS A CB  
1545 C CG  . LYS A 190 ? 1.2260 1.4869 1.3004 0.0575  0.0084  -0.0148 234 LYS A CG  
1546 C CD  . LYS A 190 ? 1.2391 1.4647 1.3092 0.0741  0.0114  -0.0092 234 LYS A CD  
1547 C CE  . LYS A 190 ? 1.2364 1.4185 1.2861 0.0638  0.0179  -0.0076 234 LYS A CE  
1548 N NZ  . LYS A 190 ? 1.2563 1.4021 1.2994 0.0774  0.0203  -0.0039 234 LYS A NZ  
1549 N N   . VAL A 191 ? 1.1609 1.4181 1.2398 -0.0021 0.0332  -0.0504 235 VAL A N   
1550 C CA  . VAL A 191 ? 1.1468 1.3897 1.2288 -0.0139 0.0419  -0.0588 235 VAL A CA  
1551 C C   . VAL A 191 ? 1.1434 1.4019 1.2279 -0.0300 0.0418  -0.0698 235 VAL A C   
1552 O O   . VAL A 191 ? 1.1472 1.4136 1.2224 -0.0343 0.0374  -0.0727 235 VAL A O   
1553 C CB  . VAL A 191 ? 1.1507 1.3608 1.2214 -0.0135 0.0462  -0.0571 235 VAL A CB  
1554 C CG1 . VAL A 191 ? 1.1439 1.3381 1.2178 -0.0221 0.0529  -0.0638 235 VAL A CG1 
1555 C CG2 . VAL A 191 ? 1.1585 1.3514 1.2244 -0.0013 0.0462  -0.0484 235 VAL A CG2 
1556 N N   . GLN A 192 ? 1.1341 1.3948 1.2286 -0.0405 0.0473  -0.0763 236 GLN A N   
1557 C CA  . GLN A 192 ? 1.1266 1.3972 1.2235 -0.0588 0.0482  -0.0884 236 GLN A CA  
1558 C C   . GLN A 192 ? 1.1115 1.3445 1.2020 -0.0669 0.0559  -0.0943 236 GLN A C   
1559 O O   . GLN A 192 ? 1.1161 1.3409 1.2002 -0.0754 0.0565  -0.1049 236 GLN A O   
1560 C CB  . GLN A 192 ? 1.1343 1.4358 1.2476 -0.0679 0.0489  -0.0912 236 GLN A CB  
1561 C CG  . GLN A 192 ? 1.1583 1.4682 1.2737 -0.0914 0.0503  -0.1049 236 GLN A CG  
1562 C CD  . GLN A 192 ? 1.1672 1.5071 1.2998 -0.1046 0.0533  -0.1077 236 GLN A CD  
1563 O OE1 . GLN A 192 ? 1.1579 1.5211 1.3033 -0.0938 0.0540  -0.1004 236 GLN A OE1 
1564 N NE2 . GLN A 192 ? 1.1919 1.5319 1.3252 -0.1292 0.0564  -0.1196 236 GLN A NE2 
1565 N N   . THR A 193 ? 1.0875 1.2982 1.1792 -0.0635 0.0613  -0.0878 237 THR A N   
1566 C CA  . THR A 193 ? 1.0846 1.2590 1.1712 -0.0689 0.0669  -0.0902 237 THR A CA  
1567 C C   . THR A 193 ? 1.0673 1.2195 1.1491 -0.0551 0.0677  -0.0799 237 THR A C   
1568 O O   . THR A 193 ? 1.0444 1.2070 1.1269 -0.0463 0.0665  -0.0720 237 THR A O   
1569 C CB  . THR A 193 ? 1.0989 1.2690 1.1890 -0.0858 0.0721  -0.0921 237 THR A CB  
1570 O OG1 . THR A 193 ? 1.1025 1.3009 1.1990 -0.1007 0.0703  -0.1027 237 THR A OG1 
1571 C CG2 . THR A 193 ? 1.1242 1.2502 1.2064 -0.0914 0.0765  -0.0931 237 THR A CG2 
1572 N N   . LEU A 194 ? 1.0751 1.1979 1.1527 -0.0527 0.0693  -0.0814 238 LEU A N   
1573 C CA  . LEU A 194 ? 1.0757 1.1795 1.1498 -0.0420 0.0687  -0.0720 238 LEU A CA  
1574 C C   . LEU A 194 ? 1.1005 1.1723 1.1710 -0.0460 0.0709  -0.0698 238 LEU A C   
1575 O O   . LEU A 194 ? 1.1149 1.1672 1.1867 -0.0436 0.0713  -0.0764 238 LEU A O   
1576 C CB  . LEU A 194 ? 1.0678 1.1726 1.1425 -0.0311 0.0662  -0.0741 238 LEU A CB  
1577 C CG  . LEU A 194 ? 1.0662 1.1589 1.1396 -0.0210 0.0639  -0.0658 238 LEU A CG  
1578 C CD1 . LEU A 194 ? 1.0516 1.1541 1.1201 -0.0182 0.0621  -0.0576 238 LEU A CD1 
1579 C CD2 . LEU A 194 ? 1.0596 1.1552 1.1380 -0.0136 0.0631  -0.0710 238 LEU A CD2 
1580 N N   . GLU A 195 ? 1.1120 1.1774 1.1768 -0.0515 0.0729  -0.0602 239 GLU A N   
1581 C CA  . GLU A 195 ? 1.1476 1.1787 1.2039 -0.0562 0.0743  -0.0533 239 GLU A CA  
1582 C C   . GLU A 195 ? 1.1411 1.1575 1.1920 -0.0411 0.0688  -0.0429 239 GLU A C   
1583 O O   . GLU A 195 ? 1.1272 1.1600 1.1751 -0.0356 0.0669  -0.0373 239 GLU A O   
1584 C CB  . GLU A 195 ? 1.1720 1.2069 1.2218 -0.0725 0.0800  -0.0471 239 GLU A CB  
1585 C CG  . GLU A 195 ? 1.2213 1.2164 1.2570 -0.0807 0.0818  -0.0365 239 GLU A CG  
1586 C CD  . GLU A 195 ? 1.2505 1.2497 1.2795 -0.1035 0.0900  -0.0325 239 GLU A CD  
1587 O OE1 . GLU A 195 ? 1.2415 1.2720 1.2707 -0.1059 0.0938  -0.0295 239 GLU A OE1 
1588 O OE2 . GLU A 195 ? 1.2932 1.2642 1.3170 -0.1194 0.0935  -0.0335 239 GLU A OE2 
1589 N N   . ALA A 196 ? 1.1622 1.1481 1.2124 -0.0342 0.0659  -0.0414 240 ALA A N   
1590 C CA  . ALA A 196 ? 1.1666 1.1427 1.2148 -0.0186 0.0585  -0.0317 240 ALA A CA  
1591 C C   . ALA A 196 ? 1.2046 1.1494 1.2358 -0.0222 0.0564  -0.0153 240 ALA A C   
1592 O O   . ALA A 196 ? 1.2477 1.1602 1.2733 -0.0299 0.0593  -0.0139 240 ALA A O   
1593 C CB  . ALA A 196 ? 1.1676 1.1368 1.2295 -0.0042 0.0558  -0.0408 240 ALA A CB  
1594 N N   . TRP A 197 ? 1.1960 1.1490 1.2165 -0.0182 0.0513  -0.0031 241 TRP A N   
1595 C CA  . TRP A 197 ? 1.2322 1.1583 1.2320 -0.0206 0.0475  0.0151  241 TRP A CA  
1596 C C   . TRP A 197 ? 1.2462 1.1633 1.2482 -0.0003 0.0346  0.0235  241 TRP A C   
1597 O O   . TRP A 197 ? 1.2248 1.1689 1.2297 0.0074  0.0284  0.0235  241 TRP A O   
1598 C CB  . TRP A 197 ? 1.2232 1.1683 1.2056 -0.0325 0.0514  0.0220  241 TRP A CB  
1599 C CG  . TRP A 197 ? 1.2199 1.1774 1.2020 -0.0515 0.0639  0.0156  241 TRP A CG  
1600 C CD1 . TRP A 197 ? 1.2285 1.1775 1.2195 -0.0627 0.0705  0.0074  241 TRP A CD1 
1601 C CD2 . TRP A 197 ? 1.2097 1.1949 1.1839 -0.0614 0.0714  0.0149  241 TRP A CD2 
1602 N NE1 . TRP A 197 ? 1.2198 1.1938 1.2112 -0.0791 0.0804  0.0029  241 TRP A NE1 
1603 C CE2 . TRP A 197 ? 1.2068 1.2035 1.1891 -0.0771 0.0818  0.0072  241 TRP A CE2 
1604 C CE3 . TRP A 197 ? 1.2010 1.2039 1.1625 -0.0584 0.0707  0.0181  241 TRP A CE3 
1605 C CZ2 . TRP A 197 ? 1.1954 1.2240 1.1772 -0.0873 0.0915  0.0033  241 TRP A CZ2 
1606 C CZ3 . TRP A 197 ? 1.1898 1.2187 1.1479 -0.0683 0.0814  0.0130  241 TRP A CZ3 
1607 C CH2 . TRP A 197 ? 1.1888 1.2320 1.1587 -0.0813 0.0918  0.0060  241 TRP A CH2 
1608 N N   . VAL A 198 ? 1.2877 1.1669 1.2893 0.0082  0.0303  0.0299  242 VAL A N   
1609 C CA  . VAL A 198 ? 1.3099 1.1820 1.3183 0.0312  0.0169  0.0379  242 VAL A CA  
1610 C C   . VAL A 198 ? 1.3598 1.2088 1.3404 0.0306  0.0078  0.0629  242 VAL A C   
1611 O O   . VAL A 198 ? 1.4002 1.2064 1.3621 0.0218  0.0103  0.0752  242 VAL A O   
1612 C CB  . VAL A 198 ? 1.3262 1.1700 1.3524 0.0461  0.0169  0.0291  242 VAL A CB  
1613 C CG1 . VAL A 198 ? 1.3390 1.1851 1.3796 0.0742  0.0029  0.0350  242 VAL A CG1 
1614 C CG2 . VAL A 198 ? 1.2872 1.1524 1.3338 0.0419  0.0277  0.0043  242 VAL A CG2 
1615 N N   . ILE A 199 ? 1.3630 1.2402 1.3390 0.0378  -0.0028 0.0705  243 ILE A N   
1616 C CA  . ILE A 199 ? 1.4184 1.2822 1.3641 0.0359  -0.0127 0.0941  243 ILE A CA  
1617 C C   . ILE A 199 ? 1.4764 1.3216 1.4279 0.0616  -0.0303 0.1081  243 ILE A C   
1618 O O   . ILE A 199 ? 1.4590 1.3301 1.4400 0.0812  -0.0376 0.0976  243 ILE A O   
1619 C CB  . ILE A 199 ? 1.3879 1.2934 1.3217 0.0272  -0.0145 0.0926  243 ILE A CB  
1620 C CG1 . ILE A 199 ? 1.3679 1.2811 1.2868 0.0029  0.0021  0.0858  243 ILE A CG1 
1621 C CG2 . ILE A 199 ? 1.4239 1.3273 1.3321 0.0327  -0.0307 0.1144  243 ILE A CG2 
1622 C CD1 . ILE A 199 ? 1.3312 1.2523 1.2737 -0.0027 0.0159  0.0656  243 ILE A CD1 
1623 N N   . HIS A 200 ? 1.5570 1.3586 1.4802 0.0613  -0.0369 0.1325  244 HIS A N   
1624 C CA  . HIS A 200 ? 1.6156 1.3919 1.5407 0.0879  -0.0553 0.1502  244 HIS A CA  
1625 C C   . HIS A 200 ? 1.6451 1.4456 1.5486 0.0923  -0.0731 0.1698  244 HIS A C   
1626 O O   . HIS A 200 ? 1.6189 1.4471 1.5015 0.0719  -0.0687 0.1692  244 HIS A O   
1627 C CB  . HIS A 200 ? 1.6829 1.3876 1.5878 0.0856  -0.0525 0.1665  244 HIS A CB  
1628 C CG  . HIS A 200 ? 1.6774 1.3568 1.6030 0.0817  -0.0369 0.1456  244 HIS A CG  
1629 N ND1 . HIS A 200 ? 1.6341 1.3338 1.5653 0.0571  -0.0184 0.1248  244 HIS A ND1 
1630 C CD2 . HIS A 200 ? 1.7126 1.3485 1.6535 0.0995  -0.0376 0.1411  244 HIS A CD2 
1631 C CE1 . HIS A 200 ? 1.6383 1.3101 1.5860 0.0581  -0.0091 0.1088  244 HIS A CE1 
1632 N NE2 . HIS A 200 ? 1.6868 1.3179 1.6401 0.0833  -0.0195 0.1170  244 HIS A NE2 
1633 N N   . GLY A 201 ? 1.7105 1.5016 1.6195 0.1200  -0.0937 0.1862  245 GLY A N   
1634 C CA  . GLY A 201 ? 1.7507 1.5659 1.6392 0.1265  -0.1146 0.2065  245 GLY A CA  
1635 C C   . GLY A 201 ? 1.8359 1.6085 1.6702 0.1104  -0.1176 0.2372  245 GLY A C   
1636 O O   . GLY A 201 ? 1.8449 1.6045 1.6538 0.0807  -0.0994 0.2352  245 GLY A O   
1637 N N   . GLY A 202 ? 1.9110 1.6649 1.7280 0.1303  -0.1408 0.2660  246 GLY A N   
1638 C CA  . GLY A 202 ? 1.9948 1.7067 1.7560 0.1164  -0.1463 0.2997  246 GLY A CA  
1639 C C   . GLY A 202 ? 2.0819 1.7128 1.8320 0.1271  -0.1475 0.3210  246 GLY A C   
1640 O O   . GLY A 202 ? 2.1510 1.7505 1.8821 0.1478  -0.1692 0.3517  246 GLY A O   
1641 N N   . ARG A 203 ? 2.0798 1.6763 1.8408 0.1123  -0.1245 0.3044  247 ARG A N   
1642 C CA  . ARG A 203 ? 2.1434 1.6589 1.8973 0.1184  -0.1215 0.3174  247 ARG A CA  
1643 C C   . ARG A 203 ? 2.1704 1.6716 1.9598 0.1647  -0.1406 0.3188  247 ARG A C   
1644 O O   . ARG A 203 ? 2.2417 1.6804 2.0128 0.1833  -0.1545 0.3466  247 ARG A O   
1645 C CB  . ARG A 203 ? 2.2261 1.6853 1.9187 0.0981  -0.1245 0.3558  247 ARG A CB  
1646 C CG  . ARG A 203 ? 2.2951 1.6655 1.9724 0.0886  -0.1135 0.3660  247 ARG A CG  
1647 C CD  . ARG A 203 ? 2.3904 1.7011 2.0046 0.0702  -0.1188 0.4086  247 ARG A CD  
1648 N NE  . ARG A 203 ? 2.3797 1.7230 1.9569 0.0276  -0.1036 0.4119  247 ARG A NE  
1649 C CZ  . ARG A 203 ? 2.3546 1.7017 1.9305 -0.0097 -0.0761 0.3932  247 ARG A CZ  
1650 N NH1 . ARG A 203 ? 2.3427 1.6610 1.9492 -0.0124 -0.0617 0.3706  247 ARG A NH1 
1651 N NH2 . ARG A 203 ? 2.3421 1.7245 1.8862 -0.0441 -0.0631 0.3962  247 ARG A NH2 
1652 N N   . GLU A 204 ? 2.1107 1.6707 1.9513 0.1832  -0.1405 0.2886  248 GLU A N   
1653 C CA  . GLU A 204 ? 2.1231 1.6847 2.0058 0.2274  -0.1553 0.2833  248 GLU A CA  
1654 C C   . GLU A 204 ? 2.1309 1.6471 2.0393 0.2327  -0.1374 0.2601  248 GLU A C   
1655 O O   . GLU A 204 ? 2.1846 1.6377 2.0948 0.2577  -0.1442 0.2711  248 GLU A O   
1656 C CB  . GLU A 204 ? 2.0494 1.7024 1.9732 0.2413  -0.1632 0.2622  248 GLU A CB  
1657 C CG  . GLU A 204 ? 2.0438 1.7455 1.9440 0.2361  -0.1823 0.2811  248 GLU A CG  
1658 C CD  . GLU A 204 ? 2.1146 1.7996 2.0015 0.2673  -0.2129 0.3158  248 GLU A CD  
1659 O OE1 . GLU A 204 ? 2.1885 1.8017 2.0346 0.2658  -0.2174 0.3462  248 GLU A OE1 
1660 O OE2 . GLU A 204 ? 2.0944 1.8392 2.0116 0.2924  -0.2327 0.3133  248 GLU A OE2 
1661 N N   . ASP A 205 ? 2.0749 1.6226 2.0012 0.2091  -0.1149 0.2278  249 ASP A N   
1662 C CA  . ASP A 205 ? 2.0684 1.5857 2.0188 0.2099  -0.0969 0.2008  249 ASP A CA  
1663 C C   . ASP A 205 ? 2.0938 1.5500 2.0078 0.1736  -0.0796 0.2060  249 ASP A C   
1664 O O   . ASP A 205 ? 2.0519 1.5353 1.9493 0.1385  -0.0666 0.2011  249 ASP A O   
1665 C CB  . ASP A 205 ? 1.9827 1.5707 1.9720 0.2050  -0.0838 0.1640  249 ASP A CB  
1666 C CG  . ASP A 205 ? 1.9528 1.6047 1.9829 0.2372  -0.0976 0.1547  249 ASP A CG  
1667 O OD1 . ASP A 205 ? 2.0002 1.6498 2.0302 0.2645  -0.1195 0.1769  249 ASP A OD1 
1668 O OD2 . ASP A 205 ? 1.8891 1.5943 1.9503 0.2338  -0.0867 0.1259  249 ASP A OD2 
1669 N N   . SER A 206 ? 2.1550 1.5288 2.0580 0.1825  -0.0794 0.2151  250 SER A N   
1670 C CA  . SER A 206 ? 2.1741 1.4865 2.0487 0.1475  -0.0615 0.2148  250 SER A CA  
1671 C C   . SER A 206 ? 2.1336 1.4445 2.0393 0.1432  -0.0430 0.1755  250 SER A C   
1672 O O   . SER A 206 ? 2.1493 1.4206 2.0384 0.1117  -0.0268 0.1677  250 SER A O   
1673 C CB  . SER A 206 ? 2.2740 1.4913 2.1134 0.1538  -0.0707 0.2473  250 SER A CB  
1674 O OG  . SER A 206 ? 2.3136 1.4919 2.1786 0.1980  -0.0817 0.2435  250 SER A OG  
1675 N N   . ARG A 207 ? 2.0745 1.4322 2.0243 0.1730  -0.0454 0.1505  251 ARG A N   
1676 C CA  . ARG A 207 ? 2.0368 1.4001 2.0153 0.1715  -0.0288 0.1123  251 ARG A CA  
1677 C C   . ARG A 207 ? 1.9540 1.3776 1.9347 0.1358  -0.0132 0.0928  251 ARG A C   
1678 O O   . ARG A 207 ? 1.9162 1.3822 1.8829 0.1188  -0.0159 0.1062  251 ARG A O   
1679 C CB  . ARG A 207 ? 2.0119 1.4116 2.0355 0.2146  -0.0358 0.0935  251 ARG A CB  
1680 C CG  . ARG A 207 ? 1.9255 1.4223 1.9739 0.2187  -0.0401 0.0856  251 ARG A CG  
1681 C CD  . ARG A 207 ? 1.9118 1.4476 2.0037 0.2612  -0.0493 0.0728  251 ARG A CD  
1682 N NE  . ARG A 207 ? 1.9698 1.4844 2.0607 0.2949  -0.0719 0.1012  251 ARG A NE  
1683 C CZ  . ARG A 207 ? 1.9680 1.5216 2.0969 0.3349  -0.0848 0.0971  251 ARG A CZ  
1684 N NH1 . ARG A 207 ? 1.9116 1.5277 2.0815 0.3437  -0.0751 0.0650  251 ARG A NH1 
1685 N NH2 . ARG A 207 ? 2.0223 1.5552 2.1480 0.3656  -0.1076 0.1257  251 ARG A NH2 
1686 N N   . ASP A 208 ? 1.9306 1.3570 1.9284 0.1261  0.0024  0.0604  252 ASP A N   
1687 C CA  . ASP A 208 ? 1.8600 1.3435 1.8636 0.0971  0.0158  0.0402  252 ASP A CA  
1688 C C   . ASP A 208 ? 1.7988 1.3557 1.8376 0.1175  0.0140  0.0211  252 ASP A C   
1689 O O   . ASP A 208 ? 1.8101 1.3665 1.8747 0.1431  0.0147  0.0026  252 ASP A O   
1690 C CB  . ASP A 208 ? 1.8786 1.3276 1.8776 0.0725  0.0321  0.0173  252 ASP A CB  
1691 C CG  . ASP A 208 ? 1.8151 1.3190 1.8163 0.0406  0.0442  0.0003  252 ASP A CG  
1692 O OD1 . ASP A 208 ? 1.7635 1.3307 1.7721 0.0402  0.0411  0.0040  252 ASP A OD1 
1693 O OD2 . ASP A 208 ? 1.8318 1.3139 1.8271 0.0164  0.0560  -0.0166 252 ASP A OD2 
1694 N N   . LEU A 209 ? 1.7395 1.3582 1.7782 0.1047  0.0130  0.0249  253 LEU A N   
1695 C CA  . LEU A 209 ? 1.6714 1.3584 1.7385 0.1195  0.0105  0.0115  253 LEU A CA  
1696 C C   . LEU A 209 ? 1.6172 1.3423 1.6945 0.1000  0.0252  -0.0146 253 LEU A C   
1697 O O   . LEU A 209 ? 1.5499 1.3314 1.6456 0.1047  0.0255  -0.0249 253 LEU A O   
1698 C CB  . LEU A 209 ? 1.6428 1.3676 1.7004 0.1182  -0.0010 0.0326  253 LEU A CB  
1699 C CG  . LEU A 209 ? 1.6900 1.3881 1.7365 0.1388  -0.0188 0.0604  253 LEU A CG  
1700 C CD1 . LEU A 209 ? 1.6611 1.4038 1.6965 0.1337  -0.0294 0.0765  253 LEU A CD1 
1701 C CD2 . LEU A 209 ? 1.7140 1.4095 1.7910 0.1770  -0.0278 0.0541  253 LEU A CD2 
1702 N N   . CYS A 210 ? 1.6452 1.3395 1.7095 0.0771  0.0367  -0.0244 254 CYS A N   
1703 C CA  . CYS A 210 ? 1.6199 1.3476 1.6914 0.0589  0.0488  -0.0482 254 CYS A CA  
1704 C C   . CYS A 210 ? 1.6359 1.3613 1.7277 0.0743  0.0552  -0.0752 254 CYS A C   
1705 O O   . CYS A 210 ? 1.6060 1.3691 1.7064 0.0651  0.0634  -0.0955 254 CYS A O   
1706 C CB  . CYS A 210 ? 1.6420 1.3464 1.6924 0.0261  0.0572  -0.0483 254 CYS A CB  
1707 S SG  . CYS A 210 ? 1.6477 1.3638 1.6749 0.0056  0.0539  -0.0209 254 CYS A SG  
1708 N N   . GLN A 211 ? 1.6842 1.3651 1.7825 0.0986  0.0514  -0.0751 255 GLN A N   
1709 C CA  . GLN A 211 ? 1.6942 1.3709 1.8132 0.1177  0.0584  -0.1022 255 GLN A CA  
1710 C C   . GLN A 211 ? 1.6481 1.3764 1.7966 0.1473  0.0527  -0.1051 255 GLN A C   
1711 O O   . GLN A 211 ? 1.6555 1.3915 1.8257 0.1669  0.0589  -0.1278 255 GLN A O   
1712 C CB  . GLN A 211 ? 1.7844 1.3816 1.8961 0.1300  0.0585  -0.1032 255 GLN A CB  
1713 C CG  . GLN A 211 ? 1.8241 1.3763 1.9148 0.0999  0.0701  -0.1180 255 GLN A CG  
1714 C CD  . GLN A 211 ? 1.8112 1.3708 1.8782 0.0630  0.0705  -0.1016 255 GLN A CD  
1715 O OE1 . GLN A 211 ? 1.8277 1.3679 1.8790 0.0591  0.0623  -0.0728 255 GLN A OE1 
1716 N NE2 . GLN A 211 ? 1.7835 1.3751 1.8477 0.0361  0.0799  -0.1202 255 GLN A NE2 
1717 N N   . ASP A 212 ? 1.5960 1.3619 1.7456 0.1489  0.0418  -0.0838 256 ASP A N   
1718 C CA  . ASP A 212 ? 1.5504 1.3732 1.7277 0.1704  0.0360  -0.0859 256 ASP A CA  
1719 C C   . ASP A 212 ? 1.5102 1.3831 1.7020 0.1617  0.0495  -0.1126 256 ASP A C   
1720 O O   . ASP A 212 ? 1.4854 1.3706 1.6613 0.1343  0.0569  -0.1172 256 ASP A O   
1721 C CB  . ASP A 212 ? 1.5076 1.3601 1.6768 0.1647  0.0232  -0.0607 256 ASP A CB  
1722 C CG  . ASP A 212 ? 1.4781 1.3842 1.6752 0.1868  0.0136  -0.0591 256 ASP A CG  
1723 O OD1 . ASP A 212 ? 1.4346 1.3913 1.6514 0.1849  0.0215  -0.0775 256 ASP A OD1 
1724 O OD2 . ASP A 212 ? 1.4960 1.3945 1.6936 0.2040  -0.0020 -0.0387 256 ASP A OD2 
1725 N N   . PRO A 213 ? 1.5043 1.4095 1.7261 0.1846  0.0532  -0.1306 257 PRO A N   
1726 C CA  . PRO A 213 ? 1.4706 1.4203 1.7023 0.1750  0.0678  -0.1564 257 PRO A CA  
1727 C C   . PRO A 213 ? 1.4114 1.4156 1.6380 0.1529  0.0682  -0.1503 257 PRO A C   
1728 O O   . PRO A 213 ? 1.4015 1.4310 1.6234 0.1365  0.0797  -0.1662 257 PRO A O   
1729 C CB  . PRO A 213 ? 1.4839 1.4601 1.7514 0.2073  0.0704  -0.1729 257 PRO A CB  
1730 C CG  . PRO A 213 ? 1.4997 1.4698 1.7802 0.2319  0.0522  -0.1493 257 PRO A CG  
1731 C CD  . PRO A 213 ? 1.5322 1.4358 1.7802 0.2212  0.0438  -0.1270 257 PRO A CD  
1732 N N   . THR A 214 ? 1.3798 1.3993 1.6048 0.1524  0.0552  -0.1274 258 THR A N   
1733 C CA  . THR A 214 ? 1.3180 1.3794 1.5359 0.1320  0.0548  -0.1207 258 THR A CA  
1734 C C   . THR A 214 ? 1.3000 1.3388 1.4878 0.1055  0.0579  -0.1145 258 THR A C   
1735 O O   . THR A 214 ? 1.2619 1.3286 1.4419 0.0878  0.0624  -0.1166 258 THR A O   
1736 C CB  . THR A 214 ? 1.2987 1.3832 1.5241 0.1396  0.0403  -0.1017 258 THR A CB  
1737 O OG1 . THR A 214 ? 1.3271 1.3680 1.5352 0.1431  0.0292  -0.0815 258 THR A OG1 
1738 C CG2 . THR A 214 ? 1.3000 1.4220 1.5601 0.1642  0.0365  -0.1088 258 THR A CG2 
1739 N N   . ILE A 215 ? 1.3284 1.3173 1.5000 0.1031  0.0553  -0.1063 259 ILE A N   
1740 C CA  . ILE A 215 ? 1.3270 1.2980 1.4746 0.0785  0.0594  -0.1033 259 ILE A CA  
1741 C C   . ILE A 215 ? 1.3365 1.3084 1.4826 0.0684  0.0716  -0.1264 259 ILE A C   
1742 O O   . ILE A 215 ? 1.3139 1.3023 1.4479 0.0485  0.0756  -0.1291 259 ILE A O   
1743 C CB  . ILE A 215 ? 1.3614 1.2820 1.4918 0.0755  0.0540  -0.0869 259 ILE A CB  
1744 C CG1 . ILE A 215 ? 1.3492 1.2775 1.4697 0.0738  0.0435  -0.0632 259 ILE A CG1 
1745 C CG2 . ILE A 215 ? 1.3707 1.2686 1.4834 0.0518  0.0618  -0.0929 259 ILE A CG2 
1746 C CD1 . ILE A 215 ? 1.3478 1.2994 1.4847 0.0952  0.0331  -0.0560 259 ILE A CD1 
1747 N N   . LYS A 216 ? 1.3694 1.3240 1.5274 0.0832  0.0770  -0.1437 260 LYS A N   
1748 C CA  . LYS A 216 ? 1.3747 1.3310 1.5298 0.0744  0.0891  -0.1691 260 LYS A CA  
1749 C C   . LYS A 216 ? 1.3249 1.3378 1.4847 0.0677  0.0948  -0.1782 260 LYS A C   
1750 O O   . LYS A 216 ? 1.3148 1.3397 1.4620 0.0505  0.1019  -0.1910 260 LYS A O   
1751 C CB  . LYS A 216 ? 1.4315 1.3570 1.5996 0.0954  0.0945  -0.1876 260 LYS A CB  
1752 C CG  . LYS A 216 ? 1.4933 1.3512 1.6517 0.0995  0.0902  -0.1800 260 LYS A CG  
1753 C CD  . LYS A 216 ? 1.5199 1.3464 1.6542 0.0710  0.0953  -0.1863 260 LYS A CD  
1754 C CE  . LYS A 216 ? 1.5763 1.3345 1.6974 0.0694  0.0910  -0.1738 260 LYS A CE  
1755 N NZ  . LYS A 216 ? 1.5959 1.3296 1.6958 0.0377  0.0968  -0.1818 260 LYS A NZ  
1756 N N   . GLU A 217 ? 1.2961 1.3438 1.4727 0.0799  0.0911  -0.1707 261 GLU A N   
1757 C CA  . GLU A 217 ? 1.2618 1.3600 1.4403 0.0705  0.0959  -0.1744 261 GLU A CA  
1758 C C   . GLU A 217 ? 1.2236 1.3273 1.3807 0.0488  0.0915  -0.1591 261 GLU A C   
1759 O O   . GLU A 217 ? 1.2073 1.3290 1.3516 0.0334  0.0971  -0.1658 261 GLU A O   
1760 C CB  . GLU A 217 ? 1.2583 1.3905 1.4606 0.0858  0.0919  -0.1689 261 GLU A CB  
1761 C CG  . GLU A 217 ? 1.2415 1.4245 1.4467 0.0745  0.0990  -0.1743 261 GLU A CG  
1762 C CD  . GLU A 217 ? 1.2339 1.4545 1.4617 0.0831  0.0942  -0.1674 261 GLU A CD  
1763 O OE1 . GLU A 217 ? 1.2295 1.4909 1.4602 0.0716  0.1010  -0.1716 261 GLU A OE1 
1764 O OE2 . GLU A 217 ? 1.2395 1.4494 1.4806 0.0997  0.0831  -0.1571 261 GLU A OE2 
1765 N N   . LEU A 218 ? 1.1990 1.2876 1.3517 0.0489  0.0813  -0.1388 262 LEU A N   
1766 C CA  . LEU A 218 ? 1.1653 1.2571 1.3006 0.0323  0.0773  -0.1250 262 LEU A CA  
1767 C C   . LEU A 218 ? 1.1711 1.2511 1.2910 0.0171  0.0817  -0.1326 262 LEU A C   
1768 O O   . LEU A 218 ? 1.1600 1.2595 1.2691 0.0043  0.0822  -0.1307 262 LEU A O   
1769 C CB  . LEU A 218 ? 1.1561 1.2279 1.2880 0.0362  0.0677  -0.1059 262 LEU A CB  
1770 C CG  . LEU A 218 ? 1.1326 1.2023 1.2473 0.0214  0.0650  -0.0938 262 LEU A CG  
1771 C CD1 . LEU A 218 ? 1.1066 1.2067 1.2182 0.0146  0.0653  -0.0913 262 LEU A CD1 
1772 C CD2 . LEU A 218 ? 1.1399 1.1901 1.2489 0.0247  0.0576  -0.0772 262 LEU A CD2 
1773 N N   . GLU A 219 ? 1.1960 1.2434 1.3150 0.0183  0.0839  -0.1409 263 GLU A N   
1774 C CA  . GLU A 219 ? 1.2088 1.2462 1.3149 0.0017  0.0879  -0.1514 263 GLU A CA  
1775 C C   . GLU A 219 ? 1.2001 1.2686 1.3021 -0.0051 0.0944  -0.1679 263 GLU A C   
1776 O O   . GLU A 219 ? 1.1829 1.2684 1.2724 -0.0205 0.0934  -0.1675 263 GLU A O   
1777 C CB  . GLU A 219 ? 1.2525 1.2448 1.3587 0.0044  0.0905  -0.1606 263 GLU A CB  
1778 C CG  . GLU A 219 ? 1.2693 1.2494 1.3621 -0.0166 0.0943  -0.1730 263 GLU A CG  
1779 C CD  . GLU A 219 ? 1.3155 1.2418 1.4047 -0.0186 0.0965  -0.1785 263 GLU A CD  
1780 O OE1 . GLU A 219 ? 1.3445 1.2454 1.4414 -0.0023 0.1003  -0.1905 263 GLU A OE1 
1781 O OE2 . GLU A 219 ? 1.3163 1.2259 1.3955 -0.0364 0.0947  -0.1709 263 GLU A OE2 
1782 N N   . SER A 220 ? 1.2081 1.2870 1.3209 0.0067  0.1010  -0.1818 264 SER A N   
1783 C CA  . SER A 220 ? 1.2098 1.3185 1.3162 -0.0002 0.1093  -0.1989 264 SER A CA  
1784 C C   . SER A 220 ? 1.1779 1.3224 1.2755 -0.0093 0.1064  -0.1852 264 SER A C   
1785 O O   . SER A 220 ? 1.1713 1.3354 1.2525 -0.0230 0.1086  -0.1906 264 SER A O   
1786 C CB  . SER A 220 ? 1.2286 1.3443 1.3512 0.0158  0.1186  -0.2168 264 SER A CB  
1787 O OG  . SER A 220 ? 1.2725 1.3482 1.4014 0.0260  0.1213  -0.2305 264 SER A OG  
1788 N N   . ILE A 221 ? 1.1618 1.3126 1.2684 -0.0022 0.1008  -0.1675 265 ILE A N   
1789 C CA  . ILE A 221 ? 1.1436 1.3189 1.2412 -0.0104 0.0980  -0.1536 265 ILE A CA  
1790 C C   . ILE A 221 ? 1.1317 1.3018 1.2125 -0.0220 0.0912  -0.1431 265 ILE A C   
1791 O O   . ILE A 221 ? 1.1268 1.3153 1.1925 -0.0320 0.0911  -0.1411 265 ILE A O   
1792 C CB  . ILE A 221 ? 1.1341 1.3128 1.2446 -0.0017 0.0931  -0.1394 265 ILE A CB  
1793 C CG1 . ILE A 221 ? 1.1464 1.3437 1.2773 0.0094  0.0992  -0.1502 265 ILE A CG1 
1794 C CG2 . ILE A 221 ? 1.1187 1.3101 1.2166 -0.0118 0.0892  -0.1241 265 ILE A CG2 
1795 C CD1 . ILE A 221 ? 1.1362 1.3391 1.2825 0.0183  0.0923  -0.1382 265 ILE A CD1 
1796 N N   . ILE A 222 ? 1.1231 1.2700 1.2068 -0.0203 0.0857  -0.1359 266 ILE A N   
1797 C CA  . ILE A 222 ? 1.1086 1.2557 1.1824 -0.0293 0.0798  -0.1266 266 ILE A CA  
1798 C C   . ILE A 222 ? 1.1196 1.2753 1.1833 -0.0414 0.0814  -0.1399 266 ILE A C   
1799 O O   . ILE A 222 ? 1.1092 1.2829 1.1631 -0.0490 0.0764  -0.1341 266 ILE A O   
1800 C CB  . ILE A 222 ? 1.1059 1.2292 1.1854 -0.0264 0.0760  -0.1175 266 ILE A CB  
1801 C CG1 . ILE A 222 ? 1.0966 1.2159 1.1817 -0.0163 0.0726  -0.1038 266 ILE A CG1 
1802 C CG2 . ILE A 222 ? 1.0990 1.2283 1.1725 -0.0365 0.0722  -0.1121 266 ILE A CG2 
1803 C CD1 . ILE A 222 ? 1.0888 1.2228 1.1672 -0.0181 0.0688  -0.0918 266 ILE A CD1 
1804 N N   . SER A 223 ? 1.1363 1.2792 1.2022 -0.0425 0.0876  -0.1584 267 SER A N   
1805 C CA  . SER A 223 ? 1.1551 1.3042 1.2100 -0.0564 0.0895  -0.1749 267 SER A CA  
1806 C C   . SER A 223 ? 1.1539 1.3362 1.1938 -0.0627 0.0905  -0.1789 267 SER A C   
1807 O O   . SER A 223 ? 1.1688 1.3682 1.1954 -0.0757 0.0866  -0.1835 267 SER A O   
1808 C CB  . SER A 223 ? 1.1858 1.3074 1.2450 -0.0551 0.0972  -0.1957 267 SER A CB  
1809 O OG  . SER A 223 ? 1.2030 1.2897 1.2701 -0.0532 0.0951  -0.1897 267 SER A OG  
1810 N N   . LYS A 224 ? 1.1385 1.3320 1.1797 -0.0550 0.0954  -0.1765 268 LYS A N   
1811 C CA  . LYS A 224 ? 1.1351 1.3579 1.1587 -0.0627 0.0982  -0.1788 268 LYS A CA  
1812 C C   . LYS A 224 ? 1.1122 1.3485 1.1241 -0.0662 0.0881  -0.1556 268 LYS A C   
1813 O O   . LYS A 224 ? 1.1115 1.3692 1.1034 -0.0744 0.0872  -0.1525 268 LYS A O   
1814 C CB  . LYS A 224 ? 1.1389 1.3711 1.1700 -0.0556 0.1090  -0.1856 268 LYS A CB  
1815 C CG  . LYS A 224 ? 1.1595 1.4222 1.1700 -0.0665 0.1159  -0.1921 268 LYS A CG  
1816 C CD  . LYS A 224 ? 1.1703 1.4471 1.1912 -0.0612 0.1307  -0.2093 268 LYS A CD  
1817 C CE  . LYS A 224 ? 1.1516 1.4317 1.1931 -0.0512 0.1317  -0.1966 268 LYS A CE  
1818 N NZ  . LYS A 224 ? 1.1573 1.4626 1.2114 -0.0471 0.1466  -0.2140 268 LYS A NZ  
1819 N N   . ARG A 225 ? 1.0930 1.3154 1.1156 -0.0594 0.0807  -0.1396 269 ARG A N   
1820 C CA  . ARG A 225 ? 1.0817 1.3119 1.0960 -0.0591 0.0710  -0.1195 269 ARG A CA  
1821 C C   . ARG A 225 ? 1.0659 1.3057 1.0783 -0.0645 0.0626  -0.1198 269 ARG A C   
1822 O O   . ARG A 225 ? 1.0444 1.2929 1.0538 -0.0612 0.0536  -0.1046 269 ARG A O   
1823 C CB  . ARG A 225 ? 1.0754 1.2884 1.1019 -0.0486 0.0689  -0.1047 269 ARG A CB  
1824 C CG  . ARG A 225 ? 1.0885 1.2960 1.1221 -0.0442 0.0761  -0.1060 269 ARG A CG  
1825 C CD  . ARG A 225 ? 1.0849 1.2824 1.1212 -0.0388 0.0725  -0.0898 269 ARG A CD  
1826 N NE  . ARG A 225 ? 1.0958 1.2979 1.1143 -0.0430 0.0684  -0.0761 269 ARG A NE  
1827 C CZ  . ARG A 225 ? 1.0976 1.2871 1.1129 -0.0381 0.0619  -0.0617 269 ARG A CZ  
1828 N NH1 . ARG A 225 ? 1.0863 1.2621 1.1142 -0.0306 0.0601  -0.0599 269 ARG A NH1 
1829 N NH2 . ARG A 225 ? 1.1190 1.3079 1.1164 -0.0403 0.0575  -0.0489 269 ARG A NH2 
1830 N N   . ASN A 226 ? 1.0760 1.3144 1.0914 -0.0728 0.0656  -0.1382 270 ASN A N   
1831 C CA  . ASN A 226 ? 1.0827 1.3353 1.0981 -0.0825 0.0585  -0.1424 270 ASN A CA  
1832 C C   . ASN A 226 ? 1.0729 1.3161 1.1056 -0.0773 0.0549  -0.1314 270 ASN A C   
1833 O O   . ASN A 226 ? 1.0671 1.3317 1.1029 -0.0782 0.0465  -0.1232 270 ASN A O   
1834 C CB  . ASN A 226 ? 1.0870 1.3727 1.0848 -0.0877 0.0488  -0.1359 270 ASN A CB  
1835 C CG  . ASN A 226 ? 1.0994 1.4083 1.0946 -0.1023 0.0425  -0.1486 270 ASN A CG  
1836 O OD1 . ASN A 226 ? 1.1002 1.4328 1.1007 -0.1020 0.0313  -0.1387 270 ASN A OD1 
1837 N ND2 . ASN A 226 ? 1.1212 1.4251 1.1095 -0.1153 0.0495  -0.1719 270 ASN A ND2 
1838 N N   . ILE A 227 ? 1.0654 1.2792 1.1093 -0.0712 0.0615  -0.1315 271 ILE A N   
1839 C CA  . ILE A 227 ? 1.0448 1.2472 1.1012 -0.0672 0.0604  -0.1212 271 ILE A CA  
1840 C C   . ILE A 227 ? 1.0584 1.2319 1.1210 -0.0731 0.0667  -0.1314 271 ILE A C   
1841 O O   . ILE A 227 ? 1.0710 1.2245 1.1320 -0.0704 0.0724  -0.1416 271 ILE A O   
1842 C CB  . ILE A 227 ? 1.0280 1.2211 1.0866 -0.0527 0.0599  -0.1055 271 ILE A CB  
1843 C CG1 . ILE A 227 ? 1.0201 1.2332 1.0707 -0.0473 0.0534  -0.0937 271 ILE A CG1 
1844 C CG2 . ILE A 227 ? 1.0260 1.2045 1.0943 -0.0492 0.0608  -0.0975 271 ILE A CG2 
1845 C CD1 . ILE A 227 ? 1.0083 1.2078 1.0581 -0.0361 0.0536  -0.0807 271 ILE A CD1 
1846 N N   . GLN A 228 ? 1.0546 1.2257 1.1240 -0.0810 0.0662  -0.1283 272 GLN A N   
1847 C CA  . GLN A 228 ? 1.0659 1.2043 1.1375 -0.0893 0.0718  -0.1344 272 GLN A CA  
1848 C C   . GLN A 228 ? 1.0595 1.1676 1.1332 -0.0751 0.0741  -0.1231 272 GLN A C   
1849 O O   . GLN A 228 ? 1.0456 1.1631 1.1211 -0.0639 0.0714  -0.1097 272 GLN A O   
1850 C CB  . GLN A 228 ? 1.0682 1.2188 1.1451 -0.1053 0.0712  -0.1327 272 GLN A CB  
1851 C CG  . GLN A 228 ? 1.0969 1.2107 1.1720 -0.1199 0.0774  -0.1387 272 GLN A CG  
1852 C CD  . GLN A 228 ? 1.1001 1.2340 1.1807 -0.1417 0.0780  -0.1401 272 GLN A CD  
1853 O OE1 . GLN A 228 ? 1.0826 1.2446 1.1714 -0.1401 0.0766  -0.1288 272 GLN A OE1 
1854 N NE2 . GLN A 228 ? 1.1322 1.2536 1.2090 -0.1632 0.0808  -0.1558 272 GLN A NE2 
1855 N N   . PHE A 229 ? 1.0804 1.1511 1.1532 -0.0754 0.0784  -0.1288 273 PHE A N   
1856 C CA  . PHE A 229 ? 1.0851 1.1276 1.1595 -0.0615 0.0784  -0.1173 273 PHE A CA  
1857 C C   . PHE A 229 ? 1.1214 1.1256 1.1914 -0.0709 0.0810  -0.1139 273 PHE A C   
1858 O O   . PHE A 229 ? 1.1488 1.1223 1.2164 -0.0752 0.0845  -0.1256 273 PHE A O   
1859 C CB  . PHE A 229 ? 1.0835 1.1167 1.1619 -0.0457 0.0797  -0.1251 273 PHE A CB  
1860 C CG  . PHE A 229 ? 1.0881 1.0973 1.1708 -0.0297 0.0775  -0.1136 273 PHE A CG  
1861 C CD1 . PHE A 229 ? 1.0647 1.0879 1.1483 -0.0220 0.0726  -0.0978 273 PHE A CD1 
1862 C CD2 . PHE A 229 ? 1.1237 1.0951 1.2086 -0.0222 0.0792  -0.1186 273 PHE A CD2 
1863 C CE1 . PHE A 229 ? 1.0723 1.0783 1.1586 -0.0085 0.0685  -0.0872 273 PHE A CE1 
1864 C CE2 . PHE A 229 ? 1.1331 1.0856 1.2221 -0.0055 0.0745  -0.1059 273 PHE A CE2 
1865 C CZ  . PHE A 229 ? 1.1058 1.0784 1.1952 0.0004  0.0686  -0.0901 273 PHE A CZ  
1866 N N   . SER A 230 ? 1.1277 1.1323 1.1948 -0.0747 0.0801  -0.0980 274 SER A N   
1867 C CA  . SER A 230 ? 1.1751 1.1410 1.2337 -0.0826 0.0824  -0.0887 274 SER A CA  
1868 C C   . SER A 230 ? 1.1901 1.1308 1.2458 -0.0627 0.0781  -0.0754 274 SER A C   
1869 O O   . SER A 230 ? 1.1598 1.1210 1.2218 -0.0463 0.0739  -0.0733 274 SER A O   
1870 C CB  . SER A 230 ? 1.1751 1.1593 1.2305 -0.0992 0.0851  -0.0795 274 SER A CB  
1871 O OG  . SER A 230 ? 1.2128 1.1585 1.2558 -0.1100 0.0883  -0.0684 274 SER A OG  
1872 N N   . CYS A 231 ? 1.2432 1.1393 1.2885 -0.0655 0.0784  -0.0658 275 CYS A N   
1873 C CA  . CYS A 231 ? 1.2642 1.1366 1.3054 -0.0465 0.0719  -0.0508 275 CYS A CA  
1874 C C   . CYS A 231 ? 1.3185 1.1466 1.3410 -0.0570 0.0724  -0.0341 275 CYS A C   
1875 O O   . CYS A 231 ? 1.3623 1.1541 1.3785 -0.0709 0.0772  -0.0392 275 CYS A O   
1876 C CB  . CYS A 231 ? 1.2762 1.1327 1.3291 -0.0254 0.0691  -0.0613 275 CYS A CB  
1877 S SG  . CYS A 231 ? 1.3002 1.1468 1.3557 0.0022  0.0580  -0.0441 275 CYS A SG  
1878 N N   . LYS A 232 ? 1.3300 1.1600 1.3411 -0.0523 0.0675  -0.0144 276 LYS A N   
1879 C CA  . LYS A 232 ? 1.3825 1.1733 1.3705 -0.0634 0.0677  0.0053  276 LYS A CA  
1880 C C   . LYS A 232 ? 1.4078 1.1805 1.3873 -0.0413 0.0559  0.0239  276 LYS A C   
1881 O O   . LYS A 232 ? 1.3754 1.1794 1.3670 -0.0226 0.0489  0.0218  276 LYS A O   
1882 C CB  . LYS A 232 ? 1.3655 1.1845 1.3424 -0.0863 0.0751  0.0119  276 LYS A CB  
1883 C CG  . LYS A 232 ? 1.3542 1.1894 1.3380 -0.1116 0.0858  -0.0024 276 LYS A CG  
1884 C CD  . LYS A 232 ? 1.3451 1.2119 1.3211 -0.1325 0.0940  0.0039  276 LYS A CD  
1885 C CE  . LYS A 232 ? 1.3952 1.2254 1.3436 -0.1489 0.0976  0.0248  276 LYS A CE  
1886 N NZ  . LYS A 232 ? 1.3838 1.2529 1.3260 -0.1686 0.1078  0.0288  276 LYS A NZ  
1887 N N   . ASN A 233 ? 1.4746 1.1968 1.4321 -0.0454 0.0533  0.0430  277 ASN A N   
1888 C CA  . ASN A 233 ? 1.5120 1.2141 1.4573 -0.0255 0.0400  0.0645  277 ASN A CA  
1889 C C   . ASN A 233 ? 1.5416 1.2503 1.4576 -0.0419 0.0403  0.0858  277 ASN A C   
1890 O O   . ASN A 233 ? 1.5785 1.2660 1.4746 -0.0678 0.0498  0.0933  277 ASN A O   
1891 C CB  . ASN A 233 ? 1.5726 1.2073 1.5109 -0.0141 0.0346  0.0737  277 ASN A CB  
1892 C CG  . ASN A 233 ? 1.5607 1.1883 1.5272 0.0049  0.0351  0.0506  277 ASN A CG  
1893 O OD1 . ASN A 233 ? 1.5223 1.1825 1.5114 0.0296  0.0282  0.0424  277 ASN A OD1 
1894 N ND2 . ASN A 233 ? 1.5920 1.1785 1.5567 -0.0081 0.0442  0.0388  277 ASN A ND2 
1895 N N   . ILE A 234 ? 1.5357 1.2759 1.4485 -0.0284 0.0307  0.0940  278 ILE A N   
1896 C CA  . ILE A 234 ? 1.5663 1.3124 1.4478 -0.0408 0.0295  0.1138  278 ILE A CA  
1897 C C   . ILE A 234 ? 1.6321 1.3418 1.4938 -0.0237 0.0128  0.1394  278 ILE A C   
1898 O O   . ILE A 234 ? 1.6126 1.3460 1.4807 -0.0027 -0.0011 0.1426  278 ILE A O   
1899 C CB  . ILE A 234 ? 1.5103 1.3161 1.3977 -0.0406 0.0307  0.1035  278 ILE A CB  
1900 C CG1 . ILE A 234 ? 1.4602 1.3005 1.3701 -0.0516 0.0446  0.0794  278 ILE A CG1 
1901 C CG2 . ILE A 234 ? 1.5290 1.3422 1.3815 -0.0544 0.0313  0.1208  278 ILE A CG2 
1902 C CD1 . ILE A 234 ? 1.4711 1.3046 1.3716 -0.0792 0.0598  0.0786  278 ILE A CD1 
1903 N N   . TYR A 235 ? 1.7107 1.3623 1.5478 -0.0337 0.0138  0.1582  279 TYR A N   
1904 C CA  . TYR A 235 ? 1.7780 1.3840 1.5951 -0.0157 -0.0030 0.1852  279 TYR A CA  
1905 C C   . TYR A 235 ? 1.8004 1.4247 1.5829 -0.0210 -0.0115 0.2083  279 TYR A C   
1906 O O   . TYR A 235 ? 1.8133 1.4367 1.5903 0.0024  -0.0309 0.2240  279 TYR A O   
1907 C CB  . TYR A 235 ? 1.8485 1.3792 1.6469 -0.0272 0.0017  0.1983  279 TYR A CB  
1908 C CG  . TYR A 235 ? 1.8448 1.3494 1.6740 -0.0180 0.0071  0.1757  279 TYR A CG  
1909 C CD1 . TYR A 235 ? 1.8365 1.3396 1.6950 0.0184  -0.0048 0.1665  279 TYR A CD1 
1910 C CD2 . TYR A 235 ? 1.8483 1.3337 1.6776 -0.0465 0.0245  0.1616  279 TYR A CD2 
1911 C CE1 . TYR A 235 ? 1.8343 1.3149 1.7190 0.0268  0.0016  0.1432  279 TYR A CE1 
1912 C CE2 . TYR A 235 ? 1.8498 1.3118 1.7039 -0.0399 0.0295  0.1386  279 TYR A CE2 
1913 C CZ  . TYR A 235 ? 1.8442 1.3024 1.7248 -0.0028 0.0186  0.1290  279 TYR A CZ  
1914 O OH  . TYR A 235 ? 1.8503 1.2866 1.7534 0.0037  0.0250  0.1039  279 TYR A OH  
1915 N N   . ARG A 236 ? 1.8061 1.4500 1.5656 -0.0519 0.0031  0.2091  280 ARG A N   
1916 C CA  . ARG A 236 ? 1.8300 1.4968 1.5540 -0.0610 -0.0010 0.2262  280 ARG A CA  
1917 C C   . ARG A 236 ? 1.7694 1.5039 1.5076 -0.0682 0.0086  0.2020  280 ARG A C   
1918 O O   . ARG A 236 ? 1.7509 1.5039 1.4888 -0.0919 0.0278  0.1899  280 ARG A O   
1919 C CB  . ARG A 236 ? 1.8960 1.5252 1.5749 -0.0917 0.0092  0.2498  280 ARG A CB  
1920 C CG  . ARG A 236 ? 1.9780 1.5361 1.6275 -0.0837 -0.0051 0.2832  280 ARG A CG  
1921 C CD  . ARG A 236 ? 1.9910 1.5531 1.6324 -0.0524 -0.0316 0.3013  280 ARG A CD  
1922 N NE  . ARG A 236 ? 1.9608 1.5801 1.5837 -0.0581 -0.0348 0.3012  280 ARG A NE  
1923 C CZ  . ARG A 236 ? 1.9392 1.5896 1.5662 -0.0339 -0.0557 0.3044  280 ARG A CZ  
1924 N NH1 . ARG A 236 ? 1.9440 1.5780 1.5954 -0.0002 -0.0757 0.3096  280 ARG A NH1 
1925 N NH2 . ARG A 236 ? 1.9147 1.6149 1.5223 -0.0438 -0.0562 0.3007  280 ARG A NH2 
1926 N N   . PRO A 237 ? 1.7420 1.5149 1.4943 -0.0477 -0.0043 0.1937  281 PRO A N   
1927 C CA  . PRO A 237 ? 1.6900 1.5189 1.4509 -0.0539 0.0035  0.1722  281 PRO A CA  
1928 C C   . PRO A 237 ? 1.7159 1.5617 1.4371 -0.0768 0.0128  0.1796  281 PRO A C   
1929 O O   . PRO A 237 ? 1.6816 1.5601 1.4087 -0.0903 0.0294  0.1607  281 PRO A O   
1930 C CB  . PRO A 237 ? 1.6658 1.5212 1.4425 -0.0294 -0.0155 0.1680  281 PRO A CB  
1931 C CG  . PRO A 237 ? 1.6845 1.5058 1.4789 -0.0062 -0.0299 0.1785  281 PRO A CG  
1932 C CD  . PRO A 237 ? 1.7514 1.5166 1.5153 -0.0175 -0.0272 0.2029  281 PRO A CD  
1933 N N   . ASP A 238 ? 1.7857 1.6102 1.4660 -0.0798 0.0017  0.2071  282 ASP A N   
1934 C CA  . ASP A 238 ? 1.8130 1.6554 1.4497 -0.1010 0.0090  0.2152  282 ASP A CA  
1935 C C   . ASP A 238 ? 1.8324 1.6676 1.4569 -0.1304 0.0338  0.2144  282 ASP A C   
1936 O O   . ASP A 238 ? 1.8112 1.6832 1.4252 -0.1470 0.0502  0.2011  282 ASP A O   
1937 C CB  . ASP A 238 ? 1.8756 1.6943 1.4682 -0.0975 -0.0105 0.2481  282 ASP A CB  
1938 C CG  . ASP A 238 ? 1.8635 1.7001 1.4685 -0.0699 -0.0364 0.2488  282 ASP A CG  
1939 O OD1 . ASP A 238 ? 1.8438 1.6668 1.4857 -0.0463 -0.0475 0.2461  282 ASP A OD1 
1940 O OD2 . ASP A 238 ? 1.8710 1.7384 1.4493 -0.0732 -0.0445 0.2504  282 ASP A OD2 
1941 N N   . LYS A 239 ? 1.8711 1.6598 1.4979 -0.1369 0.0369  0.2273  283 LYS A N   
1942 C CA  . LYS A 239 ? 1.8933 1.6745 1.5113 -0.1677 0.0598  0.2270  283 LYS A CA  
1943 C C   . LYS A 239 ? 1.8310 1.6519 1.4942 -0.1701 0.0759  0.1935  283 LYS A C   
1944 O O   . LYS A 239 ? 1.8336 1.6787 1.4950 -0.1943 0.0965  0.1848  283 LYS A O   
1945 C CB  . LYS A 239 ? 1.9497 1.6636 1.5562 -0.1749 0.0568  0.2498  283 LYS A CB  
1946 C CG  . LYS A 239 ? 2.0246 1.6917 1.5827 -0.1729 0.0405  0.2877  283 LYS A CG  
1947 C CD  . LYS A 239 ? 2.0894 1.6820 1.6316 -0.1833 0.0403  0.3109  283 LYS A CD  
1948 C CE  . LYS A 239 ? 2.1712 1.7130 1.6641 -0.1775 0.0215  0.3516  283 LYS A CE  
1949 N NZ  . LYS A 239 ? 2.2455 1.7054 1.7214 -0.1877 0.0219  0.3745  283 LYS A NZ  
1950 N N   . PHE A 240 ? 1.7800 1.6100 1.4835 -0.1448 0.0661  0.1757  284 PHE A N   
1951 C CA  . PHE A 240 ? 1.7220 1.5880 1.4665 -0.1436 0.0777  0.1462  284 PHE A CA  
1952 C C   . PHE A 240 ? 1.6955 1.6155 1.4393 -0.1466 0.0877  0.1294  284 PHE A C   
1953 O O   . PHE A 240 ? 1.6616 1.6129 1.4232 -0.1577 0.1044  0.1121  284 PHE A O   
1954 C CB  . PHE A 240 ? 1.6841 1.5452 1.4652 -0.1166 0.0643  0.1340  284 PHE A CB  
1955 C CG  . PHE A 240 ? 1.6293 1.5248 1.4492 -0.1139 0.0736  0.1064  284 PHE A CG  
1956 C CD1 . PHE A 240 ? 1.6280 1.5249 1.4617 -0.1317 0.0877  0.0977  284 PHE A CD1 
1957 C CD2 . PHE A 240 ? 1.5844 1.5110 1.4257 -0.0950 0.0675  0.0901  284 PHE A CD2 
1958 C CE1 . PHE A 240 ? 1.5764 1.5072 1.4440 -0.1280 0.0939  0.0744  284 PHE A CE1 
1959 C CE2 . PHE A 240 ? 1.5401 1.4947 1.4132 -0.0921 0.0749  0.0681  284 PHE A CE2 
1960 C CZ  . PHE A 240 ? 1.5362 1.4939 1.4222 -0.1073 0.0872  0.0608  284 PHE A CZ  
1961 N N   . LEU A 241 ? 1.7136 1.6447 1.4375 -0.1359 0.0769  0.1335  285 LEU A N   
1962 C CA  . LEU A 241 ? 1.7081 1.6833 1.4259 -0.1383 0.0859  0.1167  285 LEU A CA  
1963 C C   . LEU A 241 ? 1.7537 1.7424 1.4412 -0.1650 0.1054  0.1217  285 LEU A C   
1964 O O   . LEU A 241 ? 1.7342 1.7622 1.4314 -0.1707 0.1221  0.1014  285 LEU A O   
1965 C CB  . LEU A 241 ? 1.7173 1.6969 1.4164 -0.1242 0.0683  0.1208  285 LEU A CB  
1966 C CG  . LEU A 241 ? 1.6785 1.6618 1.4109 -0.0998 0.0527  0.1091  285 LEU A CG  
1967 C CD1 . LEU A 241 ? 1.6870 1.6826 1.3995 -0.0914 0.0366  0.1114  285 LEU A CD1 
1968 C CD2 . LEU A 241 ? 1.6241 1.6338 1.3934 -0.0947 0.0641  0.0817  285 LEU A CD2 
1969 N N   . GLN A 242 ? 1.8224 1.7782 1.4730 -0.1807 0.1034  0.1491  286 GLN A N   
1970 C CA  . GLN A 242 ? 1.8656 1.8323 1.4815 -0.2098 0.1222  0.1575  286 GLN A CA  
1971 C C   . GLN A 242 ? 1.8596 1.8341 1.5005 -0.2290 0.1419  0.1491  286 GLN A C   
1972 O O   . GLN A 242 ? 1.8609 1.8680 1.4924 -0.2512 0.1632  0.1429  286 GLN A O   
1973 C CB  . GLN A 242 ? 1.9394 1.8636 1.5038 -0.2204 0.1113  0.1930  286 GLN A CB  
1974 C CG  . GLN A 242 ? 1.9944 1.9403 1.5085 -0.2433 0.1239  0.2011  286 GLN A CG  
1975 C CD  . GLN A 242 ? 2.0245 1.9868 1.5329 -0.2758 0.1518  0.1991  286 GLN A CD  
1976 O OE1 . GLN A 242 ? 2.0698 1.9949 1.5673 -0.2952 0.1557  0.2196  286 GLN A OE1 
1977 N NE2 . GLN A 242 ? 2.0049 2.0236 1.5209 -0.2826 0.1722  0.1735  286 GLN A NE2 
1978 N N   . CYS A 243 ? 1.8500 1.7985 1.5236 -0.2207 0.1347  0.1474  287 CYS A N   
1979 C CA  . CYS A 243 ? 1.8418 1.7989 1.5431 -0.2379 0.1499  0.1369  287 CYS A CA  
1980 C C   . CYS A 243 ? 1.7919 1.8117 1.5293 -0.2330 0.1634  0.1063  287 CYS A C   
1981 O O   . CYS A 243 ? 1.7867 1.8409 1.5298 -0.2547 0.1832  0.0984  287 CYS A O   
1982 C CB  . CYS A 243 ? 1.8298 1.7453 1.5562 -0.2271 0.1373  0.1384  287 CYS A CB  
1983 S SG  . CYS A 243 ? 1.7776 1.7172 1.5484 -0.2418 0.1517  0.1158  287 CYS A SG  
1984 N N   . VAL A 244 ? 1.7436 1.7781 1.5059 -0.2042 0.1525  0.0899  288 VAL A N   
1985 C CA  . VAL A 244 ? 1.6883 1.7731 1.4858 -0.1941 0.1618  0.0626  288 VAL A CA  
1986 C C   . VAL A 244 ? 1.6957 1.8213 1.4755 -0.2009 0.1777  0.0537  288 VAL A C   
1987 O O   . VAL A 244 ? 1.6590 1.8303 1.4648 -0.1994 0.1916  0.0331  288 VAL A O   
1988 C CB  . VAL A 244 ? 1.6388 1.7213 1.4617 -0.1638 0.1459  0.0502  288 VAL A CB  
1989 C CG1 . VAL A 244 ? 1.6253 1.6770 1.4702 -0.1574 0.1341  0.0537  288 VAL A CG1 
1990 C CG2 . VAL A 244 ? 1.6469 1.7164 1.4446 -0.1497 0.1328  0.0560  288 VAL A CG2 
1991 N N   . LYS A 245 ? 1.7423 1.8526 1.4777 -0.2070 0.1750  0.0685  289 LYS A N   
1992 C CA  . LYS A 245 ? 1.7664 1.9124 1.4768 -0.2176 0.1918  0.0608  289 LYS A CA  
1993 C C   . LYS A 245 ? 1.8069 1.9771 1.5154 -0.2478 0.2147  0.0632  289 LYS A C   
1994 O O   . LYS A 245 ? 1.8030 2.0248 1.5317 -0.2501 0.2336  0.0419  289 LYS A O   
1995 C CB  . LYS A 245 ? 1.7997 1.9216 1.4589 -0.2194 0.1809  0.0784  289 LYS A CB  
1996 C CG  . LYS A 245 ? 1.8117 1.9692 1.4434 -0.2232 0.1940  0.0644  289 LYS A CG  
1997 C CD  . LYS A 245 ? 1.8546 2.0355 1.4569 -0.2538 0.2178  0.0704  289 LYS A CD  
1998 C CE  . LYS A 245 ? 1.8741 2.0856 1.4404 -0.2578 0.2296  0.0576  289 LYS A CE  
1999 N NZ  . LYS A 245 ? 1.9201 2.1557 1.4539 -0.2902 0.2539  0.0652  289 LYS A NZ  
2000 N N   . ASN A 246 ? 1.8550 1.9873 1.5403 -0.2705 0.2129  0.0891  290 ASN A N   
2001 C CA  . ASN A 246 ? 1.8847 2.0324 1.5702 -0.3037 0.2330  0.0937  290 ASN A CA  
2002 C C   . ASN A 246 ? 1.9327 2.0168 1.5977 -0.3212 0.2232  0.1228  290 ASN A C   
2003 O O   . ASN A 246 ? 1.9918 2.0413 1.6064 -0.3352 0.2203  0.1489  290 ASN A O   
2004 C CB  . ASN A 246 ? 1.9220 2.1083 1.5741 -0.3268 0.2558  0.0932  290 ASN A CB  
2005 C CG  . ASN A 246 ? 1.8790 2.1385 1.5668 -0.3200 0.2758  0.0603  290 ASN A CG  
2006 O OD1 . ASN A 246 ? 1.8476 2.1404 1.5780 -0.3256 0.2857  0.0467  290 ASN A OD1 
2007 N ND2 . ASN A 246 ? 1.8777 2.1629 1.5486 -0.3071 0.2812  0.0464  290 ASN A ND2 
2008 N N   . GLN B 1   ? 1.3427 1.0634 1.4563 0.0404  0.0117  0.1340  1   GLN H N   
2009 C CA  . GLN B 1   ? 1.3481 1.0442 1.4471 0.0180  0.0320  0.1346  1   GLN H CA  
2010 C C   . GLN B 1   ? 1.2794 1.0107 1.3771 -0.0020 0.0381  0.1169  1   GLN H C   
2011 O O   . GLN B 1   ? 1.2469 0.9756 1.3558 -0.0199 0.0511  0.1032  1   GLN H O   
2012 C CB  . GLN B 1   ? 1.4058 1.0727 1.4676 0.0171  0.0342  0.1620  1   GLN H CB  
2013 C CG  . GLN B 1   ? 1.4640 1.0970 1.5206 0.0403  0.0240  0.1860  1   GLN H CG  
2014 C CD  . GLN B 1   ? 1.5005 1.0931 1.5841 0.0454  0.0366  0.1840  1   GLN H CD  
2015 O OE1 . GLN B 1   ? 1.4967 1.0838 1.5987 0.0283  0.0536  0.1630  1   GLN H OE1 
2016 N NE2 . GLN B 1   ? 1.5512 1.1132 1.6360 0.0690  0.0283  0.2067  1   GLN H NE2 
2017 N N   . VAL B 2   ? 1.2475 1.0105 1.3303 0.0008  0.0284  0.1179  2   VAL H N   
2018 C CA  . VAL B 2   ? 1.2098 1.0050 1.2920 -0.0138 0.0344  0.1047  2   VAL H CA  
2019 C C   . VAL B 2   ? 1.1693 0.9873 1.2796 -0.0139 0.0323  0.0813  2   VAL H C   
2020 O O   . VAL B 2   ? 1.1666 0.9894 1.2924 0.0006  0.0226  0.0750  2   VAL H O   
2021 C CB  . VAL B 2   ? 1.2058 1.0203 1.2609 -0.0108 0.0288  0.1122  2   VAL H CB  
2022 C CG1 . VAL B 2   ? 1.2060 1.0359 1.2610 0.0061  0.0100  0.1097  2   VAL H CG1 
2023 C CG2 . VAL B 2   ? 1.1709 1.0140 1.2284 -0.0241 0.0389  0.1012  2   VAL H CG2 
2024 N N   . GLN B 3   ? 1.1365 0.9693 1.2535 -0.0308 0.0416  0.0694  3   GLN H N   
2025 C CA  . GLN B 3   ? 1.0994 0.9500 1.2349 -0.0344 0.0418  0.0485  3   GLN H CA  
2026 C C   . GLN B 3   ? 1.0582 0.9377 1.1903 -0.0465 0.0455  0.0440  3   GLN H C   
2027 O O   . GLN B 3   ? 1.0671 0.9481 1.1964 -0.0605 0.0522  0.0504  3   GLN H O   
2028 C CB  . GLN B 3   ? 1.1224 0.9496 1.2710 -0.0442 0.0499  0.0379  3   GLN H CB  
2029 C CG  . GLN B 3   ? 1.1653 0.9642 1.3266 -0.0288 0.0492  0.0386  3   GLN H CG  
2030 C CD  . GLN B 3   ? 1.1933 0.9661 1.3658 -0.0402 0.0618  0.0235  3   GLN H CD  
2031 O OE1 . GLN B 3   ? 1.1877 0.9719 1.3651 -0.0509 0.0661  0.0043  3   GLN H OE1 
2032 N NE2 . GLN B 3   ? 1.2386 0.9721 1.4114 -0.0391 0.0694  0.0322  3   GLN H NE2 
2033 N N   . LEU B 4   ? 1.0118 0.9143 1.1471 -0.0409 0.0417  0.0335  4   LEU H N   
2034 C CA  . LEU B 4   ? 0.9778 0.9052 1.1123 -0.0489 0.0456  0.0301  4   LEU H CA  
2035 C C   . LEU B 4   ? 0.9480 0.8805 1.0926 -0.0568 0.0466  0.0138  4   LEU H C   
2036 O O   . LEU B 4   ? 0.9389 0.8674 1.0898 -0.0503 0.0452  0.0012  4   LEU H O   
2037 C CB  . LEU B 4   ? 0.9744 0.9174 1.0997 -0.0384 0.0437  0.0303  4   LEU H CB  
2038 C CG  . LEU B 4   ? 0.9950 0.9303 1.1013 -0.0317 0.0422  0.0444  4   LEU H CG  
2039 C CD1 . LEU B 4   ? 0.9821 0.9323 1.0754 -0.0267 0.0435  0.0412  4   LEU H CD1 
2040 C CD2 . LEU B 4   ? 1.0122 0.9400 1.1119 -0.0408 0.0511  0.0592  4   LEU H CD2 
2041 N N   . VAL B 5   ? 0.9289 0.8713 1.0748 -0.0717 0.0491  0.0147  5   VAL H N   
2042 C CA  . VAL B 5   ? 0.9274 0.8731 1.0742 -0.0826 0.0489  0.0012  5   VAL H CA  
2043 C C   . VAL B 5   ? 0.9113 0.8846 1.0570 -0.0852 0.0477  0.0058  5   VAL H C   
2044 O O   . VAL B 5   ? 0.9076 0.8968 1.0590 -0.0923 0.0468  0.0177  5   VAL H O   
2045 C CB  . VAL B 5   ? 0.9501 0.8800 1.0970 -0.1008 0.0502  -0.0026 5   VAL H CB  
2046 C CG1 . VAL B 5   ? 0.9512 0.8863 1.0906 -0.1166 0.0487  -0.0154 5   VAL H CG1 
2047 C CG2 . VAL B 5   ? 0.9785 0.8750 1.1281 -0.0958 0.0546  -0.0076 5   VAL H CG2 
2048 N N   . GLN B 6   ? 0.9031 0.8814 1.0443 -0.0791 0.0488  -0.0030 6   GLN H N   
2049 C CA  . GLN B 6   ? 0.8860 0.8848 1.0253 -0.0778 0.0493  0.0026  6   GLN H CA  
2050 C C   . GLN B 6   ? 0.8916 0.8954 1.0238 -0.0925 0.0446  -0.0009 6   GLN H C   
2051 O O   . GLN B 6   ? 0.9097 0.8979 1.0348 -0.1045 0.0435  -0.0124 6   GLN H O   
2052 C CB  . GLN B 6   ? 0.8710 0.8682 1.0057 -0.0655 0.0548  -0.0048 6   GLN H CB  
2053 C CG  . GLN B 6   ? 0.8638 0.8593 0.9999 -0.0533 0.0570  -0.0014 6   GLN H CG  
2054 C CD  . GLN B 6   ? 0.8620 0.8573 0.9942 -0.0454 0.0618  -0.0118 6   GLN H CD  
2055 O OE1 . GLN B 6   ? 0.8737 0.8637 1.0084 -0.0400 0.0593  -0.0203 6   GLN H OE1 
2056 N NE2 . GLN B 6   ? 0.8582 0.8600 0.9858 -0.0450 0.0684  -0.0107 6   GLN H NE2 
2057 N N   . SER B 7   ? 0.8730 0.8970 1.0055 -0.0913 0.0424  0.0095  7   SER H N   
2058 C CA  . SER B 7   ? 0.8852 0.9165 1.0062 -0.1042 0.0348  0.0095  7   SER H CA  
2059 C C   . SER B 7   ? 0.8935 0.9060 0.9935 -0.1038 0.0409  -0.0052 7   SER H C   
2060 O O   . SER B 7   ? 0.8753 0.8762 0.9769 -0.0922 0.0506  -0.0137 7   SER H O   
2061 C CB  . SER B 7   ? 0.8771 0.9374 1.0096 -0.1000 0.0293  0.0293  7   SER H CB  
2062 O OG  . SER B 7   ? 0.8700 0.9305 1.0060 -0.0814 0.0397  0.0347  7   SER H OG  
2063 N N   . GLY B 8   ? 0.9200 0.9305 0.9993 -0.1184 0.0350  -0.0083 8   GLY H N   
2064 C CA  . GLY B 8   ? 0.9456 0.9346 1.0005 -0.1224 0.0435  -0.0236 8   GLY H CA  
2065 C C   . GLY B 8   ? 0.9401 0.9314 0.9885 -0.1099 0.0498  -0.0162 8   GLY H C   
2066 O O   . GLY B 8   ? 0.9232 0.9333 0.9839 -0.0990 0.0460  0.0023  8   GLY H O   
2067 N N   . ALA B 9   ? 0.9732 0.9428 1.0034 -0.1119 0.0622  -0.0316 9   ALA H N   
2068 C CA  . ALA B 9   ? 0.9943 0.9582 1.0136 -0.1035 0.0718  -0.0273 9   ALA H CA  
2069 C C   . ALA B 9   ? 1.0293 0.9987 1.0239 -0.1096 0.0618  -0.0097 9   ALA H C   
2070 O O   . ALA B 9   ? 1.0626 1.0353 1.0401 -0.1257 0.0491  -0.0087 9   ALA H O   
2071 C CB  . ALA B 9   ? 1.0058 0.9458 1.0145 -0.1075 0.0892  -0.0499 9   ALA H CB  
2072 N N   . GLU B 10  ? 1.0478 1.0171 1.0399 -0.0970 0.0674  0.0043  10  GLU H N   
2073 C CA  . GLU B 10  ? 1.0797 1.0549 1.0513 -0.0980 0.0568  0.0261  10  GLU H CA  
2074 C C   . GLU B 10  ? 1.0743 1.0328 1.0373 -0.0842 0.0725  0.0347  10  GLU H C   
2075 O O   . GLU B 10  ? 1.0365 0.9865 1.0166 -0.0733 0.0893  0.0259  10  GLU H O   
2076 C CB  . GLU B 10  ? 1.0782 1.0892 1.0763 -0.0930 0.0371  0.0486  10  GLU H CB  
2077 C CG  . GLU B 10  ? 1.0586 1.0837 1.0959 -0.0731 0.0450  0.0570  10  GLU H CG  
2078 C CD  . GLU B 10  ? 1.0709 1.1325 1.1405 -0.0703 0.0295  0.0755  10  GLU H CD  
2079 O OE1 . GLU B 10  ? 1.0604 1.1304 1.1549 -0.0678 0.0331  0.0699  10  GLU H OE1 
2080 O OE2 . GLU B 10  ? 1.1033 1.1860 1.1735 -0.0711 0.0136  0.0961  10  GLU H OE2 
2081 N N   . VAL B 11  ? 1.0991 1.0515 1.0328 -0.0860 0.0663  0.0524  11  VAL H N   
2082 C CA  . VAL B 11  ? 1.1196 1.0515 1.0412 -0.0729 0.0812  0.0651  11  VAL H CA  
2083 C C   . VAL B 11  ? 1.1139 1.0698 1.0637 -0.0527 0.0717  0.0959  11  VAL H C   
2084 O O   . VAL B 11  ? 1.1123 1.1013 1.0776 -0.0539 0.0486  0.1115  11  VAL H O   
2085 C CB  . VAL B 11  ? 1.1658 1.0703 1.0342 -0.0859 0.0828  0.0680  11  VAL H CB  
2086 C CG1 . VAL B 11  ? 1.1940 1.1183 1.0420 -0.0926 0.0539  0.0921  11  VAL H CG1 
2087 C CG2 . VAL B 11  ? 1.1878 1.0604 1.0408 -0.0745 0.1053  0.0758  11  VAL H CG2 
2088 N N   . LYS B 12  ? 1.1195 1.0584 1.0783 -0.0351 0.0917  0.1033  12  LYS H N   
2089 C CA  . LYS B 12  ? 1.1243 1.0799 1.1126 -0.0129 0.0897  0.1318  12  LYS H CA  
2090 C C   . LYS B 12  ? 1.1649 1.0855 1.1341 0.0001  0.1092  0.1455  12  LYS H C   
2091 O O   . LYS B 12  ? 1.1808 1.0652 1.1269 -0.0060 0.1318  0.1264  12  LYS H O   
2092 C CB  . LYS B 12  ? 1.0850 1.0561 1.1162 -0.0024 0.0995  0.1239  12  LYS H CB  
2093 C CG  . LYS B 12  ? 1.0527 1.0602 1.1086 -0.0109 0.0802  0.1195  12  LYS H CG  
2094 C CD  . LYS B 12  ? 1.0605 1.1067 1.1377 -0.0070 0.0562  0.1472  12  LYS H CD  
2095 C CE  . LYS B 12  ? 1.0436 1.1221 1.1424 -0.0200 0.0392  0.1403  12  LYS H CE  
2096 N NZ  . LYS B 12  ? 1.0641 1.1847 1.1859 -0.0198 0.0142  0.1658  12  LYS H NZ  
2097 N N   . LYS B 13  ? 1.1953 1.1276 1.1779 0.0187  0.1011  0.1795  13  LYS H N   
2098 C CA  . LYS B 13  ? 1.2410 1.1379 1.2068 0.0343  0.1191  0.1985  13  LYS H CA  
2099 C C   . LYS B 13  ? 1.2218 1.1006 1.2168 0.0507  0.1504  0.1909  13  LYS H C   
2100 O O   . LYS B 13  ? 1.1846 1.0892 1.2183 0.0559  0.1509  0.1840  13  LYS H O   
2101 C CB  . LYS B 13  ? 1.2802 1.1985 1.2530 0.0503  0.0966  0.2406  13  LYS H CB  
2102 C CG  . LYS B 13  ? 1.3156 1.2457 1.2476 0.0326  0.0652  0.2513  13  LYS H CG  
2103 C CD  . LYS B 13  ? 1.2946 1.2661 1.2354 0.0112  0.0386  0.2358  13  LYS H CD  
2104 C CE  . LYS B 13  ? 1.2619 1.2877 1.2640 0.0234  0.0213  0.2509  13  LYS H CE  
2105 N NZ  . LYS B 13  ? 1.2250 1.2831 1.2336 0.0000  0.0009  0.2318  13  LYS H NZ  
2106 N N   . PRO B 14  ? 1.2464 1.0773 1.2205 0.0570  0.1793  0.1903  14  PRO H N   
2107 C CA  . PRO B 14  ? 1.2333 1.0429 1.2314 0.0713  0.2107  0.1837  14  PRO H CA  
2108 C C   . PRO B 14  ? 1.2285 1.0610 1.2711 0.0987  0.2088  0.2141  14  PRO H C   
2109 O O   . PRO B 14  ? 1.2582 1.0937 1.3029 0.1150  0.1984  0.2487  14  PRO H O   
2110 C CB  . PRO B 14  ? 1.2816 1.0333 1.2434 0.0710  0.2392  0.1829  14  PRO H CB  
2111 C CG  . PRO B 14  ? 1.2987 1.0419 1.2150 0.0494  0.2257  0.1761  14  PRO H CG  
2112 C CD  . PRO B 14  ? 1.2884 1.0793 1.2114 0.0480  0.1862  0.1939  14  PRO H CD  
2113 N N   . GLY B 15  ? 1.1907 1.0408 1.2693 0.1034  0.2185  0.2016  15  GLY H N   
2114 C CA  . GLY B 15  ? 1.1987 1.0701 1.3252 0.1287  0.2235  0.2258  15  GLY H CA  
2115 C C   . GLY B 15  ? 1.1649 1.0972 1.3276 0.1271  0.1934  0.2344  15  GLY H C   
2116 O O   . GLY B 15  ? 1.1532 1.1088 1.3615 0.1435  0.2005  0.2460  15  GLY H O   
2117 N N   . SER B 16  ? 1.1609 1.1165 1.3033 0.1062  0.1627  0.2276  16  SER H N   
2118 C CA  . SER B 16  ? 1.1352 1.1450 1.3072 0.0996  0.1343  0.2327  16  SER H CA  
2119 C C   . SER B 16  ? 1.1010 1.1178 1.2858 0.0890  0.1443  0.2043  16  SER H C   
2120 O O   . SER B 16  ? 1.0973 1.0802 1.2678 0.0873  0.1703  0.1823  16  SER H O   
2121 C CB  . SER B 16  ? 1.1400 1.1649 1.2809 0.0793  0.1016  0.2335  16  SER H CB  
2122 O OG  . SER B 16  ? 1.1257 1.1260 1.2281 0.0562  0.1060  0.2001  16  SER H OG  
2123 N N   . SER B 17  ? 1.0797 1.1401 1.2897 0.0806  0.1229  0.2057  17  SER H N   
2124 C CA  . SER B 17  ? 1.0481 1.1160 1.2688 0.0709  0.1298  0.1836  17  SER H CA  
2125 C C   . SER B 17  ? 1.0264 1.1089 1.2288 0.0464  0.1049  0.1680  17  SER H C   
2126 O O   . SER B 17  ? 1.0267 1.1285 1.2225 0.0376  0.0797  0.1788  17  SER H O   
2127 C CB  . SER B 17  ? 1.0438 1.1440 1.3160 0.0850  0.1362  0.1992  17  SER H CB  
2128 O OG  . SER B 17  ? 1.0332 1.1317 1.3083 0.0765  0.1482  0.1786  17  SER H OG  
2129 N N   . VAL B 18  ? 1.0083 1.0796 1.2010 0.0352  0.1125  0.1427  18  VAL H N   
2130 C CA  . VAL B 18  ? 0.9983 1.0771 1.1763 0.0142  0.0942  0.1264  18  VAL H CA  
2131 C C   . VAL B 18  ? 0.9744 1.0703 1.1757 0.0112  0.0961  0.1212  18  VAL H C   
2132 O O   . VAL B 18  ? 0.9792 1.0684 1.1928 0.0219  0.1162  0.1203  18  VAL H O   
2133 C CB  . VAL B 18  ? 1.0078 1.0520 1.1480 0.0034  0.1007  0.1010  18  VAL H CB  
2134 C CG1 . VAL B 18  ? 0.9968 1.0197 1.1345 0.0077  0.1224  0.0835  18  VAL H CG1 
2135 C CG2 . VAL B 18  ? 1.0009 1.0501 1.1270 -0.0163 0.0827  0.0866  18  VAL H CG2 
2136 N N   . LYS B 19  ? 0.9558 1.0699 1.1591 -0.0049 0.0769  0.1172  19  LYS H N   
2137 C CA  . LYS B 19  ? 0.9312 1.0582 1.1527 -0.0104 0.0780  0.1134  19  LYS H CA  
2138 C C   . LYS B 19  ? 0.9239 1.0388 1.1232 -0.0286 0.0667  0.0945  19  LYS H C   
2139 O O   . LYS B 19  ? 0.9345 1.0600 1.1292 -0.0429 0.0487  0.0946  19  LYS H O   
2140 C CB  . LYS B 19  ? 0.9335 1.1020 1.1952 -0.0097 0.0684  0.1346  19  LYS H CB  
2141 C CG  . LYS B 19  ? 0.9216 1.1030 1.2082 -0.0114 0.0781  0.1352  19  LYS H CG  
2142 C CD  . LYS B 19  ? 0.9193 1.1467 1.2520 -0.0132 0.0688  0.1549  19  LYS H CD  
2143 C CE  . LYS B 19  ? 0.9122 1.1502 1.2719 -0.0132 0.0856  0.1568  19  LYS H CE  
2144 N NZ  . LYS B 19  ? 0.9200 1.1445 1.2879 0.0070  0.1148  0.1602  19  LYS H NZ  
2145 N N   . VAL B 20  ? 0.9065 0.9985 1.0919 -0.0282 0.0775  0.0783  20  VAL H N   
2146 C CA  . VAL B 20  ? 0.8860 0.9631 1.0543 -0.0408 0.0697  0.0612  20  VAL H CA  
2147 C C   . VAL B 20  ? 0.8819 0.9650 1.0625 -0.0454 0.0693  0.0632  20  VAL H C   
2148 O O   . VAL B 20  ? 0.8838 0.9652 1.0696 -0.0370 0.0821  0.0669  20  VAL H O   
2149 C CB  . VAL B 20  ? 0.8776 0.9280 1.0247 -0.0368 0.0790  0.0433  20  VAL H CB  
2150 C CG1 . VAL B 20  ? 0.8730 0.9105 1.0109 -0.0458 0.0721  0.0274  20  VAL H CG1 
2151 C CG2 . VAL B 20  ? 0.8882 0.9286 1.0215 -0.0345 0.0826  0.0407  20  VAL H CG2 
2152 N N   . SER B 21  ? 0.8757 0.9616 1.0568 -0.0602 0.0568  0.0601  21  SER H N   
2153 C CA  . SER B 21  ? 0.8665 0.9535 1.0571 -0.0669 0.0573  0.0627  21  SER H CA  
2154 C C   . SER B 21  ? 0.8677 0.9259 1.0397 -0.0665 0.0592  0.0491  21  SER H C   
2155 O O   . SER B 21  ? 0.8710 0.9139 1.0284 -0.0629 0.0586  0.0363  21  SER H O   
2156 C CB  . SER B 21  ? 0.8701 0.9741 1.0731 -0.0846 0.0445  0.0668  21  SER H CB  
2157 O OG  . SER B 21  ? 0.8778 0.9632 1.0613 -0.0971 0.0359  0.0519  21  SER H OG  
2158 N N   . CYS B 22  ? 0.8830 0.9350 1.0579 -0.0699 0.0618  0.0534  22  CYS H N   
2159 C CA  . CYS B 22  ? 0.8912 0.9172 1.0508 -0.0671 0.0619  0.0459  22  CYS H CA  
2160 C C   . CYS B 22  ? 0.9187 0.9372 1.0821 -0.0758 0.0633  0.0540  22  CYS H C   
2161 O O   . CYS B 22  ? 0.9404 0.9588 1.1022 -0.0721 0.0723  0.0642  22  CYS H O   
2162 C CB  . CYS B 22  ? 0.8884 0.9072 1.0349 -0.0532 0.0693  0.0447  22  CYS H CB  
2163 S SG  . CYS B 22  ? 0.8876 0.8814 1.0166 -0.0488 0.0663  0.0438  22  CYS H SG  
2164 N N   . LYS B 23  ? 0.9356 0.9440 1.1011 -0.0887 0.0570  0.0486  23  LYS H N   
2165 C CA  . LYS B 23  ? 0.9546 0.9525 1.1243 -0.1004 0.0600  0.0552  23  LYS H CA  
2166 C C   . LYS B 23  ? 0.9790 0.9434 1.1324 -0.0919 0.0620  0.0554  23  LYS H C   
2167 O O   . LYS B 23  ? 0.9884 0.9325 1.1370 -0.0901 0.0575  0.0451  23  LYS H O   
2168 C CB  . LYS B 23  ? 0.9645 0.9634 1.1414 -0.1206 0.0536  0.0476  23  LYS H CB  
2169 C CG  . LYS B 23  ? 0.9989 0.9849 1.1813 -0.1370 0.0584  0.0523  23  LYS H CG  
2170 C CD  . LYS B 23  ? 1.0225 1.0108 1.2098 -0.1611 0.0521  0.0422  23  LYS H CD  
2171 C CE  . LYS B 23  ? 1.0553 1.0266 1.2477 -0.1801 0.0593  0.0447  23  LYS H CE  
2172 N NZ  . LYS B 23  ? 1.0524 1.0494 1.2649 -0.1838 0.0659  0.0607  23  LYS H NZ  
2173 N N   . ALA B 24  ? 1.0092 0.9678 1.1542 -0.0863 0.0696  0.0681  24  ALA H N   
2174 C CA  . ALA B 24  ? 1.0437 0.9708 1.1702 -0.0789 0.0697  0.0737  24  ALA H CA  
2175 C C   . ALA B 24  ? 1.0752 0.9790 1.2049 -0.0926 0.0739  0.0780  24  ALA H C   
2176 O O   . ALA B 24  ? 1.0753 0.9921 1.2203 -0.1098 0.0787  0.0786  24  ALA H O   
2177 C CB  . ALA B 24  ? 1.0544 0.9810 1.1627 -0.0709 0.0770  0.0857  24  ALA H CB  
2178 N N   . SER B 25  ? 1.0989 0.9685 1.2159 -0.0849 0.0719  0.0813  25  SER H N   
2179 C CA  . SER B 25  ? 1.1378 0.9757 1.2551 -0.0964 0.0784  0.0854  25  SER H CA  
2180 C C   . SER B 25  ? 1.1733 0.9741 1.2713 -0.0811 0.0772  0.0983  25  SER H C   
2181 O O   . SER B 25  ? 1.1635 0.9628 1.2581 -0.0626 0.0663  0.0962  25  SER H O   
2182 C CB  . SER B 25  ? 1.1369 0.9690 1.2688 -0.1074 0.0765  0.0681  25  SER H CB  
2183 O OG  . SER B 25  ? 1.1246 0.9521 1.2580 -0.0917 0.0686  0.0571  25  SER H OG  
2184 N N   . GLY B 26  ? 1.2125 0.9845 1.2991 -0.0894 0.0881  0.1127  26  GLY H N   
2185 C CA  . GLY B 26  ? 1.2557 0.9879 1.3204 -0.0754 0.0871  0.1296  26  GLY H CA  
2186 C C   . GLY B 26  ? 1.2642 1.0040 1.3007 -0.0617 0.0812  0.1439  26  GLY H C   
2187 O O   . GLY B 26  ? 1.2760 0.9989 1.2965 -0.0433 0.0695  0.1540  26  GLY H O   
2188 N N   . LEU B 27  ? 1.2584 1.0242 1.2896 -0.0712 0.0898  0.1446  27  LEU H N   
2189 C CA  . LEU B 27  ? 1.2775 1.0481 1.2772 -0.0628 0.0891  0.1550  27  LEU H CA  
2190 C C   . LEU B 27  ? 1.3384 1.0699 1.3035 -0.0662 0.0998  0.1774  27  LEU H C   
2191 O O   . LEU B 27  ? 1.3382 1.0581 1.3091 -0.0833 0.1179  0.1823  27  LEU H O   
2192 C CB  . LEU B 27  ? 1.2449 1.0531 1.2551 -0.0716 0.0995  0.1467  27  LEU H CB  
2193 C CG  . LEU B 27  ? 1.1975 1.0411 1.2313 -0.0656 0.0890  0.1281  27  LEU H CG  
2194 C CD1 . LEU B 27  ? 1.1771 1.0536 1.2266 -0.0737 0.1019  0.1236  27  LEU H CD1 
2195 C CD2 . LEU B 27  ? 1.1942 1.0388 1.2082 -0.0486 0.0738  0.1252  27  LEU H CD2 
2196 N N   . PRO B 28  ? 1.3900 1.1005 1.3173 -0.0515 0.0886  0.1921  28  PRO H N   
2197 C CA  . PRO B 28  ? 1.4658 1.1344 1.3517 -0.0541 0.0981  0.2162  28  PRO H CA  
2198 C C   . PRO B 28  ? 1.4895 1.1594 1.3547 -0.0715 0.1232  0.2214  28  PRO H C   
2199 O O   . PRO B 28  ? 1.5377 1.1772 1.3918 -0.0842 0.1419  0.2345  28  PRO H O   
2200 C CB  . PRO B 28  ? 1.4983 1.1576 1.3466 -0.0347 0.0755  0.2284  28  PRO H CB  
2201 C CG  . PRO B 28  ? 1.4464 1.1361 1.3305 -0.0203 0.0536  0.2109  28  PRO H CG  
2202 C CD  . PRO B 28  ? 1.3812 1.1072 1.3031 -0.0328 0.0649  0.1871  28  PRO H CD  
2203 N N   . ASP B 29  ? 1.4613 1.1645 1.3232 -0.0723 0.1261  0.2106  29  ASP H N   
2204 C CA  . ASP B 29  ? 1.4787 1.1820 1.3179 -0.0854 0.1516  0.2155  29  ASP H CA  
2205 C C   . ASP B 29  ? 1.4151 1.1641 1.2992 -0.0931 0.1643  0.1974  29  ASP H C   
2206 O O   . ASP B 29  ? 1.3648 1.1434 1.2849 -0.0869 0.1498  0.1820  29  ASP H O   
2207 C CB  . ASP B 29  ? 1.5240 1.2136 1.3031 -0.0781 0.1465  0.2235  29  ASP H CB  
2208 C CG  . ASP B 29  ? 1.5849 1.2527 1.3223 -0.0922 0.1760  0.2349  29  ASP H CG  
2209 O OD1 . ASP B 29  ? 1.6360 1.2677 1.3550 -0.1005 0.1887  0.2525  29  ASP H OD1 
2210 O OD2 . ASP B 29  ? 1.5939 1.2782 1.3171 -0.0955 0.1889  0.2255  29  ASP H OD2 
2211 N N   . ALA B 30  ? 1.4230 1.1763 1.3051 -0.1063 0.1926  0.2008  30  ALA H N   
2212 C CA  . ALA B 30  ? 1.3713 1.1681 1.2998 -0.1122 0.2072  0.1882  30  ALA H CA  
2213 C C   . ALA B 30  ? 1.3539 1.1697 1.2700 -0.1012 0.2062  0.1773  30  ALA H C   
2214 O O   . ALA B 30  ? 1.3251 1.1778 1.2824 -0.0985 0.2074  0.1653  30  ALA H O   
2215 C CB  . ALA B 30  ? 1.3977 1.1928 1.3353 -0.1296 0.2398  0.1964  30  ALA H CB  
2216 N N   . THR B 31  ? 1.3869 1.1757 1.2438 -0.0962 0.2045  0.1823  31  THR H N   
2217 C CA  . THR B 31  ? 1.3650 1.1652 1.2022 -0.0885 0.2033  0.1701  31  THR H CA  
2218 C C   . THR B 31  ? 1.3148 1.1213 1.1505 -0.0753 0.1691  0.1617  31  THR H C   
2219 O O   . THR B 31  ? 1.3341 1.1172 1.1308 -0.0702 0.1500  0.1699  31  THR H O   
2220 C CB  . THR B 31  ? 1.4388 1.2078 1.2090 -0.0942 0.2207  0.1770  31  THR H CB  
2221 O OG1 . THR B 31  ? 1.5012 1.2340 1.2235 -0.0935 0.2037  0.1935  31  THR H OG1 
2222 C CG2 . THR B 31  ? 1.4657 1.2317 1.2409 -0.1072 0.2608  0.1815  31  THR H CG2 
2223 N N   . TYR B 32  ? 1.2429 1.0824 1.1234 -0.0696 0.1620  0.1464  32  TYR H N   
2224 C CA  . TYR B 32  ? 1.2080 1.0578 1.0942 -0.0586 0.1346  0.1353  32  TYR H CA  
2225 C C   . TYR B 32  ? 1.1626 1.0370 1.0634 -0.0553 0.1413  0.1183  32  TYR H C   
2226 O O   . TYR B 32  ? 1.1688 1.0531 1.0823 -0.0594 0.1659  0.1166  32  TYR H O   
2227 C CB  . TYR B 32  ? 1.1730 1.0300 1.0998 -0.0558 0.1181  0.1348  32  TYR H CB  
2228 C CG  . TYR B 32  ? 1.1321 1.0121 1.1073 -0.0634 0.1300  0.1312  32  TYR H CG  
2229 C CD1 . TYR B 32  ? 1.1432 1.0175 1.1286 -0.0755 0.1471  0.1421  32  TYR H CD1 
2230 C CD2 . TYR B 32  ? 1.0854 0.9942 1.0956 -0.0597 0.1235  0.1174  32  TYR H CD2 
2231 C CE1 . TYR B 32  ? 1.1103 1.0118 1.1427 -0.0841 0.1546  0.1390  32  TYR H CE1 
2232 C CE2 . TYR B 32  ? 1.0557 0.9885 1.1077 -0.0670 0.1303  0.1161  32  TYR H CE2 
2233 C CZ  . TYR B 32  ? 1.0692 1.0010 1.1342 -0.0795 0.1444  0.1267  32  TYR H CZ  
2234 O OH  . TYR B 32  ? 1.0459 1.0074 1.1551 -0.0883 0.1478  0.1256  32  TYR H OH  
2235 N N   . ALA B 33  ? 1.1301 1.0134 1.0313 -0.0476 0.1208  0.1061  33  ALA H N   
2236 C CA  . ALA B 33  ? 1.0915 0.9927 1.0039 -0.0449 0.1266  0.0895  33  ALA H CA  
2237 C C   . ALA B 33  ? 1.0421 0.9627 0.9926 -0.0386 0.1085  0.0791  33  ALA H C   
2238 O O   . ALA B 33  ? 1.0401 0.9576 0.9905 -0.0342 0.0865  0.0787  33  ALA H O   
2239 C CB  . ALA B 33  ? 1.1216 1.0105 0.9860 -0.0464 0.1245  0.0819  33  ALA H CB  
2240 N N   . ILE B 34  ? 1.0056 0.9451 0.9884 -0.0375 0.1192  0.0718  34  ILE H N   
2241 C CA  . ILE B 34  ? 0.9723 0.9276 0.9856 -0.0334 0.1060  0.0617  34  ILE H CA  
2242 C C   . ILE B 34  ? 0.9646 0.9257 0.9741 -0.0304 0.1125  0.0471  34  ILE H C   
2243 O O   . ILE B 34  ? 0.9653 0.9324 0.9855 -0.0294 0.1314  0.0470  34  ILE H O   
2244 C CB  . ILE B 34  ? 0.9503 0.9213 1.0021 -0.0362 0.1097  0.0675  34  ILE H CB  
2245 C CG1 . ILE B 34  ? 0.9638 0.9260 1.0192 -0.0427 0.1058  0.0797  34  ILE H CG1 
2246 C CG2 . ILE B 34  ? 0.9230 0.9068 0.9977 -0.0338 0.0983  0.0567  34  ILE H CG2 
2247 C CD1 . ILE B 34  ? 0.9670 0.9147 1.0163 -0.0405 0.0862  0.0779  34  ILE H CD1 
2248 N N   . GLY B 35  ? 0.9675 0.9267 0.9644 -0.0289 0.0974  0.0354  35  GLY H N   
2249 C CA  . GLY B 35  ? 0.9592 0.9220 0.9534 -0.0288 0.1028  0.0191  35  GLY H CA  
2250 C C   . GLY B 35  ? 0.9239 0.8994 0.9516 -0.0259 0.1016  0.0127  35  GLY H C   
2251 O O   . GLY B 35  ? 0.9210 0.9030 0.9705 -0.0250 0.0918  0.0180  35  GLY H O   
2252 N N   . TRP B 36  ? 0.9151 0.8901 0.9425 -0.0258 0.1133  0.0009  36  TRP H N   
2253 C CA  . TRP B 36  ? 0.8750 0.8573 0.9259 -0.0239 0.1138  -0.0050 36  TRP H CA  
2254 C C   . TRP B 36  ? 0.8634 0.8417 0.9056 -0.0272 0.1152  -0.0241 36  TRP H C   
2255 O O   . TRP B 36  ? 0.8647 0.8325 0.8866 -0.0303 0.1287  -0.0316 36  TRP H O   
2256 C CB  . TRP B 36  ? 0.8716 0.8567 0.9376 -0.0195 0.1312  0.0055  36  TRP H CB  
2257 C CG  . TRP B 36  ? 0.8708 0.8684 0.9570 -0.0190 0.1254  0.0217  36  TRP H CG  
2258 C CD1 . TRP B 36  ? 0.8867 0.8865 0.9740 -0.0196 0.1318  0.0347  36  TRP H CD1 
2259 C CD2 . TRP B 36  ? 0.8545 0.8635 0.9615 -0.0207 0.1135  0.0253  36  TRP H CD2 
2260 N NE1 . TRP B 36  ? 0.8773 0.8914 0.9882 -0.0222 0.1236  0.0456  36  TRP H NE1 
2261 C CE2 . TRP B 36  ? 0.8575 0.8771 0.9787 -0.0234 0.1115  0.0398  36  TRP H CE2 
2262 C CE3 . TRP B 36  ? 0.8387 0.8486 0.9510 -0.0224 0.1057  0.0166  36  TRP H CE3 
2263 C CZ2 . TRP B 36  ? 0.8402 0.8721 0.9794 -0.0289 0.0999  0.0448  36  TRP H CZ2 
2264 C CZ3 . TRP B 36  ? 0.8324 0.8517 0.9584 -0.0270 0.0956  0.0220  36  TRP H CZ3 
2265 C CH2 . TRP B 36  ? 0.8328 0.8634 0.9716 -0.0308 0.0916  0.0355  36  TRP H CH2 
2266 N N   . VAL B 37  ? 0.8459 0.8315 0.9037 -0.0284 0.1029  -0.0333 37  VAL H N   
2267 C CA  . VAL B 37  ? 0.8547 0.8404 0.9120 -0.0334 0.1044  -0.0525 37  VAL H CA  
2268 C C   . VAL B 37  ? 0.8382 0.8246 0.9145 -0.0331 0.1086  -0.0562 37  VAL H C   
2269 O O   . VAL B 37  ? 0.8343 0.8260 0.9246 -0.0310 0.1000  -0.0490 37  VAL H O   
2270 C CB  . VAL B 37  ? 0.8607 0.8575 0.9191 -0.0360 0.0840  -0.0615 37  VAL H CB  
2271 C CG1 . VAL B 37  ? 0.8588 0.8627 0.9277 -0.0428 0.0843  -0.0824 37  VAL H CG1 
2272 C CG2 . VAL B 37  ? 0.8873 0.8810 0.9176 -0.0381 0.0781  -0.0572 37  VAL H CG2 
2273 N N   . ARG B 38  ? 0.8479 0.8256 0.9206 -0.0370 0.1235  -0.0679 38  ARG H N   
2274 C CA  . ARG B 38  ? 0.8399 0.8147 0.9240 -0.0389 0.1285  -0.0731 38  ARG H CA  
2275 C C   . ARG B 38  ? 0.8343 0.8126 0.9247 -0.0476 0.1285  -0.0953 38  ARG H C   
2276 O O   . ARG B 38  ? 0.8398 0.8198 0.9221 -0.0531 0.1292  -0.1066 38  ARG H O   
2277 C CB  . ARG B 38  ? 0.8596 0.8190 0.9366 -0.0353 0.1477  -0.0640 38  ARG H CB  
2278 C CG  . ARG B 38  ? 0.8825 0.8239 0.9464 -0.0393 0.1683  -0.0758 38  ARG H CG  
2279 C CD  . ARG B 38  ? 0.8906 0.8139 0.9507 -0.0322 0.1872  -0.0630 38  ARG H CD  
2280 N NE  . ARG B 38  ? 0.9116 0.8107 0.9595 -0.0370 0.2103  -0.0755 38  ARG H NE  
2281 C CZ  . ARG B 38  ? 0.9310 0.8076 0.9741 -0.0299 0.2306  -0.0652 38  ARG H CZ  
2282 N NH1 . ARG B 38  ? 0.9120 0.7933 0.9640 -0.0172 0.2274  -0.0410 38  ARG H NH1 
2283 N NH2 . ARG B 38  ? 0.9666 0.8163 0.9973 -0.0359 0.2539  -0.0784 38  ARG H NH2 
2284 N N   . GLN B 39  ? 0.8789 0.8666 0.9310 0.0363  0.0917  0.1043  39  GLN H N   
2285 C CA  . GLN B 39  ? 0.8721 0.8918 0.9408 0.0269  0.1056  0.1087  39  GLN H CA  
2286 C C   . GLN B 39  ? 0.9141 0.9394 0.9797 0.0351  0.1287  0.1354  39  GLN H C   
2287 O O   . GLN B 39  ? 0.9212 0.9618 0.9637 0.0633  0.1250  0.1443  39  GLN H O   
2288 C CB  . GLN B 39  ? 0.8348 0.8923 0.8930 0.0427  0.0899  0.0952  39  GLN H CB  
2289 C CG  . GLN B 39  ? 0.8161 0.9199 0.8966 0.0299  0.1002  0.0924  39  GLN H CG  
2290 C CD  . GLN B 39  ? 0.7959 0.9368 0.8603 0.0526  0.0837  0.0783  39  GLN H CD  
2291 O OE1 . GLN B 39  ? 0.7937 0.9235 0.8275 0.0800  0.0686  0.0747  39  GLN H OE1 
2292 N NE2 . GLN B 39  ? 0.7848 0.9715 0.8685 0.0425  0.0868  0.0683  39  GLN H NE2 
2293 N N   . ALA B 40  ? 0.9544 0.9652 1.0419 0.0102  0.1533  0.1476  40  ALA H N   
2294 C CA  . ALA B 40  ? 1.0077 1.0175 1.0931 0.0141  0.1816  0.1778  40  ALA H CA  
2295 C C   . ALA B 40  ? 1.0363 1.0818 1.1516 -0.0136 0.2003  0.1800  40  ALA H C   
2296 O O   . ALA B 40  ? 1.0230 1.0739 1.1657 -0.0442 0.1977  0.1590  40  ALA H O   
2297 C CB  . ALA B 40  ? 1.0451 0.9937 1.1252 0.0094  0.1992  0.1938  40  ALA H CB  
2298 N N   . PRO B 41  ? 1.0842 1.1648 1.1962 -0.0032 0.2193  0.2040  41  PRO H N   
2299 C CA  . PRO B 41  ? 1.1121 1.2285 1.2567 -0.0353 0.2436  0.2106  41  PRO H CA  
2300 C C   . PRO B 41  ? 1.1704 1.2281 1.3372 -0.0754 0.2725  0.2205  41  PRO H C   
2301 O O   . PRO B 41  ? 1.2106 1.2100 1.3576 -0.0649 0.2910  0.2468  41  PRO H O   
2302 C CB  . PRO B 41  ? 1.1281 1.2875 1.2563 -0.0081 0.2596  0.2406  41  PRO H CB  
2303 C CG  . PRO B 41  ? 1.1043 1.2679 1.1923 0.0412  0.2322  0.2358  41  PRO H CG  
2304 C CD  . PRO B 41  ? 1.0941 1.1920 1.1723 0.0398  0.2180  0.2237  41  PRO H CD  
2305 N N   . GLY B 42  ? 1.1829 1.2567 1.3886 -0.1189 0.2757  0.1972  42  GLY H N   
2306 C CA  . GLY B 42  ? 1.2448 1.2615 1.4749 -0.1630 0.3015  0.1978  42  GLY H CA  
2307 C C   . GLY B 42  ? 1.2403 1.2185 1.4773 -0.1760 0.2808  0.1640  42  GLY H C   
2308 O O   . GLY B 42  ? 1.2503 1.2423 1.5226 -0.2160 0.2821  0.1364  42  GLY H O   
2309 N N   . GLN B 43  ? 1.2356 1.1727 1.4389 -0.1416 0.2618  0.1654  43  GLN H N   
2310 C CA  . GLN B 43  ? 1.2257 1.1338 1.4299 -0.1456 0.2402  0.1366  43  GLN H CA  
2311 C C   . GLN B 43  ? 1.1583 1.1326 1.3709 -0.1398 0.2090  0.1066  43  GLN H C   
2312 O O   . GLN B 43  ? 1.1504 1.1398 1.3867 -0.1632 0.2001  0.0769  43  GLN H O   
2313 C CB  . GLN B 43  ? 1.2470 1.1015 1.4133 -0.1102 0.2322  0.1504  43  GLN H CB  
2314 C CG  . GLN B 43  ? 1.3285 1.1073 1.4806 -0.1106 0.2625  0.1773  43  GLN H CG  
2315 C CD  . GLN B 43  ? 1.3455 1.0918 1.4572 -0.0671 0.2553  0.1942  43  GLN H CD  
2316 O OE1 . GLN B 43  ? 1.3253 1.1106 1.4205 -0.0381 0.2310  0.1904  43  GLN H OE1 
2317 N NE2 . GLN B 43  ? 1.4027 1.0774 1.4969 -0.0617 0.2776  0.2122  43  GLN H NE2 
2318 N N   . GLY B 44  ? 1.1160 1.1279 1.3060 -0.1055 0.1933  0.1143  44  GLY H N   
2319 C CA  . GLY B 44  ? 1.0529 1.1157 1.2402 -0.0916 0.1657  0.0911  44  GLY H CA  
2320 C C   . GLY B 44  ? 1.0131 1.0431 1.1745 -0.0686 0.1413  0.0826  44  GLY H C   
2321 O O   . GLY B 44  ? 1.0209 1.0078 1.1613 -0.0534 0.1427  0.0978  44  GLY H O   
2322 N N   . LEU B 45  ? 0.9633 1.0189 1.1260 -0.0654 0.1205  0.0590  45  LEU H N   
2323 C CA  . LEU B 45  ? 0.9304 0.9589 1.0712 -0.0481 0.0995  0.0513  45  LEU H CA  
2324 C C   . LEU B 45  ? 0.9230 0.9085 1.0727 -0.0645 0.1029  0.0457  45  LEU H C   
2325 O O   . LEU B 45  ? 0.9174 0.9123 1.0906 -0.0867 0.1061  0.0280  45  LEU H O   
2326 C CB  . LEU B 45  ? 0.9080 0.9750 1.0446 -0.0376 0.0811  0.0320  45  LEU H CB  
2327 C CG  . LEU B 45  ? 0.8895 0.9911 1.0067 -0.0117 0.0739  0.0355  45  LEU H CG  
2328 C CD1 . LEU B 45  ? 0.8736 1.0135 0.9857 0.0007  0.0600  0.0172  45  LEU H CD1 
2329 C CD2 . LEU B 45  ? 0.8833 0.9491 0.9676 0.0125  0.0638  0.0462  45  LEU H CD2 
2330 N N   . GLU B 46  ? 0.9143 0.8584 1.0443 -0.0512 0.1015  0.0585  46  GLU H N   
2331 C CA  . GLU B 46  ? 0.9159 0.8206 1.0475 -0.0584 0.1036  0.0548  46  GLU H CA  
2332 C C   . GLU B 46  ? 0.8836 0.7836 0.9970 -0.0422 0.0836  0.0500  46  GLU H C   
2333 O O   . GLU B 46  ? 0.8544 0.7552 0.9481 -0.0243 0.0760  0.0598  46  GLU H O   
2334 C CB  . GLU B 46  ? 0.9490 0.8123 1.0721 -0.0546 0.1234  0.0766  46  GLU H CB  
2335 C CG  . GLU B 46  ? 0.9917 0.8444 1.1338 -0.0769 0.1490  0.0840  46  GLU H CG  
2336 C CD  . GLU B 46  ? 1.0431 0.8435 1.1701 -0.0688 0.1724  0.1100  46  GLU H CD  
2337 O OE1 . GLU B 46  ? 1.0461 0.8492 1.1485 -0.0404 0.1727  0.1311  46  GLU H OE1 
2338 O OE2 . GLU B 46  ? 1.0767 0.8329 1.2141 -0.0890 0.1906  0.1080  46  GLU H OE2 
2339 N N   . TRP B 47  ? 0.8785 0.7767 0.9994 -0.0499 0.0760  0.0336  47  TRP H N   
2340 C CA  . TRP B 47  ? 0.8699 0.7632 0.9763 -0.0387 0.0614  0.0315  47  TRP H CA  
2341 C C   . TRP B 47  ? 0.8810 0.7461 0.9766 -0.0299 0.0669  0.0438  47  TRP H C   
2342 O O   . TRP B 47  ? 0.9023 0.7415 1.0029 -0.0344 0.0810  0.0464  47  TRP H O   
2343 C CB  . TRP B 47  ? 0.8596 0.7664 0.9762 -0.0458 0.0539  0.0124  47  TRP H CB  
2344 C CG  . TRP B 47  ? 0.8509 0.7550 0.9544 -0.0362 0.0427  0.0130  47  TRP H CG  
2345 C CD1 . TRP B 47  ? 0.8668 0.7638 0.9726 -0.0362 0.0423  0.0066  47  TRP H CD1 
2346 C CD2 . TRP B 47  ? 0.8497 0.7583 0.9359 -0.0266 0.0316  0.0202  47  TRP H CD2 
2347 N NE1 . TRP B 47  ? 0.8534 0.7580 0.9464 -0.0276 0.0326  0.0117  47  TRP H NE1 
2348 C CE2 . TRP B 47  ? 0.8483 0.7565 0.9301 -0.0244 0.0268  0.0200  47  TRP H CE2 
2349 C CE3 . TRP B 47  ? 0.8524 0.7628 0.9252 -0.0200 0.0262  0.0257  47  TRP H CE3 
2350 C CZ2 . TRP B 47  ? 0.8478 0.7569 0.9157 -0.0212 0.0189  0.0268  47  TRP H CZ2 
2351 C CZ3 . TRP B 47  ? 0.8559 0.7586 0.9123 -0.0157 0.0173  0.0296  47  TRP H CZ3 
2352 C CH2 . TRP B 47  ? 0.8537 0.7555 0.9092 -0.0188 0.0147  0.0310  47  TRP H CH2 
2353 N N   . MET B 48  ? 0.8729 0.7436 0.9525 -0.0171 0.0563  0.0500  48  MET H N   
2354 C CA  . MET B 48  ? 0.8943 0.7547 0.9619 -0.0039 0.0595  0.0607  48  MET H CA  
2355 C C   . MET B 48  ? 0.8946 0.7637 0.9602 -0.0028 0.0495  0.0540  48  MET H C   
2356 O O   . MET B 48  ? 0.9074 0.7655 0.9712 0.0035  0.0550  0.0545  48  MET H O   
2357 C CB  . MET B 48  ? 0.8876 0.7621 0.9410 0.0095  0.0558  0.0707  48  MET H CB  
2358 C CG  . MET B 48  ? 0.9015 0.7710 0.9526 0.0155  0.0693  0.0829  48  MET H CG  
2359 S SD  . MET B 48  ? 0.8963 0.7908 0.9277 0.0376  0.0633  0.0912  48  MET H SD  
2360 C CE  . MET B 48  ? 0.9260 0.8149 0.9430 0.0604  0.0747  0.1069  48  MET H CE  
2361 N N   . GLY B 49  ? 0.8834 0.7703 0.9471 -0.0077 0.0363  0.0488  49  GLY H N   
2362 C CA  . GLY B 49  ? 0.8758 0.7760 0.9388 -0.0095 0.0289  0.0455  49  GLY H CA  
2363 C C   . GLY B 49  ? 0.8634 0.7731 0.9207 -0.0170 0.0184  0.0446  49  GLY H C   
2364 O O   . GLY B 49  ? 0.8674 0.7697 0.9187 -0.0181 0.0153  0.0441  49  GLY H O   
2365 N N   . ARG B 50  ? 0.8537 0.7775 0.9111 -0.0216 0.0144  0.0450  50  ARG H N   
2366 C CA  . ARG B 50  ? 0.8530 0.7767 0.9044 -0.0328 0.0083  0.0461  50  ARG H CA  
2367 C C   . ARG B 50  ? 0.8543 0.8031 0.9081 -0.0406 0.0058  0.0486  50  ARG H C   
2368 O O   . ARG B 50  ? 0.8383 0.8104 0.8965 -0.0316 0.0078  0.0495  50  ARG H O   
2369 C CB  . ARG B 50  ? 0.8547 0.7768 0.9047 -0.0339 0.0090  0.0465  50  ARG H CB  
2370 C CG  . ARG B 50  ? 0.8492 0.7957 0.9062 -0.0304 0.0114  0.0473  50  ARG H CG  
2371 C CD  . ARG B 50  ? 0.8518 0.8056 0.9033 -0.0314 0.0120  0.0520  50  ARG H CD  
2372 N NE  . ARG B 50  ? 0.8489 0.8331 0.9058 -0.0247 0.0139  0.0522  50  ARG H NE  
2373 C CZ  . ARG B 50  ? 0.8487 0.8594 0.9096 -0.0287 0.0149  0.0582  50  ARG H CZ  
2374 N NH1 . ARG B 50  ? 0.8536 0.8664 0.9163 -0.0426 0.0137  0.0624  50  ARG H NH1 
2375 N NH2 . ARG B 50  ? 0.8446 0.8862 0.9078 -0.0176 0.0165  0.0576  50  ARG H NH2 
2376 N N   . ILE B 51  ? 0.8703 0.8140 0.9203 -0.0570 0.0026  0.0493  51  ILE H N   
2377 C CA  . ILE B 51  ? 0.8813 0.8556 0.9385 -0.0724 0.0017  0.0505  51  ILE H CA  
2378 C C   . ILE B 51  ? 0.9124 0.8658 0.9642 -0.0919 0.0044  0.0563  51  ILE H C   
2379 O O   . ILE B 51  ? 0.9297 0.8397 0.9672 -0.0930 0.0040  0.0562  51  ILE H O   
2380 C CB  . ILE B 51  ? 0.8796 0.8746 0.9396 -0.0768 -0.0041 0.0414  51  ILE H CB  
2381 C CG1 . ILE B 51  ? 0.8795 0.9238 0.9524 -0.0941 -0.0051 0.0391  51  ILE H CG1 
2382 C CG2 . ILE B 51  ? 0.8995 0.8577 0.9486 -0.0848 -0.0091 0.0334  51  ILE H CG2 
2383 C CD1 . ILE B 51  ? 0.8806 0.9649 0.9582 -0.0935 -0.0121 0.0265  51  ILE H CD1 
2384 N N   . ILE B 52  ? 0.9257 0.9102 0.9863 -0.1044 0.0088  0.0633  52  ILE H N   
2385 C CA  . ILE B 52  ? 0.9675 0.9337 1.0234 -0.1271 0.0154  0.0729  52  ILE H CA  
2386 C C   . ILE B 52  ? 0.9989 0.9996 1.0706 -0.1567 0.0150  0.0675  52  ILE H C   
2387 O O   . ILE B 52  ? 0.9951 1.0497 1.0813 -0.1630 0.0189  0.0728  52  ILE H O   
2388 C CB  . ILE B 52  ? 0.9641 0.9439 1.0174 -0.1176 0.0237  0.0881  52  ILE H CB  
2389 C CG1 . ILE B 52  ? 0.9394 0.9047 0.9830 -0.0880 0.0219  0.0864  52  ILE H CG1 
2390 C CG2 . ILE B 52  ? 1.0079 0.9595 1.0509 -0.1381 0.0346  0.1037  52  ILE H CG2 
2391 C CD1 . ILE B 52  ? 0.9655 0.8782 0.9890 -0.0817 0.0223  0.0878  52  ILE H CD1 
2392 N N   . PRO B 53  A 1.0366 1.0139 1.1067 -0.1753 0.0098  0.0540  52  PRO H N   
2393 C CA  . PRO B 53  A 1.0607 1.0835 1.1500 -0.2037 0.0064  0.0406  52  PRO H CA  
2394 C C   . PRO B 53  A 1.0880 1.1510 1.1946 -0.2337 0.0164  0.0500  52  PRO H C   
2395 O O   . PRO B 53  A 1.0838 1.2212 1.2121 -0.2442 0.0133  0.0409  52  PRO H O   
2396 C CB  . PRO B 53  A 1.1008 1.0666 1.1786 -0.2226 0.0021  0.0257  52  PRO H CB  
2397 C CG  . PRO B 53  A 1.0738 0.9934 1.1296 -0.1885 -0.0025 0.0266  52  PRO H CG  
2398 C CD  . PRO B 53  A 1.0510 0.9640 1.1005 -0.1680 0.0057  0.0476  52  PRO H CD  
2399 N N   . ARG B 54  ? 1.1351 1.1549 1.2310 -0.2451 0.0295  0.0695  53  ARG H N   
2400 C CA  . ARG B 54  ? 1.1678 1.2231 1.2787 -0.2745 0.0428  0.0835  53  ARG H CA  
2401 C C   . ARG B 54  ? 1.1182 1.2545 1.2420 -0.2510 0.0430  0.0917  53  ARG H C   
2402 O O   . ARG B 54  ? 1.1173 1.3301 1.2646 -0.2681 0.0442  0.0881  53  ARG H O   
2403 C CB  . ARG B 54  ? 1.2284 1.2129 1.3179 -0.2843 0.0595  0.1074  53  ARG H CB  
2404 C CG  . ARG B 54  ? 1.2596 1.2857 1.3607 -0.3033 0.0769  0.1307  53  ARG H CG  
2405 C CD  . ARG B 54  ? 1.3401 1.2921 1.4208 -0.3252 0.0976  0.1549  53  ARG H CD  
2406 N NE  . ARG B 54  ? 1.4051 1.3347 1.4995 -0.3814 0.1060  0.1469  53  ARG H NE  
2407 C CZ  . ARG B 54  ? 1.4810 1.3512 1.5636 -0.4136 0.1288  0.1687  53  ARG H CZ  
2408 N NH1 . ARG B 54  ? 1.5078 1.3382 1.5612 -0.3890 0.1455  0.2027  53  ARG H NH1 
2409 N NH2 . ARG B 54  ? 1.5316 1.3823 1.6309 -0.4702 0.1359  0.1559  53  ARG H NH2 
2410 N N   . LEU B 55  ? 1.0869 1.2084 1.1948 -0.2111 0.0415  0.1002  54  LEU H N   
2411 C CA  . LEU B 55  ? 1.0528 1.2370 1.1667 -0.1835 0.0413  0.1054  54  LEU H CA  
2412 C C   . LEU B 55  ? 1.0276 1.2620 1.1516 -0.1658 0.0294  0.0877  54  LEU H C   
2413 O O   . LEU B 55  ? 1.0241 1.3227 1.1551 -0.1482 0.0295  0.0891  54  LEU H O   
2414 C CB  . LEU B 55  ? 1.0414 1.1887 1.1352 -0.1490 0.0419  0.1132  54  LEU H CB  
2415 C CG  . LEU B 55  ? 1.0734 1.2058 1.1553 -0.1506 0.0554  0.1354  54  LEU H CG  
2416 C CD1 . LEU B 55  ? 1.1290 1.1910 1.1971 -0.1756 0.0637  0.1448  54  LEU H CD1 
2417 C CD2 . LEU B 55  ? 1.0564 1.1808 1.1232 -0.1114 0.0527  0.1359  54  LEU H CD2 
2418 N N   . ASP B 56  ? 1.0208 1.2257 1.1415 -0.1657 0.0202  0.0723  55  ASP H N   
2419 C CA  . ASP B 56  ? 0.9924 1.2327 1.1149 -0.1410 0.0109  0.0592  55  ASP H CA  
2420 C C   . ASP B 56  ? 0.9673 1.1948 1.0765 -0.1006 0.0114  0.0645  55  ASP H C   
2421 O O   . ASP B 56  ? 0.9550 1.2269 1.0640 -0.0752 0.0100  0.0624  55  ASP H O   
2422 C CB  . ASP B 56  ? 0.9920 1.3235 1.1337 -0.1505 0.0091  0.0520  55  ASP H CB  
2423 C CG  . ASP B 56  ? 0.9946 1.3614 1.1350 -0.1290 -0.0006 0.0366  55  ASP H CG  
2424 O OD1 . ASP B 56  ? 0.9707 1.3184 1.0946 -0.0899 -0.0019 0.0394  55  ASP H OD1 
2425 O OD2 . ASP B 56  ? 1.0243 1.4379 1.1797 -0.1517 -0.0059 0.0214  55  ASP H OD2 
2426 N N   . ALA B 57  ? 0.9608 1.1272 1.0576 -0.0945 0.0138  0.0699  56  ALA H N   
2427 C CA  . ALA B 57  ? 0.9462 1.0967 1.0335 -0.0638 0.0147  0.0706  56  ALA H CA  
2428 C C   . ALA B 57  ? 0.9322 1.0342 1.0111 -0.0517 0.0112  0.0631  56  ALA H C   
2429 O O   . ALA B 57  ? 0.9280 0.9907 1.0027 -0.0643 0.0096  0.0619  56  ALA H O   
2430 C CB  . ALA B 57  ? 0.9555 1.0907 1.0377 -0.0645 0.0201  0.0798  56  ALA H CB  
2431 N N   . GLU B 58  ? 0.9185 1.0225 0.9931 -0.0261 0.0116  0.0591  57  GLU H N   
2432 C CA  . GLU B 58  ? 0.9154 0.9765 0.9832 -0.0152 0.0121  0.0551  57  GLU H CA  
2433 C C   . GLU B 58  ? 0.9055 0.9426 0.9695 0.0014  0.0165  0.0516  57  GLU H C   
2434 O O   . GLU B 58  ? 0.9165 0.9748 0.9789 0.0150  0.0182  0.0504  57  GLU H O   
2435 C CB  . GLU B 58  ? 0.9313 1.0090 0.9948 -0.0014 0.0116  0.0545  57  GLU H CB  
2436 C CG  . GLU B 58  ? 0.9426 1.0513 1.0118 -0.0186 0.0052  0.0510  57  GLU H CG  
2437 C CD  . GLU B 58  ? 0.9546 1.1236 1.0350 -0.0314 0.0031  0.0503  57  GLU H CD  
2438 O OE1 . GLU B 58  ? 0.9640 1.1596 1.0446 -0.0184 0.0066  0.0547  57  GLU H OE1 
2439 O OE2 . GLU B 58  ? 0.9700 1.1609 1.0595 -0.0556 -0.0016 0.0439  57  GLU H OE2 
2440 N N   . HIS B 59  ? 0.8940 0.8905 0.9573 -0.0002 0.0183  0.0475  58  HIS H N   
2441 C CA  . HIS B 59  ? 0.8850 0.8574 0.9486 0.0091  0.0229  0.0392  58  HIS H CA  
2442 C C   . HIS B 59  ? 0.9040 0.8408 0.9673 0.0086  0.0284  0.0387  58  HIS H C   
2443 O O   . HIS B 59  ? 0.9161 0.8445 0.9818 -0.0023 0.0261  0.0396  58  HIS H O   
2444 C CB  . HIS B 59  ? 0.8534 0.8297 0.9213 0.0023  0.0198  0.0326  58  HIS H CB  
2445 C CG  . HIS B 59  ? 0.8429 0.8094 0.9140 0.0107  0.0221  0.0175  58  HIS H CG  
2446 N ND1 . HIS B 59  ? 0.8231 0.7998 0.8981 0.0089  0.0188  0.0070  58  HIS H ND1 
2447 C CD2 . HIS B 59  ? 0.8533 0.7994 0.9227 0.0212  0.0276  0.0089  58  HIS H CD2 
2448 C CE1 . HIS B 59  ? 0.8329 0.8017 0.9123 0.0150  0.0206  -0.0112 58  HIS H CE1 
2449 N NE2 . HIS B 59  ? 0.8530 0.7966 0.9284 0.0212  0.0267  -0.0100 58  HIS H NE2 
2450 N N   . TYR B 60  ? 0.9327 0.8475 0.9906 0.0224  0.0372  0.0387  59  TYR H N   
2451 C CA  . TYR B 60  ? 0.9623 0.8444 1.0182 0.0230  0.0467  0.0438  59  TYR H CA  
2452 C C   . TYR B 60  ? 0.9854 0.8325 1.0493 0.0156  0.0555  0.0324  59  TYR H C   
2453 O O   . TYR B 60  ? 0.9967 0.8419 1.0630 0.0174  0.0542  0.0191  59  TYR H O   
2454 C CB  . TYR B 60  ? 0.9893 0.8682 1.0287 0.0457  0.0540  0.0567  59  TYR H CB  
2455 C CG  . TYR B 60  ? 0.9839 0.9103 1.0187 0.0522  0.0445  0.0623  59  TYR H CG  
2456 C CD1 . TYR B 60  ? 0.9677 0.9121 1.0074 0.0389  0.0367  0.0631  59  TYR H CD1 
2457 C CD2 . TYR B 60  ? 1.0085 0.9655 1.0344 0.0711  0.0432  0.0640  59  TYR H CD2 
2458 C CE1 . TYR B 60  ? 0.9653 0.9541 1.0040 0.0391  0.0280  0.0630  59  TYR H CE1 
2459 C CE2 . TYR B 60  ? 0.9946 1.0064 1.0211 0.0725  0.0346  0.0658  59  TYR H CE2 
2460 C CZ  . TYR B 60  ? 0.9762 1.0029 1.0108 0.0537  0.0270  0.0640  59  TYR H CZ  
2461 O OH  . TYR B 60  ? 0.9782 1.0598 1.0166 0.0496  0.0185  0.0608  59  TYR H OH  
2462 N N   . ALA B 61  ? 1.0091 0.8331 1.0781 0.0062  0.0645  0.0361  60  ALA H N   
2463 C CA  . ALA B 61  ? 1.0505 0.8402 1.1299 -0.0061 0.0766  0.0256  60  ALA H CA  
2464 C C   . ALA B 61  ? 1.1096 0.8520 1.1729 0.0092  0.0928  0.0346  60  ALA H C   
2465 O O   . ALA B 61  ? 1.1233 0.8628 1.1682 0.0296  0.0976  0.0543  60  ALA H O   
2466 C CB  . ALA B 61  ? 1.0473 0.8390 1.1392 -0.0229 0.0818  0.0284  60  ALA H CB  
2467 N N   . GLN B 62  ? 1.3028 1.2092 1.2507 -0.0076 -0.0296 -0.1504 61  GLN H N   
2468 C CA  . GLN B 62  ? 1.3394 1.2106 1.2742 0.0004  -0.0067 -0.1694 61  GLN H CA  
2469 C C   . GLN B 62  ? 1.2938 1.1757 1.2921 0.0108  0.0066  -0.1576 61  GLN H C   
2470 O O   . GLN B 62  ? 1.2943 1.1626 1.2935 0.0282  0.0326  -0.1623 61  GLN H O   
2471 C CB  . GLN B 62  ? 1.4346 1.2574 1.3262 -0.0208 -0.0252 -0.1929 61  GLN H CB  
2472 C CG  . GLN B 62  ? 1.4462 1.2649 1.3844 -0.0415 -0.0529 -0.1893 61  GLN H CG  
2473 C CD  . GLN B 62  ? 1.4251 1.2798 1.3958 -0.0577 -0.0890 -0.1700 61  GLN H CD  
2474 O OE1 . GLN B 62  ? 1.4368 1.3117 1.3836 -0.0561 -0.0984 -0.1605 61  GLN H OE1 
2475 N NE2 . GLN B 62  ? 1.4037 1.2667 1.4338 -0.0735 -0.1093 -0.1627 61  GLN H NE2 
2476 N N   . LYS B 63  ? 1.2616 1.1675 1.3131 0.0005  -0.0102 -0.1411 62  LYS H N   
2477 C CA  . LYS B 63  ? 1.2311 1.1425 1.3373 0.0055  0.0032  -0.1295 62  LYS H CA  
2478 C C   . LYS B 63  ? 1.1747 1.1042 1.2878 0.0297  0.0309  -0.1175 62  LYS H C   
2479 O O   . LYS B 63  ? 1.1701 1.0844 1.2951 0.0398  0.0492  -0.1152 62  LYS H O   
2480 C CB  . LYS B 63  ? 1.2188 1.1587 1.3834 -0.0091 -0.0155 -0.1134 62  LYS H CB  
2481 C CG  . LYS B 63  ? 1.2058 1.1492 1.4254 -0.0078 0.0015  -0.1011 62  LYS H CG  
2482 C CD  . LYS B 63  ? 1.1917 1.1644 1.4775 -0.0230 -0.0130 -0.0869 62  LYS H CD  
2483 C CE  . LYS B 63  ? 1.1783 1.1508 1.5145 -0.0239 0.0100  -0.0753 62  LYS H CE  
2484 N NZ  . LYS B 63  ? 1.1393 1.1208 1.4694 -0.0025 0.0411  -0.0633 62  LYS H NZ  
2485 N N   . PHE B 64  ? 1.1476 1.1071 1.2520 0.0372  0.0312  -0.1088 63  PHE H N   
2486 C CA  . PHE B 64  ? 1.1185 1.0980 1.2319 0.0555  0.0512  -0.0962 63  PHE H CA  
2487 C C   . PHE B 64  ? 1.1504 1.1250 1.2280 0.0704  0.0660  -0.1051 63  PHE H C   
2488 O O   . PHE B 64  ? 1.1327 1.1174 1.2191 0.0858  0.0813  -0.0969 63  PHE H O   
2489 C CB  . PHE B 64  ? 1.0722 1.0853 1.2032 0.0542  0.0442  -0.0812 63  PHE H CB  
2490 C CG  . PHE B 64  ? 1.0516 1.0761 1.2300 0.0434  0.0343  -0.0707 63  PHE H CG  
2491 C CD1 . PHE B 64  ? 1.0735 1.0989 1.2644 0.0265  0.0086  -0.0731 63  PHE H CD1 
2492 C CD2 . PHE B 64  ? 1.0187 1.0523 1.2300 0.0496  0.0511  -0.0581 63  PHE H CD2 
2493 C CE1 . PHE B 64  ? 1.0632 1.1053 1.3117 0.0176  0.0004  -0.0619 63  PHE H CE1 
2494 C CE2 . PHE B 64  ? 1.0160 1.0619 1.2774 0.0409  0.0484  -0.0488 63  PHE H CE2 
2495 C CZ  . PHE B 64  ? 1.0364 1.0899 1.3230 0.0257  0.0233  -0.0501 63  PHE H CZ  
2496 N N   . GLN B 65  ? 1.2032 1.1623 1.2409 0.0648  0.0616  -0.1213 64  GLN H N   
2497 C CA  . GLN B 65  ? 1.2201 1.1794 1.2275 0.0779  0.0797  -0.1298 64  GLN H CA  
2498 C C   . GLN B 65  ? 1.2198 1.1662 1.2430 0.0972  0.1005  -0.1322 64  GLN H C   
2499 O O   . GLN B 65  ? 1.2404 1.1554 1.2705 0.0963  0.1010  -0.1392 64  GLN H O   
2500 C CB  . GLN B 65  ? 1.2890 1.2222 1.2430 0.0668  0.0756  -0.1498 64  GLN H CB  
2501 C CG  . GLN B 65  ? 1.3076 1.2468 1.2300 0.0780  0.0984  -0.1569 64  GLN H CG  
2502 C CD  . GLN B 65  ? 1.3706 1.2841 1.2281 0.0632  0.0944  -0.1737 64  GLN H CD  
2503 O OE1 . GLN B 65  ? 1.4044 1.2911 1.2370 0.0444  0.0710  -0.1824 64  GLN H OE1 
2504 N NE2 . GLN B 65  ? 1.3976 1.3186 1.2258 0.0699  0.1170  -0.1779 64  GLN H NE2 
2505 N N   . GLY B 66  ? 1.1826 1.1535 1.2149 0.1137  0.1156  -0.1247 65  GLY H N   
2506 C CA  . GLY B 66  ? 1.1725 1.1394 1.2290 0.1340  0.1302  -0.1204 65  GLY H CA  
2507 C C   . GLY B 66  ? 1.1234 1.1161 1.2095 0.1389  0.1250  -0.0976 65  GLY H C   
2508 O O   . GLY B 66  ? 1.1366 1.1463 1.2396 0.1544  0.1321  -0.0886 65  GLY H O   
2509 N N   . ARG B 67  ? 1.0820 1.0766 1.1746 0.1250  0.1124  -0.0886 66  ARG H N   
2510 C CA  . ARG B 67  ? 1.0408 1.0511 1.1506 0.1269  0.1100  -0.0699 66  ARG H CA  
2511 C C   . ARG B 67  ? 1.0359 1.0773 1.1426 0.1201  0.1041  -0.0635 66  ARG H C   
2512 O O   . ARG B 67  ? 1.0304 1.0885 1.1422 0.1250  0.1047  -0.0520 66  ARG H O   
2513 C CB  . ARG B 67  ? 1.0221 1.0121 1.1440 0.1173  0.1074  -0.0643 66  ARG H CB  
2514 C CG  . ARG B 67  ? 1.0443 0.9974 1.1683 0.1201  0.1122  -0.0707 66  ARG H CG  
2515 C CD  . ARG B 67  ? 1.0329 0.9669 1.1719 0.1135  0.1152  -0.0586 66  ARG H CD  
2516 N NE  . ARG B 67  ? 1.0071 0.9495 1.1625 0.0951  0.1095  -0.0580 66  ARG H NE  
2517 C CZ  . ARG B 67  ? 0.9688 0.9202 1.1392 0.0897  0.1154  -0.0441 66  ARG H CZ  
2518 N NH1 . ARG B 67  ? 0.9580 0.9065 1.1171 0.0989  0.1252  -0.0304 66  ARG H NH1 
2519 N NH2 . ARG B 67  ? 0.9483 0.9106 1.1449 0.0749  0.1114  -0.0440 66  ARG H NH2 
2520 N N   . VAL B 68  ? 1.0546 1.0997 1.1504 0.1079  0.0962  -0.0705 67  VAL H N   
2521 C CA  . VAL B 68  ? 1.0287 1.0967 1.1222 0.1008  0.0893  -0.0632 67  VAL H CA  
2522 C C   . VAL B 68  ? 1.0387 1.1231 1.1151 0.1043  0.0951  -0.0663 67  VAL H C   
2523 O O   . VAL B 68  ? 1.0972 1.1723 1.1541 0.1052  0.1009  -0.0787 67  VAL H O   
2524 C CB  . VAL B 68  ? 1.0309 1.0951 1.1256 0.0862  0.0744  -0.0644 67  VAL H CB  
2525 C CG1 . VAL B 68  ? 1.0272 1.1091 1.1126 0.0799  0.0661  -0.0579 67  VAL H CG1 
2526 C CG2 . VAL B 68  ? 1.0252 1.0844 1.1507 0.0822  0.0725  -0.0571 67  VAL H CG2 
2527 N N   . THR B 69  ? 1.0131 1.1197 1.0961 0.1048  0.0954  -0.0555 68  THR H N   
2528 C CA  . THR B 69  ? 1.0063 1.1325 1.0788 0.1032  0.1004  -0.0549 68  THR H CA  
2529 C C   . THR B 69  ? 0.9709 1.1084 1.0444 0.0933  0.0916  -0.0435 68  THR H C   
2530 O O   . THR B 69  ? 0.9425 1.0841 1.0297 0.0945  0.0892  -0.0356 68  THR H O   
2531 C CB  . THR B 69  ? 1.0097 1.1532 1.0987 0.1157  0.1122  -0.0534 68  THR H CB  
2532 O OG1 . THR B 69  ? 1.0004 1.1506 1.1070 0.1185  0.1052  -0.0419 68  THR H OG1 
2533 C CG2 . THR B 69  ? 1.0394 1.1684 1.1316 0.1287  0.1234  -0.0644 68  THR H CG2 
2534 N N   . ILE B 70  ? 0.9695 1.1064 1.0235 0.0830  0.0864  -0.0429 69  ILE H N   
2535 C CA  . ILE B 70  ? 0.9463 1.0888 1.0010 0.0742  0.0780  -0.0314 69  ILE H CA  
2536 C C   . ILE B 70  ? 0.9525 1.1127 0.9996 0.0703  0.0870  -0.0269 69  ILE H C   
2537 O O   . ILE B 70  ? 0.9726 1.1353 0.9987 0.0678  0.0959  -0.0315 69  ILE H O   
2538 C CB  . ILE B 70  ? 0.9523 1.0814 0.9941 0.0651  0.0625  -0.0289 69  ILE H CB  
2539 C CG1 . ILE B 70  ? 0.9484 1.0654 1.0090 0.0669  0.0537  -0.0327 69  ILE H CG1 
2540 C CG2 . ILE B 70  ? 0.9422 1.0732 0.9878 0.0583  0.0541  -0.0151 69  ILE H CG2 
2541 C CD1 . ILE B 70  ? 0.9705 1.0773 1.0216 0.0571  0.0338  -0.0315 69  ILE H CD1 
2542 N N   . THR B 71  ? 0.9314 1.1019 0.9944 0.0684  0.0860  -0.0187 70  THR H N   
2543 C CA  . THR B 71  ? 0.9321 1.1208 0.9959 0.0607  0.0920  -0.0122 70  THR H CA  
2544 C C   . THR B 71  ? 0.9412 1.1192 0.9999 0.0493  0.0822  -0.0018 70  THR H C   
2545 O O   . THR B 71  ? 0.9483 1.1078 1.0080 0.0506  0.0725  -0.0003 70  THR H O   
2546 C CB  . THR B 71  ? 0.9100 1.1199 0.9999 0.0663  0.0963  -0.0118 70  THR H CB  
2547 O OG1 . THR B 71  ? 0.8928 1.0909 0.9890 0.0676  0.0857  -0.0096 70  THR H OG1 
2548 C CG2 . THR B 71  ? 0.9041 1.1230 1.0047 0.0803  0.1069  -0.0201 70  THR H CG2 
2549 N N   . ALA B 72  ? 0.9596 1.1488 1.0173 0.0383  0.0862  0.0060  71  ALA H N   
2550 C CA  . ALA B 72  ? 0.9749 1.1488 1.0272 0.0271  0.0779  0.0165  71  ALA H CA  
2551 C C   . ALA B 72  ? 0.9942 1.1836 1.0561 0.0141  0.0831  0.0234  71  ALA H C   
2552 O O   . ALA B 72  ? 1.0125 1.2263 1.0793 0.0108  0.0959  0.0240  71  ALA H O   
2553 C CB  . ALA B 72  ? 0.9932 1.1509 1.0201 0.0223  0.0724  0.0234  71  ALA H CB  
2554 N N   . ASP B 73  ? 1.0118 1.1855 1.0787 0.0063  0.0746  0.0278  72  ASP H N   
2555 C CA  . ASP B 73  ? 1.0306 1.2110 1.1051 -0.0109 0.0755  0.0356  72  ASP H CA  
2556 C C   . ASP B 73  ? 1.0481 1.2031 1.1040 -0.0215 0.0733  0.0481  72  ASP H C   
2557 O O   . ASP B 73  ? 1.0471 1.1709 1.0977 -0.0186 0.0641  0.0497  72  ASP H O   
2558 C CB  . ASP B 73  ? 1.0482 1.2208 1.1336 -0.0150 0.0658  0.0305  72  ASP H CB  
2559 C CG  . ASP B 73  ? 1.0865 1.2681 1.1845 -0.0359 0.0629  0.0370  72  ASP H CG  
2560 O OD1 . ASP B 73  ? 1.1231 1.2846 1.2118 -0.0491 0.0634  0.0459  72  ASP H OD1 
2561 O OD2 . ASP B 73  ? 1.1050 1.3131 1.2245 -0.0398 0.0583  0.0345  72  ASP H OD2 
2562 N N   . GLU B 74  ? 1.0563 1.2236 1.1032 -0.0333 0.0834  0.0580  73  GLU H N   
2563 C CA  . GLU B 74  ? 1.0786 1.2203 1.0987 -0.0425 0.0811  0.0732  73  GLU H CA  
2564 C C   . GLU B 74  ? 1.0877 1.2047 1.1142 -0.0572 0.0742  0.0830  73  GLU H C   
2565 O O   . GLU B 74  ? 1.1067 1.1900 1.1176 -0.0589 0.0653  0.0948  73  GLU H O   
2566 C CB  . GLU B 74  ? 1.1021 1.2609 1.1017 -0.0517 0.0985  0.0803  73  GLU H CB  
2567 C CG  . GLU B 74  ? 1.1504 1.2788 1.1072 -0.0591 0.0935  0.0966  73  GLU H CG  
2568 C CD  . GLU B 74  ? 1.1892 1.3269 1.1103 -0.0687 0.1140  0.1021  73  GLU H CD  
2569 O OE1 . GLU B 74  ? 1.2295 1.3389 1.1052 -0.0767 0.1082  0.1171  73  GLU H OE1 
2570 O OE2 . GLU B 74  ? 1.1731 1.3446 1.1109 -0.0677 0.1363  0.0920  73  GLU H OE2 
2571 N N   . SER B 75  ? 1.0682 1.1998 1.1187 -0.0680 0.0762  0.0784  74  SER H N   
2572 C CA  . SER B 75  ? 1.0837 1.1889 1.1386 -0.0855 0.0698  0.0849  74  SER H CA  
2573 C C   . SER B 75  ? 1.0923 1.1567 1.1429 -0.0750 0.0578  0.0767  74  SER H C   
2574 O O   . SER B 75  ? 1.1327 1.1575 1.1747 -0.0797 0.0533  0.0857  74  SER H O   
2575 C CB  . SER B 75  ? 1.0680 1.2019 1.1508 -0.1026 0.0715  0.0817  74  SER H CB  
2576 O OG  . SER B 75  ? 1.0275 1.1790 1.1249 -0.0913 0.0642  0.0659  74  SER H OG  
2577 N N   . THR B 76  ? 1.0659 1.1379 1.1227 -0.0602 0.0552  0.0605  75  THR H N   
2578 C CA  . THR B 76  ? 1.0652 1.1000 1.1174 -0.0499 0.0506  0.0504  75  THR H CA  
2579 C C   . THR B 76  ? 1.0560 1.0772 1.1074 -0.0303 0.0504  0.0540  75  THR H C   
2580 O O   . THR B 76  ? 1.0574 1.0485 1.1126 -0.0196 0.0509  0.0479  75  THR H O   
2581 C CB  . THR B 76  ? 1.0427 1.0874 1.0959 -0.0449 0.0490  0.0336  75  THR H CB  
2582 O OG1 . THR B 76  ? 0.9988 1.0774 1.0587 -0.0300 0.0524  0.0307  75  THR H OG1 
2583 C CG2 . THR B 76  ? 1.0527 1.1099 1.1104 -0.0654 0.0419  0.0311  75  THR H CG2 
2584 N N   . SER B 77  ? 1.0582 1.1011 1.1056 -0.0265 0.0502  0.0632  76  SER H N   
2585 C CA  . SER B 77  ? 1.0754 1.1100 1.1237 -0.0114 0.0439  0.0685  76  SER H CA  
2586 C C   . SER B 77  ? 1.0605 1.1005 1.1235 0.0058  0.0462  0.0534  76  SER H C   
2587 O O   . SER B 77  ? 1.0633 1.0856 1.1421 0.0180  0.0431  0.0543  76  SER H O   
2588 C CB  . SER B 77  ? 1.1045 1.1013 1.1562 -0.0112 0.0360  0.0826  76  SER H CB  
2589 O OG  . SER B 77  ? 1.1428 1.1293 1.1781 -0.0296 0.0351  0.0980  76  SER H OG  
2590 N N   . THR B 78  ? 1.0437 1.1092 1.1057 0.0068  0.0524  0.0414  77  THR H N   
2591 C CA  . THR B 78  ? 1.0259 1.0939 1.0969 0.0204  0.0563  0.0286  77  THR H CA  
2592 C C   . THR B 78  ? 1.0115 1.1081 1.0818 0.0268  0.0573  0.0249  77  THR H C   
2593 O O   . THR B 78  ? 1.0008 1.1205 1.0660 0.0216  0.0609  0.0236  77  THR H O   
2594 C CB  . THR B 78  ? 1.0256 1.0868 1.0908 0.0158  0.0605  0.0179  77  THR H CB  
2595 O OG1 . THR B 78  ? 1.0579 1.0865 1.1174 0.0069  0.0601  0.0192  77  THR H OG1 
2596 C CG2 . THR B 78  ? 1.0088 1.0636 1.0749 0.0284  0.0669  0.0070  77  THR H CG2 
2597 N N   . ALA B 79  ? 1.0152 1.1093 1.0949 0.0380  0.0547  0.0232  78  ALA H N   
2598 C CA  . ALA B 79  ? 0.9984 1.1107 1.0764 0.0441  0.0556  0.0169  78  ALA H CA  
2599 C C   . ALA B 79  ? 0.9808 1.0935 1.0681 0.0528  0.0633  0.0064  78  ALA H C   
2600 O O   . ALA B 79  ? 0.9768 1.0722 1.0725 0.0564  0.0675  0.0043  78  ALA H O   
2601 C CB  . ALA B 79  ? 1.0034 1.1112 1.0853 0.0472  0.0446  0.0216  78  ALA H CB  
2602 N N   . TYR B 80  ? 0.9720 1.1012 1.0554 0.0564  0.0669  0.0003  79  TYR H N   
2603 C CA  . TYR B 80  ? 0.9765 1.1039 1.0645 0.0644  0.0724  -0.0063 79  TYR H CA  
2604 C C   . TYR B 80  ? 0.9896 1.1210 1.0819 0.0714  0.0732  -0.0114 79  TYR H C   
2605 O O   . TYR B 80  ? 1.0156 1.1558 1.0999 0.0697  0.0713  -0.0128 79  TYR H O   
2606 C CB  . TYR B 80  ? 0.9699 1.1104 1.0532 0.0626  0.0733  -0.0070 79  TYR H CB  
2607 C CG  . TYR B 80  ? 0.9797 1.1153 1.0568 0.0515  0.0695  -0.0034 79  TYR H CG  
2608 C CD1 . TYR B 80  ? 0.9973 1.1070 1.0639 0.0496  0.0703  -0.0060 79  TYR H CD1 
2609 C CD2 . TYR B 80  ? 0.9847 1.1385 1.0650 0.0415  0.0671  0.0015  79  TYR H CD2 
2610 C CE1 . TYR B 80  ? 1.0191 1.1172 1.0750 0.0374  0.0658  -0.0053 79  TYR H CE1 
2611 C CE2 . TYR B 80  ? 0.9994 1.1464 1.0759 0.0282  0.0620  0.0046  79  TYR H CE2 
2612 C CZ  . TYR B 80  ? 1.0174 1.1344 1.0799 0.0259  0.0598  0.0003  79  TYR H CZ  
2613 O OH  . TYR B 80  ? 1.0517 1.1550 1.1055 0.0108  0.0538  0.0009  79  TYR H OH  
2614 N N   . MET B 81  ? 0.9963 1.1169 1.0974 0.0777  0.0776  -0.0147 80  MET H N   
2615 C CA  . MET B 81  ? 1.0033 1.1230 1.1091 0.0829  0.0786  -0.0201 80  MET H CA  
2616 C C   . MET B 81  ? 0.9987 1.1114 1.1033 0.0896  0.0861  -0.0213 80  MET H C   
2617 O O   . MET B 81  ? 1.0053 1.1046 1.1093 0.0897  0.0918  -0.0186 80  MET H O   
2618 C CB  . MET B 81  ? 1.0092 1.1206 1.1335 0.0812  0.0744  -0.0198 80  MET H CB  
2619 C CG  . MET B 81  ? 1.0185 1.1246 1.1480 0.0829  0.0740  -0.0264 80  MET H CG  
2620 S SD  . MET B 81  ? 1.0321 1.1272 1.1944 0.0830  0.0804  -0.0242 80  MET H SD  
2621 C CE  . MET B 81  ? 1.0267 1.1098 1.1737 0.0898  0.0978  -0.0224 80  MET H CE  
2622 N N   . GLU B 82  ? 0.9896 1.1078 1.0916 0.0958  0.0873  -0.0247 81  GLU H N   
2623 C CA  . GLU B 82  ? 0.9859 1.0951 1.0869 0.1035  0.0911  -0.0227 81  GLU H CA  
2624 C C   . GLU B 82  ? 0.9793 1.0735 1.0873 0.1076  0.0950  -0.0277 81  GLU H C   
2625 O O   . GLU B 82  ? 0.9840 1.0806 1.0926 0.1090  0.0943  -0.0356 81  GLU H O   
2626 C CB  . GLU B 82  ? 0.9960 1.1229 1.0981 0.1093  0.0883  -0.0201 81  GLU H CB  
2627 C CG  . GLU B 82  ? 1.0176 1.1352 1.1171 0.1169  0.0858  -0.0129 81  GLU H CG  
2628 C CD  . GLU B 82  ? 1.0238 1.1642 1.1369 0.1240  0.0789  -0.0076 81  GLU H CD  
2629 O OE1 . GLU B 82  ? 1.0196 1.1850 1.1471 0.1232  0.0813  -0.0110 81  GLU H OE1 
2630 O OE2 . GLU B 82  ? 1.0437 1.1771 1.1544 0.1298  0.0712  0.0015  81  GLU H OE2 
2631 N N   . LEU B 83  ? 0.9619 1.0368 1.0715 0.1078  0.1005  -0.0236 82  LEU H N   
2632 C CA  . LEU B 83  ? 0.9611 1.0179 1.0796 0.1092  0.1047  -0.0266 82  LEU H CA  
2633 C C   . LEU B 83  ? 0.9739 1.0135 1.0829 0.1172  0.1091  -0.0186 82  LEU H C   
2634 O O   . LEU B 83  ? 0.9761 1.0059 1.0713 0.1155  0.1131  -0.0097 82  LEU H O   
2635 C CB  . LEU B 83  ? 0.9539 1.0035 1.0898 0.1000  0.1089  -0.0258 82  LEU H CB  
2636 C CG  . LEU B 83  ? 0.9630 0.9944 1.1146 0.0966  0.1126  -0.0280 82  LEU H CG  
2637 C CD1 . LEU B 83  ? 0.9718 1.0041 1.1267 0.0931  0.1011  -0.0399 82  LEU H CD1 
2638 C CD2 . LEU B 83  ? 0.9570 0.9861 1.1350 0.0880  0.1214  -0.0230 82  LEU H CD2 
2639 N N   . SER B 84  A 0.9862 1.0178 1.0991 0.1261  0.1085  -0.0219 82  SER H N   
2640 C CA  . SER B 84  A 1.0032 1.0177 1.1104 0.1364  0.1090  -0.0117 82  SER H CA  
2641 C C   . SER B 84  A 1.0338 1.0159 1.1464 0.1355  0.1162  -0.0121 82  SER H C   
2642 O O   . SER B 84  A 1.0225 0.9995 1.1464 0.1267  0.1186  -0.0228 82  SER H O   
2643 C CB  . SER B 84  A 0.9864 1.0172 1.1022 0.1502  0.1036  -0.0124 82  SER H CB  
2644 O OG  . SER B 84  A 0.9794 1.0113 1.1054 0.1535  0.1089  -0.0278 82  SER H OG  
2645 N N   . SER B 85  B 1.0671 1.0258 1.1711 0.1432  0.1170  0.0009  82  SER H N   
2646 C CA  . SER B 85  B 1.0963 1.0185 1.2032 0.1413  0.1249  0.0045  82  SER H CA  
2647 C C   . SER B 85  B 1.1029 1.0183 1.2142 0.1236  0.1356  0.0042  82  SER H C   
2648 O O   . SER B 85  B 1.1128 1.0190 1.2438 0.1148  0.1387  -0.0050 82  SER H O   
2649 C CB  . SER B 85  B 1.1033 1.0135 1.2262 0.1480  0.1250  -0.0095 82  SER H CB  
2650 O OG  . SER B 85  B 1.1054 1.0234 1.2330 0.1672  0.1202  -0.0083 82  SER H OG  
2651 N N   . LEU B 86  C 1.1073 1.0265 1.2014 0.1182  0.1414  0.0141  82  LEU H N   
2652 C CA  . LEU B 86  C 1.1066 1.0256 1.2117 0.1040  0.1562  0.0141  82  LEU H CA  
2653 C C   . LEU B 86  C 1.1466 1.0319 1.2554 0.0966  0.1714  0.0238  82  LEU H C   
2654 O O   . LEU B 86  C 1.1667 1.0234 1.2467 0.1012  0.1746  0.0383  82  LEU H O   
2655 C CB  . LEU B 86  C 1.1029 1.0285 1.1818 0.1023  0.1621  0.0197  82  LEU H CB  
2656 C CG  . LEU B 86  C 1.0655 1.0231 1.1465 0.1048  0.1499  0.0103  82  LEU H CG  
2657 C CD1 . LEU B 86  C 1.0738 1.0271 1.1223 0.1020  0.1558  0.0149  82  LEU H CD1 
2658 C CD2 . LEU B 86  C 1.0313 1.0107 1.1501 0.0986  0.1490  -0.0010 82  LEU H CD2 
2659 N N   . ARG B 87  ? 1.1574 1.0468 1.3039 0.0840  0.1788  0.0175  83  ARG H N   
2660 C CA  . ARG B 87  ? 1.2143 1.0766 1.3748 0.0723  0.1963  0.0268  83  ARG H CA  
2661 C C   . ARG B 87  ? 1.2009 1.0766 1.3831 0.0608  0.2184  0.0307  83  ARG H C   
2662 O O   . ARG B 87  ? 1.1665 1.0692 1.3528 0.0636  0.2176  0.0249  83  ARG H O   
2663 C CB  . ARG B 87  ? 1.2436 1.0987 1.4384 0.0645  0.1863  0.0161  83  ARG H CB  
2664 C CG  . ARG B 87  ? 1.2794 1.1106 1.4545 0.0768  0.1727  0.0116  83  ARG H CG  
2665 C CD  . ARG B 87  ? 1.3234 1.1271 1.5222 0.0656  0.1705  0.0041  83  ARG H CD  
2666 N NE  . ARG B 87  ? 1.3901 1.1604 1.5935 0.0549  0.1887  0.0210  83  ARG H NE  
2667 C CZ  . ARG B 87  ? 1.4168 1.1906 1.6569 0.0340  0.2013  0.0245  83  ARG H CZ  
2668 N NH1 . ARG B 87  ? 1.3922 1.2035 1.6712 0.0230  0.1938  0.0129  83  ARG H NH1 
2669 N NH2 . ARG B 87  ? 1.4566 1.1973 1.6971 0.0240  0.2214  0.0417  83  ARG H NH2 
2670 N N   . SER B 88  ? 1.2263 1.0818 1.4260 0.0482  0.2405  0.0408  84  SER H N   
2671 C CA  . SER B 88  ? 1.2264 1.0941 1.4559 0.0378  0.2685  0.0453  84  SER H CA  
2672 C C   . SER B 88  ? 1.1841 1.0942 1.4809 0.0318  0.2579  0.0335  84  SER H C   
2673 O O   . SER B 88  ? 1.1809 1.1129 1.5069 0.0304  0.2752  0.0342  84  SER H O   
2674 C CB  . SER B 88  ? 1.2751 1.1125 1.5126 0.0241  0.2960  0.0601  84  SER H CB  
2675 O OG  . SER B 88  ? 1.3299 1.1251 1.4980 0.0293  0.3059  0.0748  84  SER H OG  
2676 N N   . GLU B 89  ? 1.1643 1.0826 1.4835 0.0285  0.2291  0.0229  85  GLU H N   
2677 C CA  . GLU B 89  ? 1.1355 1.0898 1.5121 0.0205  0.2109  0.0135  85  GLU H CA  
2678 C C   . GLU B 89  ? 1.0856 1.0670 1.4483 0.0330  0.1950  0.0058  85  GLU H C   
2679 O O   . GLU B 89  ? 1.0691 1.0811 1.4756 0.0287  0.1806  0.0019  85  GLU H O   
2680 C CB  . GLU B 89  ? 1.1638 1.1081 1.5544 0.0098  0.1849  0.0035  85  GLU H CB  
2681 C CG  . GLU B 89  ? 1.1884 1.1189 1.5270 0.0222  0.1627  -0.0086 85  GLU H CG  
2682 C CD  . GLU B 89  ? 1.2327 1.1439 1.5756 0.0118  0.1413  -0.0221 85  GLU H CD  
2683 O OE1 . GLU B 89  ? 1.2426 1.1687 1.5833 0.0098  0.1165  -0.0358 85  GLU H OE1 
2684 O OE2 . GLU B 89  ? 1.2812 1.1577 1.6243 0.0047  0.1498  -0.0190 85  GLU H OE2 
2685 N N   . ASP B 90  ? 1.0690 0.9699 1.0844 0.0939  0.1789  0.0253  86  ASP H N   
2686 C CA  . ASP B 90  ? 1.0166 0.9514 1.0475 0.0904  0.1674  0.0253  86  ASP H CA  
2687 C C   . ASP B 90  ? 0.9867 0.9297 1.0201 0.0813  0.1611  0.0264  86  ASP H C   
2688 O O   . ASP B 90  ? 0.9625 0.9298 1.0063 0.0765  0.1529  0.0262  86  ASP H O   
2689 C CB  . ASP B 90  ? 1.0140 0.9688 1.0453 0.1046  0.1624  0.0315  86  ASP H CB  
2690 C CG  . ASP B 90  ? 1.0228 0.9705 1.0517 0.1146  0.1687  0.0306  86  ASP H CG  
2691 O OD1 . ASP B 90  ? 1.0161 0.9635 1.0529 0.1069  0.1710  0.0237  86  ASP H OD1 
2692 O OD2 . ASP B 90  ? 1.0391 0.9817 1.0569 0.1310  0.1714  0.0369  86  ASP H OD2 
2693 N N   . THR B 91  ? 0.9854 0.9063 1.0079 0.0788  0.1663  0.0273  87  THR H N   
2694 C CA  . THR B 91  ? 0.9612 0.8855 0.9854 0.0689  0.1624  0.0269  87  THR H CA  
2695 C C   . THR B 91  ? 0.9345 0.8652 0.9721 0.0558  0.1617  0.0189  87  THR H C   
2696 O O   . THR B 91  ? 0.9369 0.8530 0.9755 0.0504  0.1689  0.0128  87  THR H O   
2697 C CB  . THR B 91  ? 0.9846 0.8818 0.9929 0.0698  0.1698  0.0295  87  THR H CB  
2698 O OG1 . THR B 91  ? 1.0017 0.8934 0.9950 0.0851  0.1700  0.0377  87  THR H OG1 
2699 C CG2 . THR B 91  ? 0.9754 0.8750 0.9843 0.0603  0.1665  0.0291  87  THR H CG2 
2700 N N   . ALA B 92  ? 0.9067 0.8596 0.9538 0.0510  0.1535  0.0186  88  ALA H N   
2701 C CA  . ALA B 92  ? 0.8877 0.8482 0.9454 0.0421  0.1523  0.0124  88  ALA H CA  
2702 C C   . ALA B 92  ? 0.8792 0.8572 0.9410 0.0373  0.1451  0.0141  88  ALA H C   
2703 O O   . ALA B 92  ? 0.8966 0.8841 0.9554 0.0397  0.1408  0.0188  88  ALA H O   
2704 C CB  . ALA B 92  ? 0.8897 0.8548 0.9536 0.0448  0.1539  0.0083  88  ALA H CB  
2705 N N   . VAL B 93  ? 0.8642 0.8461 0.9318 0.0308  0.1443  0.0097  89  VAL H N   
2706 C CA  . VAL B 93  ? 0.8550 0.8486 0.9239 0.0260  0.1399  0.0108  89  VAL H CA  
2707 C C   . VAL B 93  ? 0.8519 0.8591 0.9267 0.0280  0.1383  0.0098  89  VAL H C   
2708 O O   . VAL B 93  ? 0.8538 0.8603 0.9322 0.0289  0.1399  0.0056  89  VAL H O   
2709 C CB  . VAL B 93  ? 0.8560 0.8433 0.9244 0.0201  0.1411  0.0078  89  VAL H CB  
2710 C CG1 . VAL B 93  ? 0.8496 0.8438 0.9159 0.0159  0.1386  0.0091  89  VAL H CG1 
2711 C CG2 . VAL B 93  ? 0.8662 0.8401 0.9289 0.0177  0.1437  0.0086  89  VAL H CG2 
2712 N N   . TYR B 94  ? 0.8617 0.8824 0.9372 0.0282  0.1353  0.0130  90  TYR H N   
2713 C CA  . TYR B 94  ? 0.8597 0.8939 0.9404 0.0299  0.1348  0.0123  90  TYR H CA  
2714 C C   . TYR B 94  ? 0.8502 0.8879 0.9293 0.0225  0.1348  0.0116  90  TYR H C   
2715 O O   . TYR B 94  ? 0.8510 0.8917 0.9268 0.0161  0.1338  0.0131  90  TYR H O   
2716 C CB  . TYR B 94  ? 0.8733 0.9226 0.9568 0.0351  0.1328  0.0153  90  TYR H CB  
2717 C CG  . TYR B 94  ? 0.8923 0.9349 0.9744 0.0453  0.1345  0.0168  90  TYR H CG  
2718 C CD1 . TYR B 94  ? 0.9003 0.9291 0.9750 0.0477  0.1353  0.0190  90  TYR H CD1 
2719 C CD2 . TYR B 94  ? 0.8961 0.9428 0.9816 0.0529  0.1366  0.0161  90  TYR H CD2 
2720 C CE1 . TYR B 94  ? 0.9135 0.9308 0.9830 0.0576  0.1389  0.0208  90  TYR H CE1 
2721 C CE2 . TYR B 94  ? 0.9045 0.9405 0.9856 0.0629  0.1400  0.0176  90  TYR H CE2 
2722 C CZ  . TYR B 94  ? 0.9152 0.9354 0.9876 0.0653  0.1415  0.0201  90  TYR H CZ  
2723 O OH  . TYR B 94  ? 0.9439 0.9486 1.0084 0.0756  0.1467  0.0220  90  TYR H OH  
2724 N N   . TYR B 95  ? 0.8501 0.8860 0.9296 0.0237  0.1366  0.0090  91  TYR H N   
2725 C CA  . TYR B 95  ? 0.8524 0.8871 0.9266 0.0191  0.1382  0.0089  91  TYR H CA  
2726 C C   . TYR B 95  ? 0.8454 0.8915 0.9217 0.0194  0.1398  0.0091  91  TYR H C   
2727 O O   . TYR B 95  ? 0.8457 0.8998 0.9281 0.0251  0.1395  0.0083  91  TYR H O   
2728 C CB  . TYR B 95  ? 0.8573 0.8824 0.9280 0.0221  0.1390  0.0061  91  TYR H CB  
2729 C CG  . TYR B 95  ? 0.8649 0.8799 0.9334 0.0208  0.1387  0.0052  91  TYR H CG  
2730 C CD1 . TYR B 95  ? 0.8724 0.8799 0.9335 0.0155  0.1397  0.0077  91  TYR H CD1 
2731 C CD2 . TYR B 95  ? 0.8698 0.8821 0.9430 0.0240  0.1385  0.0013  91  TYR H CD2 
2732 C CE1 . TYR B 95  ? 0.8739 0.8722 0.9328 0.0148  0.1401  0.0069  91  TYR H CE1 
2733 C CE2 . TYR B 95  ? 0.8752 0.8798 0.9475 0.0222  0.1392  0.0000  91  TYR H CE2 
2734 C CZ  . TYR B 95  ? 0.8731 0.8709 0.9383 0.0183  0.1398  0.0031  91  TYR H CZ  
2735 O OH  . TYR B 95  ? 0.8850 0.8754 0.9492 0.0171  0.1411  0.0017  91  TYR H OH  
2736 N N   . CYS B 96  ? 0.8512 0.8959 0.9209 0.0131  0.1428  0.0100  92  CYS H N   
2737 C CA  . CYS B 96  ? 0.8530 0.9032 0.9212 0.0127  0.1466  0.0097  92  CYS H CA  
2738 C C   . CYS B 96  ? 0.8525 0.8871 0.9074 0.0132  0.1504  0.0101  92  CYS H C   
2739 O O   . CYS B 96  ? 0.8736 0.8957 0.9216 0.0123  0.1502  0.0108  92  CYS H O   
2740 C CB  . CYS B 96  ? 0.8595 0.9228 0.9307 0.0040  0.1490  0.0101  92  CYS H CB  
2741 S SG  . CYS B 96  ? 0.8897 0.9418 0.9501 -0.0088 0.1523  0.0104  92  CYS H SG  
2742 N N   . ALA B 97  ? 0.8403 0.8752 0.8904 0.0159  0.1541  0.0100  93  ALA H N   
2743 C CA  . ALA B 97  ? 0.8579 0.8774 0.8925 0.0194  0.1579  0.0112  93  ALA H CA  
2744 C C   . ALA B 97  ? 0.8786 0.8982 0.9060 0.0195  0.1641  0.0120  93  ALA H C   
2745 O O   . ALA B 97  ? 0.8571 0.8910 0.8942 0.0200  0.1640  0.0106  93  ALA H O   
2746 C CB  . ALA B 97  ? 0.8478 0.8652 0.8826 0.0295  0.1530  0.0089  93  ALA H CB  
2747 N N   . ARG B 98  ? 0.9218 0.9238 0.9305 0.0199  0.1706  0.0145  94  ARG H N   
2748 C CA  . ARG B 98  ? 0.9535 0.9506 0.9509 0.0207  0.1782  0.0158  94  ARG H CA  
2749 C C   . ARG B 98  ? 0.9562 0.9563 0.9511 0.0341  0.1744  0.0145  94  ARG H C   
2750 O O   . ARG B 98  ? 0.9629 0.9567 0.9507 0.0434  0.1704  0.0143  94  ARG H O   
2751 C CB  . ARG B 98  ? 0.9913 0.9634 0.9652 0.0174  0.1881  0.0194  94  ARG H CB  
2752 C CG  . ARG B 98  ? 1.0230 0.9869 0.9832 0.0157  0.1988  0.0210  94  ARG H CG  
2753 C CD  . ARG B 98  ? 1.0677 1.0009 0.9999 0.0139  0.2106  0.0252  94  ARG H CD  
2754 N NE  . ARG B 98  ? 1.0917 1.0084 1.0055 0.0303  0.2085  0.0286  94  ARG H NE  
2755 C CZ  . ARG B 98  ? 1.1419 1.0289 1.0268 0.0350  0.2185  0.0335  94  ARG H CZ  
2756 N NH1 . ARG B 98  ? 1.1726 1.0397 1.0425 0.0224  0.2328  0.0351  94  ARG H NH1 
2757 N NH2 . ARG B 98  ? 1.1617 1.0390 1.0318 0.0525  0.2148  0.0364  94  ARG H NH2 
2758 N N   . GLY B 99  ? 0.9474 0.9591 0.9483 0.0349  0.1758  0.0130  95  GLY H N   
2759 C CA  . GLY B 99  ? 0.9423 0.9572 0.9397 0.0464  0.1730  0.0109  95  GLY H CA  
2760 C C   . GLY B 99  ? 0.9642 0.9617 0.9367 0.0534  0.1791  0.0140  95  GLY H C   
2761 O O   . GLY B 99  ? 0.9854 0.9709 0.9454 0.0476  0.1892  0.0175  95  GLY H O   
2762 N N   . LEU B 100 ? 0.9680 0.9647 0.9327 0.0660  0.1735  0.0123  96  LEU H N   
2763 C CA  . LEU B 100 ? 0.9904 0.9720 0.9295 0.0767  0.1778  0.0154  96  LEU H CA  
2764 C C   . LEU B 100 ? 0.9866 0.9779 0.9232 0.0857  0.1752  0.0118  96  LEU H C   
2765 O O   . LEU B 100 ? 0.9590 0.9675 0.9139 0.0840  0.1697  0.0062  96  LEU H O   
2766 C CB  . LEU B 100 ? 0.9991 0.9739 0.9285 0.0862  0.1730  0.0162  96  LEU H CB  
2767 C CG  . LEU B 100 ? 1.0121 0.9703 0.9354 0.0798  0.1779  0.0209  96  LEU H CG  
2768 C CD1 . LEU B 100 ? 1.0300 0.9787 0.9369 0.0936  0.1754  0.0229  96  LEU H CD1 
2769 C CD2 . LEU B 100 ? 1.0304 0.9689 0.9389 0.0703  0.1914  0.0261  96  LEU H CD2 
2770 N N   . GLY B 101 ? 1.0189 0.9966 0.9300 0.0959  0.1801  0.0151  97  GLY H N   
2771 C CA  . GLY B 101 ? 1.0239 1.0077 0.9266 0.1057  0.1787  0.0122  97  GLY H CA  
2772 C C   . GLY B 101 ? 1.0491 1.0106 0.9206 0.1125  0.1896  0.0188  97  GLY H C   
2773 O O   . GLY B 101 ? 1.0572 0.9973 0.9133 0.1097  0.1984  0.0253  97  GLY H O   
2774 N N   . TYR B 102 ? 1.0703 1.0346 0.9305 0.1211  0.1901  0.0170  98  TYR H N   
2775 C CA  . TYR B 102 ? 1.1085 1.0499 0.9358 0.1293  0.2010  0.0235  98  TYR H CA  
2776 C C   . TYR B 102 ? 1.0999 1.0272 0.9256 0.1145  0.2163  0.0279  98  TYR H C   
2777 O O   . TYR B 102 ? 1.1236 1.0241 0.9221 0.1158  0.2291  0.0348  98  TYR H O   
2778 C CB  . TYR B 102 ? 1.1360 1.0855 0.9516 0.1423  0.1970  0.0197  98  TYR H CB  
2779 C CG  . TYR B 102 ? 1.1952 1.1195 0.9733 0.1530  0.2084  0.0268  98  TYR H CG  
2780 C CD1 . TYR B 102 ? 1.2290 1.1308 0.9782 0.1651  0.2120  0.0341  98  TYR H CD1 
2781 C CD2 . TYR B 102 ? 1.2272 1.1478 0.9969 0.1516  0.2168  0.0269  98  TYR H CD2 
2782 C CE1 . TYR B 102 ? 1.2808 1.1550 0.9916 0.1760  0.2240  0.0416  98  TYR H CE1 
2783 C CE2 . TYR B 102 ? 1.2705 1.1652 1.0034 0.1612  0.2287  0.0338  98  TYR H CE2 
2784 C CZ  . TYR B 102 ? 1.3050 1.1752 1.0073 0.1736  0.2325  0.0415  98  TYR H CZ  
2785 O OH  . TYR B 102 ? 1.3844 1.2248 1.0465 0.1845  0.2457  0.0492  98  TYR H OH  
2786 N N   . TYR B 103 ? 1.0690 1.0148 0.9231 0.1008  0.2156  0.0235  99  TYR H N   
2787 C CA  . TYR B 103 ? 1.0711 1.0123 0.9299 0.0854  0.2287  0.0256  99  TYR H CA  
2788 C C   . TYR B 103 ? 1.0647 1.0117 0.9440 0.0711  0.2274  0.0251  99  TYR H C   
2789 O O   . TYR B 103 ? 1.0579 1.0141 0.9503 0.0732  0.2159  0.0230  99  TYR H O   
2790 C CB  . TYR B 103 ? 1.0489 1.0087 0.9227 0.0827  0.2297  0.0211  99  TYR H CB  
2791 C CG  . TYR B 103 ? 1.0553 1.0094 0.9081 0.0965  0.2310  0.0209  99  TYR H CG  
2792 C CD1 . TYR B 103 ? 1.0833 1.0126 0.9045 0.1004  0.2443  0.0266  99  TYR H CD1 
2793 C CD2 . TYR B 103 ? 1.0350 1.0066 0.8969 0.1055  0.2195  0.0146  99  TYR H CD2 
2794 C CE1 . TYR B 103 ? 1.1029 1.0264 0.9022 0.1141  0.2453  0.0267  99  TYR H CE1 
2795 C CE2 . TYR B 103 ? 1.0540 1.0214 0.8955 0.1180  0.2201  0.0134  99  TYR H CE2 
2796 C CZ  . TYR B 103 ? 1.0886 1.0327 0.8987 0.1229  0.2325  0.0198  99  TYR H CZ  
2797 O OH  . TYR B 103 ? 1.1121 1.0516 0.8996 0.1363  0.2330  0.0189  99  TYR H OH  
2798 N N   . LEU B 104 ? 1.0876 1.0302 0.9693 0.0558  0.2396  0.0264  100 LEU H N   
2799 C CA  . LEU B 104 ? 1.0901 1.0369 0.9872 0.0410  0.2401  0.0256  100 LEU H CA  
2800 C C   . LEU B 104 ? 1.0551 1.0347 0.9871 0.0345  0.2311  0.0201  100 LEU H C   
2801 O O   . LEU B 104 ? 1.0355 1.0238 0.9831 0.0251  0.2274  0.0187  100 LEU H O   
2802 C CB  . LEU B 104 ? 1.1278 1.0572 1.0114 0.0264  0.2580  0.0277  100 LEU H CB  
2803 C CG  . LEU B 104 ? 1.1716 1.0626 1.0157 0.0331  0.2705  0.0341  100 LEU H CG  
2804 C CD1 . LEU B 104 ? 1.1947 1.0661 1.0269 0.0147  0.2894  0.0349  100 LEU H CD1 
2805 C CD2 . LEU B 104 ? 1.1777 1.0528 1.0071 0.0466  0.2624  0.0378  100 LEU H CD2 
2806 N N   . TYR B 105 A 1.0464 1.0424 0.9882 0.0406  0.2281  0.0172  100 TYR H N   
2807 C CA  . TYR B 105 A 1.0198 1.0439 0.9909 0.0382  0.2204  0.0127  100 TYR H CA  
2808 C C   . TYR B 105 A 1.0038 1.0338 0.9826 0.0491  0.2063  0.0103  100 TYR H C   
2809 O O   . TYR B 105 A 0.9827 1.0309 0.9824 0.0490  0.1998  0.0070  100 TYR H O   
2810 C CB  . TYR B 105 A 1.0214 1.0587 0.9984 0.0381  0.2270  0.0106  100 TYR H CB  
2811 C CG  . TYR B 105 A 1.0374 1.0642 0.9959 0.0505  0.2289  0.0109  100 TYR H CG  
2812 C CD1 . TYR B 105 A 1.0340 1.0645 0.9937 0.0628  0.2180  0.0080  100 TYR H CD1 
2813 C CD2 . TYR B 105 A 1.0593 1.0722 0.9980 0.0492  0.2424  0.0134  100 TYR H CD2 
2814 C CE1 . TYR B 105 A 1.0513 1.0742 0.9934 0.0739  0.2191  0.0071  100 TYR H CE1 
2815 C CE2 . TYR B 105 A 1.0779 1.0810 0.9974 0.0613  0.2440  0.0137  100 TYR H CE2 
2816 C CZ  . TYR B 105 A 1.0717 1.0810 0.9932 0.0739  0.2317  0.0103  100 TYR H CZ  
2817 O OH  . TYR B 105 A 1.0849 1.0867 0.9870 0.0857  0.2325  0.0095  100 TYR H OH  
2818 N N   . SER B 106 B 1.0150 1.0296 0.9760 0.0586  0.2025  0.0115  100 SER H N   
2819 C CA  . SER B 106 B 1.0002 1.0214 0.9672 0.0680  0.1905  0.0076  100 SER H CA  
2820 C C   . SER B 106 B 0.9765 1.0022 0.9583 0.0628  0.1833  0.0070  100 SER H C   
2821 O O   . SER B 106 B 0.9717 0.9877 0.9489 0.0562  0.1866  0.0106  100 SER H O   
2822 C CB  . SER B 106 B 1.0199 1.0284 0.9640 0.0803  0.1886  0.0082  100 SER H CB  
2823 O OG  . SER B 106 B 1.0472 1.0501 0.9751 0.0858  0.1955  0.0090  100 SER H OG  
2824 N N   . SER B 107 C 0.9642 1.0023 0.9619 0.0655  0.1747  0.0022  100 SER H N   
2825 C CA  . SER B 107 C 0.9499 0.9908 0.9598 0.0622  0.1680  0.0012  100 SER H CA  
2826 C C   . SER B 107 C 0.9390 0.9854 0.9541 0.0691  0.1599  -0.0049 100 SER H C   
2827 O O   . SER B 107 C 0.9318 0.9866 0.9615 0.0678  0.1572  -0.0085 100 SER H O   
2828 C CB  . SER B 107 C 0.9303 0.9818 0.9579 0.0536  0.1687  0.0021  100 SER H CB  
2829 O OG  . SER B 107 C 0.9306 0.9941 0.9695 0.0565  0.1682  -0.0009 100 SER H OG  
2830 N N   . TYR B 108 D 0.9461 0.9877 0.9482 0.0766  0.1568  -0.0065 100 TYR H N   
2831 C CA  . TYR B 108 D 0.9450 0.9947 0.9516 0.0820  0.1494  -0.0143 100 TYR H CA  
2832 C C   . TYR B 108 D 0.9334 0.9829 0.9449 0.0807  0.1444  -0.0151 100 TYR H C   
2833 O O   . TYR B 108 D 0.9136 0.9697 0.9392 0.0774  0.1404  -0.0205 100 TYR H O   
2834 C CB  . TYR B 108 D 0.9679 1.0183 0.9578 0.0925  0.1482  -0.0172 100 TYR H CB  
2835 C CG  . TYR B 108 D 0.9939 1.0413 0.9744 0.0944  0.1547  -0.0152 100 TYR H CG  
2836 C CD1 . TYR B 108 D 0.9945 1.0472 0.9872 0.0897  0.1577  -0.0170 100 TYR H CD1 
2837 C CD2 . TYR B 108 D 1.0259 1.0641 0.9836 0.1023  0.1585  -0.0113 100 TYR H CD2 
2838 C CE1 . TYR B 108 D 1.0061 1.0573 0.9910 0.0916  0.1643  -0.0154 100 TYR H CE1 
2839 C CE2 . TYR B 108 D 1.0434 1.0777 0.9915 0.1038  0.1656  -0.0095 100 TYR H CE2 
2840 C CZ  . TYR B 108 D 1.0335 1.0755 0.9964 0.0979  0.1684  -0.0120 100 TYR H CZ  
2841 O OH  . TYR B 108 D 1.0452 1.0848 0.9996 0.0994  0.1761  -0.0106 100 TYR H OH  
2842 N N   . TYR B 109 E 0.9363 0.9760 0.9345 0.0835  0.1460  -0.0096 100 TYR H N   
2843 C CA  . TYR B 109 E 0.9387 0.9764 0.9394 0.0830  0.1428  -0.0091 100 TYR H CA  
2844 C C   . TYR B 109 E 0.9536 0.9769 0.9492 0.0761  0.1488  -0.0011 100 TYR H C   
2845 O O   . TYR B 109 E 0.9665 0.9825 0.9549 0.0724  0.1556  0.0033  100 TYR H O   
2846 C CB  . TYR B 109 E 0.9422 0.9829 0.9303 0.0953  0.1386  -0.0115 100 TYR H CB  
2847 C CG  . TYR B 109 E 0.9571 0.9881 0.9213 0.1054  0.1426  -0.0068 100 TYR H CG  
2848 C CD1 . TYR B 109 E 0.9605 0.9970 0.9189 0.1102  0.1426  -0.0099 100 TYR H CD1 
2849 C CD2 . TYR B 109 E 0.9629 0.9762 0.9075 0.1106  0.1476  0.0009  100 TYR H CD2 
2850 C CE1 . TYR B 109 E 0.9768 1.0023 0.9107 0.1200  0.1472  -0.0050 100 TYR H CE1 
2851 C CE2 . TYR B 109 E 0.9862 0.9862 0.9051 0.1206  0.1531  0.0061  100 TYR H CE2 
2852 C CZ  . TYR B 109 E 0.9896 0.9961 0.9031 0.1255  0.1527  0.0032  100 TYR H CZ  
2853 O OH  . TYR B 109 E 1.0079 0.9996 0.8937 0.1361  0.1588  0.0086  100 TYR H OH  
2854 N N   . PHE B 110 F 0.9514 0.9714 0.9510 0.0733  0.1470  -0.0002 100 PHE H N   
2855 C CA  . PHE B 110 F 0.9543 0.9622 0.9517 0.0643  0.1521  0.0055  100 PHE H CA  
2856 C C   . PHE B 110 F 0.9543 0.9508 0.9409 0.0683  0.1525  0.0080  100 PHE H C   
2857 O O   . PHE B 110 F 0.9518 0.9563 0.9455 0.0729  0.1467  0.0039  100 PHE H O   
2858 C CB  . PHE B 110 F 0.9426 0.9588 0.9594 0.0542  0.1500  0.0038  100 PHE H CB  
2859 C CG  . PHE B 110 F 0.9490 0.9777 0.9775 0.0538  0.1486  0.0004  100 PHE H CG  
2860 C CD1 . PHE B 110 F 0.9513 0.9892 0.9885 0.0581  0.1436  -0.0060 100 PHE H CD1 
2861 C CD2 . PHE B 110 F 0.9542 0.9854 0.9840 0.0490  0.1533  0.0029  100 PHE H CD2 
2862 C CE1 . PHE B 110 F 0.9588 1.0045 1.0041 0.0583  0.1437  -0.0091 100 PHE H CE1 
2863 C CE2 . PHE B 110 F 0.9589 1.0011 0.9984 0.0504  0.1526  0.0001  100 PHE H CE2 
2864 C CZ  . PHE B 110 F 0.9574 1.0049 1.0035 0.0555  0.1481  -0.0055 100 PHE H CZ  
2865 N N   . ASP B 111 ? 0.9612 0.9386 0.9305 0.0661  0.1604  0.0142  101 ASP H N   
2866 C CA  . ASP B 111 ? 0.9704 0.9322 0.9244 0.0718  0.1629  0.0176  101 ASP H CA  
2867 C C   . ASP B 111 ? 0.9564 0.9085 0.9138 0.0594  0.1662  0.0195  101 ASP H C   
2868 O O   . ASP B 111 ? 0.9519 0.9024 0.9115 0.0614  0.1636  0.0189  101 ASP H O   
2869 C CB  . ASP B 111 ? 1.0112 0.9526 0.9368 0.0807  0.1710  0.0232  101 ASP H CB  
2870 C CG  . ASP B 111 ? 1.0310 0.9579 0.9467 0.0700  0.1816  0.0269  101 ASP H CG  
2871 O OD1 . ASP B 111 ? 1.0154 0.9548 0.9488 0.0574  0.1810  0.0244  101 ASP H OD1 
2872 O OD2 . ASP B 111 ? 1.0625 0.9656 0.9519 0.0747  0.1913  0.0322  101 ASP H OD2 
2873 N N   . ILE B 112 ? 0.9496 0.8970 0.9075 0.0465  0.1721  0.0212  102 ILE H N   
2874 C CA  . ILE B 112 ? 0.9416 0.8826 0.9026 0.0334  0.1750  0.0219  102 ILE H CA  
2875 C C   . ILE B 112 ? 0.9118 0.8744 0.8971 0.0255  0.1682  0.0181  102 ILE H C   
2876 O O   . ILE B 112 ? 0.8900 0.8653 0.8842 0.0225  0.1679  0.0169  102 ILE H O   
2877 C CB  . ILE B 112 ? 0.9633 0.8856 0.9074 0.0233  0.1868  0.0249  102 ILE H CB  
2878 C CG1 . ILE B 112 ? 0.9984 0.8914 0.9143 0.0307  0.1954  0.0296  102 ILE H CG1 
2879 C CG2 . ILE B 112 ? 0.9533 0.8797 0.9071 0.0065  0.1881  0.0229  102 ILE H CG2 
2880 C CD1 . ILE B 112 ? 1.0149 0.9013 0.9146 0.0462  0.1974  0.0324  102 ILE H CD1 
2881 N N   . TRP B 113 ? 0.8974 0.8626 0.8915 0.0233  0.1635  0.0168  103 TRP H N   
2882 C CA  . TRP B 113 ? 0.8661 0.8477 0.8793 0.0181  0.1576  0.0142  103 TRP H CA  
2883 C C   . TRP B 113 ? 0.8802 0.8586 0.8933 0.0059  0.1598  0.0150  103 TRP H C   
2884 O O   . TRP B 113 ? 0.9086 0.8703 0.9074 0.0011  0.1656  0.0168  103 TRP H O   
2885 C CB  . TRP B 113 ? 0.8322 0.8193 0.8548 0.0248  0.1514  0.0114  103 TRP H CB  
2886 C CG  . TRP B 113 ? 0.8059 0.8019 0.8324 0.0347  0.1481  0.0081  103 TRP H CG  
2887 C CD1 . TRP B 113 ? 0.8023 0.7945 0.8173 0.0440  0.1492  0.0083  103 TRP H CD1 
2888 C CD2 . TRP B 113 ? 0.7856 0.7951 0.8268 0.0366  0.1435  0.0036  103 TRP H CD2 
2889 N NE1 . TRP B 113 ? 0.7909 0.7966 0.8141 0.0506  0.1446  0.0033  103 TRP H NE1 
2890 C CE2 . TRP B 113 ? 0.7861 0.8011 0.8253 0.0454  0.1417  0.0001  103 TRP H CE2 
2891 C CE3 . TRP B 113 ? 0.7743 0.7901 0.8281 0.0323  0.1413  0.0022  103 TRP H CE3 
2892 C CZ2 . TRP B 113 ? 0.7798 0.8062 0.8300 0.0477  0.1384  -0.0057 103 TRP H CZ2 
2893 C CZ3 . TRP B 113 ? 0.7701 0.7939 0.8331 0.0358  0.1391  -0.0024 103 TRP H CZ3 
2894 C CH2 . TRP B 113 ? 0.7723 0.8012 0.8340 0.0424  0.1378  -0.0069 103 TRP H CH2 
2895 N N   . GLY B 114 ? 0.8811 0.8752 0.9088 0.0016  0.1552  0.0135  104 GLY H N   
2896 C CA  . GLY B 114 ? 0.8987 0.8942 0.9278 -0.0081 0.1548  0.0134  104 GLY H CA  
2897 C C   . GLY B 114 ? 0.9184 0.9063 0.9475 -0.0058 0.1516  0.0135  104 GLY H C   
2898 O O   . GLY B 114 ? 0.8966 0.8811 0.9273 0.0026  0.1497  0.0129  104 GLY H O   
2899 N N   . GLN B 115 ? 0.9526 0.9395 0.9801 -0.0141 0.1512  0.0133  105 GLN H N   
2900 C CA  . GLN B 115 ? 0.9688 0.9472 0.9945 -0.0134 0.1494  0.0135  105 GLN H CA  
2901 C C   . GLN B 115 ? 0.9602 0.9484 0.9981 -0.0068 0.1439  0.0131  105 GLN H C   
2902 O O   . GLN B 115 ? 0.9861 0.9667 1.0241 -0.0035 0.1434  0.0127  105 GLN H O   
2903 C CB  . GLN B 115 ? 0.9920 0.9671 1.0109 -0.0244 0.1506  0.0130  105 GLN H CB  
2904 C CG  . GLN B 115 ? 1.0034 0.9993 1.0307 -0.0304 0.1471  0.0116  105 GLN H CG  
2905 C CD  . GLN B 115 ? 1.0375 1.0339 1.0590 -0.0407 0.1465  0.0098  105 GLN H CD  
2906 O OE1 . GLN B 115 ? 1.0771 1.0559 1.0877 -0.0435 0.1491  0.0099  105 GLN H OE1 
2907 N NE2 . GLN B 115 ? 1.0456 1.0642 1.0744 -0.0459 0.1430  0.0076  105 GLN H NE2 
2908 N N   . GLY B 116 ? 0.9407 0.9447 0.9882 -0.0051 0.1409  0.0129  106 GLY H N   
2909 C CA  . GLY B 116 ? 0.9214 0.9312 0.9774 0.0013  0.1375  0.0129  106 GLY H CA  
2910 C C   . GLY B 116 ? 0.9157 0.9317 0.9718 -0.0009 0.1344  0.0144  106 GLY H C   
2911 O O   . GLY B 116 ? 0.9219 0.9341 0.9710 -0.0079 0.1347  0.0146  106 GLY H O   
2912 N N   . THR B 117 ? 0.9130 0.9379 0.9754 0.0059  0.1320  0.0154  107 THR H N   
2913 C CA  . THR B 117 ? 0.9222 0.9549 0.9833 0.0074  0.1285  0.0174  107 THR H CA  
2914 C C   . THR B 117 ? 0.9402 0.9634 1.0006 0.0168  0.1291  0.0192  107 THR H C   
2915 O O   . THR B 117 ? 0.9603 0.9857 1.0258 0.0239  0.1302  0.0190  107 THR H O   
2916 C CB  . THR B 117 ? 0.9129 0.9696 0.9806 0.0077  0.1256  0.0173  107 THR H CB  
2917 O OG1 . THR B 117 ? 0.9001 0.9623 0.9674 -0.0029 0.1275  0.0148  107 THR H OG1 
2918 C CG2 . THR B 117 ? 0.9138 0.9835 0.9798 0.0107  0.1209  0.0190  107 THR H CG2 
2919 N N   . LEU B 118 ? 0.9461 0.9566 0.9986 0.0162  0.1297  0.0206  108 LEU H N   
2920 C CA  . LEU B 118 ? 0.9471 0.9440 0.9958 0.0238  0.1324  0.0222  108 LEU H CA  
2921 C C   . LEU B 118 ? 0.9516 0.9574 0.9962 0.0327  0.1293  0.0264  108 LEU H C   
2922 O O   . LEU B 118 ? 0.9665 0.9750 1.0034 0.0324  0.1262  0.0286  108 LEU H O   
2923 C CB  . LEU B 118 ? 0.9509 0.9295 0.9916 0.0195  0.1356  0.0220  108 LEU H CB  
2924 C CG  . LEU B 118 ? 0.9563 0.9171 0.9902 0.0254  0.1406  0.0236  108 LEU H CG  
2925 C CD1 . LEU B 118 ? 0.9544 0.9087 0.9948 0.0285  0.1456  0.0203  108 LEU H CD1 
2926 C CD2 . LEU B 118 ? 0.9676 0.9122 0.9941 0.0199  0.1443  0.0229  108 LEU H CD2 
2927 N N   . VAL B 119 ? 0.9521 0.9630 1.0012 0.0415  0.1302  0.0272  109 VAL H N   
2928 C CA  . VAL B 119 ? 0.9645 0.9824 1.0086 0.0538  0.1282  0.0317  109 VAL H CA  
2929 C C   . VAL B 119 ? 0.9622 0.9530 0.9942 0.0614  0.1347  0.0344  109 VAL H C   
2930 O O   . VAL B 119 ? 0.9464 0.9208 0.9799 0.0607  0.1413  0.0317  109 VAL H O   
2931 C CB  . VAL B 119 ? 0.9705 1.0064 1.0240 0.0607  0.1270  0.0314  109 VAL H CB  
2932 C CG1 . VAL B 119 ? 0.9791 1.0239 1.0269 0.0762  0.1250  0.0365  109 VAL H CG1 
2933 C CG2 . VAL B 119 ? 0.9653 1.0253 1.0300 0.0514  0.1228  0.0281  109 VAL H CG2 
2934 N N   . THR B 120 ? 0.9627 0.9490 0.9817 0.0680  0.1334  0.0392  110 THR H N   
2935 C CA  . THR B 120 ? 0.9742 0.9318 0.9777 0.0759  0.1410  0.0427  110 THR H CA  
2936 C C   . THR B 120 ? 0.9831 0.9440 0.9771 0.0941  0.1404  0.0488  110 THR H C   
2937 O O   . THR B 120 ? 0.9739 0.9573 0.9659 0.1008  0.1323  0.0520  110 THR H O   
2938 C CB  . THR B 120 ? 0.9783 0.9226 0.9699 0.0708  0.1417  0.0441  110 THR H CB  
2939 O OG1 . THR B 120 ? 0.9666 0.9110 0.9678 0.0556  0.1419  0.0386  110 THR H OG1 
2940 C CG2 . THR B 120 ? 1.0025 0.9135 0.9768 0.0770  0.1518  0.0474  110 THR H CG2 
2941 N N   . VAL B 121 ? 0.9956 0.9347 0.9833 0.1023  0.1494  0.0499  111 VAL H N   
2942 C CA  . VAL B 121 ? 1.0225 0.9586 0.9979 0.1220  0.1511  0.0564  111 VAL H CA  
2943 C C   . VAL B 121 ? 1.0587 0.9606 1.0092 0.1304  0.1595  0.0621  111 VAL H C   
2944 O O   . VAL B 121 ? 1.0583 0.9270 1.0008 0.1269  0.1717  0.0603  111 VAL H O   
2945 C CB  . VAL B 121 ? 1.0216 0.9528 1.0028 0.1269  0.1571  0.0542  111 VAL H CB  
2946 C CG1 . VAL B 121 ? 1.0442 0.9695 1.0105 0.1495  0.1602  0.0615  111 VAL H CG1 
2947 C CG2 . VAL B 121 ? 0.9959 0.9587 0.9998 0.1184  0.1498  0.0488  111 VAL H CG2 
2948 N N   . SER B 122 ? 1.0904 1.0015 1.0282 0.1408  0.1533  0.0683  112 SER H N   
2949 C CA  . SER B 122 ? 1.1485 1.0279 1.0597 0.1499  0.1605  0.0746  112 SER H CA  
2950 C C   . SER B 122 ? 1.1855 1.0821 1.0821 0.1705  0.1524  0.0827  112 SER H C   
2951 O O   . SER B 122 ? 1.1584 1.0955 1.0679 0.1698  0.1390  0.0811  112 SER H O   
2952 C CB  . SER B 122 ? 1.1522 1.0196 1.0621 0.1333  0.1621  0.0714  112 SER H CB  
2953 O OG  . SER B 122 ? 1.1876 1.0248 1.0702 0.1422  0.1694  0.0779  112 SER H OG  
2954 N N   . SER B 123 ? 1.2545 1.1199 1.1231 0.1888  0.1613  0.0908  113 SER H N   
2955 C CA  . SER B 123 ? 1.3038 1.1822 1.1539 0.2122  0.1545  0.0994  113 SER H CA  
2956 C C   . SER B 123 ? 1.3341 1.2149 1.1722 0.2083  0.1487  0.1010  113 SER H C   
2957 O O   . SER B 123 ? 1.3564 1.2620 1.1852 0.2230  0.1381  0.1054  113 SER H O   
2958 C CB  . SER B 123 ? 1.3445 1.1852 1.1659 0.2352  0.1674  0.1083  113 SER H CB  
2959 O OG  . SER B 123 ? 1.3684 1.1573 1.1700 0.2281  0.1837  0.1093  113 SER H OG  
2960 N N   . ALA B 124 ? 1.3486 1.2049 1.1867 0.1888  0.1556  0.0968  114 ALA H N   
2961 C CA  . ALA B 124 ? 1.3639 1.2186 1.1904 0.1830  0.1518  0.0975  114 ALA H CA  
2962 C C   . ALA B 124 ? 1.3513 1.2549 1.1984 0.1731  0.1347  0.0917  114 ALA H C   
2963 O O   . ALA B 124 ? 1.3223 1.2503 1.1964 0.1600  0.1299  0.0846  114 ALA H O   
2964 C CB  . ALA B 124 ? 1.3559 1.1759 1.1814 0.1641  0.1640  0.0934  114 ALA H CB  
2965 N N   . SER B 125 ? 1.3818 1.2979 1.2140 0.1791  0.1265  0.0944  115 SER H N   
2966 C CA  . SER B 125 ? 1.3642 1.3260 1.2121 0.1698  0.1111  0.0882  115 SER H CA  
2967 C C   . SER B 125 ? 1.3402 1.2968 1.2008 0.1433  0.1124  0.0803  115 SER H C   
2968 O O   . SER B 125 ? 1.3492 1.2690 1.1996 0.1362  0.1232  0.0812  115 SER H O   
2969 C CB  . SER B 125 ? 1.3862 1.3639 1.2124 0.1858  0.1018  0.0928  115 SER H CB  
2970 O OG  . SER B 125 ? 1.3685 1.3963 1.2117 0.1774  0.0867  0.0853  115 SER H OG  
2971 N N   . THR B 126 ? 1.3025 1.2961 1.1850 0.1291  0.1023  0.0724  116 THR H N   
2972 C CA  . THR B 126 ? 1.2662 1.2565 1.1602 0.1054  0.1035  0.0650  116 THR H CA  
2973 C C   . THR B 126 ? 1.2706 1.2521 1.1455 0.1016  0.1017  0.0651  116 THR H C   
2974 O O   . THR B 126 ? 1.2900 1.2856 1.1490 0.1141  0.0944  0.0682  116 THR H O   
2975 C CB  . THR B 126 ? 1.2341 1.2621 1.1536 0.0921  0.0953  0.0568  116 THR H CB  
2976 O OG1 . THR B 126 ? 1.2243 1.2435 1.1502 0.0712  0.0980  0.0507  116 THR H OG1 
2977 C CG2 . THR B 126 ? 1.2372 1.3082 1.1580 0.0971  0.0823  0.0544  116 THR H CG2 
2978 N N   . LYS B 127 ? 1.2526 1.2116 1.1285 0.0851  0.1085  0.0616  117 LYS H N   
2979 C CA  . LYS B 127 ? 1.2586 1.2040 1.1159 0.0799  0.1091  0.0614  117 LYS H CA  
2980 C C   . LYS B 127 ? 1.2204 1.1668 1.0906 0.0578  0.1101  0.0534  117 LYS H C   
2981 O O   . LYS B 127 ? 1.1972 1.1282 1.0802 0.0490  0.1179  0.0513  117 LYS H O   
2982 C CB  . LYS B 127 ? 1.2945 1.1971 1.1305 0.0883  0.1216  0.0683  117 LYS H CB  
2983 C CG  . LYS B 127 ? 1.3282 1.2117 1.1432 0.0837  0.1245  0.0688  117 LYS H CG  
2984 C CD  . LYS B 127 ? 1.3530 1.2574 1.1499 0.0925  0.1131  0.0701  117 LYS H CD  
2985 C CE  . LYS B 127 ? 1.3688 1.2531 1.1436 0.0872  0.1163  0.0700  117 LYS H CE  
2986 N NZ  . LYS B 127 ? 1.3941 1.2340 1.1477 0.0955  0.1308  0.0775  117 LYS H NZ  
2987 N N   . GLY B 128 ? 1.2036 1.1679 1.0687 0.0495  0.1024  0.0486  118 GLY H N   
2988 C CA  . GLY B 128 ? 1.1674 1.1302 1.0400 0.0295  0.1041  0.0411  118 GLY H CA  
2989 C C   . GLY B 128 ? 1.1587 1.0853 1.0175 0.0246  0.1142  0.0425  118 GLY H C   
2990 O O   . GLY B 128 ? 1.1803 1.0891 1.0184 0.0343  0.1171  0.0478  118 GLY H O   
2991 N N   . PRO B 129 ? 1.1260 1.0407 0.9948 0.0104  0.1205  0.0380  119 PRO H N   
2992 C CA  . PRO B 129 ? 1.1224 1.0055 0.9810 0.0060  0.1309  0.0387  119 PRO H CA  
2993 C C   . PRO B 129 ? 1.1312 1.0083 0.9694 0.0006  0.1296  0.0366  119 PRO H C   
2994 O O   . PRO B 129 ? 1.1158 1.0149 0.9504 -0.0041 0.1206  0.0324  119 PRO H O   
2995 C CB  . PRO B 129 ? 1.1026 0.9825 0.9796 -0.0054 0.1360  0.0339  119 PRO H CB  
2996 C CG  . PRO B 129 ? 1.0967 1.0049 0.9852 -0.0124 0.1274  0.0291  119 PRO H CG  
2997 C CD  . PRO B 129 ? 1.1000 1.0308 0.9892 -0.0009 0.1187  0.0321  119 PRO H CD  
2998 N N   . SER B 130 ? 1.1544 1.0022 0.9794 0.0008  0.1393  0.0389  120 SER H N   
2999 C CA  . SER B 130 ? 1.1742 1.0104 0.9792 -0.0052 0.1407  0.0367  120 SER H CA  
3000 C C   . SER B 130 ? 1.1637 0.9806 0.9745 -0.0163 0.1509  0.0331  120 SER H C   
3001 O O   . SER B 130 ? 1.1747 0.9713 0.9883 -0.0136 0.1612  0.0356  120 SER H O   
3002 C CB  . SER B 130 ? 1.2073 1.0253 0.9877 0.0063  0.1439  0.0431  120 SER H CB  
3003 O OG  . SER B 130 ? 1.2194 1.0556 0.9932 0.0197  0.1345  0.0472  120 SER H OG  
3004 N N   . VAL B 131 ? 1.1502 0.9739 0.9623 -0.0285 0.1486  0.0267  121 VAL H N   
3005 C CA  . VAL B 131 ? 1.1257 0.9337 0.9437 -0.0373 0.1576  0.0233  121 VAL H CA  
3006 C C   . VAL B 131 ? 1.1296 0.9140 0.9264 -0.0400 0.1649  0.0228  121 VAL H C   
3007 O O   . VAL B 131 ? 1.1345 0.9206 0.9124 -0.0429 0.1602  0.0210  121 VAL H O   
3008 C CB  . VAL B 131 ? 1.1129 0.9345 0.9395 -0.0485 0.1539  0.0171  121 VAL H CB  
3009 C CG1 . VAL B 131 ? 1.1083 0.9127 0.9402 -0.0539 0.1636  0.0149  121 VAL H CG1 
3010 C CG2 . VAL B 131 ? 1.0944 0.9418 0.9395 -0.0461 0.1460  0.0173  121 VAL H CG2 
3011 N N   . PHE B 132 ? 1.1264 0.8906 0.9269 -0.0392 0.1763  0.0238  122 PHE H N   
3012 C CA  . PHE B 132 ? 1.1524 0.8930 0.9346 -0.0413 0.1852  0.0234  122 PHE H CA  
3013 C C   . PHE B 132 ? 1.1561 0.8861 0.9471 -0.0466 0.1943  0.0199  122 PHE H C   
3014 O O   . PHE B 132 ? 1.1450 0.8799 0.9565 -0.0440 0.1974  0.0200  122 PHE H O   
3015 C CB  . PHE B 132 ? 1.1564 0.8817 0.9310 -0.0326 0.1923  0.0288  122 PHE H CB  
3016 C CG  . PHE B 132 ? 1.1626 0.8936 0.9227 -0.0243 0.1847  0.0335  122 PHE H CG  
3017 C CD1 . PHE B 132 ? 1.1837 0.9171 0.9209 -0.0252 0.1779  0.0327  122 PHE H CD1 
3018 C CD2 . PHE B 132 ? 1.1499 0.8842 0.9180 -0.0148 0.1845  0.0384  122 PHE H CD2 
3019 C CE1 . PHE B 132 ? 1.1999 0.9412 0.9228 -0.0149 0.1702  0.0373  122 PHE H CE1 
3020 C CE2 . PHE B 132 ? 1.1701 0.9084 0.9226 -0.0044 0.1780  0.0436  122 PHE H CE2 
3021 C CZ  . PHE B 132 ? 1.1918 0.9348 0.9218 -0.0036 0.1705  0.0433  122 PHE H CZ  
3022 N N   . PRO B 133 ? 1.1839 0.8991 0.9584 -0.0532 0.1990  0.0164  123 PRO H N   
3023 C CA  . PRO B 133 ? 1.1775 0.8813 0.9572 -0.0560 0.2080  0.0135  123 PRO H CA  
3024 C C   . PRO B 133 ? 1.1723 0.8624 0.9564 -0.0504 0.2199  0.0151  123 PRO H C   
3025 O O   . PRO B 133 ? 1.1893 0.8655 0.9585 -0.0491 0.2251  0.0168  123 PRO H O   
3026 C CB  . PRO B 133 ? 1.2055 0.8963 0.9617 -0.0649 0.2092  0.0093  123 PRO H CB  
3027 C CG  . PRO B 133 ? 1.2246 0.9128 0.9610 -0.0642 0.2053  0.0108  123 PRO H CG  
3028 C CD  . PRO B 133 ? 1.2104 0.9190 0.9588 -0.0573 0.1959  0.0150  123 PRO H CD  
3029 N N   . LEU B 134 ? 1.1574 0.8528 0.9620 -0.0471 0.2244  0.0142  124 LEU H N   
3030 C CA  . LEU B 134 ? 1.1709 0.8575 0.9820 -0.0431 0.2364  0.0134  124 LEU H CA  
3031 C C   . LEU B 134 ? 1.1904 0.8626 0.9907 -0.0447 0.2436  0.0106  124 LEU H C   
3032 O O   . LEU B 134 ? 1.1591 0.8362 0.9701 -0.0419 0.2450  0.0090  124 LEU H O   
3033 C CB  . LEU B 134 ? 1.1495 0.8537 0.9886 -0.0380 0.2367  0.0127  124 LEU H CB  
3034 C CG  . LEU B 134 ? 1.1427 0.8589 0.9921 -0.0363 0.2307  0.0151  124 LEU H CG  
3035 C CD1 . LEU B 134 ? 1.1244 0.8549 0.9997 -0.0326 0.2340  0.0127  124 LEU H CD1 
3036 C CD2 . LEU B 134 ? 1.1633 0.8655 0.9960 -0.0363 0.2340  0.0182  124 LEU H CD2 
3037 N N   . ALA B 135 ? 1.2279 0.8809 1.0045 -0.0483 0.2484  0.0102  125 ALA H N   
3038 C CA  . ALA B 135 ? 1.2468 0.8818 1.0070 -0.0509 0.2553  0.0074  125 ALA H CA  
3039 C C   . ALA B 135 ? 1.2443 0.8748 1.0148 -0.0436 0.2675  0.0064  125 ALA H C   
3040 O O   . ALA B 135 ? 1.2548 0.8881 1.0346 -0.0401 0.2736  0.0069  125 ALA H O   
3041 C CB  . ALA B 135 ? 1.2703 0.8873 1.0019 -0.0569 0.2566  0.0067  125 ALA H CB  
3042 N N   . PRO B 136 ? 1.2348 0.8584 1.0032 -0.0407 0.2723  0.0047  126 PRO H N   
3043 C CA  . PRO B 136 ? 1.2313 0.8527 1.0081 -0.0316 0.2838  0.0035  126 PRO H CA  
3044 C C   . PRO B 136 ? 1.2512 0.8504 1.0080 -0.0329 0.2951  0.0024  126 PRO H C   
3045 O O   . PRO B 136 ? 1.2725 0.8520 1.0032 -0.0402 0.2950  0.0019  126 PRO H O   
3046 C CB  . PRO B 136 ? 1.2401 0.8573 1.0145 -0.0271 0.2845  0.0031  126 PRO H CB  
3047 C CG  . PRO B 136 ? 1.2545 0.8575 1.0068 -0.0382 0.2787  0.0026  126 PRO H CG  
3048 C CD  . PRO B 136 ? 1.2376 0.8546 0.9945 -0.0455 0.2679  0.0036  126 PRO H CD  
3049 N N   . SER B 137 ? 1.2480 0.8522 1.0175 -0.0261 0.3050  0.0013  127 SER H N   
3050 C CA  . SER B 137 ? 1.2766 0.8617 1.0296 -0.0269 0.3170  0.0002  127 SER H CA  
3051 C C   . SER B 137 ? 1.2657 0.8592 1.0350 -0.0166 0.3290  -0.0022 127 SER H C   
3052 O O   . SER B 137 ? 1.2307 0.8435 1.0207 -0.0082 0.3271  -0.0032 127 SER H O   
3053 C CB  . SER B 137 ? 1.2870 0.8697 1.0348 -0.0332 0.3163  0.0017  127 SER H CB  
3054 O OG  . SER B 137 ? 1.2703 0.8740 1.0448 -0.0308 0.3172  0.0012  127 SER H OG  
3055 N N   . SER B 138 ? 1.2723 0.8524 1.0315 -0.0168 0.3414  -0.0036 128 SER H N   
3056 C CA  . SER B 138 ? 1.2623 0.8539 1.0387 -0.0081 0.3539  -0.0070 128 SER H CA  
3057 C C   . SER B 138 ? 1.2448 0.8704 1.0568 -0.0061 0.3513  -0.0096 128 SER H C   
3058 O O   . SER B 138 ? 1.2163 0.8636 1.0501 0.0033  0.3559  -0.0132 128 SER H O   
3059 C CB  . SER B 138 ? 1.2732 0.8456 1.0332 -0.0116 0.3671  -0.0080 128 SER H CB  
3060 O OG  . SER B 138 ? 1.2698 0.8572 1.0492 -0.0041 0.3799  -0.0122 128 SER H OG  
3061 N N   . LYS B 139 ? 1.2612 0.8916 1.0777 -0.0146 0.3440  -0.0081 129 LYS H N   
3062 C CA  . LYS B 139 ? 1.2534 0.9103 1.0996 -0.0158 0.3440  -0.0114 129 LYS H CA  
3063 C C   . LYS B 139 ? 1.2313 0.9142 1.0997 -0.0105 0.3323  -0.0122 129 LYS H C   
3064 O O   . LYS B 139 ? 1.2137 0.9242 1.1102 -0.0084 0.3335  -0.0172 129 LYS H O   
3065 C CB  . LYS B 139 ? 1.2630 0.9095 1.1008 -0.0257 0.3424  -0.0088 129 LYS H CB  
3066 C CG  . LYS B 139 ? 1.2939 0.9110 1.1036 -0.0305 0.3521  -0.0066 129 LYS H CG  
3067 C CD  . LYS B 139 ? 1.3085 0.9239 1.1223 -0.0286 0.3694  -0.0112 129 LYS H CD  
3068 C CE  . LYS B 139 ? 1.3441 0.9289 1.1284 -0.0336 0.3797  -0.0088 129 LYS H CE  
3069 N NZ  . LYS B 139 ? 1.3655 0.9493 1.1543 -0.0317 0.3975  -0.0136 129 LYS H NZ  
3070 N N   . SER B 140 ? 1.2393 0.9137 1.0944 -0.0092 0.3217  -0.0081 130 SER H N   
3071 C CA  . SER B 140 ? 1.2271 0.9224 1.0993 -0.0045 0.3107  -0.0080 130 SER H CA  
3072 C C   . SER B 140 ? 1.2487 0.9437 1.1176 0.0071  0.3121  -0.0078 130 SER H C   
3073 O O   . SER B 140 ? 1.2422 0.9313 1.1021 0.0084  0.3041  -0.0047 130 SER H O   
3074 C CB  . SER B 140 ? 1.2102 0.8990 1.0724 -0.0117 0.2982  -0.0037 130 SER H CB  
3075 O OG  . SER B 140 ? 1.2226 0.8873 1.0574 -0.0142 0.2963  -0.0006 130 SER H OG  
3076 N N   . THR B 141 ? 1.2738 0.9750 1.1494 0.0160  0.3230  -0.0112 131 THR H N   
3077 C CA  . THR B 141 ? 1.2866 0.9901 1.1605 0.0309  0.3256  -0.0109 131 THR H CA  
3078 C C   . THR B 141 ? 1.2779 1.0179 1.1827 0.0418  0.3295  -0.0169 131 THR H C   
3079 O O   . THR B 141 ? 1.2887 1.0385 1.2051 0.0390  0.3387  -0.0218 131 THR H O   
3080 C CB  . THR B 141 ? 1.3101 0.9809 1.1548 0.0338  0.3362  -0.0089 131 THR H CB  
3081 O OG1 . THR B 141 ? 1.3249 0.9934 1.1709 0.0296  0.3471  -0.0121 131 THR H OG1 
3082 C CG2 . THR B 141 ? 1.3234 0.9610 1.1372 0.0237  0.3319  -0.0046 131 THR H CG2 
3083 N N   . SER B 142 ? 1.2773 1.0380 1.1944 0.0541  0.3229  -0.0171 132 SER H N   
3084 C CA  . SER B 142 ? 1.2673 1.0688 1.2150 0.0654  0.3240  -0.0237 132 SER H CA  
3085 C C   . SER B 142 ? 1.2835 1.0875 1.2245 0.0870  0.3267  -0.0218 132 SER H C   
3086 O O   . SER B 142 ? 1.2788 1.1005 1.2277 0.0982  0.3186  -0.0211 132 SER H O   
3087 C CB  . SER B 142 ? 1.2381 1.0685 1.2099 0.0607  0.3126  -0.0269 132 SER H CB  
3088 O OG  . SER B 142 ? 1.2229 1.0962 1.2249 0.0704  0.3132  -0.0350 132 SER H OG  
3089 N N   . GLY B 143 ? 1.3036 1.0876 1.2276 0.0938  0.3388  -0.0207 133 GLY H N   
3090 C CA  . GLY B 143 ? 1.3102 1.0962 1.2273 0.1168  0.3443  -0.0192 133 GLY H CA  
3091 C C   . GLY B 143 ? 1.3198 1.0734 1.2069 0.1242  0.3408  -0.0108 133 GLY H C   
3092 O O   . GLY B 143 ? 1.3108 1.0795 1.2023 0.1401  0.3354  -0.0091 133 GLY H O   
3093 N N   . GLY B 144 ? 1.3256 1.0349 1.1816 0.1121  0.3446  -0.0062 134 GLY H N   
3094 C CA  . GLY B 144 ? 1.3309 1.0035 1.1547 0.1162  0.3451  0.0003  134 GLY H CA  
3095 C C   . GLY B 144 ? 1.3041 0.9710 1.1252 0.1016  0.3328  0.0028  134 GLY H C   
3096 O O   . GLY B 144 ? 1.3163 0.9508 1.1102 0.0996  0.3338  0.0073  134 GLY H O   
3097 N N   . THR B 145 ? 1.2612 0.9591 1.1100 0.0914  0.3225  -0.0004 135 THR H N   
3098 C CA  . THR B 145 ? 1.2416 0.9383 1.0908 0.0782  0.3108  0.0014  135 THR H CA  
3099 C C   . THR B 145 ? 1.2211 0.9158 1.0743 0.0578  0.3078  -0.0005 135 THR H C   
3100 O O   . THR B 145 ? 1.2259 0.9423 1.1001 0.0549  0.3090  -0.0049 135 THR H O   
3101 C CB  . THR B 145 ? 1.2123 0.9457 1.0880 0.0864  0.3006  0.0000  135 THR H CB  
3102 O OG1 . THR B 145 ? 1.2054 0.9736 1.1120 0.0832  0.2989  -0.0064 135 THR H OG1 
3103 C CG2 . THR B 145 ? 1.2234 0.9624 1.0952 0.1097  0.3032  0.0022  135 THR H CG2 
3104 N N   . ALA B 146 ? 1.2144 0.8829 1.0462 0.0441  0.3045  0.0023  136 ALA H N   
3105 C CA  . ALA B 146 ? 1.1930 0.8592 1.0248 0.0268  0.3001  0.0013  136 ALA H CA  
3106 C C   . ALA B 146 ? 1.1630 0.8503 1.0123 0.0208  0.2871  0.0018  136 ALA H C   
3107 O O   . ALA B 146 ? 1.1627 0.8560 1.0147 0.0261  0.2816  0.0035  136 ALA H O   
3108 C CB  . ALA B 146 ? 1.2126 0.8436 1.0123 0.0159  0.3031  0.0029  136 ALA H CB  
3109 N N   . ALA B 147 ? 1.1417 0.8382 1.0011 0.0106  0.2834  0.0004  137 ALA H N   
3110 C CA  . ALA B 147 ? 1.1060 0.8193 0.9793 0.0044  0.2720  0.0010  137 ALA H CA  
3111 C C   . ALA B 147 ? 1.1119 0.8094 0.9685 -0.0088 0.2678  0.0030  137 ALA H C   
3112 O O   . ALA B 147 ? 1.1133 0.7969 0.9579 -0.0137 0.2736  0.0027  137 ALA H O   
3113 C CB  . ALA B 147 ? 1.0852 0.8259 0.9866 0.0063  0.2719  -0.0028 137 ALA H CB  
3114 N N   . LEU B 148 ? 1.1143 0.8153 0.9695 -0.0139 0.2578  0.0049  138 LEU H N   
3115 C CA  . LEU B 148 ? 1.1233 0.8170 0.9658 -0.0249 0.2515  0.0064  138 LEU H CA  
3116 C C   . LEU B 148 ? 1.1021 0.8155 0.9596 -0.0266 0.2403  0.0075  138 LEU H C   
3117 O O   . LEU B 148 ? 1.0855 0.8139 0.9592 -0.0203 0.2378  0.0071  138 LEU H O   
3118 C CB  . LEU B 148 ? 1.1554 0.8258 0.9709 -0.0313 0.2532  0.0063  138 LEU H CB  
3119 C CG  . LEU B 148 ? 1.1643 0.8294 0.9750 -0.0288 0.2534  0.0065  138 LEU H CG  
3120 C CD1 . LEU B 148 ? 1.1574 0.8337 0.9717 -0.0360 0.2428  0.0070  138 LEU H CD1 
3121 C CD2 . LEU B 148 ? 1.1896 0.8249 0.9726 -0.0319 0.2626  0.0052  138 LEU H CD2 
3122 N N   . GLY B 149 ? 1.1093 0.8233 0.9605 -0.0339 0.2336  0.0089  139 GLY H N   
3123 C CA  . GLY B 149 ? 1.1035 0.8361 0.9684 -0.0346 0.2236  0.0101  139 GLY H CA  
3124 C C   . GLY B 149 ? 1.1172 0.8492 0.9702 -0.0412 0.2165  0.0117  139 GLY H C   
3125 O O   . GLY B 149 ? 1.1136 0.8318 0.9460 -0.0467 0.2176  0.0112  139 GLY H O   
3126 N N   . CYS B 150 ? 1.1303 0.8787 0.9961 -0.0396 0.2091  0.0134  140 CYS H N   
3127 C CA  . CYS B 150 ? 1.1574 0.9097 1.0141 -0.0423 0.2016  0.0155  140 CYS H CA  
3128 C C   . CYS B 150 ? 1.1363 0.8972 1.0053 -0.0366 0.2002  0.0180  140 CYS H C   
3129 O O   . CYS B 150 ? 1.1200 0.8895 1.0078 -0.0329 0.2022  0.0170  140 CYS H O   
3130 C CB  . CYS B 150 ? 1.1775 0.9418 1.0328 -0.0474 0.1924  0.0145  140 CYS H CB  
3131 S SG  . CYS B 150 ? 1.2764 1.0263 1.1076 -0.0579 0.1939  0.0107  140 CYS H SG  
3132 N N   . LEU B 151 ? 1.1401 0.8979 0.9961 -0.0356 0.1971  0.0210  141 LEU H N   
3133 C CA  . LEU B 151 ? 1.1380 0.8976 0.9992 -0.0296 0.1976  0.0242  141 LEU H CA  
3134 C C   . LEU B 151 ? 1.1368 0.9094 0.9930 -0.0268 0.1864  0.0271  141 LEU H C   
3135 O O   . LEU B 151 ? 1.1484 0.9177 0.9855 -0.0265 0.1826  0.0289  141 LEU H O   
3136 C CB  . LEU B 151 ? 1.1571 0.8955 1.0032 -0.0281 0.2074  0.0260  141 LEU H CB  
3137 C CG  . LEU B 151 ? 1.1604 0.8925 1.0066 -0.0223 0.2117  0.0294  141 LEU H CG  
3138 C CD1 . LEU B 151 ? 1.1450 0.8831 1.0151 -0.0227 0.2179  0.0259  141 LEU H CD1 
3139 C CD2 . LEU B 151 ? 1.1860 0.8940 1.0101 -0.0211 0.2211  0.0321  141 LEU H CD2 
3140 N N   . VAL B 152 ? 1.1235 0.9130 0.9971 -0.0242 0.1811  0.0272  142 VAL H N   
3141 C CA  . VAL B 152 ? 1.1295 0.9345 1.0017 -0.0198 0.1712  0.0299  142 VAL H CA  
3142 C C   . VAL B 152 ? 1.1222 0.9196 0.9932 -0.0106 0.1749  0.0343  142 VAL H C   
3143 O O   . VAL B 152 ? 1.1019 0.8966 0.9872 -0.0094 0.1808  0.0332  142 VAL H O   
3144 C CB  . VAL B 152 ? 1.1247 0.9513 1.0143 -0.0223 0.1640  0.0274  142 VAL H CB  
3145 C CG1 . VAL B 152 ? 1.1263 0.9537 1.0145 -0.0318 0.1638  0.0230  142 VAL H CG1 
3146 C CG2 . VAL B 152 ? 1.1077 0.9379 1.0172 -0.0190 0.1674  0.0268  142 VAL H CG2 
3147 N N   . LYS B 153 ? 1.1328 0.9259 0.9847 -0.0039 0.1720  0.0388  143 LYS H N   
3148 C CA  . LYS B 153 ? 1.1479 0.9233 0.9896 0.0051  0.1791  0.0439  143 LYS H CA  
3149 C C   . LYS B 153 ? 1.1452 0.9315 0.9767 0.0166  0.1702  0.0491  143 LYS H C   
3150 O O   . LYS B 153 ? 1.1374 0.9424 0.9634 0.0168  0.1593  0.0486  143 LYS H O   
3151 C CB  . LYS B 153 ? 1.1765 0.9263 0.9977 0.0038  0.1887  0.0452  143 LYS H CB  
3152 C CG  . LYS B 153 ? 1.2065 0.9307 1.0174 0.0098  0.2013  0.0492  143 LYS H CG  
3153 C CD  . LYS B 153 ? 1.2276 0.9263 1.0202 0.0067  0.2126  0.0496  143 LYS H CD  
3154 C CE  . LYS B 153 ? 1.2403 0.9111 1.0226 0.0106  0.2279  0.0526  143 LYS H CE  
3155 N NZ  . LYS B 153 ? 1.2618 0.9226 1.0222 0.0245  0.2259  0.0607  143 LYS H NZ  
3156 N N   . ASP B 154 ? 1.1491 0.9239 0.9782 0.0262  0.1758  0.0535  144 ASP H N   
3157 C CA  . ASP B 154 ? 1.1602 0.9417 0.9776 0.0408  0.1695  0.0596  144 ASP H CA  
3158 C C   . ASP B 154 ? 1.1406 0.9573 0.9756 0.0407  0.1559  0.0571  144 ASP H C   
3159 O O   . ASP B 154 ? 1.1559 0.9932 0.9842 0.0429  0.1449  0.0570  144 ASP H O   
3160 C CB  . ASP B 154 ? 1.1840 0.9567 0.9715 0.0491  0.1672  0.0647  144 ASP H CB  
3161 C CG  . ASP B 154 ? 1.2076 0.9426 0.9739 0.0507  0.1820  0.0683  144 ASP H CG  
3162 O OD1 . ASP B 154 ? 1.1955 0.9124 0.9720 0.0443  0.1946  0.0660  144 ASP H OD1 
3163 O OD2 . ASP B 154 ? 1.2324 0.9575 0.9718 0.0581  0.1810  0.0728  144 ASP H OD2 
3164 N N   . TYR B 155 ? 1.1098 0.9341 0.9671 0.0378  0.1572  0.0543  145 TYR H N   
3165 C CA  . TYR B 155 ? 1.0922 0.9478 0.9665 0.0380  0.1464  0.0521  145 TYR H CA  
3166 C C   . TYR B 155 ? 1.0869 0.9415 0.9721 0.0456  0.1498  0.0539  145 TYR H C   
3167 O O   . TYR B 155 ? 1.0856 0.9179 0.9725 0.0445  0.1608  0.0536  145 TYR H O   
3168 C CB  . TYR B 155 ? 1.0617 0.9313 0.9524 0.0228  0.1432  0.0451  145 TYR H CB  
3169 C CG  . TYR B 155 ? 1.0326 0.8939 0.9406 0.0155  0.1507  0.0413  145 TYR H CG  
3170 C CD1 . TYR B 155 ? 1.0186 0.8913 0.9443 0.0173  0.1497  0.0399  145 TYR H CD1 
3171 C CD2 . TYR B 155 ? 1.0279 0.8722 0.9346 0.0074  0.1586  0.0385  145 TYR H CD2 
3172 C CE1 . TYR B 155 ? 0.9982 0.8663 0.9390 0.0114  0.1555  0.0358  145 TYR H CE1 
3173 C CE2 . TYR B 155 ? 1.0069 0.8482 0.9300 0.0022  0.1645  0.0343  145 TYR H CE2 
3174 C CZ  . TYR B 155 ? 0.9897 0.8435 0.9297 0.0042  0.1625  0.0328  145 TYR H CZ  
3175 O OH  . TYR B 155 ? 0.9706 0.8243 0.9260 0.0000  0.1674  0.0281  145 TYR H OH  
3176 N N   . PHE B 156 ? 1.0839 0.9638 0.9764 0.0527  0.1407  0.0548  146 PHE H N   
3177 C CA  . PHE B 156 ? 1.0838 0.9652 0.9862 0.0605  0.1429  0.0562  146 PHE H CA  
3178 C C   . PHE B 156 ? 1.0595 0.9769 0.9763 0.0626  0.1315  0.0545  146 PHE H C   
3179 O O   . PHE B 156 ? 1.0591 0.9980 0.9701 0.0662  0.1222  0.0552  146 PHE H O   
3180 C CB  . PHE B 156 ? 1.1192 0.9781 1.0009 0.0770  0.1495  0.0637  146 PHE H CB  
3181 C CG  . PHE B 156 ? 1.1251 0.9797 1.0136 0.0854  0.1541  0.0650  146 PHE H CG  
3182 C CD1 . PHE B 156 ? 1.1248 0.9585 1.0214 0.0780  0.1655  0.0613  146 PHE H CD1 
3183 C CD2 . PHE B 156 ? 1.1360 1.0094 1.0232 0.1003  0.1471  0.0691  146 PHE H CD2 
3184 C CE1 . PHE B 156 ? 1.1286 0.9571 1.0302 0.0846  0.1702  0.0615  146 PHE H CE1 
3185 C CE2 . PHE B 156 ? 1.1430 1.0106 1.0353 0.1082  0.1522  0.0702  146 PHE H CE2 
3186 C CZ  . PHE B 156 ? 1.1398 0.9836 1.0385 0.0999  0.1639  0.0663  146 PHE H CZ  
3187 N N   . PRO B 157 ? 1.0376 0.9645 0.9735 0.0600  0.1321  0.0515  147 PRO H N   
3188 C CA  . PRO B 157 ? 1.0290 0.9367 0.9743 0.0536  0.1416  0.0485  147 PRO H CA  
3189 C C   . PRO B 157 ? 1.0072 0.9183 0.9644 0.0378  0.1416  0.0423  147 PRO H C   
3190 O O   . PRO B 157 ? 0.9921 0.9106 0.9454 0.0311  0.1370  0.0410  147 PRO H O   
3191 C CB  . PRO B 157 ? 1.0148 0.9357 0.9727 0.0602  0.1401  0.0483  147 PRO H CB  
3192 C CG  . PRO B 157 ? 1.0059 0.9613 0.9718 0.0600  0.1285  0.0474  147 PRO H CG  
3193 C CD  . PRO B 157 ? 1.0234 0.9824 0.9728 0.0635  0.1235  0.0503  147 PRO H CD  
3194 N N   . GLU B 158 ? 1.0033 0.9083 0.9736 0.0326  0.1471  0.0383  148 GLU H N   
3195 C CA  . GLU B 158 ? 0.9950 0.9069 0.9776 0.0212  0.1464  0.0329  148 GLU H CA  
3196 C C   . GLU B 158 ? 0.9877 0.9250 0.9814 0.0196  0.1385  0.0315  148 GLU H C   
3197 O O   . GLU B 158 ? 0.9920 0.9420 0.9880 0.0274  0.1347  0.0337  148 GLU H O   
3198 C CB  . GLU B 158 ? 0.9925 0.8924 0.9844 0.0181  0.1544  0.0287  148 GLU H CB  
3199 C CG  . GLU B 158 ? 1.0096 0.8858 0.9921 0.0165  0.1637  0.0284  148 GLU H CG  
3200 C CD  . GLU B 158 ? 1.0133 0.8838 1.0076 0.0106  0.1711  0.0219  148 GLU H CD  
3201 O OE1 . GLU B 158 ? 1.0073 0.8883 1.0118 0.0050  0.1689  0.0179  148 GLU H OE1 
3202 O OE2 . GLU B 158 ? 1.0368 0.8925 1.0293 0.0118  0.1796  0.0203  148 GLU H OE2 
3203 N N   . PRO B 159 ? 0.9813 0.9257 0.9811 0.0100  0.1368  0.0278  149 PRO H N   
3204 C CA  . PRO B 159 ? 0.9723 0.9027 0.9685 0.0024  0.1412  0.0255  149 PRO H CA  
3205 C C   . PRO B 159 ? 0.9660 0.8958 0.9503 -0.0036 0.1387  0.0257  149 PRO H C   
3206 O O   . PRO B 159 ? 0.9515 0.8965 0.9326 -0.0041 0.1325  0.0263  149 PRO H O   
3207 C CB  . PRO B 159 ? 0.9606 0.8986 0.9687 -0.0017 0.1414  0.0219  149 PRO H CB  
3208 C CG  . PRO B 159 ? 0.9649 0.9231 0.9775 -0.0019 0.1352  0.0223  149 PRO H CG  
3209 C CD  . PRO B 159 ? 0.9750 0.9397 0.9846 0.0064  0.1320  0.0258  149 PRO H CD  
3210 N N   . VAL B 160 ? 0.9717 0.8853 0.9499 -0.0085 0.1440  0.0243  150 VAL H N   
3211 C CA  . VAL B 160 ? 0.9798 0.8895 0.9465 -0.0160 0.1434  0.0232  150 VAL H CA  
3212 C C   . VAL B 160 ? 0.9768 0.8797 0.9469 -0.0219 0.1478  0.0201  150 VAL H C   
3213 O O   . VAL B 160 ? 1.0008 0.8936 0.9753 -0.0195 0.1534  0.0192  150 VAL H O   
3214 C CB  . VAL B 160 ? 0.9928 0.8861 0.9444 -0.0145 0.1466  0.0253  150 VAL H CB  
3215 C CG1 . VAL B 160 ? 0.9976 0.8814 0.9372 -0.0229 0.1485  0.0232  150 VAL H CG1 
3216 C CG2 . VAL B 160 ? 1.0073 0.9074 0.9504 -0.0073 0.1414  0.0292  150 VAL H CG2 
3217 N N   . THR B 161 ? 0.9691 0.8780 0.9366 -0.0291 0.1458  0.0180  151 THR H N   
3218 C CA  . THR B 161 ? 0.9597 0.8588 0.9257 -0.0332 0.1509  0.0159  151 THR H CA  
3219 C C   . THR B 161 ? 0.9754 0.8584 0.9250 -0.0398 0.1549  0.0147  151 THR H C   
3220 O O   . THR B 161 ? 0.9763 0.8621 0.9162 -0.0452 0.1516  0.0140  151 THR H O   
3221 C CB  . THR B 161 ? 0.9461 0.8561 0.9165 -0.0374 0.1492  0.0144  151 THR H CB  
3222 O OG1 . THR B 161 ? 0.9431 0.8615 0.9063 -0.0463 0.1459  0.0124  151 THR H OG1 
3223 C CG2 . THR B 161 ? 0.9294 0.8550 0.9148 -0.0308 0.1456  0.0154  151 THR H CG2 
3224 N N   . VAL B 162 ? 0.9798 0.8470 0.9260 -0.0386 0.1617  0.0142  152 VAL H N   
3225 C CA  . VAL B 162 ? 0.9970 0.8458 0.9270 -0.0437 0.1672  0.0130  152 VAL H CA  
3226 C C   . VAL B 162 ? 0.9963 0.8330 0.9207 -0.0445 0.1734  0.0120  152 VAL H C   
3227 O O   . VAL B 162 ? 0.9880 0.8257 0.9213 -0.0365 0.1756  0.0128  152 VAL H O   
3228 C CB  . VAL B 162 ? 1.0057 0.8439 0.9339 -0.0388 0.1713  0.0141  152 VAL H CB  
3229 C CG1 . VAL B 162 ? 1.0202 0.8383 0.9311 -0.0431 0.1779  0.0129  152 VAL H CG1 
3230 C CG2 . VAL B 162 ? 1.0052 0.8498 0.9342 -0.0366 0.1670  0.0160  152 VAL H CG2 
3231 N N   . SER B 163 ? 1.0086 0.8338 0.9170 -0.0541 0.1766  0.0098  153 SER H N   
3232 C CA  . SER B 163 ? 1.0253 0.8309 0.9216 -0.0547 0.1851  0.0093  153 SER H CA  
3233 C C   . SER B 163 ? 1.0470 0.8305 0.9235 -0.0605 0.1916  0.0076  153 SER H C   
3234 O O   . SER B 163 ? 1.0547 0.8407 0.9267 -0.0658 0.1884  0.0062  153 SER H O   
3235 C CB  . SER B 163 ? 1.0325 0.8403 0.9258 -0.0620 0.1857  0.0078  153 SER H CB  
3236 O OG  . SER B 163 ? 1.0454 0.8576 0.9310 -0.0762 0.1835  0.0037  153 SER H OG  
3237 N N   . TRP B 164 ? 1.0573 0.8182 0.9201 -0.0582 0.2012  0.0078  154 TRP H N   
3238 C CA  . TRP B 164 ? 1.0705 0.8069 0.9132 -0.0618 0.2092  0.0063  154 TRP H CA  
3239 C C   . TRP B 164 ? 1.0873 0.8005 0.9084 -0.0711 0.2180  0.0038  154 TRP H C   
3240 O O   . TRP B 164 ? 1.0830 0.7882 0.9015 -0.0661 0.2229  0.0057  154 TRP H O   
3241 C CB  . TRP B 164 ? 1.0697 0.7978 0.9149 -0.0476 0.2147  0.0090  154 TRP H CB  
3242 C CG  . TRP B 164 ? 1.0479 0.7910 0.9078 -0.0430 0.2098  0.0097  154 TRP H CG  
3243 C CD1 . TRP B 164 ? 1.0232 0.7870 0.9050 -0.0347 0.2046  0.0111  154 TRP H CD1 
3244 C CD2 . TRP B 164 ? 1.0582 0.7936 0.9096 -0.0470 0.2113  0.0087  154 TRP H CD2 
3245 N NE1 . TRP B 164 ? 1.0190 0.7871 0.9063 -0.0339 0.2037  0.0110  154 TRP H NE1 
3246 C CE2 . TRP B 164 ? 1.0407 0.7916 0.9093 -0.0407 0.2077  0.0100  154 TRP H CE2 
3247 C CE3 . TRP B 164 ? 1.0852 0.8011 0.9149 -0.0556 0.2160  0.0064  154 TRP H CE3 
3248 C CZ2 . TRP B 164 ? 1.0467 0.7926 0.9104 -0.0421 0.2093  0.0099  154 TRP H CZ2 
3249 C CZ3 . TRP B 164 ? 1.0828 0.7958 0.9081 -0.0564 0.2163  0.0062  154 TRP H CZ3 
3250 C CH2 . TRP B 164 ? 1.0665 0.7936 0.9083 -0.0494 0.2133  0.0084  154 TRP H CH2 
3251 N N   . ASN B 165 ? 1.1045 0.8059 0.9086 -0.0848 0.2207  -0.0008 155 ASN H N   
3252 C CA  . ASN B 165 ? 1.1380 0.8138 0.9187 -0.0970 0.2309  -0.0050 155 ASN H CA  
3253 C C   . ASN B 165 ? 1.1382 0.8234 0.9241 -0.1038 0.2301  -0.0063 155 ASN H C   
3254 O O   . ASN B 165 ? 1.1610 0.8222 0.9311 -0.1058 0.2410  -0.0063 155 ASN H O   
3255 C CB  . ASN B 165 ? 1.1642 0.8057 0.9259 -0.0874 0.2444  -0.0022 155 ASN H CB  
3256 C CG  . ASN B 165 ? 1.1681 0.7995 0.9229 -0.0830 0.2468  -0.0020 155 ASN H CG  
3257 O OD1 . ASN B 165 ? 1.1832 0.8069 0.9246 -0.0956 0.2476  -0.0070 155 ASN H OD1 
3258 N ND2 . ASN B 165 ? 1.1566 0.7894 0.9206 -0.0654 0.2480  0.0029  155 ASN H ND2 
3259 N N   . SER B 166 ? 1.1128 0.8315 0.9194 -0.1069 0.2180  -0.0072 156 SER H N   
3260 C CA  . SER B 166 ? 1.1004 0.8344 0.9160 -0.1130 0.2157  -0.0087 156 SER H CA  
3261 C C   . SER B 166 ? 1.1004 0.8240 0.9177 -0.0999 0.2212  -0.0030 156 SER H C   
3262 O O   . SER B 166 ? 1.1318 0.8443 0.9400 -0.1062 0.2286  -0.0042 156 SER H O   
3263 C CB  . SER B 166 ? 1.1266 0.8521 0.9265 -0.1342 0.2220  -0.0170 156 SER H CB  
3264 O OG  . SER B 166 ? 1.1258 0.8627 0.9228 -0.1451 0.2162  -0.0230 156 SER H OG  
3265 N N   . GLY B 167 ? 1.0721 0.8002 0.9006 -0.0819 0.2179  0.0027  157 GLY H N   
3266 C CA  . GLY B 167 ? 1.0550 0.7807 0.8879 -0.0672 0.2203  0.0078  157 GLY H CA  
3267 C C   . GLY B 167 ? 1.0837 0.7746 0.8933 -0.0592 0.2336  0.0105  157 GLY H C   
3268 O O   . GLY B 167 ? 1.0921 0.7787 0.9009 -0.0455 0.2364  0.0148  157 GLY H O   
3269 N N   . ALA B 168 ? 1.1102 0.7762 0.8994 -0.0664 0.2417  0.0079  158 ALA H N   
3270 C CA  . ALA B 168 ? 1.1435 0.7727 0.9070 -0.0585 0.2558  0.0105  158 ALA H CA  
3271 C C   . ALA B 168 ? 1.1476 0.7795 0.9178 -0.0384 0.2548  0.0148  158 ALA H C   
3272 O O   . ALA B 168 ? 1.1719 0.7838 0.9282 -0.0234 0.2635  0.0189  158 ALA H O   
3273 C CB  . ALA B 168 ? 1.1674 0.7685 0.9059 -0.0752 0.2656  0.0051  158 ALA H CB  
3274 N N   . LEU B 169 ? 1.1268 0.7835 0.9175 -0.0378 0.2449  0.0136  159 LEU H N   
3275 C CA  . LEU B 169 ? 1.1176 0.7825 0.9190 -0.0215 0.2437  0.0160  159 LEU H CA  
3276 C C   . LEU B 169 ? 1.0855 0.7856 0.9164 -0.0135 0.2322  0.0171  159 LEU H C   
3277 O O   . LEU B 169 ? 1.0599 0.7807 0.9063 -0.0224 0.2231  0.0152  159 LEU H O   
3278 C CB  . LEU B 169 ? 1.1181 0.7789 0.9165 -0.0284 0.2441  0.0132  159 LEU H CB  
3279 C CG  . LEU B 169 ? 1.1028 0.7729 0.9131 -0.0146 0.2442  0.0145  159 LEU H CG  
3280 C CD1 . LEU B 169 ? 1.1287 0.7802 0.9258 0.0017  0.2546  0.0173  159 LEU H CD1 
3281 C CD2 . LEU B 169 ? 1.1079 0.7737 0.9143 -0.0233 0.2447  0.0118  159 LEU H CD2 
3282 N N   . THR B 170 ? 1.0836 0.7898 0.9204 0.0039  0.2330  0.0199  160 THR H N   
3283 C CA  . THR B 170 ? 1.0487 0.7872 0.9120 0.0120  0.2233  0.0197  160 THR H CA  
3284 C C   . THR B 170 ? 1.0420 0.7918 0.9157 0.0282  0.2244  0.0194  160 THR H C   
3285 O O   . THR B 170 ? 1.0097 0.7860 0.9068 0.0301  0.2175  0.0168  160 THR H O   
3286 C CB  . THR B 170 ? 1.0437 0.7869 0.9071 0.0160  0.2212  0.0218  160 THR H CB  
3287 O OG1 . THR B 170 ? 1.0739 0.7994 0.9200 0.0311  0.2293  0.0253  160 THR H OG1 
3288 C CG2 . THR B 170 ? 1.0449 0.7790 0.8991 -0.0005 0.2215  0.0212  160 THR H CG2 
3289 N N   . SER B 171 ? 1.0736 0.8035 0.9295 0.0399  0.2337  0.0216  161 SER H N   
3290 C CA  . SER B 171 ? 1.0823 0.8255 0.9478 0.0567  0.2354  0.0207  161 SER H CA  
3291 C C   . SER B 171 ? 1.0784 0.8294 0.9556 0.0499  0.2355  0.0170  161 SER H C   
3292 O O   . SER B 171 ? 1.0872 0.8163 0.9495 0.0392  0.2406  0.0170  161 SER H O   
3293 C CB  . SER B 171 ? 1.1191 0.8370 0.9599 0.0719  0.2462  0.0245  161 SER H CB  
3294 O OG  . SER B 171 ? 1.1412 0.8541 0.9717 0.0821  0.2465  0.0284  161 SER H OG  
3295 N N   . GLY B 172 ? 1.0667 0.8486 0.9696 0.0556  0.2305  0.0132  162 GLY H N   
3296 C CA  . GLY B 172 ? 1.0567 0.8468 0.9716 0.0507  0.2324  0.0093  162 GLY H CA  
3297 C C   . GLY B 172 ? 1.0392 0.8390 0.9670 0.0350  0.2258  0.0073  162 GLY H C   
3298 O O   . GLY B 172 ? 1.0366 0.8438 0.9750 0.0306  0.2275  0.0041  162 GLY H O   
3299 N N   . VAL B 173 ? 1.0249 0.8240 0.9509 0.0274  0.2193  0.0092  163 VAL H N   
3300 C CA  . VAL B 173 ? 1.0021 0.8067 0.9354 0.0142  0.2134  0.0085  163 VAL H CA  
3301 C C   . VAL B 173 ? 0.9854 0.8178 0.9444 0.0165  0.2082  0.0048  163 VAL H C   
3302 O O   . VAL B 173 ? 0.9757 0.8247 0.9454 0.0252  0.2050  0.0034  163 VAL H O   
3303 C CB  . VAL B 173 ? 0.9886 0.7851 0.9114 0.0057  0.2089  0.0112  163 VAL H CB  
3304 C CG1 . VAL B 173 ? 0.9640 0.7706 0.8956 -0.0045 0.2020  0.0107  163 VAL H CG1 
3305 C CG2 . VAL B 173 ? 1.0172 0.7854 0.9140 0.0002  0.2154  0.0130  163 VAL H CG2 
3306 N N   . HIS B 174 ? 0.9870 0.8222 0.9532 0.0087  0.2081  0.0030  164 HIS H N   
3307 C CA  . HIS B 174 ? 0.9688 0.8244 0.9557 0.0073  0.2046  -0.0007 164 HIS H CA  
3308 C C   . HIS B 174 ? 0.9490 0.7979 0.9320 -0.0025 0.2014  0.0015  164 HIS H C   
3309 O O   . HIS B 174 ? 0.9314 0.7669 0.9051 -0.0077 0.2054  0.0025  164 HIS H O   
3310 C CB  . HIS B 174 ? 0.9891 0.8554 0.9895 0.0099  0.2111  -0.0063 164 HIS H CB  
3311 C CG  . HIS B 174 ? 1.0146 0.8969 1.0239 0.0218  0.2127  -0.0098 164 HIS H CG  
3312 N ND1 . HIS B 174 ? 1.0154 0.9186 1.0368 0.0290  0.2067  -0.0122 164 HIS H ND1 
3313 C CD2 . HIS B 174 ? 1.0368 0.9187 1.0441 0.0292  0.2195  -0.0114 164 HIS H CD2 
3314 C CE1 . HIS B 174 ? 1.0303 0.9466 1.0565 0.0411  0.2092  -0.0151 164 HIS H CE1 
3315 N NE2 . HIS B 174 ? 1.0417 0.9456 1.0599 0.0418  0.2171  -0.0146 164 HIS H NE2 
3316 N N   . THR B 175 ? 0.9413 0.7996 0.9303 -0.0037 0.1942  0.0025  165 THR H N   
3317 C CA  . THR B 175 ? 0.9311 0.7870 0.9181 -0.0100 0.1905  0.0046  165 THR H CA  
3318 C C   . THR B 175 ? 0.9221 0.7901 0.9257 -0.0095 0.1911  0.0009  165 THR H C   
3319 O O   . THR B 175 ? 0.9230 0.8067 0.9400 -0.0061 0.1879  -0.0018 165 THR H O   
3320 C CB  . THR B 175 ? 0.9195 0.7773 0.9009 -0.0120 0.1833  0.0080  165 THR H CB  
3321 O OG1 . THR B 175 ? 0.9283 0.7726 0.8931 -0.0146 0.1850  0.0099  165 THR H OG1 
3322 C CG2 . THR B 175 ? 0.9136 0.7722 0.8927 -0.0162 0.1789  0.0103  165 THR H CG2 
3323 N N   . PHE B 176 ? 0.9149 0.7736 0.9157 -0.0134 0.1962  0.0007  166 PHE H N   
3324 C CA  . PHE B 176 ? 0.8866 0.7511 0.9003 -0.0148 0.2005  -0.0038 166 PHE H CA  
3325 C C   . PHE B 176 ? 0.8706 0.7362 0.8846 -0.0150 0.1955  -0.0013 166 PHE H C   
3326 O O   . PHE B 176 ? 0.8582 0.7166 0.8595 -0.0150 0.1906  0.0045  166 PHE H O   
3327 C CB  . PHE B 176 ? 0.8907 0.7404 0.8980 -0.0188 0.2103  -0.0047 166 PHE H CB  
3328 C CG  . PHE B 176 ? 0.8875 0.7378 0.8964 -0.0180 0.2166  -0.0080 166 PHE H CG  
3329 C CD1 . PHE B 176 ? 0.8754 0.7430 0.9030 -0.0170 0.2213  -0.0160 166 PHE H CD1 
3330 C CD2 . PHE B 176 ? 0.8999 0.7353 0.8916 -0.0178 0.2177  -0.0038 166 PHE H CD2 
3331 C CE1 . PHE B 176 ? 0.8806 0.7515 0.9104 -0.0143 0.2270  -0.0190 166 PHE H CE1 
3332 C CE2 . PHE B 176 ? 0.9064 0.7414 0.8987 -0.0156 0.2242  -0.0065 166 PHE H CE2 
3333 C CZ  . PHE B 176 ? 0.8970 0.7503 0.9086 -0.0130 0.2288  -0.0138 166 PHE H CZ  
3334 N N   . PRO B 177 ? 0.8600 0.7359 0.8882 -0.0151 0.1966  -0.0062 167 PRO H N   
3335 C CA  . PRO B 177 ? 0.8577 0.7300 0.8842 -0.0148 0.1947  -0.0040 167 PRO H CA  
3336 C C   . PRO B 177 ? 0.8707 0.7216 0.8807 -0.0160 0.1998  0.0008  167 PRO H C   
3337 O O   . PRO B 177 ? 0.8978 0.7368 0.9029 -0.0193 0.2084  -0.0005 167 PRO H O   
3338 C CB  . PRO B 177 ? 0.8541 0.7367 0.8972 -0.0168 0.1992  -0.0124 167 PRO H CB  
3339 C CG  . PRO B 177 ? 0.8449 0.7464 0.9012 -0.0155 0.1977  -0.0183 167 PRO H CG  
3340 C CD  . PRO B 177 ? 0.8548 0.7475 0.9011 -0.0150 0.1997  -0.0148 167 PRO H CD  
3341 N N   . ALA B 178 ? 0.8685 0.7154 0.8692 -0.0122 0.1946  0.0068  168 ALA H N   
3342 C CA  . ALA B 178 ? 0.8863 0.7140 0.8683 -0.0103 0.1980  0.0125  168 ALA H CA  
3343 C C   . ALA B 178 ? 0.9033 0.7154 0.8843 -0.0117 0.2097  0.0098  168 ALA H C   
3344 O O   . ALA B 178 ? 0.8971 0.7162 0.8920 -0.0134 0.2122  0.0041  168 ALA H O   
3345 C CB  . ALA B 178 ? 0.8869 0.7198 0.8609 -0.0041 0.1887  0.0188  168 ALA H CB  
3346 N N   . VAL B 179 ? 0.9182 0.7080 0.8814 -0.0115 0.2175  0.0135  169 VAL H N   
3347 C CA  . VAL B 179 ? 0.9370 0.7050 0.8930 -0.0127 0.2307  0.0122  169 VAL H CA  
3348 C C   . VAL B 179 ? 0.9698 0.7228 0.9054 -0.0027 0.2289  0.0212  169 VAL H C   
3349 O O   . VAL B 179 ? 0.9756 0.7324 0.8993 0.0037  0.2196  0.0280  169 VAL H O   
3350 C CB  . VAL B 179 ? 0.9441 0.6945 0.8924 -0.0190 0.2434  0.0100  169 VAL H CB  
3351 C CG1 . VAL B 179 ? 0.9259 0.6943 0.8957 -0.0272 0.2456  0.0006  169 VAL H CG1 
3352 C CG2 . VAL B 179 ? 0.9550 0.6924 0.8808 -0.0147 0.2411  0.0180  169 VAL H CG2 
3353 N N   . LEU B 180 ? 0.9923 0.7290 0.9236 -0.0011 0.2383  0.0204  170 LEU H N   
3354 C CA  . LEU B 180 ? 1.0152 0.7330 0.9241 0.0106  0.2395  0.0292  170 LEU H CA  
3355 C C   . LEU B 180 ? 1.0593 0.7443 0.9430 0.0116  0.2526  0.0334  170 LEU H C   
3356 O O   . LEU B 180 ? 1.0669 0.7312 0.9490 0.0039  0.2685  0.0284  170 LEU H O   
3357 C CB  . LEU B 180 ? 1.0157 0.7279 0.9296 0.0123  0.2449  0.0263  170 LEU H CB  
3358 C CG  . LEU B 180 ? 1.0351 0.7255 0.9249 0.0268  0.2479  0.0355  170 LEU H CG  
3359 C CD1 . LEU B 180 ? 1.0269 0.7403 0.9152 0.0393  0.2307  0.0430  170 LEU H CD1 
3360 C CD2 . LEU B 180 ? 1.0368 0.7134 0.9292 0.0258  0.2583  0.0310  170 LEU H CD2 
3361 N N   . GLN B 181 ? 1.0934 0.7746 0.9571 0.0204  0.2460  0.0421  171 GLN H N   
3362 C CA  . GLN B 181 ? 1.1432 0.7929 0.9790 0.0236  0.2573  0.0475  171 GLN H CA  
3363 C C   . GLN B 181 ? 1.1920 0.8115 1.0053 0.0344  0.2679  0.0534  171 GLN H C   
3364 O O   . GLN B 181 ? 1.2070 0.8334 1.0259 0.0410  0.2639  0.0543  171 GLN H O   
3365 C CB  . GLN B 181 ? 1.1480 0.8053 0.9681 0.0306  0.2457  0.0542  171 GLN H CB  
3366 C CG  . GLN B 181 ? 1.1211 0.8037 0.9593 0.0205  0.2364  0.0488  171 GLN H CG  
3367 C CD  . GLN B 181 ? 1.1356 0.8253 0.9573 0.0260  0.2255  0.0541  171 GLN H CD  
3368 O OE1 . GLN B 181 ? 1.1129 0.8297 0.9450 0.0257  0.2111  0.0532  171 GLN H OE1 
3369 N NE2 . GLN B 181 ? 1.1735 0.8382 0.9682 0.0303  0.2329  0.0592  171 GLN H NE2 
3370 N N   . SER B 182 ? 1.2100 0.8407 1.0723 0.0619  0.3864  0.0532  172 SER H N   
3371 C CA  . SER B 182 ? 1.2474 0.8495 1.0923 0.0728  0.4102  0.0591  172 SER H CA  
3372 C C   . SER B 182 ? 1.2526 0.8553 1.0309 0.0867  0.3812  0.0645  172 SER H C   
3373 O O   . SER B 182 ? 1.2422 0.8455 1.0180 0.0900  0.3833  0.0653  172 SER H O   
3374 C CB  . SER B 182 ? 1.3190 0.8529 1.1396 0.0888  0.4652  0.0704  172 SER H CB  
3375 O OG  . SER B 182 ? 1.3740 0.8665 1.1152 0.1092  0.4661  0.0808  172 SER H OG  
3376 N N   . SER B 183 ? 1.2592 0.8630 0.9905 0.0950  0.3529  0.0661  173 SER H N   
3377 C CA  . SER B 183 ? 1.2713 0.8749 0.9485 0.1101  0.3222  0.0671  173 SER H CA  
3378 C C   . SER B 183 ? 1.2203 0.8865 0.9396 0.0928  0.2861  0.0591  173 SER H C   
3379 O O   . SER B 183 ? 1.2348 0.9079 0.9274 0.1021  0.2625  0.0581  173 SER H O   
3380 C CB  . SER B 183 ? 1.2929 0.8740 0.9159 0.1265  0.3037  0.0677  173 SER H CB  
3381 O OG  . SER B 183 ? 1.2355 0.8576 0.8996 0.1076  0.2827  0.0615  173 SER H OG  
3382 N N   . GLY B 184 ? 1.1700 0.8775 0.9532 0.0705  0.2821  0.0526  174 GLY H N   
3383 C CA  . GLY B 184 ? 1.1222 0.8805 0.9380 0.0577  0.2528  0.0467  174 GLY H CA  
3384 C C   . GLY B 184 ? 1.0959 0.8808 0.9163 0.0510  0.2255  0.0442  174 GLY H C   
3385 O O   . GLY B 184 ? 1.0503 0.8724 0.8979 0.0411  0.2067  0.0409  174 GLY H O   
3386 N N   . LEU B 185 ? 1.1135 0.8746 0.9048 0.0588  0.2259  0.0464  175 LEU H N   
3387 C CA  . LEU B 185 ? 1.0846 0.8662 0.8833 0.0527  0.2035  0.0436  175 LEU H CA  
3388 C C   . LEU B 185 ? 1.0608 0.8552 0.8973 0.0381  0.2121  0.0406  175 LEU H C   
3389 O O   . LEU B 185 ? 1.0579 0.8352 0.9095 0.0366  0.2370  0.0398  175 LEU H O   
3390 C CB  . LEU B 185 ? 1.1234 0.8699 0.8719 0.0706  0.1972  0.0446  175 LEU H CB  
3391 C CG  . LEU B 185 ? 1.1534 0.8790 0.8586 0.0914  0.1847  0.0437  175 LEU H CG  
3392 C CD1 . LEU B 185 ? 1.2009 0.8894 0.8546 0.1137  0.1708  0.0403  175 LEU H CD1 
3393 C CD2 . LEU B 185 ? 1.1124 0.8804 0.8491 0.0837  0.1589  0.0388  175 LEU H CD2 
3394 N N   . TYR B 186 ? 1.0385 0.8611 0.8938 0.0287  0.1922  0.0378  176 TYR H N   
3395 C CA  . TYR B 186 ? 1.0090 0.8451 0.8973 0.0173  0.1942  0.0332  176 TYR H CA  
3396 C C   . TYR B 186 ? 1.0204 0.8402 0.8942 0.0187  0.1953  0.0343  176 TYR H C   
3397 O O   . TYR B 186 ? 1.0454 0.8516 0.8865 0.0277  0.1856  0.0371  176 TYR H O   
3398 C CB  . TYR B 186 ? 0.9816 0.8522 0.8920 0.0095  0.1751  0.0309  176 TYR H CB  
3399 C CG  . TYR B 186 ? 0.9622 0.8470 0.8863 0.0098  0.1740  0.0287  176 TYR H CG  
3400 C CD1 . TYR B 186 ? 0.9562 0.8424 0.9078 0.0080  0.1805  0.0200  176 TYR H CD1 
3401 C CD2 . TYR B 186 ? 0.9520 0.8480 0.8658 0.0130  0.1652  0.0334  176 TYR H CD2 
3402 C CE1 . TYR B 186 ? 0.9537 0.8506 0.9156 0.0107  0.1763  0.0160  176 TYR H CE1 
3403 C CE2 . TYR B 186 ? 0.9519 0.8585 0.8740 0.0148  0.1649  0.0320  176 TYR H CE2 
3404 C CZ  . TYR B 186 ? 0.9552 0.8612 0.8978 0.0144  0.1695  0.0234  176 TYR H CZ  
3405 O OH  . TYR B 186 ? 0.9600 0.8741 0.9086 0.0187  0.1661  0.0201  176 TYR H OH  
3406 N N   . SER B 187 ? 1.0102 0.8311 0.9113 0.0112  0.2045  0.0298  177 SER H N   
3407 C CA  . SER B 187 ? 1.0265 0.8330 0.9182 0.0114  0.2073  0.0304  177 SER H CA  
3408 C C   . SER B 187 ? 1.0006 0.8309 0.9310 0.0000  0.1990  0.0229  177 SER H C   
3409 O O   . SER B 187 ? 0.9785 0.8197 0.9460 -0.0044 0.2030  0.0145  177 SER H O   
3410 C CB  . SER B 187 ? 1.0702 0.8351 0.9457 0.0204  0.2379  0.0338  177 SER H CB  
3411 O OG  . SER B 187 ? 1.0895 0.8357 0.9471 0.0237  0.2408  0.0357  177 SER H OG  
3412 N N   . LEU B 188 ? 1.0214 0.8573 0.9432 -0.0024 0.1855  0.0240  178 LEU H N   
3413 C CA  . LEU B 188 ? 1.0230 0.8791 0.9712 -0.0103 0.1741  0.0179  178 LEU H CA  
3414 C C   . LEU B 188 ? 1.0325 0.8764 0.9744 -0.0115 0.1762  0.0183  178 LEU H C   
3415 O O   . LEU B 188 ? 1.0517 0.8780 0.9621 -0.0058 0.1763  0.0241  178 LEU H O   
3416 C CB  . LEU B 188 ? 1.0247 0.9033 0.9683 -0.0118 0.1547  0.0211  178 LEU H CB  
3417 C CG  . LEU B 188 ? 1.0262 0.9188 0.9843 -0.0146 0.1437  0.0166  178 LEU H CG  
3418 C CD1 . LEU B 188 ? 1.0327 0.9370 0.9963 -0.0101 0.1375  0.0138  178 LEU H CD1 
3419 C CD2 . LEU B 188 ? 1.0365 0.9330 0.9836 -0.0171 0.1348  0.0229  178 LEU H CD2 
3420 N N   . SER B 189 ? 1.0195 0.8708 0.9907 -0.0166 0.1754  0.0100  179 SER H N   
3421 C CA  . SER B 189 ? 1.0164 0.8598 0.9856 -0.0187 0.1756  0.0094  179 SER H CA  
3422 C C   . SER B 189 ? 0.9876 0.8517 0.9663 -0.0226 0.1553  0.0055  179 SER H C   
3423 O O   . SER B 189 ? 0.9715 0.8498 0.9662 -0.0213 0.1458  -0.0011 179 SER H O   
3424 C CB  . SER B 189 ? 1.0301 0.8569 1.0269 -0.0191 0.1976  0.0029  179 SER H CB  
3425 O OG  . SER B 189 ? 1.0698 0.8645 1.0422 -0.0118 0.2225  0.0110  179 SER H OG  
3426 N N   . SER B 190 ? 0.9853 0.8460 0.9491 -0.0243 0.1491  0.0096  180 SER H N   
3427 C CA  . SER B 190 ? 0.9721 0.8445 0.9409 -0.0266 0.1350  0.0071  180 SER H CA  
3428 C C   . SER B 190 ? 0.9722 0.8339 0.9407 -0.0289 0.1374  0.0057  180 SER H C   
3429 O O   . SER B 190 ? 0.9781 0.8278 0.9252 -0.0283 0.1391  0.0120  180 SER H O   
3430 C CB  . SER B 190 ? 0.9658 0.8475 0.9193 -0.0268 0.1248  0.0157  180 SER H CB  
3431 O OG  . SER B 190 ? 0.9507 0.8370 0.9048 -0.0262 0.1167  0.0151  180 SER H OG  
3432 N N   . VAL B 191 ? 0.9735 0.8381 0.9655 -0.0293 0.1351  -0.0046 181 VAL H N   
3433 C CA  . VAL B 191 ? 0.9869 0.8415 0.9842 -0.0314 0.1394  -0.0073 181 VAL H CA  
3434 C C   . VAL B 191 ? 0.9890 0.8525 0.9877 -0.0308 0.1224  -0.0118 181 VAL H C   
3435 O O   . VAL B 191 ? 1.0031 0.8756 1.0020 -0.0256 0.1102  -0.0159 181 VAL H O   
3436 C CB  . VAL B 191 ? 0.9929 0.8379 1.0261 -0.0314 0.1575  -0.0175 181 VAL H CB  
3437 C CG1 . VAL B 191 ? 1.0161 0.8440 1.0416 -0.0292 0.1803  -0.0108 181 VAL H CG1 
3438 C CG2 . VAL B 191 ? 0.9758 0.8354 1.0525 -0.0292 0.1468  -0.0355 181 VAL H CG2 
3439 N N   . VAL B 192 ? 0.9941 0.8502 0.9880 -0.0333 0.1227  -0.0108 182 VAL H N   
3440 C CA  . VAL B 192 ? 0.9899 0.8495 0.9822 -0.0316 0.1089  -0.0147 182 VAL H CA  
3441 C C   . VAL B 192 ? 0.9918 0.8428 0.9991 -0.0338 0.1143  -0.0210 182 VAL H C   
3442 O O   . VAL B 192 ? 0.9823 0.8203 0.9824 -0.0366 0.1286  -0.0153 182 VAL H O   
3443 C CB  . VAL B 192 ? 0.9935 0.8539 0.9579 -0.0331 0.1023  -0.0021 182 VAL H CB  
3444 C CG1 . VAL B 192 ? 0.9997 0.8528 0.9510 -0.0380 0.1072  0.0063  182 VAL H CG1 
3445 C CG2 . VAL B 192 ? 0.9956 0.8533 0.9532 -0.0297 0.0926  -0.0040 182 VAL H CG2 
3446 N N   . THR B 193 ? 0.9994 0.8540 1.0242 -0.0296 0.1026  -0.0336 183 THR H N   
3447 C CA  . THR B 193 ? 1.0070 0.8551 1.0488 -0.0313 0.1057  -0.0405 183 THR H CA  
3448 C C   . THR B 193 ? 1.0171 0.8621 1.0288 -0.0312 0.0945  -0.0332 183 THR H C   
3449 O O   . THR B 193 ? 1.0236 0.8709 1.0179 -0.0248 0.0804  -0.0328 183 THR H O   
3450 C CB  . THR B 193 ? 1.0088 0.8626 1.0993 -0.0255 0.0983  -0.0632 183 THR H CB  
3451 O OG1 . THR B 193 ? 1.0225 0.8821 1.1020 -0.0139 0.0741  -0.0717 183 THR H OG1 
3452 C CG2 . THR B 193 ? 1.0094 0.8636 1.1444 -0.0279 0.1161  -0.0715 183 THR H CG2 
3453 N N   . VAL B 194 ? 1.0207 0.8558 1.0239 -0.0364 0.1030  -0.0271 184 VAL H N   
3454 C CA  . VAL B 194 ? 1.0188 0.8499 0.9989 -0.0376 0.0942  -0.0208 184 VAL H CA  
3455 C C   . VAL B 194 ? 1.0302 0.8525 1.0233 -0.0386 0.0990  -0.0272 184 VAL H C   
3456 O O   . VAL B 194 ? 1.0406 0.8569 1.0577 -0.0390 0.1144  -0.0329 184 VAL H O   
3457 C CB  . VAL B 194 ? 1.0186 0.8456 0.9722 -0.0417 0.0958  -0.0066 184 VAL H CB  
3458 C CG1 . VAL B 194 ? 1.0157 0.8519 0.9642 -0.0411 0.0940  -0.0010 184 VAL H CG1 
3459 C CG2 . VAL B 194 ? 1.0254 0.8370 0.9696 -0.0418 0.1079  -0.0036 184 VAL H CG2 
3460 N N   . PRO B 195 ? 1.0388 0.8577 1.0188 -0.0385 0.0895  -0.0259 185 PRO H N   
3461 C CA  . PRO B 195 ? 1.0379 0.8474 1.0274 -0.0394 0.0946  -0.0308 185 PRO H CA  
3462 C C   . PRO B 195 ? 1.0505 0.8430 1.0261 -0.0413 0.1122  -0.0225 185 PRO H C   
3463 O O   . PRO B 195 ? 1.0498 0.8365 0.9964 -0.0415 0.1104  -0.0122 185 PRO H O   
3464 C CB  . PRO B 195 ? 1.0436 0.8511 1.0119 -0.0389 0.0806  -0.0271 185 PRO H CB  
3465 C CG  . PRO B 195 ? 1.0432 0.8572 0.9985 -0.0343 0.0699  -0.0243 185 PRO H CG  
3466 C CD  . PRO B 195 ? 1.0407 0.8612 0.9974 -0.0366 0.0770  -0.0192 185 PRO H CD  
3467 N N   . SER B 196 ? 1.0654 0.8462 1.0621 -0.0399 0.1293  -0.0284 186 SER H N   
3468 C CA  . SER B 196 ? 1.0867 0.8403 1.0620 -0.0358 0.1515  -0.0202 186 SER H CA  
3469 C C   . SER B 196 ? 1.0999 0.8390 1.0365 -0.0334 0.1425  -0.0134 186 SER H C   
3470 O O   . SER B 196 ? 1.1361 0.8508 1.0339 -0.0257 0.1485  -0.0054 186 SER H O   
3471 C CB  . SER B 196 ? 1.1027 0.8443 1.1173 -0.0341 0.1787  -0.0278 186 SER H CB  
3472 O OG  . SER B 196 ? 1.1654 0.8710 1.1503 -0.0257 0.2073  -0.0172 186 SER H OG  
3473 N N   . SER B 197 ? 1.0844 0.8358 1.0298 -0.0375 0.1262  -0.0182 187 SER H N   
3474 C CA  . SER B 197 ? 1.0954 0.8349 1.0130 -0.0362 0.1169  -0.0140 187 SER H CA  
3475 C C   . SER B 197 ? 1.1117 0.8529 1.0016 -0.0365 0.0997  -0.0069 187 SER H C   
3476 O O   . SER B 197 ? 1.1424 0.8658 1.0050 -0.0313 0.0939  -0.0043 187 SER H O   
3477 C CB  . SER B 197 ? 1.0744 0.8256 1.0104 -0.0397 0.1054  -0.0212 187 SER H CB  
3478 O OG  . SER B 197 ? 1.0390 0.8105 0.9844 -0.0423 0.0897  -0.0236 187 SER H OG  
3479 N N   . SER B 198 ? 1.1155 0.8765 1.0162 -0.0411 0.0913  -0.0057 188 SER H N   
3480 C CA  . SER B 198 ? 1.1229 0.8898 1.0149 -0.0434 0.0765  -0.0010 188 SER H CA  
3481 C C   . SER B 198 ? 1.1338 0.8960 1.0140 -0.0389 0.0769  0.0015  188 SER H C   
3482 O O   . SER B 198 ? 1.1434 0.9177 1.0319 -0.0420 0.0676  0.0035  188 SER H O   
3483 C CB  . SER B 198 ? 1.1095 0.8948 1.0177 -0.0486 0.0708  0.0001  188 SER H CB  
3484 O OG  . SER B 198 ? 1.1037 0.8998 1.0219 -0.0477 0.0764  -0.0007 188 SER H OG  
3485 N N   . LEU B 199 ? 1.1469 0.8876 1.0070 -0.0299 0.0896  0.0016  189 LEU H N   
3486 C CA  . LEU B 199 ? 1.1596 0.8885 0.9990 -0.0211 0.0897  0.0035  189 LEU H CA  
3487 C C   . LEU B 199 ? 1.1767 0.8895 0.9912 -0.0115 0.0688  0.0005  189 LEU H C   
3488 O O   . LEU B 199 ? 1.1913 0.9023 0.9983 -0.0051 0.0572  -0.0015 189 LEU H O   
3489 C CB  . LEU B 199 ? 1.1854 0.8881 1.0068 -0.0112 0.1155  0.0058  189 LEU H CB  
3490 C CG  . LEU B 199 ? 1.1659 0.8850 1.0231 -0.0191 0.1341  0.0048  189 LEU H CG  
3491 C CD1 . LEU B 199 ? 1.1969 0.8851 1.0425 -0.0088 0.1651  0.0077  189 LEU H CD1 
3492 C CD2 . LEU B 199 ? 1.1440 0.8896 1.0180 -0.0257 0.1236  0.0050  189 LEU H CD2 
3493 N N   . GLY B 200 ? 1.1902 0.8910 0.9950 -0.0091 0.0616  -0.0021 190 GLY H N   
3494 C CA  . GLY B 200 ? 1.2154 0.8980 0.9992 0.0027  0.0380  -0.0089 190 GLY H CA  
3495 C C   . GLY B 200 ? 1.1982 0.9077 1.0230 -0.0083 0.0158  -0.0141 190 GLY H C   
3496 O O   . GLY B 200 ? 1.2127 0.9156 1.0381 0.0008  -0.0069 -0.0234 190 GLY H O   
3497 N N   . THR B 201 ? 1.1685 0.9045 1.0285 -0.0256 0.0234  -0.0092 191 THR H N   
3498 C CA  . THR B 201 ? 1.1491 0.9036 1.0489 -0.0358 0.0121  -0.0112 191 THR H CA  
3499 C C   . THR B 201 ? 1.1267 0.9017 1.0550 -0.0424 0.0161  -0.0080 191 THR H C   
3500 O O   . THR B 201 ? 1.1083 0.8918 1.0712 -0.0451 0.0047  -0.0131 191 THR H O   
3501 C CB  . THR B 201 ? 1.1341 0.8957 1.0457 -0.0459 0.0210  -0.0061 191 THR H CB  
3502 O OG1 . THR B 201 ? 1.1195 0.8919 1.0301 -0.0505 0.0383  0.0007  191 THR H OG1 
3503 C CG2 . THR B 201 ? 1.1466 0.8892 1.0338 -0.0402 0.0176  -0.0093 191 THR H CG2 
3504 N N   . GLN B 202 ? 1.1173 0.8998 1.0366 -0.0444 0.0325  -0.0010 192 GLN H N   
3505 C CA  . GLN B 202 ? 1.0906 0.8911 1.0321 -0.0500 0.0394  0.0036  192 GLN H CA  
3506 C C   . GLN B 202 ? 1.0843 0.8826 1.0205 -0.0424 0.0318  -0.0006 192 GLN H C   
3507 O O   . GLN B 202 ? 1.0996 0.8793 1.0024 -0.0312 0.0295  -0.0038 192 GLN H O   
3508 C CB  . GLN B 202 ? 1.0812 0.8887 1.0147 -0.0526 0.0560  0.0099  192 GLN H CB  
3509 C CG  . GLN B 202 ? 1.0878 0.8932 1.0194 -0.0553 0.0604  0.0116  192 GLN H CG  
3510 C CD  . GLN B 202 ? 1.1000 0.9069 1.0506 -0.0600 0.0605  0.0157  192 GLN H CD  
3511 O OE1 . GLN B 202 ? 1.0927 0.8922 1.0457 -0.0616 0.0555  0.0140  192 GLN H OE1 
3512 N NE2 . GLN B 202 ? 1.1108 0.9245 1.0761 -0.0615 0.0694  0.0219  192 GLN H NE2 
3513 N N   . THR B 203 ? 1.0676 0.8814 1.0353 -0.0468 0.0306  -0.0001 193 THR H N   
3514 C CA  . THR B 203 ? 1.0717 0.8864 1.0387 -0.0399 0.0232  -0.0045 193 THR H CA  
3515 C C   . THR B 203 ? 1.0491 0.8777 1.0180 -0.0448 0.0410  0.0047  193 THR H C   
3516 O O   . THR B 203 ? 1.0300 0.8695 1.0152 -0.0528 0.0541  0.0123  193 THR H O   
3517 C CB  . THR B 203 ? 1.0766 0.8982 1.0872 -0.0393 0.0044  -0.0153 193 THR H CB  
3518 O OG1 . THR B 203 ? 1.1022 0.9115 1.1159 -0.0349 -0.0135 -0.0255 193 THR H OG1 
3519 C CG2 . THR B 203 ? 1.0867 0.9050 1.0926 -0.0275 -0.0104 -0.0242 193 THR H CG2 
3520 N N   . TYR B 204 ? 1.0463 0.8698 0.9938 -0.0372 0.0414  0.0037  194 TYR H N   
3521 C CA  . TYR B 204 ? 1.0243 0.8589 0.9711 -0.0401 0.0563  0.0106  194 TYR H CA  
3522 C C   . TYR B 204 ? 1.0320 0.8688 0.9820 -0.0340 0.0492  0.0072  194 TYR H C   
3523 O O   . TYR B 204 ? 1.0321 0.8508 0.9518 -0.0221 0.0438  0.0030  194 TYR H O   
3524 C CB  . TYR B 204 ? 1.0130 0.8376 0.9328 -0.0375 0.0696  0.0129  194 TYR H CB  
3525 C CG  . TYR B 204 ? 0.9994 0.8233 0.9205 -0.0423 0.0748  0.0138  194 TYR H CG  
3526 C CD1 . TYR B 204 ? 0.9773 0.8138 0.9130 -0.0478 0.0794  0.0173  194 TYR H CD1 
3527 C CD2 . TYR B 204 ? 1.0078 0.8142 0.9111 -0.0382 0.0751  0.0108  194 TYR H CD2 
3528 C CE1 . TYR B 204 ? 0.9731 0.8062 0.9066 -0.0490 0.0809  0.0161  194 TYR H CE1 
3529 C CE2 . TYR B 204 ? 0.9993 0.8059 0.9069 -0.0422 0.0786  0.0102  194 TYR H CE2 
3530 C CZ  . TYR B 204 ? 0.9840 0.8050 0.9075 -0.0475 0.0798  0.0120  194 TYR H CZ  
3531 O OH  . TYR B 204 ? 0.9864 0.8049 0.9109 -0.0484 0.0801  0.0096  194 TYR H OH  
3532 N N   . ILE B 205 ? 1.0359 0.8909 1.0203 -0.0402 0.0514  0.0095  195 ILE H N   
3533 C CA  . ILE B 205 ? 1.0508 0.9115 1.0461 -0.0354 0.0448  0.0057  195 ILE H CA  
3534 C C   . ILE B 205 ? 1.0455 0.9181 1.0404 -0.0397 0.0630  0.0154  195 ILE H C   
3535 O O   . ILE B 205 ? 1.0285 0.9095 1.0381 -0.0465 0.0764  0.0231  195 ILE H O   
3536 C CB  . ILE B 205 ? 1.0496 0.9208 1.0968 -0.0376 0.0314  -0.0028 195 ILE H CB  
3537 C CG1 . ILE B 205 ? 1.0683 0.9288 1.1239 -0.0337 0.0112  -0.0145 195 ILE H CG1 
3538 C CG2 . ILE B 205 ? 1.0564 0.9323 1.1163 -0.0300 0.0197  -0.0106 195 ILE H CG2 
3539 C CD1 . ILE B 205 ? 1.0631 0.9280 1.1420 -0.0453 0.0224  -0.0087 195 ILE H CD1 
3540 N N   . CYS B 206 ? 1.0640 0.9325 1.0374 -0.0329 0.0635  0.0147  196 CYS H N   
3541 C CA  . CYS B 206 ? 1.0691 0.9486 1.0446 -0.0351 0.0766  0.0213  196 CYS H CA  
3542 C C   . CYS B 206 ? 1.0701 0.9617 1.0759 -0.0346 0.0712  0.0192  196 CYS H C   
3543 O O   . CYS B 206 ? 1.0833 0.9701 1.0939 -0.0274 0.0537  0.0094  196 CYS H O   
3544 C CB  . CYS B 206 ? 1.0847 0.9533 1.0284 -0.0288 0.0831  0.0215  196 CYS H CB  
3545 S SG  . CYS B 206 ? 1.1208 0.9730 1.0425 -0.0145 0.0711  0.0150  196 CYS H SG  
3546 N N   . ASN B 207 ? 1.0578 0.9615 1.0823 -0.0396 0.0858  0.0273  197 ASN H N   
3547 C CA  . ASN B 207 ? 1.0443 0.9598 1.1057 -0.0403 0.0866  0.0265  197 ASN H CA  
3548 C C   . ASN B 207 ? 1.0477 0.9672 1.0919 -0.0366 0.0945  0.0311  197 ASN H C   
3549 O O   . ASN B 207 ? 1.0343 0.9544 1.0673 -0.0371 0.1106  0.0403  197 ASN H O   
3550 C CB  . ASN B 207 ? 1.0258 0.9457 1.1245 -0.0468 0.1035  0.0339  197 ASN H CB  
3551 C CG  . ASN B 207 ? 1.0086 0.9215 1.1145 -0.0510 0.1016  0.0327  197 ASN H CG  
3552 O OD1 . ASN B 207 ? 0.9999 0.9138 1.1317 -0.0518 0.0842  0.0212  197 ASN H OD1 
3553 N ND2 . ASN B 207 ? 1.0009 0.9045 1.0821 -0.0513 0.1169  0.0427  197 ASN H ND2 
3554 N N   . VAL B 208 ? 1.0648 0.9832 1.1027 -0.0299 0.0812  0.0235  198 VAL H N   
3555 C CA  . VAL B 208 ? 1.0670 0.9884 1.0900 -0.0260 0.0873  0.0268  198 VAL H CA  
3556 C C   . VAL B 208 ? 1.0684 1.0044 1.1331 -0.0272 0.0896  0.0266  198 VAL H C   
3557 O O   . VAL B 208 ? 1.0817 1.0230 1.1865 -0.0272 0.0772  0.0172  198 VAL H O   
3558 C CB  . VAL B 208 ? 1.0861 0.9920 1.0736 -0.0154 0.0761  0.0202  198 VAL H CB  
3559 C CG1 . VAL B 208 ? 1.0865 0.9947 1.0624 -0.0110 0.0823  0.0229  198 VAL H CG1 
3560 C CG2 . VAL B 208 ? 1.0966 0.9852 1.0495 -0.0142 0.0814  0.0216  198 VAL H CG2 
3561 N N   . ASN B 209 ? 1.0632 1.0045 1.1225 -0.0272 0.1051  0.0353  199 ASN H N   
3562 C CA  . ASN B 209 ? 1.0610 1.0139 1.1588 -0.0278 0.1134  0.0374  199 ASN H CA  
3563 C C   . ASN B 209 ? 1.0406 0.9952 1.1145 -0.0225 0.1180  0.0409  199 ASN H C   
3564 O O   . ASN B 209 ? 1.0382 0.9871 1.0790 -0.0208 0.1286  0.0482  199 ASN H O   
3565 C CB  . ASN B 209 ? 1.0748 1.0265 1.1960 -0.0323 0.1375  0.0486  199 ASN H CB  
3566 C CG  . ASN B 209 ? 1.0838 1.0445 1.2608 -0.0338 0.1508  0.0499  199 ASN H CG  
3567 O OD1 . ASN B 209 ? 1.0950 1.0661 1.3249 -0.0364 0.1373  0.0373  199 ASN H OD1 
3568 N ND2 . ASN B 209 ? 1.0932 1.0477 1.2613 -0.0300 0.1770  0.0636  199 ASN H ND2 
3569 N N   . HIS B 210 ? 1.0236 0.9854 1.1169 -0.0184 0.1070  0.0333  200 HIS H N   
3570 C CA  . HIS B 210 ? 1.0074 0.9713 1.0826 -0.0132 0.1105  0.0358  200 HIS H CA  
3571 C C   . HIS B 210 ? 0.9947 0.9724 1.1195 -0.0135 0.1161  0.0350  200 HIS H C   
3572 O O   . HIS B 210 ? 0.9841 0.9679 1.1393 -0.0095 0.0976  0.0218  200 HIS H O   
3573 C CB  . HIS B 210 ? 1.0121 0.9646 1.0520 -0.0044 0.0928  0.0272  200 HIS H CB  
3574 C CG  . HIS B 210 ? 0.9994 0.9503 1.0156 0.0010  0.0979  0.0302  200 HIS H CG  
3575 N ND1 . HIS B 210 ? 1.0015 0.9499 1.0160 0.0108  0.0844  0.0222  200 HIS H ND1 
3576 C CD2 . HIS B 210 ? 0.9848 0.9345 0.9787 -0.0001 0.1128  0.0384  200 HIS H CD2 
3577 C CE1 . HIS B 210 ? 0.9969 0.9432 0.9884 0.0136  0.0943  0.0277  200 HIS H CE1 
3578 N NE2 . HIS B 210 ? 0.9844 0.9323 0.9658 0.0066  0.1110  0.0368  200 HIS H NE2 
3579 N N   . LYS B 211 ? 0.9992 0.9779 1.1312 -0.0156 0.1417  0.0481  201 LYS H N   
3580 C CA  . LYS B 211 ? 1.0050 0.9928 1.1900 -0.0164 0.1570  0.0504  201 LYS H CA  
3581 C C   . LYS B 211 ? 0.9914 0.9884 1.1809 -0.0109 0.1475  0.0445  201 LYS H C   
3582 O O   . LYS B 211 ? 0.9852 0.9943 1.2329 -0.0111 0.1444  0.0360  201 LYS H O   
3583 C CB  . LYS B 211 ? 1.0251 1.0004 1.1995 -0.0147 0.1913  0.0685  201 LYS H CB  
3584 C CG  . LYS B 211 ? 1.0433 1.0059 1.2192 -0.0179 0.2044  0.0750  201 LYS H CG  
3585 C CD  . LYS B 211 ? 1.0658 1.0069 1.2300 -0.0105 0.2418  0.0931  201 LYS H CD  
3586 C CE  . LYS B 211 ? 1.0824 1.0065 1.2457 -0.0116 0.2560  0.0997  201 LYS H CE  
3587 N NZ  . LYS B 211 ? 1.1197 1.0129 1.2649 0.0006  0.2969  0.1188  201 LYS H NZ  
3588 N N   . PRO B 212 ? 0.9903 0.9818 1.1255 -0.0054 0.1431  0.0474  202 PRO H N   
3589 C CA  . PRO B 212 ? 0.9892 0.9867 1.1236 0.0008  0.1329  0.0414  202 PRO H CA  
3590 C C   . PRO B 212 ? 1.0027 1.0047 1.1628 0.0061  0.1039  0.0228  202 PRO H C   
3591 O O   . PRO B 212 ? 1.0117 1.0217 1.1944 0.0118  0.0964  0.0157  202 PRO H O   
3592 C CB  . PRO B 212 ? 0.9812 0.9671 1.0525 0.0050  0.1312  0.0453  202 PRO H CB  
3593 C CG  . PRO B 212 ? 0.9800 0.9581 1.0298 0.0019  0.1479  0.0560  202 PRO H CG  
3594 C CD  . PRO B 212 ? 0.9895 0.9683 1.0687 -0.0042 0.1486  0.0551  202 PRO H CD  
3595 N N   . SER B 213 ? 1.0196 1.0138 1.1731 0.0070  0.0857  0.0137  203 SER H N   
3596 C CA  . SER B 213 ? 1.0399 1.0308 1.2081 0.0180  0.0531  -0.0067 203 SER H CA  
3597 C C   . SER B 213 ? 1.0544 1.0549 1.2886 0.0134  0.0426  -0.0190 203 SER H C   
3598 O O   . SER B 213 ? 1.0763 1.0729 1.3281 0.0249  0.0100  -0.0402 203 SER H O   
3599 C CB  . SER B 213 ? 1.0512 1.0166 1.1493 0.0293  0.0383  -0.0096 203 SER H CB  
3600 O OG  . SER B 213 ? 1.0266 0.9838 1.1092 0.0229  0.0426  -0.0053 203 SER H OG  
3601 N N   . ASN B 214 ? 1.0564 1.0658 1.3257 -0.0005 0.0695  -0.0069 204 ASN H N   
3602 C CA  . ASN B 214 ? 1.0698 1.0861 1.4044 -0.0071 0.0666  -0.0159 204 ASN H CA  
3603 C C   . ASN B 214 ? 1.0961 1.0992 1.4016 -0.0010 0.0375  -0.0284 204 ASN H C   
3604 O O   . ASN B 214 ? 1.1145 1.1211 1.4702 0.0036  0.0116  -0.0495 204 ASN H O   
3605 C CB  . ASN B 214 ? 1.0650 1.0990 1.4934 -0.0057 0.0569  -0.0342 204 ASN H CB  
3606 C CG  . ASN B 214 ? 1.0585 1.1030 1.5242 -0.0117 0.0920  -0.0206 204 ASN H CG  
3607 O OD1 . ASN B 214 ? 1.0632 1.1175 1.5549 -0.0054 0.0829  -0.0299 204 ASN H OD1 
3608 N ND2 . ASN B 214 ? 1.0549 1.0933 1.5197 -0.0212 0.1324  0.0012  204 ASN H ND2 
3609 N N   . THR B 215 ? 1.1092 1.0955 1.3371 0.0001  0.0421  -0.0168 205 THR H N   
3610 C CA  . THR B 215 ? 1.1389 1.1069 1.3280 0.0080  0.0198  -0.0257 205 THR H CA  
3611 C C   . THR B 215 ? 1.1435 1.1093 1.3264 -0.0043 0.0375  -0.0139 205 THR H C   
3612 O O   . THR B 215 ? 1.1399 1.1003 1.2797 -0.0096 0.0585  0.0022  205 THR H O   
3613 C CB  . THR B 215 ? 1.1595 1.1044 1.2687 0.0216  0.0132  -0.0234 205 THR H CB  
3614 O OG1 . THR B 215 ? 1.1785 1.1231 1.2916 0.0350  -0.0030 -0.0342 205 THR H OG1 
3615 C CG2 . THR B 215 ? 1.1787 1.0967 1.2411 0.0336  -0.0047 -0.0309 205 THR H CG2 
3616 N N   . LYS B 216 ? 1.1580 1.1278 1.3889 -0.0077 0.0267  -0.0246 206 LYS H N   
3617 C CA  . LYS B 216 ? 1.1581 1.1223 1.3804 -0.0166 0.0376  -0.0166 206 LYS H CA  
3618 C C   . LYS B 216 ? 1.1634 1.1097 1.3543 -0.0055 0.0079  -0.0308 206 LYS H C   
3619 O O   . LYS B 216 ? 1.1697 1.1135 1.3869 0.0063  -0.0231 -0.0521 206 LYS H O   
3620 C CB  . LYS B 216 ? 1.1691 1.1468 1.4687 -0.0286 0.0539  -0.0157 206 LYS H CB  
3621 C CG  . LYS B 216 ? 1.1928 1.1629 1.4823 -0.0375 0.0701  -0.0048 206 LYS H CG  
3622 C CD  . LYS B 216 ? 1.2058 1.1823 1.5683 -0.0477 0.0943  -0.0008 206 LYS H CD  
3623 C CE  . LYS B 216 ? 1.2140 1.1786 1.5597 -0.0540 0.1097  0.0098  206 LYS H CE  
3624 N NZ  . LYS B 216 ? 1.2255 1.1898 1.6402 -0.0620 0.1400  0.0160  206 LYS H NZ  
3625 N N   . VAL B 217 ? 1.1540 1.0853 1.2883 -0.0069 0.0168  -0.0203 207 VAL H N   
3626 C CA  . VAL B 217 ? 1.1739 1.0820 1.2674 0.0052  -0.0044 -0.0299 207 VAL H CA  
3627 C C   . VAL B 217 ? 1.1524 1.0576 1.2366 -0.0057 0.0093  -0.0204 207 VAL H C   
3628 O O   . VAL B 217 ? 1.1208 1.0305 1.1890 -0.0160 0.0347  -0.0044 207 VAL H O   
3629 C CB  . VAL B 217 ? 1.2076 1.0903 1.2279 0.0210  -0.0063 -0.0276 207 VAL H CB  
3630 C CG1 . VAL B 217 ? 1.2476 1.0972 1.2158 0.0368  -0.0207 -0.0342 207 VAL H CG1 
3631 C CG2 . VAL B 217 ? 1.2254 1.1073 1.2485 0.0345  -0.0214 -0.0374 207 VAL H CG2 
3632 N N   . ASP B 218 ? 1.1662 1.0625 1.2605 -0.0010 -0.0107 -0.0327 208 ASP H N   
3633 C CA  . ASP B 218 ? 1.1628 1.0526 1.2430 -0.0085 -0.0020 -0.0261 208 ASP H CA  
3634 C C   . ASP B 218 ? 1.1947 1.0535 1.2151 0.0085  -0.0189 -0.0332 208 ASP H C   
3635 O O   . ASP B 218 ? 1.2300 1.0735 1.2456 0.0265  -0.0486 -0.0509 208 ASP H O   
3636 C CB  . ASP B 218 ? 1.1542 1.0580 1.3012 -0.0188 -0.0053 -0.0323 208 ASP H CB  
3637 C CG  . ASP B 218 ? 1.1424 1.0680 1.3468 -0.0328 0.0189  -0.0231 208 ASP H CG  
3638 O OD1 . ASP B 218 ? 1.1430 1.0706 1.3220 -0.0393 0.0461  -0.0049 208 ASP H OD1 
3639 O OD2 . ASP B 218 ? 1.1474 1.0849 1.4233 -0.0350 0.0110  -0.0354 208 ASP H OD2 
3640 N N   . LYS B 219 ? 1.1865 1.0328 1.1619 0.0055  0.0002  -0.0205 209 LYS H N   
3641 C CA  . LYS B 219 ? 1.2239 1.0350 1.1383 0.0224  -0.0052 -0.0231 209 LYS H CA  
3642 C C   . LYS B 219 ? 1.2133 1.0208 1.1209 0.0133  0.0060  -0.0167 209 LYS H C   
3643 O O   . LYS B 219 ? 1.1861 1.0056 1.0976 -0.0005 0.0294  -0.0045 209 LYS H O   
3644 C CB  . LYS B 219 ? 1.2473 1.0404 1.1134 0.0308  0.0130  -0.0142 209 LYS H CB  
3645 C CG  . LYS B 219 ? 1.3076 1.0531 1.1049 0.0561  0.0101  -0.0172 209 LYS H CG  
3646 C CD  . LYS B 219 ? 1.3626 1.0855 1.1378 0.0822  -0.0218 -0.0335 209 LYS H CD  
3647 C CE  . LYS B 219 ? 1.4381 1.1028 1.1330 0.1140  -0.0266 -0.0371 209 LYS H CE  
3648 N NZ  . LYS B 219 ? 1.4514 1.1039 1.1400 0.1167  -0.0372 -0.0423 209 LYS H NZ  
3649 N N   . LYS B 220 ? 1.2282 1.0175 1.1252 0.0237  -0.0138 -0.0273 210 LYS H N   
3650 C CA  . LYS B 220 ? 1.2205 1.0026 1.1067 0.0178  -0.0056 -0.0227 210 LYS H CA  
3651 C C   . LYS B 220 ? 1.2210 0.9700 1.0453 0.0295  0.0127  -0.0150 210 LYS H C   
3652 O O   . LYS B 220 ? 1.2538 0.9673 1.0287 0.0529  0.0054  -0.0198 210 LYS H O   
3653 C CB  . LYS B 220 ? 1.2637 1.0372 1.1634 0.0258  -0.0344 -0.0380 210 LYS H CB  
3654 C CG  . LYS B 220 ? 1.2784 1.0439 1.1675 0.0204  -0.0279 -0.0340 210 LYS H CG  
3655 C CD  . LYS B 220 ? 1.2987 1.0609 1.2132 0.0253  -0.0566 -0.0500 210 LYS H CD  
3656 C CE  . LYS B 220 ? 1.3637 1.0913 1.2402 0.0556  -0.0897 -0.0686 210 LYS H CE  
3657 N NZ  . LYS B 220 ? 1.3852 1.1083 1.2886 0.0617  -0.1207 -0.0870 210 LYS H NZ  
3658 N N   . VAL B 221 ? 1.1865 0.9438 1.0152 0.0154  0.0376  -0.0040 211 VAL H N   
3659 C CA  . VAL B 221 ? 1.2000 0.9302 0.9896 0.0226  0.0620  0.0031  211 VAL H CA  
3660 C C   . VAL B 221 ? 1.2139 0.9217 0.9822 0.0282  0.0616  0.0016  211 VAL H C   
3661 O O   . VAL B 221 ? 1.1875 0.9121 0.9810 0.0134  0.0689  0.0044  211 VAL H O   
3662 C CB  . VAL B 221 ? 1.1596 0.9129 0.9773 0.0058  0.0862  0.0112  211 VAL H CB  
3663 C CG1 . VAL B 221 ? 1.1852 0.9125 0.9814 0.0112  0.1144  0.0160  211 VAL H CG1 
3664 C CG2 . VAL B 221 ? 1.1360 0.9099 0.9719 0.0014  0.0860  0.0127  211 VAL H CG2 
3665 N N   . GLU B 222 ? 1.2629 0.9288 0.9793 0.0529  0.0519  -0.0034 212 GLU H N   
3666 C CA  . GLU B 222 ? 1.2915 0.9293 0.9785 0.0631  0.0499  -0.0054 212 GLU H CA  
3667 C C   . GLU B 222 ? 1.3062 0.9143 0.9638 0.0677  0.0885  0.0058  212 GLU H C   
3668 O O   . GLU B 222 ? 1.3129 0.9015 0.9494 0.0760  0.1116  0.0123  212 GLU H O   
3669 C CB  . GLU B 222 ? 1.3579 0.9572 0.9965 0.0930  0.0200  -0.0179 212 GLU H CB  
3670 C CG  . GLU B 222 ? 1.3549 0.9828 1.0363 0.0899  -0.0187 -0.0333 212 GLU H CG  
3671 C CD  . GLU B 222 ? 1.4218 1.0159 1.0700 0.1195  -0.0579 -0.0525 212 GLU H CD  
3672 O OE1 . GLU B 222 ? 1.4517 1.0305 1.0818 0.1404  -0.0808 -0.0643 212 GLU H OE1 
3673 O OE2 . GLU B 222 ? 1.4514 1.0335 1.0922 0.1232  -0.0680 -0.0575 212 GLU H OE2 
3674 N N   . PRO B 223 ? 1.3100 0.9123 0.9701 0.0628  0.0986  0.0079  213 PRO H N   
3675 C CA  . PRO B 223 ? 1.3296 0.9052 0.9765 0.0658  0.1384  0.0169  213 PRO H CA  
3676 C C   . PRO B 223 ? 1.4038 0.9111 0.9735 0.0990  0.1564  0.0216  213 PRO H C   
3677 O O   . PRO B 223 ? 1.4367 0.9138 0.9542 0.1230  0.1304  0.0151  213 PRO H O   
3678 C CB  . PRO B 223 ? 1.3028 0.8945 0.9771 0.0522  0.1363  0.0151  213 PRO H CB  
3679 C CG  . PRO B 223 ? 1.3072 0.9049 0.9730 0.0563  0.0968  0.0060  213 PRO H CG  
3680 C CD  . PRO B 223 ? 1.2906 0.9115 0.9727 0.0539  0.0743  0.0010  213 PRO H CD  
3681 N N   . LYS B 224 ? 1.4353 0.9152 0.9997 0.1024  0.2020  0.0318  214 LYS H N   
3682 C CA  . LYS B 224 ? 1.5395 0.9449 1.0275 0.1357  0.2323  0.0403  214 LYS H CA  
3683 C C   . LYS B 224 ? 1.5455 0.9309 1.0513 0.1316  0.2775  0.0482  214 LYS H C   
3684 O O   . LYS B 224 ? 1.5590 0.9247 1.0398 0.1401  0.2724  0.0472  214 LYS H O   
3685 C CB  . LYS B 224 ? 1.5818 0.9615 1.0433 0.1494  0.2531  0.0467  214 LYS H CB  
3686 C CG  . LYS B 224 ? 1.5985 0.9893 1.0371 0.1588  0.2108  0.0381  214 LYS H CG  
3687 C CD  . LYS B 224 ? 1.6456 1.0071 1.0528 0.1742  0.2327  0.0450  214 LYS H CD  
3688 C CE  . LYS B 224 ? 1.6493 1.0290 1.0465 0.1808  0.1892  0.0344  214 LYS H CE  
3689 N NZ  . LYS B 224 ? 1.6779 1.0293 1.0444 0.1954  0.2114  0.0415  214 LYS H NZ  
3690 N N   . GLU C 1   ? 0.9897 0.9856 1.2433 0.0066  0.1823  -0.1194 1   GLU L N   
3691 C CA  . GLU C 1   ? 0.9562 0.9737 1.1914 -0.0008 0.1841  -0.1078 1   GLU L CA  
3692 C C   . GLU C 1   ? 0.9427 0.9579 1.1402 -0.0146 0.1884  -0.0965 1   GLU L C   
3693 O O   . GLU C 1   ? 0.9497 0.9446 1.1323 -0.0179 0.1872  -0.0942 1   GLU L O   
3694 C CB  . GLU C 1   ? 0.9530 0.9671 1.1917 0.0111  0.1668  -0.0954 1   GLU L CB  
3695 C CG  . GLU C 1   ? 0.9800 0.9626 1.1989 0.0164  0.1507  -0.0813 1   GLU L CG  
3696 C CD  . GLU C 1   ? 0.9933 0.9697 1.2135 0.0263  0.1330  -0.0701 1   GLU L CD  
3697 O OE1 . GLU C 1   ? 1.0090 0.9894 1.2611 0.0388  0.1242  -0.0778 1   GLU L OE1 
3698 O OE2 . GLU C 1   ? 0.9998 0.9692 1.1905 0.0205  0.1285  -0.0554 1   GLU L OE2 
3699 N N   . ILE C 2   ? 0.9239 0.9595 1.1070 -0.0224 0.1926  -0.0902 2   ILE L N   
3700 C CA  . ILE C 2   ? 0.9175 0.9587 1.0721 -0.0343 0.1956  -0.0823 2   ILE L CA  
3701 C C   . ILE C 2   ? 0.9040 0.9380 1.0438 -0.0299 0.1841  -0.0673 2   ILE L C   
3702 O O   . ILE C 2   ? 0.8735 0.9076 1.0187 -0.0209 0.1757  -0.0605 2   ILE L O   
3703 C CB  . ILE C 2   ? 0.9106 0.9729 1.0562 -0.0437 0.2025  -0.0830 2   ILE L CB  
3704 C CG1 . ILE C 2   ? 0.9203 0.9880 1.0781 -0.0516 0.2160  -0.0999 2   ILE L CG1 
3705 C CG2 . ILE C 2   ? 0.9140 0.9844 1.0348 -0.0543 0.2025  -0.0764 2   ILE L CG2 
3706 C CD1 . ILE C 2   ? 0.9281 1.0083 1.0659 -0.0664 0.2228  -0.1005 2   ILE L CD1 
3707 N N   . VAL C 3   ? 0.9113 0.9398 1.0317 -0.0386 0.1853  -0.0642 3   VAL L N   
3708 C CA  . VAL C 3   ? 0.9179 0.9389 1.0227 -0.0389 0.1780  -0.0540 3   VAL L CA  
3709 C C   . VAL C 3   ? 0.9054 0.9524 1.0017 -0.0442 0.1795  -0.0498 3   VAL L C   
3710 O O   . VAL C 3   ? 0.9156 0.9756 1.0042 -0.0544 0.1851  -0.0537 3   VAL L O   
3711 C CB  . VAL C 3   ? 0.9348 0.9314 1.0229 -0.0473 0.1791  -0.0554 3   VAL L CB  
3712 C CG1 . VAL C 3   ? 0.9376 0.9267 1.0051 -0.0531 0.1747  -0.0473 3   VAL L CG1 
3713 C CG2 . VAL C 3   ? 0.9530 0.9188 1.0502 -0.0393 0.1742  -0.0595 3   VAL L CG2 
3714 N N   . MET C 4   ? 0.8893 0.9434 0.9884 -0.0365 0.1735  -0.0425 4   MET L N   
3715 C CA  . MET C 4   ? 0.8748 0.9506 0.9696 -0.0378 0.1725  -0.0390 4   MET L CA  
3716 C C   . MET C 4   ? 0.8880 0.9630 0.9722 -0.0448 0.1731  -0.0385 4   MET L C   
3717 O O   . MET C 4   ? 0.8941 0.9500 0.9713 -0.0444 0.1703  -0.0350 4   MET L O   
3718 C CB  . MET C 4   ? 0.8569 0.9365 0.9576 -0.0275 0.1671  -0.0329 4   MET L CB  
3719 C CG  . MET C 4   ? 0.8466 0.9289 0.9542 -0.0243 0.1683  -0.0346 4   MET L CG  
3720 S SD  . MET C 4   ? 0.8383 0.9359 0.9375 -0.0331 0.1720  -0.0384 4   MET L SD  
3721 C CE  . MET C 4   ? 0.8476 0.9360 0.9519 -0.0412 0.1818  -0.0497 4   MET L CE  
3722 N N   . THR C 5   ? 0.8981 0.9942 0.9801 -0.0529 0.1764  -0.0432 5   THR L N   
3723 C CA  . THR C 5   ? 0.9102 1.0120 0.9848 -0.0628 0.1799  -0.0469 5   THR L CA  
3724 C C   . THR C 5   ? 0.8925 1.0271 0.9794 -0.0593 0.1775  -0.0494 5   THR L C   
3725 O O   . THR C 5   ? 0.8813 1.0380 0.9750 -0.0600 0.1754  -0.0528 5   THR L O   
3726 C CB  . THR C 5   ? 0.9317 1.0292 0.9950 -0.0781 0.1870  -0.0542 5   THR L CB  
3727 O OG1 . THR C 5   ? 0.9496 1.0144 1.0052 -0.0775 0.1874  -0.0525 5   THR L OG1 
3728 C CG2 . THR C 5   ? 0.9493 1.0489 1.0008 -0.0927 0.1930  -0.0600 5   THR L CG2 
3729 N N   . GLN C 6   ? 0.8889 1.0248 0.9784 -0.0557 0.1770  -0.0483 6   GLN L N   
3730 C CA  . GLN C 6   ? 0.8770 1.0423 0.9830 -0.0497 0.1745  -0.0527 6   GLN L CA  
3731 C C   . GLN C 6   ? 0.8842 1.0688 0.9928 -0.0636 0.1827  -0.0653 6   GLN L C   
3732 O O   . GLN C 6   ? 0.8987 1.0657 0.9892 -0.0789 0.1908  -0.0681 6   GLN L O   
3733 C CB  . GLN C 6   ? 0.8643 1.0211 0.9735 -0.0387 0.1716  -0.0471 6   GLN L CB  
3734 C CG  . GLN C 6   ? 0.8508 0.9898 0.9572 -0.0276 0.1652  -0.0366 6   GLN L CG  
3735 C CD  . GLN C 6   ? 0.8425 0.9733 0.9502 -0.0189 0.1631  -0.0320 6   GLN L CD  
3736 O OE1 . GLN C 6   ? 0.8345 0.9432 0.9330 -0.0193 0.1629  -0.0266 6   GLN L OE1 
3737 N NE2 . GLN C 6   ? 0.8442 0.9925 0.9641 -0.0107 0.1604  -0.0348 6   GLN L NE2 
3738 N N   . SER C 7   ? 0.8830 1.1029 1.0142 -0.0584 0.1799  -0.0737 7   SER L N   
3739 C CA  . SER C 7   ? 0.8927 1.1404 1.0346 -0.0713 0.1885  -0.0900 7   SER L CA  
3740 C C   . SER C 7   ? 0.8781 1.1620 1.0531 -0.0576 0.1826  -0.0989 7   SER L C   
3741 O O   . SER C 7   ? 0.8723 1.1629 1.0593 -0.0401 0.1685  -0.0921 7   SER L O   
3742 C CB  . SER C 7   ? 0.9007 1.1605 1.0381 -0.0858 0.1916  -0.0968 7   SER L CB  
3743 O OG  . SER C 7   ? 0.8926 1.1659 1.0394 -0.0756 0.1794  -0.0922 7   SER L OG  
3744 N N   . PRO C 8   ? 0.8723 1.1789 1.0626 -0.0656 0.1929  -0.1155 8   PRO L N   
3745 C CA  . PRO C 8   ? 0.8805 1.1731 1.0489 -0.0899 0.2103  -0.1235 8   PRO L CA  
3746 C C   . PRO C 8   ? 0.8736 1.1249 1.0160 -0.0909 0.2137  -0.1122 8   PRO L C   
3747 O O   . PRO C 8   ? 0.8550 1.0930 1.0004 -0.0725 0.2042  -0.0999 8   PRO L O   
3748 C CB  . PRO C 8   ? 0.8869 1.2232 1.0851 -0.0977 0.2205  -0.1480 8   PRO L CB  
3749 C CG  . PRO C 8   ? 0.8723 1.2484 1.1127 -0.0743 0.2047  -0.1525 8   PRO L CG  
3750 C CD  . PRO C 8   ? 0.8640 1.2108 1.0937 -0.0526 0.1883  -0.1294 8   PRO L CD  
3751 N N   . ALA C 9   ? 0.8856 1.1146 0.9993 -0.1144 0.2267  -0.1165 9   ALA L N   
3752 C CA  . ALA C 9   ? 0.8953 1.0828 0.9793 -0.1191 0.2283  -0.1061 9   ALA L CA  
3753 C C   . ALA C 9   ? 0.8834 1.0849 0.9857 -0.1106 0.2314  -0.1124 9   ALA L C   
3754 O O   . ALA C 9   ? 0.8652 1.0472 0.9639 -0.0962 0.2232  -0.0993 9   ALA L O   
3755 C CB  . ALA C 9   ? 0.9324 1.0915 0.9776 -0.1488 0.2402  -0.1106 9   ALA L CB  
3756 N N   . THR C 10  ? 0.8929 1.1293 1.0161 -0.1206 0.2444  -0.1345 10  THR L N   
3757 C CA  . THR C 10  ? 0.8867 1.1434 1.0357 -0.1116 0.2491  -0.1457 10  THR L CA  
3758 C C   . THR C 10  ? 0.8674 1.1788 1.0681 -0.0971 0.2465  -0.1633 10  THR L C   
3759 O O   . THR C 10  ? 0.8698 1.2059 1.0815 -0.1031 0.2461  -0.1712 10  THR L O   
3760 C CB  . THR C 10  ? 0.9124 1.1577 1.0391 -0.1391 0.2690  -0.1597 10  THR L CB  
3761 O OG1 . THR C 10  ? 0.9390 1.1992 1.0586 -0.1654 0.2830  -0.1766 10  THR L OG1 
3762 C CG2 . THR C 10  ? 0.9363 1.1255 1.0130 -0.1498 0.2666  -0.1409 10  THR L CG2 
3763 N N   . LEU C 11  ? 0.8558 1.1845 1.0877 -0.0778 0.2435  -0.1696 11  LEU L N   
3764 C CA  . LEU C 11  ? 0.8358 1.2125 1.1198 -0.0585 0.2357  -0.1850 11  LEU L CA  
3765 C C   . LEU C 11  ? 0.8323 1.2277 1.1460 -0.0529 0.2460  -0.2048 11  LEU L C   
3766 O O   . LEU C 11  ? 0.8339 1.2001 1.1329 -0.0466 0.2466  -0.1953 11  LEU L O   
3767 C CB  . LEU C 11  ? 0.8255 1.1931 1.1148 -0.0306 0.2110  -0.1641 11  LEU L CB  
3768 C CG  . LEU C 11  ? 0.8197 1.2289 1.1491 -0.0142 0.1954  -0.1727 11  LEU L CG  
3769 C CD1 . LEU C 11  ? 0.8166 1.2048 1.1351 0.0061  0.1722  -0.1491 11  LEU L CD1 
3770 C CD2 . LEU C 11  ? 0.8233 1.2712 1.2034 0.0006  0.1955  -0.1959 11  LEU L CD2 
3771 N N   . SER C 12  ? 0.8341 1.2799 1.1915 -0.0564 0.2549  -0.2342 12  SER L N   
3772 C CA  . SER C 12  ? 0.8399 1.3092 1.2311 -0.0544 0.2690  -0.2597 12  SER L CA  
3773 C C   . SER C 12  ? 0.8276 1.3450 1.2843 -0.0239 0.2533  -0.2757 12  SER L C   
3774 O O   . SER C 12  ? 0.8249 1.3881 1.3155 -0.0262 0.2514  -0.2935 12  SER L O   
3775 C CB  . SER C 12  ? 0.8595 1.3445 1.2429 -0.0914 0.2983  -0.2859 12  SER L CB  
3776 O OG  . SER C 12  ? 0.8820 1.3802 1.2882 -0.0945 0.3161  -0.3098 12  SER L OG  
3777 N N   . VAL C 13  ? 0.8202 1.3249 1.2932 0.0043  0.2408  -0.2692 13  VAL L N   
3778 C CA  . VAL C 13  ? 0.8081 1.3458 1.3375 0.0381  0.2195  -0.2790 13  VAL L CA  
3779 C C   . VAL C 13  ? 0.8082 1.3460 1.3666 0.0537  0.2262  -0.2948 13  VAL L C   
3780 O O   . VAL C 13  ? 0.8060 1.3061 1.3300 0.0432  0.2406  -0.2872 13  VAL L O   
3781 C CB  . VAL C 13  ? 0.8014 1.3122 1.3130 0.0620  0.1875  -0.2473 13  VAL L CB  
3782 C CG1 . VAL C 13  ? 0.7936 1.3245 1.3017 0.0539  0.1769  -0.2422 13  VAL L CG1 
3783 C CG2 . VAL C 13  ? 0.7972 1.2467 1.2512 0.0592  0.1868  -0.2164 13  VAL L CG2 
3784 N N   . SER C 14  ? 0.8048 1.3852 1.4279 0.0794  0.2144  -0.3175 14  SER L N   
3785 C CA  . SER C 14  ? 0.8165 1.3992 1.4759 0.0995  0.2178  -0.3351 14  SER L CA  
3786 C C   . SER C 14  ? 0.8268 1.3682 1.4758 0.1343  0.1871  -0.3078 14  SER L C   
3787 O O   . SER C 14  ? 0.8307 1.3627 1.4678 0.1478  0.1595  -0.2854 14  SER L O   
3788 C CB  . SER C 14  ? 0.8132 1.4633 1.5520 0.1100  0.2211  -0.3769 14  SER L CB  
3789 O OG  . SER C 14  ? 0.8106 1.4984 1.5554 0.0735  0.2520  -0.4041 14  SER L OG  
3790 N N   . PRO C 15  ? 0.8411 1.3537 1.4898 0.1471  0.1917  -0.3092 15  PRO L N   
3791 C CA  . PRO C 15  ? 0.8543 1.3257 1.4933 0.1794  0.1632  -0.2863 15  PRO L CA  
3792 C C   . PRO C 15  ? 0.8664 1.3658 1.5577 0.2140  0.1297  -0.2933 15  PRO L C   
3793 O O   . PRO C 15  ? 0.8675 1.4152 1.6254 0.2269  0.1318  -0.3271 15  PRO L O   
3794 C CB  . PRO C 15  ? 0.8665 1.3165 1.5110 0.1839  0.1804  -0.2991 15  PRO L CB  
3795 C CG  . PRO C 15  ? 0.8585 1.3181 1.4837 0.1448  0.2188  -0.3142 15  PRO L CG  
3796 C CD  . PRO C 15  ? 0.8475 1.3610 1.4989 0.1281  0.2255  -0.3323 15  PRO L CD  
3797 N N   . GLY C 16  ? 0.8820 1.3507 1.5422 0.2276  0.0986  -0.2621 16  GLY L N   
3798 C CA  . GLY C 16  ? 0.9068 1.3924 1.6039 0.2587  0.0613  -0.2626 16  GLY L CA  
3799 C C   . GLY C 16  ? 0.9061 1.4160 1.5943 0.2475  0.0474  -0.2527 16  GLY L C   
3800 O O   . GLY C 16  ? 0.9253 1.4348 1.6225 0.2688  0.0122  -0.2425 16  GLY L O   
3801 N N   . GLU C 17  ? 0.8946 1.4223 1.5623 0.2132  0.0745  -0.2557 17  GLU L N   
3802 C CA  . GLU C 17  ? 0.8879 1.4364 1.5430 0.1980  0.0668  -0.2478 17  GLU L CA  
3803 C C   . GLU C 17  ? 0.8894 1.3815 1.4721 0.1879  0.0590  -0.2094 17  GLU L C   
3804 O O   . GLU C 17  ? 0.8851 1.3282 1.4289 0.1873  0.0655  -0.1922 17  GLU L O   
3805 C CB  . GLU C 17  ? 0.8706 1.4612 1.5367 0.1652  0.1001  -0.2711 17  GLU L CB  
3806 C CG  . GLU C 17  ? 0.8731 1.5274 1.6137 0.1703  0.1109  -0.3138 17  GLU L CG  
3807 C CD  . GLU C 17  ? 0.8621 1.5551 1.6081 0.1331  0.1461  -0.3388 17  GLU L CD  
3808 O OE1 . GLU C 17  ? 0.8500 1.5168 1.5396 0.1043  0.1601  -0.3210 17  GLU L OE1 
3809 O OE2 . GLU C 17  ? 0.8618 1.6097 1.6682 0.1324  0.1595  -0.3773 17  GLU L OE2 
3810 N N   . ARG C 18  ? 0.8970 1.3990 1.4641 0.1783  0.0467  -0.1986 18  ARG L N   
3811 C CA  . ARG C 18  ? 0.9049 1.3599 1.4101 0.1691  0.0378  -0.1661 18  ARG L CA  
3812 C C   . ARG C 18  ? 0.8880 1.3422 1.3605 0.1356  0.0650  -0.1629 18  ARG L C   
3813 O O   . ARG C 18  ? 0.8854 1.3746 1.3693 0.1209  0.0690  -0.1731 18  ARG L O   
3814 C CB  . ARG C 18  ? 0.9276 1.3884 1.4338 0.1812  0.0035  -0.1559 18  ARG L CB  
3815 C CG  . ARG C 18  ? 0.9416 1.3516 1.3840 0.1725  -0.0071 -0.1242 18  ARG L CG  
3816 C CD  . ARG C 18  ? 0.9695 1.3874 1.4086 0.1780  -0.0387 -0.1160 18  ARG L CD  
3817 N NE  . ARG C 18  ? 1.0060 1.4391 1.4863 0.2085  -0.0708 -0.1243 18  ARG L NE  
3818 C CZ  . ARG C 18  ? 1.0413 1.4347 1.5141 0.2324  -0.0905 -0.1140 18  ARG L CZ  
3819 N NH1 . ARG C 18  ? 1.0523 1.3893 1.4749 0.2270  -0.0805 -0.0945 18  ARG L NH1 
3820 N NH2 . ARG C 18  ? 1.0631 1.4725 1.5789 0.2619  -0.1211 -0.1240 18  ARG L NH2 
3821 N N   . ALA C 19  ? 0.8877 1.3001 1.3188 0.1241  0.0820  -0.1487 19  ALA L N   
3822 C CA  . ALA C 19  ? 0.8709 1.2723 1.2667 0.0956  0.1034  -0.1423 19  ALA L CA  
3823 C C   . ALA C 19  ? 0.8651 1.2419 1.2226 0.0903  0.0903  -0.1194 19  ALA L C   
3824 O O   . ALA C 19  ? 0.8683 1.2105 1.2023 0.1021  0.0748  -0.1008 19  ALA L O   
3825 C CB  . ALA C 19  ? 0.8724 1.2411 1.2433 0.0872  0.1229  -0.1372 19  ALA L CB  
3826 N N   . THR C 20  ? 0.8519 1.2450 1.2012 0.0701  0.0984  -0.1223 20  THR L N   
3827 C CA  . THR C 20  ? 0.8550 1.2300 1.1716 0.0622  0.0892  -0.1052 20  THR L CA  
3828 C C   . THR C 20  ? 0.8481 1.2026 1.1321 0.0387  0.1105  -0.0995 20  THR L C   
3829 O O   . THR C 20  ? 0.8318 1.2070 1.1205 0.0209  0.1242  -0.1116 20  THR L O   
3830 C CB  . THR C 20  ? 0.8519 1.2645 1.1899 0.0619  0.0743  -0.1140 20  THR L CB  
3831 O OG1 . THR C 20  ? 0.8617 1.2878 1.2295 0.0871  0.0498  -0.1174 20  THR L OG1 
3832 C CG2 . THR C 20  ? 0.8563 1.2509 1.1588 0.0502  0.0669  -0.0986 20  THR L CG2 
3833 N N   . LEU C 21  ? 0.8563 1.1690 1.1073 0.0386  0.1123  -0.0819 21  LEU L N   
3834 C CA  . LEU C 21  ? 0.8615 1.1509 1.0841 0.0207  0.1282  -0.0755 21  LEU L CA  
3835 C C   . LEU C 21  ? 0.8737 1.1512 1.0736 0.0129  0.1227  -0.0653 21  LEU L C   
3836 O O   . LEU C 21  ? 0.8766 1.1431 1.0672 0.0217  0.1080  -0.0553 21  LEU L O   
3837 C CB  . LEU C 21  ? 0.8574 1.1131 1.0632 0.0254  0.1332  -0.0653 21  LEU L CB  
3838 C CG  . LEU C 21  ? 0.8513 1.1131 1.0758 0.0342  0.1379  -0.0742 21  LEU L CG  
3839 C CD1 . LEU C 21  ? 0.8502 1.0786 1.0525 0.0316  0.1462  -0.0649 21  LEU L CD1 
3840 C CD2 . LEU C 21  ? 0.8482 1.1422 1.0953 0.0234  0.1509  -0.0945 21  LEU L CD2 
3841 N N   . SER C 22  ? 0.8764 1.1528 1.0647 -0.0051 0.1352  -0.0685 22  SER L N   
3842 C CA  . SER C 22  ? 0.8756 1.1421 1.0444 -0.0149 0.1338  -0.0625 22  SER L CA  
3843 C C   . SER C 22  ? 0.8838 1.1148 1.0291 -0.0209 0.1433  -0.0534 22  SER L C   
3844 O O   . SER C 22  ? 0.8816 1.0993 1.0244 -0.0220 0.1519  -0.0532 22  SER L O   
3845 C CB  . SER C 22  ? 0.8731 1.1642 1.0476 -0.0304 0.1394  -0.0744 22  SER L CB  
3846 O OG  . SER C 22  ? 0.8715 1.2010 1.0737 -0.0241 0.1290  -0.0850 22  SER L OG  
3847 N N   . CYS C 23  ? 0.9002 1.1171 1.0292 -0.0253 0.1412  -0.0472 23  CYS L N   
3848 C CA  . CYS C 23  ? 0.9068 1.0949 1.0203 -0.0298 0.1492  -0.0417 23  CYS L CA  
3849 C C   . CYS C 23  ? 0.9239 1.1086 1.0255 -0.0419 0.1523  -0.0437 23  CYS L C   
3850 O O   . CYS C 23  ? 0.9324 1.1223 1.0275 -0.0430 0.1446  -0.0418 23  CYS L O   
3851 C CB  . CYS C 23  ? 0.9083 1.0782 1.0164 -0.0191 0.1444  -0.0327 23  CYS L CB  
3852 S SG  . CYS C 23  ? 0.9060 1.0486 1.0023 -0.0242 0.1526  -0.0298 23  CYS L SG  
3853 N N   . ARG C 24  ? 0.9392 1.1115 1.0352 -0.0519 0.1631  -0.0477 24  ARG L N   
3854 C CA  . ARG C 24  ? 0.9526 1.1192 1.0383 -0.0642 0.1688  -0.0520 24  ARG L CA  
3855 C C   . ARG C 24  ? 0.9417 1.0809 1.0235 -0.0631 0.1755  -0.0507 24  ARG L C   
3856 O O   . ARG C 24  ? 0.9256 1.0487 1.0098 -0.0593 0.1780  -0.0494 24  ARG L O   
3857 C CB  . ARG C 24  ? 0.9773 1.1518 1.0606 -0.0778 0.1759  -0.0605 24  ARG L CB  
3858 C CG  . ARG C 24  ? 1.0022 1.1749 1.0742 -0.0922 0.1815  -0.0664 24  ARG L CG  
3859 C CD  . ARG C 24  ? 1.0328 1.1985 1.0968 -0.1067 0.1919  -0.0743 24  ARG L CD  
3860 N NE  . ARG C 24  ? 1.0507 1.2389 1.1208 -0.1116 0.1916  -0.0794 24  ARG L NE  
3861 C CZ  . ARG C 24  ? 1.0799 1.2926 1.1499 -0.1257 0.1938  -0.0889 24  ARG L CZ  
3862 N NH1 . ARG C 24  ? 1.0953 1.3112 1.1562 -0.1365 0.1953  -0.0925 24  ARG L NH1 
3863 N NH2 . ARG C 24  ? 1.0896 1.3254 1.1693 -0.1306 0.1955  -0.0965 24  ARG L NH2 
3864 N N   . ALA C 25  ? 0.9483 1.0825 1.0240 -0.0675 0.1777  -0.0524 25  ALA L N   
3865 C CA  . ALA C 25  ? 0.9519 1.0661 1.0302 -0.0676 0.1857  -0.0562 25  ALA L CA  
3866 C C   . ALA C 25  ? 0.9671 1.0739 1.0407 -0.0801 0.1954  -0.0656 25  ALA L C   
3867 O O   . ALA C 25  ? 0.9909 1.1092 1.0540 -0.0923 0.1971  -0.0694 25  ALA L O   
3868 C CB  . ALA C 25  ? 0.9539 1.0669 1.0283 -0.0679 0.1857  -0.0557 25  ALA L CB  
3869 N N   . SER C 26  ? 0.9700 1.0558 1.0509 -0.0768 0.2004  -0.0695 26  SER L N   
3870 C CA  . SER C 26  ? 0.9866 1.0586 1.0633 -0.0868 0.2096  -0.0790 26  SER L CA  
3871 C C   . SER C 26  ? 0.9945 1.0713 1.0686 -0.0975 0.2190  -0.0887 26  SER L C   
3872 O O   . SER C 26  ? 0.9934 1.0697 1.0565 -0.1118 0.2266  -0.0961 26  SER L O   
3873 C CB  . SER C 26  ? 0.9915 1.0358 1.0779 -0.0776 0.2092  -0.0807 26  SER L CB  
3874 O OG  . SER C 26  ? 0.9803 1.0221 1.0860 -0.0665 0.2085  -0.0834 26  SER L OG  
3875 N N   . GLN C 27  ? 1.1811 0.9406 1.1633 0.0180  0.0440  -0.2084 27  GLN L N   
3876 C CA  . GLN C 27  ? 1.2121 0.9900 1.1625 0.0316  0.0335  -0.2253 27  GLN L CA  
3877 C C   . GLN C 27  ? 1.1685 0.9912 1.1062 0.0383  0.0234  -0.2090 27  GLN L C   
3878 O O   . GLN C 27  ? 1.1235 0.9551 1.0723 0.0359  0.0282  -0.1834 27  GLN L O   
3879 C CB  . GLN C 27  ? 1.2475 1.0047 1.1710 0.0510  0.0467  -0.2226 27  GLN L CB  
3880 C CG  . GLN C 27  ? 1.3031 1.0108 1.2357 0.0485  0.0571  -0.2401 27  GLN L CG  
3881 C CD  . GLN C 27  ? 1.3335 1.0229 1.2425 0.0713  0.0721  -0.2322 27  GLN L CD  
3882 O OE1 . GLN C 27  ? 1.3923 1.0661 1.2819 0.0829  0.0728  -0.2557 27  GLN L OE1 
3883 N NE2 . GLN C 27  ? 1.3118 1.0058 1.2226 0.0786  0.0841  -0.2000 27  GLN L NE2 
3884 N N   . SER C 28  ? 1.1762 1.0256 1.0892 0.0475  0.0101  -0.2241 28  SER L N   
3885 C CA  . SER C 28  ? 1.1457 1.0356 1.0445 0.0557  0.0008  -0.2078 28  SER L CA  
3886 C C   . SER C 28  ? 1.1123 1.0037 0.9968 0.0670  0.0146  -0.1757 28  SER L C   
3887 O O   . SER C 28  ? 1.1243 1.0021 0.9920 0.0774  0.0264  -0.1734 28  SER L O   
3888 C CB  . SER C 28  ? 1.1720 1.0897 1.0416 0.0666  -0.0137 -0.2284 28  SER L CB  
3889 O OG  . SER C 28  ? 1.1517 1.1076 1.0078 0.0757  -0.0219 -0.2091 28  SER L OG  
3890 N N   . VAL C 29  ? 1.0833 0.9919 0.9765 0.0649  0.0132  -0.1521 29  VAL L N   
3891 C CA  . VAL C 29  ? 1.0619 0.9731 0.9461 0.0713  0.0250  -0.1232 29  VAL L CA  
3892 C C   . VAL C 29  ? 1.0638 1.0051 0.9313 0.0798  0.0177  -0.1079 29  VAL L C   
3893 O O   . VAL C 29  ? 1.0479 0.9916 0.9177 0.0796  0.0245  -0.0833 29  VAL L O   
3894 C CB  . VAL C 29  ? 1.0295 0.9238 0.9412 0.0597  0.0342  -0.1078 29  VAL L CB  
3895 C CG1 . VAL C 29  ? 1.0384 0.9028 0.9654 0.0530  0.0426  -0.1187 29  VAL L CG1 
3896 C CG2 . VAL C 29  ? 1.0078 0.9132 0.9415 0.0511  0.0255  -0.1035 29  VAL L CG2 
3897 N N   . SER C 30  ? 1.0878 1.0513 0.9377 0.0875  0.0042  -0.1230 30  SER L N   
3898 C CA  A SER C 30  ? 1.0922 1.0858 0.9236 0.0984  -0.0032 -0.1075 30  SER L CA  
3899 C CA  B SER C 30  ? 1.0935 1.0871 0.9248 0.0984  -0.0031 -0.1074 30  SER L CA  
3900 C C   . SER C 30  ? 1.0700 1.0643 0.9254 0.0920  -0.0051 -0.0881 30  SER L C   
3901 O O   . SER C 30  ? 1.0667 1.0584 0.9495 0.0819  -0.0124 -0.0996 30  SER L O   
3902 C CB  A SER C 30  ? 1.0987 1.1004 0.9005 0.1109  0.0083  -0.0889 30  SER L CB  
3903 C CB  B SER C 30  ? 1.1007 1.1023 0.9028 0.1108  0.0084  -0.0885 30  SER L CB  
3904 O OG  A SER C 30  ? 1.1214 1.1229 0.9018 0.1191  0.0112  -0.1088 30  SER L OG  
3905 O OG  B SER C 30  ? 1.1135 1.1419 0.8966 0.1218  0.0032  -0.0699 30  SER L OG  
3906 N N   . SER C 31  ? 1.0584 1.0560 0.9050 0.0978  0.0023  -0.0593 31  SER L N   
3907 C CA  A SER C 31  ? 1.0332 1.0244 0.9011 0.0933  0.0034  -0.0409 31  SER L CA  
3908 C CA  B SER C 31  ? 1.0368 1.0281 0.9046 0.0933  0.0034  -0.0408 31  SER L CA  
3909 C C   . SER C 31  ? 1.0059 0.9736 0.8822 0.0850  0.0202  -0.0240 31  SER L C   
3910 O O   . SER C 31  ? 0.9943 0.9547 0.8790 0.0835  0.0247  -0.0048 31  SER L O   
3911 C CB  A SER C 31  ? 1.0531 1.0657 0.9061 0.1070  -0.0036 -0.0226 31  SER L CB  
3912 C CB  B SER C 31  ? 1.0611 1.0738 0.9137 0.1071  -0.0035 -0.0224 31  SER L CB  
3913 O OG  A SER C 31  ? 1.0723 1.1132 0.9200 0.1147  -0.0216 -0.0397 31  SER L OG  
3914 O OG  B SER C 31  ? 1.0843 1.1020 0.9083 0.1159  0.0057  -0.0037 31  SER L OG  
3915 N N   . ASN C 32  ? 0.9876 0.9438 0.8619 0.0804  0.0291  -0.0324 32  ASN L N   
3916 C CA  . ASN C 32  ? 0.9664 0.9072 0.8486 0.0728  0.0434  -0.0194 32  ASN L CA  
3917 C C   . ASN C 32  ? 0.9554 0.8783 0.8655 0.0611  0.0450  -0.0270 32  ASN L C   
3918 O O   . ASN C 32  ? 0.9458 0.8577 0.8612 0.0573  0.0505  -0.0366 32  ASN L O   
3919 C CB  . ASN C 32  ? 0.9617 0.9055 0.8274 0.0774  0.0525  -0.0214 32  ASN L CB  
3920 C CG  . ASN C 32  ? 0.9774 0.9424 0.8157 0.0888  0.0547  -0.0098 32  ASN L CG  
3921 O OD1 . ASN C 32  ? 1.0042 0.9804 0.8224 0.0992  0.0536  -0.0217 32  ASN L OD1 
3922 N ND2 . ASN C 32  ? 0.9698 0.9392 0.8068 0.0871  0.0591  0.0134  32  ASN L ND2 
3923 N N   . LEU C 33  ? 0.9591 0.8795 0.8858 0.0573  0.0414  -0.0212 33  LEU L N   
3924 C CA  . LEU C 33  ? 0.9421 0.8510 0.8949 0.0478  0.0427  -0.0282 33  LEU L CA  
3925 C C   . LEU C 33  ? 0.9350 0.8371 0.8985 0.0450  0.0471  -0.0138 33  LEU L C   
3926 O O   . LEU C 33  ? 0.9502 0.8576 0.9107 0.0517  0.0422  -0.0043 33  LEU L O   
3927 C CB  . LEU C 33  ? 0.9523 0.8714 0.9178 0.0477  0.0304  -0.0450 33  LEU L CB  
3928 C CG  . LEU C 33  ? 0.9375 0.8486 0.9317 0.0368  0.0326  -0.0549 33  LEU L CG  
3929 C CD1 . LEU C 33  ? 0.9198 0.8288 0.9310 0.0347  0.0368  -0.0438 33  LEU L CD1 
3930 C CD2 . LEU C 33  ? 0.9406 0.8331 0.9353 0.0305  0.0434  -0.0594 33  LEU L CD2 
3931 N N   . ALA C 34  ? 0.9105 0.8002 0.8850 0.0365  0.0565  -0.0124 34  ALA L N   
3932 C CA  . ALA C 34  ? 0.8923 0.7727 0.8764 0.0327  0.0616  -0.0036 34  ALA L CA  
3933 C C   . ALA C 34  ? 0.8697 0.7470 0.8759 0.0283  0.0629  -0.0122 34  ALA L C   
3934 O O   . ALA C 34  ? 0.8498 0.7285 0.8635 0.0244  0.0641  -0.0215 34  ALA L O   
3935 C CB  . ALA C 34  ? 0.8786 0.7534 0.8549 0.0264  0.0712  0.0042  34  ALA L CB  
3936 N N   . TRP C 35  ? 0.8690 0.7411 0.8858 0.0296  0.0641  -0.0082 35  TRP L N   
3937 C CA  . TRP C 35  ? 0.8548 0.7269 0.8919 0.0268  0.0676  -0.0149 35  TRP L CA  
3938 C C   . TRP C 35  ? 0.8445 0.7037 0.8806 0.0222  0.0773  -0.0122 35  TRP L C   
3939 O O   . TRP C 35  ? 0.8521 0.7003 0.8790 0.0224  0.0789  -0.0049 35  TRP L O   
3940 C CB  . TRP C 35  ? 0.8584 0.7405 0.9107 0.0354  0.0601  -0.0161 35  TRP L CB  
3941 C CG  . TRP C 35  ? 0.8622 0.7639 0.9229 0.0366  0.0499  -0.0249 35  TRP L CG  
3942 C CD1 . TRP C 35  ? 0.8766 0.7909 0.9271 0.0441  0.0383  -0.0244 35  TRP L CD1 
3943 C CD2 . TRP C 35  ? 0.8535 0.7661 0.9357 0.0291  0.0502  -0.0365 35  TRP L CD2 
3944 N NE1 . TRP C 35  ? 0.8749 0.8079 0.9391 0.0409  0.0299  -0.0382 35  TRP L NE1 
3945 C CE2 . TRP C 35  ? 0.8637 0.7943 0.9494 0.0305  0.0375  -0.0453 35  TRP L CE2 
3946 C CE3 . TRP C 35  ? 0.8416 0.7516 0.9401 0.0210  0.0606  -0.0398 35  TRP L CE3 
3947 C CZ2 . TRP C 35  ? 0.8553 0.7988 0.9638 0.0212  0.0348  -0.0588 35  TRP L CZ2 
3948 C CZ3 . TRP C 35  ? 0.8387 0.7609 0.9590 0.0131  0.0597  -0.0494 35  TRP L CZ3 
3949 C CH2 . TRP C 35  ? 0.8430 0.7804 0.9700 0.0118  0.0469  -0.0595 35  TRP L CH2 
3950 N N   . TYR C 36  ? 0.8344 0.6957 0.8801 0.0174  0.0842  -0.0183 36  TYR L N   
3951 C CA  . TYR C 36  ? 0.8462 0.7003 0.8892 0.0131  0.0926  -0.0195 36  TYR L CA  
3952 C C   . TYR C 36  ? 0.8523 0.7105 0.9115 0.0158  0.0976  -0.0259 36  TYR L C   
3953 O O   . TYR C 36  ? 0.8546 0.7244 0.9292 0.0179  0.0962  -0.0283 36  TYR L O   
3954 C CB  . TYR C 36  ? 0.8418 0.7006 0.8738 0.0066  0.0976  -0.0189 36  TYR L CB  
3955 C CG  . TYR C 36  ? 0.8501 0.7090 0.8671 0.0045  0.0950  -0.0127 36  TYR L CG  
3956 C CD1 . TYR C 36  ? 0.8588 0.7215 0.8707 0.0083  0.0900  -0.0103 36  TYR L CD1 
3957 C CD2 . TYR C 36  ? 0.8592 0.7168 0.8680 -0.0017 0.0979  -0.0107 36  TYR L CD2 
3958 C CE1 . TYR C 36  ? 0.8636 0.7301 0.8613 0.0083  0.0893  -0.0043 36  TYR L CE1 
3959 C CE2 . TYR C 36  ? 0.8624 0.7254 0.8606 -0.0042 0.0969  -0.0038 36  TYR L CE2 
3960 C CZ  . TYR C 36  ? 0.8676 0.7357 0.8596 0.0019  0.0933  0.0002  36  TYR L CZ  
3961 O OH  . TYR C 36  ? 0.8747 0.7518 0.8559 0.0012  0.0938  0.0073  36  TYR L OH  
3962 N N   . GLN C 37  ? 0.8626 0.7127 0.9188 0.0149  0.1039  -0.0299 37  GLN L N   
3963 C CA  . GLN C 37  ? 0.8577 0.7131 0.9253 0.0187  0.1110  -0.0370 37  GLN L CA  
3964 C C   . GLN C 37  ? 0.8571 0.7142 0.9123 0.0128  0.1189  -0.0426 37  GLN L C   
3965 O O   . GLN C 37  ? 0.8697 0.7147 0.9139 0.0087  0.1187  -0.0466 37  GLN L O   
3966 C CB  . GLN C 37  ? 0.8751 0.7180 0.9506 0.0282  0.1104  -0.0395 37  GLN L CB  
3967 C CG  . GLN C 37  ? 0.8916 0.7413 0.9785 0.0349  0.1191  -0.0484 37  GLN L CG  
3968 C CD  . GLN C 37  ? 0.9119 0.7415 1.0016 0.0453  0.1208  -0.0528 37  GLN L CD  
3969 O OE1 . GLN C 37  ? 0.9284 0.7643 1.0348 0.0583  0.1209  -0.0524 37  GLN L OE1 
3970 N NE2 . GLN C 37  ? 0.9179 0.7231 0.9927 0.0396  0.1226  -0.0573 37  GLN L NE2 
3971 N N   . GLN C 38  ? 0.8479 0.7214 0.9054 0.0121  0.1257  -0.0426 38  GLN L N   
3972 C CA  . GLN C 38  ? 0.8578 0.7398 0.9014 0.0093  0.1328  -0.0469 38  GLN L CA  
3973 C C   . GLN C 38  ? 0.8741 0.7654 0.9244 0.0156  0.1422  -0.0544 38  GLN L C   
3974 O O   . GLN C 38  ? 0.8650 0.7704 0.9281 0.0184  0.1485  -0.0495 38  GLN L O   
3975 C CB  . GLN C 38  ? 0.8445 0.7392 0.8806 0.0062  0.1351  -0.0376 38  GLN L CB  
3976 C CG  . GLN C 38  ? 0.8511 0.7588 0.8685 0.0045  0.1391  -0.0401 38  GLN L CG  
3977 C CD  . GLN C 38  ? 0.8513 0.7701 0.8600 0.0048  0.1406  -0.0280 38  GLN L CD  
3978 O OE1 . GLN C 38  ? 0.8394 0.7533 0.8568 0.0062  0.1418  -0.0186 38  GLN L OE1 
3979 N NE2 . GLN C 38  ? 0.8654 0.7999 0.8573 0.0040  0.1405  -0.0290 38  GLN L NE2 
3980 N N   . LYS C 39  ? 0.8949 0.7778 0.9371 0.0172  0.1441  -0.0671 39  LYS L N   
3981 C CA  . LYS C 39  ? 0.9072 0.8001 0.9503 0.0247  0.1541  -0.0773 39  LYS L CA  
3982 C C   . LYS C 39  ? 0.9061 0.8198 0.9298 0.0220  0.1602  -0.0792 39  LYS L C   
3983 O O   . LYS C 39  ? 0.8989 0.8152 0.9085 0.0145  0.1548  -0.0765 39  LYS L O   
3984 C CB  . LYS C 39  ? 0.9348 0.8052 0.9769 0.0291  0.1537  -0.0926 39  LYS L CB  
3985 C CG  . LYS C 39  ? 0.9332 0.7850 0.9935 0.0365  0.1489  -0.0880 39  LYS L CG  
3986 C CD  . LYS C 39  ? 0.9650 0.7884 1.0242 0.0430  0.1505  -0.1011 39  LYS L CD  
3987 C CE  . LYS C 39  ? 0.9709 0.7777 1.0468 0.0539  0.1460  -0.0925 39  LYS L CE  
3988 N NZ  . LYS C 39  ? 1.0134 0.7884 1.0894 0.0636  0.1502  -0.1039 39  LYS L NZ  
3989 N N   . PRO C 40  ? 0.9234 0.8568 0.9457 0.0296  0.1719  -0.0826 40  PRO L N   
3990 C CA  . PRO C 40  ? 0.9389 0.8970 0.9404 0.0299  0.1784  -0.0814 40  PRO L CA  
3991 C C   . PRO C 40  ? 0.9512 0.9095 0.9292 0.0241  0.1714  -0.0958 40  PRO L C   
3992 O O   . PRO C 40  ? 0.9659 0.9088 0.9407 0.0230  0.1688  -0.1154 40  PRO L O   
3993 C CB  . PRO C 40  ? 0.9560 0.9318 0.9595 0.0408  0.1924  -0.0874 40  PRO L CB  
3994 C CG  . PRO C 40  ? 0.9447 0.9125 0.9786 0.0448  0.1942  -0.0823 40  PRO L CG  
3995 C CD  . PRO C 40  ? 0.9313 0.8689 0.9721 0.0399  0.1801  -0.0862 40  PRO L CD  
3996 N N   . GLY C 41  ? 0.9576 0.9338 0.9212 0.0203  0.1685  -0.0860 41  GLY L N   
3997 C CA  . GLY C 41  ? 0.9812 0.9700 0.9240 0.0143  0.1615  -0.0988 41  GLY L CA  
3998 C C   . GLY C 41  ? 0.9837 0.9492 0.9326 0.0016  0.1495  -0.1074 41  GLY L C   
3999 O O   . GLY C 41  ? 1.0076 0.9772 0.9456 -0.0065 0.1439  -0.1253 41  GLY L O   
4000 N N   . GLN C 42  ? 0.9620 0.9052 0.9282 -0.0005 0.1459  -0.0947 42  GLN L N   
4001 C CA  . GLN C 42  ? 0.9602 0.8805 0.9329 -0.0111 0.1370  -0.0985 42  GLN L CA  
4002 C C   . GLN C 42  ? 0.9379 0.8596 0.9159 -0.0134 0.1320  -0.0791 42  GLN L C   
4003 O O   . GLN C 42  ? 0.9190 0.8499 0.8995 -0.0062 0.1356  -0.0645 42  GLN L O   
4004 C CB  . GLN C 42  ? 0.9647 0.8519 0.9517 -0.0082 0.1383  -0.1048 42  GLN L CB  
4005 C CG  . GLN C 42  ? 0.9905 0.8690 0.9724 -0.0053 0.1434  -0.1272 42  GLN L CG  
4006 C CD  . GLN C 42  ? 1.0006 0.8434 0.9971 0.0000  0.1448  -0.1315 42  GLN L CD  
4007 O OE1 . GLN C 42  ? 0.9773 0.8053 0.9870 0.0018  0.1412  -0.1167 42  GLN L OE1 
4008 N NE2 . GLN C 42  ? 1.0396 0.8692 1.0324 0.0045  0.1502  -0.1522 42  GLN L NE2 
4009 N N   . ALA C 43  ? 0.9402 0.8514 0.9203 -0.0236 0.1249  -0.0796 43  ALA L N   
4010 C CA  . ALA C 43  ? 0.9236 0.8337 0.9083 -0.0245 0.1207  -0.0634 43  ALA L CA  
4011 C C   . ALA C 43  ? 0.9144 0.7995 0.9120 -0.0191 0.1204  -0.0565 43  ALA L C   
4012 O O   . ALA C 43  ? 0.9177 0.7842 0.9221 -0.0166 0.1222  -0.0642 43  ALA L O   
4013 C CB  . ALA C 43  ? 0.9243 0.8378 0.9075 -0.0374 0.1149  -0.0656 43  ALA L CB  
4014 N N   . PRO C 44  ? 0.8983 0.7841 0.8993 -0.0155 0.1180  -0.0430 44  PRO L N   
4015 C CA  . PRO C 44  ? 0.8905 0.7585 0.9020 -0.0107 0.1152  -0.0377 44  PRO L CA  
4016 C C   . PRO C 44  ? 0.8888 0.7358 0.9026 -0.0146 0.1118  -0.0389 44  PRO L C   
4017 O O   . PRO C 44  ? 0.8817 0.7275 0.8900 -0.0242 0.1108  -0.0401 44  PRO L O   
4018 C CB  . PRO C 44  ? 0.8767 0.7522 0.8858 -0.0085 0.1122  -0.0266 44  PRO L CB  
4019 C CG  . PRO C 44  ? 0.8726 0.7672 0.8742 -0.0074 0.1168  -0.0243 44  PRO L CG  
4020 C CD  . PRO C 44  ? 0.8823 0.7870 0.8763 -0.0137 0.1178  -0.0331 44  PRO L CD  
4021 N N   . ARG C 45  ? 0.8814 0.7136 0.9050 -0.0067 0.1106  -0.0374 45  ARG L N   
4022 C CA  . ARG C 45  ? 0.9035 0.7122 0.9295 -0.0062 0.1087  -0.0344 45  ARG L CA  
4023 C C   . ARG C 45  ? 0.8961 0.7056 0.9239 0.0011  0.1026  -0.0216 45  ARG L C   
4024 O O   . ARG C 45  ? 0.8807 0.6989 0.9170 0.0100  0.1000  -0.0213 45  ARG L O   
4025 C CB  . ARG C 45  ? 0.9282 0.7208 0.9628 0.0010  0.1128  -0.0438 45  ARG L CB  
4026 C CG  . ARG C 45  ? 0.9624 0.7254 1.0007 0.0057  0.1123  -0.0385 45  ARG L CG  
4027 C CD  . ARG C 45  ? 0.9933 0.7421 1.0411 0.0173  0.1173  -0.0482 45  ARG L CD  
4028 N NE  . ARG C 45  ? 1.0356 0.7518 1.0876 0.0254  0.1183  -0.0419 45  ARG L NE  
4029 C CZ  . ARG C 45  ? 1.0556 0.7672 1.1186 0.0440  0.1179  -0.0370 45  ARG L CZ  
4030 N NH1 . ARG C 45  ? 1.0304 0.7716 1.1039 0.0539  0.1156  -0.0383 45  ARG L NH1 
4031 N NH2 . ARG C 45  ? 1.0985 0.7767 1.1637 0.0530  0.1202  -0.0298 45  ARG L NH2 
4032 N N   . LEU C 46  ? 0.8999 0.7033 0.9200 -0.0032 0.1004  -0.0117 46  LEU L N   
4033 C CA  . LEU C 46  ? 0.8932 0.7008 0.9098 0.0044  0.0946  0.0001  46  LEU L CA  
4034 C C   . LEU C 46  ? 0.9045 0.6986 0.9284 0.0169  0.0919  0.0048  46  LEU L C   
4035 O O   . LEU C 46  ? 0.9337 0.7042 0.9583 0.0172  0.0955  0.0093  46  LEU L O   
4036 C CB  . LEU C 46  ? 0.9043 0.7115 0.9098 -0.0029 0.0956  0.0108  46  LEU L CB  
4037 C CG  . LEU C 46  ? 0.9025 0.7165 0.8991 0.0059  0.0905  0.0236  46  LEU L CG  
4038 C CD1 . LEU C 46  ? 0.8800 0.7164 0.8717 0.0097  0.0861  0.0189  46  LEU L CD1 
4039 C CD2 . LEU C 46  ? 0.9232 0.7330 0.9111 -0.0011 0.0948  0.0373  46  LEU L CD2 
4040 N N   . LEU C 47  ? 0.8948 0.7043 0.9254 0.0272  0.0856  0.0039  47  LEU L N   
4041 C CA  . LEU C 47  ? 0.9137 0.7205 0.9525 0.0419  0.0810  0.0093  47  LEU L CA  
4042 C C   . LEU C 47  ? 0.9191 0.7322 0.9455 0.0488  0.0737  0.0231  47  LEU L C   
4043 O O   . LEU C 47  ? 0.9320 0.7293 0.9534 0.0563  0.0745  0.0366  47  LEU L O   
4044 C CB  . LEU C 47  ? 0.9042 0.7320 0.9603 0.0478  0.0775  -0.0005 47  LEU L CB  
4045 C CG  . LEU C 47  ? 0.8946 0.7212 0.9620 0.0437  0.0861  -0.0124 47  LEU L CG  
4046 C CD1 . LEU C 47  ? 0.8878 0.7386 0.9759 0.0497  0.0838  -0.0187 47  LEU L CD1 
4047 C CD2 . LEU C 47  ? 0.9184 0.7192 0.9864 0.0478  0.0931  -0.0135 47  LEU L CD2 
4048 N N   . ILE C 48  ? 0.9113 0.7465 0.9319 0.0470  0.0675  0.0195  48  ILE L N   
4049 C CA  . ILE C 48  ? 0.9240 0.7726 0.9311 0.0556  0.0592  0.0284  48  ILE L CA  
4050 C C   . ILE C 48  ? 0.9168 0.7706 0.9068 0.0471  0.0616  0.0293  48  ILE L C   
4051 O O   . ILE C 48  ? 0.8887 0.7435 0.8812 0.0370  0.0661  0.0199  48  ILE L O   
4052 C CB  . ILE C 48  ? 0.9173 0.7917 0.9348 0.0638  0.0476  0.0191  48  ILE L CB  
4053 C CG1 . ILE C 48  ? 0.9132 0.7897 0.9531 0.0718  0.0465  0.0162  48  ILE L CG1 
4054 C CG2 . ILE C 48  ? 0.9376 0.8295 0.9384 0.0748  0.0373  0.0266  48  ILE L CG2 
4055 C CD1 . ILE C 48  ? 0.9359 0.7975 0.9738 0.0860  0.0476  0.0320  48  ILE L CD1 
4056 N N   . TYR C 49  ? 0.9617 0.8209 0.9338 0.0535  0.0594  0.0422  49  TYR L N   
4057 C CA  . TYR C 49  ? 0.9699 0.8417 0.9247 0.0505  0.0605  0.0424  49  TYR L CA  
4058 C C   . TYR C 49  ? 0.9906 0.8807 0.9278 0.0644  0.0519  0.0490  49  TYR L C   
4059 O O   . TYR C 49  ? 1.0152 0.9051 0.9510 0.0755  0.0476  0.0605  49  TYR L O   
4060 C CB  . TYR C 49  ? 0.9721 0.8332 0.9213 0.0398  0.0720  0.0532  49  TYR L CB  
4061 C CG  . TYR C 49  ? 0.9982 0.8459 0.9413 0.0420  0.0770  0.0741  49  TYR L CG  
4062 C CD1 . TYR C 49  ? 1.0156 0.8756 0.9394 0.0513  0.0763  0.0897  49  TYR L CD1 
4063 C CD2 . TYR C 49  ? 1.0099 0.8309 0.9658 0.0349  0.0836  0.0786  49  TYR L CD2 
4064 C CE1 . TYR C 49  ? 1.0429 0.8883 0.9612 0.0533  0.0831  0.1128  49  TYR L CE1 
4065 C CE2 . TYR C 49  ? 1.0400 0.8417 0.9921 0.0359  0.0901  0.0989  49  TYR L CE2 
4066 C CZ  . TYR C 49  ? 1.0533 0.8669 0.9870 0.0450  0.0904  0.1180  49  TYR L CZ  
4067 O OH  . TYR C 49  ? 1.0822 0.8746 1.0122 0.0462  0.0988  0.1419  49  TYR L OH  
4068 N N   . GLY C 50  ? 0.9984 0.9053 0.9208 0.0657  0.0494  0.0412  50  GLY L N   
4069 C CA  . GLY C 50  ? 1.0311 0.9599 0.9333 0.0793  0.0404  0.0427  50  GLY L CA  
4070 C C   . GLY C 50  ? 1.0494 0.9925 0.9614 0.0871  0.0256  0.0303  50  GLY L C   
4071 O O   . GLY C 50  ? 1.0712 1.0334 0.9697 0.1009  0.0164  0.0366  50  GLY L O   
4072 N N   . ALA C 51  ? 1.0447 0.9820 0.9811 0.0781  0.0239  0.0137  51  ALA L N   
4073 C CA  . ALA C 51  ? 1.0468 1.0014 1.0000 0.0810  0.0110  -0.0009 51  ALA L CA  
4074 C C   . ALA C 51  ? 1.0564 1.0110 1.0256 0.0889  0.0088  0.0106  51  ALA L C   
4075 O O   . ALA C 51  ? 1.0429 0.9976 1.0382 0.0841  0.0082  0.0013  51  ALA L O   
4076 C CB  . ALA C 51  ? 1.0715 1.0538 1.0074 0.0899  -0.0024 -0.0114 51  ALA L CB  
4077 N N   . SER C 52  ? 1.0830 1.0373 1.0368 0.1024  0.0087  0.0319  52  SER L N   
4078 C CA  . SER C 52  ? 1.0957 1.0524 1.0619 0.1158  0.0049  0.0437  52  SER L CA  
4079 C C   . SER C 52  ? 1.1035 1.0259 1.0675 0.1178  0.0186  0.0660  52  SER L C   
4080 O O   . SER C 52  ? 1.1161 1.0299 1.0952 0.1272  0.0193  0.0733  52  SER L O   
4081 C CB  . SER C 52  ? 1.1223 1.1129 1.0746 0.1344  -0.0101 0.0491  52  SER L CB  
4082 O OG  . SER C 52  ? 1.1492 1.1398 1.0688 0.1415  -0.0071 0.0659  52  SER L OG  
4083 N N   . THR C 53  ? 1.0953 0.9987 1.0428 0.1088  0.0298  0.0759  53  THR L N   
4084 C CA  . THR C 53  ? 1.1099 0.9813 1.0545 0.1087  0.0424  0.0976  53  THR L CA  
4085 C C   . THR C 53  ? 1.0941 0.9369 1.0595 0.0944  0.0524  0.0879  53  THR L C   
4086 O O   . THR C 53  ? 1.0593 0.9016 1.0280 0.0784  0.0565  0.0739  53  THR L O   
4087 C CB  . THR C 53  ? 1.1168 0.9853 1.0382 0.1034  0.0508  0.1126  53  THR L CB  
4088 O OG1 . THR C 53  ? 1.1361 1.0355 1.0349 0.1183  0.0413  0.1188  53  THR L OG1 
4089 C CG2 . THR C 53  ? 1.1431 0.9781 1.0634 0.1012  0.0644  0.1367  53  THR L CG2 
4090 N N   . ARG C 54  ? 1.1186 0.9380 1.0962 0.1020  0.0566  0.0960  54  ARG L N   
4091 C CA  . ARG C 54  ? 1.1177 0.9100 1.1126 0.0909  0.0659  0.0853  54  ARG L CA  
4092 C C   . ARG C 54  ? 1.1216 0.8858 1.1095 0.0740  0.0786  0.0923  54  ARG L C   
4093 O O   . ARG C 54  ? 1.1435 0.9014 1.1169 0.0747  0.0825  0.1119  54  ARG L O   
4094 C CB  . ARG C 54  ? 1.1509 0.9257 1.1602 0.1071  0.0671  0.0904  54  ARG L CB  
4095 C CG  . ARG C 54  ? 1.1509 0.9587 1.1741 0.1228  0.0551  0.0820  54  ARG L CG  
4096 C CD  . ARG C 54  ? 1.1669 0.9593 1.2099 0.1360  0.0593  0.0804  54  ARG L CD  
4097 N NE  . ARG C 54  ? 1.2240 0.9860 1.2612 0.1528  0.0646  0.1030  54  ARG L NE  
4098 C CZ  . ARG C 54  ? 1.2627 1.0398 1.2922 0.1748  0.0566  0.1230  54  ARG L CZ  
4099 N NH1 . ARG C 54  ? 1.2445 1.0702 1.2716 0.1815  0.0414  0.1195  54  ARG L NH1 
4100 N NH2 . ARG C 54  ? 1.3142 1.0573 1.3382 0.1904  0.0640  0.1464  54  ARG L NH2 
4101 N N   . ALA C 55  ? 1.1099 0.8607 1.1089 0.0586  0.0850  0.0762  55  ALA L N   
4102 C CA  . ALA C 55  ? 1.1286 0.8573 1.1258 0.0399  0.0956  0.0778  55  ALA L CA  
4103 C C   . ALA C 55  ? 1.1705 0.8566 1.1757 0.0414  0.1042  0.0843  55  ALA L C   
4104 O O   . ALA C 55  ? 1.1966 0.8718 1.2076 0.0599  0.1022  0.0886  55  ALA L O   
4105 C CB  . ALA C 55  ? 1.1014 0.8416 1.1044 0.0242  0.0968  0.0566  55  ALA L CB  
4106 N N   . THR C 56  ? 1.1874 0.8502 1.1943 0.0219  0.1138  0.0840  56  THR L N   
4107 C CA  . THR C 56  ? 1.2292 0.8445 1.2441 0.0193  0.1235  0.0882  56  THR L CA  
4108 C C   . THR C 56  ? 1.2290 0.8297 1.2562 0.0227  0.1242  0.0645  56  THR L C   
4109 O O   . THR C 56  ? 1.2015 0.8194 1.2317 0.0107  0.1226  0.0427  56  THR L O   
4110 C CB  . THR C 56  ? 1.2463 0.8450 1.2628 -0.0069 0.1331  0.0907  56  THR L CB  
4111 O OG1 . THR C 56  ? 1.2547 0.8722 1.2597 -0.0081 0.1340  0.1140  56  THR L OG1 
4112 C CG2 . THR C 56  ? 1.2997 0.8429 1.3262 -0.0129 0.1442  0.0936  56  THR L CG2 
4113 N N   . GLY C 57  ? 1.2582 0.8286 1.2915 0.0414  0.1272  0.0703  57  GLY L N   
4114 C CA  . GLY C 57  ? 1.2697 0.8226 1.3142 0.0477  0.1303  0.0489  57  GLY L CA  
4115 C C   . GLY C 57  ? 1.2288 0.8237 1.2780 0.0594  0.1218  0.0349  57  GLY L C   
4116 O O   . GLY C 57  ? 1.2238 0.8202 1.2794 0.0566  0.1245  0.0126  57  GLY L O   
4117 N N   . ILE C 58  ? 1.2060 0.8357 1.2519 0.0716  0.1122  0.0479  58  ILE L N   
4118 C CA  . ILE C 58  ? 1.1648 0.8338 1.2191 0.0818  0.1043  0.0372  58  ILE L CA  
4119 C C   . ILE C 58  ? 1.1856 0.8572 1.2491 0.1095  0.1005  0.0485  58  ILE L C   
4120 O O   . ILE C 58  ? 1.2127 0.8838 1.2686 0.1211  0.0962  0.0700  58  ILE L O   
4121 C CB  . ILE C 58  ? 1.1140 0.8226 1.1601 0.0732  0.0954  0.0385  58  ILE L CB  
4122 C CG1 . ILE C 58  ? 1.0924 0.8024 1.1305 0.0494  0.0993  0.0289  58  ILE L CG1 
4123 C CG2 . ILE C 58  ? 1.0844 0.8304 1.1425 0.0822  0.0876  0.0288  58  ILE L CG2 
4124 C CD1 . ILE C 58  ? 1.0711 0.7810 1.1164 0.0406  0.1045  0.0072  58  ILE L CD1 
4125 N N   . PRO C 59  ? 1.1801 0.8586 1.2599 0.1223  0.1022  0.0355  59  PRO L N   
4126 C CA  . PRO C 59  ? 1.1956 0.8827 1.2876 0.1508  0.0984  0.0460  59  PRO L CA  
4127 C C   . PRO C 59  ? 1.1783 0.9089 1.2692 0.1606  0.0838  0.0592  59  PRO L C   
4128 O O   . PRO C 59  ? 1.1512 0.9106 1.2363 0.1454  0.0767  0.0537  59  PRO L O   
4129 C CB  . PRO C 59  ? 1.1845 0.8893 1.2957 0.1570  0.1022  0.0256  59  PRO L CB  
4130 C CG  . PRO C 59  ? 1.1806 0.8624 1.2849 0.1353  0.1123  0.0063  59  PRO L CG  
4131 C CD  . PRO C 59  ? 1.1607 0.8430 1.2477 0.1120  0.1085  0.0113  59  PRO L CD  
4132 N N   . ALA C 60  ? 1.2034 0.9390 1.2997 0.1874  0.0792  0.0758  60  ALA L N   
4133 C CA  . ALA C 60  ? 1.1924 0.9739 1.2877 0.2000  0.0637  0.0869  60  ALA L CA  
4134 C C   . ALA C 60  ? 1.1544 0.9882 1.2728 0.2000  0.0549  0.0685  60  ALA L C   
4135 O O   . ALA C 60  ? 1.1347 1.0130 1.2552 0.2037  0.0403  0.0699  60  ALA L O   
4136 C CB  . ALA C 60  ? 1.2342 1.0064 1.3276 0.2305  0.0619  0.1119  60  ALA L CB  
4137 N N   . ARG C 61  ? 1.1459 0.9750 1.2816 0.1956  0.0643  0.0510  61  ARG L N   
4138 C CA  . ARG C 61  ? 1.1173 0.9924 1.2769 0.1909  0.0604  0.0339  61  ARG L CA  
4139 C C   . ARG C 61  ? 1.0713 0.9714 1.2243 0.1673  0.0521  0.0256  61  ARG L C   
4140 O O   . ARG C 61  ? 1.0446 0.9897 1.2116 0.1679  0.0400  0.0213  61  ARG L O   
4141 C CB  . ARG C 61  ? 1.1286 0.9864 1.2992 0.1863  0.0756  0.0179  61  ARG L CB  
4142 C CG  . ARG C 61  ? 1.1104 1.0134 1.3065 0.1803  0.0759  0.0025  61  ARG L CG  
4143 C CD  . ARG C 61  ? 1.1205 1.0107 1.3261 0.1836  0.0920  -0.0104 61  ARG L CD  
4144 N NE  . ARG C 61  ? 1.1251 0.9734 1.3080 0.1664  0.1024  -0.0185 61  ARG L NE  
4145 C CZ  . ARG C 61  ? 1.1593 0.9615 1.3304 0.1730  0.1122  -0.0206 61  ARG L CZ  
4146 N NH1 . ARG C 61  ? 1.1946 0.9791 1.3722 0.1982  0.1141  -0.0124 61  ARG L NH1 
4147 N NH2 . ARG C 61  ? 1.1655 0.9391 1.3186 0.1544  0.1199  -0.0313 61  ARG L NH2 
4148 N N   . PHE C 62  ? 1.0512 0.9221 1.1841 0.1469  0.0586  0.0225  62  PHE L N   
4149 C CA  . PHE C 62  ? 1.0177 0.9045 1.1419 0.1265  0.0533  0.0152  62  PHE L CA  
4150 C C   . PHE C 62  ? 1.0224 0.9227 1.1304 0.1317  0.0403  0.0267  62  PHE L C   
4151 O O   . PHE C 62  ? 1.0503 0.9268 1.1396 0.1394  0.0417  0.0431  62  PHE L O   
4152 C CB  . PHE C 62  ? 1.0080 0.8631 1.1158 0.1073  0.0643  0.0103  62  PHE L CB  
4153 C CG  . PHE C 62  ? 1.0045 0.8485 1.1227 0.1026  0.0768  -0.0020 62  PHE L CG  
4154 C CD1 . PHE C 62  ? 0.9785 0.8482 1.1121 0.0945  0.0793  -0.0145 62  PHE L CD1 
4155 C CD2 . PHE C 62  ? 1.0286 0.8360 1.1406 0.1063  0.0868  -0.0016 62  PHE L CD2 
4156 C CE1 . PHE C 62  ? 0.9733 0.8368 1.1131 0.0921  0.0916  -0.0248 62  PHE L CE1 
4157 C CE2 . PHE C 62  ? 1.0273 0.8273 1.1456 0.1033  0.0978  -0.0159 62  PHE L CE2 
4158 C CZ  . PHE C 62  ? 1.0005 0.8308 1.1313 0.0972  0.1002  -0.0267 62  PHE L CZ  
4159 N N   . SER C 63  ? 0.9956 0.9338 1.1106 0.1265  0.0285  0.0176  63  SER L N   
4160 C CA  . SER C 63  ? 0.9945 0.9546 1.0947 0.1339  0.0141  0.0244  63  SER L CA  
4161 C C   . SER C 63  ? 0.9704 0.9481 1.0662 0.1159  0.0078  0.0089  63  SER L C   
4162 O O   . SER C 63  ? 0.9524 0.9566 1.0711 0.1079  0.0030  -0.0068 63  SER L O   
4163 C CB  . SER C 63  ? 1.0044 1.0013 1.1215 0.1551  0.0018  0.0286  63  SER L CB  
4164 O OG  . SER C 63  ? 1.0160 1.0402 1.1164 0.1631  -0.0135 0.0336  63  SER L OG  
4165 N N   . GLY C 64  ? 0.9756 0.9379 1.0432 0.1098  0.0089  0.0137  64  GLY L N   
4166 C CA  . GLY C 64  ? 0.9610 0.9345 1.0202 0.0962  0.0039  -0.0005 64  GLY L CA  
4167 C C   . GLY C 64  ? 0.9712 0.9768 1.0173 0.1061  -0.0126 -0.0023 64  GLY L C   
4168 O O   . GLY C 64  ? 0.9955 1.0072 1.0267 0.1236  -0.0175 0.0144  64  GLY L O   
4169 N N   . SER C 65  ? 0.9617 0.9867 1.0127 0.0951  -0.0209 -0.0230 65  SER L N   
4170 C CA  . SER C 65  ? 0.9865 1.0450 1.0245 0.1023  -0.0381 -0.0313 65  SER L CA  
4171 C C   . SER C 65  ? 0.9890 1.0497 1.0272 0.0853  -0.0412 -0.0563 65  SER L C   
4172 O O   . SER C 65  ? 0.9626 1.0017 1.0157 0.0692  -0.0304 -0.0647 65  SER L O   
4173 C CB  . SER C 65  ? 0.9882 1.0874 1.0476 0.1145  -0.0529 -0.0332 65  SER L CB  
4174 O OG  . SER C 65  ? 0.9690 1.0796 1.0671 0.1012  -0.0522 -0.0490 65  SER L OG  
4175 N N   . GLY C 66  ? 1.0224 1.1087 1.0422 0.0904  -0.0557 -0.0678 66  GLY L N   
4176 C CA  . GLY C 66  ? 1.0423 1.1294 1.0607 0.0763  -0.0601 -0.0946 66  GLY L CA  
4177 C C   . GLY C 66  ? 1.0681 1.1315 1.0506 0.0779  -0.0516 -0.0922 66  GLY L C   
4178 O O   . GLY C 66  ? 1.0751 1.1183 1.0405 0.0846  -0.0394 -0.0695 66  GLY L O   
4179 N N   . SER C 67  ? 1.0983 1.1652 1.0713 0.0716  -0.0578 -0.1171 67  SER L N   
4180 C CA  . SER C 67  ? 1.1227 1.1715 1.0627 0.0751  -0.0499 -0.1185 67  SER L CA  
4181 C C   . SER C 67  ? 1.1507 1.1898 1.0949 0.0628  -0.0526 -0.1505 67  SER L C   
4182 O O   . SER C 67  ? 1.1757 1.2310 1.1423 0.0527  -0.0651 -0.1733 67  SER L O   
4183 C CB  . SER C 67  ? 1.1458 1.2197 1.0487 0.0948  -0.0571 -0.1077 67  SER L CB  
4184 O OG  . SER C 67  ? 1.1719 1.2853 1.0715 0.1002  -0.0780 -0.1270 67  SER L OG  
4185 N N   . GLY C 68  ? 1.1598 1.1723 1.0838 0.0637  -0.0402 -0.1519 68  GLY L N   
4186 C CA  . GLY C 68  ? 1.1838 1.1779 1.1084 0.0550  -0.0396 -0.1806 68  GLY L CA  
4187 C C   . GLY C 68  ? 1.1796 1.1389 1.1363 0.0380  -0.0266 -0.1818 68  GLY L C   
4188 O O   . GLY C 68  ? 1.1725 1.1063 1.1252 0.0395  -0.0102 -0.1650 68  GLY L O   
4189 N N   . THR C 69  ? 1.1907 1.1530 1.1799 0.0217  -0.0341 -0.2009 69  THR L N   
4190 C CA  . THR C 69  ? 1.1765 1.1072 1.1968 0.0048  -0.0213 -0.2021 69  THR L CA  
4191 C C   . THR C 69  ? 1.1586 1.1070 1.2163 -0.0061 -0.0234 -0.1936 69  THR L C   
4192 O O   . THR C 69  ? 1.1484 1.0781 1.2357 -0.0216 -0.0137 -0.1950 69  THR L O   
4193 C CB  . THR C 69  ? 1.2058 1.1156 1.2346 -0.0078 -0.0233 -0.2339 69  THR L CB  
4194 O OG1 . THR C 69  ? 1.2168 1.1606 1.2593 -0.0161 -0.0436 -0.2586 69  THR L OG1 
4195 C CG2 . THR C 69  ? 1.2318 1.1203 1.2246 0.0048  -0.0187 -0.2441 69  THR L CG2 
4196 N N   . GLU C 70  ? 1.1540 1.1385 1.2103 0.0035  -0.0346 -0.1832 70  GLU L N   
4197 C CA  . GLU C 70  ? 1.1337 1.1403 1.2251 -0.0028 -0.0373 -0.1763 70  GLU L CA  
4198 C C   . GLU C 70  ? 1.1116 1.1318 1.1910 0.0143  -0.0365 -0.1494 70  GLU L C   
4199 O O   . GLU C 70  ? 1.1234 1.1691 1.1827 0.0292  -0.0490 -0.1461 70  GLU L O   
4200 C CB  . GLU C 70  ? 1.1560 1.2015 1.2699 -0.0111 -0.0571 -0.2009 70  GLU L CB  
4201 C CG  . GLU C 70  ? 1.1851 1.2146 1.3204 -0.0334 -0.0571 -0.2295 70  GLU L CG  
4202 C CD  . GLU C 70  ? 1.1817 1.1857 1.3535 -0.0522 -0.0396 -0.2236 70  GLU L CD  
4203 O OE1 . GLU C 70  ? 1.1493 1.1547 1.3317 -0.0480 -0.0290 -0.1995 70  GLU L OE1 
4204 O OE2 . GLU C 70  ? 1.2186 1.2001 1.4073 -0.0708 -0.0359 -0.2433 70  GLU L OE2 
4205 N N   . PHE C 71  ? 1.0801 1.0820 1.1716 0.0124  -0.0212 -0.1306 71  PHE L N   
4206 C CA  . PHE C 71  ? 1.0633 1.0695 1.1475 0.0262  -0.0179 -0.1070 71  PHE L CA  
4207 C C   . PHE C 71  ? 1.0393 1.0563 1.1589 0.0217  -0.0137 -0.1021 71  PHE L C   
4208 O O   . PHE C 71  ? 1.0308 1.0480 1.1786 0.0063  -0.0095 -0.1130 71  PHE L O   
4209 C CB  . PHE C 71  ? 1.0568 1.0305 1.1164 0.0300  -0.0027 -0.0903 71  PHE L CB  
4210 C CG  . PHE C 71  ? 1.0716 1.0368 1.0980 0.0355  -0.0036 -0.0935 71  PHE L CG  
4211 C CD1 . PHE C 71  ? 1.0810 1.0299 1.1045 0.0273  -0.0002 -0.1095 71  PHE L CD1 
4212 C CD2 . PHE C 71  ? 1.0716 1.0444 1.0699 0.0500  -0.0065 -0.0795 71  PHE L CD2 
4213 C CE1 . PHE C 71  ? 1.0937 1.0365 1.0864 0.0350  0.0000  -0.1134 71  PHE L CE1 
4214 C CE2 . PHE C 71  ? 1.0860 1.0556 1.0540 0.0560  -0.0056 -0.0818 71  PHE L CE2 
4215 C CZ  . PHE C 71  ? 1.0975 1.0535 1.0626 0.0493  -0.0026 -0.0998 71  PHE L CZ  
4216 N N   . THR C 72  ? 1.0205 1.0453 1.1385 0.0358  -0.0134 -0.0849 72  THR L N   
4217 C CA  . THR C 72  ? 0.9935 1.0319 1.1426 0.0365  -0.0095 -0.0801 72  THR L CA  
4218 C C   . THR C 72  ? 0.9855 1.0049 1.1223 0.0497  0.0003  -0.0596 72  THR L C   
4219 O O   . THR C 72  ? 1.0033 1.0147 1.1137 0.0621  -0.0026 -0.0478 72  THR L O   
4220 C CB  . THR C 72  ? 0.9937 1.0784 1.1653 0.0425  -0.0267 -0.0884 72  THR L CB  
4221 O OG1 . THR C 72  ? 1.0096 1.1100 1.1964 0.0257  -0.0353 -0.1112 72  THR L OG1 
4222 C CG2 . THR C 72  ? 0.9824 1.0865 1.1873 0.0469  -0.0222 -0.0826 72  THR L CG2 
4223 N N   . LEU C 73  ? 0.9695 0.9815 1.1259 0.0462  0.0129  -0.0562 73  LEU L N   
4224 C CA  . LEU C 73  ? 0.9595 0.9565 1.1112 0.0585  0.0214  -0.0419 73  LEU L CA  
4225 C C   . LEU C 73  ? 0.9655 0.9904 1.1487 0.0675  0.0199  -0.0426 73  LEU L C   
4226 O O   . LEU C 73  ? 0.9641 1.0081 1.1757 0.0570  0.0231  -0.0523 73  LEU L O   
4227 C CB  . LEU C 73  ? 0.9379 0.9037 1.0813 0.0488  0.0383  -0.0394 73  LEU L CB  
4228 C CG  . LEU C 73  ? 0.9386 0.8839 1.0756 0.0580  0.0481  -0.0293 73  LEU L CG  
4229 C CD1 . LEU C 73  ? 0.9541 0.8814 1.0654 0.0677  0.0443  -0.0171 73  LEU L CD1 
4230 C CD2 . LEU C 73  ? 0.9252 0.8506 1.0574 0.0471  0.0629  -0.0312 73  LEU L CD2 
4231 N N   . THR C 74  ? 0.9818 1.0090 1.1610 0.0876  0.0161  -0.0309 74  THR L N   
4232 C CA  . THR C 74  ? 0.9849 1.0415 1.1930 0.1018  0.0138  -0.0299 74  THR L CA  
4233 C C   . THR C 74  ? 1.0098 1.0374 1.2133 0.1156  0.0271  -0.0191 74  THR L C   
4234 O O   . THR C 74  ? 1.0399 1.0392 1.2193 0.1264  0.0278  -0.0064 74  THR L O   
4235 C CB  . THR C 74  ? 0.9903 1.0829 1.2005 0.1178  -0.0052 -0.0264 74  THR L CB  
4236 O OG1 . THR C 74  ? 0.9835 1.1016 1.1975 0.1025  -0.0177 -0.0415 74  THR L OG1 
4237 C CG2 . THR C 74  ? 0.9923 1.1215 1.2343 0.1357  -0.0086 -0.0240 74  THR L CG2 
4238 N N   . ILE C 75  ? 1.0207 1.0551 1.2476 0.1145  0.0387  -0.0250 75  ILE L N   
4239 C CA  . ILE C 75  ? 1.0524 1.0613 1.2772 0.1281  0.0519  -0.0200 75  ILE L CA  
4240 C C   . ILE C 75  ? 1.0754 1.1180 1.3290 0.1505  0.0488  -0.0176 75  ILE L C   
4241 O O   . ILE C 75  ? 1.0662 1.1451 1.3505 0.1471  0.0518  -0.0261 75  ILE L O   
4242 C CB  . ILE C 75  ? 1.0387 1.0312 1.2634 0.1133  0.0687  -0.0288 75  ILE L CB  
4243 C CG1 . ILE C 75  ? 1.0167 0.9923 1.2211 0.0909  0.0694  -0.0318 75  ILE L CG1 
4244 C CG2 . ILE C 75  ? 1.0593 1.0169 1.2726 0.1250  0.0813  -0.0271 75  ILE L CG2 
4245 C CD1 . ILE C 75  ? 1.0033 0.9685 1.2060 0.0782  0.0848  -0.0381 75  ILE L CD1 
4246 N N   . SER C 76  ? 1.1116 1.1430 1.3560 0.1740  0.0438  -0.0043 76  SER L N   
4247 C CA  . SER C 76  ? 1.1509 1.2200 1.4204 0.1996  0.0367  0.0012  76  SER L CA  
4248 C C   . SER C 76  ? 1.1782 1.2523 1.4718 0.2113  0.0518  -0.0044 76  SER L C   
4249 O O   . SER C 76  ? 1.2025 1.3210 1.5274 0.2051  0.0532  -0.0144 76  SER L O   
4250 C CB  . SER C 76  ? 1.1882 1.2393 1.4381 0.2235  0.0292  0.0205  76  SER L CB  
4251 O OG  . SER C 76  ? 1.1945 1.2578 1.4259 0.2160  0.0137  0.0251  76  SER L OG  
4252 N N   . SER C 77  ? 1.2041 1.2330 1.4840 0.2279  0.0638  0.0012  77  SER L N   
4253 C CA  . SER C 77  ? 1.2070 1.2369 1.5056 0.2429  0.0790  -0.0057 77  SER L CA  
4254 C C   . SER C 77  ? 1.1796 1.1821 1.4663 0.2214  0.0950  -0.0201 77  SER L C   
4255 O O   . SER C 77  ? 1.2039 1.1558 1.4693 0.2242  0.1060  -0.0227 77  SER L O   
4256 C CB  . SER C 77  ? 1.2562 1.2510 1.5476 0.2745  0.0838  0.0057  77  SER L CB  
4257 O OG  . SER C 77  ? 1.2877 1.2174 1.5446 0.2672  0.0885  0.0110  77  SER L OG  
4258 N N   . LEU C 78  ? 1.1232 1.1607 1.4245 0.1999  0.0962  -0.0295 78  LEU L N   
4259 C CA  . LEU C 78  ? 1.0920 1.1107 1.3797 0.1783  0.1093  -0.0400 78  LEU L CA  
4260 C C   . LEU C 78  ? 1.0870 1.0869 1.3727 0.1924  0.1272  -0.0487 78  LEU L C   
4261 O O   . LEU C 78  ? 1.1048 1.1273 1.4134 0.2153  0.1322  -0.0494 78  LEU L O   
4262 C CB  . LEU C 78  ? 1.0759 1.1404 1.3871 0.1585  0.1094  -0.0450 78  LEU L CB  
4263 C CG  . LEU C 78  ? 1.0743 1.1231 1.3697 0.1354  0.1211  -0.0513 78  LEU L CG  
4264 C CD1 . LEU C 78  ? 1.0562 1.0893 1.3326 0.1140  0.1107  -0.0483 78  LEU L CD1 
4265 C CD2 . LEU C 78  ? 1.0668 1.1583 1.3916 0.1281  0.1329  -0.0556 78  LEU L CD2 
4266 N N   . GLN C 79  ? 1.0613 1.0227 1.3193 0.1792  0.1365  -0.0565 79  GLN L N   
4267 C CA  . GLN C 79  ? 1.0670 1.0082 1.3170 0.1892  0.1531  -0.0693 79  GLN L CA  
4268 C C   . GLN C 79  ? 1.0443 0.9977 1.2855 0.1693  0.1636  -0.0787 79  GLN L C   
4269 O O   . GLN C 79  ? 1.0134 0.9801 1.2522 0.1481  0.1581  -0.0736 79  GLN L O   
4270 C CB  . GLN C 79  ? 1.0932 0.9732 1.3156 0.1938  0.1536  -0.0713 79  GLN L CB  
4271 C CG  . GLN C 79  ? 1.1134 0.9759 1.3416 0.2153  0.1452  -0.0576 79  GLN L CG  
4272 C CD  . GLN C 79  ? 1.1433 0.9413 1.3460 0.2156  0.1473  -0.0570 79  GLN L CD  
4273 O OE1 . GLN C 79  ? 1.1463 0.9148 1.3280 0.1977  0.1533  -0.0691 79  GLN L OE1 
4274 N NE2 . GLN C 79  ? 1.1695 0.9468 1.3751 0.2358  0.1424  -0.0420 79  GLN L NE2 
4275 N N   . SER C 80  ? 1.0612 1.0092 1.2958 0.1781  0.1793  -0.0923 80  SER L N   
4276 C CA  . SER C 80  ? 1.0476 1.0096 1.2702 0.1636  0.1908  -0.1002 80  SER L CA  
4277 C C   . SER C 80  ? 1.0447 0.9720 1.2336 0.1433  0.1860  -0.1029 80  SER L C   
4278 O O   . SER C 80  ? 1.0252 0.9675 1.2042 0.1271  0.1897  -0.1020 80  SER L O   
4279 C CB  . SER C 80  ? 1.0713 1.0396 1.2926 0.1810  0.2083  -0.1154 80  SER L CB  
4280 O OG  . SER C 80  ? 1.1130 1.0317 1.3122 0.1915  0.2099  -0.1291 80  SER L OG  
4281 N N   . GLU C 81  ? 1.0595 0.9423 1.2327 0.1447  0.1784  -0.1045 81  GLU L N   
4282 C CA  . GLU C 81  ? 1.0582 0.9110 1.2033 0.1256  0.1735  -0.1073 81  GLU L CA  
4283 C C   . GLU C 81  ? 1.0150 0.8787 1.1605 0.1086  0.1614  -0.0917 81  GLU L C   
4284 O O   . GLU C 81  ? 0.9979 0.8481 1.1232 0.0921  0.1578  -0.0917 81  GLU L O   
4285 C CB  . GLU C 81  ? 1.0929 0.8947 1.2254 0.1308  0.1709  -0.1128 81  GLU L CB  
4286 C CG  . GLU C 81  ? 1.1319 0.9121 1.2583 0.1450  0.1833  -0.1334 81  GLU L CG  
4287 C CD  . GLU C 81  ? 1.1563 0.9438 1.3052 0.1736  0.1899  -0.1333 81  GLU L CD  
4288 O OE1 . GLU C 81  ? 1.1346 0.9480 1.3062 0.1822  0.1833  -0.1162 81  GLU L OE1 
4289 O OE2 . GLU C 81  ? 1.1959 0.9655 1.3399 0.1880  0.2014  -0.1516 81  GLU L OE2 
4290 N N   . ASP C 82  ? 0.9976 0.8880 1.1669 0.1130  0.1551  -0.0799 82  ASP L N   
4291 C CA  . ASP C 82  ? 0.9842 0.8854 1.1550 0.0986  0.1436  -0.0683 82  ASP L CA  
4292 C C   . ASP C 82  ? 0.9557 0.8856 1.1311 0.0846  0.1496  -0.0674 82  ASP L C   
4293 O O   . ASP C 82  ? 0.9307 0.8727 1.1129 0.0736  0.1421  -0.0597 82  ASP L O   
4294 C CB  . ASP C 82  ? 0.9925 0.9099 1.1852 0.1091  0.1324  -0.0588 82  ASP L CB  
4295 C CG  . ASP C 82  ? 1.0235 0.9117 1.2108 0.1255  0.1272  -0.0544 82  ASP L CG  
4296 O OD1 . ASP C 82  ? 1.0532 0.9025 1.2200 0.1247  0.1321  -0.0591 82  ASP L OD1 
4297 O OD2 . ASP C 82  ? 1.0265 0.9318 1.2308 0.1390  0.1185  -0.0460 82  ASP L OD2 
4298 N N   . PHE C 83  ? 0.9582 0.8977 1.1291 0.0858  0.1637  -0.0751 83  PHE L N   
4299 C CA  . PHE C 83  ? 0.9272 0.8874 1.0958 0.0732  0.1717  -0.0712 83  PHE L CA  
4300 C C   . PHE C 83  ? 0.9135 0.8531 1.0548 0.0591  0.1663  -0.0685 83  PHE L C   
4301 O O   . PHE C 83  ? 0.9264 0.8477 1.0441 0.0589  0.1677  -0.0769 83  PHE L O   
4302 C CB  . PHE C 83  ? 0.9345 0.9112 1.0993 0.0808  0.1888  -0.0792 83  PHE L CB  
4303 C CG  . PHE C 83  ? 0.9207 0.9153 1.0762 0.0697  0.1988  -0.0725 83  PHE L CG  
4304 C CD1 . PHE C 83  ? 0.9011 0.9230 1.0808 0.0625  0.2046  -0.0602 83  PHE L CD1 
4305 C CD2 . PHE C 83  ? 0.9252 0.9097 1.0484 0.0661  0.2021  -0.0775 83  PHE L CD2 
4306 C CE1 . PHE C 83  ? 0.8993 0.9329 1.0699 0.0535  0.2155  -0.0503 83  PHE L CE1 
4307 C CE2 . PHE C 83  ? 0.9155 0.9177 1.0283 0.0591  0.2114  -0.0678 83  PHE L CE2 
4308 C CZ  . PHE C 83  ? 0.9054 0.9295 1.0413 0.0535  0.2190  -0.0528 83  PHE L CZ  
4309 N N   . ALA C 84  ? 0.8959 0.8401 1.0420 0.0476  0.1600  -0.0582 84  ALA L N   
4310 C CA  . ALA C 84  ? 0.8925 0.8208 1.0157 0.0368  0.1548  -0.0542 84  ALA L CA  
4311 C C   . ALA C 84  ? 0.8712 0.8076 1.0046 0.0268  0.1520  -0.0441 84  ALA L C   
4312 O O   . ALA C 84  ? 0.8606 0.8129 1.0198 0.0259  0.1516  -0.0420 84  ALA L O   
4313 C CB  . ALA C 84  ? 0.8931 0.7954 1.0038 0.0377  0.1433  -0.0565 84  ALA L CB  
4314 N N   . VAL C 85  ? 0.8650 0.7910 0.9789 0.0194  0.1503  -0.0391 85  VAL L N   
4315 C CA  . VAL C 85  ? 0.8532 0.7772 0.9724 0.0113  0.1464  -0.0315 85  VAL L CA  
4316 C C   . VAL C 85  ? 0.8281 0.7364 0.9383 0.0109  0.1321  -0.0329 85  VAL L C   
4317 O O   . VAL C 85  ? 0.8018 0.6984 0.8917 0.0117  0.1290  -0.0338 85  VAL L O   
4318 C CB  . VAL C 85  ? 0.8618 0.7855 0.9657 0.0073  0.1553  -0.0229 85  VAL L CB  
4319 C CG1 . VAL C 85  ? 0.8608 0.7772 0.9729 0.0002  0.1539  -0.0160 85  VAL L CG1 
4320 C CG2 . VAL C 85  ? 0.8743 0.8153 0.9800 0.0101  0.1708  -0.0197 85  VAL L CG2 
4321 N N   . TYR C 86  ? 0.8203 0.7317 0.9462 0.0088  0.1238  -0.0334 86  TYR L N   
4322 C CA  . TYR C 86  ? 0.8255 0.7272 0.9425 0.0106  0.1106  -0.0342 86  TYR L CA  
4323 C C   . TYR C 86  ? 0.8296 0.7248 0.9394 0.0041  0.1076  -0.0323 86  TYR L C   
4324 O O   . TYR C 86  ? 0.8099 0.7097 0.9352 -0.0020 0.1103  -0.0335 86  TYR L O   
4325 C CB  . TYR C 86  ? 0.8255 0.7393 0.9615 0.0166  0.1015  -0.0378 86  TYR L CB  
4326 C CG  . TYR C 86  ? 0.8338 0.7499 0.9757 0.0270  0.1047  -0.0392 86  TYR L CG  
4327 C CD1 . TYR C 86  ? 0.8438 0.7742 1.0018 0.0289  0.1157  -0.0419 86  TYR L CD1 
4328 C CD2 . TYR C 86  ? 0.8423 0.7443 0.9729 0.0359  0.0986  -0.0372 86  TYR L CD2 
4329 C CE1 . TYR C 86  ? 0.8537 0.7845 1.0161 0.0408  0.1198  -0.0451 86  TYR L CE1 
4330 C CE2 . TYR C 86  ? 0.8592 0.7568 0.9950 0.0470  0.1028  -0.0391 86  TYR L CE2 
4331 C CZ  . TYR C 86  ? 0.8633 0.7752 1.0146 0.0502  0.1131  -0.0444 86  TYR L CZ  
4332 O OH  . TYR C 86  ? 0.8776 0.7837 1.0333 0.0635  0.1182  -0.0483 86  TYR L OH  
4333 N N   . TYR C 87  ? 0.8549 0.7385 0.9423 0.0055  0.1032  -0.0296 87  TYR L N   
4334 C CA  . TYR C 87  ? 0.8642 0.7406 0.9409 0.0029  0.1015  -0.0282 87  TYR L CA  
4335 C C   . TYR C 87  ? 0.8622 0.7371 0.9293 0.0066  0.0896  -0.0303 87  TYR L C   
4336 O O   . TYR C 87  ? 0.8731 0.7483 0.9346 0.0112  0.0849  -0.0279 87  TYR L O   
4337 C CB  . TYR C 87  ? 0.8648 0.7364 0.9225 0.0032  0.1087  -0.0216 87  TYR L CB  
4338 C CG  . TYR C 87  ? 0.8755 0.7519 0.9367 0.0018  0.1206  -0.0177 87  TYR L CG  
4339 C CD1 . TYR C 87  ? 0.8896 0.7627 0.9574 -0.0001 0.1284  -0.0130 87  TYR L CD1 
4340 C CD2 . TYR C 87  ? 0.8756 0.7589 0.9326 0.0031  0.1249  -0.0186 87  TYR L CD2 
4341 C CE1 . TYR C 87  ? 0.8909 0.7703 0.9597 0.0001  0.1408  -0.0058 87  TYR L CE1 
4342 C CE2 . TYR C 87  ? 0.8790 0.7711 0.9356 0.0036  0.1360  -0.0150 87  TYR L CE2 
4343 C CZ  . TYR C 87  ? 0.8818 0.7735 0.9436 0.0026  0.1442  -0.0069 87  TYR L CZ  
4344 O OH  . TYR C 87  ? 0.8953 0.7976 0.9546 0.0046  0.1566  0.0000  87  TYR L OH  
4345 N N   . CYS C 88  ? 0.8657 0.7376 0.9300 0.0053  0.0857  -0.0346 88  CYS L N   
4346 C CA  . CYS C 88  ? 0.8763 0.7487 0.9249 0.0104  0.0762  -0.0363 88  CYS L CA  
4347 C C   . CYS C 88  ? 0.8840 0.7482 0.9130 0.0123  0.0812  -0.0324 88  CYS L C   
4348 O O   . CYS C 88  ? 0.8765 0.7342 0.9064 0.0103  0.0904  -0.0293 88  CYS L O   
4349 C CB  . CYS C 88  ? 0.8820 0.7617 0.9408 0.0093  0.0661  -0.0482 88  CYS L CB  
4350 S SG  . CYS C 88  ? 0.8976 0.7664 0.9726 -0.0005 0.0720  -0.0579 88  CYS L SG  
4351 N N   . GLN C 89  ? 0.8958 0.7634 0.9071 0.0180  0.0758  -0.0308 89  GLN L N   
4352 C CA  . GLN C 89  ? 0.9035 0.7692 0.8971 0.0220  0.0805  -0.0267 89  GLN L CA  
4353 C C   . GLN C 89  ? 0.9225 0.7943 0.9000 0.0290  0.0733  -0.0305 89  GLN L C   
4354 O O   . GLN C 89  ? 0.9353 0.8157 0.9059 0.0317  0.0680  -0.0252 89  GLN L O   
4355 C CB  . GLN C 89  ? 0.9013 0.7723 0.8881 0.0205  0.0862  -0.0153 89  GLN L CB  
4356 C CG  . GLN C 89  ? 0.9204 0.7977 0.8927 0.0249  0.0914  -0.0100 89  GLN L CG  
4357 C CD  . GLN C 89  ? 0.9317 0.8208 0.8958 0.0227  0.0924  -0.0005 89  GLN L CD  
4358 O OE1 . GLN C 89  ? 0.9444 0.8313 0.9137 0.0165  0.0912  0.0025  89  GLN L OE1 
4359 N NE2 . GLN C 89  ? 0.9432 0.8443 0.8958 0.0276  0.0958  0.0039  89  GLN L NE2 
4360 N N   . GLN C 90  ? 0.9360 0.8020 0.9062 0.0333  0.0743  -0.0391 90  GLN L N   
4361 C CA  . GLN C 90  ? 0.9625 0.8363 0.9130 0.0421  0.0693  -0.0441 90  GLN L CA  
4362 C C   . GLN C 90  ? 0.9582 0.8412 0.8926 0.0480  0.0771  -0.0313 90  GLN L C   
4363 O O   . GLN C 90  ? 0.9355 0.8162 0.8742 0.0467  0.0857  -0.0242 90  GLN L O   
4364 C CB  . GLN C 90  ? 0.9952 0.8568 0.9447 0.0445  0.0675  -0.0622 90  GLN L CB  
4365 C CG  . GLN C 90  ? 1.0086 0.8536 0.9569 0.0484  0.0792  -0.0611 90  GLN L CG  
4366 C CD  . GLN C 90  ? 1.0200 0.8728 0.9458 0.0618  0.0839  -0.0583 90  GLN L CD  
4367 O OE1 . GLN C 90  ? 1.0299 0.9006 0.9392 0.0675  0.0792  -0.0576 90  GLN L OE1 
4368 N NE2 . GLN C 90  ? 1.0277 0.8691 0.9525 0.0686  0.0943  -0.0550 90  GLN L NE2 
4369 N N   . TYR C 91  ? 0.9742 0.8719 0.8910 0.0547  0.0741  -0.0275 91  TYR L N   
4370 C CA  . TYR C 91  ? 0.9807 0.8925 0.8838 0.0601  0.0821  -0.0160 91  TYR L CA  
4371 C C   . TYR C 91  ? 0.9978 0.9222 0.8780 0.0724  0.0798  -0.0213 91  TYR L C   
4372 O O   . TYR C 91  ? 1.0156 0.9585 0.8829 0.0764  0.0841  -0.0086 91  TYR L O   
4373 C CB  . TYR C 91  ? 0.9807 0.9005 0.8892 0.0516  0.0852  0.0011  91  TYR L CB  
4374 C CG  . TYR C 91  ? 0.9932 0.9124 0.9011 0.0496  0.0784  0.0067  91  TYR L CG  
4375 C CD1 . TYR C 91  ? 1.0063 0.9392 0.8967 0.0564  0.0775  0.0160  91  TYR L CD1 
4376 C CD2 . TYR C 91  ? 0.9939 0.9006 0.9184 0.0428  0.0741  0.0051  91  TYR L CD2 
4377 C CE1 . TYR C 91  ? 1.0197 0.9514 0.9085 0.0574  0.0719  0.0247  91  TYR L CE1 
4378 C CE2 . TYR C 91  ? 0.9976 0.9036 0.9224 0.0443  0.0683  0.0118  91  TYR L CE2 
4379 C CZ  . TYR C 91  ? 1.0120 0.9295 0.9186 0.0520  0.0670  0.0225  91  TYR L CZ  
4380 O OH  . TYR C 91  ? 1.0247 0.9409 0.9302 0.0564  0.0619  0.0326  91  TYR L OH  
4381 N N   . ASN C 92  ? 0.9997 0.9144 0.8755 0.0776  0.0738  -0.0410 92  ASN L N   
4382 C CA  . ASN C 92  ? 1.0185 0.9442 0.8703 0.0907  0.0711  -0.0520 92  ASN L CA  
4383 C C   . ASN C 92  ? 1.0181 0.9370 0.8626 0.1010  0.0810  -0.0593 92  ASN L C   
4384 O O   . ASN C 92  ? 1.0345 0.9683 0.8571 0.1146  0.0845  -0.0624 92  ASN L O   
4385 C CB  . ASN C 92  ? 1.0357 0.9569 0.8865 0.0900  0.0574  -0.0733 92  ASN L CB  
4386 C CG  . ASN C 92  ? 1.0598 0.9997 0.8813 0.1037  0.0520  -0.0844 92  ASN L CG  
4387 O OD1 . ASN C 92  ? 1.0986 1.0296 0.9119 0.1089  0.0489  -0.1086 92  ASN L OD1 
4388 N ND2 . ASN C 92  ? 1.0534 1.0181 0.8582 0.1097  0.0515  -0.0672 92  ASN L ND2 
4389 N N   . ASN C 93  ? 1.0010 0.8983 0.8632 0.0966  0.0864  -0.0610 93  ASN L N   
4390 C CA  . ASN C 93  ? 1.0146 0.8991 0.8727 0.1084  0.0959  -0.0675 93  ASN L CA  
4391 C C   . ASN C 93  ? 0.9912 0.8772 0.8636 0.1063  0.1057  -0.0492 93  ASN L C   
4392 O O   . ASN C 93  ? 0.9863 0.8630 0.8767 0.0937  0.1042  -0.0432 93  ASN L O   
4393 C CB  . ASN C 93  ? 1.0373 0.8889 0.9012 0.1071  0.0923  -0.0910 93  ASN L CB  
4394 C CG  . ASN C 93  ? 1.0572 0.8844 0.9213 0.1189  0.1039  -0.0953 93  ASN L CG  
4395 O OD1 . ASN C 93  ? 1.0559 0.8721 0.9350 0.1168  0.1117  -0.0820 93  ASN L OD1 
4396 N ND2 . ASN C 93  ? 1.0883 0.9061 0.9349 0.1328  0.1053  -0.1144 93  ASN L ND2 
4397 N N   . TRP C 94  ? 0.9898 0.8918 0.8537 0.1200  0.1154  -0.0410 94  TRP L N   
4398 C CA  . TRP C 94  ? 0.9625 0.8737 0.8383 0.1209  0.1235  -0.0247 94  TRP L CA  
4399 C C   . TRP C 94  ? 0.9894 0.8705 0.8705 0.1306  0.1299  -0.0301 94  TRP L C   
4400 O O   . TRP C 94  ? 1.0247 0.8878 0.8953 0.1445  0.1331  -0.0440 94  TRP L O   
4401 C CB  . TRP C 94  ? 0.9474 0.8971 0.8153 0.1308  0.1307  -0.0120 94  TRP L CB  
4402 C CG  . TRP C 94  ? 0.9140 0.8827 0.7947 0.1322  0.1371  0.0034  94  TRP L CG  
4403 C CD1 . TRP C 94  ? 0.9180 0.8795 0.8017 0.1473  0.1443  0.0058  94  TRP L CD1 
4404 C CD2 . TRP C 94  ? 0.8742 0.8731 0.7665 0.1180  0.1363  0.0181  94  TRP L CD2 
4405 N NE1 . TRP C 94  ? 0.8910 0.8824 0.7861 0.1448  0.1468  0.0215  94  TRP L NE1 
4406 C CE2 . TRP C 94  ? 0.8657 0.8804 0.7669 0.1254  0.1416  0.0273  94  TRP L CE2 
4407 C CE3 . TRP C 94  ? 0.8561 0.8691 0.7523 0.1001  0.1318  0.0242  94  TRP L CE3 
4408 C CZ2 . TRP C 94  ? 0.8446 0.8925 0.7584 0.1137  0.1409  0.0390  94  TRP L CZ2 
4409 C CZ3 . TRP C 94  ? 0.8392 0.8780 0.7490 0.0876  0.1326  0.0356  94  TRP L CZ3 
4410 C CH2 . TRP C 94  ? 0.8321 0.8903 0.7507 0.0934  0.1363  0.0413  94  TRP L CH2 
4411 N N   . PRO C 95  ? 0.9901 0.8636 0.8865 0.1250  0.1330  -0.0191 95  PRO L N   
4412 C CA  . PRO C 95  ? 0.9626 0.8559 0.8703 0.1092  0.1295  -0.0063 95  PRO L CA  
4413 C C   . PRO C 95  ? 0.9602 0.8381 0.8766 0.0913  0.1206  -0.0137 95  PRO L C   
4414 O O   . PRO C 95  ? 0.9757 0.8279 0.8938 0.0894  0.1172  -0.0278 95  PRO L O   
4415 C CB  . PRO C 95  ? 0.9551 0.8448 0.8715 0.1143  0.1367  0.0052  95  PRO L CB  
4416 C CG  . PRO C 95  ? 0.9867 0.8354 0.9031 0.1234  0.1418  -0.0036 95  PRO L CG  
4417 C CD  . PRO C 95  ? 1.0114 0.8555 0.9134 0.1348  0.1412  -0.0183 95  PRO L CD  
4418 N N   . TRP C 96  ? 0.9375 0.8325 0.8608 0.0783  0.1170  -0.0051 96  TRP L N   
4419 C CA  . TRP C 96  ? 0.9207 0.8047 0.8542 0.0640  0.1098  -0.0098 96  TRP L CA  
4420 C C   . TRP C 96  ? 0.9103 0.7732 0.8574 0.0601  0.1132  -0.0111 96  TRP L C   
4421 O O   . TRP C 96  ? 0.8963 0.7609 0.8451 0.0651  0.1207  -0.0020 96  TRP L O   
4422 C CB  . TRP C 96  ? 0.9148 0.8175 0.8522 0.0529  0.1071  -0.0007 96  TRP L CB  
4423 C CG  . TRP C 96  ? 0.9297 0.8564 0.8572 0.0548  0.1081  0.0068  96  TRP L CG  
4424 C CD1 . TRP C 96  ? 0.9245 0.8726 0.8563 0.0472  0.1107  0.0170  96  TRP L CD1 
4425 C CD2 . TRP C 96  ? 0.9547 0.8891 0.8673 0.0638  0.1075  0.0046  96  TRP L CD2 
4426 N NE1 . TRP C 96  ? 0.9362 0.9042 0.8596 0.0494  0.1127  0.0233  96  TRP L NE1 
4427 C CE2 . TRP C 96  ? 0.9515 0.9126 0.8614 0.0609  0.1113  0.0169  96  TRP L CE2 
4428 C CE3 . TRP C 96  ? 0.9756 0.8990 0.8766 0.0734  0.1043  -0.0076 96  TRP L CE3 
4429 C CZ2 . TRP C 96  ? 0.9659 0.9438 0.8613 0.0687  0.1136  0.0202  96  TRP L CZ2 
4430 C CZ3 . TRP C 96  ? 0.9859 0.9261 0.8696 0.0824  0.1051  -0.0068 96  TRP L CZ3 
4431 C CH2 . TRP C 96  ? 0.9810 0.9487 0.8615 0.0807  0.1106  0.0084  96  TRP L CH2 
4432 N N   . THR C 97  ? 0.9086 0.7554 0.8657 0.0516  0.1078  -0.0213 97  THR L N   
4433 C CA  . THR C 97  ? 0.9147 0.7433 0.8878 0.0455  0.1121  -0.0219 97  THR L CA  
4434 C C   . THR C 97  ? 0.9104 0.7441 0.8976 0.0330  0.1061  -0.0244 97  THR L C   
4435 O O   . THR C 97  ? 0.8985 0.7397 0.8843 0.0304  0.0967  -0.0308 97  THR L O   
4436 C CB  . THR C 97  ? 0.9351 0.7367 0.9116 0.0481  0.1140  -0.0341 97  THR L CB  
4437 O OG1 . THR C 97  ? 0.9322 0.7354 0.9055 0.0455  0.1030  -0.0502 97  THR L OG1 
4438 C CG2 . THR C 97  ? 0.9523 0.7438 0.9162 0.0637  0.1226  -0.0305 97  THR L CG2 
4439 N N   . PHE C 98  ? 0.9231 0.7545 0.9228 0.0275  0.1123  -0.0180 98  PHE L N   
4440 C CA  . PHE C 98  ? 0.9149 0.7521 0.9296 0.0179  0.1091  -0.0201 98  PHE L CA  
4441 C C   . PHE C 98  ? 0.9171 0.7406 0.9519 0.0108  0.1123  -0.0258 98  PHE L C   
4442 O O   . PHE C 98  ? 0.9386 0.7444 0.9753 0.0124  0.1198  -0.0246 98  PHE L O   
4443 C CB  . PHE C 98  ? 0.9123 0.7620 0.9257 0.0167  0.1145  -0.0102 98  PHE L CB  
4444 C CG  . PHE C 98  ? 0.9183 0.7827 0.9165 0.0196  0.1123  -0.0053 98  PHE L CG  
4445 C CD1 . PHE C 98  ? 0.9312 0.8022 0.9168 0.0272  0.1162  0.0012  98  PHE L CD1 
4446 C CD2 . PHE C 98  ? 0.9205 0.7923 0.9191 0.0147  0.1070  -0.0068 98  PHE L CD2 
4447 C CE1 . PHE C 98  ? 0.9318 0.8217 0.9080 0.0273  0.1143  0.0054  98  PHE L CE1 
4448 C CE2 . PHE C 98  ? 0.9252 0.8089 0.9134 0.0138  0.1060  -0.0025 98  PHE L CE2 
4449 C CZ  . PHE C 98  ? 0.9248 0.8200 0.9030 0.0189  0.1094  0.0032  98  PHE L CZ  
4450 N N   . GLY C 99  ? 0.9112 0.7433 0.9630 0.0032  0.1074  -0.0313 99  GLY L N   
4451 C CA  . GLY C 99  ? 0.9262 0.7532 1.0027 -0.0062 0.1118  -0.0351 99  GLY L CA  
4452 C C   . GLY C 99  ? 0.9314 0.7594 1.0136 -0.0073 0.1259  -0.0217 99  GLY L C   
4453 O O   . GLY C 99  ? 0.9032 0.7396 0.9701 -0.0010 0.1294  -0.0126 99  GLY L O   
4454 N N   . GLN C 100 ? 0.9702 0.7917 1.0747 -0.0162 0.1341  -0.0209 100 GLN L N   
4455 C CA  . GLN C 100 ? 0.9937 0.8174 1.1028 -0.0165 0.1495  -0.0062 100 GLN L CA  
4456 C C   . GLN C 100 ? 0.9758 0.8246 1.0909 -0.0168 0.1495  -0.0057 100 GLN L C   
4457 O O   . GLN C 100 ? 0.9805 0.8380 1.0886 -0.0128 0.1600  0.0050  100 GLN L O   
4458 C CB  . GLN C 100 ? 1.0335 0.8402 1.1657 -0.0269 0.1607  -0.0031 100 GLN L CB  
4459 C CG  . GLN C 100 ? 1.0522 0.8730 1.2179 -0.0412 0.1587  -0.0126 100 GLN L CG  
4460 C CD  . GLN C 100 ? 1.0684 0.8901 1.2450 -0.0479 0.1420  -0.0333 100 GLN L CD  
4461 O OE1 . GLN C 100 ? 1.0937 0.9016 1.2519 -0.0423 0.1330  -0.0414 100 GLN L OE1 
4462 N NE2 . GLN C 100 ? 1.0661 0.9086 1.2729 -0.0591 0.1378  -0.0423 100 GLN L NE2 
4463 N N   . GLY C 101 ? 0.9578 0.8189 1.0850 -0.0197 0.1378  -0.0179 101 GLY L N   
4464 C CA  . GLY C 101 ? 0.9454 0.8267 1.0772 -0.0166 0.1369  -0.0191 101 GLY L CA  
4465 C C   . GLY C 101 ? 0.9528 0.8510 1.1174 -0.0237 0.1370  -0.0249 101 GLY L C   
4466 O O   . GLY C 101 ? 0.9667 0.8624 1.1525 -0.0342 0.1421  -0.0252 101 GLY L O   
4467 N N   . THR C 102 ? 0.9543 0.8698 1.1244 -0.0178 0.1318  -0.0295 102 THR L N   
4468 C CA  . THR C 102 ? 0.9495 0.8891 1.1517 -0.0209 0.1321  -0.0341 102 THR L CA  
4469 C C   . THR C 102 ? 0.9312 0.8844 1.1318 -0.0108 0.1394  -0.0319 102 THR L C   
4470 O O   . THR C 102 ? 0.9193 0.8710 1.1087 -0.0007 0.1315  -0.0358 102 THR L O   
4471 C CB  . THR C 102 ? 0.9507 0.9005 1.1647 -0.0207 0.1143  -0.0451 102 THR L CB  
4472 O OG1 . THR C 102 ? 0.9553 0.8930 1.1713 -0.0309 0.1087  -0.0508 102 THR L OG1 
4473 C CG2 . THR C 102 ? 0.9470 0.9294 1.1958 -0.0212 0.1126  -0.0499 102 THR L CG2 
4474 N N   . LYS C 103 ? 0.9425 0.9076 1.1538 -0.0133 0.1557  -0.0255 103 LYS L N   
4475 C CA  . LYS C 103 ? 0.9526 0.9310 1.1594 -0.0029 0.1650  -0.0252 103 LYS L CA  
4476 C C   . LYS C 103 ? 0.9381 0.9431 1.1752 0.0019  0.1626  -0.0317 103 LYS L C   
4477 O O   . LYS C 103 ? 0.9330 0.9590 1.2025 -0.0068 0.1656  -0.0309 103 LYS L O   
4478 C CB  . LYS C 103 ? 0.9730 0.9579 1.1760 -0.0053 0.1844  -0.0144 103 LYS L CB  
4479 C CG  . LYS C 103 ? 0.9944 0.9931 1.1852 0.0064  0.1949  -0.0162 103 LYS L CG  
4480 C CD  . LYS C 103 ? 1.0211 1.0293 1.2020 0.0059  0.2137  -0.0038 103 LYS L CD  
4481 C CE  . LYS C 103 ? 1.0439 1.0690 1.2098 0.0187  0.2237  -0.0091 103 LYS L CE  
4482 N NZ  . LYS C 103 ? 1.0679 1.1078 1.2220 0.0197  0.2425  0.0048  103 LYS L NZ  
4483 N N   . VAL C 104 ? 0.9361 0.9401 1.1642 0.0162  0.1575  -0.0379 104 VAL L N   
4484 C CA  . VAL C 104 ? 0.9389 0.9679 1.1933 0.0264  0.1555  -0.0430 104 VAL L CA  
4485 C C   . VAL C 104 ? 0.9532 0.9966 1.2086 0.0361  0.1728  -0.0437 104 VAL L C   
4486 O O   . VAL C 104 ? 0.9711 0.9961 1.1980 0.0437  0.1772  -0.0471 104 VAL L O   
4487 C CB  . VAL C 104 ? 0.9354 0.9510 1.1800 0.0389  0.1400  -0.0475 104 VAL L CB  
4488 C CG1 . VAL C 104 ? 0.9383 0.9802 1.2093 0.0540  0.1385  -0.0508 104 VAL L CG1 
4489 C CG2 . VAL C 104 ? 0.9286 0.9337 1.1680 0.0310  0.1237  -0.0469 104 VAL L CG2 
4490 N N   . GLU C 105 ? 0.9663 1.0452 1.2551 0.0352  0.1826  -0.0419 105 GLU L N   
4491 C CA  . GLU C 105 ? 0.9855 1.0854 1.2781 0.0458  0.2007  -0.0426 105 GLU L CA  
4492 C C   . GLU C 105 ? 0.9980 1.1224 1.3160 0.0631  0.1980  -0.0495 105 GLU L C   
4493 O O   . GLU C 105 ? 0.9787 1.1199 1.3237 0.0618  0.1853  -0.0499 105 GLU L O   
4494 C CB  . GLU C 105 ? 0.9853 1.1097 1.2966 0.0324  0.2180  -0.0318 105 GLU L CB  
4495 C CG  . GLU C 105 ? 0.9933 1.0928 1.2763 0.0209  0.2237  -0.0223 105 GLU L CG  
4496 C CD  . GLU C 105 ? 1.0038 1.1210 1.3046 0.0074  0.2420  -0.0074 105 GLU L CD  
4497 O OE1 . GLU C 105 ? 1.0119 1.1090 1.2898 0.0008  0.2479  0.0031  105 GLU L OE1 
4498 O OE2 . GLU C 105 ? 1.0097 1.1618 1.3485 0.0038  0.2510  -0.0050 105 GLU L OE2 
4499 N N   . ILE C 106 ? 1.0315 1.1227 0.9891 0.0564  0.0198  -0.0711 106 ILE L N   
4500 C CA  . ILE C 106 ? 1.0486 1.1103 1.0000 0.0383  0.0155  -0.0585 106 ILE L CA  
4501 C C   . ILE C 106 ? 1.0311 1.0460 1.0052 0.0372  0.0072  -0.0650 106 ILE L C   
4502 O O   . ILE C 106 ? 1.0047 1.0100 0.9984 0.0320  0.0110  -0.0631 106 ILE L O   
4503 C CB  . ILE C 106 ? 1.0586 1.1294 0.9984 0.0106  0.0219  -0.0323 106 ILE L CB  
4504 C CG1 . ILE C 106 ? 1.0774 1.2141 0.9994 0.0037  0.0312  -0.0199 106 ILE L CG1 
4505 C CG2 . ILE C 106 ? 1.0857 1.1140 1.0081 -0.0016 0.0101  -0.0220 106 ILE L CG2 
4506 C CD1 . ILE C 106 ? 1.1093 1.2767 1.0065 0.0148  0.0291  -0.0236 106 ILE L CD1 
4507 N N   . LYS C 107 ? 1.0477 1.0421 1.0188 0.0415  -0.0040 -0.0715 107 LYS L N   
4508 C CA  . LYS C 107 ? 1.0464 1.0165 1.0403 0.0385  -0.0118 -0.0750 107 LYS L CA  
4509 C C   . LYS C 107 ? 1.0446 1.0025 1.0324 0.0303  -0.0120 -0.0633 107 LYS L C   
4510 O O   . LYS C 107 ? 1.0631 1.0132 1.0245 0.0298  -0.0175 -0.0576 107 LYS L O   
4511 C CB  . LYS C 107 ? 1.0725 1.0334 1.0681 0.0482  -0.0274 -0.0894 107 LYS L CB  
4512 C CG  . LYS C 107 ? 1.0991 1.0527 1.0960 0.0589  -0.0376 -0.1046 107 LYS L CG  
4513 C CD  . LYS C 107 ? 1.1212 1.0555 1.1230 0.0613  -0.0595 -0.1165 107 LYS L CD  
4514 C CE  . LYS C 107 ? 1.1373 1.0758 1.1168 0.0730  -0.0661 -0.1233 107 LYS L CE  
4515 N NZ  . LYS C 107 ? 1.1627 1.0817 1.1469 0.0747  -0.0906 -0.1360 107 LYS L NZ  
4516 N N   . ARG C 108 ? 1.0244 0.9784 1.0320 0.0262  -0.0090 -0.0602 108 ARG L N   
4517 C CA  . ARG C 108 ? 1.0292 0.9690 1.0280 0.0280  -0.0141 -0.0551 108 ARG L CA  
4518 C C   . ARG C 108 ? 1.0149 0.9718 1.0429 0.0345  -0.0162 -0.0621 108 ARG L C   
4519 O O   . ARG C 108 ? 1.0077 0.9821 1.0614 0.0291  -0.0149 -0.0658 108 ARG L O   
4520 C CB  . ARG C 108 ? 1.0320 0.9598 1.0178 0.0183  -0.0085 -0.0428 108 ARG L CB  
4521 C CG  . ARG C 108 ? 1.0063 0.9500 1.0171 0.0128  0.0041  -0.0418 108 ARG L CG  
4522 C CD  . ARG C 108 ? 1.0147 0.9448 1.0176 0.0083  0.0052  -0.0334 108 ARG L CD  
4523 N NE  . ARG C 108 ? 1.0279 0.9490 1.0294 0.0225  -0.0032 -0.0391 108 ARG L NE  
4524 C CZ  . ARG C 108 ? 1.0408 0.9288 1.0118 0.0292  -0.0170 -0.0371 108 ARG L CZ  
4525 N NH1 . ARG C 108 ? 1.0636 0.9201 1.0043 0.0134  -0.0247 -0.0242 108 ARG L NH1 
4526 N NH2 . ARG C 108 ? 1.0444 0.9330 1.0127 0.0521  -0.0263 -0.0477 108 ARG L NH2 
4527 N N   . THR C 109 ? 1.0214 0.9748 1.0414 0.0464  -0.0226 -0.0633 109 THR L N   
4528 C CA  . THR C 109 ? 0.9832 0.9733 1.0301 0.0554  -0.0227 -0.0688 109 THR L CA  
4529 C C   . THR C 109 ? 0.9454 0.9510 1.0107 0.0460  -0.0095 -0.0618 109 THR L C   
4530 O O   . THR C 109 ? 0.9255 0.9061 0.9773 0.0387  -0.0033 -0.0552 109 THR L O   
4531 C CB  . THR C 109 ? 0.9996 0.9861 1.0259 0.0817  -0.0367 -0.0772 109 THR L CB  
4532 O OG1 . THR C 109 ? 1.0182 0.9589 1.0088 0.0862  -0.0421 -0.0729 109 THR L OG1 
4533 C CG2 . THR C 109 ? 1.0165 0.9903 1.0258 0.0926  -0.0521 -0.0844 109 THR L CG2 
4534 N N   . VAL C 110 ? 0.9191 0.9723 1.0152 0.0439  -0.0060 -0.0614 110 VAL L N   
4535 C CA  . VAL C 110 ? 0.8984 0.9723 1.0116 0.0331  0.0053  -0.0526 110 VAL L CA  
4536 C C   . VAL C 110 ? 0.8922 0.9564 0.9840 0.0520  0.0073  -0.0550 110 VAL L C   
4537 O O   . VAL C 110 ? 0.9130 0.9756 0.9853 0.0773  -0.0031 -0.0652 110 VAL L O   
4538 C CB  . VAL C 110 ? 0.8916 1.0284 1.0400 0.0212  0.0061  -0.0467 110 VAL L CB  
4539 C CG1 . VAL C 110 ? 0.9061 1.0954 1.0611 0.0427  -0.0003 -0.0557 110 VAL L CG1 
4540 C CG2 . VAL C 110 ? 0.8749 1.0375 1.0366 0.0089  0.0172  -0.0345 110 VAL L CG2 
4541 N N   . ALA C 111 ? 0.8647 0.9165 0.9558 0.0420  0.0167  -0.0472 111 ALA L N   
4542 C CA  . ALA C 111 ? 0.8735 0.9078 0.9413 0.0574  0.0154  -0.0494 111 ALA L CA  
4543 C C   . ALA C 111 ? 0.8472 0.9049 0.9311 0.0476  0.0282  -0.0408 111 ALA L C   
4544 O O   . ALA C 111 ? 0.8286 0.8739 0.9231 0.0263  0.0352  -0.0318 111 ALA L O   
4545 C CB  . ALA C 111 ? 0.8941 0.8683 0.9298 0.0523  0.0079  -0.0470 111 ALA L CB  
4546 N N   . ALA C 112 ? 0.8424 0.9353 0.9240 0.0674  0.0293  -0.0451 112 ALA L N   
4547 C CA  . ALA C 112 ? 0.8242 0.9477 0.9181 0.0601  0.0412  -0.0360 112 ALA L CA  
4548 C C   . ALA C 112 ? 0.8229 0.8937 0.8937 0.0588  0.0403  -0.0346 112 ALA L C   
4549 O O   . ALA C 112 ? 0.8531 0.8767 0.8924 0.0723  0.0272  -0.0426 112 ALA L O   
4550 C CB  . ALA C 112 ? 0.8387 1.0294 0.9346 0.0864  0.0426  -0.0427 112 ALA L CB  
4551 N N   . PRO C 113 ? 0.8055 0.8806 0.8884 0.0406  0.0507  -0.0230 113 PRO L N   
4552 C CA  . PRO C 113 ? 0.8204 0.8540 0.8851 0.0382  0.0496  -0.0212 113 PRO L CA  
4553 C C   . PRO C 113 ? 0.8420 0.8799 0.8846 0.0617  0.0457  -0.0278 113 PRO L C   
4554 O O   . PRO C 113 ? 0.8652 0.9566 0.9161 0.0735  0.0526  -0.0279 113 PRO L O   
4555 C CB  . PRO C 113 ? 0.8012 0.8422 0.8868 0.0147  0.0595  -0.0082 113 PRO L CB  
4556 C CG  . PRO C 113 ? 0.7986 0.8936 0.9063 0.0076  0.0651  -0.0002 113 PRO L CG  
4557 C CD  . PRO C 113 ? 0.7986 0.9151 0.9104 0.0188  0.0600  -0.0091 113 PRO L CD  
4558 N N   . SER C 114 ? 0.8664 0.8508 0.8785 0.0672  0.0323  -0.0324 114 SER L N   
4559 C CA  . SER C 114 ? 0.8967 0.8691 0.8826 0.0867  0.0243  -0.0387 114 SER L CA  
4560 C C   . SER C 114 ? 0.8723 0.8530 0.8727 0.0682  0.0370  -0.0268 114 SER L C   
4561 O O   . SER C 114 ? 0.8463 0.8037 0.8552 0.0446  0.0390  -0.0180 114 SER L O   
4562 C CB  . SER C 114 ? 0.9541 0.8562 0.8973 0.0941  -0.0021 -0.0459 114 SER L CB  
4563 O OG  . SER C 114 ? 0.9916 0.8773 0.9148 0.1139  -0.0183 -0.0573 114 SER L OG  
4564 N N   . VAL C 115 ? 0.8791 0.8997 0.8808 0.0815  0.0450  -0.0268 115 VAL L N   
4565 C CA  . VAL C 115 ? 0.8722 0.9041 0.8867 0.0646  0.0566  -0.0139 115 VAL L CA  
4566 C C   . VAL C 115 ? 0.9109 0.9149 0.8949 0.0803  0.0461  -0.0206 115 VAL L C   
4567 O O   . VAL C 115 ? 0.9452 0.9591 0.9037 0.1118  0.0377  -0.0338 115 VAL L O   
4568 C CB  . VAL C 115 ? 0.8555 0.9551 0.8928 0.0587  0.0723  -0.0024 115 VAL L CB  
4569 C CG1 . VAL C 115 ? 0.8533 0.9548 0.8963 0.0405  0.0797  0.0128  115 VAL L CG1 
4570 C CG2 . VAL C 115 ? 0.8306 0.9514 0.8952 0.0401  0.0768  0.0044  115 VAL L CG2 
4571 N N   . PHE C 116 ? 0.9171 0.8885 0.9023 0.0611  0.0443  -0.0132 116 PHE L N   
4572 C CA  . PHE C 116 ? 0.9573 0.9006 0.9167 0.0695  0.0327  -0.0170 116 PHE L CA  
4573 C C   . PHE C 116 ? 0.9403 0.8989 0.9167 0.0537  0.0449  -0.0044 116 PHE L C   
4574 O O   . PHE C 116 ? 0.9448 0.9115 0.9469 0.0333  0.0544  0.0055  116 PHE L O   
4575 C CB  . PHE C 116 ? 1.0040 0.8892 0.9432 0.0587  0.0111  -0.0193 116 PHE L CB  
4576 C CG  . PHE C 116 ? 1.0485 0.9052 0.9702 0.0646  -0.0043 -0.0267 116 PHE L CG  
4577 C CD1 . PHE C 116 ? 1.0341 0.9046 0.9792 0.0495  0.0052  -0.0212 116 PHE L CD1 
4578 C CD2 . PHE C 116 ? 1.1155 0.9240 0.9914 0.0874  -0.0329 -0.0402 116 PHE L CD2 
4579 C CE1 . PHE C 116 ? 1.0644 0.9063 0.9903 0.0549  -0.0103 -0.0269 116 PHE L CE1 
4580 C CE2 . PHE C 116 ? 1.1566 0.9288 1.0098 0.0938  -0.0522 -0.0465 116 PHE L CE2 
4581 C CZ  . PHE C 116 ? 1.1260 0.9173 1.0055 0.0763  -0.0394 -0.0387 116 PHE L CZ  
4582 N N   . ILE C 117 ? 0.9522 0.9097 0.9091 0.0667  0.0410  -0.0067 117 ILE L N   
4583 C CA  . ILE C 117 ? 0.9456 0.9112 0.9121 0.0545  0.0487  0.0046  117 ILE L CA  
4584 C C   . ILE C 117 ? 0.9675 0.8979 0.9102 0.0597  0.0325  -0.0010 117 ILE L C   
4585 O O   . ILE C 117 ? 1.0029 0.9100 0.9141 0.0795  0.0160  -0.0138 117 ILE L O   
4586 C CB  . ILE C 117 ? 0.9499 0.9655 0.9195 0.0598  0.0633  0.0141  117 ILE L CB  
4587 C CG1 . ILE C 117 ? 0.9461 0.9601 0.9243 0.0418  0.0683  0.0298  117 ILE L CG1 
4588 C CG2 . ILE C 117 ? 0.9906 1.0269 0.9296 0.0922  0.0591  0.0025  117 ILE L CG2 
4589 C CD1 . ILE C 117 ? 0.9560 1.0169 0.9360 0.0353  0.0800  0.0470  117 ILE L CD1 
4590 N N   . PHE C 118 ? 0.9552 0.8800 0.9102 0.0436  0.0337  0.0073  118 PHE L N   
4591 C CA  . PHE C 118 ? 0.9776 0.8763 0.9161 0.0428  0.0178  0.0043  118 PHE L CA  
4592 C C   . PHE C 118 ? 0.9757 0.8886 0.9166 0.0442  0.0246  0.0116  118 PHE L C   
4593 O O   . PHE C 118 ? 0.9429 0.8685 0.9054 0.0329  0.0339  0.0207  118 PHE L O   
4594 C CB  . PHE C 118 ? 0.9673 0.8532 0.9194 0.0200  0.0086  0.0075  118 PHE L CB  
4595 C CG  . PHE C 118 ? 0.9663 0.8365 0.9150 0.0121  0.0009  0.0052  118 PHE L CG  
4596 C CD1 . PHE C 118 ? 0.9394 0.8288 0.9091 0.0087  0.0153  0.0070  118 PHE L CD1 
4597 C CD2 . PHE C 118 ? 1.0017 0.8308 0.9215 0.0067  -0.0249 0.0021  118 PHE L CD2 
4598 C CE1 . PHE C 118 ? 0.9449 0.8185 0.9085 0.0021  0.0073  0.0055  118 PHE L CE1 
4599 C CE2 . PHE C 118 ? 1.0242 0.8311 0.9347 -0.0025 -0.0358 0.0025  118 PHE L CE2 
4600 C CZ  . PHE C 118 ? 0.9874 0.8194 0.9207 -0.0036 -0.0180 0.0039  118 PHE L CZ  
4601 N N   . PRO C 119 ? 1.0278 0.9333 0.9414 0.0604  0.0163  0.0070  119 PRO L N   
4602 C CA  . PRO C 119 ? 1.0403 0.9544 0.9516 0.0610  0.0196  0.0148  119 PRO L CA  
4603 C C   . PRO C 119 ? 1.0321 0.9329 0.9567 0.0467  0.0095  0.0164  119 PRO L C   
4604 O O   . PRO C 119 ? 1.0181 0.9096 0.9518 0.0342  -0.0002 0.0130  119 PRO L O   
4605 C CB  . PRO C 119 ? 1.0735 0.9834 0.9475 0.0859  0.0106  0.0056  119 PRO L CB  
4606 C CG  . PRO C 119 ? 1.0962 0.9725 0.9494 0.0956  -0.0093 -0.0102 119 PRO L CG  
4607 C CD  . PRO C 119 ? 1.0694 0.9530 0.9467 0.0829  -0.0003 -0.0077 119 PRO L CD  
4608 N N   . PRO C 120 ? 1.0523 0.9580 0.9775 0.0478  0.0105  0.0230  120 PRO L N   
4609 C CA  . PRO C 120 ? 1.0582 0.9633 0.9955 0.0407  -0.0002 0.0220  120 PRO L CA  
4610 C C   . PRO C 120 ? 1.0851 0.9763 1.0076 0.0387  -0.0202 0.0150  120 PRO L C   
4611 O O   . PRO C 120 ? 1.0972 0.9685 0.9895 0.0515  -0.0286 0.0094  120 PRO L O   
4612 C CB  . PRO C 120 ? 1.0718 0.9769 1.0018 0.0488  0.0014  0.0294  120 PRO L CB  
4613 C CG  . PRO C 120 ? 1.0761 0.9852 0.9985 0.0492  0.0157  0.0401  120 PRO L CG  
4614 C CD  . PRO C 120 ? 1.0739 0.9906 0.9869 0.0547  0.0204  0.0335  120 PRO L CD  
4615 N N   . SER C 121 ? 1.0946 1.0003 1.0366 0.0227  -0.0300 0.0154  121 SER L N   
4616 C CA  . SER C 121 ? 1.1304 1.0263 1.0613 0.0108  -0.0537 0.0137  121 SER L CA  
4617 C C   . SER C 121 ? 1.1711 1.0626 1.0870 0.0239  -0.0627 0.0114  121 SER L C   
4618 O O   . SER C 121 ? 1.1700 1.0775 1.0943 0.0362  -0.0520 0.0136  121 SER L O   
4619 C CB  . SER C 121 ? 1.1136 1.0469 1.0734 -0.0144 -0.0594 0.0196  121 SER L CB  
4620 O OG  . SER C 121 ? 1.1591 1.0883 1.1095 -0.0339 -0.0857 0.0227  121 SER L OG  
4621 N N   . ASP C 122 ? 1.2318 1.0943 1.1207 0.0214  -0.0869 0.0070  122 ASP L N   
4622 C CA  . ASP C 122 ? 1.2735 1.1284 1.1438 0.0341  -0.0992 0.0036  122 ASP L CA  
4623 C C   . ASP C 122 ? 1.2631 1.1598 1.1631 0.0202  -0.1061 0.0084  122 ASP L C   
4624 O O   . ASP C 122 ? 1.2615 1.1659 1.1572 0.0347  -0.1086 0.0067  122 ASP L O   
4625 C CB  . ASP C 122 ? 1.3382 1.1436 1.1658 0.0378  -0.1284 -0.0053 122 ASP L CB  
4626 C CG  . ASP C 122 ? 1.3671 1.1402 1.1605 0.0625  -0.1243 -0.0151 122 ASP L CG  
4627 O OD1 . ASP C 122 ? 1.3542 1.1432 1.1391 0.0873  -0.1034 -0.0160 122 ASP L OD1 
4628 O OD2 . ASP C 122 ? 1.4039 1.1395 1.1777 0.0563  -0.1440 -0.0206 122 ASP L OD2 
4629 N N   . GLU C 123 ? 1.2686 1.1986 1.1972 -0.0067 -0.1099 0.0146  123 GLU L N   
4630 C CA  . GLU C 123 ? 1.2692 1.2630 1.2314 -0.0172 -0.1133 0.0186  123 GLU L CA  
4631 C C   . GLU C 123 ? 1.2325 1.2546 1.2129 0.0096  -0.0914 0.0144  123 GLU L C   
4632 O O   . GLU C 123 ? 1.2341 1.2868 1.2236 0.0238  -0.0963 0.0108  123 GLU L O   
4633 C CB  . GLU C 123 ? 1.2814 1.3180 1.2686 -0.0532 -0.1192 0.0292  123 GLU L CB  
4634 C CG  . GLU C 123 ? 1.3377 1.3399 1.3027 -0.0881 -0.1511 0.0376  123 GLU L CG  
4635 C CD  . GLU C 123 ? 1.3729 1.2990 1.3027 -0.0898 -0.1576 0.0355  123 GLU L CD  
4636 O OE1 . GLU C 123 ? 1.3642 1.2907 1.2971 -0.1202 -0.1653 0.0466  123 GLU L OE1 
4637 O OE2 . GLU C 123 ? 1.3872 1.2582 1.2843 -0.0594 -0.1564 0.0230  123 GLU L OE2 
4638 N N   . GLN C 124 ? 1.2013 1.2075 1.1830 0.0170  -0.0716 0.0144  124 GLN L N   
4639 C CA  . GLN C 124 ? 1.1715 1.1888 1.1635 0.0388  -0.0574 0.0112  124 GLN L CA  
4640 C C   . GLN C 124 ? 1.2082 1.1888 1.1741 0.0609  -0.0589 0.0109  124 GLN L C   
4641 O O   . GLN C 124 ? 1.2290 1.2164 1.1966 0.0798  -0.0619 0.0078  124 GLN L O   
4642 C CB  . GLN C 124 ? 1.1281 1.1313 1.1246 0.0355  -0.0403 0.0132  124 GLN L CB  
4643 C CG  . GLN C 124 ? 1.1052 1.1158 1.1111 0.0541  -0.0326 0.0093  124 GLN L CG  
4644 C CD  . GLN C 124 ? 1.0784 1.0705 1.0865 0.0492  -0.0185 0.0119  124 GLN L CD  
4645 O OE1 . GLN C 124 ? 1.0576 1.0438 1.0681 0.0618  -0.0163 0.0089  124 GLN L OE1 
4646 N NE2 . GLN C 124 ? 1.0707 1.0492 1.0742 0.0329  -0.0129 0.0161  124 GLN L NE2 
4647 N N   . LEU C 125 ? 1.2414 1.1833 1.1786 0.0608  -0.0592 0.0139  125 LEU L N   
4648 C CA  . LEU C 125 ? 1.2778 1.1915 1.1864 0.0778  -0.0586 0.0180  125 LEU L CA  
4649 C C   . LEU C 125 ? 1.3011 1.2231 1.2044 0.0892  -0.0759 0.0142  125 LEU L C   
4650 O O   . LEU C 125 ? 1.3311 1.2374 1.2190 0.1048  -0.0785 0.0178  125 LEU L O   
4651 C CB  . LEU C 125 ? 1.2986 1.1872 1.1773 0.0793  -0.0549 0.0196  125 LEU L CB  
4652 C CG  . LEU C 125 ? 1.2937 1.1789 1.1727 0.0753  -0.0366 0.0243  125 LEU L CG  
4653 C CD1 . LEU C 125 ? 1.3212 1.1957 1.1677 0.0863  -0.0352 0.0218  125 LEU L CD1 
4654 C CD2 . LEU C 125 ? 1.2927 1.1767 1.1754 0.0754  -0.0248 0.0363  125 LEU L CD2 
4655 N N   . LYS C 126 ? 1.3005 1.2456 1.2146 0.0789  -0.0911 0.0086  126 LYS L N   
4656 C CA  . LYS C 126 ? 1.3127 1.2765 1.2266 0.0881  -0.1093 0.0042  126 LYS L CA  
4657 C C   . LYS C 126 ? 1.2793 1.2851 1.2190 0.1023  -0.1101 -0.0004 126 LYS L C   
4658 O O   . LYS C 126 ? 1.3103 1.3259 1.2445 0.1213  -0.1237 -0.0053 126 LYS L O   
4659 C CB  . LYS C 126 ? 1.3354 1.3159 1.2545 0.0668  -0.1292 0.0022  126 LYS L CB  
4660 C CG  . LYS C 126 ? 1.3898 1.3218 1.2685 0.0702  -0.1434 0.0000  126 LYS L CG  
4661 C CD  . LYS C 126 ? 1.4274 1.3506 1.2845 0.0932  -0.1530 -0.0026 126 LYS L CD  
4662 C CE  . LYS C 126 ? 1.4665 1.3428 1.2771 0.1037  -0.1642 -0.0064 126 LYS L CE  
4663 N NZ  . LYS C 126 ? 1.4966 1.3613 1.2996 0.0852  -0.1928 -0.0122 126 LYS L NZ  
4664 N N   . SER C 127 ? 1.2622 1.2974 1.1166 -0.0394 -0.0582 -0.0016 127 SER L N   
4665 C CA  . SER C 127 ? 1.2484 1.3264 1.1315 0.0017  -0.0798 -0.0180 127 SER L CA  
4666 C C   . SER C 127 ? 1.2644 1.2715 1.1308 0.0191  -0.1052 -0.0222 127 SER L C   
4667 O O   . SER C 127 ? 1.3147 1.3218 1.1824 0.0409  -0.1376 -0.0281 127 SER L O   
4668 C CB  . SER C 127 ? 1.2164 1.3461 1.1270 0.0209  -0.0660 -0.0307 127 SER L CB  
4669 O OG  . SER C 127 ? 1.2257 1.4024 1.1624 0.0661  -0.0879 -0.0522 127 SER L OG  
4670 N N   . GLY C 128 ? 1.2318 1.1791 1.0797 0.0074  -0.0939 -0.0183 128 GLY L N   
4671 C CA  . GLY C 128 ? 1.2448 1.1219 1.0688 0.0129  -0.1198 -0.0175 128 GLY L CA  
4672 C C   . GLY C 128 ? 1.2166 1.0694 1.0406 0.0173  -0.1090 -0.0218 128 GLY L C   
4673 O O   . GLY C 128 ? 1.2519 1.0447 1.0466 -0.0007 -0.1179 -0.0126 128 GLY L O   
4674 N N   . THR C 129 ? 1.1539 1.0582 1.0087 0.0373  -0.0912 -0.0340 129 THR L N   
4675 C CA  . THR C 129 ? 1.1242 1.0135 0.9827 0.0421  -0.0799 -0.0382 129 THR L CA  
4676 C C   . THR C 129 ? 1.0777 0.9647 0.9314 0.0100  -0.0441 -0.0273 129 THR L C   
4677 O O   . THR C 129 ? 1.0592 0.9625 0.9098 -0.0092 -0.0284 -0.0206 129 THR L O   
4678 C CB  . THR C 129 ? 1.1008 1.0479 0.9917 0.0784  -0.0800 -0.0576 129 THR L CB  
4679 O OG1 . THR C 129 ? 1.1271 1.0850 1.0230 0.1148  -0.1151 -0.0733 129 THR L OG1 
4680 C CG2 . THR C 129 ? 1.0927 1.0195 0.9851 0.0866  -0.0746 -0.0629 129 THR L CG2 
4681 N N   . ALA C 130 ? 1.0593 0.9239 0.9099 0.0062  -0.0350 -0.0268 130 ALA L N   
4682 C CA  . ALA C 130 ? 1.0346 0.9044 0.8861 -0.0134 -0.0040 -0.0223 130 ALA L CA  
4683 C C   . ALA C 130 ? 1.0154 0.8922 0.8832 -0.0006 0.0033  -0.0282 130 ALA L C   
4684 O O   . ALA C 130 ? 1.0453 0.8919 0.9019 -0.0011 -0.0097 -0.0263 130 ALA L O   
4685 C CB  . ALA C 130 ? 1.0551 0.8913 0.8770 -0.0428 0.0001  -0.0123 130 ALA L CB  
4686 N N   . SER C 131 ? 0.9786 0.8919 0.8682 0.0064  0.0210  -0.0329 131 SER L N   
4687 C CA  . SER C 131 ? 0.9585 0.8828 0.8645 0.0182  0.0276  -0.0381 131 SER L CA  
4688 C C   . SER C 131 ? 0.9357 0.8569 0.8429 0.0041  0.0502  -0.0344 131 SER L C   
4689 O O   . SER C 131 ? 0.9283 0.8580 0.8343 -0.0040 0.0613  -0.0329 131 SER L O   
4690 C CB  . SER C 131 ? 0.9474 0.9196 0.8750 0.0368  0.0259  -0.0468 131 SER L CB  
4691 O OG  . SER C 131 ? 0.9781 0.9602 0.9078 0.0602  0.0025  -0.0572 131 SER L OG  
4692 N N   . VAL C 132 ? 0.9328 0.8406 0.8399 0.0021  0.0530  -0.0335 132 VAL L N   
4693 C CA  . VAL C 132 ? 0.9307 0.8449 0.8443 -0.0034 0.0717  -0.0341 132 VAL L CA  
4694 C C   . VAL C 132 ? 0.9125 0.8418 0.8468 0.0099  0.0732  -0.0370 132 VAL L C   
4695 O O   . VAL C 132 ? 0.9279 0.8527 0.8646 0.0170  0.0618  -0.0375 132 VAL L O   
4696 C CB  . VAL C 132 ? 0.9501 0.8565 0.8504 -0.0196 0.0754  -0.0304 132 VAL L CB  
4697 C CG1 . VAL C 132 ? 0.9435 0.8705 0.8541 -0.0190 0.0947  -0.0364 132 VAL L CG1 
4698 C CG2 . VAL C 132 ? 0.9767 0.8685 0.8515 -0.0372 0.0704  -0.0259 132 VAL L CG2 
4699 N N   . VAL C 133 ? 0.9032 0.8434 0.8469 0.0120  0.0832  -0.0386 133 VAL L N   
4700 C CA  . VAL C 133 ? 0.8883 0.8436 0.8482 0.0204  0.0829  -0.0394 133 VAL L CA  
4701 C C   . VAL C 133 ? 0.8923 0.8440 0.8605 0.0217  0.0916  -0.0403 133 VAL L C   
4702 O O   . VAL C 133 ? 0.8997 0.8427 0.8627 0.0208  0.0975  -0.0435 133 VAL L O   
4703 C CB  . VAL C 133 ? 0.8844 0.8565 0.8441 0.0167  0.0805  -0.0371 133 VAL L CB  
4704 C CG1 . VAL C 133 ? 0.8712 0.8612 0.8430 0.0192  0.0794  -0.0359 133 VAL L CG1 
4705 C CG2 . VAL C 133 ? 0.8886 0.8828 0.8453 0.0176  0.0723  -0.0383 133 VAL L CG2 
4706 N N   . CYS C 134 ? 0.8984 0.8573 0.8784 0.0262  0.0897  -0.0395 134 CYS L N   
4707 C CA  . CYS C 134 ? 0.9089 0.8742 0.9024 0.0299  0.0952  -0.0402 134 CYS L CA  
4708 C C   . CYS C 134 ? 0.9107 0.8809 0.9126 0.0340  0.0901  -0.0380 134 CYS L C   
4709 O O   . CYS C 134 ? 0.9133 0.8936 0.9134 0.0340  0.0843  -0.0373 134 CYS L O   
4710 C CB  . CYS C 134 ? 0.9116 0.8842 0.9092 0.0252  0.0944  -0.0372 134 CYS L CB  
4711 S SG  . CYS C 134 ? 0.9169 0.9135 0.9352 0.0297  0.1020  -0.0390 134 CYS L SG  
4712 N N   . LEU C 135 ? 0.9062 0.8727 0.9157 0.0381  0.0903  -0.0383 135 LEU L N   
4713 C CA  . LEU C 135 ? 0.9002 0.8662 0.9118 0.0357  0.0818  -0.0330 135 LEU L CA  
4714 C C   . LEU C 135 ? 0.8955 0.8616 0.9223 0.0438  0.0797  -0.0332 135 LEU L C   
4715 O O   . LEU C 135 ? 0.9048 0.8603 0.9342 0.0541  0.0785  -0.0393 135 LEU L O   
4716 C CB  . LEU C 135 ? 0.9336 0.8793 0.9266 0.0273  0.0733  -0.0297 135 LEU L CB  
4717 C CG  . LEU C 135 ? 0.9631 0.8992 0.9488 0.0170  0.0585  -0.0204 135 LEU L CG  
4718 C CD1 . LEU C 135 ? 0.9451 0.9187 0.9349 0.0059  0.0590  -0.0147 135 LEU L CD1 
4719 C CD2 . LEU C 135 ? 1.0015 0.9050 0.9586 0.0025  0.0434  -0.0142 135 LEU L CD2 
4720 N N   . LEU C 136 ? 0.8931 0.8731 0.9290 0.0416  0.0775  -0.0288 136 LEU L N   
4721 C CA  . LEU C 136 ? 0.9144 0.8959 0.9637 0.0458  0.0719  -0.0259 136 LEU L CA  
4722 C C   . LEU C 136 ? 0.9364 0.9072 0.9755 0.0360  0.0588  -0.0178 136 LEU L C   
4723 O O   . LEU C 136 ? 0.9434 0.9303 0.9744 0.0248  0.0583  -0.0143 136 LEU L O   
4724 C CB  . LEU C 136 ? 0.9020 0.9008 0.9610 0.0439  0.0742  -0.0237 136 LEU L CB  
4725 C CG  . LEU C 136 ? 0.9068 0.9178 0.9710 0.0435  0.0817  -0.0260 136 LEU L CG  
4726 C CD1 . LEU C 136 ? 0.9069 0.9093 0.9547 0.0390  0.0852  -0.0288 136 LEU L CD1 
4727 C CD2 . LEU C 136 ? 0.9107 0.9305 0.9787 0.0360  0.0767  -0.0197 136 LEU L CD2 
4728 N N   . ASN C 137 ? 0.9693 0.9150 1.0059 0.0401  0.0454  -0.0160 137 ASN L N   
4729 C CA  . ASN C 137 ? 0.9982 0.9222 1.0140 0.0228  0.0264  -0.0044 137 ASN L CA  
4730 C C   . ASN C 137 ? 1.0047 0.9196 1.0285 0.0246  0.0117  0.0016  137 ASN L C   
4731 O O   . ASN C 137 ? 1.0063 0.9084 1.0445 0.0461  0.0056  -0.0056 137 ASN L O   
4732 C CB  . ASN C 137 ? 1.0455 0.9271 1.0369 0.0211  0.0119  -0.0047 137 ASN L CB  
4733 C CG  . ASN C 137 ? 1.0869 0.9554 1.0461 -0.0117 -0.0058 0.0119  137 ASN L CG  
4734 O OD1 . ASN C 137 ? 1.1157 0.9714 1.0628 -0.0282 -0.0251 0.0248  137 ASN L OD1 
4735 N ND2 . ASN C 137 ? 1.0901 0.9662 1.0332 -0.0257 -0.0011 0.0137  137 ASN L ND2 
4736 N N   . ASN C 138 ? 1.0048 0.9344 1.0199 0.0029  0.0061  0.0134  138 ASN L N   
4737 C CA  . ASN C 138 ? 1.0245 0.9403 1.0381 -0.0041 -0.0127 0.0238  138 ASN L CA  
4738 C C   . ASN C 138 ? 0.9945 0.9225 1.0393 0.0188  -0.0066 0.0166  138 ASN L C   
4739 O O   . ASN C 138 ? 1.0285 0.9375 1.0852 0.0401  -0.0171 0.0106  138 ASN L O   
4740 C CB  . ASN C 138 ? 1.0909 0.9501 1.0786 -0.0114 -0.0447 0.0329  138 ASN L CB  
4741 C CG  . ASN C 138 ? 1.1303 0.9807 1.0801 -0.0471 -0.0562 0.0469  138 ASN L CG  
4742 O OD1 . ASN C 138 ? 1.1161 1.0162 1.0641 -0.0643 -0.0379 0.0481  138 ASN L OD1 
4743 N ND2 . ASN C 138 ? 1.1992 0.9875 1.1159 -0.0586 -0.0899 0.0569  138 ASN L ND2 
4744 N N   . PHE C 139 ? 0.9526 0.9151 1.0084 0.0148  0.0076  0.0162  139 PHE L N   
4745 C CA  . PHE C 139 ? 0.9307 0.9090 1.0110 0.0268  0.0111  0.0141  139 PHE L CA  
4746 C C   . PHE C 139 ? 0.9239 0.9170 0.9991 0.0111  0.0091  0.0216  139 PHE L C   
4747 O O   . PHE C 139 ? 0.9027 0.9041 0.9578 -0.0047 0.0098  0.0236  139 PHE L O   
4748 C CB  . PHE C 139 ? 0.8916 0.8910 0.9861 0.0389  0.0299  0.0037  139 PHE L CB  
4749 C CG  . PHE C 139 ? 0.8671 0.8747 0.9475 0.0310  0.0419  0.0001  139 PHE L CG  
4750 C CD1 . PHE C 139 ? 0.8633 0.8650 0.9313 0.0311  0.0479  -0.0050 139 PHE L CD1 
4751 C CD2 . PHE C 139 ? 0.8523 0.8699 0.9296 0.0256  0.0433  0.0005  139 PHE L CD2 
4752 C CE1 . PHE C 139 ? 0.8480 0.8592 0.9051 0.0292  0.0550  -0.0107 139 PHE L CE1 
4753 C CE2 . PHE C 139 ? 0.8445 0.8624 0.9061 0.0256  0.0476  -0.0069 139 PHE L CE2 
4754 C CZ  . PHE C 139 ? 0.8422 0.8597 0.8959 0.0291  0.0535  -0.0131 139 PHE L CZ  
4755 N N   . TYR C 140 ? 0.9403 0.9433 1.0333 0.0158  0.0064  0.0242  140 TYR L N   
4756 C CA  . TYR C 140 ? 0.9605 0.9733 1.0471 0.0023  0.0031  0.0302  140 TYR L CA  
4757 C C   . TYR C 140 ? 0.9693 0.9973 1.0773 0.0078  0.0036  0.0321  140 TYR L C   
4758 O O   . TYR C 140 ? 0.9881 1.0244 1.1192 0.0200  -0.0017 0.0330  140 TYR L O   
4759 C CB  . TYR C 140 ? 0.9874 0.9879 1.0609 -0.0136 -0.0152 0.0423  140 TYR L CB  
4760 C CG  . TYR C 140 ? 0.9989 1.0110 1.0623 -0.0291 -0.0192 0.0476  140 TYR L CG  
4761 C CD1 . TYR C 140 ? 0.9965 1.0110 1.0756 -0.0275 -0.0265 0.0538  140 TYR L CD1 
4762 C CD2 . TYR C 140 ? 1.0060 1.0338 1.0432 -0.0450 -0.0159 0.0447  140 TYR L CD2 
4763 C CE1 . TYR C 140 ? 1.0006 1.0207 1.0660 -0.0427 -0.0319 0.0584  140 TYR L CE1 
4764 C CE2 . TYR C 140 ? 1.0133 1.0531 1.0374 -0.0568 -0.0198 0.0455  140 TYR L CE2 
4765 C CZ  . TYR C 140 ? 1.0155 1.0452 1.0518 -0.0563 -0.0285 0.0532  140 TYR L CZ  
4766 O OH  . TYR C 140 ? 1.0453 1.0817 1.0644 -0.0691 -0.0342 0.0540  140 TYR L OH  
4767 N N   . PRO C 141 ? 0.9786 1.0123 1.0773 -0.0008 0.0066  0.0321  141 PRO L N   
4768 C CA  . PRO C 141 ? 0.9875 1.0130 1.0579 -0.0073 0.0084  0.0253  141 PRO L CA  
4769 C C   . PRO C 141 ? 0.9854 1.0069 1.0453 0.0017  0.0188  0.0128  141 PRO L C   
4770 O O   . PRO C 141 ? 0.9783 1.0011 1.0504 0.0088  0.0263  0.0114  141 PRO L O   
4771 C CB  . PRO C 141 ? 1.0040 1.0254 1.0660 -0.0165 -0.0002 0.0295  141 PRO L CB  
4772 C CG  . PRO C 141 ? 1.0025 1.0352 1.0856 -0.0172 0.0005  0.0367  141 PRO L CG  
4773 C CD  . PRO C 141 ? 0.9845 1.0341 1.0962 -0.0050 0.0047  0.0378  141 PRO L CD  
4774 N N   . ARG C 142 ? 1.0019 1.0211 1.0381 0.0037  0.0174  0.0015  142 ARG L N   
4775 C CA  . ARG C 142 ? 1.0099 1.0270 1.0343 0.0158  0.0227  -0.0127 142 ARG L CA  
4776 C C   . ARG C 142 ? 1.0001 0.9950 1.0234 0.0186  0.0209  -0.0119 142 ARG L C   
4777 O O   . ARG C 142 ? 0.9883 0.9806 1.0114 0.0254  0.0269  -0.0172 142 ARG L O   
4778 C CB  . ARG C 142 ? 1.0498 1.0738 1.0496 0.0239  0.0165  -0.0296 142 ARG L CB  
4779 C CG  . ARG C 142 ? 1.0811 1.1135 1.0704 0.0421  0.0190  -0.0484 142 ARG L CG  
4780 C CD  . ARG C 142 ? 1.1358 1.1776 1.1010 0.0592  0.0089  -0.0717 142 ARG L CD  
4781 N NE  . ARG C 142 ? 1.1544 1.2401 1.1167 0.0494  0.0131  -0.0737 142 ARG L NE  
4782 C CZ  . ARG C 142 ? 1.1957 1.2957 1.1368 0.0598  0.0048  -0.0925 142 ARG L CZ  
4783 N NH1 . ARG C 142 ? 1.2549 1.3175 1.1736 0.0844  -0.0120 -0.1122 142 ARG L NH1 
4784 N NH2 . ARG C 142 ? 1.2053 1.3532 1.1427 0.0444  0.0102  -0.0917 142 ARG L NH2 
4785 N N   . GLU C 143 ? 1.0078 0.9884 1.0270 0.0082  0.0107  -0.0032 143 GLU L N   
4786 C CA  . GLU C 143 ? 1.0261 0.9854 1.0334 0.0005  0.0030  0.0010  143 GLU L CA  
4787 C C   . GLU C 143 ? 1.0032 0.9859 1.0340 -0.0026 0.0174  0.0073  143 GLU L C   
4788 O O   . GLU C 143 ? 1.0078 1.0202 1.0641 -0.0079 0.0237  0.0162  143 GLU L O   
4789 C CB  . GLU C 143 ? 1.0561 1.0030 1.0526 -0.0185 -0.0126 0.0137  143 GLU L CB  
4790 C CG  . GLU C 143 ? 1.0966 1.0110 1.0614 -0.0144 -0.0308 0.0047  143 GLU L CG  
4791 C CD  . GLU C 143 ? 1.0895 1.0275 1.0653 -0.0100 -0.0249 0.0018  143 GLU L CD  
4792 O OE1 . GLU C 143 ? 1.0744 1.0349 1.0731 -0.0228 -0.0214 0.0170  143 GLU L OE1 
4793 O OE2 . GLU C 143 ? 1.1011 1.0400 1.0615 0.0056  -0.0253 -0.0161 143 GLU L OE2 
4794 N N   . ALA C 144 ? 0.9935 0.9652 1.0148 0.0032  0.0209  0.0004  144 ALA L N   
4795 C CA  . ALA C 144 ? 0.9787 0.9720 1.0165 0.0014  0.0348  0.0028  144 ALA L CA  
4796 C C   . ALA C 144 ? 1.0302 0.9999 1.0436 -0.0062 0.0278  0.0025  144 ALA L C   
4797 O O   . ALA C 144 ? 1.0701 1.0095 1.0627 0.0049  0.0186  -0.0072 144 ALA L O   
4798 C CB  . ALA C 144 ? 0.9423 0.9479 0.9957 0.0171  0.0478  -0.0050 144 ALA L CB  
4799 N N   . LYS C 145 ? 1.0543 1.0440 1.0700 -0.0255 0.0308  0.0126  145 LYS L N   
4800 C CA  . LYS C 145 ? 1.0870 1.0536 1.0740 -0.0425 0.0203  0.0175  145 LYS L CA  
4801 C C   . LYS C 145 ? 1.0465 1.0334 1.0446 -0.0351 0.0383  0.0106  145 LYS L C   
4802 O O   . LYS C 145 ? 1.0111 1.0410 1.0383 -0.0266 0.0577  0.0063  145 LYS L O   
4803 C CB  . LYS C 145 ? 1.1386 1.1231 1.1141 -0.0787 0.0104  0.0361  145 LYS L CB  
4804 C CG  . LYS C 145 ? 1.2105 1.1537 1.1407 -0.1077 -0.0132 0.0478  145 LYS L CG  
4805 C CD  . LYS C 145 ? 1.2750 1.1366 1.1622 -0.1045 -0.0482 0.0467  145 LYS L CD  
4806 C CE  . LYS C 145 ? 1.3449 1.1513 1.1782 -0.1381 -0.0825 0.0619  145 LYS L CE  
4807 N NZ  . LYS C 145 ? 1.3446 1.1424 1.1708 -0.1338 -0.0788 0.0571  145 LYS L NZ  
4808 N N   . VAL C 146 ? 1.0666 1.0174 1.0385 -0.0364 0.0281  0.0084  146 VAL L N   
4809 C CA  . VAL C 146 ? 1.0637 1.0271 1.0384 -0.0345 0.0416  0.0038  146 VAL L CA  
4810 C C   . VAL C 146 ? 1.1241 1.0614 1.0629 -0.0621 0.0239  0.0150  146 VAL L C   
4811 O O   . VAL C 146 ? 1.1809 1.0639 1.0872 -0.0671 -0.0046 0.0189  146 VAL L O   
4812 C CB  . VAL C 146 ? 1.0432 0.9911 1.0230 -0.0072 0.0460  -0.0101 146 VAL L CB  
4813 C CG1 . VAL C 146 ? 1.0307 0.9826 1.0066 -0.0084 0.0555  -0.0132 146 VAL L CG1 
4814 C CG2 . VAL C 146 ? 1.0185 0.9893 1.0256 0.0105  0.0590  -0.0166 146 VAL L CG2 
4815 N N   . GLN C 147 ? 1.1227 1.0967 1.0634 -0.0799 0.0379  0.0189  147 GLN L N   
4816 C CA  . GLN C 147 ? 1.1618 1.1160 1.0647 -0.1133 0.0213  0.0322  147 GLN L CA  
4817 C C   . GLN C 147 ? 1.1174 1.0921 1.0238 -0.1102 0.0392  0.0246  147 GLN L C   
4818 O O   . GLN C 147 ? 1.0902 1.1243 1.0228 -0.1047 0.0658  0.0162  147 GLN L O   
4819 C CB  . GLN C 147 ? 1.2154 1.2098 1.1075 -0.1561 0.0170  0.0508  147 GLN L CB  
4820 C CG  . GLN C 147 ? 1.2581 1.2264 1.1393 -0.1661 -0.0049 0.0616  147 GLN L CG  
4821 C CD  . GLN C 147 ? 1.3077 1.3150 1.1698 -0.2184 -0.0148 0.0849  147 GLN L CD  
4822 O OE1 . GLN C 147 ? 1.3291 1.3867 1.1830 -0.2504 -0.0063 0.0935  147 GLN L OE1 
4823 N NE2 . GLN C 147 ? 1.3439 1.3333 1.1962 -0.2310 -0.0338 0.0960  147 GLN L NE2 
4824 N N   . TRP C 148 ? 1.1514 0.9731 1.0609 -0.0738 0.1492  0.0046  148 TRP L N   
4825 C CA  . TRP C 148 ? 1.1411 0.9673 1.0448 -0.0670 0.1535  0.0067  148 TRP L CA  
4826 C C   . TRP C 148 ? 1.1455 0.9777 1.0355 -0.0859 0.1576  0.0168  148 TRP L C   
4827 O O   . TRP C 148 ? 1.1828 0.9909 1.0566 -0.1027 0.1518  0.0252  148 TRP L O   
4828 C CB  . TRP C 148 ? 1.1587 0.9538 1.0507 -0.0537 0.1457  0.0077  148 TRP L CB  
4829 C CG  . TRP C 148 ? 1.1445 0.9451 1.0514 -0.0357 0.1442  -0.0005 148 TRP L CG  
4830 C CD1 . TRP C 148 ? 1.1460 0.9319 1.0555 -0.0268 0.1396  -0.0040 148 TRP L CD1 
4831 C CD2 . TRP C 148 ? 1.1255 0.9456 1.0424 -0.0262 0.1474  -0.0056 148 TRP L CD2 
4832 N NE1 . TRP C 148 ? 1.1246 0.9261 1.0487 -0.0133 0.1405  -0.0095 148 TRP L NE1 
4833 C CE2 . TRP C 148 ? 1.1139 0.9338 1.0419 -0.0142 0.1442  -0.0102 148 TRP L CE2 
4834 C CE3 . TRP C 148 ? 1.1201 0.9538 1.0328 -0.0274 0.1526  -0.0070 148 TRP L CE3 
4835 C CZ2 . TRP C 148 ? 1.0999 0.9329 1.0362 -0.0071 0.1449  -0.0142 148 TRP L CZ2 
4836 C CZ3 . TRP C 148 ? 1.1062 0.9458 1.0231 -0.0190 0.1526  -0.0130 148 TRP L CZ3 
4837 C CH2 . TRP C 148 ? 1.0919 0.9314 1.0212 -0.0106 0.1482  -0.0156 148 TRP L CH2 
4838 N N   . LYS C 149 ? 1.1239 0.9852 1.0165 -0.0834 0.1679  0.0160  149 LYS L N   
4839 C CA  . LYS C 149 ? 1.1376 1.0100 1.0153 -0.0995 0.1742  0.0258  149 LYS L CA  
4840 C C   . LYS C 149 ? 1.1272 0.9927 0.9876 -0.0900 0.1767  0.0247  149 LYS L C   
4841 O O   . LYS C 149 ? 1.1176 0.9934 0.9834 -0.0740 0.1811  0.0145  149 LYS L O   
4842 C CB  . LYS C 149 ? 1.1326 1.0562 1.0279 -0.1063 0.1870  0.0264  149 LYS L CB  
4843 C CG  . LYS C 149 ? 1.1394 1.0777 1.0504 -0.1228 0.1829  0.0306  149 LYS L CG  
4844 C CD  . LYS C 149 ? 1.1477 1.1464 1.0759 -0.1344 0.1950  0.0370  149 LYS L CD  
4845 C CE  . LYS C 149 ? 1.1585 1.1763 1.1020 -0.1559 0.1880  0.0430  149 LYS L CE  
4846 N NZ  . LYS C 149 ? 1.1419 1.1612 1.1050 -0.1391 0.1824  0.0322  149 LYS L NZ  
4847 N N   . VAL C 150 ? 1.1477 0.9918 0.9831 -0.1017 0.1724  0.0359  150 VAL L N   
4848 C CA  . VAL C 150 ? 1.1637 1.0013 0.9778 -0.0969 0.1726  0.0370  150 VAL L CA  
4849 C C   . VAL C 150 ? 1.1922 1.0467 0.9874 -0.1140 0.1827  0.0466  150 VAL L C   
4850 O O   . VAL C 150 ? 1.2173 1.0542 0.9960 -0.1318 0.1778  0.0608  150 VAL L O   
4851 C CB  . VAL C 150 ? 1.1819 0.9816 0.9821 -0.0917 0.1569  0.0436  150 VAL L CB  
4852 C CG1 . VAL C 150 ? 1.2055 1.0011 0.9811 -0.0911 0.1543  0.0477  150 VAL L CG1 
4853 C CG2 . VAL C 150 ? 1.1575 0.9500 0.9777 -0.0740 0.1494  0.0349  150 VAL L CG2 
4854 N N   . ASP C 151 ? 1.1867 1.0729 0.9812 -0.1075 0.1974  0.0389  151 ASP L N   
4855 C CA  . ASP C 151 ? 1.2085 1.1253 0.9904 -0.1203 0.2122  0.0460  151 ASP L CA  
4856 C C   . ASP C 151 ? 1.2017 1.1486 1.0052 -0.1374 0.2173  0.0547  151 ASP L C   
4857 O O   . ASP C 151 ? 1.2127 1.1720 1.0040 -0.1604 0.2215  0.0693  151 ASP L O   
4858 C CB  . ASP C 151 ? 1.2411 1.1355 0.9865 -0.1342 0.2077  0.0588  151 ASP L CB  
4859 C CG  . ASP C 151 ? 1.2514 1.1230 0.9734 -0.1210 0.2015  0.0516  151 ASP L CG  
4860 O OD1 . ASP C 151 ? 1.2500 1.1361 0.9670 -0.1074 0.2120  0.0379  151 ASP L OD1 
4861 O OD2 . ASP C 151 ? 1.2662 1.1050 0.9730 -0.1245 0.1857  0.0604  151 ASP L OD2 
4862 N N   . ASN C 152 ? 1.1801 1.1397 1.0144 -0.1284 0.2156  0.0466  152 ASN L N   
4863 C CA  . ASN C 152 ? 1.1803 1.1729 1.0378 -0.1449 0.2179  0.0536  152 ASN L CA  
4864 C C   . ASN C 152 ? 1.2015 1.1553 1.0454 -0.1713 0.2027  0.0667  152 ASN L C   
4865 O O   . ASN C 152 ? 1.2107 1.1855 1.0614 -0.1966 0.2027  0.0774  152 ASN L O   
4866 C CB  . ASN C 152 ? 1.1965 1.2516 1.0605 -0.1521 0.2372  0.0602  152 ASN L CB  
4867 C CG  . ASN C 152 ? 1.1867 1.2962 1.0861 -0.1594 0.2417  0.0637  152 ASN L CG  
4868 O OD1 . ASN C 152 ? 1.1760 1.2742 1.0937 -0.1575 0.2303  0.0590  152 ASN L OD1 
4869 N ND2 . ASN C 152 ? 1.1899 1.3633 1.0991 -0.1674 0.2583  0.0727  152 ASN L ND2 
4870 N N   . ALA C 153 ? 1.2135 1.1102 1.0368 -0.1650 0.1890  0.0661  153 ALA L N   
4871 C CA  . ALA C 153 ? 1.2484 1.0950 1.0505 -0.1833 0.1742  0.0774  153 ALA L CA  
4872 C C   . ALA C 153 ? 1.2375 1.0501 1.0490 -0.1685 0.1620  0.0674  153 ALA L C   
4873 O O   . ALA C 153 ? 1.2178 1.0135 1.0312 -0.1439 0.1580  0.0588  153 ALA L O   
4874 C CB  . ALA C 153 ? 1.2751 1.0849 1.0431 -0.1844 0.1688  0.0872  153 ALA L CB  
4875 N N   . LEU C 154 ? 1.2462 1.0508 1.0613 -0.1856 0.1561  0.0695  154 LEU L N   
4876 C CA  . LEU C 154 ? 1.2321 1.0143 1.0570 -0.1725 0.1475  0.0584  154 LEU L CA  
4877 C C   . LEU C 154 ? 1.2583 0.9762 1.0575 -0.1576 0.1356  0.0584  154 LEU L C   
4878 O O   . LEU C 154 ? 1.3064 0.9763 1.0734 -0.1722 0.1270  0.0691  154 LEU L O   
4879 C CB  . LEU C 154 ? 1.2528 1.0390 1.0796 -0.1999 0.1425  0.0620  154 LEU L CB  
4880 C CG  . LEU C 154 ? 1.2425 1.0425 1.0926 -0.1890 0.1398  0.0491  154 LEU L CG  
4881 C CD1 . LEU C 154 ? 1.2749 1.0741 1.1197 -0.2215 0.1315  0.0545  154 LEU L CD1 
4882 C CD2 . LEU C 154 ? 1.2378 0.9903 1.0786 -0.1618 0.1325  0.0382  154 LEU L CD2 
4883 N N   . GLN C 155 ? 1.2354 0.9540 1.0481 -0.1280 0.1353  0.0476  155 GLN L N   
4884 C CA  . GLN C 155 ? 1.2579 0.9311 1.0536 -0.1079 0.1259  0.0482  155 GLN L CA  
4885 C C   . GLN C 155 ? 1.2879 0.9191 1.0722 -0.1048 0.1178  0.0432  155 GLN L C   
4886 O O   . GLN C 155 ? 1.2628 0.9076 1.0587 -0.1150 0.1191  0.0363  155 GLN L O   
4887 C CB  . GLN C 155 ? 1.2181 0.9165 1.0344 -0.0815 0.1287  0.0401  155 GLN L CB  
4888 C CG  . GLN C 155 ? 1.2105 0.9366 1.0269 -0.0832 0.1343  0.0438  155 GLN L CG  
4889 C CD  . GLN C 155 ? 1.2592 0.9560 1.0461 -0.0879 0.1276  0.0581  155 GLN L CD  
4890 O OE1 . GLN C 155 ? 1.2779 0.9478 1.0550 -0.0716 0.1181  0.0624  155 GLN L OE1 
4891 N NE2 . GLN C 155 ? 1.2819 0.9871 1.0544 -0.1092 0.1329  0.0668  155 GLN L NE2 
4892 N N   . SER C 156 ? 1.3374 0.9175 1.0967 -0.0887 0.1093  0.0468  156 SER L N   
4893 C CA  . SER C 156 ? 1.3867 0.9134 1.1229 -0.0833 0.1019  0.0420  156 SER L CA  
4894 C C   . SER C 156 ? 1.4182 0.9094 1.1398 -0.0490 0.0969  0.0431  156 SER L C   
4895 O O   . SER C 156 ? 1.4668 0.9229 1.1624 -0.0453 0.0909  0.0554  156 SER L O   
4896 C CB  . SER C 156 ? 1.4497 0.9303 1.1501 -0.1153 0.0950  0.0506  156 SER L CB  
4897 O OG  . SER C 156 ? 1.5147 0.9329 1.1839 -0.1109 0.0869  0.0441  156 SER L OG  
4898 N N   . GLY C 157 ? 1.3989 0.9039 1.1382 -0.0232 0.0997  0.0317  157 GLY L N   
4899 C CA  . GLY C 157 ? 1.4225 0.8973 1.1486 0.0118  0.0963  0.0316  157 GLY L CA  
4900 C C   . GLY C 157 ? 1.3818 0.9027 1.1352 0.0350  0.0981  0.0371  157 GLY L C   
4901 O O   . GLY C 157 ? 1.4190 0.9197 1.1595 0.0603  0.0932  0.0452  157 GLY L O   
4902 N N   . ASN C 158 ? 1.3080 0.8897 1.0970 0.0265  0.1041  0.0333  158 ASN L N   
4903 C CA  . ASN C 158 ? 1.2560 0.8825 1.0691 0.0413  0.1040  0.0379  158 ASN L CA  
4904 C C   . ASN C 158 ? 1.1751 0.8515 1.0218 0.0402  0.1110  0.0272  158 ASN L C   
4905 O O   . ASN C 158 ? 1.1241 0.8391 0.9888 0.0367  0.1115  0.0292  158 ASN L O   
4906 C CB  . ASN C 158 ? 1.2684 0.9035 1.0747 0.0265  0.1005  0.0493  158 ASN L CB  
4907 C CG  . ASN C 158 ? 1.2632 0.9099 1.0701 -0.0037 0.1065  0.0462  158 ASN L CG  
4908 O OD1 . ASN C 158 ? 1.2531 0.9047 1.0684 -0.0143 0.1120  0.0366  158 ASN L OD1 
4909 N ND2 . ASN C 158 ? 1.2591 0.9137 1.0565 -0.0166 0.1055  0.0551  158 ASN L ND2 
4910 N N   . SER C 159 ? 1.1528 0.8233 1.0030 0.0426  0.1152  0.0164  159 SER L N   
4911 C CA  . SER C 159 ? 1.0926 0.8032 0.9700 0.0409  0.1212  0.0073  159 SER L CA  
4912 C C   . SER C 159 ? 1.0968 0.7969 0.9725 0.0554  0.1239  -0.0012 159 SER L C   
4913 O O   . SER C 159 ? 1.1347 0.7901 0.9839 0.0607  0.1216  -0.0034 159 SER L O   
4914 C CB  . SER C 159 ? 1.0625 0.7871 0.9468 0.0166  0.1250  0.0031  159 SER L CB  
4915 O OG  . SER C 159 ? 1.0772 0.7730 0.9450 0.0030  0.1242  0.0002  159 SER L OG  
4916 N N   . GLN C 160 ? 1.0552 0.7926 0.9543 0.0606  0.1284  -0.0062 160 GLN L N   
4917 C CA  . GLN C 160 ? 1.0559 0.7913 0.9541 0.0744  0.1324  -0.0139 160 GLN L CA  
4918 C C   . GLN C 160 ? 1.0079 0.7723 0.9246 0.0621  0.1362  -0.0205 160 GLN L C   
4919 O O   . GLN C 160 ? 0.9651 0.7612 0.9011 0.0544  0.1369  -0.0176 160 GLN L O   
4920 C CB  . GLN C 160 ? 1.0597 0.8163 0.9668 0.1013  0.1344  -0.0089 160 GLN L CB  
4921 C CG  . GLN C 160 ? 1.0956 0.8310 0.9881 0.1184  0.1298  0.0003  160 GLN L CG  
4922 C CD  . GLN C 160 ? 1.0948 0.8583 0.9982 0.1495  0.1328  0.0060  160 GLN L CD  
4923 O OE1 . GLN C 160 ? 1.0742 0.8795 0.9990 0.1539  0.1298  0.0172  160 GLN L OE1 
4924 N NE2 . GLN C 160 ? 1.1210 0.8648 1.0091 0.1712  0.1389  -0.0014 160 GLN L NE2 
4925 N N   . GLU C 161 ? 1.0222 0.7711 0.9286 0.0604  0.1376  -0.0291 161 GLU L N   
4926 C CA  . GLU C 161 ? 0.9987 0.7723 0.9196 0.0516  0.1402  -0.0341 161 GLU L CA  
4927 C C   . GLU C 161 ? 0.9801 0.7707 0.9057 0.0683  0.1450  -0.0363 161 GLU L C   
4928 O O   . GLU C 161 ? 1.0085 0.7887 0.9231 0.0878  0.1474  -0.0363 161 GLU L O   
4929 C CB  . GLU C 161 ? 1.0250 0.7778 0.9319 0.0362  0.1370  -0.0404 161 GLU L CB  
4930 C CG  . GLU C 161 ? 1.0353 0.7902 0.9458 0.0155  0.1342  -0.0368 161 GLU L CG  
4931 C CD  . GLU C 161 ? 1.0637 0.8149 0.9682 -0.0026 0.1303  -0.0405 161 GLU L CD  
4932 O OE1 . GLU C 161 ? 1.0786 0.8436 0.9908 -0.0195 0.1294  -0.0363 161 GLU L OE1 
4933 O OE2 . GLU C 161 ? 1.0745 0.8127 0.9663 -0.0002 0.1282  -0.0470 161 GLU L OE2 
4934 N N   . SER C 162 ? 0.9562 0.7733 0.8967 0.0616  0.1470  -0.0374 162 SER L N   
4935 C CA  . SER C 162 ? 0.9522 0.7866 0.8948 0.0722  0.1519  -0.0389 162 SER L CA  
4936 C C   . SER C 162 ? 0.9256 0.7729 0.8751 0.0597  0.1511  -0.0408 162 SER L C   
4937 O O   . SER C 162 ? 0.9090 0.7726 0.8735 0.0503  0.1498  -0.0365 162 SER L O   
4938 C CB  . SER C 162 ? 0.9427 0.8100 0.9020 0.0823  0.1553  -0.0304 162 SER L CB  
4939 O OG  . SER C 162 ? 0.9442 0.8337 0.9057 0.0909  0.1614  -0.0301 162 SER L OG  
4940 N N   . VAL C 163 ? 0.9431 0.7793 0.8775 0.0609  0.1513  -0.0474 163 VAL L N   
4941 C CA  . VAL C 163 ? 0.9471 0.7957 0.8857 0.0515  0.1494  -0.0479 163 VAL L CA  
4942 C C   . VAL C 163 ? 0.9691 0.8398 0.9105 0.0594  0.1550  -0.0444 163 VAL L C   
4943 O O   . VAL C 163 ? 0.9977 0.8710 0.9309 0.0734  0.1612  -0.0454 163 VAL L O   
4944 C CB  . VAL C 163 ? 0.9615 0.7891 0.8810 0.0438  0.1439  -0.0554 163 VAL L CB  
4945 C CG1 . VAL C 163 ? 1.0014 0.8091 0.8933 0.0548  0.1468  -0.0629 163 VAL L CG1 
4946 C CG2 . VAL C 163 ? 0.9389 0.7843 0.8678 0.0335  0.1393  -0.0531 163 VAL L CG2 
4947 N N   . THR C 164 ? 0.9693 0.8560 0.9205 0.0511  0.1534  -0.0394 164 THR L N   
4948 C CA  . THR C 164 ? 0.9713 0.8776 0.9222 0.0533  0.1576  -0.0340 164 THR L CA  
4949 C C   . THR C 164 ? 0.9963 0.8954 0.9272 0.0557  0.1577  -0.0396 164 THR L C   
4950 O O   . THR C 164 ? 1.0029 0.8828 0.9225 0.0517  0.1519  -0.0466 164 THR L O   
4951 C CB  . THR C 164 ? 0.9556 0.8713 0.9174 0.0424  0.1543  -0.0254 164 THR L CB  
4952 O OG1 . THR C 164 ? 0.9361 0.8394 0.8961 0.0377  0.1480  -0.0280 164 THR L OG1 
4953 C CG2 . THR C 164 ? 0.9441 0.8645 0.9190 0.0376  0.1535  -0.0204 164 THR L CG2 
4954 N N   . GLU C 165 ? 1.0208 0.9377 0.9460 0.0598  0.1639  -0.0353 165 GLU L N   
4955 C CA  . GLU C 165 ? 1.0581 0.9712 0.9621 0.0599  0.1636  -0.0386 165 GLU L CA  
4956 C C   . GLU C 165 ? 1.0370 0.9488 0.9454 0.0473  0.1541  -0.0333 165 GLU L C   
4957 O O   . GLU C 165 ? 1.0420 0.9557 0.9680 0.0415  0.1504  -0.0273 165 GLU L O   
4958 C CB  . GLU C 165 ? 1.0936 1.0314 0.9908 0.0675  0.1745  -0.0335 165 GLU L CB  
4959 C CG  . GLU C 165 ? 1.1050 1.0699 1.0191 0.0566  0.1755  -0.0183 165 GLU L CG  
4960 C CD  . GLU C 165 ? 1.1068 1.0885 1.0449 0.0537  0.1768  -0.0109 165 GLU L CD  
4961 O OE1 . GLU C 165 ? 1.1128 1.0879 1.0576 0.0628  0.1773  -0.0169 165 GLU L OE1 
4962 O OE2 . GLU C 165 ? 1.1071 1.1063 1.0543 0.0406  0.1759  0.0015  165 GLU L OE2 
4963 N N   . GLN C 166 ? 1.0334 0.9407 0.9228 0.0451  0.1500  -0.0355 166 GLN L N   
4964 C CA  . GLN C 166 ? 1.0187 0.9271 0.9111 0.0371  0.1399  -0.0295 166 GLN L CA  
4965 C C   . GLN C 166 ? 1.0235 0.9427 0.9210 0.0343  0.1417  -0.0160 166 GLN L C   
4966 O O   . GLN C 166 ? 1.0388 0.9696 0.9272 0.0348  0.1494  -0.0116 166 GLN L O   
4967 C CB  . GLN C 166 ? 1.0278 0.9304 0.8960 0.0344  0.1333  -0.0346 166 GLN L CB  
4968 C CG  . GLN C 166 ? 1.0204 0.9283 0.8956 0.0279  0.1202  -0.0291 166 GLN L CG  
4969 C CD  . GLN C 166 ? 1.0426 0.9472 0.8943 0.0213  0.1107  -0.0346 166 GLN L CD  
4970 O OE1 . GLN C 166 ? 1.0711 0.9633 0.8944 0.0220  0.1146  -0.0431 166 GLN L OE1 
4971 N NE2 . GLN C 166 ? 1.0422 0.9592 0.9038 0.0155  0.0979  -0.0295 166 GLN L NE2 
4972 N N   . ASP C 167 ? 1.0165 0.9307 0.9260 0.0314  0.1350  -0.0093 167 ASP L N   
4973 C CA  . ASP C 167 ? 1.0207 0.9321 0.9294 0.0269  0.1348  0.0033  167 ASP L CA  
4974 C C   . ASP C 167 ? 1.0423 0.9557 0.9311 0.0245  0.1317  0.0116  167 ASP L C   
4975 O O   . ASP C 167 ? 1.0394 0.9542 0.9190 0.0273  0.1254  0.0084  167 ASP L O   
4976 C CB  . ASP C 167 ? 1.0193 0.9153 0.9385 0.0287  0.1288  0.0061  167 ASP L CB  
4977 C CG  . ASP C 167 ? 1.0384 0.9191 0.9522 0.0218  0.1290  0.0165  167 ASP L CG  
4978 O OD1 . ASP C 167 ? 1.0358 0.9216 0.9552 0.0144  0.1343  0.0167  167 ASP L OD1 
4979 O OD2 . ASP C 167 ? 1.0611 0.9234 0.9631 0.0233  0.1226  0.0250  167 ASP L OD2 
4980 N N   . SER C 168 ? 1.0601 0.9744 0.9407 0.0165  0.1349  0.0236  168 SER L N   
4981 C CA  A SER C 168 ? 1.0927 1.0097 0.9512 0.0119  0.1334  0.0338  168 SER L CA  
4982 C CA  B SER C 168 ? 1.0886 1.0056 0.9472 0.0118  0.1335  0.0339  168 SER L CA  
4983 C C   . SER C 168 ? 1.1073 1.0027 0.9576 0.0141  0.1209  0.0429  168 SER L C   
4984 O O   . SER C 168 ? 1.1159 1.0125 0.9482 0.0146  0.1155  0.0489  168 SER L O   
4985 C CB  A SER C 168 ? 1.1127 1.0419 0.9655 -0.0004 0.1415  0.0456  168 SER L CB  
4986 C CB  B SER C 168 ? 1.1003 1.0292 0.9534 -0.0006 0.1415  0.0457  168 SER L CB  
4987 O OG  A SER C 168 ? 1.1320 1.0430 0.9905 -0.0102 0.1376  0.0542  168 SER L OG  
4988 O OG  B SER C 168 ? 1.1296 1.0636 0.9589 -0.0065 0.1415  0.0566  168 SER L OG  
4989 N N   . LYS C 169 ? 1.1200 0.9950 0.9810 0.0176  0.1165  0.0440  169 LYS L N   
4990 C CA  . LYS C 169 ? 1.1446 0.9956 0.9968 0.0255  0.1059  0.0532  169 LYS L CA  
4991 C C   . LYS C 169 ? 1.1159 0.9763 0.9852 0.0409  0.1002  0.0448  169 LYS L C   
4992 O O   . LYS C 169 ? 1.1152 0.9830 0.9797 0.0485  0.0913  0.0497  169 LYS L O   
4993 C CB  . LYS C 169 ? 1.1750 0.9918 1.0202 0.0207  0.1053  0.0601  169 LYS L CB  
4994 C CG  . LYS C 169 ? 1.2120 1.0217 1.0393 0.0000  0.1085  0.0723  169 LYS L CG  
4995 C CD  . LYS C 169 ? 1.2456 1.0190 1.0629 -0.0107 0.1064  0.0775  169 LYS L CD  
4996 C CE  . LYS C 169 ? 1.2794 1.0524 1.0800 -0.0372 0.1083  0.0921  169 LYS L CE  
4997 N NZ  . LYS C 169 ? 1.3147 1.0502 1.1025 -0.0530 0.1041  0.0963  169 LYS L NZ  
4998 N N   . ASP C 170 ? 1.0899 0.9542 0.9793 0.0438  0.1049  0.0338  170 ASP L N   
4999 C CA  . ASP C 170 ? 1.0749 0.9515 0.9826 0.0562  0.1010  0.0279  170 ASP L CA  
5000 C C   . ASP C 170 ? 1.0426 0.9482 0.9571 0.0521  0.0983  0.0204  170 ASP L C   
5001 O O   . ASP C 170 ? 1.0449 0.9690 0.9696 0.0586  0.0906  0.0213  170 ASP L O   
5002 C CB  . ASP C 170 ? 1.0742 0.9440 0.9968 0.0583  0.1076  0.0197  170 ASP L CB  
5003 C CG  . ASP C 170 ? 1.1212 0.9554 1.0315 0.0614  0.1086  0.0249  170 ASP L CG  
5004 O OD1 . ASP C 170 ? 1.1615 0.9725 1.0513 0.0621  0.1037  0.0360  170 ASP L OD1 
5005 O OD2 . ASP C 170 ? 1.1254 0.9511 1.0425 0.0620  0.1135  0.0180  170 ASP L OD2 
5006 N N   . SER C 171 ? 1.0181 0.9274 0.9251 0.0417  0.1044  0.0134  171 SER L N   
5007 C CA  . SER C 171 ? 1.0038 0.9270 0.9088 0.0364  0.1027  0.0032  171 SER L CA  
5008 C C   . SER C 171 ? 0.9842 0.9117 0.9086 0.0358  0.1046  -0.0061 171 SER L C   
5009 O O   . SER C 171 ? 0.9746 0.9114 0.8990 0.0298  0.0994  -0.0125 171 SER L O   
5010 C CB  . SER C 171 ? 1.0089 0.9456 0.9046 0.0356  0.0905  0.0074  171 SER L CB  
5011 O OG  . SER C 171 ? 1.0266 0.9576 0.9024 0.0364  0.0881  0.0182  171 SER L OG  
5012 N N   . THR C 172 ? 0.9785 0.8970 0.9154 0.0393  0.1114  -0.0063 172 THR L N   
5013 C CA  . THR C 172 ? 0.9715 0.8937 0.9252 0.0390  0.1139  -0.0129 172 THR L CA  
5014 C C   . THR C 172 ? 0.9659 0.8778 0.9172 0.0347  0.1222  -0.0202 172 THR L C   
5015 O O   . THR C 172 ? 0.9688 0.8759 0.9096 0.0340  0.1271  -0.0190 172 THR L O   
5016 C CB  . THR C 172 ? 0.9700 0.8893 0.9361 0.0486  0.1150  -0.0083 172 THR L CB  
5017 O OG1 . THR C 172 ? 0.9778 0.8751 0.9346 0.0490  0.1195  -0.0046 172 THR L OG1 
5018 C CG2 . THR C 172 ? 0.9786 0.9110 0.9490 0.0591  0.1073  -0.0003 172 THR L CG2 
5019 N N   . TYR C 173 ? 0.9592 0.8714 0.9206 0.0323  0.1238  -0.0261 173 TYR L N   
5020 C CA  . TYR C 173 ? 0.9471 0.8491 0.9070 0.0309  0.1303  -0.0316 173 TYR L CA  
5021 C C   . TYR C 173 ? 0.9215 0.8212 0.8946 0.0323  0.1338  -0.0301 173 TYR L C   
5022 O O   . TYR C 173 ? 0.9190 0.8240 0.9008 0.0349  0.1320  -0.0276 173 TYR L O   
5023 C CB  . TYR C 173 ? 0.9618 0.8567 0.9133 0.0252  0.1281  -0.0396 173 TYR L CB  
5024 C CG  . TYR C 173 ? 0.9911 0.8815 0.9219 0.0221  0.1235  -0.0436 173 TYR L CG  
5025 C CD1 . TYR C 173 ? 0.9970 0.9000 0.9271 0.0155  0.1139  -0.0412 173 TYR L CD1 
5026 C CD2 . TYR C 173 ? 1.0111 0.8865 0.9214 0.0270  0.1288  -0.0495 173 TYR L CD2 
5027 C CE1 . TYR C 173 ? 1.0261 0.9230 0.9324 0.0103  0.1081  -0.0452 173 TYR L CE1 
5028 C CE2 . TYR C 173 ? 1.0441 0.9104 0.9285 0.0249  0.1253  -0.0549 173 TYR L CE2 
5029 C CZ  . TYR C 173 ? 1.0539 0.9291 0.9347 0.0147  0.1142  -0.0530 173 TYR L CZ  
5030 O OH  . TYR C 173 ? 1.0989 0.9635 0.9495 0.0103  0.1091  -0.0587 173 TYR L OH  
5031 N N   . SER C 174 ? 0.9062 0.7996 0.8789 0.0322  0.1387  -0.0315 174 SER L N   
5032 C CA  . SER C 174 ? 0.8944 0.7839 0.8748 0.0313  0.1410  -0.0313 174 SER L CA  
5033 C C   . SER C 174 ? 0.9012 0.7854 0.8799 0.0305  0.1430  -0.0351 174 SER L C   
5034 O O   . SER C 174 ? 0.9213 0.8027 0.8918 0.0342  0.1445  -0.0372 174 SER L O   
5035 C CB  . SER C 174 ? 0.8885 0.7747 0.8679 0.0302  0.1423  -0.0258 174 SER L CB  
5036 O OG  . SER C 174 ? 0.9052 0.7853 0.8806 0.0320  0.1397  -0.0219 174 SER L OG  
5037 N N   . LEU C 175 ? 0.8970 0.7777 0.8802 0.0277  0.1435  -0.0357 175 LEU L N   
5038 C CA  . LEU C 175 ? 0.9030 0.7739 0.8818 0.0270  0.1441  -0.0374 175 LEU L CA  
5039 C C   . LEU C 175 ? 0.8913 0.7629 0.8740 0.0265  0.1455  -0.0339 175 LEU L C   
5040 O O   . LEU C 175 ? 0.8750 0.7494 0.8608 0.0241  0.1459  -0.0325 175 LEU L O   
5041 C CB  . LEU C 175 ? 0.9203 0.7860 0.8964 0.0190  0.1416  -0.0400 175 LEU L CB  
5042 C CG  . LEU C 175 ? 0.9380 0.7819 0.9004 0.0166  0.1401  -0.0418 175 LEU L CG  
5043 C CD1 . LEU C 175 ? 0.9594 0.7866 0.9047 0.0171  0.1371  -0.0472 175 LEU L CD1 
5044 C CD2 . LEU C 175 ? 0.9429 0.7852 0.9057 0.0043  0.1388  -0.0397 175 LEU L CD2 
5045 N N   . SER C 176 ? 0.9005 0.7671 0.8798 0.0300  0.1456  -0.0323 176 SER L N   
5046 C CA  . SER C 176 ? 0.9084 0.7775 0.8896 0.0283  0.1448  -0.0278 176 SER L CA  
5047 C C   . SER C 176 ? 0.9393 0.7948 0.9129 0.0306  0.1435  -0.0267 176 SER L C   
5048 O O   . SER C 176 ? 0.9585 0.8113 0.9287 0.0411  0.1433  -0.0248 176 SER L O   
5049 C CB  . SER C 176 ? 0.8996 0.7856 0.8869 0.0306  0.1443  -0.0223 176 SER L CB  
5050 O OG  . SER C 176 ? 0.8905 0.7811 0.8783 0.0255  0.1410  -0.0173 176 SER L OG  
5051 N N   . SER C 177 ? 0.9594 0.8061 0.9285 0.0221  0.1431  -0.0270 177 SER L N   
5052 C CA  . SER C 177 ? 0.9757 0.8059 0.9339 0.0208  0.1409  -0.0236 177 SER L CA  
5053 C C   . SER C 177 ? 0.9662 0.8039 0.9248 0.0204  0.1390  -0.0176 177 SER L C   
5054 O O   . SER C 177 ? 0.9566 0.8059 0.9191 0.0149  0.1398  -0.0184 177 SER L O   
5055 C CB  . SER C 177 ? 0.9918 0.8133 0.9438 0.0083  0.1416  -0.0248 177 SER L CB  
5056 O OG  . SER C 177 ? 1.0218 0.8173 0.9571 0.0056  0.1383  -0.0212 177 SER L OG  
5057 N N   . THR C 178 ? 0.9823 0.8100 0.9331 0.0266  0.1353  -0.0116 178 THR L N   
5058 C CA  . THR C 178 ? 0.9842 0.8232 0.9353 0.0267  0.1310  -0.0041 178 THR L CA  
5059 C C   . THR C 178 ? 1.0142 0.8326 0.9495 0.0269  0.1272  0.0025  178 THR L C   
5060 O O   . THR C 178 ? 1.0589 0.8625 0.9874 0.0402  0.1247  0.0065  178 THR L O   
5061 C CB  . THR C 178 ? 0.9776 0.8400 0.9413 0.0388  0.1285  0.0008  178 THR L CB  
5062 O OG1 . THR C 178 ? 0.9638 0.8408 0.9386 0.0370  0.1323  -0.0041 178 THR L OG1 
5063 C CG2 . THR C 178 ? 0.9716 0.8543 0.9382 0.0342  0.1217  0.0097  178 THR L CG2 
5064 N N   . LEU C 179 ? 1.0209 0.8360 0.9468 0.0135  0.1273  0.0039  179 LEU L N   
5065 C CA  . LEU C 179 ? 1.0500 0.8467 0.9580 0.0104  0.1233  0.0124  179 LEU L CA  
5066 C C   . LEU C 179 ? 1.0531 0.8638 0.9612 0.0168  0.1153  0.0217  179 LEU L C   
5067 O O   . LEU C 179 ? 1.0450 0.8757 0.9568 0.0090  0.1138  0.0208  179 LEU L O   
5068 C CB  . LEU C 179 ? 1.0550 0.8500 0.9527 -0.0067 0.1282  0.0109  179 LEU L CB  
5069 C CG  . LEU C 179 ? 1.0924 0.8676 0.9681 -0.0146 0.1252  0.0208  179 LEU L CG  
5070 C CD1 . LEU C 179 ? 1.1200 0.8688 0.9851 -0.0216 0.1262  0.0224  179 LEU L CD1 
5071 C CD2 . LEU C 179 ? 1.0971 0.8845 0.9628 -0.0279 0.1298  0.0208  179 LEU L CD2 
5072 N N   . THR C 180 ? 1.0789 0.8774 0.9804 0.0310  0.1094  0.0309  180 THR L N   
5073 C CA  . THR C 180 ? 1.0873 0.9068 0.9926 0.0400  0.1004  0.0424  180 THR L CA  
5074 C C   . THR C 180 ? 1.1280 0.9235 1.0097 0.0390  0.0937  0.0539  180 THR L C   
5075 O O   . THR C 180 ? 1.1514 0.9113 1.0171 0.0481  0.0932  0.0574  180 THR L O   
5076 C CB  . THR C 180 ? 1.0819 0.9182 1.0035 0.0643  0.0993  0.0459  180 THR L CB  
5077 O OG1 . THR C 180 ? 1.0458 0.8978 0.9842 0.0629  0.1067  0.0353  180 THR L OG1 
5078 C CG2 . THR C 180 ? 1.0814 0.9574 1.0158 0.0722  0.0898  0.0591  180 THR L CG2 
5079 N N   . LEU C 181 ? 1.1469 0.9580 1.0219 0.0266  0.0877  0.0597  181 LEU L N   
5080 C CA  . LEU C 181 ? 1.1965 0.9897 1.0472 0.0236  0.0802  0.0724  181 LEU L CA  
5081 C C   . LEU C 181 ? 1.2109 1.0371 1.0663 0.0268  0.0674  0.0841  181 LEU L C   
5082 O O   . LEU C 181 ? 1.1998 1.0621 1.0751 0.0240  0.0652  0.0809  181 LEU L O   
5083 C CB  . LEU C 181 ? 1.2084 0.9875 1.0391 0.0000  0.0868  0.0673  181 LEU L CB  
5084 C CG  . LEU C 181 ? 1.2193 0.9745 1.0465 -0.0075 0.0979  0.0590  181 LEU L CG  
5085 C CD1 . LEU C 181 ? 1.2273 0.9833 1.0389 -0.0289 0.1058  0.0560  181 LEU L CD1 
5086 C CD2 . LEU C 181 ? 1.2645 0.9800 1.0759 0.0009  0.0942  0.0675  181 LEU L CD2 
5087 N N   . SER C 182 ? 1.2589 1.0725 1.0943 0.0304  0.0577  0.0991  182 SER L N   
5088 C CA  . SER C 182 ? 1.2809 1.1265 1.1155 0.0280  0.0435  0.1118  182 SER L CA  
5089 C C   . SER C 182 ? 1.2870 1.1349 1.1023 -0.0006 0.0439  0.1051  182 SER L C   
5090 O O   . SER C 182 ? 1.2791 1.1027 1.0805 -0.0137 0.0561  0.0936  182 SER L O   
5091 C CB  . SER C 182 ? 1.3234 1.1531 1.1410 0.0442  0.0322  0.1313  182 SER L CB  
5092 O OG  . SER C 182 ? 1.3510 1.1346 1.1344 0.0315  0.0356  0.1332  182 SER L OG  
5093 N N   . LYS C 183 ? 1.3063 1.1846 1.1190 -0.0098 0.0305  0.1124  183 LYS L N   
5094 C CA  . LYS C 183 ? 1.3287 1.2032 1.1142 -0.0357 0.0294  0.1055  183 LYS L CA  
5095 C C   . LYS C 183 ? 1.3701 1.2132 1.1198 -0.0421 0.0309  0.1120  183 LYS L C   
5096 O O   . LYS C 183 ? 1.3808 1.2063 1.1070 -0.0582 0.0414  0.1010  183 LYS L O   
5097 C CB  . LYS C 183 ? 1.3399 1.2515 1.1263 -0.0472 0.0116  0.1130  183 LYS L CB  
5098 C CG  . LYS C 183 ? 1.3647 1.2649 1.1151 -0.0746 0.0095  0.1033  183 LYS L CG  
5099 C CD  . LYS C 183 ? 1.3706 1.3034 1.1203 -0.0922 -0.0088 0.1075  183 LYS L CD  
5100 C CE  . LYS C 183 ? 1.3924 1.3599 1.1464 -0.0878 -0.0301 0.1314  183 LYS L CE  
5101 N NZ  . LYS C 183 ? 1.4071 1.4109 1.1591 -0.1111 -0.0499 0.1363  183 LYS L NZ  
5102 N N   . ALA C 184 ? 1.4053 1.2418 1.1497 -0.0280 0.0209  0.1309  184 ALA L N   
5103 C CA  . ALA C 184 ? 1.4441 1.2477 1.1528 -0.0344 0.0210  0.1409  184 ALA L CA  
5104 C C   . ALA C 184 ? 1.4470 1.2189 1.1472 -0.0428 0.0403  0.1290  184 ALA L C   
5105 O O   . ALA C 184 ? 1.4744 1.2337 1.1458 -0.0609 0.0474  0.1272  184 ALA L O   
5106 C CB  . ALA C 184 ? 1.4722 1.2650 1.1789 -0.0124 0.0082  0.1626  184 ALA L CB  
5107 N N   . ASP C 185 ? 1.4298 1.1932 1.1550 -0.0300 0.0487  0.1216  185 ASP L N   
5108 C CA  . ASP C 185 ? 1.4284 1.1679 1.1502 -0.0387 0.0647  0.1119  185 ASP L CA  
5109 C C   . ASP C 185 ? 1.3856 1.1446 1.1156 -0.0518 0.0782  0.0928  185 ASP L C   
5110 O O   . ASP C 185 ? 1.3861 1.1373 1.1057 -0.0646 0.0913  0.0872  185 ASP L O   
5111 C CB  . ASP C 185 ? 1.4337 1.1541 1.1738 -0.0213 0.0669  0.1106  185 ASP L CB  
5112 C CG  . ASP C 185 ? 1.4899 1.1687 1.2073 -0.0112 0.0585  0.1276  185 ASP L CG  
5113 O OD1 . ASP C 185 ? 1.5239 1.2045 1.2310 0.0000  0.0449  0.1431  185 ASP L OD1 
5114 O OD2 . ASP C 185 ? 1.5108 1.1538 1.2188 -0.0151 0.0646  0.1258  185 ASP L OD2 
5115 N N   . TYR C 186 ? 1.3480 1.1329 1.0958 -0.0484 0.0746  0.0841  186 TYR L N   
5116 C CA  . TYR C 186 ? 1.3134 1.1088 1.0655 -0.0569 0.0858  0.0660  186 TYR L CA  
5117 C C   . TYR C 186 ? 1.3362 1.1285 1.0536 -0.0729 0.0897  0.0625  186 TYR L C   
5118 O O   . TYR C 186 ? 1.3205 1.1109 1.0312 -0.0780 0.1049  0.0498  186 TYR L O   
5119 C CB  . TYR C 186 ? 1.2737 1.0910 1.0483 -0.0520 0.0790  0.0600  186 TYR L CB  
5120 C CG  . TYR C 186 ? 1.2427 1.0613 1.0165 -0.0593 0.0887  0.0422  186 TYR L CG  
5121 C CD1 . TYR C 186 ? 1.2116 1.0247 0.9989 -0.0547 0.1036  0.0311  186 TYR L CD1 
5122 C CD2 . TYR C 186 ? 1.2470 1.0689 1.0027 -0.0711 0.0819  0.0368  186 TYR L CD2 
5123 C CE1 . TYR C 186 ? 1.1990 1.0105 0.9836 -0.0571 0.1123  0.0160  186 TYR L CE1 
5124 C CE2 . TYR C 186 ? 1.2398 1.0520 0.9876 -0.0755 0.0905  0.0204  186 TYR L CE2 
5125 C CZ  . TYR C 186 ? 1.2173 1.0244 0.9803 -0.0663 0.1062  0.0102  186 TYR L CZ  
5126 O OH  . TYR C 186 ? 1.2142 1.0095 0.9679 -0.0664 0.1145  -0.0048 186 TYR L OH  
5127 N N   . GLU C 187 ? 1.3722 1.1653 1.0661 -0.0790 0.0762  0.0741  187 GLU L N   
5128 C CA  . GLU C 187 ? 1.4203 1.2090 1.0750 -0.0941 0.0780  0.0702  187 GLU L CA  
5129 C C   . GLU C 187 ? 1.4594 1.2348 1.0904 -0.1012 0.0909  0.0752  187 GLU L C   
5130 O O   . GLU C 187 ? 1.4944 1.2675 1.0933 -0.1115 0.0999  0.0685  187 GLU L O   
5131 C CB  . GLU C 187 ? 1.4491 1.2461 1.0860 -0.1003 0.0567  0.0825  187 GLU L CB  
5132 C CG  . GLU C 187 ? 1.4365 1.2546 1.0946 -0.0996 0.0433  0.0792  187 GLU L CG  
5133 C CD  . GLU C 187 ? 1.4556 1.2673 1.0949 -0.1131 0.0467  0.0603  187 GLU L CD  
5134 O OE1 . GLU C 187 ? 1.4233 1.2354 1.0851 -0.1082 0.0544  0.0479  187 GLU L OE1 
5135 O OE2 . GLU C 187 ? 1.5195 1.3215 1.1173 -0.1283 0.0407  0.0582  187 GLU L OE2 
5136 N N   . LYS C 188 ? 1.4610 1.2265 1.1045 -0.0966 0.0919  0.0871  188 LYS L N   
5137 C CA  . LYS C 188 ? 1.4876 1.2414 1.1096 -0.1080 0.1024  0.0954  188 LYS L CA  
5138 C C   . LYS C 188 ? 1.4787 1.2452 1.1085 -0.1125 0.1246  0.0807  188 LYS L C   
5139 O O   . LYS C 188 ? 1.5133 1.2849 1.1194 -0.1246 0.1370  0.0829  188 LYS L O   
5140 C CB  . LYS C 188 ? 1.4972 1.2282 1.1264 -0.1038 0.0953  0.1117  188 LYS L CB  
5141 C CG  . LYS C 188 ? 1.5377 1.2521 1.1471 -0.0993 0.0759  0.1322  188 LYS L CG  
5142 C CD  . LYS C 188 ? 1.5556 1.2389 1.1714 -0.0873 0.0678  0.1455  188 LYS L CD  
5143 C CE  . LYS C 188 ? 1.5838 1.2393 1.1843 -0.1029 0.0778  0.1513  188 LYS L CE  
5144 N NZ  . LYS C 188 ? 1.6318 1.2795 1.1923 -0.1237 0.0795  0.1653  188 LYS L NZ  
5145 N N   . HIS C 189 ? 1.4491 1.2248 1.1125 -0.1020 0.1296  0.0672  189 HIS L N   
5146 C CA  . HIS C 189 ? 1.4394 1.2311 1.1171 -0.1028 0.1486  0.0561  189 HIS L CA  
5147 C C   . HIS C 189 ? 1.4247 1.2273 1.1024 -0.0943 0.1565  0.0369  189 HIS L C   
5148 O O   . HIS C 189 ? 1.4223 1.2174 1.0974 -0.0896 0.1451  0.0315  189 HIS L O   
5149 C CB  . HIS C 189 ? 1.4181 1.2069 1.1287 -0.0984 0.1479  0.0575  189 HIS L CB  
5150 C CG  . HIS C 189 ? 1.4502 1.2156 1.1520 -0.1067 0.1396  0.0752  189 HIS L CG  
5151 N ND1 . HIS C 189 ? 1.4700 1.2117 1.1615 -0.1002 0.1225  0.0870  189 HIS L ND1 
5152 C CD2 . HIS C 189 ? 1.4674 1.2265 1.1662 -0.1211 0.1449  0.0840  189 HIS L CD2 
5153 C CE1 . HIS C 189 ? 1.5044 1.2186 1.1832 -0.1078 0.1182  0.1015  189 HIS L CE1 
5154 N NE2 . HIS C 189 ? 1.5048 1.2273 1.1866 -0.1233 0.1311  0.0998  189 HIS L NE2 
5155 N N   . LYS C 190 ? 1.4093 1.2298 1.0889 -0.0925 0.1758  0.0276  190 LYS L N   
5156 C CA  . LYS C 190 ? 1.3957 1.2192 1.0645 -0.0819 0.1859  0.0095  190 LYS L CA  
5157 C C   . LYS C 190 ? 1.3275 1.1616 1.0317 -0.0685 0.1919  -0.0007 190 LYS L C   
5158 O O   . LYS C 190 ? 1.3014 1.1220 1.0104 -0.0600 0.1850  -0.0106 190 LYS L O   
5159 C CB  . LYS C 190 ? 1.4470 1.2849 1.0864 -0.0840 0.2051  0.0069  190 LYS L CB  
5160 C CG  . LYS C 190 ? 1.4897 1.3162 1.0978 -0.0720 0.2140  -0.0117 190 LYS L CG  
5161 C CD  . LYS C 190 ? 1.5439 1.3400 1.1104 -0.0806 0.1991  -0.0134 190 LYS L CD  
5162 C CE  . LYS C 190 ? 1.5943 1.3701 1.1157 -0.0718 0.2090  -0.0325 190 LYS L CE  
5163 N NZ  . LYS C 190 ? 1.6366 1.3847 1.1110 -0.0860 0.1935  -0.0323 190 LYS L NZ  
5164 N N   . VAL C 191 ? 1.2917 1.1512 1.0190 -0.0690 0.2036  0.0032  191 VAL L N   
5165 C CA  . VAL C 191 ? 1.2506 1.1268 1.0092 -0.0562 0.2107  -0.0053 191 VAL L CA  
5166 C C   . VAL C 191 ? 1.2066 1.0744 0.9951 -0.0584 0.1968  -0.0002 191 VAL L C   
5167 O O   . VAL C 191 ? 1.2262 1.0910 1.0196 -0.0708 0.1907  0.0121  191 VAL L O   
5168 C CB  . VAL C 191 ? 1.2520 1.1686 1.0222 -0.0568 0.2294  -0.0023 191 VAL L CB  
5169 C CG1 . VAL C 191 ? 1.2161 1.1550 1.0224 -0.0448 0.2337  -0.0077 191 VAL L CG1 
5170 C CG2 . VAL C 191 ? 1.2921 1.2208 1.0318 -0.0489 0.2468  -0.0089 191 VAL L CG2 
5171 N N   . TYR C 192 ? 1.1586 1.0189 0.9623 -0.0460 0.1922  -0.0100 192 TYR L N   
5172 C CA  . TYR C 192 ? 1.1065 0.9628 0.9377 -0.0446 0.1822  -0.0075 192 TYR L CA  
5173 C C   . TYR C 192 ? 1.0762 0.9501 0.9309 -0.0336 0.1899  -0.0156 192 TYR L C   
5174 O O   . TYR C 192 ? 1.0945 0.9679 0.9429 -0.0213 0.1962  -0.0258 192 TYR L O   
5175 C CB  . TYR C 192 ? 1.0935 0.9287 0.9215 -0.0418 0.1676  -0.0082 192 TYR L CB  
5176 C CG  . TYR C 192 ? 1.1118 0.9346 0.9213 -0.0504 0.1572  0.0024  192 TYR L CG  
5177 C CD1 . TYR C 192 ? 1.1388 0.9565 0.9174 -0.0565 0.1582  0.0026  192 TYR L CD1 
5178 C CD2 . TYR C 192 ? 1.1126 0.9269 0.9319 -0.0507 0.1463  0.0128  192 TYR L CD2 
5179 C CE1 . TYR C 192 ? 1.1660 0.9742 0.9267 -0.0643 0.1471  0.0143  192 TYR L CE1 
5180 C CE2 . TYR C 192 ? 1.1370 0.9401 0.9391 -0.0550 0.1360  0.0245  192 TYR L CE2 
5181 C CZ  . TYR C 192 ? 1.1638 0.9658 0.9378 -0.0628 0.1357  0.0262  192 TYR L CZ  
5182 O OH  . TYR C 192 ? 1.1896 0.9823 0.9457 -0.0669 0.1240  0.0395  192 TYR L OH  
5183 N N   . ALA C 193 ? 1.0553 0.9407 0.9329 -0.0381 0.1881  -0.0106 193 ALA L N   
5184 C CA  . ALA C 193 ? 1.0519 0.9602 0.9529 -0.0298 0.1940  -0.0154 193 ALA L CA  
5185 C C   . ALA C 193 ? 1.0467 0.9493 0.9661 -0.0346 0.1841  -0.0124 193 ALA L C   
5186 O O   . ALA C 193 ? 1.0640 0.9467 0.9766 -0.0446 0.1756  -0.0058 193 ALA L O   
5187 C CB  . ALA C 193 ? 1.0537 0.9993 0.9598 -0.0336 0.2076  -0.0116 193 ALA L CB  
5188 N N   . CYS C 194 ? 1.0324 0.9493 0.9711 -0.0256 0.1852  -0.0174 194 CYS L N   
5189 C CA  . CYS C 194 ? 1.0334 0.9481 0.9863 -0.0308 0.1772  -0.0156 194 CYS L CA  
5190 C C   . CYS C 194 ? 1.0172 0.9681 0.9909 -0.0291 0.1821  -0.0158 194 CYS L C   
5191 O O   . CYS C 194 ? 0.9977 0.9622 0.9790 -0.0125 0.1875  -0.0211 194 CYS L O   
5192 C CB  . CYS C 194 ? 1.0335 0.9247 0.9872 -0.0208 0.1690  -0.0205 194 CYS L CB  
5193 S SG  . CYS C 194 ? 1.0461 0.9418 1.0051 -0.0029 0.1726  -0.0290 194 CYS L SG  
5194 N N   . GLU C 195 ? 1.0307 0.9954 1.0108 -0.0471 0.1789  -0.0088 195 GLU L N   
5195 C CA  . GLU C 195 ? 1.0223 1.0295 1.0242 -0.0503 0.1810  -0.0059 195 GLU L CA  
5196 C C   . GLU C 195 ? 1.0030 0.9974 1.0111 -0.0504 0.1699  -0.0093 195 GLU L C   
5197 O O   . GLU C 195 ? 1.0153 0.9721 1.0088 -0.0587 0.1609  -0.0103 195 GLU L O   
5198 C CB  . GLU C 195 ? 1.0462 1.0795 1.0495 -0.0758 0.1826  0.0052  195 GLU L CB  
5199 C CG  . GLU C 195 ? 1.0527 1.1456 1.0827 -0.0809 0.1853  0.0111  195 GLU L CG  
5200 C CD  . GLU C 195 ? 1.0896 1.2186 1.1229 -0.1097 0.1880  0.0246  195 GLU L CD  
5201 O OE1 . GLU C 195 ? 1.1060 1.2490 1.1324 -0.1097 0.1998  0.0287  195 GLU L OE1 
5202 O OE2 . GLU C 195 ? 1.1179 1.2605 1.1578 -0.1342 0.1779  0.0315  195 GLU L OE2 
5203 N N   . VAL C 196 ? 0.9793 1.0049 1.0067 -0.0390 0.1709  -0.0106 196 VAL L N   
5204 C CA  . VAL C 196 ? 0.9707 0.9857 1.0017 -0.0357 0.1614  -0.0143 196 VAL L CA  
5205 C C   . VAL C 196 ? 0.9735 1.0343 1.0242 -0.0450 0.1575  -0.0081 196 VAL L C   
5206 O O   . VAL C 196 ? 0.9677 1.0725 1.0378 -0.0317 0.1644  -0.0048 196 VAL L O   
5207 C CB  . VAL C 196 ? 0.9549 0.9560 0.9856 -0.0108 0.1639  -0.0211 196 VAL L CB  
5208 C CG1 . VAL C 196 ? 0.9464 0.9445 0.9815 -0.0069 0.1554  -0.0230 196 VAL L CG1 
5209 C CG2 . VAL C 196 ? 0.9539 0.9151 0.9663 -0.0063 0.1648  -0.0256 196 VAL L CG2 
5210 N N   . THR C 197 ? 0.9987 1.0479 1.0420 -0.0669 0.1457  -0.0065 197 THR L N   
5211 C CA  . THR C 197 ? 1.0122 1.1027 1.0711 -0.0809 0.1378  -0.0003 197 THR L CA  
5212 C C   . THR C 197 ? 1.0205 1.0947 1.0752 -0.0723 0.1284  -0.0061 197 THR L C   
5213 O O   . THR C 197 ? 1.0227 1.0465 1.0554 -0.0688 0.1252  -0.0141 197 THR L O   
5214 C CB  . THR C 197 ? 1.0398 1.1272 1.0871 -0.1176 0.1293  0.0064  197 THR L CB  
5215 O OG1 . THR C 197 ? 1.0430 1.1426 1.0910 -0.1254 0.1390  0.0128  197 THR L OG1 
5216 C CG2 . THR C 197 ? 1.0476 1.1859 1.1120 -0.1380 0.1194  0.0149  197 THR L CG2 
5217 N N   . HIS C 198 ? 1.0298 1.1512 1.1058 -0.0677 0.1246  -0.0009 198 HIS L N   
5218 C CA  . HIS C 198 ? 1.0406 1.1532 1.1127 -0.0595 0.1156  -0.0044 198 HIS L CA  
5219 C C   . HIS C 198 ? 1.0490 1.2242 1.1454 -0.0644 0.1078  0.0056  198 HIS L C   
5220 O O   . HIS C 198 ? 1.0665 1.2967 1.1881 -0.0638 0.1135  0.0149  198 HIS L O   
5221 C CB  . HIS C 198 ? 1.0379 1.1280 1.1079 -0.0283 0.1233  -0.0101 198 HIS L CB  
5222 C CG  . HIS C 198 ? 1.0514 1.1186 1.1088 -0.0226 0.1154  -0.0142 198 HIS L CG  
5223 N ND1 . HIS C 198 ? 1.0510 1.1418 1.1194 -0.0067 0.1120  -0.0098 198 HIS L ND1 
5224 C CD2 . HIS C 198 ? 1.0683 1.0924 1.1012 -0.0295 0.1106  -0.0215 198 HIS L CD2 
5225 C CE1 . HIS C 198 ? 1.0650 1.1278 1.1152 -0.0071 0.1054  -0.0140 198 HIS L CE1 
5226 N NE2 . HIS C 198 ? 1.0757 1.0996 1.1047 -0.0200 0.1054  -0.0217 198 HIS L NE2 
5227 N N   . GLN C 199 ? 1.0629 1.2333 1.1512 -0.0686 0.0950  0.0046  199 GLN L N   
5228 C CA  . GLN C 199 ? 1.0678 1.2984 1.1776 -0.0742 0.0843  0.0153  199 GLN L CA  
5229 C C   . GLN C 199 ? 1.0416 1.3197 1.1816 -0.0400 0.0935  0.0228  199 GLN L C   
5230 O O   . GLN C 199 ? 1.0372 1.3842 1.2070 -0.0403 0.0934  0.0349  199 GLN L O   
5231 C CB  . GLN C 199 ? 1.0921 1.3005 1.1814 -0.0806 0.0694  0.0115  199 GLN L CB  
5232 C CG  . GLN C 199 ? 1.1339 1.3087 1.1924 -0.1175 0.0563  0.0063  199 GLN L CG  
5233 C CD  . GLN C 199 ? 1.1620 1.3310 1.2019 -0.1258 0.0402  0.0046  199 GLN L CD  
5234 O OE1 . GLN C 199 ? 1.1479 1.3729 1.2088 -0.1262 0.0304  0.0154  199 GLN L OE1 
5235 N NE2 . GLN C 199 ? 1.1937 1.2965 1.1926 -0.1308 0.0376  -0.0085 199 GLN L NE2 
5236 N N   . GLY C 200 ? 1.0229 1.2630 1.1529 -0.0105 0.1011  0.0162  200 GLY L N   
5237 C CA  . GLY C 200 ? 1.0079 1.2729 1.1550 0.0251  0.1090  0.0214  200 GLY L CA  
5238 C C   . GLY C 200 ? 0.9877 1.2882 1.1541 0.0376  0.1241  0.0249  200 GLY L C   
5239 O O   . GLY C 200 ? 0.9935 1.3387 1.1808 0.0643  0.1293  0.0328  200 GLY L O   
5240 N N   . LEU C 201 ? 0.9766 1.2562 1.1336 0.0205  0.1316  0.0194  201 LEU L N   
5241 C CA  . LEU C 201 ? 0.9750 1.2851 1.1447 0.0289  0.1470  0.0221  201 LEU L CA  
5242 C C   . LEU C 201 ? 0.9747 1.3648 1.1742 0.0100  0.1443  0.0360  201 LEU L C   
5243 O O   . LEU C 201 ? 0.9743 1.3709 1.1720 -0.0261 0.1313  0.0398  201 LEU L O   
5244 C CB  . LEU C 201 ? 0.9689 1.2273 1.1150 0.0143  0.1535  0.0132  201 LEU L CB  
5245 C CG  . LEU C 201 ? 0.9700 1.1588 1.0896 0.0299  0.1564  0.0014  201 LEU L CG  
5246 C CD1 . LEU C 201 ? 0.9736 1.1234 1.0739 0.0151  0.1613  -0.0045 201 LEU L CD1 
5247 C CD2 . LEU C 201 ? 0.9803 1.1668 1.0995 0.0662  0.1665  -0.0005 201 LEU L CD2 
5248 N N   . SER C 202 ? 0.9737 1.4241 1.1984 0.0348  0.1570  0.0439  202 SER L N   
5249 C CA  A SER C 202 ? 0.9749 1.5149 1.2328 0.0191  0.1578  0.0594  202 SER L CA  
5250 C CA  B SER C 202 ? 0.9761 1.5161 1.2340 0.0190  0.1578  0.0594  202 SER L CA  
5251 C C   . SER C 202 ? 0.9801 1.5186 1.2306 -0.0096 0.1664  0.0598  202 SER L C   
5252 O O   . SER C 202 ? 0.9836 1.5789 1.2519 -0.0422 0.1619  0.0726  202 SER L O   
5253 C CB  A SER C 202 ? 0.9753 1.5830 1.2622 0.0609  0.1704  0.0679  202 SER L CB  
5254 C CB  B SER C 202 ? 0.9783 1.5862 1.2652 0.0608  0.1703  0.0680  202 SER L CB  
5255 O OG  A SER C 202 ? 0.9753 1.5833 1.2672 0.0865  0.1603  0.0701  202 SER L OG  
5256 O OG  B SER C 202 ? 0.9882 1.5633 1.2587 0.0938  0.1906  0.0580  202 SER L OG  
5257 N N   . SER C 203 ? 0.9788 1.4525 1.2012 0.0007  0.1776  0.0471  203 SER L N   
5258 C CA  . SER C 203 ? 0.9811 1.4400 1.1894 -0.0242 0.1848  0.0470  203 SER L CA  
5259 C C   . SER C 203 ? 0.9755 1.3435 1.1468 -0.0177 0.1870  0.0315  203 SER L C   
5260 O O   . SER C 203 ? 0.9653 1.2952 1.1259 0.0113  0.1885  0.0218  203 SER L O   
5261 C CB  . SER C 203 ? 0.9868 1.5123 1.2142 -0.0109 0.2045  0.0552  203 SER L CB  
5262 O OG  . SER C 203 ? 0.9854 1.4990 1.2073 0.0365  0.2197  0.0463  203 SER L OG  
5263 N N   . PRO C 204 ? 0.9802 1.3117 1.1302 -0.0454 0.1859  0.0304  204 PRO L N   
5264 C CA  . PRO C 204 ? 0.9772 1.2309 1.0952 -0.0398 0.1865  0.0181  204 PRO L CA  
5265 C C   . PRO C 204 ? 0.9747 1.2121 1.0835 -0.0051 0.2009  0.0095  204 PRO L C   
5266 O O   . PRO C 204 ? 0.9767 1.2555 1.0942 0.0091  0.2157  0.0128  204 PRO L O   
5267 C CB  . PRO C 204 ? 0.9896 1.2288 1.0917 -0.0716 0.1864  0.0234  204 PRO L CB  
5268 C CG  . PRO C 204 ? 0.9996 1.2854 1.1180 -0.1045 0.1771  0.0364  204 PRO L CG  
5269 C CD  . PRO C 204 ? 0.9901 1.3529 1.1444 -0.0850 0.1824  0.0427  204 PRO L CD  
5270 N N   . VAL C 205 ? 0.9798 1.1565 1.0682 0.0072  0.1964  -0.0012 205 VAL L N   
5271 C CA  . VAL C 205 ? 0.9926 1.1398 1.0640 0.0344  0.2061  -0.0104 205 VAL L CA  
5272 C C   . VAL C 205 ? 1.0038 1.1045 1.0487 0.0223  0.2066  -0.0151 205 VAL L C   
5273 O O   . VAL C 205 ? 1.0038 1.0733 1.0407 0.0039  0.1958  -0.0151 205 VAL L O   
5274 C CB  . VAL C 205 ? 0.9864 1.1029 1.0535 0.0543  0.1995  -0.0166 205 VAL L CB  
5275 C CG1 . VAL C 205 ? 1.0011 1.0714 1.0417 0.0742  0.2057  -0.0263 205 VAL L CG1 
5276 C CG2 . VAL C 205 ? 0.9852 1.1475 1.0762 0.0713  0.1990  -0.0107 205 VAL L CG2 
5277 N N   . THR C 206 ? 1.0269 1.1228 1.0560 0.0349  0.2190  -0.0191 206 THR L N   
5278 C CA  . THR C 206 ? 1.0473 1.1056 1.0503 0.0238  0.2192  -0.0220 206 THR L CA  
5279 C C   . THR C 206 ? 1.0700 1.0884 1.0472 0.0441  0.2229  -0.0329 206 THR L C   
5280 O O   . THR C 206 ? 1.1232 1.1519 1.0929 0.0658  0.2351  -0.0374 206 THR L O   
5281 C CB  . THR C 206 ? 1.0635 1.1534 1.0643 0.0106  0.2295  -0.0145 206 THR L CB  
5282 O OG1 . THR C 206 ? 1.0594 1.1858 1.0821 -0.0120 0.2247  -0.0032 206 THR L OG1 
5283 C CG2 . THR C 206 ? 1.0697 1.1213 1.0423 -0.0027 0.2275  -0.0151 206 THR L CG2 
5284 N N   . LYS C 207 ? 1.0596 1.0325 1.0217 0.0369  0.2120  -0.0367 207 LYS L N   
5285 C CA  . LYS C 207 ? 1.0755 1.0076 1.0076 0.0445  0.2121  -0.0450 207 LYS L CA  
5286 C C   . LYS C 207 ? 1.0595 0.9790 0.9738 0.0274  0.2104  -0.0424 207 LYS L C   
5287 O O   . LYS C 207 ? 1.0421 0.9651 0.9660 0.0104  0.2031  -0.0349 207 LYS L O   
5288 C CB  . LYS C 207 ? 1.0879 0.9867 1.0172 0.0462  0.2004  -0.0484 207 LYS L CB  
5289 C CG  . LYS C 207 ? 1.1260 1.0078 1.0455 0.0673  0.2032  -0.0548 207 LYS L CG  
5290 C CD  . LYS C 207 ? 1.1346 1.0523 1.0771 0.0842  0.2094  -0.0520 207 LYS L CD  
5291 C CE  . LYS C 207 ? 1.1760 1.0701 1.1016 0.1103  0.2133  -0.0579 207 LYS L CE  
5292 N NZ  . LYS C 207 ? 1.1768 1.1115 1.1279 0.1293  0.2178  -0.0528 207 LYS L NZ  
5293 N N   . SER C 208 ? 1.0783 0.9795 0.9626 0.0329  0.2167  -0.0485 208 SER L N   
5294 C CA  . SER C 208 ? 1.0850 0.9782 0.9493 0.0178  0.2157  -0.0450 208 SER L CA  
5295 C C   . SER C 208 ? 1.1107 0.9678 0.9355 0.0224  0.2159  -0.0543 208 SER L C   
5296 O O   . SER C 208 ? 1.1114 0.9487 0.9210 0.0386  0.2198  -0.0644 208 SER L O   
5297 C CB  . SER C 208 ? 1.0879 1.0192 0.9581 0.0126  0.2280  -0.0379 208 SER L CB  
5298 O OG  . SER C 208 ? 1.1110 1.0611 0.9727 0.0323  0.2449  -0.0444 208 SER L OG  
5299 N N   . PHE C 209 ? 1.1262 0.9716 0.9309 0.0071  0.2105  -0.0504 209 PHE L N   
5300 C CA  . PHE C 209 ? 1.1652 0.9771 0.9278 0.0057  0.2082  -0.0582 209 PHE L CA  
5301 C C   . PHE C 209 ? 1.1718 0.9877 0.9154 -0.0095 0.2070  -0.0508 209 PHE L C   
5302 O O   . PHE C 209 ? 1.1344 0.9726 0.8976 -0.0199 0.2058  -0.0386 209 PHE L O   
5303 C CB  . PHE C 209 ? 1.1696 0.9501 0.9267 -0.0010 0.1912  -0.0605 209 PHE L CB  
5304 C CG  . PHE C 209 ? 1.1490 0.9382 0.9268 -0.0165 0.1759  -0.0484 209 PHE L CG  
5305 C CD1 . PHE C 209 ? 1.1164 0.9247 0.9316 -0.0149 0.1732  -0.0419 209 PHE L CD1 
5306 C CD2 . PHE C 209 ? 1.1692 0.9477 0.9267 -0.0307 0.1644  -0.0435 209 PHE L CD2 
5307 C CE1 . PHE C 209 ? 1.1024 0.9155 0.9325 -0.0237 0.1610  -0.0318 209 PHE L CE1 
5308 C CE2 . PHE C 209 ? 1.1489 0.9385 0.9262 -0.0394 0.1512  -0.0313 209 PHE L CE2 
5309 C CZ  . PHE C 209 ? 1.1166 0.9219 0.9293 -0.0341 0.1505  -0.0261 209 PHE L CZ  
5310 N N   . ASN C 210 ? 1.2201 1.0092 0.9204 -0.0118 0.2066  -0.0581 210 ASN L N   
5311 C CA  . ASN C 210 ? 1.2513 1.0377 0.9261 -0.0274 0.2020  -0.0510 210 ASN L CA  
5312 C C   . ASN C 210 ? 1.2733 1.0300 0.9286 -0.0405 0.1814  -0.0511 210 ASN L C   
5313 O O   . ASN C 210 ? 1.3037 1.0390 0.9570 -0.0379 0.1744  -0.0590 210 ASN L O   
5314 C CB  . ASN C 210 ? 1.3007 1.0860 0.9359 -0.0207 0.2193  -0.0587 210 ASN L CB  
5315 C CG  . ASN C 210 ? 1.2852 1.1092 0.9409 -0.0057 0.2413  -0.0585 210 ASN L CG  
5316 O OD1 . ASN C 210 ? 1.2529 1.1046 0.9522 -0.0040 0.2418  -0.0515 210 ASN L OD1 
5317 N ND2 . ASN C 210 ? 1.3187 1.1481 0.9421 0.0049  0.2597  -0.0657 210 ASN L ND2 
5318 N N   . ARG C 211 ? 1.2904 1.0479 0.9306 -0.0559 0.1711  -0.0407 211 ARG L N   
5319 C CA  . ARG C 211 ? 1.3138 1.0514 0.9323 -0.0700 0.1511  -0.0393 211 ARG L CA  
5320 C C   . ARG C 211 ? 1.3835 1.0880 0.9449 -0.0725 0.1546  -0.0540 211 ARG L C   
5321 O O   . ARG C 211 ? 1.4265 1.1302 0.9556 -0.0749 0.1625  -0.0541 211 ARG L O   
5322 C CB  . ARG C 211 ? 1.3119 1.0642 0.9344 -0.0828 0.1375  -0.0213 211 ARG L CB  
5323 C CG  . ARG C 211 ? 1.2687 1.0442 0.9353 -0.0780 0.1370  -0.0076 211 ARG L CG  
5324 C CD  . ARG C 211 ? 1.2736 1.0557 0.9441 -0.0858 0.1191  0.0100  211 ARG L CD  
5325 N NE  . ARG C 211 ? 1.3247 1.0988 0.9542 -0.0980 0.1118  0.0150  211 ARG L NE  
5326 C CZ  . ARG C 211 ? 1.3540 1.1247 0.9550 -0.1023 0.1227  0.0169  211 ARG L CZ  
5327 N NH1 . ARG C 211 ? 1.3461 1.1251 0.9583 -0.0965 0.1414  0.0153  211 ARG L NH1 
5328 N NH2 . ARG C 211 ? 1.3955 1.1579 0.9560 -0.1140 0.1143  0.0215  211 ARG L NH2 
5329 N N   . GLY C 212 ? 1.3991 1.0724 0.9437 -0.0724 0.1489  -0.0663 212 GLY L N   
5330 C CA  . GLY C 212 ? 1.4570 1.0855 0.9395 -0.0741 0.1511  -0.0828 212 GLY L CA  
5331 C C   . GLY C 212 ? 1.4723 1.0622 0.9428 -0.0679 0.1496  -0.0964 212 GLY L C   
5332 O O   . GLY C 212 ? 1.4297 1.0279 0.9279 -0.0465 0.1639  -0.1003 212 GLY L O   
# 
