data_8Y4Y
# 
_entry.id   8Y4Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Y4Y         pdb_00008y4y 10.2210/pdb8y4y/pdb 
WWPDB D_1300044878 ?            ?                   
# 
_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       2025-02-05 
# 
_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                        8Y4Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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                 2 
_pdbx_contact_author.email              aknagata@mail.ecc.u-tokyo.ac.jp 
_pdbx_contact_author.name_first         Koji 
_pdbx_contact_author.name_last          Nagata 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4704-0603 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jiang, J.Y.' 1 0000-0001-6963-7200 
'Lu, P.'      2 0000-0002-1405-5294 
'Nagata, K.'  3 0000-0002-4704-0603 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of ferric iron-binding protein (FecB) from Vibrio alginolyticus in complex with ferric citrate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiang, J.Y.' 1 0000-0001-6963-7200 
primary 'Lu, P.'      2 0000-0002-1405-5294 
primary 'Nagata, K.'  3 0000-0002-4704-0603 
# 
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 'ABC transporter substrate-binding protein' 30240.568 1  ? ? ? ? 
2 non-polymer syn GLYCEROL                                    92.094    3  ? ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                     106.120   1  ? ? ? ? 
4 non-polymer syn 'CITRATE ANION'                             189.100   2  ? ? ? ? 
5 non-polymer syn 'FE (III) ION'                              55.845    1  ? ? ? ? 
6 water       nat water                                       18.015    15 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;RSVQDEQGTFELEAIPQRIVVLEFSFVDALAAVDVSPVGVADDNDATRVIPAVRDKIEPWQSVGMRSQPSLEAIAVLKPD
LIIADAERHRAIYQDLQRIAPTLLLKSRGETYKENLESAQKIGVAIGKQAQMTQRIEQHKQTMAEFKQHFATQETIQFGV
VSDKGMWLHSPVSYAGGVLSTLGIQSPLAPSEQKAYIPTSFELLLKTNPDWLLVGLYSQPNIVDEWRKNPLFKLLTAAKK
QQLVEVSPELWSLNRGMLAAEEIARNLEALL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSVQDEQGTFELEAIPQRIVVLEFSFVDALAAVDVSPVGVADDNDATRVIPAVRDKIEPWQSVGMRSQPSLEAIAVLKPD
LIIADAERHRAIYQDLQRIAPTLLLKSRGETYKENLESAQKIGVAIGKQAQMTQRIEQHKQTMAEFKQHFATQETIQFGV
VSDKGMWLHSPVSYAGGVLSTLGIQSPLAPSEQKAYIPTSFELLLKTNPDWLLVGLYSQPNIVDEWRKNPLFKLLTAAKK
QQLVEVSPELWSLNRGMLAAEEIARNLEALL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL                GOL 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 'CITRATE ANION'         FLC 
5 'FE (III) ION'          FE  
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   SER n 
1 3   VAL n 
1 4   GLN n 
1 5   ASP n 
1 6   GLU n 
1 7   GLN n 
1 8   GLY n 
1 9   THR n 
1 10  PHE n 
1 11  GLU n 
1 12  LEU n 
1 13  GLU n 
1 14  ALA n 
1 15  ILE n 
1 16  PRO n 
1 17  GLN n 
1 18  ARG n 
1 19  ILE n 
1 20  VAL n 
1 21  VAL n 
1 22  LEU n 
1 23  GLU n 
1 24  PHE n 
1 25  SER n 
1 26  PHE n 
1 27  VAL n 
1 28  ASP n 
1 29  ALA n 
1 30  LEU n 
1 31  ALA n 
1 32  ALA n 
1 33  VAL n 
1 34  ASP n 
1 35  VAL n 
1 36  SER n 
1 37  PRO n 
1 38  VAL n 
1 39  GLY n 
1 40  VAL n 
1 41  ALA n 
1 42  ASP n 
1 43  ASP n 
1 44  ASN n 
1 45  ASP n 
1 46  ALA n 
1 47  THR n 
1 48  ARG n 
1 49  VAL n 
1 50  ILE n 
1 51  PRO n 
1 52  ALA n 
1 53  VAL n 
1 54  ARG n 
1 55  ASP n 
1 56  LYS n 
1 57  ILE n 
1 58  GLU n 
1 59  PRO n 
1 60  TRP n 
1 61  GLN n 
1 62  SER n 
1 63  VAL n 
1 64  GLY n 
1 65  MET n 
1 66  ARG n 
1 67  SER n 
1 68  GLN n 
1 69  PRO n 
1 70  SER n 
1 71  LEU n 
1 72  GLU n 
1 73  ALA n 
1 74  ILE n 
1 75  ALA n 
1 76  VAL n 
1 77  LEU n 
1 78  LYS n 
1 79  PRO n 
1 80  ASP n 
1 81  LEU n 
1 82  ILE n 
1 83  ILE n 
1 84  ALA n 
1 85  ASP n 
1 86  ALA n 
1 87  GLU n 
1 88  ARG n 
1 89  HIS n 
1 90  ARG n 
1 91  ALA n 
1 92  ILE n 
1 93  TYR n 
1 94  GLN n 
1 95  ASP n 
1 96  LEU n 
1 97  GLN n 
1 98  ARG n 
1 99  ILE n 
1 100 ALA n 
1 101 PRO n 
1 102 THR n 
1 103 LEU n 
1 104 LEU n 
1 105 LEU n 
1 106 LYS n 
1 107 SER n 
1 108 ARG n 
1 109 GLY n 
1 110 GLU n 
1 111 THR n 
1 112 TYR n 
1 113 LYS n 
1 114 GLU n 
1 115 ASN n 
1 116 LEU n 
1 117 GLU n 
1 118 SER n 
1 119 ALA n 
1 120 GLN n 
1 121 LYS n 
1 122 ILE n 
1 123 GLY n 
1 124 VAL n 
1 125 ALA n 
1 126 ILE n 
1 127 GLY n 
1 128 LYS n 
1 129 GLN n 
1 130 ALA n 
1 131 GLN n 
1 132 MET n 
1 133 THR n 
1 134 GLN n 
1 135 ARG n 
1 136 ILE n 
1 137 GLU n 
1 138 GLN n 
1 139 HIS n 
1 140 LYS n 
1 141 GLN n 
1 142 THR n 
1 143 MET n 
1 144 ALA n 
1 145 GLU n 
1 146 PHE n 
1 147 LYS n 
1 148 GLN n 
1 149 HIS n 
1 150 PHE n 
1 151 ALA n 
1 152 THR n 
1 153 GLN n 
1 154 GLU n 
1 155 THR n 
1 156 ILE n 
1 157 GLN n 
1 158 PHE n 
1 159 GLY n 
1 160 VAL n 
1 161 VAL n 
1 162 SER n 
1 163 ASP n 
1 164 LYS n 
1 165 GLY n 
1 166 MET n 
1 167 TRP n 
1 168 LEU n 
1 169 HIS n 
1 170 SER n 
1 171 PRO n 
1 172 VAL n 
1 173 SER n 
1 174 TYR n 
1 175 ALA n 
1 176 GLY n 
1 177 GLY n 
1 178 VAL n 
1 179 LEU n 
1 180 SER n 
1 181 THR n 
1 182 LEU n 
1 183 GLY n 
1 184 ILE n 
1 185 GLN n 
1 186 SER n 
1 187 PRO n 
1 188 LEU n 
1 189 ALA n 
1 190 PRO n 
1 191 SER n 
1 192 GLU n 
1 193 GLN n 
1 194 LYS n 
1 195 ALA n 
1 196 TYR n 
1 197 ILE n 
1 198 PRO n 
1 199 THR n 
1 200 SER n 
1 201 PHE n 
1 202 GLU n 
1 203 LEU n 
1 204 LEU n 
1 205 LEU n 
1 206 LYS n 
1 207 THR n 
1 208 ASN n 
1 209 PRO n 
1 210 ASP n 
1 211 TRP n 
1 212 LEU n 
1 213 LEU n 
1 214 VAL n 
1 215 GLY n 
1 216 LEU n 
1 217 TYR n 
1 218 SER n 
1 219 GLN n 
1 220 PRO n 
1 221 ASN n 
1 222 ILE n 
1 223 VAL n 
1 224 ASP n 
1 225 GLU n 
1 226 TRP n 
1 227 ARG n 
1 228 LYS n 
1 229 ASN n 
1 230 PRO n 
1 231 LEU n 
1 232 PHE n 
1 233 LYS n 
1 234 LEU n 
1 235 LEU n 
1 236 THR n 
1 237 ALA n 
1 238 ALA n 
1 239 LYS n 
1 240 LYS n 
1 241 GLN n 
1 242 GLN n 
1 243 LEU n 
1 244 VAL n 
1 245 GLU n 
1 246 VAL n 
1 247 SER n 
1 248 PRO n 
1 249 GLU n 
1 250 LEU n 
1 251 TRP n 
1 252 SER n 
1 253 LEU n 
1 254 ASN n 
1 255 ARG n 
1 256 GLY n 
1 257 MET n 
1 258 LEU n 
1 259 ALA n 
1 260 ALA n 
1 261 GLU n 
1 262 GLU n 
1 263 ILE n 
1 264 ALA n 
1 265 ARG n 
1 266 ASN n 
1 267 LEU n 
1 268 GLU n 
1 269 ALA n 
1 270 LEU n 
1 271 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   271 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 HKB16_09180 
_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      'Vibrio alginolyticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     663 
_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      'Escherichia coli KRX' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1452720 
_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                   ? 
# 
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 
FE  non-polymer         . 'FE (III) ION'          ?                               'Fe 3'           55.845  
FLC non-polymer         . 'CITRATE ANION'         ?                               'C6 H5 O7 -3'    189.100 
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  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE               ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
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   23  23  ARG ARG A . n 
A 1 2   SER 2   24  24  SER SER A . n 
A 1 3   VAL 3   25  25  VAL VAL A . n 
A 1 4   GLN 4   26  26  GLN GLN A . n 
A 1 5   ASP 5   27  27  ASP ASP A . n 
A 1 6   GLU 6   28  28  GLU GLU A . n 
A 1 7   GLN 7   29  29  GLN GLN A . n 
A 1 8   GLY 8   30  30  GLY GLY A . n 
A 1 9   THR 9   31  31  THR THR A . n 
A 1 10  PHE 10  32  32  PHE PHE A . n 
A 1 11  GLU 11  33  33  GLU GLU A . n 
A 1 12  LEU 12  34  34  LEU LEU A . n 
A 1 13  GLU 13  35  35  GLU GLU A . n 
A 1 14  ALA 14  36  36  ALA ALA A . n 
A 1 15  ILE 15  37  37  ILE ILE A . n 
A 1 16  PRO 16  38  38  PRO PRO A . n 
A 1 17  GLN 17  39  39  GLN GLN A . n 
A 1 18  ARG 18  40  40  ARG ARG A . n 
A 1 19  ILE 19  41  41  ILE ILE A . n 
A 1 20  VAL 20  42  42  VAL VAL A . n 
A 1 21  VAL 21  43  43  VAL VAL A . n 
A 1 22  LEU 22  44  44  LEU LEU A . n 
A 1 23  GLU 23  45  45  GLU GLU A . n 
A 1 24  PHE 24  46  46  PHE PHE A . n 
A 1 25  SER 25  47  47  SER SER A . n 
A 1 26  PHE 26  48  48  PHE PHE A . n 
A 1 27  VAL 27  49  49  VAL VAL A . n 
A 1 28  ASP 28  50  50  ASP ASP A . n 
A 1 29  ALA 29  51  51  ALA ALA A . n 
A 1 30  LEU 30  52  52  LEU LEU A . n 
A 1 31  ALA 31  53  53  ALA ALA A . n 
A 1 32  ALA 32  54  54  ALA ALA A . n 
A 1 33  VAL 33  55  55  VAL VAL A . n 
A 1 34  ASP 34  56  56  ASP ASP A . n 
A 1 35  VAL 35  57  57  VAL VAL A . n 
A 1 36  SER 36  58  58  SER SER A . n 
A 1 37  PRO 37  59  59  PRO PRO A . n 
A 1 38  VAL 38  60  60  VAL VAL A . n 
A 1 39  GLY 39  61  61  GLY GLY A . n 
A 1 40  VAL 40  62  62  VAL VAL A . n 
A 1 41  ALA 41  63  63  ALA ALA A . n 
A 1 42  ASP 42  64  64  ASP ASP A . n 
A 1 43  ASP 43  65  65  ASP ASP A . n 
A 1 44  ASN 44  66  66  ASN ASN A . n 
A 1 45  ASP 45  67  67  ASP ASP A . n 
A 1 46  ALA 46  68  68  ALA ALA A . n 
A 1 47  THR 47  69  69  THR THR A . n 
A 1 48  ARG 48  70  70  ARG ARG A . n 
A 1 49  VAL 49  71  71  VAL VAL A . n 
A 1 50  ILE 50  72  72  ILE ILE A . n 
A 1 51  PRO 51  73  73  PRO PRO A . n 
A 1 52  ALA 52  74  74  ALA ALA A . n 
A 1 53  VAL 53  75  75  VAL VAL A . n 
A 1 54  ARG 54  76  76  ARG ARG A . n 
A 1 55  ASP 55  77  77  ASP ASP A . n 
A 1 56  LYS 56  78  78  LYS LYS A . n 
A 1 57  ILE 57  79  79  ILE ILE A . n 
A 1 58  GLU 58  80  80  GLU GLU A . n 
A 1 59  PRO 59  81  81  PRO PRO A . n 
A 1 60  TRP 60  82  82  TRP TRP A . n 
A 1 61  GLN 61  83  83  GLN GLN A . n 
A 1 62  SER 62  84  84  SER SER A . n 
A 1 63  VAL 63  85  85  VAL VAL A . n 
A 1 64  GLY 64  86  86  GLY GLY A . n 
A 1 65  MET 65  87  87  MET MET A . n 
A 1 66  ARG 66  88  88  ARG ARG A . n 
A 1 67  SER 67  89  89  SER SER A . n 
A 1 68  GLN 68  90  90  GLN GLN A . n 
A 1 69  PRO 69  91  91  PRO PRO A . n 
A 1 70  SER 70  92  92  SER SER A . n 
A 1 71  LEU 71  93  93  LEU LEU A . n 
A 1 72  GLU 72  94  94  GLU GLU A . n 
A 1 73  ALA 73  95  95  ALA ALA A . n 
A 1 74  ILE 74  96  96  ILE ILE A . n 
A 1 75  ALA 75  97  97  ALA ALA A . n 
A 1 76  VAL 76  98  98  VAL VAL A . n 
A 1 77  LEU 77  99  99  LEU LEU A . n 
A 1 78  LYS 78  100 100 LYS LYS A . n 
A 1 79  PRO 79  101 101 PRO PRO A . n 
A 1 80  ASP 80  102 102 ASP ASP A . n 
A 1 81  LEU 81  103 103 LEU LEU A . n 
A 1 82  ILE 82  104 104 ILE ILE A . n 
A 1 83  ILE 83  105 105 ILE ILE A . n 
A 1 84  ALA 84  106 106 ALA ALA A . n 
A 1 85  ASP 85  107 107 ASP ASP A . n 
A 1 86  ALA 86  108 108 ALA ALA A . n 
A 1 87  GLU 87  109 109 GLU GLU A . n 
A 1 88  ARG 88  110 110 ARG ARG A . n 
A 1 89  HIS 89  111 111 HIS HIS A . n 
A 1 90  ARG 90  112 112 ARG ARG A . n 
A 1 91  ALA 91  113 113 ALA ALA A . n 
A 1 92  ILE 92  114 114 ILE ILE A . n 
A 1 93  TYR 93  115 115 TYR TYR A . n 
A 1 94  GLN 94  116 116 GLN GLN A . n 
A 1 95  ASP 95  117 117 ASP ASP A . n 
A 1 96  LEU 96  118 118 LEU LEU A . n 
A 1 97  GLN 97  119 119 GLN GLN A . n 
A 1 98  ARG 98  120 120 ARG ARG A . n 
A 1 99  ILE 99  121 121 ILE ILE A . n 
A 1 100 ALA 100 122 122 ALA ALA A . n 
A 1 101 PRO 101 123 123 PRO PRO A . n 
A 1 102 THR 102 124 124 THR THR A . n 
A 1 103 LEU 103 125 125 LEU LEU A . n 
A 1 104 LEU 104 126 126 LEU LEU A . n 
A 1 105 LEU 105 127 127 LEU LEU A . n 
A 1 106 LYS 106 128 128 LYS LYS A . n 
A 1 107 SER 107 129 129 SER SER A . n 
A 1 108 ARG 108 130 130 ARG ARG A . n 
A 1 109 GLY 109 131 131 GLY GLY A . n 
A 1 110 GLU 110 132 132 GLU GLU A . n 
A 1 111 THR 111 133 133 THR THR A . n 
A 1 112 TYR 112 134 134 TYR TYR A . n 
A 1 113 LYS 113 135 135 LYS LYS A . n 
A 1 114 GLU 114 136 136 GLU GLU A . n 
A 1 115 ASN 115 137 137 ASN ASN A . n 
A 1 116 LEU 116 138 138 LEU LEU A . n 
A 1 117 GLU 117 139 139 GLU GLU A . n 
A 1 118 SER 118 140 140 SER SER A . n 
A 1 119 ALA 119 141 141 ALA ALA A . n 
A 1 120 GLN 120 142 142 GLN GLN A . n 
A 1 121 LYS 121 143 143 LYS LYS A . n 
A 1 122 ILE 122 144 144 ILE ILE A . n 
A 1 123 GLY 123 145 145 GLY GLY A . n 
A 1 124 VAL 124 146 146 VAL VAL A . n 
A 1 125 ALA 125 147 147 ALA ALA A . n 
A 1 126 ILE 126 148 148 ILE ILE A . n 
A 1 127 GLY 127 149 149 GLY GLY A . n 
A 1 128 LYS 128 150 150 LYS LYS A . n 
A 1 129 GLN 129 151 151 GLN GLN A . n 
A 1 130 ALA 130 152 152 ALA ALA A . n 
A 1 131 GLN 131 153 153 GLN GLN A . n 
A 1 132 MET 132 154 154 MET MET A . n 
A 1 133 THR 133 155 155 THR THR A . n 
A 1 134 GLN 134 156 156 GLN GLN A . n 
A 1 135 ARG 135 157 157 ARG ARG A . n 
A 1 136 ILE 136 158 158 ILE ILE A . n 
A 1 137 GLU 137 159 159 GLU GLU A . n 
A 1 138 GLN 138 160 160 GLN GLN A . n 
A 1 139 HIS 139 161 161 HIS HIS A . n 
A 1 140 LYS 140 162 162 LYS LYS A . n 
A 1 141 GLN 141 163 163 GLN GLN A . n 
A 1 142 THR 142 164 164 THR THR A . n 
A 1 143 MET 143 165 165 MET MET A . n 
A 1 144 ALA 144 166 166 ALA ALA A . n 
A 1 145 GLU 145 167 167 GLU GLU A . n 
A 1 146 PHE 146 168 168 PHE PHE A . n 
A 1 147 LYS 147 169 169 LYS LYS A . n 
A 1 148 GLN 148 170 170 GLN GLN A . n 
A 1 149 HIS 149 171 171 HIS HIS A . n 
A 1 150 PHE 150 172 172 PHE PHE A . n 
A 1 151 ALA 151 173 173 ALA ALA A . n 
A 1 152 THR 152 174 174 THR THR A . n 
A 1 153 GLN 153 175 175 GLN GLN A . n 
A 1 154 GLU 154 176 176 GLU GLU A . n 
A 1 155 THR 155 177 177 THR THR A . n 
A 1 156 ILE 156 178 178 ILE ILE A . n 
A 1 157 GLN 157 179 179 GLN GLN A . n 
A 1 158 PHE 158 180 180 PHE PHE A . n 
A 1 159 GLY 159 181 181 GLY GLY A . n 
A 1 160 VAL 160 182 182 VAL VAL A . n 
A 1 161 VAL 161 183 183 VAL VAL A . n 
A 1 162 SER 162 184 184 SER SER A . n 
A 1 163 ASP 163 185 185 ASP ASP A . n 
A 1 164 LYS 164 186 186 LYS LYS A . n 
A 1 165 GLY 165 187 187 GLY GLY A . n 
A 1 166 MET 166 188 188 MET MET A . n 
A 1 167 TRP 167 189 189 TRP TRP A . n 
A 1 168 LEU 168 190 190 LEU LEU A . n 
A 1 169 HIS 169 191 191 HIS HIS A . n 
A 1 170 SER 170 192 192 SER SER A . n 
A 1 171 PRO 171 193 193 PRO PRO A . n 
A 1 172 VAL 172 194 194 VAL VAL A . n 
A 1 173 SER 173 195 195 SER SER A . n 
A 1 174 TYR 174 196 196 TYR TYR A . n 
A 1 175 ALA 175 197 197 ALA ALA A . n 
A 1 176 GLY 176 198 198 GLY GLY A . n 
A 1 177 GLY 177 199 199 GLY GLY A . n 
A 1 178 VAL 178 200 200 VAL VAL A . n 
A 1 179 LEU 179 201 201 LEU LEU A . n 
A 1 180 SER 180 202 202 SER SER A . n 
A 1 181 THR 181 203 203 THR THR A . n 
A 1 182 LEU 182 204 204 LEU LEU A . n 
A 1 183 GLY 183 205 205 GLY GLY A . n 
A 1 184 ILE 184 206 206 ILE ILE A . n 
A 1 185 GLN 185 207 207 GLN GLN A . n 
A 1 186 SER 186 208 208 SER SER A . n 
A 1 187 PRO 187 209 209 PRO PRO A . n 
A 1 188 LEU 188 210 210 LEU LEU A . n 
A 1 189 ALA 189 211 211 ALA ALA A . n 
A 1 190 PRO 190 212 212 PRO PRO A . n 
A 1 191 SER 191 213 213 SER SER A . n 
A 1 192 GLU 192 214 214 GLU GLU A . n 
A 1 193 GLN 193 215 215 GLN GLN A . n 
A 1 194 LYS 194 216 216 LYS LYS A . n 
A 1 195 ALA 195 217 217 ALA ALA A . n 
A 1 196 TYR 196 218 218 TYR TYR A . n 
A 1 197 ILE 197 219 219 ILE ILE A . n 
A 1 198 PRO 198 220 220 PRO PRO A . n 
A 1 199 THR 199 221 221 THR THR A . n 
A 1 200 SER 200 222 222 SER SER A . n 
A 1 201 PHE 201 223 223 PHE PHE A . n 
A 1 202 GLU 202 224 224 GLU GLU A . n 
A 1 203 LEU 203 225 225 LEU LEU A . n 
A 1 204 LEU 204 226 226 LEU LEU A . n 
A 1 205 LEU 205 227 227 LEU LEU A . n 
A 1 206 LYS 206 228 228 LYS LYS A . n 
A 1 207 THR 207 229 229 THR THR A . n 
A 1 208 ASN 208 230 230 ASN ASN A . n 
A 1 209 PRO 209 231 231 PRO PRO A . n 
A 1 210 ASP 210 232 232 ASP ASP A . n 
A 1 211 TRP 211 233 233 TRP TRP A . n 
A 1 212 LEU 212 234 234 LEU LEU A . n 
A 1 213 LEU 213 235 235 LEU LEU A . n 
A 1 214 VAL 214 236 236 VAL VAL A . n 
A 1 215 GLY 215 237 237 GLY GLY A . n 
A 1 216 LEU 216 238 238 LEU LEU A . n 
A 1 217 TYR 217 239 239 TYR TYR A . n 
A 1 218 SER 218 240 240 SER SER A . n 
A 1 219 GLN 219 241 241 GLN GLN A . n 
A 1 220 PRO 220 242 242 PRO PRO A . n 
A 1 221 ASN 221 243 243 ASN ASN A . n 
A 1 222 ILE 222 244 244 ILE ILE A . n 
A 1 223 VAL 223 245 245 VAL VAL A . n 
A 1 224 ASP 224 246 246 ASP ASP A . n 
A 1 225 GLU 225 247 247 GLU GLU A . n 
A 1 226 TRP 226 248 248 TRP TRP A . n 
A 1 227 ARG 227 249 249 ARG ARG A . n 
A 1 228 LYS 228 250 250 LYS LYS A . n 
A 1 229 ASN 229 251 251 ASN ASN A . n 
A 1 230 PRO 230 252 252 PRO PRO A . n 
A 1 231 LEU 231 253 253 LEU LEU A . n 
A 1 232 PHE 232 254 254 PHE PHE A . n 
A 1 233 LYS 233 255 255 LYS LYS A . n 
A 1 234 LEU 234 256 256 LEU LEU A . n 
A 1 235 LEU 235 257 257 LEU LEU A . n 
A 1 236 THR 236 258 258 THR THR A . n 
A 1 237 ALA 237 259 259 ALA ALA A . n 
A 1 238 ALA 238 260 260 ALA ALA A . n 
A 1 239 LYS 239 261 261 LYS LYS A . n 
A 1 240 LYS 240 262 262 LYS LYS A . n 
A 1 241 GLN 241 263 263 GLN GLN A . n 
A 1 242 GLN 242 264 264 GLN GLN A . n 
A 1 243 LEU 243 265 265 LEU LEU A . n 
A 1 244 VAL 244 266 266 VAL VAL A . n 
A 1 245 GLU 245 267 267 GLU GLU A . n 
A 1 246 VAL 246 268 268 VAL VAL A . n 
A 1 247 SER 247 269 269 SER SER A . n 
A 1 248 PRO 248 270 270 PRO PRO A . n 
A 1 249 GLU 249 271 271 GLU GLU A . n 
A 1 250 LEU 250 272 272 LEU LEU A . n 
A 1 251 TRP 251 273 273 TRP TRP A . n 
A 1 252 SER 252 274 274 SER SER A . n 
A 1 253 LEU 253 275 275 LEU LEU A . n 
A 1 254 ASN 254 276 276 ASN ASN A . n 
A 1 255 ARG 255 277 277 ARG ARG A . n 
A 1 256 GLY 256 278 278 GLY GLY A . n 
A 1 257 MET 257 279 279 MET MET A . n 
A 1 258 LEU 258 280 280 LEU LEU A . n 
A 1 259 ALA 259 281 281 ALA ALA A . n 
A 1 260 ALA 260 282 282 ALA ALA A . n 
A 1 261 GLU 261 283 283 GLU GLU A . n 
A 1 262 GLU 262 284 284 GLU GLU A . n 
A 1 263 ILE 263 285 285 ILE ILE A . n 
A 1 264 ALA 264 286 286 ALA ALA A . n 
A 1 265 ARG 265 287 287 ARG ARG A . n 
A 1 266 ASN 266 288 288 ASN ASN A . n 
A 1 267 LEU 267 289 289 LEU LEU A . n 
A 1 268 GLU 268 290 290 GLU GLU A . n 
A 1 269 ALA 269 291 291 ALA ALA A . n 
A 1 270 LEU 270 292 292 LEU LEU A . n 
A 1 271 LEU 271 293 293 LEU LEU A . 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 
B 2 GOL 1  301 301 GOL GOL A . 
C 2 GOL 1  302 302 GOL GOL A . 
D 2 GOL 1  303 303 GOL GOL A . 
E 3 PEG 1  304 304 PEG PEG A . 
F 4 FLC 1  305 743 FLC FLC A . 
G 4 FLC 1  306 744 FLC FLC A . 
H 5 FE  1  307 1   FE  FE  A . 
I 6 HOH 1  401 1   HOH HOH A . 
I 6 HOH 2  402 14  HOH HOH A . 
I 6 HOH 3  403 6   HOH HOH A . 
I 6 HOH 4  404 2   HOH HOH A . 
I 6 HOH 5  405 10  HOH HOH A . 
I 6 HOH 6  406 13  HOH HOH A . 
I 6 HOH 7  407 4   HOH HOH A . 
I 6 HOH 8  408 15  HOH HOH A . 
I 6 HOH 9  409 11  HOH HOH A . 
I 6 HOH 10 410 5   HOH HOH A . 
I 6 HOH 11 411 12  HOH HOH A . 
I 6 HOH 12 412 3   HOH HOH A . 
I 6 HOH 13 413 7   HOH HOH A . 
I 6 HOH 14 414 8   HOH HOH A . 
I 6 HOH 15 415 9   HOH HOH A . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     FLC 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      305 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     CAC 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    F 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    FLC 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    CAC 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.21RC1_5058: ???)' 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                     2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .                     3 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                     4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .                     5 
# 
_cell.entry_id           8Y4Y 
_cell.length_a           100.497 
_cell.length_b           100.497 
_cell.length_c           205.983 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         8Y4Y 
_symmetry.space_group_name_H-M             'I 4 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                97 
# 
_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                   8Y4Y 
_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             4.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.06 
_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              8.0 
_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    '0.1M HEPES pH7.5, 20% w/v Polyethylene glycol 10000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-23 
_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   1.0 
_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                        'PHOTON FACTORY BEAMLINE AR-NE3A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   AR-NE3A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     8Y4Y 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             45.160 
_reflns.d_resolution_high            2.510 
_reflns.number_obs                   18412 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.10600 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        1.2300 
_reflns.B_iso_Wilson_estimate        61.62 
_reflns.pdbx_redundancy              6.860 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_CC_star                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.51 
_reflns_shell.d_res_low              2.67 
_reflns_shell.percent_possible_all   ? 
_reflns_shell.Rmerge_I_obs           1.45700 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.230 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_unique_obs      18412 
_reflns_shell.pdbx_CC_half           ? 
_reflns_shell.pdbx_CC_star           ? 
_reflns_shell.pdbx_Rpim_I_all        ? 
_reflns_shell.pdbx_Rrim_I_all        ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 8Y4Y 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     18412 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             33.06 
_refine.ls_d_res_high                            2.51 
_refine.ls_percent_reflns_obs                    99.5 
_refine.ls_R_factor_obs                          0.226 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.224 
_refine.ls_R_factor_R_free                       0.262 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.620 
_refine.ls_number_reflns_R_free                  850 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               68.45 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.360 
_refine.pdbx_overall_phase_error                 29.550 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2129 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               2195 
_refine_hist.d_res_high                       2.51 
_refine_hist.d_res_low                        33.06 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.004  ? ? ?   'X-RAY DIFFRACTION' ? 
f_angle_d          0.618  ? ? ?   'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 15.334 ? ? 836 'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.041  ? ? 339 'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 388 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.5100 2.6700  2815 0.3160 97.00  0.3391 . . 120 . . . . 
'X-RAY DIFFRACTION' . 2.6700 2.8700  2887 0.3140 100.00 0.4046 . . 143 . . . . 
'X-RAY DIFFRACTION' . 2.8700 3.1600  2860 0.2886 100.00 0.3456 . . 164 . . . . 
'X-RAY DIFFRACTION' . 3.1600 3.6200  2938 0.2557 100.00 0.2802 . . 129 . . . . 
'X-RAY DIFFRACTION' . 3.6200 4.5500  2962 0.1966 100.00 0.2509 . . 138 . . . . 
'X-RAY DIFFRACTION' . 4.5600 33.0600 3100 0.1902 100.00 0.2147 . . 156 . . . . 
# 
_struct.entry_id                     8Y4Y 
_struct.title                        
'Crystal structure of ferric iron-binding protein (FecB) from Vibrio alginolyticus in complex with ferric citrate' 
_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        8Y4Y 
_struct_keywords.text            'Vibrio alginolyticus; periplasmic binding protein; ferric citrate, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A7Y0SGI3_VIBPH 
_struct_ref.pdbx_db_accession          A0A7Y0SGI3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RSVQDEQGTFELEAIPQRIVVLEFSFVDALAAVDVSPVGVADDNDATRVIPAVRDKIEPWQSVGMRSQPSLEAIAVLKPD
LIIADAERHRAIYQDLQRIAPTLLLKSRGETYQENLESAQKIGVAIGKQAQMTQRIEQHKQTMAEFKQHFATQETIQFGV
VSDKGMWLHSPVSYAGGVLSTLGIQSPLAPSEQNAYIPTSFELLLKTNPDWLLVGLYSQPNIVDEWRKNPLFKLLTAAKK
QQLVEVSPELWSLNRGMLAAEEIARNLEALL
;
_struct_ref.pdbx_align_begin           34 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8Y4Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 271 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A7Y0SGI3 
_struct_ref_seq.db_align_beg                  34 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  304 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       23 
_struct_ref_seq.pdbx_auth_seq_align_end       293 
# 
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 8Y4Y LYS A 113 ? UNP A0A7Y0SGI3 GLN 146 conflict 135 1 
1 8Y4Y LYS A 194 ? UNP A0A7Y0SGI3 ASN 227 conflict 216 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_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 GLU A 23  ? ALA A 32  ? GLU A 45  ALA A 54  1 ? 10 
HELX_P HELX_P2  AA2 ASP A 45  ? VAL A 49  ? ASP A 67  VAL A 71  5 ? 5  
HELX_P HELX_P3  AA3 ILE A 50  ? ASP A 55  ? ILE A 72  ASP A 77  1 ? 6  
HELX_P HELX_P4  AA4 SER A 70  ? LEU A 77  ? SER A 92  LEU A 99  1 ? 8  
HELX_P HELX_P5  AA5 ILE A 92  ? ALA A 100 ? ILE A 114 ALA A 122 1 ? 9  
HELX_P HELX_P6  AA6 THR A 111 ? GLY A 127 ? THR A 133 GLY A 149 1 ? 17 
HELX_P HELX_P7  AA7 LYS A 128 ? PHE A 150 ? LYS A 150 PHE A 172 1 ? 23 
HELX_P HELX_P8  AA8 SER A 173 ? LEU A 182 ? SER A 195 LEU A 204 1 ? 10 
HELX_P HELX_P9  AA9 SER A 200 ? ASN A 208 ? SER A 222 ASN A 230 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 221 ? LYS A 228 ? ASN A 243 LYS A 250 1 ? 8  
HELX_P HELX_P11 AB2 ASN A 229 ? LEU A 234 ? ASN A 251 LEU A 256 5 ? 6  
HELX_P HELX_P12 AB3 LEU A 235 ? LYS A 240 ? LEU A 257 LYS A 262 1 ? 6  
HELX_P HELX_P13 AB4 SER A 247 ? SER A 252 ? SER A 269 SER A 274 1 ? 6  
HELX_P HELX_P14 AB5 GLY A 256 ? LEU A 271 ? GLY A 278 LEU A 293 1 ? 16 
# 
_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 
metalc1 metalc ? ? F FLC . OB2 ? ? ? 1_555 H FE . FE ? ? A FLC 305 A FE 307 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc2 metalc ? ? F FLC . OG2 ? ? ? 1_555 H FE . FE ? ? A FLC 305 A FE 307 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc3 metalc ? ? F FLC . OHB ? ? ? 1_555 H FE . FE ? ? A FLC 305 A FE 307 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc4 metalc ? ? G FLC . OA1 ? ? ? 1_555 H FE . FE ? ? A FLC 306 A FE 307 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc5 metalc ? ? G FLC . OHB ? ? ? 1_555 H FE . FE ? ? A FLC 306 A FE 307 1_555 ? ? ? ? ? ? ? 2.695 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OB2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OG2 ? F FLC . ? A FLC 305 ? 1_555 85.7  ? 
2  OB2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? F FLC . ? A FLC 305 ? 1_555 70.5  ? 
3  OG2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? F FLC . ? A FLC 305 ? 1_555 77.3  ? 
4  OB2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OA1 ? G FLC . ? A FLC 306 ? 1_555 98.5  ? 
5  OG2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OA1 ? G FLC . ? A FLC 306 ? 1_555 102.9 ? 
6  OHB ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OA1 ? G FLC . ? A FLC 306 ? 1_555 169.0 ? 
7  OB2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? G FLC . ? A FLC 306 ? 1_555 165.6 ? 
8  OG2 ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? G FLC . ? A FLC 306 ? 1_555 108.5 ? 
9  OHB ? F FLC . ? A FLC 305 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? G FLC . ? A FLC 306 ? 1_555 109.5 ? 
10 OA1 ? G FLC . ? A FLC 306 ? 1_555 FE ? H FE . ? A FE 307 ? 1_555 OHB ? G FLC . ? A FLC 306 ? 1_555 81.0  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLN 
_struct_mon_prot_cis.label_seq_id           219 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLN 
_struct_mon_prot_cis.auth_seq_id            241 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    220 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     242 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.42 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? 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 SER A 2   ? ASP A 5   ? SER A 24  ASP A 27  
AA1 2 GLY A 8   ? GLU A 11  ? GLY A 30  GLU A 33  
AA2 1 GLN A 61  ? SER A 62  ? GLN A 83  SER A 84  
AA2 2 GLY A 39  ? VAL A 40  ? GLY A 61  VAL A 62  
AA2 3 ILE A 19  ? VAL A 21  ? ILE A 41  VAL A 43  
AA2 4 LEU A 81  ? ASP A 85  ? LEU A 103 ASP A 107 
AA2 5 THR A 102 ? LEU A 105 ? THR A 124 LEU A 127 
AA3 1 TYR A 196 ? THR A 199 ? TYR A 218 THR A 221 
AA3 2 MET A 166 ? HIS A 169 ? MET A 188 HIS A 191 
AA3 3 ILE A 156 ? VAL A 161 ? ILE A 178 VAL A 183 
AA3 4 TRP A 211 ? LEU A 216 ? TRP A 233 LEU A 238 
AA3 5 LEU A 243 ? VAL A 246 ? LEU A 265 VAL A 268 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 3   ? N VAL A 25  O PHE A 10  ? O PHE A 32  
AA2 1 2 O GLN A 61  ? O GLN A 83  N VAL A 40  ? N VAL A 62  
AA2 2 3 O GLY A 39  ? O GLY A 61  N VAL A 21  ? N VAL A 43  
AA2 3 4 N VAL A 20  ? N VAL A 42  O LEU A 81  ? O LEU A 103 
AA2 4 5 N ILE A 82  ? N ILE A 104 O LEU A 103 ? O LEU A 125 
AA3 1 2 O THR A 199 ? O THR A 221 N MET A 166 ? N MET A 188 
AA3 2 3 O TRP A 167 ? O TRP A 189 N VAL A 160 ? N VAL A 182 
AA3 3 4 N GLN A 157 ? N GLN A 179 O LEU A 213 ? O LEU A 235 
AA3 4 5 N VAL A 214 ? N VAL A 236 O VAL A 246 ? O VAL A 268 
# 
_pdbx_entry_details.entry_id                   8Y4Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 67  ? ? -166.00 89.98  
2 1 SER A 129 ? ? -148.09 -50.83 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y,x,z               
3  y,-x,z               
4  x,-y,-z              
5  -x,y,-z              
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1/2,x+1/2,z+1/2   
11 y+1/2,-x+1/2,z+1/2   
12 x+1/2,-y+1/2,-z+1/2  
13 -x+1/2,y+1/2,-z+1/2  
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
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  
FE  FE   FE N N 74  
FLC CAC  C  N N 75  
FLC CA   C  N N 76  
FLC CB   C  N N 77  
FLC CBC  C  N N 78  
FLC CG   C  N N 79  
FLC CGC  C  N N 80  
FLC OA1  O  N N 81  
FLC OA2  O  N N 82  
FLC OB1  O  N N 83  
FLC OB2  O  N N 84  
FLC OG1  O  N N 85  
FLC OG2  O  N N 86  
FLC OHB  O  N N 87  
FLC HA1  H  N N 88  
FLC HA2  H  N N 89  
FLC HG1  H  N N 90  
FLC HG2  H  N N 91  
FLC HOB  H  N N 92  
GLN N    N  N N 93  
GLN CA   C  N S 94  
GLN C    C  N N 95  
GLN O    O  N N 96  
GLN CB   C  N N 97  
GLN CG   C  N N 98  
GLN CD   C  N N 99  
GLN OE1  O  N N 100 
GLN NE2  N  N N 101 
GLN OXT  O  N N 102 
GLN H    H  N N 103 
GLN H2   H  N N 104 
GLN HA   H  N N 105 
GLN HB2  H  N N 106 
GLN HB3  H  N N 107 
GLN HG2  H  N N 108 
GLN HG3  H  N N 109 
GLN HE21 H  N N 110 
GLN HE22 H  N N 111 
GLN HXT  H  N N 112 
GLU N    N  N N 113 
GLU CA   C  N S 114 
GLU C    C  N N 115 
GLU O    O  N N 116 
GLU CB   C  N N 117 
GLU CG   C  N N 118 
GLU CD   C  N N 119 
GLU OE1  O  N N 120 
GLU OE2  O  N N 121 
GLU OXT  O  N N 122 
GLU H    H  N N 123 
GLU H2   H  N N 124 
GLU HA   H  N N 125 
GLU HB2  H  N N 126 
GLU HB3  H  N N 127 
GLU HG2  H  N N 128 
GLU HG3  H  N N 129 
GLU HE2  H  N N 130 
GLU HXT  H  N N 131 
GLY N    N  N N 132 
GLY CA   C  N N 133 
GLY C    C  N N 134 
GLY O    O  N N 135 
GLY OXT  O  N N 136 
GLY H    H  N N 137 
GLY H2   H  N N 138 
GLY HA2  H  N N 139 
GLY HA3  H  N N 140 
GLY HXT  H  N N 141 
GOL C1   C  N N 142 
GOL O1   O  N N 143 
GOL C2   C  N N 144 
GOL O2   O  N N 145 
GOL C3   C  N N 146 
GOL O3   O  N N 147 
GOL H11  H  N N 148 
GOL H12  H  N N 149 
GOL HO1  H  N N 150 
GOL H2   H  N N 151 
GOL HO2  H  N N 152 
GOL H31  H  N N 153 
GOL H32  H  N N 154 
GOL HO3  H  N N 155 
HIS N    N  N N 156 
HIS CA   C  N S 157 
HIS C    C  N N 158 
HIS O    O  N N 159 
HIS CB   C  N N 160 
HIS CG   C  Y N 161 
HIS ND1  N  Y N 162 
HIS CD2  C  Y N 163 
HIS CE1  C  Y N 164 
HIS NE2  N  Y N 165 
HIS OXT  O  N N 166 
HIS H    H  N N 167 
HIS H2   H  N N 168 
HIS HA   H  N N 169 
HIS HB2  H  N N 170 
HIS HB3  H  N N 171 
HIS HD1  H  N N 172 
HIS HD2  H  N N 173 
HIS HE1  H  N N 174 
HIS HE2  H  N N 175 
HIS HXT  H  N N 176 
HOH O    O  N N 177 
HOH H1   H  N N 178 
HOH H2   H  N N 179 
ILE N    N  N N 180 
ILE CA   C  N S 181 
ILE C    C  N N 182 
ILE O    O  N N 183 
ILE CB   C  N S 184 
ILE CG1  C  N N 185 
ILE CG2  C  N N 186 
ILE CD1  C  N N 187 
ILE OXT  O  N N 188 
ILE H    H  N N 189 
ILE H2   H  N N 190 
ILE HA   H  N N 191 
ILE HB   H  N N 192 
ILE HG12 H  N N 193 
ILE HG13 H  N N 194 
ILE HG21 H  N N 195 
ILE HG22 H  N N 196 
ILE HG23 H  N N 197 
ILE HD11 H  N N 198 
ILE HD12 H  N N 199 
ILE HD13 H  N N 200 
ILE HXT  H  N N 201 
LEU N    N  N N 202 
LEU CA   C  N S 203 
LEU C    C  N N 204 
LEU O    O  N N 205 
LEU CB   C  N N 206 
LEU CG   C  N N 207 
LEU CD1  C  N N 208 
LEU CD2  C  N N 209 
LEU OXT  O  N N 210 
LEU H    H  N N 211 
LEU H2   H  N N 212 
LEU HA   H  N N 213 
LEU HB2  H  N N 214 
LEU HB3  H  N N 215 
LEU HG   H  N N 216 
LEU HD11 H  N N 217 
LEU HD12 H  N N 218 
LEU HD13 H  N N 219 
LEU HD21 H  N N 220 
LEU HD22 H  N N 221 
LEU HD23 H  N N 222 
LEU HXT  H  N N 223 
LYS N    N  N N 224 
LYS CA   C  N S 225 
LYS C    C  N N 226 
LYS O    O  N N 227 
LYS CB   C  N N 228 
LYS CG   C  N N 229 
LYS CD   C  N N 230 
LYS CE   C  N N 231 
LYS NZ   N  N N 232 
LYS OXT  O  N N 233 
LYS H    H  N N 234 
LYS H2   H  N N 235 
LYS HA   H  N N 236 
LYS HB2  H  N N 237 
LYS HB3  H  N N 238 
LYS HG2  H  N N 239 
LYS HG3  H  N N 240 
LYS HD2  H  N N 241 
LYS HD3  H  N N 242 
LYS HE2  H  N N 243 
LYS HE3  H  N N 244 
LYS HZ1  H  N N 245 
LYS HZ2  H  N N 246 
LYS HZ3  H  N N 247 
LYS HXT  H  N N 248 
MET N    N  N N 249 
MET CA   C  N S 250 
MET C    C  N N 251 
MET O    O  N N 252 
MET CB   C  N N 253 
MET CG   C  N N 254 
MET SD   S  N N 255 
MET CE   C  N N 256 
MET OXT  O  N N 257 
MET H    H  N N 258 
MET H2   H  N N 259 
MET HA   H  N N 260 
MET HB2  H  N N 261 
MET HB3  H  N N 262 
MET HG2  H  N N 263 
MET HG3  H  N N 264 
MET HE1  H  N N 265 
MET HE2  H  N N 266 
MET HE3  H  N N 267 
MET HXT  H  N N 268 
PEG C1   C  N N 269 
PEG O1   O  N N 270 
PEG C2   C  N N 271 
PEG O2   O  N N 272 
PEG C3   C  N N 273 
PEG C4   C  N N 274 
PEG O4   O  N N 275 
PEG H11  H  N N 276 
PEG H12  H  N N 277 
PEG HO1  H  N N 278 
PEG H21  H  N N 279 
PEG H22  H  N N 280 
PEG H31  H  N N 281 
PEG H32  H  N N 282 
PEG H41  H  N N 283 
PEG H42  H  N N 284 
PEG HO4  H  N N 285 
PHE N    N  N N 286 
PHE CA   C  N S 287 
PHE C    C  N N 288 
PHE O    O  N N 289 
PHE CB   C  N N 290 
PHE CG   C  Y N 291 
PHE CD1  C  Y N 292 
PHE CD2  C  Y N 293 
PHE CE1  C  Y N 294 
PHE CE2  C  Y N 295 
PHE CZ   C  Y N 296 
PHE OXT  O  N N 297 
PHE H    H  N N 298 
PHE H2   H  N N 299 
PHE HA   H  N N 300 
PHE HB2  H  N N 301 
PHE HB3  H  N N 302 
PHE HD1  H  N N 303 
PHE HD2  H  N N 304 
PHE HE1  H  N N 305 
PHE HE2  H  N N 306 
PHE HZ   H  N N 307 
PHE HXT  H  N N 308 
PRO N    N  N N 309 
PRO CA   C  N S 310 
PRO C    C  N N 311 
PRO O    O  N N 312 
PRO CB   C  N N 313 
PRO CG   C  N N 314 
PRO CD   C  N N 315 
PRO OXT  O  N N 316 
PRO H    H  N N 317 
PRO HA   H  N N 318 
PRO HB2  H  N N 319 
PRO HB3  H  N N 320 
PRO HG2  H  N N 321 
PRO HG3  H  N N 322 
PRO HD2  H  N N 323 
PRO HD3  H  N N 324 
PRO HXT  H  N N 325 
SER N    N  N N 326 
SER CA   C  N S 327 
SER C    C  N N 328 
SER O    O  N N 329 
SER CB   C  N N 330 
SER OG   O  N N 331 
SER OXT  O  N N 332 
SER H    H  N N 333 
SER H2   H  N N 334 
SER HA   H  N N 335 
SER HB2  H  N N 336 
SER HB3  H  N N 337 
SER HG   H  N N 338 
SER HXT  H  N N 339 
THR N    N  N N 340 
THR CA   C  N S 341 
THR C    C  N N 342 
THR O    O  N N 343 
THR CB   C  N R 344 
THR OG1  O  N N 345 
THR CG2  C  N N 346 
THR OXT  O  N N 347 
THR H    H  N N 348 
THR H2   H  N N 349 
THR HA   H  N N 350 
THR HB   H  N N 351 
THR HG1  H  N N 352 
THR HG21 H  N N 353 
THR HG22 H  N N 354 
THR HG23 H  N N 355 
THR HXT  H  N N 356 
TRP N    N  N N 357 
TRP CA   C  N S 358 
TRP C    C  N N 359 
TRP O    O  N N 360 
TRP CB   C  N N 361 
TRP CG   C  Y N 362 
TRP CD1  C  Y N 363 
TRP CD2  C  Y N 364 
TRP NE1  N  Y N 365 
TRP CE2  C  Y N 366 
TRP CE3  C  Y N 367 
TRP CZ2  C  Y N 368 
TRP CZ3  C  Y N 369 
TRP CH2  C  Y N 370 
TRP OXT  O  N N 371 
TRP H    H  N N 372 
TRP H2   H  N N 373 
TRP HA   H  N N 374 
TRP HB2  H  N N 375 
TRP HB3  H  N N 376 
TRP HD1  H  N N 377 
TRP HE1  H  N N 378 
TRP HE3  H  N N 379 
TRP HZ2  H  N N 380 
TRP HZ3  H  N N 381 
TRP HH2  H  N N 382 
TRP HXT  H  N N 383 
TYR N    N  N N 384 
TYR CA   C  N S 385 
TYR C    C  N N 386 
TYR O    O  N N 387 
TYR CB   C  N N 388 
TYR CG   C  Y N 389 
TYR CD1  C  Y N 390 
TYR CD2  C  Y N 391 
TYR CE1  C  Y N 392 
TYR CE2  C  Y N 393 
TYR CZ   C  Y N 394 
TYR OH   O  N N 395 
TYR OXT  O  N N 396 
TYR H    H  N N 397 
TYR H2   H  N N 398 
TYR HA   H  N N 399 
TYR HB2  H  N N 400 
TYR HB3  H  N N 401 
TYR HD1  H  N N 402 
TYR HD2  H  N N 403 
TYR HE1  H  N N 404 
TYR HE2  H  N N 405 
TYR HH   H  N N 406 
TYR HXT  H  N N 407 
VAL N    N  N N 408 
VAL CA   C  N S 409 
VAL C    C  N N 410 
VAL O    O  N N 411 
VAL CB   C  N N 412 
VAL CG1  C  N N 413 
VAL CG2  C  N N 414 
VAL OXT  O  N N 415 
VAL H    H  N N 416 
VAL H2   H  N N 417 
VAL HA   H  N N 418 
VAL HB   H  N N 419 
VAL HG11 H  N N 420 
VAL HG12 H  N N 421 
VAL HG13 H  N N 422 
VAL HG21 H  N N 423 
VAL HG22 H  N N 424 
VAL HG23 H  N N 425 
VAL HXT  H  N N 426 
# 
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  
FLC CAC CA   sing N N 70  
FLC CAC OA1  doub N N 71  
FLC CAC OA2  sing N N 72  
FLC CA  CB   sing N N 73  
FLC CA  HA1  sing N N 74  
FLC CA  HA2  sing N N 75  
FLC CB  CBC  sing N N 76  
FLC CB  CG   sing N N 77  
FLC CB  OHB  sing N N 78  
FLC CBC OB1  doub N N 79  
FLC CBC OB2  sing N N 80  
FLC CG  CGC  sing N N 81  
FLC CG  HG1  sing N N 82  
FLC CG  HG2  sing N N 83  
FLC CGC OG1  doub N N 84  
FLC CGC OG2  sing N N 85  
FLC OHB HOB  sing N N 86  
GLN N   CA   sing N N 87  
GLN N   H    sing N N 88  
GLN N   H2   sing N N 89  
GLN CA  C    sing N N 90  
GLN CA  CB   sing N N 91  
GLN CA  HA   sing N N 92  
GLN C   O    doub N N 93  
GLN C   OXT  sing N N 94  
GLN CB  CG   sing N N 95  
GLN CB  HB2  sing N N 96  
GLN CB  HB3  sing N N 97  
GLN CG  CD   sing N N 98  
GLN CG  HG2  sing N N 99  
GLN CG  HG3  sing N N 100 
GLN CD  OE1  doub N N 101 
GLN CD  NE2  sing N N 102 
GLN NE2 HE21 sing N N 103 
GLN NE2 HE22 sing N N 104 
GLN OXT HXT  sing N N 105 
GLU N   CA   sing N N 106 
GLU N   H    sing N N 107 
GLU N   H2   sing N N 108 
GLU CA  C    sing N N 109 
GLU CA  CB   sing N N 110 
GLU CA  HA   sing N N 111 
GLU C   O    doub N N 112 
GLU C   OXT  sing N N 113 
GLU CB  CG   sing N N 114 
GLU CB  HB2  sing N N 115 
GLU CB  HB3  sing N N 116 
GLU CG  CD   sing N N 117 
GLU CG  HG2  sing N N 118 
GLU CG  HG3  sing N N 119 
GLU CD  OE1  doub N N 120 
GLU CD  OE2  sing N N 121 
GLU OE2 HE2  sing N N 122 
GLU OXT HXT  sing N N 123 
GLY N   CA   sing N N 124 
GLY N   H    sing N N 125 
GLY N   H2   sing N N 126 
GLY CA  C    sing N N 127 
GLY CA  HA2  sing N N 128 
GLY CA  HA3  sing N N 129 
GLY C   O    doub N N 130 
GLY C   OXT  sing N N 131 
GLY OXT HXT  sing N N 132 
GOL C1  O1   sing N N 133 
GOL C1  C2   sing N N 134 
GOL C1  H11  sing N N 135 
GOL C1  H12  sing N N 136 
GOL O1  HO1  sing N N 137 
GOL C2  O2   sing N N 138 
GOL C2  C3   sing N N 139 
GOL C2  H2   sing N N 140 
GOL O2  HO2  sing N N 141 
GOL C3  O3   sing N N 142 
GOL C3  H31  sing N N 143 
GOL C3  H32  sing N N 144 
GOL O3  HO3  sing N N 145 
HIS N   CA   sing N N 146 
HIS N   H    sing N N 147 
HIS N   H2   sing N N 148 
HIS CA  C    sing N N 149 
HIS CA  CB   sing N N 150 
HIS CA  HA   sing N N 151 
HIS C   O    doub N N 152 
HIS C   OXT  sing N N 153 
HIS CB  CG   sing N N 154 
HIS CB  HB2  sing N N 155 
HIS CB  HB3  sing N N 156 
HIS CG  ND1  sing Y N 157 
HIS CG  CD2  doub Y N 158 
HIS ND1 CE1  doub Y N 159 
HIS ND1 HD1  sing N N 160 
HIS CD2 NE2  sing Y N 161 
HIS CD2 HD2  sing N N 162 
HIS CE1 NE2  sing Y N 163 
HIS CE1 HE1  sing N N 164 
HIS NE2 HE2  sing N N 165 
HIS OXT HXT  sing N N 166 
HOH O   H1   sing N N 167 
HOH O   H2   sing N N 168 
ILE N   CA   sing N N 169 
ILE N   H    sing N N 170 
ILE N   H2   sing N N 171 
ILE CA  C    sing N N 172 
ILE CA  CB   sing N N 173 
ILE CA  HA   sing N N 174 
ILE C   O    doub N N 175 
ILE C   OXT  sing N N 176 
ILE CB  CG1  sing N N 177 
ILE CB  CG2  sing N N 178 
ILE CB  HB   sing N N 179 
ILE CG1 CD1  sing N N 180 
ILE CG1 HG12 sing N N 181 
ILE CG1 HG13 sing N N 182 
ILE CG2 HG21 sing N N 183 
ILE CG2 HG22 sing N N 184 
ILE CG2 HG23 sing N N 185 
ILE CD1 HD11 sing N N 186 
ILE CD1 HD12 sing N N 187 
ILE CD1 HD13 sing N N 188 
ILE OXT HXT  sing N N 189 
LEU N   CA   sing N N 190 
LEU N   H    sing N N 191 
LEU N   H2   sing N N 192 
LEU CA  C    sing N N 193 
LEU CA  CB   sing N N 194 
LEU CA  HA   sing N N 195 
LEU C   O    doub N N 196 
LEU C   OXT  sing N N 197 
LEU CB  CG   sing N N 198 
LEU CB  HB2  sing N N 199 
LEU CB  HB3  sing N N 200 
LEU CG  CD1  sing N N 201 
LEU CG  CD2  sing N N 202 
LEU CG  HG   sing N N 203 
LEU CD1 HD11 sing N N 204 
LEU CD1 HD12 sing N N 205 
LEU CD1 HD13 sing N N 206 
LEU CD2 HD21 sing N N 207 
LEU CD2 HD22 sing N N 208 
LEU CD2 HD23 sing N N 209 
LEU OXT HXT  sing N N 210 
LYS N   CA   sing N N 211 
LYS N   H    sing N N 212 
LYS N   H2   sing N N 213 
LYS CA  C    sing N N 214 
LYS CA  CB   sing N N 215 
LYS CA  HA   sing N N 216 
LYS C   O    doub N N 217 
LYS C   OXT  sing N N 218 
LYS CB  CG   sing N N 219 
LYS CB  HB2  sing N N 220 
LYS CB  HB3  sing N N 221 
LYS CG  CD   sing N N 222 
LYS CG  HG2  sing N N 223 
LYS CG  HG3  sing N N 224 
LYS CD  CE   sing N N 225 
LYS CD  HD2  sing N N 226 
LYS CD  HD3  sing N N 227 
LYS CE  NZ   sing N N 228 
LYS CE  HE2  sing N N 229 
LYS CE  HE3  sing N N 230 
LYS NZ  HZ1  sing N N 231 
LYS NZ  HZ2  sing N N 232 
LYS NZ  HZ3  sing N N 233 
LYS OXT HXT  sing N N 234 
MET N   CA   sing N N 235 
MET N   H    sing N N 236 
MET N   H2   sing N N 237 
MET CA  C    sing N N 238 
MET CA  CB   sing N N 239 
MET CA  HA   sing N N 240 
MET C   O    doub N N 241 
MET C   OXT  sing N N 242 
MET CB  CG   sing N N 243 
MET CB  HB2  sing N N 244 
MET CB  HB3  sing N N 245 
MET CG  SD   sing N N 246 
MET CG  HG2  sing N N 247 
MET CG  HG3  sing N N 248 
MET SD  CE   sing N N 249 
MET CE  HE1  sing N N 250 
MET CE  HE2  sing N N 251 
MET CE  HE3  sing N N 252 
MET OXT HXT  sing N N 253 
PEG C1  O1   sing N N 254 
PEG C1  C2   sing N N 255 
PEG C1  H11  sing N N 256 
PEG C1  H12  sing N N 257 
PEG O1  HO1  sing N N 258 
PEG C2  O2   sing N N 259 
PEG C2  H21  sing N N 260 
PEG C2  H22  sing N N 261 
PEG O2  C3   sing N N 262 
PEG C3  C4   sing N N 263 
PEG C3  H31  sing N N 264 
PEG C3  H32  sing N N 265 
PEG C4  O4   sing N N 266 
PEG C4  H41  sing N N 267 
PEG C4  H42  sing N N 268 
PEG O4  HO4  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
THR N   CA   sing N N 323 
THR N   H    sing N N 324 
THR N   H2   sing N N 325 
THR CA  C    sing N N 326 
THR CA  CB   sing N N 327 
THR CA  HA   sing N N 328 
THR C   O    doub N N 329 
THR C   OXT  sing N N 330 
THR CB  OG1  sing N N 331 
THR CB  CG2  sing N N 332 
THR CB  HB   sing N N 333 
THR OG1 HG1  sing N N 334 
THR CG2 HG21 sing N N 335 
THR CG2 HG22 sing N N 336 
THR CG2 HG23 sing N N 337 
THR OXT HXT  sing N N 338 
TRP N   CA   sing N N 339 
TRP N   H    sing N N 340 
TRP N   H2   sing N N 341 
TRP CA  C    sing N N 342 
TRP CA  CB   sing N N 343 
TRP CA  HA   sing N N 344 
TRP C   O    doub N N 345 
TRP C   OXT  sing N N 346 
TRP CB  CG   sing N N 347 
TRP CB  HB2  sing N N 348 
TRP CB  HB3  sing N N 349 
TRP CG  CD1  doub Y N 350 
TRP CG  CD2  sing Y N 351 
TRP CD1 NE1  sing Y N 352 
TRP CD1 HD1  sing N N 353 
TRP CD2 CE2  doub Y N 354 
TRP CD2 CE3  sing Y N 355 
TRP NE1 CE2  sing Y N 356 
TRP NE1 HE1  sing N N 357 
TRP CE2 CZ2  sing Y N 358 
TRP CE3 CZ3  doub Y N 359 
TRP CE3 HE3  sing N N 360 
TRP CZ2 CH2  doub Y N 361 
TRP CZ2 HZ2  sing N N 362 
TRP CZ3 CH2  sing Y N 363 
TRP CZ3 HZ3  sing N N 364 
TRP CH2 HH2  sing N N 365 
TRP OXT HXT  sing N N 366 
TYR N   CA   sing N N 367 
TYR N   H    sing N N 368 
TYR N   H2   sing N N 369 
TYR CA  C    sing N N 370 
TYR CA  CB   sing N N 371 
TYR CA  HA   sing N N 372 
TYR C   O    doub N N 373 
TYR C   OXT  sing N N 374 
TYR CB  CG   sing N N 375 
TYR CB  HB2  sing N N 376 
TYR CB  HB3  sing N N 377 
TYR CG  CD1  doub Y N 378 
TYR CG  CD2  sing Y N 379 
TYR CD1 CE1  sing Y N 380 
TYR CD1 HD1  sing N N 381 
TYR CD2 CE2  doub Y N 382 
TYR CD2 HD2  sing N N 383 
TYR CE1 CZ   doub Y N 384 
TYR CE1 HE1  sing N N 385 
TYR CE2 CZ   sing Y N 386 
TYR CE2 HE2  sing N N 387 
TYR CZ  OH   sing N N 388 
TYR OH  HH   sing N N 389 
TYR OXT HXT  sing N N 390 
VAL N   CA   sing N N 391 
VAL N   H    sing N N 392 
VAL N   H2   sing N N 393 
VAL CA  C    sing N N 394 
VAL CA  CB   sing N N 395 
VAL CA  HA   sing N N 396 
VAL C   O    doub N N 397 
VAL C   OXT  sing N N 398 
VAL CB  CG1  sing N N 399 
VAL CB  CG2  sing N N 400 
VAL CB  HB   sing N N 401 
VAL CG1 HG11 sing N N 402 
VAL CG1 HG12 sing N N 403 
VAL CG1 HG13 sing N N 404 
VAL CG2 HG21 sing N N 405 
VAL CG2 HG22 sing N N 406 
VAL CG2 HG23 sing N N 407 
VAL OXT HXT  sing N N 408 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan 19H05771                          1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP20K22561                        2 
'Japan Science and Technology'                      Japan JPMJSP2108                        3 
'Other private'                                     ?     'Japan Science Society 2023-4016' 4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 4 2 2' 
_space_group.name_Hall        'I 4 2' 
_space_group.IT_number        97 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Y4Y 
_atom_sites.fract_transf_matrix[1][1]   0.009951 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009951 
_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]   0.004855 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG A 1 1   ? 24.220 28.323 52.963 1.00 63.45  ? 23  ARG A N   1 
ATOM   2    C  CA  . ARG A 1 1   ? 24.125 28.892 51.617 1.00 74.51  ? 23  ARG A CA  1 
ATOM   3    C  C   . ARG A 1 1   ? 25.409 28.721 50.818 1.00 75.47  ? 23  ARG A C   1 
ATOM   4    O  O   . ARG A 1 1   ? 26.504 28.902 51.349 1.00 79.54  ? 23  ARG A O   1 
ATOM   5    C  CB  . ARG A 1 1   ? 23.780 30.376 51.681 1.00 43.33  ? 23  ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 1   ? 22.380 30.677 52.153 1.00 75.06  ? 23  ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 1   ? 22.210 32.171 52.334 1.00 59.59  ? 23  ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 1   ? 23.215 32.708 53.243 1.00 70.15  ? 23  ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 1   ? 23.485 33.998 53.377 1.00 72.42  ? 23  ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 1   ? 22.833 34.914 52.683 1.00 76.73  ? 23  ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 1   ? 24.444 34.378 54.215 1.00 78.93  ? 23  ARG A NH2 1 
ATOM   12   N  N   . SER A 1 2   ? 25.267 28.397 49.532 1.00 78.81  ? 24  SER A N   1 
ATOM   13   C  CA  . SER A 1 2   ? 26.420 28.179 48.669 1.00 65.92  ? 24  SER A CA  1 
ATOM   14   C  C   . SER A 1 2   ? 26.024 28.416 47.216 1.00 72.39  ? 24  SER A C   1 
ATOM   15   O  O   . SER A 1 2   ? 24.927 28.036 46.799 1.00 75.28  ? 24  SER A O   1 
ATOM   16   C  CB  . SER A 1 2   ? 26.973 26.760 48.848 1.00 56.81  ? 24  SER A CB  1 
ATOM   17   O  OG  . SER A 1 2   ? 28.258 26.631 48.269 1.00 84.63  ? 24  SER A OG  1 
ATOM   18   N  N   . VAL A 1 3   ? 26.919 29.057 46.454 1.00 60.98  ? 25  VAL A N   1 
ATOM   19   C  CA  . VAL A 1 3   ? 26.746 29.252 45.019 1.00 61.81  ? 25  VAL A CA  1 
ATOM   20   C  C   . VAL A 1 3   ? 28.035 28.888 44.303 1.00 55.10  ? 25  VAL A C   1 
ATOM   21   O  O   . VAL A 1 3   ? 29.108 28.782 44.902 1.00 60.57  ? 25  VAL A O   1 
ATOM   22   C  CB  . VAL A 1 3   ? 26.351 30.697 44.626 1.00 52.39  ? 25  VAL A CB  1 
ATOM   23   C  CG1 . VAL A 1 3   ? 24.867 30.926 44.802 1.00 61.29  ? 25  VAL A CG1 1 
ATOM   24   C  CG2 . VAL A 1 3   ? 27.170 31.717 45.407 1.00 77.29  ? 25  VAL A CG2 1 
ATOM   25   N  N   . GLN A 1 4   ? 27.911 28.717 42.995 1.00 58.94  ? 26  GLN A N   1 
ATOM   26   C  CA  . GLN A 1 4   ? 29.053 28.570 42.108 1.00 60.66  ? 26  GLN A CA  1 
ATOM   27   C  C   . GLN A 1 4   ? 29.233 29.894 41.369 1.00 55.62  ? 26  GLN A C   1 
ATOM   28   O  O   . GLN A 1 4   ? 28.393 30.268 40.544 1.00 49.44  ? 26  GLN A O   1 
ATOM   29   C  CB  . GLN A 1 4   ? 28.844 27.402 41.143 1.00 58.44  ? 26  GLN A CB  1 
ATOM   30   C  CG  . GLN A 1 4   ? 28.990 26.026 41.792 1.00 55.73  ? 26  GLN A CG  1 
ATOM   31   C  CD  . GLN A 1 4   ? 30.378 25.807 42.382 1.00 71.32  ? 26  GLN A CD  1 
ATOM   32   O  OE1 . GLN A 1 4   ? 30.528 25.544 43.579 1.00 60.70  ? 26  GLN A OE1 1 
ATOM   33   N  NE2 . GLN A 1 4   ? 31.400 25.918 41.539 1.00 74.65  ? 26  GLN A NE2 1 
ATOM   34   N  N   . ASP A 1 5   ? 30.297 30.630 41.695 1.00 56.42  ? 27  ASP A N   1 
ATOM   35   C  CA  . ASP A 1 5   ? 30.626 31.832 40.947 1.00 56.51  ? 27  ASP A CA  1 
ATOM   36   C  C   . ASP A 1 5   ? 31.701 31.503 39.915 1.00 57.41  ? 27  ASP A C   1 
ATOM   37   O  O   . ASP A 1 5   ? 32.011 30.336 39.656 1.00 62.37  ? 27  ASP A O   1 
ATOM   38   C  CB  . ASP A 1 5   ? 31.043 32.979 41.878 1.00 50.39  ? 27  ASP A CB  1 
ATOM   39   C  CG  . ASP A 1 5   ? 32.345 32.714 42.610 1.00 57.39  ? 27  ASP A CG  1 
ATOM   40   O  OD1 . ASP A 1 5   ? 32.891 31.594 42.510 1.00 73.30  ? 27  ASP A OD1 1 
ATOM   41   O  OD2 . ASP A 1 5   ? 32.818 33.641 43.303 1.00 58.69  ? 27  ASP A OD2 1 
ATOM   42   N  N   . GLU A 1 6   ? 32.290 32.539 39.324 1.00 66.32  ? 28  GLU A N   1 
ATOM   43   C  CA  . GLU A 1 6   ? 33.202 32.296 38.211 1.00 62.94  ? 28  GLU A CA  1 
ATOM   44   C  C   . GLU A 1 6   ? 34.554 31.774 38.649 1.00 54.76  ? 28  GLU A C   1 
ATOM   45   O  O   . GLU A 1 6   ? 35.420 31.602 37.787 1.00 63.88  ? 28  GLU A O   1 
ATOM   46   C  CB  . GLU A 1 6   ? 33.361 33.571 37.380 1.00 58.47  ? 28  GLU A CB  1 
ATOM   47   C  CG  . GLU A 1 6   ? 32.112 33.919 36.576 1.00 53.23  ? 28  GLU A CG  1 
ATOM   48   C  CD  . GLU A 1 6   ? 31.586 32.739 35.775 1.00 62.12  ? 28  GLU A CD  1 
ATOM   49   O  OE1 . GLU A 1 6   ? 32.380 32.115 35.035 1.00 62.38  ? 28  GLU A OE1 1 
ATOM   50   O  OE2 . GLU A 1 6   ? 30.382 32.430 35.894 1.00 60.47  ? 28  GLU A OE2 1 
ATOM   51   N  N   . GLN A 1 7   ? 34.748 31.501 39.941 1.00 56.82  ? 29  GLN A N   1 
ATOM   52   C  CA  . GLN A 1 7   ? 35.973 30.886 40.432 1.00 71.80  ? 29  GLN A CA  1 
ATOM   53   C  C   . GLN A 1 7   ? 35.723 29.596 41.189 1.00 63.66  ? 29  GLN A C   1 
ATOM   54   O  O   . GLN A 1 7   ? 36.667 29.036 41.758 1.00 52.29  ? 29  GLN A O   1 
ATOM   55   C  CB  . GLN A 1 7   ? 36.729 31.838 41.344 1.00 56.02  ? 29  GLN A CB  1 
ATOM   56   C  CG  . GLN A 1 7   ? 37.383 32.954 40.618 1.00 107.71 ? 29  GLN A CG  1 
ATOM   57   C  CD  . GLN A 1 7   ? 37.522 34.135 41.513 1.00 131.05 ? 29  GLN A CD  1 
ATOM   58   O  OE1 . GLN A 1 7   ? 36.815 34.232 42.514 1.00 127.74 ? 29  GLN A OE1 1 
ATOM   59   N  NE2 . GLN A 1 7   ? 38.422 35.047 41.171 1.00 130.48 ? 29  GLN A NE2 1 
ATOM   60   N  N   . GLY A 1 8   ? 34.488 29.123 41.232 1.00 63.23  ? 30  GLY A N   1 
ATOM   61   C  CA  . GLY A 1 8   ? 34.187 27.940 42.001 1.00 49.44  ? 30  GLY A CA  1 
ATOM   62   C  C   . GLY A 1 8   ? 33.126 28.209 43.038 1.00 58.34  ? 30  GLY A C   1 
ATOM   63   O  O   . GLY A 1 8   ? 32.084 28.795 42.735 1.00 70.01  ? 30  GLY A O   1 
ATOM   64   N  N   . THR A 1 9   ? 33.396 27.814 44.275 1.00 62.76  ? 31  THR A N   1 
ATOM   65   C  CA  . THR A 1 9   ? 32.404 27.821 45.337 1.00 57.69  ? 31  THR A CA  1 
ATOM   66   C  C   . THR A 1 9   ? 32.517 29.095 46.162 1.00 64.12  ? 31  THR A C   1 
ATOM   67   O  O   . THR A 1 9   ? 33.618 29.490 46.561 1.00 59.09  ? 31  THR A O   1 
ATOM   68   C  CB  . THR A 1 9   ? 32.583 26.600 46.235 1.00 70.52  ? 31  THR A CB  1 
ATOM   69   O  OG1 . THR A 1 9   ? 32.496 25.411 45.439 1.00 82.97  ? 31  THR A OG1 1 
ATOM   70   C  CG2 . THR A 1 9   ? 31.515 26.572 47.314 1.00 59.31  ? 31  THR A CG2 1 
ATOM   71   N  N   . PHE A 1 10  ? 31.376 29.727 46.416 1.00 62.34  ? 32  PHE A N   1 
ATOM   72   C  CA  . PHE A 1 10  ? 31.278 30.843 47.345 1.00 63.61  ? 32  PHE A CA  1 
ATOM   73   C  C   . PHE A 1 10  ? 30.297 30.454 48.443 1.00 70.43  ? 32  PHE A C   1 
ATOM   74   O  O   . PHE A 1 10  ? 29.149 30.101 48.151 1.00 65.95  ? 32  PHE A O   1 
ATOM   75   C  CB  . PHE A 1 10  ? 30.824 32.118 46.627 1.00 45.52  ? 32  PHE A CB  1 
ATOM   76   C  CG  . PHE A 1 10  ? 30.623 33.288 47.547 1.00 55.33  ? 32  PHE A CG  1 
ATOM   77   C  CD1 . PHE A 1 10  ? 31.687 34.100 47.902 1.00 58.95  ? 32  PHE A CD1 1 
ATOM   78   C  CD2 . PHE A 1 10  ? 29.367 33.568 48.066 1.00 41.11  ? 32  PHE A CD2 1 
ATOM   79   C  CE1 . PHE A 1 10  ? 31.505 35.174 48.756 1.00 57.32  ? 32  PHE A CE1 1 
ATOM   80   C  CE2 . PHE A 1 10  ? 29.178 34.637 48.922 1.00 44.75  ? 32  PHE A CE2 1 
ATOM   81   C  CZ  . PHE A 1 10  ? 30.249 35.443 49.266 1.00 59.82  ? 32  PHE A CZ  1 
ATOM   82   N  N   . GLU A 1 11  ? 30.748 30.502 49.698 1.00 75.22  ? 33  GLU A N   1 
ATOM   83   C  CA  . GLU A 1 11  ? 29.913 30.141 50.839 1.00 67.74  ? 33  GLU A CA  1 
ATOM   84   C  C   . GLU A 1 11  ? 29.772 31.317 51.797 1.00 65.36  ? 33  GLU A C   1 
ATOM   85   O  O   . GLU A 1 11  ? 30.712 32.089 52.006 1.00 67.65  ? 33  GLU A O   1 
ATOM   86   C  CB  . GLU A 1 11  ? 30.480 28.943 51.609 1.00 75.19  ? 33  GLU A CB  1 
ATOM   87   C  CG  . GLU A 1 11  ? 30.437 27.634 50.847 1.00 100.98 ? 33  GLU A CG  1 
ATOM   88   C  CD  . GLU A 1 11  ? 30.277 26.423 51.754 1.00 110.07 ? 33  GLU A CD  1 
ATOM   89   O  OE1 . GLU A 1 11  ? 29.349 26.418 52.595 1.00 100.33 ? 33  GLU A OE1 1 
ATOM   90   O  OE2 . GLU A 1 11  ? 31.079 25.474 51.620 1.00 94.97  ? 33  GLU A OE2 1 
ATOM   91   N  N   . LEU A 1 12  ? 28.589 31.432 52.391 1.00 62.00  ? 34  LEU A N   1 
ATOM   92   C  CA  . LEU A 1 12  ? 28.323 32.465 53.378 1.00 65.44  ? 34  LEU A CA  1 
ATOM   93   C  C   . LEU A 1 12  ? 27.388 31.907 54.438 1.00 65.47  ? 34  LEU A C   1 
ATOM   94   O  O   . LEU A 1 12  ? 26.403 31.237 54.113 1.00 62.23  ? 34  LEU A O   1 
ATOM   95   C  CB  . LEU A 1 12  ? 27.707 33.711 52.730 1.00 63.18  ? 34  LEU A CB  1 
ATOM   96   C  CG  . LEU A 1 12  ? 28.548 34.985 52.762 1.00 53.13  ? 34  LEU A CG  1 
ATOM   97   C  CD1 . LEU A 1 12  ? 27.704 36.175 52.335 1.00 67.53  ? 34  LEU A CD1 1 
ATOM   98   C  CD2 . LEU A 1 12  ? 29.138 35.212 54.148 1.00 51.61  ? 34  LEU A CD2 1 
ATOM   99   N  N   . GLU A 1 13  ? 27.708 32.171 55.703 1.00 66.48  ? 35  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 13  ? 26.850 31.787 56.818 1.00 68.94  ? 35  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 13  ? 25.969 32.950 57.258 1.00 66.18  ? 35  GLU A C   1 
ATOM   102  O  O   . GLU A 1 13  ? 24.739 32.848 57.244 1.00 55.16  ? 35  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 13  ? 27.699 31.283 57.993 1.00 90.84  ? 35  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 13  ? 27.752 29.769 58.128 1.00 112.07 ? 35  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 13  ? 26.829 29.246 59.216 1.00 121.23 ? 35  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 13  ? 26.951 29.705 60.373 1.00 107.63 ? 35  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 13  ? 25.978 28.382 58.912 1.00 123.72 ? 35  GLU A OE2 1 
ATOM   108  N  N   . ALA A 1 14  ? 26.582 34.065 57.638 1.00 66.61  ? 36  ALA A N   1 
ATOM   109  C  CA  . ALA A 1 14  ? 25.821 35.201 58.122 1.00 54.35  ? 36  ALA A CA  1 
ATOM   110  C  C   . ALA A 1 14  ? 25.151 35.935 56.964 1.00 58.06  ? 36  ALA A C   1 
ATOM   111  O  O   . ALA A 1 14  ? 25.584 35.866 55.810 1.00 59.95  ? 36  ALA A O   1 
ATOM   112  C  CB  . ALA A 1 14  ? 26.727 36.152 58.901 1.00 53.32  ? 36  ALA A CB  1 
ATOM   113  N  N   . ILE A 1 15  ? 24.072 36.640 57.291 1.00 58.00  ? 37  ILE A N   1 
ATOM   114  C  CA  . ILE A 1 15  ? 23.385 37.515 56.345 1.00 54.50  ? 37  ILE A CA  1 
ATOM   115  C  C   . ILE A 1 15  ? 24.188 38.804 56.192 1.00 64.29  ? 37  ILE A C   1 
ATOM   116  O  O   . ILE A 1 15  ? 24.357 39.548 57.170 1.00 67.21  ? 37  ILE A O   1 
ATOM   117  C  CB  . ILE A 1 15  ? 21.949 37.816 56.802 1.00 58.63  ? 37  ILE A CB  1 
ATOM   118  C  CG1 . ILE A 1 15  ? 21.095 36.545 56.767 1.00 45.62  ? 37  ILE A CG1 1 
ATOM   119  C  CG2 . ILE A 1 15  ? 21.333 38.915 55.940 1.00 44.10  ? 37  ILE A CG2 1 
ATOM   120  C  CD1 . ILE A 1 15  ? 20.825 36.031 55.372 1.00 59.36  ? 37  ILE A CD1 1 
ATOM   121  N  N   . PRO A 1 16  ? 24.693 39.111 54.996 1.00 60.42  ? 38  PRO A N   1 
ATOM   122  C  CA  . PRO A 1 16  ? 25.489 40.335 54.817 1.00 58.98  ? 38  PRO A CA  1 
ATOM   123  C  C   . PRO A 1 16  ? 24.620 41.582 54.911 1.00 61.14  ? 38  PRO A C   1 
ATOM   124  O  O   . PRO A 1 16  ? 23.580 41.684 54.256 1.00 61.51  ? 38  PRO A O   1 
ATOM   125  C  CB  . PRO A 1 16  ? 26.083 40.164 53.415 1.00 51.41  ? 38  PRO A CB  1 
ATOM   126  C  CG  . PRO A 1 16  ? 25.117 39.262 52.710 1.00 51.90  ? 38  PRO A CG  1 
ATOM   127  C  CD  . PRO A 1 16  ? 24.601 38.320 53.756 1.00 64.97  ? 38  PRO A CD  1 
ATOM   128  N  N   . GLN A 1 17  ? 25.059 42.538 55.726 1.00 49.73  ? 39  GLN A N   1 
ATOM   129  C  CA  . GLN A 1 17  ? 24.317 43.776 55.939 1.00 70.58  ? 39  GLN A CA  1 
ATOM   130  C  C   . GLN A 1 17  ? 24.841 44.925 55.093 1.00 70.07  ? 39  GLN A C   1 
ATOM   131  O  O   . GLN A 1 17  ? 24.050 45.687 54.526 1.00 67.82  ? 39  GLN A O   1 
ATOM   132  C  CB  . GLN A 1 17  ? 24.365 44.176 57.419 1.00 80.96  ? 39  GLN A CB  1 
ATOM   133  C  CG  . GLN A 1 17  ? 23.797 43.140 58.383 1.00 84.75  ? 39  GLN A CG  1 
ATOM   134  C  CD  . GLN A 1 17  ? 22.301 43.276 58.582 1.00 84.69  ? 39  GLN A CD  1 
ATOM   135  O  OE1 . GLN A 1 17  ? 21.835 44.185 59.272 1.00 106.38 ? 39  GLN A OE1 1 
ATOM   136  N  NE2 . GLN A 1 17  ? 21.539 42.370 57.981 1.00 91.24  ? 39  GLN A NE2 1 
ATOM   137  N  N   . ARG A 1 18  ? 26.160 45.061 55.000 1.00 54.19  ? 40  ARG A N   1 
ATOM   138  C  CA  . ARG A 1 18  ? 26.812 46.117 54.237 1.00 54.04  ? 40  ARG A CA  1 
ATOM   139  C  C   . ARG A 1 18  ? 27.407 45.497 52.978 1.00 52.45  ? 40  ARG A C   1 
ATOM   140  O  O   . ARG A 1 18  ? 28.415 44.785 53.043 1.00 67.97  ? 40  ARG A O   1 
ATOM   141  C  CB  . ARG A 1 18  ? 27.880 46.804 55.084 1.00 58.50  ? 40  ARG A CB  1 
ATOM   142  C  CG  . ARG A 1 18  ? 27.333 47.317 56.404 1.00 52.35  ? 40  ARG A CG  1 
ATOM   143  C  CD  . ARG A 1 18  ? 28.399 48.005 57.233 1.00 51.43  ? 40  ARG A CD  1 
ATOM   144  N  NE  . ARG A 1 18  ? 29.045 49.087 56.499 1.00 65.66  ? 40  ARG A NE  1 
ATOM   145  C  CZ  . ARG A 1 18  ? 28.547 50.309 56.373 1.00 65.50  ? 40  ARG A CZ  1 
ATOM   146  N  NH1 . ARG A 1 18  ? 27.388 50.643 56.917 1.00 58.05  ? 40  ARG A NH1 1 
ATOM   147  N  NH2 . ARG A 1 18  ? 29.229 51.219 55.684 1.00 65.17  ? 40  ARG A NH2 1 
ATOM   148  N  N   . ILE A 1 19  ? 26.779 45.766 51.835 1.00 48.45  ? 41  ILE A N   1 
ATOM   149  C  CA  . ILE A 1 19  ? 27.169 45.184 50.557 1.00 40.48  ? 41  ILE A CA  1 
ATOM   150  C  C   . ILE A 1 19  ? 27.789 46.265 49.688 1.00 46.86  ? 41  ILE A C   1 
ATOM   151  O  O   . ILE A 1 19  ? 27.237 47.364 49.561 1.00 42.38  ? 41  ILE A O   1 
ATOM   152  C  CB  . ILE A 1 19  ? 25.970 44.547 49.840 1.00 45.96  ? 41  ILE A CB  1 
ATOM   153  C  CG1 . ILE A 1 19  ? 25.292 43.538 50.762 1.00 55.90  ? 41  ILE A CG1 1 
ATOM   154  C  CG2 . ILE A 1 19  ? 26.423 43.911 48.535 1.00 29.07  ? 41  ILE A CG2 1 
ATOM   155  C  CD1 . ILE A 1 19  ? 24.084 42.895 50.155 1.00 46.27  ? 41  ILE A CD1 1 
ATOM   156  N  N   . VAL A 1 20  ? 28.926 45.943 49.079 1.00 49.87  ? 42  VAL A N   1 
ATOM   157  C  CA  . VAL A 1 20  ? 29.593 46.802 48.110 1.00 45.68  ? 42  VAL A CA  1 
ATOM   158  C  C   . VAL A 1 20  ? 29.603 46.069 46.779 1.00 48.51  ? 42  VAL A C   1 
ATOM   159  O  O   . VAL A 1 20  ? 30.126 44.952 46.684 1.00 42.31  ? 42  VAL A O   1 
ATOM   160  C  CB  . VAL A 1 20  ? 31.022 47.153 48.546 1.00 48.61  ? 42  VAL A CB  1 
ATOM   161  C  CG1 . VAL A 1 20  ? 31.780 47.816 47.404 1.00 46.77  ? 42  VAL A CG1 1 
ATOM   162  C  CG2 . VAL A 1 20  ? 30.988 48.042 49.769 1.00 37.68  ? 42  VAL A CG2 1 
ATOM   163  N  N   . VAL A 1 21  ? 29.022 46.686 45.756 1.00 38.64  ? 43  VAL A N   1 
ATOM   164  C  CA  . VAL A 1 21  ? 28.955 46.096 44.427 1.00 51.76  ? 43  VAL A CA  1 
ATOM   165  C  C   . VAL A 1 21  ? 29.824 46.920 43.489 1.00 46.85  ? 43  VAL A C   1 
ATOM   166  O  O   . VAL A 1 21  ? 29.930 48.144 43.631 1.00 48.53  ? 43  VAL A O   1 
ATOM   167  C  CB  . VAL A 1 21  ? 27.503 46.000 43.920 1.00 47.45  ? 43  VAL A CB  1 
ATOM   168  C  CG1 . VAL A 1 21  ? 26.704 45.075 44.825 1.00 48.24  ? 43  VAL A CG1 1 
ATOM   169  C  CG2 . VAL A 1 21  ? 26.859 47.371 43.865 1.00 51.75  ? 43  VAL A CG2 1 
ATOM   170  N  N   . LEU A 1 22  ? 30.463 46.242 42.540 1.00 52.45  ? 44  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 22  ? 31.415 46.890 41.652 1.00 55.68  ? 44  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 22  ? 30.897 47.015 40.227 1.00 55.59  ? 44  LEU A C   1 
ATOM   173  O  O   . LEU A 1 22  ? 31.679 47.332 39.324 1.00 50.78  ? 44  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 22  ? 32.747 46.138 41.674 1.00 39.82  ? 44  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 22  ? 33.355 46.002 43.070 1.00 38.52  ? 44  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 22  ? 34.737 45.387 43.002 1.00 40.39  ? 44  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 22  ? 33.405 47.367 43.748 1.00 31.28  ? 44  LEU A CD2 1 
ATOM   178  N  N   . GLU A 1 23  ? 29.601 46.788 40.006 1.00 46.62  ? 45  GLU A N   1 
ATOM   179  C  CA  . GLU A 1 23  ? 28.995 46.998 38.698 1.00 47.08  ? 45  GLU A CA  1 
ATOM   180  C  C   . GLU A 1 23  ? 27.535 47.382 38.840 1.00 47.52  ? 45  GLU A C   1 
ATOM   181  O  O   . GLU A 1 23  ? 26.928 47.246 39.903 1.00 54.02  ? 45  GLU A O   1 
ATOM   182  C  CB  . GLU A 1 23  ? 29.083 45.772 37.825 1.00 45.16  ? 45  GLU A CB  1 
ATOM   183  C  CG  . GLU A 1 23  ? 30.381 45.678 37.153 1.00 68.72  ? 45  GLU A CG  1 
ATOM   184  C  CD  . GLU A 1 23  ? 30.357 44.647 36.105 1.00 104.64 ? 45  GLU A CD  1 
ATOM   185  O  OE1 . GLU A 1 23  ? 30.109 43.471 36.453 1.00 125.45 ? 45  GLU A OE1 1 
ATOM   186  O  OE2 . GLU A 1 23  ? 30.563 45.022 34.934 1.00 103.35 ? 45  GLU A OE2 1 
ATOM   187  N  N   . PHE A 1 24  ? 26.962 47.831 37.727 1.00 44.11  ? 46  PHE A N   1 
ATOM   188  C  CA  . PHE A 1 24  ? 25.603 48.348 37.779 1.00 51.02  ? 46  PHE A CA  1 
ATOM   189  C  C   . PHE A 1 24  ? 24.566 47.238 37.747 1.00 51.53  ? 46  PHE A C   1 
ATOM   190  O  O   . PHE A 1 24  ? 23.490 47.393 38.334 1.00 55.13  ? 46  PHE A O   1 
ATOM   191  C  CB  . PHE A 1 24  ? 25.366 49.319 36.630 1.00 51.74  ? 46  PHE A CB  1 
ATOM   192  C  CG  . PHE A 1 24  ? 26.240 50.523 36.678 1.00 49.12  ? 46  PHE A CG  1 
ATOM   193  C  CD1 . PHE A 1 24  ? 26.580 51.105 37.886 1.00 54.99  ? 46  PHE A CD1 1 
ATOM   194  C  CD2 . PHE A 1 24  ? 26.736 51.071 35.509 1.00 57.08  ? 46  PHE A CD2 1 
ATOM   195  C  CE1 . PHE A 1 24  ? 27.393 52.226 37.924 1.00 48.05  ? 46  PHE A CE1 1 
ATOM   196  C  CE2 . PHE A 1 24  ? 27.544 52.185 35.540 1.00 50.47  ? 46  PHE A CE2 1 
ATOM   197  C  CZ  . PHE A 1 24  ? 27.877 52.764 36.747 1.00 49.15  ? 46  PHE A CZ  1 
ATOM   198  N  N   . SER A 1 25  ? 24.863 46.122 37.075 1.00 54.73  ? 47  SER A N   1 
ATOM   199  C  CA  . SER A 1 25  ? 23.931 44.999 37.068 1.00 51.29  ? 47  SER A CA  1 
ATOM   200  C  C   . SER A 1 25  ? 23.671 44.496 38.479 1.00 53.64  ? 47  SER A C   1 
ATOM   201  O  O   . SER A 1 25  ? 22.548 44.098 38.812 1.00 44.59  ? 47  SER A O   1 
ATOM   202  C  CB  . SER A 1 25  ? 24.481 43.868 36.202 1.00 38.62  ? 47  SER A CB  1 
ATOM   203  O  OG  . SER A 1 25  ? 25.678 43.361 36.765 1.00 58.37  ? 47  SER A OG  1 
ATOM   204  N  N   . PHE A 1 26  ? 24.703 44.509 39.321 1.00 55.02  ? 48  PHE A N   1 
ATOM   205  C  CA  . PHE A 1 26  ? 24.544 44.056 40.694 1.00 46.39  ? 48  PHE A CA  1 
ATOM   206  C  C   . PHE A 1 26  ? 23.666 45.008 41.486 1.00 56.07  ? 48  PHE A C   1 
ATOM   207  O  O   . PHE A 1 26  ? 22.910 44.569 42.360 1.00 58.10  ? 48  PHE A O   1 
ATOM   208  C  CB  . PHE A 1 26  ? 25.914 43.911 41.353 1.00 49.51  ? 48  PHE A CB  1 
ATOM   209  C  CG  . PHE A 1 26  ? 26.878 43.060 40.569 1.00 41.43  ? 48  PHE A CG  1 
ATOM   210  C  CD1 . PHE A 1 26  ? 26.421 42.061 39.718 1.00 38.27  ? 48  PHE A CD1 1 
ATOM   211  C  CD2 . PHE A 1 26  ? 28.245 43.258 40.685 1.00 52.27  ? 48  PHE A CD2 1 
ATOM   212  C  CE1 . PHE A 1 26  ? 27.309 41.276 39.002 1.00 46.64  ? 48  PHE A CE1 1 
ATOM   213  C  CE2 . PHE A 1 26  ? 29.137 42.474 39.971 1.00 49.41  ? 48  PHE A CE2 1 
ATOM   214  C  CZ  . PHE A 1 26  ? 28.669 41.484 39.130 1.00 38.26  ? 48  PHE A CZ  1 
ATOM   215  N  N   . VAL A 1 27  ? 23.743 46.308 41.184 1.00 43.81  ? 49  VAL A N   1 
ATOM   216  C  CA  . VAL A 1 27  ? 22.835 47.268 41.803 1.00 51.75  ? 49  VAL A CA  1 
ATOM   217  C  C   . VAL A 1 27  ? 21.390 46.928 41.470 1.00 63.06  ? 49  VAL A C   1 
ATOM   218  O  O   . VAL A 1 27  ? 20.491 47.122 42.298 1.00 54.03  ? 49  VAL A O   1 
ATOM   219  C  CB  . VAL A 1 27  ? 23.172 48.708 41.369 1.00 60.07  ? 49  VAL A CB  1 
ATOM   220  C  CG1 . VAL A 1 27  ? 22.345 49.686 42.172 1.00 40.51  ? 49  VAL A CG1 1 
ATOM   221  C  CG2 . VAL A 1 27  ? 24.659 49.007 41.531 1.00 44.77  ? 49  VAL A CG2 1 
ATOM   222  N  N   . ASP A 1 28  ? 21.136 46.429 40.258 1.00 58.88  ? 50  ASP A N   1 
ATOM   223  C  CA  . ASP A 1 28  ? 19.782 46.015 39.905 1.00 65.81  ? 50  ASP A CA  1 
ATOM   224  C  C   . ASP A 1 28  ? 19.329 44.848 40.771 1.00 56.22  ? 50  ASP A C   1 
ATOM   225  O  O   . ASP A 1 28  ? 18.258 44.901 41.387 1.00 64.78  ? 50  ASP A O   1 
ATOM   226  C  CB  . ASP A 1 28  ? 19.711 45.640 38.428 1.00 75.91  ? 50  ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 28  ? 18.403 44.968 38.056 1.00 71.53  ? 50  ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 28  ? 17.339 45.622 38.133 1.00 79.68  ? 50  ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 28  ? 18.442 43.782 37.675 1.00 84.19  ? 50  ASP A OD2 1 
ATOM   230  N  N   . ALA A 1 29  ? 20.138 43.782 40.830 1.00 55.28  ? 51  ALA A N   1 
ATOM   231  C  CA  . ALA A 1 29  ? 19.761 42.597 41.595 1.00 60.53  ? 51  ALA A CA  1 
ATOM   232  C  C   . ALA A 1 29  ? 19.442 42.949 43.042 1.00 47.64  ? 51  ALA A C   1 
ATOM   233  O  O   . ALA A 1 29  ? 18.443 42.476 43.597 1.00 62.47  ? 51  ALA A O   1 
ATOM   234  C  CB  . ALA A 1 29  ? 20.876 41.555 41.529 1.00 46.77  ? 51  ALA A CB  1 
ATOM   235  N  N   . LEU A 1 30  ? 20.266 43.794 43.664 1.00 49.43  ? 52  LEU A N   1 
ATOM   236  C  CA  . LEU A 1 30  ? 19.988 44.196 45.037 1.00 47.06  ? 52  LEU A CA  1 
ATOM   237  C  C   . LEU A 1 30  ? 18.713 45.027 45.126 1.00 56.74  ? 52  LEU A C   1 
ATOM   238  O  O   . LEU A 1 30  ? 17.896 44.820 46.030 1.00 61.33  ? 52  LEU A O   1 
ATOM   239  C  CB  . LEU A 1 30  ? 21.175 44.964 45.612 1.00 37.28  ? 52  LEU A CB  1 
ATOM   240  C  CG  . LEU A 1 30  ? 22.493 44.202 45.743 1.00 53.00  ? 52  LEU A CG  1 
ATOM   241  C  CD1 . LEU A 1 30  ? 23.497 45.093 46.466 1.00 51.36  ? 52  LEU A CD1 1 
ATOM   242  C  CD2 . LEU A 1 30  ? 22.308 42.867 46.478 1.00 42.22  ? 52  LEU A CD2 1 
ATOM   243  N  N   . ALA A 1 31  ? 18.520 45.965 44.192 1.00 63.85  ? 53  ALA A N   1 
ATOM   244  C  CA  . ALA A 1 31  ? 17.332 46.814 44.230 1.00 58.02  ? 53  ALA A CA  1 
ATOM   245  C  C   . ALA A 1 31  ? 16.055 46.014 44.002 1.00 73.46  ? 53  ALA A C   1 
ATOM   246  O  O   . ALA A 1 31  ? 14.997 46.375 44.531 1.00 64.95  ? 53  ALA A O   1 
ATOM   247  C  CB  . ALA A 1 31  ? 17.448 47.933 43.193 1.00 49.45  ? 53  ALA A CB  1 
ATOM   248  N  N   . ALA A 1 32  ? 16.133 44.927 43.229 1.00 56.00  ? 54  ALA A N   1 
ATOM   249  C  CA  . ALA A 1 32  ? 14.957 44.104 42.966 1.00 57.00  ? 54  ALA A CA  1 
ATOM   250  C  C   . ALA A 1 32  ? 14.396 43.462 44.228 1.00 63.30  ? 54  ALA A C   1 
ATOM   251  O  O   . ALA A 1 32  ? 13.245 43.009 44.220 1.00 68.80  ? 54  ALA A O   1 
ATOM   252  C  CB  . ALA A 1 32  ? 15.301 43.018 41.944 1.00 47.48  ? 54  ALA A CB  1 
ATOM   253  N  N   . VAL A 1 33  ? 15.182 43.395 45.302 1.00 59.37  ? 55  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 33  ? 14.742 42.791 46.555 1.00 53.53  ? 55  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 33  ? 15.000 43.776 47.686 1.00 62.25  ? 55  VAL A C   1 
ATOM   256  O  O   . VAL A 1 33  ? 15.255 43.377 48.828 1.00 61.37  ? 55  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 33  ? 15.444 41.444 46.813 1.00 52.97  ? 55  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 33  ? 15.041 40.426 45.750 1.00 45.51  ? 55  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 33  ? 16.958 41.628 46.852 1.00 61.16  ? 55  VAL A CG2 1 
ATOM   260  N  N   . ASP A 1 34  ? 14.961 45.069 47.354 1.00 66.21  ? 56  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 34  ? 14.953 46.156 48.336 1.00 64.93  ? 56  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 34  ? 16.192 46.137 49.228 1.00 71.19  ? 56  ASP A C   1 
ATOM   263  O  O   . ASP A 1 34  ? 16.121 46.426 50.425 1.00 74.53  ? 56  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 34  ? 13.679 46.119 49.181 1.00 64.11  ? 56  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 34  ? 12.415 46.134 48.334 1.00 100.17 ? 56  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 34  ? 12.347 46.919 47.361 1.00 87.53  ? 56  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 34  ? 11.492 45.349 48.641 1.00 109.66 ? 56  ASP A OD2 1 
ATOM   268  N  N   . VAL A 1 35  ? 17.338 45.799 48.646 1.00 67.39  ? 57  VAL A N   1 
ATOM   269  C  CA  . VAL A 1 35  ? 18.618 45.843 49.342 1.00 53.12  ? 57  VAL A CA  1 
ATOM   270  C  C   . VAL A 1 35  ? 19.396 47.039 48.813 1.00 54.24  ? 57  VAL A C   1 
ATOM   271  O  O   . VAL A 1 35  ? 19.601 47.168 47.600 1.00 60.66  ? 57  VAL A O   1 
ATOM   272  C  CB  . VAL A 1 35  ? 19.415 44.543 49.160 1.00 66.09  ? 57  VAL A CB  1 
ATOM   273  C  CG1 . VAL A 1 35  ? 20.819 44.713 49.718 1.00 47.79  ? 57  VAL A CG1 1 
ATOM   274  C  CG2 . VAL A 1 35  ? 18.701 43.383 49.833 1.00 56.86  ? 57  VAL A CG2 1 
ATOM   275  N  N   . SER A 1 36  ? 19.825 47.913 49.721 1.00 49.77  ? 58  SER A N   1 
ATOM   276  C  CA  . SER A 1 36  ? 20.615 49.075 49.351 1.00 59.20  ? 58  SER A CA  1 
ATOM   277  C  C   . SER A 1 36  ? 22.090 48.761 49.540 1.00 62.00  ? 58  SER A C   1 
ATOM   278  O  O   . SER A 1 36  ? 22.526 48.567 50.686 1.00 54.36  ? 58  SER A O   1 
ATOM   279  C  CB  . SER A 1 36  ? 20.224 50.285 50.197 1.00 55.41  ? 58  SER A CB  1 
ATOM   280  O  OG  . SER A 1 36  ? 18.959 50.798 49.831 1.00 55.95  ? 58  SER A OG  1 
ATOM   281  N  N   . PRO A 1 37  ? 22.894 48.707 48.479 1.00 58.61  ? 59  PRO A N   1 
ATOM   282  C  CA  . PRO A 1 37  ? 24.342 48.581 48.673 1.00 53.90  ? 59  PRO A CA  1 
ATOM   283  C  C   . PRO A 1 37  ? 24.910 49.844 49.299 1.00 47.86  ? 59  PRO A C   1 
ATOM   284  O  O   . PRO A 1 37  ? 24.510 50.959 48.958 1.00 61.06  ? 59  PRO A O   1 
ATOM   285  C  CB  . PRO A 1 37  ? 24.872 48.374 47.250 1.00 48.62  ? 59  PRO A CB  1 
ATOM   286  C  CG  . PRO A 1 37  ? 23.875 49.090 46.395 1.00 50.46  ? 59  PRO A CG  1 
ATOM   287  C  CD  . PRO A 1 37  ? 22.541 48.856 47.057 1.00 60.15  ? 59  PRO A CD  1 
ATOM   288  N  N   . VAL A 1 38  ? 25.841 49.660 50.239 1.00 42.52  ? 60  VAL A N   1 
ATOM   289  C  CA  . VAL A 1 38  ? 26.504 50.811 50.845 1.00 41.10  ? 60  VAL A CA  1 
ATOM   290  C  C   . VAL A 1 38  ? 27.585 51.379 49.937 1.00 57.60  ? 60  VAL A C   1 
ATOM   291  O  O   . VAL A 1 38  ? 27.968 52.545 50.091 1.00 52.13  ? 60  VAL A O   1 
ATOM   292  C  CB  . VAL A 1 38  ? 27.106 50.455 52.217 1.00 59.80  ? 60  VAL A CB  1 
ATOM   293  C  CG1 . VAL A 1 38  ? 26.017 49.961 53.165 1.00 49.54  ? 60  VAL A CG1 1 
ATOM   294  C  CG2 . VAL A 1 38  ? 28.221 49.421 52.070 1.00 48.02  ? 60  VAL A CG2 1 
ATOM   295  N  N   . GLY A 1 39  ? 28.079 50.594 48.989 1.00 62.29  ? 61  GLY A N   1 
ATOM   296  C  CA  . GLY A 1 39  ? 29.102 51.073 48.089 1.00 56.44  ? 61  GLY A CA  1 
ATOM   297  C  C   . GLY A 1 39  ? 28.871 50.600 46.674 1.00 51.41  ? 61  GLY A C   1 
ATOM   298  O  O   . GLY A 1 39  ? 28.518 49.439 46.444 1.00 47.78  ? 61  GLY A O   1 
ATOM   299  N  N   . VAL A 1 40  ? 29.059 51.497 45.714 1.00 52.27  ? 62  VAL A N   1 
ATOM   300  C  CA  . VAL A 1 40  ? 28.913 51.180 44.301 1.00 57.38  ? 62  VAL A CA  1 
ATOM   301  C  C   . VAL A 1 40  ? 30.087 51.790 43.552 1.00 61.48  ? 62  VAL A C   1 
ATOM   302  O  O   . VAL A 1 40  ? 30.425 52.960 43.764 1.00 48.28  ? 62  VAL A O   1 
ATOM   303  C  CB  . VAL A 1 40  ? 27.582 51.696 43.723 1.00 51.36  ? 62  VAL A CB  1 
ATOM   304  C  CG1 . VAL A 1 40  ? 27.539 51.463 42.222 1.00 43.44  ? 62  VAL A CG1 1 
ATOM   305  C  CG2 . VAL A 1 40  ? 26.403 51.023 44.404 1.00 57.17  ? 62  VAL A CG2 1 
ATOM   306  N  N   . ALA A 1 41  ? 30.721 50.993 42.697 1.00 46.15  ? 63  ALA A N   1 
ATOM   307  C  CA  . ALA A 1 41  ? 31.661 51.520 41.713 1.00 59.42  ? 63  ALA A CA  1 
ATOM   308  C  C   . ALA A 1 41  ? 30.846 52.145 40.593 1.00 40.89  ? 63  ALA A C   1 
ATOM   309  O  O   . ALA A 1 41  ? 30.349 51.449 39.706 1.00 54.89  ? 63  ALA A O   1 
ATOM   310  C  CB  . ALA A 1 41  ? 32.570 50.414 41.191 1.00 49.87  ? 63  ALA A CB  1 
ATOM   311  N  N   . ASP A 1 42  ? 30.673 53.462 40.643 1.00 53.03  ? 64  ASP A N   1 
ATOM   312  C  CA  . ASP A 1 42  ? 29.823 54.160 39.690 1.00 49.49  ? 64  ASP A CA  1 
ATOM   313  C  C   . ASP A 1 42  ? 30.617 55.086 38.783 1.00 56.70  ? 64  ASP A C   1 
ATOM   314  O  O   . ASP A 1 42  ? 30.040 55.990 38.170 1.00 52.56  ? 64  ASP A O   1 
ATOM   315  C  CB  . ASP A 1 42  ? 28.742 54.942 40.431 1.00 37.87  ? 64  ASP A CB  1 
ATOM   316  C  CG  . ASP A 1 42  ? 29.317 55.863 41.486 1.00 54.91  ? 64  ASP A CG  1 
ATOM   317  O  OD1 . ASP A 1 42  ? 30.561 55.976 41.570 1.00 56.42  ? 64  ASP A OD1 1 
ATOM   318  O  OD2 . ASP A 1 42  ? 28.524 56.471 42.234 1.00 63.06  ? 64  ASP A OD2 1 
ATOM   319  N  N   . ASP A 1 43  ? 31.931 54.882 38.692 1.00 51.05  ? 65  ASP A N   1 
ATOM   320  C  CA  . ASP A 1 43  ? 32.805 55.748 37.906 1.00 53.68  ? 65  ASP A CA  1 
ATOM   321  C  C   . ASP A 1 43  ? 32.617 57.212 38.296 1.00 54.86  ? 65  ASP A C   1 
ATOM   322  O  O   . ASP A 1 43  ? 32.719 58.108 37.456 1.00 52.61  ? 65  ASP A O   1 
ATOM   323  C  CB  . ASP A 1 43  ? 32.579 55.558 36.401 1.00 36.05  ? 65  ASP A CB  1 
ATOM   324  C  CG  . ASP A 1 43  ? 32.607 54.093 35.975 1.00 52.62  ? 65  ASP A CG  1 
ATOM   325  O  OD1 . ASP A 1 43  ? 33.566 53.374 36.323 1.00 56.68  ? 65  ASP A OD1 1 
ATOM   326  O  OD2 . ASP A 1 43  ? 31.657 53.665 35.281 1.00 49.58  ? 65  ASP A OD2 1 
ATOM   327  N  N   . ASN A 1 44  ? 32.310 57.451 39.574 1.00 55.38  ? 66  ASN A N   1 
ATOM   328  C  CA  . ASN A 1 44  ? 32.134 58.799 40.118 1.00 60.16  ? 66  ASN A CA  1 
ATOM   329  C  C   . ASN A 1 44  ? 31.027 59.563 39.386 1.00 71.43  ? 66  ASN A C   1 
ATOM   330  O  O   . ASN A 1 44  ? 31.187 60.725 39.006 1.00 82.01  ? 66  ASN A O   1 
ATOM   331  C  CB  . ASN A 1 44  ? 33.454 59.570 40.084 1.00 59.64  ? 66  ASN A CB  1 
ATOM   332  C  CG  . ASN A 1 44  ? 34.514 58.948 40.968 1.00 73.64  ? 66  ASN A CG  1 
ATOM   333  O  OD1 . ASN A 1 44  ? 34.248 58.585 42.115 1.00 73.00  ? 66  ASN A OD1 1 
ATOM   334  N  ND2 . ASN A 1 44  ? 35.725 58.814 40.436 1.00 65.52  ? 66  ASN A ND2 1 
ATOM   335  N  N   . ASP A 1 45  ? 29.890 58.892 39.191 1.00 65.54  ? 67  ASP A N   1 
ATOM   336  C  CA  . ASP A 1 45  ? 28.738 59.485 38.517 1.00 63.97  ? 67  ASP A CA  1 
ATOM   337  C  C   . ASP A 1 45  ? 27.500 58.629 38.745 1.00 61.46  ? 67  ASP A C   1 
ATOM   338  O  O   . ASP A 1 45  ? 27.208 57.726 37.953 1.00 56.17  ? 67  ASP A O   1 
ATOM   339  C  CB  . ASP A 1 45  ? 28.991 59.645 37.015 1.00 57.61  ? 67  ASP A CB  1 
ATOM   340  C  CG  . ASP A 1 45  ? 27.908 60.464 36.325 1.00 66.38  ? 67  ASP A CG  1 
ATOM   341  O  OD1 . ASP A 1 45  ? 27.017 60.987 37.031 1.00 60.83  ? 67  ASP A OD1 1 
ATOM   342  O  OD2 . ASP A 1 45  ? 27.946 60.589 35.081 1.00 68.68  ? 67  ASP A OD2 1 
ATOM   343  N  N   . ALA A 1 46  ? 26.763 58.921 39.818 1.00 53.91  ? 68  ALA A N   1 
ATOM   344  C  CA  . ALA A 1 46  ? 25.618 58.095 40.186 1.00 62.80  ? 68  ALA A CA  1 
ATOM   345  C  C   . ALA A 1 46  ? 24.559 58.056 39.090 1.00 63.15  ? 68  ALA A C   1 
ATOM   346  O  O   . ALA A 1 46  ? 23.779 57.100 39.022 1.00 63.55  ? 68  ALA A O   1 
ATOM   347  C  CB  . ALA A 1 46  ? 25.010 58.601 41.495 1.00 50.64  ? 68  ALA A CB  1 
ATOM   348  N  N   . THR A 1 47  ? 24.515 59.070 38.220 1.00 73.57  ? 69  THR A N   1 
ATOM   349  C  CA  . THR A 1 47  ? 23.503 59.084 37.170 1.00 73.00  ? 69  THR A CA  1 
ATOM   350  C  C   . THR A 1 47  ? 23.734 58.013 36.114 1.00 67.81  ? 69  THR A C   1 
ATOM   351  O  O   . THR A 1 47  ? 22.908 57.882 35.205 1.00 79.83  ? 69  THR A O   1 
ATOM   352  C  CB  . THR A 1 47  ? 23.438 60.453 36.488 1.00 63.18  ? 69  THR A CB  1 
ATOM   353  O  OG1 . THR A 1 47  ? 24.658 60.700 35.774 1.00 67.68  ? 69  THR A OG1 1 
ATOM   354  C  CG2 . THR A 1 47  ? 23.218 61.542 37.513 1.00 55.53  ? 69  THR A CG2 1 
ATOM   355  N  N   . ARG A 1 48  ? 24.834 57.260 36.198 1.00 59.59  ? 70  ARG A N   1 
ATOM   356  C  CA  . ARG A 1 48  ? 25.025 56.149 35.275 1.00 60.53  ? 70  ARG A CA  1 
ATOM   357  C  C   . ARG A 1 48  ? 24.071 55.002 35.591 1.00 62.43  ? 70  ARG A C   1 
ATOM   358  O  O   . ARG A 1 48  ? 23.725 54.218 34.700 1.00 61.42  ? 70  ARG A O   1 
ATOM   359  C  CB  . ARG A 1 48  ? 26.486 55.687 35.304 1.00 62.66  ? 70  ARG A CB  1 
ATOM   360  C  CG  . ARG A 1 48  ? 27.495 56.808 35.013 1.00 50.57  ? 70  ARG A CG  1 
ATOM   361  C  CD  . ARG A 1 48  ? 28.901 56.269 34.715 1.00 51.84  ? 70  ARG A CD  1 
ATOM   362  N  NE  . ARG A 1 48  ? 29.038 55.850 33.324 1.00 69.58  ? 70  ARG A NE  1 
ATOM   363  C  CZ  . ARG A 1 48  ? 30.140 55.333 32.798 1.00 64.95  ? 70  ARG A CZ  1 
ATOM   364  N  NH1 . ARG A 1 48  ? 31.236 55.169 33.516 1.00 78.18  ? 70  ARG A NH1 1 
ATOM   365  N  NH2 . ARG A 1 48  ? 30.141 54.968 31.519 1.00 72.09  ? 70  ARG A NH2 1 
ATOM   366  N  N   . VAL A 1 49  ? 23.630 54.895 36.841 1.00 57.41  ? 71  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 49  ? 22.536 54.000 37.195 1.00 60.56  ? 71  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 49  ? 21.225 54.669 36.808 1.00 65.10  ? 71  VAL A C   1 
ATOM   369  O  O   . VAL A 1 49  ? 21.006 55.849 37.112 1.00 67.51  ? 71  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 49  ? 22.569 53.669 38.696 1.00 64.86  ? 71  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 49  ? 21.368 52.824 39.087 1.00 50.09  ? 71  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 49  ? 23.863 52.960 39.059 1.00 60.39  ? 71  VAL A CG2 1 
ATOM   373  N  N   . ILE A 1 50  ? 20.352 53.928 36.134 1.00 57.62  ? 72  ILE A N   1 
ATOM   374  C  CA  . ILE A 1 50  ? 19.076 54.487 35.688 1.00 68.97  ? 72  ILE A CA  1 
ATOM   375  C  C   . ILE A 1 50  ? 18.241 54.882 36.901 1.00 78.63  ? 72  ILE A C   1 
ATOM   376  O  O   . ILE A 1 50  ? 18.361 54.258 37.968 1.00 63.42  ? 72  ILE A O   1 
ATOM   377  C  CB  . ILE A 1 50  ? 18.313 53.502 34.791 1.00 63.68  ? 72  ILE A CB  1 
ATOM   378  C  CG1 . ILE A 1 50  ? 17.854 52.288 35.603 1.00 66.46  ? 72  ILE A CG1 1 
ATOM   379  C  CG2 . ILE A 1 50  ? 19.178 53.110 33.603 1.00 47.77  ? 72  ILE A CG2 1 
ATOM   380  C  CD1 . ILE A 1 50  ? 16.831 51.426 34.899 1.00 61.98  ? 72  ILE A CD1 1 
ATOM   381  N  N   . PRO A 1 51  ? 17.397 55.912 36.788 1.00 85.97  ? 73  PRO A N   1 
ATOM   382  C  CA  . PRO A 1 51  ? 16.650 56.385 37.965 1.00 73.92  ? 73  PRO A CA  1 
ATOM   383  C  C   . PRO A 1 51  ? 15.687 55.362 38.545 1.00 63.08  ? 73  PRO A C   1 
ATOM   384  O  O   . PRO A 1 51  ? 15.363 55.456 39.735 1.00 70.13  ? 73  PRO A O   1 
ATOM   385  C  CB  . PRO A 1 51  ? 15.901 57.616 37.433 1.00 73.09  ? 73  PRO A CB  1 
ATOM   386  C  CG  . PRO A 1 51  ? 16.683 58.055 36.243 1.00 65.23  ? 73  PRO A CG  1 
ATOM   387  C  CD  . PRO A 1 51  ? 17.218 56.801 35.627 1.00 70.42  ? 73  PRO A CD  1 
ATOM   388  N  N   . ALA A 1 52  ? 15.216 54.392 37.755 1.00 69.70  ? 74  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 14.294 53.393 38.288 1.00 67.75  ? 74  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 14.939 52.521 39.357 1.00 76.46  ? 74  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 14.226 51.947 40.188 1.00 73.39  ? 74  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 13.755 52.505 37.166 1.00 66.70  ? 74  ALA A CB  1 
ATOM   393  N  N   . VAL A 1 53  ? 16.263 52.406 39.352 1.00 77.70  ? 75  VAL A N   1 
ATOM   394  C  CA  . VAL A 1 53  ? 16.970 51.650 40.377 1.00 57.86  ? 75  VAL A CA  1 
ATOM   395  C  C   . VAL A 1 53  ? 17.241 52.503 41.602 1.00 54.15  ? 75  VAL A C   1 
ATOM   396  O  O   . VAL A 1 53  ? 16.991 52.078 42.733 1.00 60.62  ? 75  VAL A O   1 
ATOM   397  C  CB  . VAL A 1 53  ? 18.279 51.081 39.801 1.00 70.81  ? 75  VAL A CB  1 
ATOM   398  C  CG1 . VAL A 1 53  ? 19.108 50.448 40.903 1.00 67.17  ? 75  VAL A CG1 1 
ATOM   399  C  CG2 . VAL A 1 53  ? 17.964 50.076 38.733 1.00 52.29  ? 75  VAL A CG2 1 
ATOM   400  N  N   . ARG A 1 54  ? 17.764 53.714 41.400 1.00 59.69  ? 76  ARG A N   1 
ATOM   401  C  CA  . ARG A 1 54  ? 18.106 54.564 42.533 1.00 64.93  ? 76  ARG A CA  1 
ATOM   402  C  C   . ARG A 1 54  ? 16.878 54.985 43.325 1.00 61.03  ? 76  ARG A C   1 
ATOM   403  O  O   . ARG A 1 54  ? 17.012 55.387 44.487 1.00 69.58  ? 76  ARG A O   1 
ATOM   404  C  CB  . ARG A 1 54  ? 18.873 55.793 42.053 1.00 65.00  ? 76  ARG A CB  1 
ATOM   405  C  CG  . ARG A 1 54  ? 20.248 55.482 41.504 1.00 68.73  ? 76  ARG A CG  1 
ATOM   406  C  CD  . ARG A 1 54  ? 20.489 56.246 40.226 1.00 70.09  ? 76  ARG A CD  1 
ATOM   407  N  NE  . ARG A 1 54  ? 20.285 57.678 40.397 1.00 77.48  ? 76  ARG A NE  1 
ATOM   408  C  CZ  . ARG A 1 54  ? 20.061 58.524 39.400 1.00 78.98  ? 76  ARG A CZ  1 
ATOM   409  N  NH1 . ARG A 1 54  ? 19.982 58.110 38.146 1.00 73.02  ? 76  ARG A NH1 1 
ATOM   410  N  NH2 . ARG A 1 54  ? 19.909 59.817 39.669 1.00 73.21  ? 76  ARG A NH2 1 
ATOM   411  N  N   . ASP A 1 55  ? 15.687 54.901 42.723 1.00 65.30  ? 77  ASP A N   1 
ATOM   412  C  CA  . ASP A 1 55  ? 14.451 55.155 43.458 1.00 73.59  ? 77  ASP A CA  1 
ATOM   413  C  C   . ASP A 1 55  ? 14.134 54.029 44.434 1.00 71.52  ? 77  ASP A C   1 
ATOM   414  O  O   . ASP A 1 55  ? 13.507 54.271 45.472 1.00 79.67  ? 77  ASP A O   1 
ATOM   415  C  CB  . ASP A 1 55  ? 13.286 55.341 42.484 1.00 76.26  ? 77  ASP A CB  1 
ATOM   416  C  CG  . ASP A 1 55  ? 13.360 56.651 41.721 1.00 92.12  ? 77  ASP A CG  1 
ATOM   417  O  OD1 . ASP A 1 55  ? 14.003 57.598 42.223 1.00 107.71 ? 77  ASP A OD1 1 
ATOM   418  O  OD2 . ASP A 1 55  ? 12.765 56.736 40.624 1.00 79.41  ? 77  ASP A OD2 1 
ATOM   419  N  N   . LYS A 1 56  ? 14.550 52.801 44.118 1.00 67.59  ? 78  LYS A N   1 
ATOM   420  C  CA  . LYS A 1 56  ? 14.265 51.648 44.962 1.00 51.49  ? 78  LYS A CA  1 
ATOM   421  C  C   . LYS A 1 56  ? 15.210 51.532 46.151 1.00 65.38  ? 78  LYS A C   1 
ATOM   422  O  O   . LYS A 1 56  ? 14.892 50.818 47.108 1.00 77.66  ? 78  LYS A O   1 
ATOM   423  C  CB  . LYS A 1 56  ? 14.348 50.362 44.137 1.00 59.76  ? 78  LYS A CB  1 
ATOM   424  C  CG  . LYS A 1 56  ? 13.495 50.364 42.884 1.00 51.64  ? 78  LYS A CG  1 
ATOM   425  C  CD  . LYS A 1 56  ? 12.037 50.133 43.221 1.00 82.33  ? 78  LYS A CD  1 
ATOM   426  C  CE  . LYS A 1 56  ? 11.828 48.736 43.778 1.00 80.62  ? 78  LYS A CE  1 
ATOM   427  N  NZ  . LYS A 1 56  ? 12.152 47.703 42.756 1.00 85.07  ? 78  LYS A NZ  1 
ATOM   428  N  N   . ILE A 1 57  ? 16.362 52.206 46.114 1.00 62.62  ? 79  ILE A N   1 
ATOM   429  C  CA  . ILE A 1 57  ? 17.424 51.984 47.085 1.00 56.80  ? 79  ILE A CA  1 
ATOM   430  C  C   . ILE A 1 57  ? 17.924 53.311 47.638 1.00 50.73  ? 79  ILE A C   1 
ATOM   431  O  O   . ILE A 1 57  ? 17.769 54.372 47.029 1.00 56.97  ? 79  ILE A O   1 
ATOM   432  C  CB  . ILE A 1 57  ? 18.609 51.208 46.480 1.00 61.65  ? 79  ILE A CB  1 
ATOM   433  C  CG1 . ILE A 1 57  ? 19.128 51.938 45.243 1.00 58.92  ? 79  ILE A CG1 1 
ATOM   434  C  CG2 . ILE A 1 57  ? 18.205 49.792 46.142 1.00 53.85  ? 79  ILE A CG2 1 
ATOM   435  C  CD1 . ILE A 1 57  ? 20.285 51.252 44.584 1.00 68.04  ? 79  ILE A CD1 1 
ATOM   436  N  N   . GLU A 1 58  ? 18.561 53.220 48.802 1.00 50.71  ? 80  GLU A N   1 
ATOM   437  C  CA  . GLU A 1 58  ? 19.209 54.353 49.434 1.00 63.50  ? 80  GLU A CA  1 
ATOM   438  C  C   . GLU A 1 58  ? 20.406 54.826 48.607 1.00 59.34  ? 80  GLU A C   1 
ATOM   439  O  O   . GLU A 1 58  ? 20.944 54.077 47.787 1.00 73.05  ? 80  GLU A O   1 
ATOM   440  C  CB  . GLU A 1 58  ? 19.668 53.964 50.838 1.00 64.89  ? 80  GLU A CB  1 
ATOM   441  C  CG  . GLU A 1 58  ? 18.543 53.531 51.760 1.00 67.48  ? 80  GLU A CG  1 
ATOM   442  C  CD  . GLU A 1 58  ? 17.756 54.709 52.299 1.00 86.91  ? 80  GLU A CD  1 
ATOM   443  O  OE1 . GLU A 1 58  ? 18.388 55.704 52.714 1.00 81.69  ? 80  GLU A OE1 1 
ATOM   444  O  OE2 . GLU A 1 58  ? 16.508 54.644 52.304 1.00 110.14 ? 80  GLU A OE2 1 
ATOM   445  N  N   . PRO A 1 59  ? 20.842 56.069 48.806 1.00 62.17  ? 81  PRO A N   1 
ATOM   446  C  CA  . PRO A 1 59  ? 22.106 56.503 48.201 1.00 67.52  ? 81  PRO A CA  1 
ATOM   447  C  C   . PRO A 1 59  ? 23.279 55.731 48.778 1.00 61.59  ? 81  PRO A C   1 
ATOM   448  O  O   . PRO A 1 59  ? 23.242 55.248 49.912 1.00 64.49  ? 81  PRO A O   1 
ATOM   449  C  CB  . PRO A 1 59  ? 22.186 57.991 48.562 1.00 64.95  ? 81  PRO A CB  1 
ATOM   450  C  CG  . PRO A 1 59  ? 21.313 58.137 49.763 1.00 68.14  ? 81  PRO A CG  1 
ATOM   451  C  CD  . PRO A 1 59  ? 20.192 57.154 49.558 1.00 69.85  ? 81  PRO A CD  1 
ATOM   452  N  N   . TRP A 1 60  ? 24.332 55.622 47.978 1.00 61.77  ? 82  TRP A N   1 
ATOM   453  C  CA  . TRP A 1 60  ? 25.512 54.849 48.328 1.00 49.81  ? 82  TRP A CA  1 
ATOM   454  C  C   . TRP A 1 60  ? 26.734 55.757 48.397 1.00 60.33  ? 82  TRP A C   1 
ATOM   455  O  O   . TRP A 1 60  ? 26.685 56.934 48.033 1.00 57.96  ? 82  TRP A O   1 
ATOM   456  C  CB  . TRP A 1 60  ? 25.746 53.723 47.311 1.00 40.90  ? 82  TRP A CB  1 
ATOM   457  C  CG  . TRP A 1 60  ? 25.872 54.212 45.891 1.00 58.77  ? 82  TRP A CG  1 
ATOM   458  C  CD1 . TRP A 1 60  ? 26.965 54.808 45.322 1.00 57.05  ? 82  TRP A CD1 1 
ATOM   459  C  CD2 . TRP A 1 60  ? 24.875 54.136 44.861 1.00 57.35  ? 82  TRP A CD2 1 
ATOM   460  N  NE1 . TRP A 1 60  ? 26.704 55.115 44.007 1.00 54.08  ? 82  TRP A NE1 1 
ATOM   461  C  CE2 . TRP A 1 60  ? 25.431 54.711 43.699 1.00 54.06  ? 82  TRP A CE2 1 
ATOM   462  C  CE3 . TRP A 1 60  ? 23.569 53.639 44.808 1.00 55.50  ? 82  TRP A CE3 1 
ATOM   463  C  CZ2 . TRP A 1 60  ? 24.728 54.798 42.499 1.00 53.63  ? 82  TRP A CZ2 1 
ATOM   464  C  CZ3 . TRP A 1 60  ? 22.873 53.730 43.617 1.00 55.47  ? 82  TRP A CZ3 1 
ATOM   465  C  CH2 . TRP A 1 60  ? 23.453 54.303 42.479 1.00 62.69  ? 82  TRP A CH2 1 
ATOM   466  N  N   . GLN A 1 61  ? 27.834 55.189 48.884 1.00 64.22  ? 83  GLN A N   1 
ATOM   467  C  CA  . GLN A 1 61  ? 29.150 55.810 48.807 1.00 54.83  ? 83  GLN A CA  1 
ATOM   468  C  C   . GLN A 1 61  ? 29.890 55.256 47.595 1.00 57.25  ? 83  GLN A C   1 
ATOM   469  O  O   . GLN A 1 61  ? 30.023 54.035 47.450 1.00 59.70  ? 83  GLN A O   1 
ATOM   470  C  CB  . GLN A 1 61  ? 29.960 55.541 50.077 1.00 51.86  ? 83  GLN A CB  1 
ATOM   471  C  CG  . GLN A 1 61  ? 29.992 56.693 51.064 1.00 78.01  ? 83  GLN A CG  1 
ATOM   472  C  CD  . GLN A 1 61  ? 30.965 57.779 50.654 1.00 95.46  ? 83  GLN A CD  1 
ATOM   473  O  OE1 . GLN A 1 61  ? 31.891 57.540 49.870 1.00 76.53  ? 83  GLN A OE1 1 
ATOM   474  N  NE2 . GLN A 1 61  ? 30.763 58.983 51.181 1.00 102.68 ? 83  GLN A NE2 1 
ATOM   475  N  N   . SER A 1 62  ? 30.377 56.148 46.736 1.00 50.33  ? 84  SER A N   1 
ATOM   476  C  CA  . SER A 1 62  ? 31.125 55.712 45.566 1.00 54.11  ? 84  SER A CA  1 
ATOM   477  C  C   . SER A 1 62  ? 32.467 55.124 45.974 1.00 59.03  ? 84  SER A C   1 
ATOM   478  O  O   . SER A 1 62  ? 33.179 55.687 46.811 1.00 50.11  ? 84  SER A O   1 
ATOM   479  C  CB  . SER A 1 62  ? 31.350 56.879 44.607 1.00 48.88  ? 84  SER A CB  1 
ATOM   480  O  OG  . SER A 1 62  ? 32.111 56.455 43.488 1.00 56.46  ? 84  SER A OG  1 
ATOM   481  N  N   . VAL A 1 63  ? 32.813 53.985 45.379 1.00 51.83  ? 85  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 63  ? 34.137 53.405 45.550 1.00 63.07  ? 85  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 63  ? 34.997 53.586 44.305 1.00 51.62  ? 85  VAL A C   1 
ATOM   484  O  O   . VAL A 1 63  ? 36.059 52.968 44.192 1.00 55.81  ? 85  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 63  ? 34.047 51.927 45.954 1.00 45.66  ? 85  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 63  ? 33.306 51.802 47.269 1.00 45.12  ? 85  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 63  ? 33.357 51.119 44.863 1.00 46.01  ? 85  VAL A CG2 1 
ATOM   488  N  N   . GLY A 1 64  ? 34.565 54.424 43.372 1.00 47.33  ? 86  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 64  ? 35.431 54.799 42.278 1.00 48.41  ? 86  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 64  ? 35.033 54.207 40.947 1.00 42.18  ? 86  GLY A C   1 
ATOM   491  O  O   . GLY A 1 64  ? 33.854 53.926 40.704 1.00 49.23  ? 86  GLY A O   1 
ATOM   492  N  N   . MET A 1 65  ? 36.021 54.007 40.080 1.00 35.99  ? 87  MET A N   1 
ATOM   493  C  CA  . MET A 1 65  ? 35.765 53.555 38.723 1.00 43.55  ? 87  MET A CA  1 
ATOM   494  C  C   . MET A 1 65  ? 35.527 52.051 38.696 1.00 49.51  ? 87  MET A C   1 
ATOM   495  O  O   . MET A 1 65  ? 36.192 51.287 39.402 1.00 48.74  ? 87  MET A O   1 
ATOM   496  C  CB  . MET A 1 65  ? 36.938 53.915 37.810 1.00 58.64  ? 87  MET A CB  1 
ATOM   497  C  CG  . MET A 1 65  ? 37.414 55.359 37.928 1.00 44.80  ? 87  MET A CG  1 
ATOM   498  S  SD  . MET A 1 65  ? 36.199 56.547 37.340 1.00 66.15  ? 87  MET A SD  1 
ATOM   499  C  CE  . MET A 1 65  ? 36.069 56.072 35.622 1.00 51.80  ? 87  MET A CE  1 
ATOM   500  N  N   . ARG A 1 66  ? 34.571 51.631 37.863 1.00 48.37  ? 88  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 66  ? 34.262 50.210 37.738 1.00 53.41  ? 88  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 66  ? 35.477 49.416 37.285 1.00 50.56  ? 88  ARG A C   1 
ATOM   503  O  O   . ARG A 1 66  ? 35.703 48.292 37.749 1.00 57.09  ? 88  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 66  ? 33.104 50.012 36.764 1.00 33.23  ? 88  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 66  ? 31.821 50.643 37.247 1.00 57.06  ? 88  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 66  ? 30.693 50.401 36.278 1.00 45.94  ? 88  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 66  ? 31.016 50.973 34.979 1.00 47.71  ? 88  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 66  ? 30.402 50.658 33.850 1.00 42.19  ? 88  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 66  ? 29.405 49.790 33.828 1.00 65.24  ? 88  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 66  ? 30.806 51.219 32.715 1.00 54.99  ? 88  ARG A NH2 1 
ATOM   511  N  N   . SER A 1 67  ? 36.271 49.983 36.376 1.00 52.92  ? 89  SER A N   1 
ATOM   512  C  CA  . SER A 1 67  ? 37.448 49.294 35.863 1.00 46.87  ? 89  SER A CA  1 
ATOM   513  C  C   . SER A 1 67  ? 38.583 49.239 36.875 1.00 48.81  ? 89  SER A C   1 
ATOM   514  O  O   . SER A 1 67  ? 39.429 48.343 36.788 1.00 67.64  ? 89  SER A O   1 
ATOM   515  C  CB  . SER A 1 67  ? 37.940 49.977 34.589 1.00 49.80  ? 89  SER A CB  1 
ATOM   516  O  OG  . SER A 1 67  ? 38.338 51.312 34.853 1.00 63.64  ? 89  SER A OG  1 
ATOM   517  N  N   . GLN A 1 68  ? 38.621 50.166 37.833 1.00 51.04  ? 90  GLN A N   1 
ATOM   518  C  CA  . GLN A 1 68  ? 39.749 50.284 38.757 1.00 52.57  ? 90  GLN A CA  1 
ATOM   519  C  C   . GLN A 1 68  ? 39.245 50.825 40.089 1.00 53.99  ? 90  GLN A C   1 
ATOM   520  O  O   . GLN A 1 68  ? 39.483 51.986 40.444 1.00 58.34  ? 90  GLN A O   1 
ATOM   521  C  CB  . GLN A 1 68  ? 40.828 51.184 38.161 1.00 65.22  ? 90  GLN A CB  1 
ATOM   522  C  CG  . GLN A 1 68  ? 42.167 51.147 38.858 1.00 97.08  ? 90  GLN A CG  1 
ATOM   523  C  CD  . GLN A 1 68  ? 43.170 52.059 38.183 1.00 119.57 ? 90  GLN A CD  1 
ATOM   524  O  OE1 . GLN A 1 68  ? 42.807 52.864 37.321 1.00 87.58  ? 90  GLN A OE1 1 
ATOM   525  N  NE2 . GLN A 1 68  ? 44.438 51.936 38.565 1.00 139.76 ? 90  GLN A NE2 1 
ATOM   526  N  N   . PRO A 1 69  ? 38.530 50.002 40.854 1.00 59.20  ? 91  PRO A N   1 
ATOM   527  C  CA  . PRO A 1 69  ? 37.939 50.487 42.106 1.00 49.73  ? 91  PRO A CA  1 
ATOM   528  C  C   . PRO A 1 69  ? 38.999 50.836 43.139 1.00 55.93  ? 91  PRO A C   1 
ATOM   529  O  O   . PRO A 1 69  ? 40.117 50.315 43.135 1.00 62.98  ? 91  PRO A O   1 
ATOM   530  C  CB  . PRO A 1 69  ? 37.085 49.306 42.581 1.00 44.27  ? 91  PRO A CB  1 
ATOM   531  C  CG  . PRO A 1 69  ? 36.891 48.454 41.376 1.00 47.51  ? 91  PRO A CG  1 
ATOM   532  C  CD  . PRO A 1 69  ? 38.129 48.617 40.559 1.00 51.06  ? 91  PRO A CD  1 
ATOM   533  N  N   . SER A 1 70  ? 38.617 51.732 44.045 1.00 47.58  ? 92  SER A N   1 
ATOM   534  C  CA  . SER A 1 70  ? 39.470 52.107 45.166 1.00 63.54  ? 92  SER A CA  1 
ATOM   535  C  C   . SER A 1 70  ? 39.316 51.075 46.275 1.00 53.95  ? 92  SER A C   1 
ATOM   536  O  O   . SER A 1 70  ? 38.281 51.027 46.946 1.00 48.12  ? 92  SER A O   1 
ATOM   537  C  CB  . SER A 1 70  ? 39.113 53.502 45.669 1.00 54.91  ? 92  SER A CB  1 
ATOM   538  O  OG  . SER A 1 70  ? 39.759 53.774 46.901 1.00 63.39  ? 92  SER A OG  1 
ATOM   539  N  N   . LEU A 1 71  ? 40.346 50.246 46.470 1.00 53.64  ? 93  LEU A N   1 
ATOM   540  C  CA  . LEU A 1 71  ? 40.320 49.293 47.574 1.00 56.83  ? 93  LEU A CA  1 
ATOM   541  C  C   . LEU A 1 71  ? 40.186 50.000 48.916 1.00 61.30  ? 93  LEU A C   1 
ATOM   542  O  O   . LEU A 1 71  ? 39.552 49.470 49.836 1.00 57.24  ? 93  LEU A O   1 
ATOM   543  C  CB  . LEU A 1 71  ? 41.582 48.429 47.560 1.00 49.26  ? 93  LEU A CB  1 
ATOM   544  C  CG  . LEU A 1 71  ? 41.845 47.620 46.289 1.00 68.89  ? 93  LEU A CG  1 
ATOM   545  C  CD1 . LEU A 1 71  ? 43.158 46.858 46.396 1.00 56.75  ? 93  LEU A CD1 1 
ATOM   546  C  CD2 . LEU A 1 71  ? 40.701 46.666 46.032 1.00 52.26  ? 93  LEU A CD2 1 
ATOM   547  N  N   . GLU A 1 72  ? 40.777 51.188 49.052 1.00 63.56  ? 94  GLU A N   1 
ATOM   548  C  CA  . GLU A 1 72  ? 40.641 51.933 50.298 1.00 73.43  ? 94  GLU A CA  1 
ATOM   549  C  C   . GLU A 1 72  ? 39.187 52.292 50.561 1.00 62.20  ? 94  GLU A C   1 
ATOM   550  O  O   . GLU A 1 72  ? 38.653 52.017 51.642 1.00 57.02  ? 94  GLU A O   1 
ATOM   551  C  CB  . GLU A 1 72  ? 41.507 53.190 50.258 1.00 76.65  ? 94  GLU A CB  1 
ATOM   552  C  CG  . GLU A 1 72  ? 42.892 52.989 50.833 1.00 81.17  ? 94  GLU A CG  1 
ATOM   553  C  CD  . GLU A 1 72  ? 42.868 52.764 52.331 1.00 92.77  ? 94  GLU A CD  1 
ATOM   554  O  OE1 . GLU A 1 72  ? 41.863 53.131 52.976 1.00 92.42  ? 94  GLU A OE1 1 
ATOM   555  O  OE2 . GLU A 1 72  ? 43.857 52.219 52.863 1.00 116.72 ? 94  GLU A OE2 1 
ATOM   556  N  N   . ALA A 1 73  ? 38.528 52.904 49.574 1.00 66.72  ? 95  ALA A N   1 
ATOM   557  C  CA  . ALA A 1 73  ? 37.131 53.291 49.736 1.00 62.49  ? 95  ALA A CA  1 
ATOM   558  C  C   . ALA A 1 73  ? 36.261 52.090 50.081 1.00 54.43  ? 95  ALA A C   1 
ATOM   559  O  O   . ALA A 1 73  ? 35.365 52.186 50.928 1.00 62.22  ? 95  ALA A O   1 
ATOM   560  C  CB  . ALA A 1 73  ? 36.627 53.973 48.465 1.00 51.44  ? 95  ALA A CB  1 
ATOM   561  N  N   . ILE A 1 74  ? 36.514 50.948 49.436 1.00 58.35  ? 96  ILE A N   1 
ATOM   562  C  CA  . ILE A 1 74  ? 35.760 49.733 49.736 1.00 49.17  ? 96  ILE A CA  1 
ATOM   563  C  C   . ILE A 1 74  ? 35.977 49.318 51.185 1.00 53.71  ? 96  ILE A C   1 
ATOM   564  O  O   . ILE A 1 74  ? 35.024 49.029 51.920 1.00 55.56  ? 96  ILE A O   1 
ATOM   565  C  CB  . ILE A 1 74  ? 36.156 48.606 48.768 1.00 45.18  ? 96  ILE A CB  1 
ATOM   566  C  CG1 . ILE A 1 74  ? 35.852 49.019 47.324 1.00 45.62  ? 96  ILE A CG1 1 
ATOM   567  C  CG2 . ILE A 1 74  ? 35.455 47.303 49.154 1.00 42.25  ? 96  ILE A CG2 1 
ATOM   568  C  CD1 . ILE A 1 74  ? 36.288 48.001 46.287 1.00 48.67  ? 96  ILE A CD1 1 
ATOM   569  N  N   . ALA A 1 75  ? 37.238 49.292 51.619 1.00 51.27  ? 97  ALA A N   1 
ATOM   570  C  CA  . ALA A 1 75  ? 37.553 48.804 52.957 1.00 55.30  ? 97  ALA A CA  1 
ATOM   571  C  C   . ALA A 1 75  ? 37.001 49.726 54.034 1.00 52.59  ? 97  ALA A C   1 
ATOM   572  O  O   . ALA A 1 75  ? 36.535 49.255 55.077 1.00 54.39  ? 97  ALA A O   1 
ATOM   573  C  CB  . ALA A 1 75  ? 39.063 48.642 53.110 1.00 45.83  ? 97  ALA A CB  1 
ATOM   574  N  N   . VAL A 1 76  ? 37.040 51.040 53.800 1.00 59.71  ? 98  VAL A N   1 
ATOM   575  C  CA  . VAL A 1 76  ? 36.534 51.991 54.788 1.00 64.41  ? 98  VAL A CA  1 
ATOM   576  C  C   . VAL A 1 76  ? 35.043 51.784 55.026 1.00 54.45  ? 98  VAL A C   1 
ATOM   577  O  O   . VAL A 1 76  ? 34.552 51.960 56.149 1.00 62.88  ? 98  VAL A O   1 
ATOM   578  C  CB  . VAL A 1 76  ? 36.844 53.436 54.349 1.00 59.25  ? 98  VAL A CB  1 
ATOM   579  C  CG1 . VAL A 1 76  ? 35.967 54.429 55.085 1.00 64.39  ? 98  VAL A CG1 1 
ATOM   580  C  CG2 . VAL A 1 76  ? 38.306 53.751 54.599 1.00 71.93  ? 98  VAL A CG2 1 
ATOM   581  N  N   . LEU A 1 77  ? 34.303 51.385 53.991 1.00 57.28  ? 99  LEU A N   1 
ATOM   582  C  CA  . LEU A 1 77  ? 32.881 51.112 54.143 1.00 58.88  ? 99  LEU A CA  1 
ATOM   583  C  C   . LEU A 1 77  ? 32.597 49.890 55.001 1.00 61.98  ? 99  LEU A C   1 
ATOM   584  O  O   . LEU A 1 77  ? 31.423 49.628 55.290 1.00 56.07  ? 99  LEU A O   1 
ATOM   585  C  CB  . LEU A 1 77  ? 32.237 50.923 52.777 1.00 44.44  ? 99  LEU A CB  1 
ATOM   586  C  CG  . LEU A 1 77  ? 32.191 52.176 51.916 1.00 47.11  ? 99  LEU A CG  1 
ATOM   587  C  CD1 . LEU A 1 77  ? 31.677 51.799 50.548 1.00 44.86  ? 99  LEU A CD1 1 
ATOM   588  C  CD2 . LEU A 1 77  ? 31.287 53.205 52.571 1.00 40.27  ? 99  LEU A CD2 1 
ATOM   589  N  N   . LYS A 1 78  ? 33.626 49.149 55.405 1.00 46.33  ? 100 LYS A N   1 
ATOM   590  C  CA  . LYS A 1 78  ? 33.475 47.975 56.261 1.00 54.18  ? 100 LYS A CA  1 
ATOM   591  C  C   . LYS A 1 78  ? 32.366 47.043 55.752 1.00 56.46  ? 100 LYS A C   1 
ATOM   592  O  O   . LYS A 1 78  ? 31.382 46.806 56.452 1.00 51.96  ? 100 LYS A O   1 
ATOM   593  C  CB  . LYS A 1 78  ? 33.218 48.388 57.698 1.00 50.30  ? 100 LYS A CB  1 
ATOM   594  C  CG  . LYS A 1 78  ? 34.438 48.992 58.403 1.00 76.00  ? 100 LYS A CG  1 
ATOM   595  C  CD  . LYS A 1 78  ? 34.139 49.350 59.861 1.00 87.11  ? 100 LYS A CD  1 
ATOM   596  C  CE  . LYS A 1 78  ? 35.351 49.967 60.557 1.00 81.48  ? 100 LYS A CE  1 
ATOM   597  N  NZ  . LYS A 1 78  ? 35.087 50.299 61.992 1.00 99.93  ? 100 LYS A NZ  1 
ATOM   598  N  N   . PRO A 1 79  ? 32.493 46.524 54.534 1.00 68.66  ? 101 PRO A N   1 
ATOM   599  C  CA  . PRO A 1 79  ? 31.454 45.643 54.000 1.00 60.30  ? 101 PRO A CA  1 
ATOM   600  C  C   . PRO A 1 79  ? 31.642 44.218 54.493 1.00 51.42  ? 101 PRO A C   1 
ATOM   601  O  O   . PRO A 1 79  ? 32.712 43.827 54.961 1.00 68.69  ? 101 PRO A O   1 
ATOM   602  C  CB  . PRO A 1 79  ? 31.670 45.730 52.487 1.00 52.72  ? 101 PRO A CB  1 
ATOM   603  C  CG  . PRO A 1 79  ? 33.151 45.913 52.360 1.00 51.69  ? 101 PRO A CG  1 
ATOM   604  C  CD  . PRO A 1 79  ? 33.594 46.714 53.569 1.00 46.62  ? 101 PRO A CD  1 
ATOM   605  N  N   . ASP A 1 80  ? 30.572 43.437 54.387 1.00 42.18  ? 102 ASP A N   1 
ATOM   606  C  CA  . ASP A 1 80  ? 30.664 42.005 54.639 1.00 57.28  ? 102 ASP A CA  1 
ATOM   607  C  C   . ASP A 1 80  ? 30.303 41.195 53.402 1.00 48.97  ? 102 ASP A C   1 
ATOM   608  O  O   . ASP A 1 80  ? 30.169 39.967 53.490 1.00 61.45  ? 102 ASP A O   1 
ATOM   609  C  CB  . ASP A 1 80  ? 29.801 41.602 55.842 1.00 57.56  ? 102 ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 80  ? 28.551 42.439 55.979 1.00 55.02  ? 102 ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 80  ? 27.976 42.826 54.946 1.00 65.91  ? 102 ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 80  ? 28.155 42.726 57.126 1.00 56.88  ? 102 ASP A OD2 1 
ATOM   613  N  N   . LEU A 1 81  ? 30.160 41.853 52.252 1.00 58.66  ? 103 LEU A N   1 
ATOM   614  C  CA  . LEU A 1 81  ? 29.987 41.180 50.971 1.00 44.94  ? 103 LEU A CA  1 
ATOM   615  C  C   . LEU A 1 81  ? 30.397 42.142 49.867 1.00 51.58  ? 103 LEU A C   1 
ATOM   616  O  O   . LEU A 1 81  ? 29.928 43.286 49.834 1.00 43.35  ? 103 LEU A O   1 
ATOM   617  C  CB  . LEU A 1 81  ? 28.542 40.727 50.763 1.00 40.06  ? 103 LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 81  ? 28.284 40.081 49.404 1.00 41.10  ? 103 LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 81  ? 29.167 38.866 49.244 1.00 41.81  ? 103 LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 81  ? 26.828 39.702 49.253 1.00 45.48  ? 103 LEU A CD2 1 
ATOM   621  N  N   . ILE A 1 82  ? 31.277 41.685 48.981 1.00 51.40  ? 104 ILE A N   1 
ATOM   622  C  CA  . ILE A 1 82  ? 31.688 42.438 47.803 1.00 46.05  ? 104 ILE A CA  1 
ATOM   623  C  C   . ILE A 1 82  ? 31.282 41.638 46.577 1.00 55.04  ? 104 ILE A C   1 
ATOM   624  O  O   . ILE A 1 82  ? 31.583 40.442 46.484 1.00 51.08  ? 104 ILE A O   1 
ATOM   625  C  CB  . ILE A 1 82  ? 33.203 42.710 47.794 1.00 46.69  ? 104 ILE A CB  1 
ATOM   626  C  CG1 . ILE A 1 82  ? 33.614 43.508 49.028 1.00 40.36  ? 104 ILE A CG1 1 
ATOM   627  C  CG2 . ILE A 1 82  ? 33.599 43.476 46.540 1.00 39.73  ? 104 ILE A CG2 1 
ATOM   628  C  CD1 . ILE A 1 82  ? 35.113 43.609 49.192 1.00 38.08  ? 104 ILE A CD1 1 
ATOM   629  N  N   . ILE A 1 83  ? 30.592 42.285 45.647 1.00 46.49  ? 105 ILE A N   1 
ATOM   630  C  CA  . ILE A 1 83  ? 30.182 41.643 44.405 1.00 51.54  ? 105 ILE A CA  1 
ATOM   631  C  C   . ILE A 1 83  ? 30.980 42.282 43.280 1.00 47.54  ? 105 ILE A C   1 
ATOM   632  O  O   . ILE A 1 83  ? 30.783 43.458 42.945 1.00 53.28  ? 105 ILE A O   1 
ATOM   633  C  CB  . ILE A 1 83  ? 28.674 41.758 44.160 1.00 46.16  ? 105 ILE A CB  1 
ATOM   634  C  CG1 . ILE A 1 83  ? 27.904 41.516 45.464 1.00 54.22  ? 105 ILE A CG1 1 
ATOM   635  C  CG2 . ILE A 1 83  ? 28.262 40.757 43.097 1.00 34.81  ? 105 ILE A CG2 1 
ATOM   636  C  CD1 . ILE A 1 83  ? 26.385 41.462 45.308 1.00 48.11  ? 105 ILE A CD1 1 
ATOM   637  N  N   . ALA A 1 84  ? 31.887 41.508 42.701 1.00 42.33  ? 106 ALA A N   1 
ATOM   638  C  CA  . ALA A 1 84  ? 32.804 41.994 41.685 1.00 46.45  ? 106 ALA A CA  1 
ATOM   639  C  C   . ALA A 1 84  ? 32.447 41.398 40.329 1.00 49.92  ? 106 ALA A C   1 
ATOM   640  O  O   . ALA A 1 84  ? 31.635 40.474 40.221 1.00 42.91  ? 106 ALA A O   1 
ATOM   641  C  CB  . ALA A 1 84  ? 34.249 41.657 42.066 1.00 49.31  ? 106 ALA A CB  1 
ATOM   642  N  N   . ASP A 1 85  ? 33.056 41.954 39.284 1.00 53.78  ? 107 ASP A N   1 
ATOM   643  C  CA  . ASP A 1 85  ? 32.905 41.433 37.932 1.00 42.58  ? 107 ASP A CA  1 
ATOM   644  C  C   . ASP A 1 85  ? 33.971 40.389 37.649 1.00 46.91  ? 107 ASP A C   1 
ATOM   645  O  O   . ASP A 1 85  ? 35.142 40.567 37.997 1.00 62.76  ? 107 ASP A O   1 
ATOM   646  C  CB  . ASP A 1 85  ? 33.010 42.543 36.885 1.00 60.37  ? 107 ASP A CB  1 
ATOM   647  C  CG  . ASP A 1 85  ? 32.736 42.040 35.466 1.00 53.37  ? 107 ASP A CG  1 
ATOM   648  O  OD1 . ASP A 1 85  ? 33.312 41.016 35.040 1.00 75.11  ? 107 ASP A OD1 1 
ATOM   649  O  OD2 . ASP A 1 85  ? 31.931 42.668 34.761 1.00 53.54  ? 107 ASP A OD2 1 
ATOM   650  N  N   . ALA A 1 86  ? 33.564 39.325 36.958 1.00 44.22  ? 108 ALA A N   1 
ATOM   651  C  CA  . ALA A 1 86  ? 34.493 38.248 36.639 1.00 58.87  ? 108 ALA A CA  1 
ATOM   652  C  C   . ALA A 1 86  ? 35.538 38.695 35.624 1.00 54.59  ? 108 ALA A C   1 
ATOM   653  O  O   . ALA A 1 86  ? 36.710 38.312 35.723 1.00 65.92  ? 108 ALA A O   1 
ATOM   654  C  CB  . ALA A 1 86  ? 33.718 37.038 36.125 1.00 57.36  ? 108 ALA A CB  1 
ATOM   655  N  N   . GLU A 1 87  ? 35.136 39.515 34.648 1.00 50.42  ? 109 GLU A N   1 
ATOM   656  C  CA  . GLU A 1 87  ? 36.061 40.008 33.630 1.00 56.45  ? 109 GLU A CA  1 
ATOM   657  C  C   . GLU A 1 87  ? 36.960 41.122 34.164 1.00 57.35  ? 109 GLU A C   1 
ATOM   658  O  O   . GLU A 1 87  ? 38.181 41.094 33.969 1.00 66.08  ? 109 GLU A O   1 
ATOM   659  C  CB  . GLU A 1 87  ? 35.277 40.505 32.415 1.00 50.17  ? 109 GLU A CB  1 
ATOM   660  C  CG  . GLU A 1 87  ? 36.111 41.322 31.444 1.00 73.09  ? 109 GLU A CG  1 
ATOM   661  C  CD  . GLU A 1 87  ? 35.266 42.006 30.391 1.00 87.29  ? 109 GLU A CD  1 
ATOM   662  O  OE1 . GLU A 1 87  ? 34.396 41.334 29.794 1.00 80.61  ? 109 GLU A OE1 1 
ATOM   663  O  OE2 . GLU A 1 87  ? 35.466 43.220 30.168 1.00 91.58  ? 109 GLU A OE2 1 
ATOM   664  N  N   . ARG A 1 88  ? 36.367 42.104 34.847 1.00 46.26  ? 110 ARG A N   1 
ATOM   665  C  CA  . ARG A 1 88  ? 37.070 43.322 35.221 1.00 46.79  ? 110 ARG A CA  1 
ATOM   666  C  C   . ARG A 1 88  ? 37.953 43.153 36.446 1.00 44.87  ? 110 ARG A C   1 
ATOM   667  O  O   . ARG A 1 88  ? 38.954 43.865 36.575 1.00 63.08  ? 110 ARG A O   1 
ATOM   668  C  CB  . ARG A 1 88  ? 36.072 44.448 35.501 1.00 46.73  ? 110 ARG A CB  1 
ATOM   669  C  CG  . ARG A 1 88  ? 35.276 44.922 34.312 1.00 53.48  ? 110 ARG A CG  1 
ATOM   670  C  CD  . ARG A 1 88  ? 35.300 46.433 34.240 1.00 87.68  ? 110 ARG A CD  1 
ATOM   671  N  NE  . ARG A 1 88  ? 34.409 46.932 33.202 1.00 92.00  ? 110 ARG A NE  1 
ATOM   672  C  CZ  . ARG A 1 88  ? 34.193 48.215 32.955 1.00 79.31  ? 110 ARG A CZ  1 
ATOM   673  N  NH1 . ARG A 1 88  ? 34.793 49.164 33.655 1.00 107.40 ? 110 ARG A NH1 1 
ATOM   674  N  NH2 . ARG A 1 88  ? 33.357 48.555 31.979 1.00 91.14  ? 110 ARG A NH2 1 
ATOM   675  N  N   . HIS A 1 89  ? 37.597 42.262 37.371 1.00 53.78  ? 111 HIS A N   1 
ATOM   676  C  CA  . HIS A 1 89  ? 38.222 42.254 38.689 1.00 56.71  ? 111 HIS A CA  1 
ATOM   677  C  C   . HIS A 1 89  ? 38.887 40.923 39.014 1.00 38.51  ? 111 HIS A C   1 
ATOM   678  O  O   . HIS A 1 89  ? 39.049 40.574 40.185 1.00 56.90  ? 111 HIS A O   1 
ATOM   679  C  CB  . HIS A 1 89  ? 37.196 42.624 39.755 1.00 42.10  ? 111 HIS A CB  1 
ATOM   680  C  CG  . HIS A 1 89  ? 36.484 43.903 39.460 1.00 59.88  ? 111 HIS A CG  1 
ATOM   681  N  ND1 . HIS A 1 89  ? 35.111 44.018 39.489 1.00 41.72  ? 111 HIS A ND1 1 
ATOM   682  C  CD2 . HIS A 1 89  ? 36.959 45.118 39.104 1.00 57.29  ? 111 HIS A CD2 1 
ATOM   683  C  CE1 . HIS A 1 89  ? 34.773 45.254 39.170 1.00 51.31  ? 111 HIS A CE1 1 
ATOM   684  N  NE2 . HIS A 1 89  ? 35.876 45.942 38.934 1.00 44.21  ? 111 HIS A NE2 1 
ATOM   685  N  N   . ARG A 1 90  ? 39.293 40.180 37.986 1.00 46.34  ? 112 ARG A N   1 
ATOM   686  C  CA  . ARG A 1 90  ? 40.037 38.948 38.226 1.00 60.17  ? 112 ARG A CA  1 
ATOM   687  C  C   . ARG A 1 90  ? 41.349 39.233 38.948 1.00 47.14  ? 112 ARG A C   1 
ATOM   688  O  O   . ARG A 1 90  ? 41.699 38.544 39.914 1.00 59.81  ? 112 ARG A O   1 
ATOM   689  C  CB  . ARG A 1 90  ? 40.292 38.227 36.904 1.00 55.78  ? 112 ARG A CB  1 
ATOM   690  C  CG  . ARG A 1 90  ? 40.533 36.731 37.050 1.00 89.74  ? 112 ARG A CG  1 
ATOM   691  C  CD  . ARG A 1 90  ? 39.242 35.999 37.360 1.00 98.40  ? 112 ARG A CD  1 
ATOM   692  N  NE  . ARG A 1 90  ? 38.239 36.255 36.334 1.00 113.32 ? 112 ARG A NE  1 
ATOM   693  C  CZ  . ARG A 1 90  ? 38.089 35.527 35.237 1.00 118.96 ? 112 ARG A CZ  1 
ATOM   694  N  NH1 . ARG A 1 90  ? 38.835 34.458 35.010 1.00 131.19 ? 112 ARG A NH1 1 
ATOM   695  N  NH2 . ARG A 1 90  ? 37.171 35.882 34.343 1.00 109.30 ? 112 ARG A NH2 1 
ATOM   696  N  N   . ALA A 1 91  ? 42.075 40.263 38.510 1.00 41.69  ? 113 ALA A N   1 
ATOM   697  C  CA  . ALA A 1 91  ? 43.361 40.572 39.125 1.00 54.31  ? 113 ALA A CA  1 
ATOM   698  C  C   . ALA A 1 91  ? 43.201 41.025 40.573 1.00 47.41  ? 113 ALA A C   1 
ATOM   699  O  O   . ALA A 1 91  ? 43.963 40.594 41.446 1.00 69.70  ? 113 ALA A O   1 
ATOM   700  C  CB  . ALA A 1 91  ? 44.096 41.631 38.304 1.00 40.50  ? 113 ALA A CB  1 
ATOM   701  N  N   . ILE A 1 92  ? 42.215 41.885 40.861 1.00 49.15  ? 114 ILE A N   1 
ATOM   702  C  CA  . ILE A 1 92  ? 42.067 42.414 42.216 1.00 47.80  ? 114 ILE A CA  1 
ATOM   703  C  C   . ILE A 1 92  ? 41.173 41.558 43.098 1.00 41.63  ? 114 ILE A C   1 
ATOM   704  O  O   . ILE A 1 92  ? 40.915 41.940 44.249 1.00 56.38  ? 114 ILE A O   1 
ATOM   705  C  CB  . ILE A 1 92  ? 41.508 43.851 42.227 1.00 53.74  ? 114 ILE A CB  1 
ATOM   706  C  CG1 . ILE A 1 92  ? 40.070 43.870 41.699 1.00 50.35  ? 114 ILE A CG1 1 
ATOM   707  C  CG2 . ILE A 1 92  ? 42.409 44.776 41.430 1.00 42.54  ? 114 ILE A CG2 1 
ATOM   708  C  CD1 . ILE A 1 92  ? 39.409 45.231 41.776 1.00 53.00  ? 114 ILE A CD1 1 
ATOM   709  N  N   . TYR A 1 93  ? 40.696 40.413 42.603 1.00 42.49  ? 115 TYR A N   1 
ATOM   710  C  CA  . TYR A 1 93  ? 39.779 39.582 43.381 1.00 47.55  ? 115 TYR A CA  1 
ATOM   711  C  C   . TYR A 1 93  ? 40.382 39.190 44.720 1.00 50.14  ? 115 TYR A C   1 
ATOM   712  O  O   . TYR A 1 93  ? 39.750 39.349 45.772 1.00 66.97  ? 115 TYR A O   1 
ATOM   713  C  CB  . TYR A 1 93  ? 39.402 38.326 42.598 1.00 49.22  ? 115 TYR A CB  1 
ATOM   714  C  CG  . TYR A 1 93  ? 38.681 37.287 43.438 1.00 66.24  ? 115 TYR A CG  1 
ATOM   715  C  CD1 . TYR A 1 93  ? 37.332 37.427 43.738 1.00 50.55  ? 115 TYR A CD1 1 
ATOM   716  C  CD2 . TYR A 1 93  ? 39.348 36.167 43.933 1.00 63.67  ? 115 TYR A CD2 1 
ATOM   717  C  CE1 . TYR A 1 93  ? 36.665 36.487 44.500 1.00 63.39  ? 115 TYR A CE1 1 
ATOM   718  C  CE2 . TYR A 1 93  ? 38.685 35.215 44.695 1.00 57.00  ? 115 TYR A CE2 1 
ATOM   719  C  CZ  . TYR A 1 93  ? 37.343 35.385 44.980 1.00 72.24  ? 115 TYR A CZ  1 
ATOM   720  O  OH  . TYR A 1 93  ? 36.670 34.449 45.734 1.00 73.22  ? 115 TYR A OH  1 
ATOM   721  N  N   . GLN A 1 94  ? 41.605 38.661 44.699 1.00 66.45  ? 116 GLN A N   1 
ATOM   722  C  CA  . GLN A 1 94  ? 42.232 38.217 45.936 1.00 56.92  ? 116 GLN A CA  1 
ATOM   723  C  C   . GLN A 1 94  ? 42.435 39.376 46.902 1.00 63.14  ? 116 GLN A C   1 
ATOM   724  O  O   . GLN A 1 94  ? 42.326 39.195 48.121 1.00 64.03  ? 116 GLN A O   1 
ATOM   725  C  CB  . GLN A 1 94  ? 43.553 37.519 45.622 1.00 55.75  ? 116 GLN A CB  1 
ATOM   726  C  CG  . GLN A 1 94  ? 43.696 36.179 46.311 1.00 62.88  ? 116 GLN A CG  1 
ATOM   727  C  CD  . GLN A 1 94  ? 42.543 35.244 46.009 1.00 70.04  ? 116 GLN A CD  1 
ATOM   728  O  OE1 . GLN A 1 94  ? 42.311 34.879 44.855 1.00 67.08  ? 116 GLN A OE1 1 
ATOM   729  N  NE2 . GLN A 1 94  ? 41.809 34.851 47.051 1.00 64.96  ? 116 GLN A NE2 1 
ATOM   730  N  N   . ASP A 1 95  ? 42.707 40.574 46.380 1.00 55.95  ? 117 ASP A N   1 
ATOM   731  C  CA  . ASP A 1 95  ? 42.777 41.757 47.231 1.00 60.56  ? 117 ASP A CA  1 
ATOM   732  C  C   . ASP A 1 95  ? 41.404 42.116 47.782 1.00 60.16  ? 117 ASP A C   1 
ATOM   733  O  O   . ASP A 1 95  ? 41.286 42.569 48.926 1.00 55.04  ? 117 ASP A O   1 
ATOM   734  C  CB  . ASP A 1 95  ? 43.365 42.930 46.450 1.00 66.04  ? 117 ASP A CB  1 
ATOM   735  C  CG  . ASP A 1 95  ? 44.763 42.648 45.946 1.00 68.85  ? 117 ASP A CG  1 
ATOM   736  O  OD1 . ASP A 1 95  ? 45.581 42.130 46.737 1.00 71.88  ? 117 ASP A OD1 1 
ATOM   737  O  OD2 . ASP A 1 95  ? 45.041 42.927 44.760 1.00 63.04  ? 117 ASP A OD2 1 
ATOM   738  N  N   . LEU A 1 96  ? 40.355 41.926 46.977 1.00 61.90  ? 118 LEU A N   1 
ATOM   739  C  CA  . LEU A 1 96  ? 38.999 42.149 47.467 1.00 56.18  ? 118 LEU A CA  1 
ATOM   740  C  C   . LEU A 1 96  ? 38.645 41.161 48.573 1.00 60.68  ? 118 LEU A C   1 
ATOM   741  O  O   . LEU A 1 96  ? 37.966 41.522 49.542 1.00 54.57  ? 118 LEU A O   1 
ATOM   742  C  CB  . LEU A 1 96  ? 37.996 42.053 46.315 1.00 48.99  ? 118 LEU A CB  1 
ATOM   743  C  CG  . LEU A 1 96  ? 38.028 43.157 45.251 1.00 57.44  ? 118 LEU A CG  1 
ATOM   744  C  CD1 . LEU A 1 96  ? 37.069 42.828 44.127 1.00 44.23  ? 118 LEU A CD1 1 
ATOM   745  C  CD2 . LEU A 1 96  ? 37.712 44.536 45.843 1.00 43.60  ? 118 LEU A CD2 1 
ATOM   746  N  N   . GLN A 1 97  ? 39.102 39.908 48.453 1.00 54.92  ? 119 GLN A N   1 
ATOM   747  C  CA  . GLN A 1 97  ? 38.811 38.919 49.488 1.00 50.04  ? 119 GLN A CA  1 
ATOM   748  C  C   . GLN A 1 97  ? 39.447 39.293 50.814 1.00 57.53  ? 119 GLN A C   1 
ATOM   749  O  O   . GLN A 1 97  ? 38.946 38.898 51.873 1.00 55.07  ? 119 GLN A O   1 
ATOM   750  C  CB  . GLN A 1 97  ? 39.294 37.537 49.063 1.00 61.44  ? 119 GLN A CB  1 
ATOM   751  C  CG  . GLN A 1 97  ? 38.458 36.909 47.982 1.00 70.94  ? 119 GLN A CG  1 
ATOM   752  C  CD  . GLN A 1 97  ? 37.876 35.581 48.405 1.00 89.62  ? 119 GLN A CD  1 
ATOM   753  O  OE1 . GLN A 1 97  ? 38.605 34.596 48.578 1.00 79.97  ? 119 GLN A OE1 1 
ATOM   754  N  NE2 . GLN A 1 97  ? 36.552 35.541 48.578 1.00 59.93  ? 119 GLN A NE2 1 
ATOM   755  N  N   . ARG A 1 98  ? 40.554 40.040 50.781 1.00 58.84  ? 120 ARG A N   1 
ATOM   756  C  CA  . ARG A 1 98  ? 41.163 40.485 52.028 1.00 60.88  ? 120 ARG A CA  1 
ATOM   757  C  C   . ARG A 1 98  ? 40.235 41.420 52.787 1.00 56.05  ? 120 ARG A C   1 
ATOM   758  O  O   . ARG A 1 98  ? 40.281 41.475 54.021 1.00 61.64  ? 120 ARG A O   1 
ATOM   759  C  CB  . ARG A 1 98  ? 42.507 41.176 51.766 1.00 56.95  ? 120 ARG A CB  1 
ATOM   760  C  CG  . ARG A 1 98  ? 43.530 40.387 50.930 1.00 71.42  ? 120 ARG A CG  1 
ATOM   761  C  CD  . ARG A 1 98  ? 43.529 38.895 51.234 1.00 76.81  ? 120 ARG A CD  1 
ATOM   762  N  NE  . ARG A 1 98  ? 43.573 38.621 52.665 1.00 87.68  ? 120 ARG A NE  1 
ATOM   763  C  CZ  . ARG A 1 98  ? 43.020 37.560 53.234 1.00 101.13 ? 120 ARG A CZ  1 
ATOM   764  N  NH1 . ARG A 1 98  ? 42.402 36.635 52.519 1.00 91.51  ? 120 ARG A NH1 1 
ATOM   765  N  NH2 . ARG A 1 98  ? 43.077 37.430 54.556 1.00 88.15  ? 120 ARG A NH2 1 
ATOM   766  N  N   . ILE A 1 99  ? 39.382 42.152 52.071 1.00 58.16  ? 121 ILE A N   1 
ATOM   767  C  CA  . ILE A 1 99  ? 38.473 43.088 52.722 1.00 50.71  ? 121 ILE A CA  1 
ATOM   768  C  C   . ILE A 1 99  ? 37.244 42.364 53.260 1.00 47.57  ? 121 ILE A C   1 
ATOM   769  O  O   . ILE A 1 99  ? 36.838 42.572 54.408 1.00 51.35  ? 121 ILE A O   1 
ATOM   770  C  CB  . ILE A 1 99  ? 38.086 44.214 51.748 1.00 53.42  ? 121 ILE A CB  1 
ATOM   771  C  CG1 . ILE A 1 99  ? 39.346 44.889 51.203 1.00 52.78  ? 121 ILE A CG1 1 
ATOM   772  C  CG2 . ILE A 1 99  ? 37.172 45.227 52.437 1.00 44.37  ? 121 ILE A CG2 1 
ATOM   773  C  CD1 . ILE A 1 99  ? 39.066 45.972 50.190 1.00 66.15  ? 121 ILE A CD1 1 
ATOM   774  N  N   . ALA A 1 100 ? 36.638 41.509 52.447 1.00 44.73  ? 122 ALA A N   1 
ATOM   775  C  CA  . ALA A 1 100 ? 35.402 40.833 52.814 1.00 61.54  ? 122 ALA A CA  1 
ATOM   776  C  C   . ALA A 1 100 ? 35.175 39.689 51.830 1.00 48.16  ? 122 ALA A C   1 
ATOM   777  O  O   . ALA A 1 100 ? 35.825 39.640 50.781 1.00 57.46  ? 122 ALA A O   1 
ATOM   778  C  CB  . ALA A 1 100 ? 34.210 41.806 52.804 1.00 60.35  ? 122 ALA A CB  1 
ATOM   779  N  N   . PRO A 1 101 ? 34.285 38.751 52.156 1.00 60.32  ? 123 PRO A N   1 
ATOM   780  C  CA  . PRO A 1 101 ? 33.930 37.708 51.183 1.00 44.39  ? 123 PRO A CA  1 
ATOM   781  C  C   . PRO A 1 101 ? 33.456 38.322 49.876 1.00 59.74  ? 123 PRO A C   1 
ATOM   782  O  O   . PRO A 1 101 ? 32.570 39.180 49.855 1.00 48.79  ? 123 PRO A O   1 
ATOM   783  C  CB  . PRO A 1 101 ? 32.810 36.937 51.886 1.00 55.52  ? 123 PRO A CB  1 
ATOM   784  C  CG  . PRO A 1 101 ? 33.086 37.123 53.330 1.00 52.24  ? 123 PRO A CG  1 
ATOM   785  C  CD  . PRO A 1 101 ? 33.682 38.501 53.477 1.00 51.81  ? 123 PRO A CD  1 
ATOM   786  N  N   . THR A 1 102 ? 34.063 37.887 48.777 1.00 52.09  ? 124 THR A N   1 
ATOM   787  C  CA  . THR A 1 102 ? 33.832 38.483 47.471 1.00 43.49  ? 124 THR A CA  1 
ATOM   788  C  C   . THR A 1 102 ? 33.238 37.446 46.527 1.00 41.93  ? 124 THR A C   1 
ATOM   789  O  O   . THR A 1 102 ? 33.743 36.321 46.430 1.00 45.22  ? 124 THR A O   1 
ATOM   790  C  CB  . THR A 1 102 ? 35.134 39.063 46.904 1.00 45.96  ? 124 THR A CB  1 
ATOM   791  O  OG1 . THR A 1 102 ? 35.700 39.966 47.859 1.00 45.97  ? 124 THR A OG1 1 
ATOM   792  C  CG2 . THR A 1 102 ? 34.873 39.815 45.611 1.00 41.21  ? 124 THR A CG2 1 
ATOM   793  N  N   . LEU A 1 103 ? 32.168 37.838 45.838 1.00 53.38  ? 125 LEU A N   1 
ATOM   794  C  CA  . LEU A 1 103 ? 31.470 37.010 44.862 1.00 44.62  ? 125 LEU A CA  1 
ATOM   795  C  C   . LEU A 1 103 ? 31.826 37.495 43.463 1.00 49.43  ? 125 LEU A C   1 
ATOM   796  O  O   . LEU A 1 103 ? 31.573 38.656 43.124 1.00 56.09  ? 125 LEU A O   1 
ATOM   797  C  CB  . LEU A 1 103 ? 29.960 37.082 45.087 1.00 42.27  ? 125 LEU A CB  1 
ATOM   798  C  CG  . LEU A 1 103 ? 29.020 36.153 44.326 1.00 55.12  ? 125 LEU A CG  1 
ATOM   799  C  CD1 . LEU A 1 103 ? 29.400 34.703 44.562 1.00 50.11  ? 125 LEU A CD1 1 
ATOM   800  C  CD2 . LEU A 1 103 ? 27.602 36.419 44.787 1.00 49.13  ? 125 LEU A CD2 1 
ATOM   801  N  N   . LEU A 1 104 ? 32.405 36.611 42.652 1.00 42.14  ? 126 LEU A N   1 
ATOM   802  C  CA  . LEU A 1 104 ? 32.901 36.963 41.323 1.00 48.71  ? 126 LEU A CA  1 
ATOM   803  C  C   . LEU A 1 104 ? 31.867 36.558 40.276 1.00 48.29  ? 126 LEU A C   1 
ATOM   804  O  O   . LEU A 1 104 ? 31.744 35.373 39.946 1.00 53.93  ? 126 LEU A O   1 
ATOM   805  C  CB  . LEU A 1 104 ? 34.242 36.282 41.049 1.00 57.75  ? 126 LEU A CB  1 
ATOM   806  C  CG  . LEU A 1 104 ? 35.021 37.002 39.950 1.00 57.25  ? 126 LEU A CG  1 
ATOM   807  C  CD1 . LEU A 1 104 ? 35.603 38.296 40.486 1.00 53.29  ? 126 LEU A CD1 1 
ATOM   808  C  CD2 . LEU A 1 104 ? 36.093 36.134 39.332 1.00 63.19  ? 126 LEU A CD2 1 
ATOM   809  N  N   . LEU A 1 105 ? 31.148 37.537 39.725 1.00 49.88  ? 127 LEU A N   1 
ATOM   810  C  CA  . LEU A 1 105 ? 30.056 37.246 38.803 1.00 45.11  ? 127 LEU A CA  1 
ATOM   811  C  C   . LEU A 1 105 ? 30.243 38.008 37.498 1.00 60.79  ? 127 LEU A C   1 
ATOM   812  O  O   . LEU A 1 105 ? 31.079 38.909 37.389 1.00 67.11  ? 127 LEU A O   1 
ATOM   813  C  CB  . LEU A 1 105 ? 28.696 37.576 39.431 1.00 47.17  ? 127 LEU A CB  1 
ATOM   814  C  CG  . LEU A 1 105 ? 28.326 36.762 40.671 1.00 49.00  ? 127 LEU A CG  1 
ATOM   815  C  CD1 . LEU A 1 105 ? 27.076 37.308 41.332 1.00 48.73  ? 127 LEU A CD1 1 
ATOM   816  C  CD2 . LEU A 1 105 ? 28.150 35.293 40.308 1.00 54.39  ? 127 LEU A CD2 1 
ATOM   817  N  N   . LYS A 1 106 ? 29.437 37.655 36.507 1.00 43.45  ? 128 LYS A N   1 
ATOM   818  C  CA  . LYS A 1 106 ? 29.582 38.220 35.178 1.00 65.98  ? 128 LYS A CA  1 
ATOM   819  C  C   . LYS A 1 106 ? 28.529 39.285 34.912 1.00 54.00  ? 128 LYS A C   1 
ATOM   820  O  O   . LYS A 1 106 ? 27.388 39.173 35.360 1.00 55.13  ? 128 LYS A O   1 
ATOM   821  C  CB  . LYS A 1 106 ? 29.470 37.116 34.144 1.00 48.22  ? 128 LYS A CB  1 
ATOM   822  C  CG  . LYS A 1 106 ? 28.502 36.068 34.593 1.00 51.42  ? 128 LYS A CG  1 
ATOM   823  C  CD  . LYS A 1 106 ? 28.357 34.973 33.570 1.00 63.56  ? 128 LYS A CD  1 
ATOM   824  C  CE  . LYS A 1 106 ? 29.696 34.358 33.240 1.00 55.10  ? 128 LYS A CE  1 
ATOM   825  N  NZ  . LYS A 1 106 ? 29.564 33.218 32.283 1.00 59.86  ? 128 LYS A NZ  1 
ATOM   826  N  N   . SER A 1 107 ? 28.928 40.319 34.182 1.00 67.55  ? 129 SER A N   1 
ATOM   827  C  CA  . SER A 1 107 ? 28.031 41.353 33.689 1.00 67.02  ? 129 SER A CA  1 
ATOM   828  C  C   . SER A 1 107 ? 28.519 41.897 32.350 1.00 59.47  ? 129 SER A C   1 
ATOM   829  O  O   . SER A 1 107 ? 27.748 41.969 31.383 1.00 66.64  ? 129 SER A O   1 
ATOM   830  C  CB  . SER A 1 107 ? 27.913 42.522 34.683 1.00 47.62  ? 129 SER A CB  1 
ATOM   831  O  OG  . SER A 1 107 ? 26.976 43.486 34.202 1.00 120.21 ? 129 SER A OG  1 
ATOM   832  N  N   . ARG A 1 108 ? 29.793 42.280 32.293 1.00 69.04  ? 130 ARG A N   1 
ATOM   833  C  CA  . ARG A 1 108 ? 30.338 42.864 31.091 1.00 66.76  ? 130 ARG A CA  1 
ATOM   834  C  C   . ARG A 1 108 ? 30.601 41.770 30.065 1.00 69.56  ? 130 ARG A C   1 
ATOM   835  O  O   . ARG A 1 108 ? 31.231 40.756 30.377 1.00 69.83  ? 130 ARG A O   1 
ATOM   836  C  CB  . ARG A 1 108 ? 31.606 43.632 31.434 1.00 65.53  ? 130 ARG A CB  1 
ATOM   837  C  CG  . ARG A 1 108 ? 32.319 44.187 30.235 1.00 67.66  ? 130 ARG A CG  1 
ATOM   838  C  CD  . ARG A 1 108 ? 32.366 45.688 30.248 1.00 106.22 ? 130 ARG A CD  1 
ATOM   839  N  NE  . ARG A 1 108 ? 32.933 46.194 29.008 1.00 102.79 ? 130 ARG A NE  1 
ATOM   840  C  CZ  . ARG A 1 108 ? 34.232 46.306 28.790 1.00 97.12  ? 130 ARG A CZ  1 
ATOM   841  N  NH1 . ARG A 1 108 ? 35.117 45.899 29.685 1.00 107.56 ? 130 ARG A NH1 1 
ATOM   842  N  NH2 . ARG A 1 108 ? 34.652 46.850 27.652 1.00 93.14  ? 130 ARG A NH2 1 
ATOM   843  N  N   . GLY A 1 109 ? 30.084 41.956 28.846 1.00 52.91  ? 131 GLY A N   1 
ATOM   844  C  CA  . GLY A 1 109 ? 30.340 41.008 27.767 1.00 58.23  ? 131 GLY A CA  1 
ATOM   845  C  C   . GLY A 1 109 ? 29.588 39.705 27.869 1.00 51.85  ? 131 GLY A C   1 
ATOM   846  O  O   . GLY A 1 109 ? 29.820 38.797 27.063 1.00 71.57  ? 131 GLY A O   1 
ATOM   847  N  N   . GLU A 1 110 ? 28.692 39.588 28.834 1.00 54.49  ? 132 GLU A N   1 
ATOM   848  C  CA  . GLU A 1 110 ? 27.918 38.378 29.028 1.00 57.25  ? 132 GLU A CA  1 
ATOM   849  C  C   . GLU A 1 110 ? 26.469 38.611 28.627 1.00 54.53  ? 132 GLU A C   1 
ATOM   850  O  O   . GLU A 1 110 ? 26.013 39.746 28.467 1.00 54.35  ? 132 GLU A O   1 
ATOM   851  C  CB  . GLU A 1 110 ? 28.008 37.906 30.476 1.00 55.09  ? 132 GLU A CB  1 
ATOM   852  C  CG  . GLU A 1 110 ? 28.950 36.731 30.637 1.00 79.73  ? 132 GLU A CG  1 
ATOM   853  C  CD  . GLU A 1 110 ? 30.403 37.117 30.509 1.00 66.20  ? 132 GLU A CD  1 
ATOM   854  O  OE1 . GLU A 1 110 ? 30.824 38.071 31.196 1.00 92.71  ? 132 GLU A OE1 1 
ATOM   855  O  OE2 . GLU A 1 110 ? 31.125 36.463 29.730 1.00 63.13  ? 132 GLU A OE2 1 
ATOM   856  N  N   . THR A 1 111 ? 25.749 37.510 28.453 1.00 52.04  ? 133 THR A N   1 
ATOM   857  C  CA  . THR A 1 111 ? 24.419 37.588 27.879 1.00 55.22  ? 133 THR A CA  1 
ATOM   858  C  C   . THR A 1 111 ? 23.420 38.152 28.884 1.00 54.44  ? 133 THR A C   1 
ATOM   859  O  O   . THR A 1 111 ? 23.689 38.284 30.082 1.00 54.09  ? 133 THR A O   1 
ATOM   860  C  CB  . THR A 1 111 ? 23.946 36.214 27.429 1.00 46.14  ? 133 THR A CB  1 
ATOM   861  O  OG1 . THR A 1 111 ? 23.731 35.402 28.585 1.00 53.89  ? 133 THR A OG1 1 
ATOM   862  C  CG2 . THR A 1 111 ? 24.993 35.564 26.548 1.00 43.87  ? 133 THR A CG2 1 
ATOM   863  N  N   . TYR A 1 112 ? 22.240 38.485 28.362 1.00 51.73  ? 134 TYR A N   1 
ATOM   864  C  CA  . TYR A 1 112 ? 21.123 38.866 29.217 1.00 50.51  ? 134 TYR A CA  1 
ATOM   865  C  C   . TYR A 1 112 ? 20.730 37.715 30.133 1.00 57.20  ? 134 TYR A C   1 
ATOM   866  O  O   . TYR A 1 112 ? 20.408 37.926 31.308 1.00 57.31  ? 134 TYR A O   1 
ATOM   867  C  CB  . TYR A 1 112 ? 19.954 39.317 28.339 1.00 54.18  ? 134 TYR A CB  1 
ATOM   868  C  CG  . TYR A 1 112 ? 18.585 39.310 28.984 1.00 59.62  ? 134 TYR A CG  1 
ATOM   869  C  CD1 . TYR A 1 112 ? 18.221 40.284 29.906 1.00 62.19  ? 134 TYR A CD1 1 
ATOM   870  C  CD2 . TYR A 1 112 ? 17.639 38.352 28.634 1.00 61.81  ? 134 TYR A CD2 1 
ATOM   871  C  CE1 . TYR A 1 112 ? 16.957 40.291 30.481 1.00 59.62  ? 134 TYR A CE1 1 
ATOM   872  C  CE2 . TYR A 1 112 ? 16.377 38.348 29.204 1.00 59.49  ? 134 TYR A CE2 1 
ATOM   873  C  CZ  . TYR A 1 112 ? 16.040 39.319 30.127 1.00 61.07  ? 134 TYR A CZ  1 
ATOM   874  O  OH  . TYR A 1 112 ? 14.787 39.318 30.696 1.00 72.20  ? 134 TYR A OH  1 
ATOM   875  N  N   . LYS A 1 113 ? 20.772 36.487 29.614 1.00 56.71  ? 135 LYS A N   1 
ATOM   876  C  CA  . LYS A 1 113 ? 20.534 35.313 30.446 1.00 57.39  ? 135 LYS A CA  1 
ATOM   877  C  C   . LYS A 1 113 ? 21.551 35.228 31.585 1.00 58.33  ? 135 LYS A C   1 
ATOM   878  O  O   . LYS A 1 113 ? 21.174 35.124 32.758 1.00 58.87  ? 135 LYS A O   1 
ATOM   879  C  CB  . LYS A 1 113 ? 20.571 34.053 29.581 1.00 51.38  ? 135 LYS A CB  1 
ATOM   880  C  CG  . LYS A 1 113 ? 20.801 32.769 30.357 1.00 79.63  ? 135 LYS A CG  1 
ATOM   881  C  CD  . LYS A 1 113 ? 21.365 31.656 29.469 1.00 99.27  ? 135 LYS A CD  1 
ATOM   882  C  CE  . LYS A 1 113 ? 22.823 31.903 29.056 1.00 101.93 ? 135 LYS A CE  1 
ATOM   883  N  NZ  . LYS A 1 113 ? 23.005 32.836 27.894 1.00 67.12  ? 135 LYS A NZ  1 
ATOM   884  N  N   . GLU A 1 114 ? 22.849 35.282 31.258 1.00 52.13  ? 136 GLU A N   1 
ATOM   885  C  CA  . GLU A 1 114 ? 23.878 35.178 32.292 1.00 45.49  ? 136 GLU A CA  1 
ATOM   886  C  C   . GLU A 1 114 ? 23.769 36.299 33.319 1.00 51.05  ? 136 GLU A C   1 
ATOM   887  O  O   . GLU A 1 114 ? 24.082 36.093 34.497 1.00 55.34  ? 136 GLU A O   1 
ATOM   888  C  CB  . GLU A 1 114 ? 25.269 35.179 31.659 1.00 45.40  ? 136 GLU A CB  1 
ATOM   889  C  CG  . GLU A 1 114 ? 25.588 33.935 30.850 1.00 51.20  ? 136 GLU A CG  1 
ATOM   890  C  CD  . GLU A 1 114 ? 26.850 34.081 30.014 1.00 66.94  ? 136 GLU A CD  1 
ATOM   891  O  OE1 . GLU A 1 114 ? 26.891 34.980 29.142 1.00 70.72  ? 136 GLU A OE1 1 
ATOM   892  O  OE2 . GLU A 1 114 ? 27.801 33.299 30.228 1.00 76.42  ? 136 GLU A OE2 1 
ATOM   893  N  N   . ASN A 1 115 ? 23.332 37.489 32.902 1.00 48.05  ? 137 ASN A N   1 
ATOM   894  C  CA  . ASN A 1 115 ? 23.092 38.539 33.881 1.00 43.96  ? 137 ASN A CA  1 
ATOM   895  C  C   . ASN A 1 115 ? 21.929 38.185 34.796 1.00 51.48  ? 137 ASN A C   1 
ATOM   896  O  O   . ASN A 1 115 ? 21.955 38.519 35.985 1.00 51.61  ? 137 ASN A O   1 
ATOM   897  C  CB  . ASN A 1 115 ? 22.850 39.872 33.181 1.00 52.59  ? 137 ASN A CB  1 
ATOM   898  C  CG  . ASN A 1 115 ? 24.139 40.607 32.893 1.00 55.90  ? 137 ASN A CG  1 
ATOM   899  O  OD1 . ASN A 1 115 ? 24.515 41.526 33.614 1.00 55.86  ? 137 ASN A OD1 1 
ATOM   900  N  ND2 . ASN A 1 115 ? 24.844 40.179 31.853 1.00 52.19  ? 137 ASN A ND2 1 
ATOM   901  N  N   . LEU A 1 116 ? 20.913 37.496 34.269 1.00 57.17  ? 138 LEU A N   1 
ATOM   902  C  CA  . LEU A 1 116 ? 19.845 36.995 35.127 1.00 58.75  ? 138 LEU A CA  1 
ATOM   903  C  C   . LEU A 1 116 ? 20.364 35.919 36.081 1.00 62.39  ? 138 LEU A C   1 
ATOM   904  O  O   . LEU A 1 116 ? 20.011 35.917 37.267 1.00 48.07  ? 138 LEU A O   1 
ATOM   905  C  CB  . LEU A 1 116 ? 18.688 36.466 34.274 1.00 51.91  ? 138 LEU A CB  1 
ATOM   906  C  CG  . LEU A 1 116 ? 17.873 37.515 33.502 1.00 47.77  ? 138 LEU A CG  1 
ATOM   907  C  CD1 . LEU A 1 116 ? 16.957 36.874 32.479 1.00 54.01  ? 138 LEU A CD1 1 
ATOM   908  C  CD2 . LEU A 1 116 ? 17.072 38.392 34.449 1.00 49.39  ? 138 LEU A CD2 1 
ATOM   909  N  N   . GLU A 1 117 ? 21.222 35.013 35.590 1.00 52.89  ? 139 GLU A N   1 
ATOM   910  C  CA  . GLU A 1 117 ? 21.822 34.007 36.466 1.00 44.70  ? 139 GLU A CA  1 
ATOM   911  C  C   . GLU A 1 117 ? 22.577 34.650 37.622 1.00 44.63  ? 139 GLU A C   1 
ATOM   912  O  O   . GLU A 1 117 ? 22.481 34.187 38.765 1.00 67.14  ? 139 GLU A O   1 
ATOM   913  C  CB  . GLU A 1 117 ? 22.757 33.097 35.674 1.00 52.48  ? 139 GLU A CB  1 
ATOM   914  C  CG  . GLU A 1 117 ? 22.062 32.204 34.670 1.00 51.26  ? 139 GLU A CG  1 
ATOM   915  C  CD  . GLU A 1 117 ? 23.037 31.338 33.895 1.00 88.73  ? 139 GLU A CD  1 
ATOM   916  O  OE1 . GLU A 1 117 ? 24.254 31.404 34.183 1.00 96.38  ? 139 GLU A OE1 1 
ATOM   917  O  OE2 . GLU A 1 117 ? 22.588 30.592 32.999 1.00 84.09  ? 139 GLU A OE2 1 
ATOM   918  N  N   . SER A 1 118 ? 23.335 35.716 37.348 1.00 50.62  ? 140 SER A N   1 
ATOM   919  C  CA  . SER A 1 118 ? 24.092 36.365 38.414 1.00 44.81  ? 140 SER A CA  1 
ATOM   920  C  C   . SER A 1 118 ? 23.172 36.981 39.455 1.00 36.09  ? 140 SER A C   1 
ATOM   921  O  O   . SER A 1 118 ? 23.516 37.016 40.641 1.00 56.77  ? 140 SER A O   1 
ATOM   922  C  CB  . SER A 1 118 ? 25.023 37.432 37.835 1.00 38.20  ? 140 SER A CB  1 
ATOM   923  O  OG  . SER A 1 118 ? 25.944 36.864 36.919 1.00 57.63  ? 140 SER A OG  1 
ATOM   924  N  N   . ALA A 1 119 ? 22.008 37.481 39.032 1.00 49.60  ? 141 ALA A N   1 
ATOM   925  C  CA  . ALA A 1 119 ? 21.046 38.019 39.987 1.00 57.71  ? 141 ALA A CA  1 
ATOM   926  C  C   . ALA A 1 119 ? 20.539 36.926 40.921 1.00 55.27  ? 141 ALA A C   1 
ATOM   927  O  O   . ALA A 1 119 ? 20.344 37.163 42.119 1.00 46.66  ? 141 ALA A O   1 
ATOM   928  C  CB  . ALA A 1 119 ? 19.885 38.681 39.244 1.00 34.72  ? 141 ALA A CB  1 
ATOM   929  N  N   . GLN A 1 120 ? 20.324 35.719 40.385 1.00 54.64  ? 142 GLN A N   1 
ATOM   930  C  CA  . GLN A 1 120 ? 19.947 34.578 41.216 1.00 60.22  ? 142 GLN A CA  1 
ATOM   931  C  C   . GLN A 1 120 ? 21.030 34.265 42.240 1.00 66.11  ? 142 GLN A C   1 
ATOM   932  O  O   . GLN A 1 120 ? 20.738 34.043 43.421 1.00 58.46  ? 142 GLN A O   1 
ATOM   933  C  CB  . GLN A 1 120 ? 19.671 33.357 40.334 1.00 66.13  ? 142 GLN A CB  1 
ATOM   934  C  CG  . GLN A 1 120 ? 19.656 32.006 41.072 1.00 52.10  ? 142 GLN A CG  1 
ATOM   935  C  CD  . GLN A 1 120 ? 18.570 31.918 42.140 1.00 98.27  ? 142 GLN A CD  1 
ATOM   936  O  OE1 . GLN A 1 120 ? 17.571 32.646 42.103 1.00 91.47  ? 142 GLN A OE1 1 
ATOM   937  N  NE2 . GLN A 1 120 ? 18.764 31.017 43.099 1.00 91.07  ? 142 GLN A NE2 1 
ATOM   938  N  N   . LYS A 1 121 ? 22.292 34.235 41.804 1.00 52.47  ? 143 LYS A N   1 
ATOM   939  C  CA  . LYS A 1 121 ? 23.373 33.940 42.736 1.00 47.30  ? 143 LYS A CA  1 
ATOM   940  C  C   . LYS A 1 121 ? 23.517 35.033 43.780 1.00 49.45  ? 143 LYS A C   1 
ATOM   941  O  O   . LYS A 1 121 ? 23.892 34.753 44.924 1.00 57.51  ? 143 LYS A O   1 
ATOM   942  C  CB  . LYS A 1 121 ? 24.678 33.738 41.971 1.00 39.53  ? 143 LYS A CB  1 
ATOM   943  C  CG  . LYS A 1 121 ? 24.521 32.737 40.844 1.00 40.81  ? 143 LYS A CG  1 
ATOM   944  C  CD  . LYS A 1 121 ? 25.847 32.322 40.244 1.00 53.65  ? 143 LYS A CD  1 
ATOM   945  C  CE  . LYS A 1 121 ? 25.618 31.500 38.985 1.00 44.44  ? 143 LYS A CE  1 
ATOM   946  N  NZ  . LYS A 1 121 ? 26.825 30.720 38.609 1.00 72.27  ? 143 LYS A NZ  1 
ATOM   947  N  N   . ILE A 1 122 ? 23.208 36.276 43.413 1.00 52.82  ? 144 ILE A N   1 
ATOM   948  C  CA  . ILE A 1 122 ? 23.218 37.352 44.393 1.00 45.93  ? 144 ILE A CA  1 
ATOM   949  C  C   . ILE A 1 122 ? 22.116 37.134 45.422 1.00 46.91  ? 144 ILE A C   1 
ATOM   950  O  O   . ILE A 1 122 ? 22.337 37.287 46.629 1.00 49.71  ? 144 ILE A O   1 
ATOM   951  C  CB  . ILE A 1 122 ? 23.092 38.716 43.690 1.00 53.53  ? 144 ILE A CB  1 
ATOM   952  C  CG1 . ILE A 1 122 ? 24.369 39.043 42.914 1.00 51.88  ? 144 ILE A CG1 1 
ATOM   953  C  CG2 . ILE A 1 122 ? 22.832 39.815 44.684 1.00 39.36  ? 144 ILE A CG2 1 
ATOM   954  C  CD1 . ILE A 1 122 ? 24.326 40.388 42.221 1.00 46.73  ? 144 ILE A CD1 1 
ATOM   955  N  N   . GLY A 1 123 ? 20.921 36.743 44.964 1.00 67.88  ? 145 GLY A N   1 
ATOM   956  C  CA  . GLY A 1 123 ? 19.840 36.445 45.891 1.00 60.70  ? 145 GLY A CA  1 
ATOM   957  C  C   . GLY A 1 123 ? 20.203 35.362 46.890 1.00 60.94  ? 145 GLY A C   1 
ATOM   958  O  O   . GLY A 1 123 ? 19.827 35.435 48.062 1.00 52.05  ? 145 GLY A O   1 
ATOM   959  N  N   . VAL A 1 124 ? 20.947 34.348 46.446 1.00 49.72  ? 146 VAL A N   1 
ATOM   960  C  CA  . VAL A 1 124 ? 21.425 33.331 47.375 1.00 58.26  ? 146 VAL A CA  1 
ATOM   961  C  C   . VAL A 1 124 ? 22.395 33.941 48.375 1.00 53.65  ? 146 VAL A C   1 
ATOM   962  O  O   . VAL A 1 124 ? 22.236 33.789 49.592 1.00 67.30  ? 146 VAL A O   1 
ATOM   963  C  CB  . VAL A 1 124 ? 22.077 32.168 46.610 1.00 51.92  ? 146 VAL A CB  1 
ATOM   964  C  CG1 . VAL A 1 124 ? 22.609 31.131 47.589 1.00 48.17  ? 146 VAL A CG1 1 
ATOM   965  C  CG2 . VAL A 1 124 ? 21.086 31.547 45.652 1.00 46.49  ? 146 VAL A CG2 1 
ATOM   966  N  N   . ALA A 1 125 ? 23.405 34.655 47.877 1.00 60.93  ? 147 ALA A N   1 
ATOM   967  C  CA  . ALA A 1 125 ? 24.477 35.123 48.747 1.00 51.15  ? 147 ALA A CA  1 
ATOM   968  C  C   . ALA A 1 125 ? 23.968 36.095 49.800 1.00 47.73  ? 147 ALA A C   1 
ATOM   969  O  O   . ALA A 1 125 ? 24.558 36.198 50.880 1.00 56.77  ? 147 ALA A O   1 
ATOM   970  C  CB  . ALA A 1 125 ? 25.585 35.761 47.913 1.00 46.93  ? 147 ALA A CB  1 
ATOM   971  N  N   . ILE A 1 126 ? 22.873 36.805 49.518 1.00 46.45  ? 148 ILE A N   1 
ATOM   972  C  CA  . ILE A 1 126 ? 22.315 37.746 50.485 1.00 59.66  ? 148 ILE A CA  1 
ATOM   973  C  C   . ILE A 1 126 ? 21.201 37.142 51.326 1.00 56.83  ? 148 ILE A C   1 
ATOM   974  O  O   . ILE A 1 126 ? 20.775 37.769 52.309 1.00 57.95  ? 148 ILE A O   1 
ATOM   975  C  CB  . ILE A 1 126 ? 21.806 39.033 49.802 1.00 52.80  ? 148 ILE A CB  1 
ATOM   976  C  CG1 . ILE A 1 126 ? 20.605 38.734 48.908 1.00 52.53  ? 148 ILE A CG1 1 
ATOM   977  C  CG2 . ILE A 1 126 ? 22.912 39.668 48.984 1.00 42.19  ? 148 ILE A CG2 1 
ATOM   978  C  CD1 . ILE A 1 126 ? 20.046 39.964 48.230 1.00 49.82  ? 148 ILE A CD1 1 
ATOM   979  N  N   . GLY A 1 127 ? 20.714 35.954 50.981 1.00 63.97  ? 149 GLY A N   1 
ATOM   980  C  CA  . GLY A 1 127 ? 19.696 35.315 51.788 1.00 63.24  ? 149 GLY A CA  1 
ATOM   981  C  C   . GLY A 1 127 ? 18.285 35.663 51.369 1.00 62.99  ? 149 GLY A C   1 
ATOM   982  O  O   . GLY A 1 127 ? 17.395 35.790 52.220 1.00 59.22  ? 149 GLY A O   1 
ATOM   983  N  N   . LYS A 1 128 ? 18.070 35.825 50.067 1.00 55.10  ? 150 LYS A N   1 
ATOM   984  C  CA  . LYS A 1 128 ? 16.746 36.088 49.508 1.00 34.17  ? 150 LYS A CA  1 
ATOM   985  C  C   . LYS A 1 128 ? 16.506 35.242 48.263 1.00 52.03  ? 150 LYS A C   1 
ATOM   986  O  O   . LYS A 1 128 ? 15.943 35.719 47.273 1.00 50.14  ? 150 LYS A O   1 
ATOM   987  C  CB  . LYS A 1 128 ? 16.562 37.571 49.188 1.00 44.12  ? 150 LYS A CB  1 
ATOM   988  C  CG  . LYS A 1 128 ? 16.710 38.486 50.396 1.00 40.08  ? 150 LYS A CG  1 
ATOM   989  C  CD  . LYS A 1 128 ? 16.098 39.854 50.138 1.00 43.18  ? 150 LYS A CD  1 
ATOM   990  C  CE  . LYS A 1 128 ? 16.089 40.697 51.409 1.00 40.76  ? 150 LYS A CE  1 
ATOM   991  N  NZ  . LYS A 1 128 ? 15.651 42.096 51.140 1.00 57.52  ? 150 LYS A NZ  1 
ATOM   992  N  N   . GLN A 1 129 ? 16.926 33.970 48.304 1.00 39.74  ? 151 GLN A N   1 
ATOM   993  C  CA  . GLN A 1 129 ? 16.663 33.043 47.204 1.00 45.21  ? 151 GLN A CA  1 
ATOM   994  C  C   . GLN A 1 129 ? 15.200 33.078 46.776 1.00 56.69  ? 151 GLN A C   1 
ATOM   995  O  O   . GLN A 1 129 ? 14.891 33.194 45.586 1.00 67.76  ? 151 GLN A O   1 
ATOM   996  C  CB  . GLN A 1 129 ? 17.040 31.613 47.606 1.00 57.27  ? 151 GLN A CB  1 
ATOM   997  C  CG  . GLN A 1 129 ? 18.482 31.384 48.024 1.00 73.38  ? 151 GLN A CG  1 
ATOM   998  C  CD  . GLN A 1 129 ? 18.772 31.754 49.479 1.00 82.31  ? 151 GLN A CD  1 
ATOM   999  O  OE1 . GLN A 1 129 ? 18.043 32.533 50.107 1.00 66.30  ? 151 GLN A OE1 1 
ATOM   1000 N  NE2 . GLN A 1 129 ? 19.850 31.190 50.020 1.00 75.05  ? 151 GLN A NE2 1 
ATOM   1001 N  N   . ALA A 1 130 ? 14.282 32.955 47.736 1.00 59.34  ? 152 ALA A N   1 
ATOM   1002 C  CA  . ALA A 1 130 ? 12.871 32.858 47.380 1.00 65.33  ? 152 ALA A CA  1 
ATOM   1003 C  C   . ALA A 1 130 ? 12.369 34.167 46.787 1.00 58.27  ? 152 ALA A C   1 
ATOM   1004 O  O   . ALA A 1 130 ? 11.705 34.175 45.744 1.00 56.32  ? 152 ALA A O   1 
ATOM   1005 C  CB  . ALA A 1 130 ? 12.043 32.459 48.601 1.00 46.88  ? 152 ALA A CB  1 
ATOM   1006 N  N   . GLN A 1 131 ? 12.696 35.290 47.428 1.00 61.29  ? 153 GLN A N   1 
ATOM   1007 C  CA  . GLN A 1 131 ? 12.240 36.578 46.919 1.00 52.58  ? 153 GLN A CA  1 
ATOM   1008 C  C   . GLN A 1 131 ? 12.884 36.902 45.573 1.00 62.53  ? 153 GLN A C   1 
ATOM   1009 O  O   . GLN A 1 131 ? 12.197 37.350 44.647 1.00 69.71  ? 153 GLN A O   1 
ATOM   1010 C  CB  . GLN A 1 131 ? 12.521 37.672 47.948 1.00 45.00  ? 153 GLN A CB  1 
ATOM   1011 C  CG  . GLN A 1 131 ? 11.908 39.017 47.607 1.00 41.16  ? 153 GLN A CG  1 
ATOM   1012 C  CD  . GLN A 1 131 ? 12.151 40.052 48.687 1.00 53.99  ? 153 GLN A CD  1 
ATOM   1013 O  OE1 . GLN A 1 131 ? 12.623 39.729 49.780 1.00 68.25  ? 153 GLN A OE1 1 
ATOM   1014 N  NE2 . GLN A 1 131 ? 11.835 41.306 48.386 1.00 51.08  ? 153 GLN A NE2 1 
ATOM   1015 N  N   . MET A 1 132 ? 14.195 36.664 45.433 1.00 69.81  ? 154 MET A N   1 
ATOM   1016 C  CA  . MET A 1 132 ? 14.853 36.900 44.148 1.00 64.64  ? 154 MET A CA  1 
ATOM   1017 C  C   . MET A 1 132 ? 14.302 35.979 43.064 1.00 57.73  ? 154 MET A C   1 
ATOM   1018 O  O   . MET A 1 132 ? 14.062 36.421 41.934 1.00 57.97  ? 154 MET A O   1 
ATOM   1019 C  CB  . MET A 1 132 ? 16.367 36.716 44.276 1.00 56.81  ? 154 MET A CB  1 
ATOM   1020 C  CG  . MET A 1 132 ? 17.133 36.960 42.971 1.00 58.10  ? 154 MET A CG  1 
ATOM   1021 S  SD  . MET A 1 132 ? 17.167 38.702 42.486 1.00 58.43  ? 154 MET A SD  1 
ATOM   1022 C  CE  . MET A 1 132 ? 18.159 39.381 43.814 1.00 46.63  ? 154 MET A CE  1 
ATOM   1023 N  N   . THR A 1 133 ? 14.107 34.694 43.381 1.00 57.47  ? 155 THR A N   1 
ATOM   1024 C  CA  . THR A 1 133 ? 13.557 33.774 42.390 1.00 62.68  ? 155 THR A CA  1 
ATOM   1025 C  C   . THR A 1 133 ? 12.190 34.241 41.909 1.00 63.07  ? 155 THR A C   1 
ATOM   1026 O  O   . THR A 1 133 ? 11.890 34.179 40.711 1.00 71.26  ? 155 THR A O   1 
ATOM   1027 C  CB  . THR A 1 133 ? 13.462 32.360 42.965 1.00 59.42  ? 155 THR A CB  1 
ATOM   1028 O  OG1 . THR A 1 133 ? 14.764 31.920 43.378 1.00 64.34  ? 155 THR A OG1 1 
ATOM   1029 C  CG2 . THR A 1 133 ? 12.912 31.393 41.920 1.00 56.42  ? 155 THR A CG2 1 
ATOM   1030 N  N   . GLN A 1 134 ? 11.355 34.733 42.826 1.00 59.19  ? 156 GLN A N   1 
ATOM   1031 C  CA  . GLN A 1 134 ? 10.037 35.224 42.438 1.00 70.66  ? 156 GLN A CA  1 
ATOM   1032 C  C   . GLN A 1 134 ? 10.142 36.507 41.623 1.00 71.85  ? 156 GLN A C   1 
ATOM   1033 O  O   . GLN A 1 134 ? 9.375  36.711 40.675 1.00 76.55  ? 156 GLN A O   1 
ATOM   1034 C  CB  . GLN A 1 134 ? 9.173  35.444 43.678 1.00 81.43  ? 156 GLN A CB  1 
ATOM   1035 C  CG  . GLN A 1 134 ? 7.744  35.857 43.370 1.00 88.99  ? 156 GLN A CG  1 
ATOM   1036 C  CD  . GLN A 1 134 ? 6.867  35.874 44.604 1.00 110.86 ? 156 GLN A CD  1 
ATOM   1037 O  OE1 . GLN A 1 134 ? 7.318  35.549 45.704 1.00 121.85 ? 156 GLN A OE1 1 
ATOM   1038 N  NE2 . GLN A 1 134 ? 5.605  36.253 44.430 1.00 119.34 ? 156 GLN A NE2 1 
ATOM   1039 N  N   . ARG A 1 135 ? 11.085 37.384 41.976 1.00 72.18  ? 157 ARG A N   1 
ATOM   1040 C  CA  . ARG A 1 135 ? 11.265 38.621 41.220 1.00 61.21  ? 157 ARG A CA  1 
ATOM   1041 C  C   . ARG A 1 135 ? 11.749 38.337 39.804 1.00 64.28  ? 157 ARG A C   1 
ATOM   1042 O  O   . ARG A 1 135 ? 11.354 39.025 38.855 1.00 73.89  ? 157 ARG A O   1 
ATOM   1043 C  CB  . ARG A 1 135 ? 12.241 39.543 41.949 1.00 58.87  ? 157 ARG A CB  1 
ATOM   1044 C  CG  . ARG A 1 135 ? 12.645 40.772 41.150 1.00 70.74  ? 157 ARG A CG  1 
ATOM   1045 C  CD  . ARG A 1 135 ? 11.475 41.721 40.962 1.00 79.29  ? 157 ARG A CD  1 
ATOM   1046 N  NE  . ARG A 1 135 ? 11.765 42.792 40.015 1.00 53.65  ? 157 ARG A NE  1 
ATOM   1047 C  CZ  . ARG A 1 135 ? 11.446 42.758 38.728 1.00 58.46  ? 157 ARG A CZ  1 
ATOM   1048 N  NH1 . ARG A 1 135 ? 10.853 41.704 38.191 1.00 61.75  ? 157 ARG A NH1 1 
ATOM   1049 N  NH2 . ARG A 1 135 ? 11.724 43.809 37.962 1.00 62.35  ? 157 ARG A NH2 1 
ATOM   1050 N  N   . ILE A 1 136 ? 12.599 37.324 39.640 1.00 58.91  ? 158 ILE A N   1 
ATOM   1051 C  CA  . ILE A 1 136 ? 13.087 36.972 38.311 1.00 56.32  ? 158 ILE A CA  1 
ATOM   1052 C  C   . ILE A 1 136 ? 11.958 36.408 37.455 1.00 66.65  ? 158 ILE A C   1 
ATOM   1053 O  O   . ILE A 1 136 ? 11.857 36.715 36.260 1.00 68.23  ? 158 ILE A O   1 
ATOM   1054 C  CB  . ILE A 1 136 ? 14.274 35.996 38.427 1.00 55.11  ? 158 ILE A CB  1 
ATOM   1055 C  CG1 . ILE A 1 136 ? 15.515 36.745 38.917 1.00 52.71  ? 158 ILE A CG1 1 
ATOM   1056 C  CG2 . ILE A 1 136 ? 14.543 35.295 37.108 1.00 38.35  ? 158 ILE A CG2 1 
ATOM   1057 C  CD1 . ILE A 1 136 ? 16.769 35.898 38.968 1.00 56.72  ? 158 ILE A CD1 1 
ATOM   1058 N  N   . GLU A 1 137 ? 11.077 35.597 38.050 1.00 73.23  ? 159 GLU A N   1 
ATOM   1059 C  CA  . GLU A 1 137 ? 9.957  35.042 37.291 1.00 75.41  ? 159 GLU A CA  1 
ATOM   1060 C  C   . GLU A 1 137 ? 8.977  36.132 36.865 1.00 69.20  ? 159 GLU A C   1 
ATOM   1061 O  O   . GLU A 1 137 ? 8.464  36.104 35.740 1.00 68.83  ? 159 GLU A O   1 
ATOM   1062 C  CB  . GLU A 1 137 ? 9.239  33.965 38.106 1.00 77.42  ? 159 GLU A CB  1 
ATOM   1063 C  CG  . GLU A 1 137 ? 10.138 32.842 38.593 1.00 94.25  ? 159 GLU A CG  1 
ATOM   1064 C  CD  . GLU A 1 137 ? 11.001 32.260 37.489 1.00 117.73 ? 159 GLU A CD  1 
ATOM   1065 O  OE1 . GLU A 1 137 ? 10.491 31.418 36.716 1.00 105.36 ? 159 GLU A OE1 1 
ATOM   1066 O  OE2 . GLU A 1 137 ? 12.188 32.652 37.391 1.00 102.88 ? 159 GLU A OE2 1 
ATOM   1067 N  N   . GLN A 1 138 ? 8.700  37.098 37.748 1.00 63.65  ? 160 GLN A N   1 
ATOM   1068 C  CA  . GLN A 1 138 ? 7.839  38.215 37.367 1.00 64.31  ? 160 GLN A CA  1 
ATOM   1069 C  C   . GLN A 1 138 ? 8.462  39.042 36.252 1.00 80.56  ? 160 GLN A C   1 
ATOM   1070 O  O   . GLN A 1 138 ? 7.742  39.635 35.441 1.00 89.89  ? 160 GLN A O   1 
ATOM   1071 C  CB  . GLN A 1 138 ? 7.547  39.101 38.578 1.00 64.65  ? 160 GLN A CB  1 
ATOM   1072 C  CG  . GLN A 1 138 ? 6.719  38.419 39.650 1.00 105.23 ? 160 GLN A CG  1 
ATOM   1073 C  CD  . GLN A 1 138 ? 6.620  39.230 40.926 1.00 112.37 ? 160 GLN A CD  1 
ATOM   1074 O  OE1 . GLN A 1 138 ? 7.247  40.284 41.062 1.00 104.70 ? 160 GLN A OE1 1 
ATOM   1075 N  NE2 . GLN A 1 138 ? 5.828  38.738 41.875 1.00 85.54  ? 160 GLN A NE2 1 
ATOM   1076 N  N   . HIS A 1 139 ? 9.794  39.095 36.197 1.00 82.93  ? 161 HIS A N   1 
ATOM   1077 C  CA  . HIS A 1 139 ? 10.452 39.786 35.097 1.00 79.27  ? 161 HIS A CA  1 
ATOM   1078 C  C   . HIS A 1 139 ? 10.336 38.995 33.798 1.00 73.25  ? 161 HIS A C   1 
ATOM   1079 O  O   . HIS A 1 139 ? 10.051 39.570 32.742 1.00 65.97  ? 161 HIS A O   1 
ATOM   1080 C  CB  . HIS A 1 139 ? 11.917 40.048 35.437 1.00 71.77  ? 161 HIS A CB  1 
ATOM   1081 C  CG  . HIS A 1 139 ? 12.736 40.451 34.253 1.00 68.01  ? 161 HIS A CG  1 
ATOM   1082 N  ND1 . HIS A 1 139 ? 12.702 41.723 33.723 1.00 53.06  ? 161 HIS A ND1 1 
ATOM   1083 C  CD2 . HIS A 1 139 ? 13.585 39.739 33.473 1.00 56.64  ? 161 HIS A CD2 1 
ATOM   1084 C  CE1 . HIS A 1 139 ? 13.508 41.780 32.677 1.00 59.80  ? 161 HIS A CE1 1 
ATOM   1085 N  NE2 . HIS A 1 139 ? 14.054 40.590 32.503 1.00 63.03  ? 161 HIS A NE2 1 
ATOM   1086 N  N   . LYS A 1 140 ? 10.557 37.676 33.853 1.00 60.80  ? 162 LYS A N   1 
ATOM   1087 C  CA  . LYS A 1 140 ? 10.468 36.860 32.644 1.00 56.27  ? 162 LYS A CA  1 
ATOM   1088 C  C   . LYS A 1 140 ? 9.072  36.914 32.037 1.00 71.57  ? 162 LYS A C   1 
ATOM   1089 O  O   . LYS A 1 140 ? 8.922  36.920 30.808 1.00 74.82  ? 162 LYS A O   1 
ATOM   1090 C  CB  . LYS A 1 140 ? 10.855 35.413 32.949 1.00 62.34  ? 162 LYS A CB  1 
ATOM   1091 C  CG  . LYS A 1 140 ? 12.333 35.194 33.207 1.00 58.39  ? 162 LYS A CG  1 
ATOM   1092 C  CD  . LYS A 1 140 ? 12.647 33.709 33.285 1.00 61.33  ? 162 LYS A CD  1 
ATOM   1093 C  CE  . LYS A 1 140 ? 14.137 33.463 33.367 1.00 59.89  ? 162 LYS A CE  1 
ATOM   1094 N  NZ  . LYS A 1 140 ? 14.449 32.010 33.351 1.00 82.77  ? 162 LYS A NZ  1 
ATOM   1095 N  N   . GLN A 1 141 ? 8.038  36.945 32.882 1.00 85.14  ? 163 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 141 ? 6.671  37.032 32.379 1.00 92.38  ? 163 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 141 ? 6.353  38.427 31.857 1.00 86.06  ? 163 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 141 ? 5.598  38.563 30.887 1.00 87.92  ? 163 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 141 ? 5.678  36.633 33.474 1.00 93.79  ? 163 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 141 ? 5.799  35.182 33.933 1.00 99.99  ? 163 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 141 ? 4.987  34.887 35.188 1.00 111.72 ? 163 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 141 ? 4.390  35.785 35.787 1.00 91.65  ? 163 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 141 ? 4.968  33.621 35.592 1.00 108.20 ? 163 GLN A NE2 1 
ATOM   1104 N  N   . THR A 1 142 ? 6.907  39.470 32.485 1.00 75.83  ? 164 THR A N   1 
ATOM   1105 C  CA  . THR A 1 142 ? 6.728  40.823 31.966 1.00 65.63  ? 164 THR A CA  1 
ATOM   1106 C  C   . THR A 1 142 ? 7.304  40.950 30.561 1.00 82.97  ? 164 THR A C   1 
ATOM   1107 O  O   . THR A 1 142 ? 6.690  41.567 29.683 1.00 86.04  ? 164 THR A O   1 
ATOM   1108 C  CB  . THR A 1 142 ? 7.379  41.848 32.900 1.00 65.54  ? 164 THR A CB  1 
ATOM   1109 O  OG1 . THR A 1 142 ? 6.781  41.776 34.200 1.00 61.77  ? 164 THR A OG1 1 
ATOM   1110 C  CG2 . THR A 1 142 ? 7.198  43.257 32.352 1.00 69.19  ? 164 THR A CG2 1 
ATOM   1111 N  N   . MET A 1 143 ? 8.482  40.366 30.327 1.00 84.78  ? 165 MET A N   1 
ATOM   1112 C  CA  . MET A 1 143 ? 9.079  40.429 28.996 1.00 86.34  ? 165 MET A CA  1 
ATOM   1113 C  C   . MET A 1 143 ? 8.309  39.559 28.008 1.00 85.27  ? 165 MET A C   1 
ATOM   1114 O  O   . MET A 1 143 ? 8.153  39.930 26.838 1.00 88.88  ? 165 MET A O   1 
ATOM   1115 C  CB  . MET A 1 143 ? 10.554 40.023 29.056 1.00 68.87  ? 165 MET A CB  1 
ATOM   1116 C  CG  . MET A 1 143 ? 11.405 40.854 30.024 1.00 66.90  ? 165 MET A CG  1 
ATOM   1117 S  SD  . MET A 1 143 ? 11.623 42.597 29.564 1.00 68.94  ? 165 MET A SD  1 
ATOM   1118 C  CE  . MET A 1 143 ? 12.727 42.427 28.160 1.00 73.07  ? 165 MET A CE  1 
ATOM   1119 N  N   . ALA A 1 144 ? 7.808  38.404 28.459 1.00 84.71  ? 166 ALA A N   1 
ATOM   1120 C  CA  . ALA A 1 144 ? 6.975  37.576 27.591 1.00 86.16  ? 166 ALA A CA  1 
ATOM   1121 C  C   . ALA A 1 144 ? 5.689  38.297 27.198 1.00 80.90  ? 166 ALA A C   1 
ATOM   1122 O  O   . ALA A 1 144 ? 5.167  38.079 26.098 1.00 77.29  ? 166 ALA A O   1 
ATOM   1123 C  CB  . ALA A 1 144 ? 6.659  36.244 28.274 1.00 56.90  ? 166 ALA A CB  1 
ATOM   1124 N  N   . GLU A 1 145 ? 5.170  39.162 28.077 1.00 76.99  ? 167 GLU A N   1 
ATOM   1125 C  CA  . GLU A 1 145 ? 4.026  39.995 27.716 1.00 80.75  ? 167 GLU A CA  1 
ATOM   1126 C  C   . GLU A 1 145 ? 4.414  41.048 26.685 1.00 89.21  ? 167 GLU A C   1 
ATOM   1127 O  O   . GLU A 1 145 ? 3.664  41.300 25.735 1.00 94.92  ? 167 GLU A O   1 
ATOM   1128 C  CB  . GLU A 1 145 ? 3.440  40.663 28.962 1.00 87.78  ? 167 GLU A CB  1 
ATOM   1129 C  CG  . GLU A 1 145 ? 2.782  39.706 29.948 1.00 79.95  ? 167 GLU A CG  1 
ATOM   1130 C  CD  . GLU A 1 145 ? 2.318  40.405 31.217 1.00 92.03  ? 167 GLU A CD  1 
ATOM   1131 O  OE1 . GLU A 1 145 ? 2.449  41.647 31.299 1.00 79.96  ? 167 GLU A OE1 1 
ATOM   1132 O  OE2 . GLU A 1 145 ? 1.823  39.710 32.131 1.00 88.62  ? 167 GLU A OE2 1 
ATOM   1133 N  N   . PHE A 1 146 ? 5.576  41.684 26.863 1.00 90.94  ? 168 PHE A N   1 
ATOM   1134 C  CA  . PHE A 1 146 ? 6.056  42.629 25.862 1.00 81.16  ? 168 PHE A CA  1 
ATOM   1135 C  C   . PHE A 1 146 ? 6.349  41.935 24.539 1.00 78.07  ? 168 PHE A C   1 
ATOM   1136 O  O   . PHE A 1 146 ? 6.232  42.554 23.477 1.00 89.41  ? 168 PHE A O   1 
ATOM   1137 C  CB  . PHE A 1 146 ? 7.306  43.354 26.363 1.00 77.81  ? 168 PHE A CB  1 
ATOM   1138 C  CG  . PHE A 1 146 ? 7.020  44.488 27.309 1.00 79.71  ? 168 PHE A CG  1 
ATOM   1139 C  CD1 . PHE A 1 146 ? 6.350  45.620 26.872 1.00 84.91  ? 168 PHE A CD1 1 
ATOM   1140 C  CD2 . PHE A 1 146 ? 7.444  44.435 28.628 1.00 77.81  ? 168 PHE A CD2 1 
ATOM   1141 C  CE1 . PHE A 1 146 ? 6.094  46.670 27.738 1.00 86.20  ? 168 PHE A CE1 1 
ATOM   1142 C  CE2 . PHE A 1 146 ? 7.194  45.482 29.496 1.00 78.87  ? 168 PHE A CE2 1 
ATOM   1143 C  CZ  . PHE A 1 146 ? 6.517  46.600 29.051 1.00 78.30  ? 168 PHE A CZ  1 
ATOM   1144 N  N   . LYS A 1 147 ? 6.724  40.653 24.577 1.00 64.84  ? 169 LYS A N   1 
ATOM   1145 C  CA  . LYS A 1 147 ? 6.971  39.919 23.340 1.00 72.64  ? 169 LYS A CA  1 
ATOM   1146 C  C   . LYS A 1 147 ? 5.715  39.800 22.488 1.00 86.30  ? 169 LYS A C   1 
ATOM   1147 O  O   . LYS A 1 147 ? 5.815  39.626 21.268 1.00 80.28  ? 169 LYS A O   1 
ATOM   1148 C  CB  . LYS A 1 147 ? 7.523  38.528 23.653 1.00 65.78  ? 169 LYS A CB  1 
ATOM   1149 C  CG  . LYS A 1 147 ? 8.018  37.768 22.435 1.00 59.78  ? 169 LYS A CG  1 
ATOM   1150 C  CD  . LYS A 1 147 ? 8.462  36.366 22.806 1.00 64.98  ? 169 LYS A CD  1 
ATOM   1151 C  CE  . LYS A 1 147 ? 8.883  35.575 21.581 1.00 71.20  ? 169 LYS A CE  1 
ATOM   1152 N  NZ  . LYS A 1 147 ? 9.223  34.158 21.910 1.00 78.74  ? 169 LYS A NZ  1 
ATOM   1153 N  N   . GLN A 1 148 ? 4.535  39.896 23.104 1.00 99.20  ? 170 GLN A N   1 
ATOM   1154 C  CA  . GLN A 1 148 ? 3.287  39.845 22.355 1.00 93.44  ? 170 GLN A CA  1 
ATOM   1155 C  C   . GLN A 1 148 ? 2.926  41.196 21.752 1.00 91.73  ? 170 GLN A C   1 
ATOM   1156 O  O   . GLN A 1 148 ? 2.368  41.245 20.651 1.00 100.23 ? 170 GLN A O   1 
ATOM   1157 C  CB  . GLN A 1 148 ? 2.161  39.346 23.260 1.00 94.15  ? 170 GLN A CB  1 
ATOM   1158 C  CG  . GLN A 1 148 ? 2.441  37.983 23.870 1.00 91.78  ? 170 GLN A CG  1 
ATOM   1159 C  CD  . GLN A 1 148 ? 2.781  36.945 22.819 1.00 112.50 ? 170 GLN A CD  1 
ATOM   1160 O  OE1 . GLN A 1 148 ? 2.085  36.815 21.810 1.00 121.91 ? 170 GLN A OE1 1 
ATOM   1161 N  NE2 . GLN A 1 148 ? 3.864  36.206 23.044 1.00 98.15  ? 170 GLN A NE2 1 
ATOM   1162 N  N   . HIS A 1 149 ? 3.237  42.295 22.448 1.00 89.97  ? 171 HIS A N   1 
ATOM   1163 C  CA  . HIS A 1 149 ? 2.995  43.623 21.892 1.00 96.06  ? 171 HIS A CA  1 
ATOM   1164 C  C   . HIS A 1 149 ? 3.806  43.867 20.623 1.00 98.55  ? 171 HIS A C   1 
ATOM   1165 O  O   . HIS A 1 149 ? 3.409  44.697 19.797 1.00 102.71 ? 171 HIS A O   1 
ATOM   1166 C  CB  . HIS A 1 149 ? 3.317  44.711 22.927 1.00 95.54  ? 171 HIS A CB  1 
ATOM   1167 C  CG  . HIS A 1 149 ? 2.501  44.629 24.185 1.00 123.23 ? 171 HIS A CG  1 
ATOM   1168 N  ND1 . HIS A 1 149 ? 2.705  45.473 25.256 1.00 111.98 ? 171 HIS A ND1 1 
ATOM   1169 C  CD2 . HIS A 1 149 ? 1.484  43.809 24.542 1.00 123.43 ? 171 HIS A CD2 1 
ATOM   1170 C  CE1 . HIS A 1 149 ? 1.852  45.175 26.220 1.00 96.90  ? 171 HIS A CE1 1 
ATOM   1171 N  NE2 . HIS A 1 149 ? 1.099  44.169 25.812 1.00 115.78 ? 171 HIS A NE2 1 
ATOM   1172 N  N   . PHE A 1 150 ? 4.928  43.168 20.450 1.00 97.69  ? 172 PHE A N   1 
ATOM   1173 C  CA  . PHE A 1 150 ? 5.769  43.302 19.267 1.00 91.36  ? 172 PHE A CA  1 
ATOM   1174 C  C   . PHE A 1 150 ? 5.427  42.206 18.269 1.00 97.02  ? 172 PHE A C   1 
ATOM   1175 O  O   . PHE A 1 150 ? 5.363  41.025 18.629 1.00 100.18 ? 172 PHE A O   1 
ATOM   1176 C  CB  . PHE A 1 150 ? 7.254  43.237 19.631 1.00 80.79  ? 172 PHE A CB  1 
ATOM   1177 C  CG  . PHE A 1 150 ? 7.710  44.360 20.517 1.00 78.62  ? 172 PHE A CG  1 
ATOM   1178 C  CD1 . PHE A 1 150 ? 7.647  45.671 20.080 1.00 84.03  ? 172 PHE A CD1 1 
ATOM   1179 C  CD2 . PHE A 1 150 ? 8.208  44.105 21.784 1.00 71.10  ? 172 PHE A CD2 1 
ATOM   1180 C  CE1 . PHE A 1 150 ? 8.064  46.709 20.893 1.00 83.72  ? 172 PHE A CE1 1 
ATOM   1181 C  CE2 . PHE A 1 150 ? 8.625  45.139 22.602 1.00 68.03  ? 172 PHE A CE2 1 
ATOM   1182 C  CZ  . PHE A 1 150 ? 8.554  46.442 22.155 1.00 83.07  ? 172 PHE A CZ  1 
ATOM   1183 N  N   . ALA A 1 151 ? 5.207  42.603 17.013 1.00 95.37  ? 173 ALA A N   1 
ATOM   1184 C  CA  . ALA A 1 151 ? 4.896  41.683 15.930 1.00 101.55 ? 173 ALA A CA  1 
ATOM   1185 C  C   . ALA A 1 151 ? 5.538  42.241 14.657 1.00 98.63  ? 173 ALA A C   1 
ATOM   1186 O  O   . ALA A 1 151 ? 4.870  42.641 13.706 1.00 102.70 ? 173 ALA A O   1 
ATOM   1187 C  CB  . ALA A 1 151 ? 3.387  41.490 15.768 1.00 91.89  ? 173 ALA A CB  1 
ATOM   1188 N  N   . THR A 1 152 ? 6.870  42.274 14.642 1.00 98.64  ? 174 THR A N   1 
ATOM   1189 C  CA  . THR A 1 152 ? 7.615  42.770 13.498 1.00 83.07  ? 174 THR A CA  1 
ATOM   1190 C  C   . THR A 1 152 ? 8.822  41.886 13.247 1.00 79.27  ? 174 THR A C   1 
ATOM   1191 O  O   . THR A 1 152 ? 9.423  41.366 14.189 1.00 87.90  ? 174 THR A O   1 
ATOM   1192 C  CB  . THR A 1 152 ? 8.073  44.214 13.708 1.00 74.43  ? 174 THR A CB  1 
ATOM   1193 O  OG1 . THR A 1 152 ? 9.008  44.570 12.681 1.00 79.52  ? 174 THR A OG1 1 
ATOM   1194 C  CG2 . THR A 1 152 ? 8.728  44.374 15.071 1.00 75.18  ? 174 THR A CG2 1 
ATOM   1195 N  N   . GLN A 1 153 ? 9.171  41.723 11.974 1.00 82.67  ? 175 GLN A N   1 
ATOM   1196 C  CA  . GLN A 1 153 ? 10.360 40.985 11.574 1.00 90.27  ? 175 GLN A CA  1 
ATOM   1197 C  C   . GLN A 1 153 ? 11.499 41.905 11.157 1.00 80.01  ? 175 GLN A C   1 
ATOM   1198 O  O   . GLN A 1 153 ? 12.512 41.425 10.637 1.00 74.37  ? 175 GLN A O   1 
ATOM   1199 C  CB  . GLN A 1 153 ? 10.031 40.015 10.440 1.00 86.55  ? 175 GLN A CB  1 
ATOM   1200 C  CG  . GLN A 1 153 ? 9.137  38.867 10.864 1.00 90.39  ? 175 GLN A CG  1 
ATOM   1201 C  CD  . GLN A 1 153 ? 9.767  38.014 11.945 1.00 108.71 ? 175 GLN A CD  1 
ATOM   1202 O  OE1 . GLN A 1 153 ? 10.731 37.287 11.695 1.00 116.49 ? 175 GLN A OE1 1 
ATOM   1203 N  NE2 . GLN A 1 153 ? 9.230  38.103 13.158 1.00 97.40  ? 175 GLN A NE2 1 
ATOM   1204 N  N   . GLU A 1 154 ? 11.349 43.211 11.362 1.00 66.85  ? 176 GLU A N   1 
ATOM   1205 C  CA  . GLU A 1 154 ? 12.449 44.133 11.126 1.00 72.76  ? 176 GLU A CA  1 
ATOM   1206 C  C   . GLU A 1 154 ? 13.627 43.794 12.032 1.00 86.09  ? 176 GLU A C   1 
ATOM   1207 O  O   . GLU A 1 154 ? 13.459 43.344 13.170 1.00 73.04  ? 176 GLU A O   1 
ATOM   1208 C  CB  . GLU A 1 154 ? 12.003 45.576 11.373 1.00 71.72  ? 176 GLU A CB  1 
ATOM   1209 C  CG  . GLU A 1 154 ? 11.194 46.192 10.245 1.00 69.01  ? 176 GLU A CG  1 
ATOM   1210 C  CD  . GLU A 1 154 ? 10.819 47.635 10.528 1.00 79.51  ? 176 GLU A CD  1 
ATOM   1211 O  OE1 . GLU A 1 154 ? 10.176 47.886 11.569 1.00 86.88  ? 176 GLU A OE1 1 
ATOM   1212 O  OE2 . GLU A 1 154 ? 11.175 48.520 9.719  1.00 87.25  ? 176 GLU A OE2 1 
ATOM   1213 N  N   . THR A 1 155 ? 14.831 43.999 11.508 1.00 76.61  ? 177 THR A N   1 
ATOM   1214 C  CA  . THR A 1 155 ? 16.050 43.817 12.280 1.00 66.60  ? 177 THR A CA  1 
ATOM   1215 C  C   . THR A 1 155 ? 16.361 45.101 13.035 1.00 70.82  ? 177 THR A C   1 
ATOM   1216 O  O   . THR A 1 155 ? 16.355 46.190 12.453 1.00 72.16  ? 177 THR A O   1 
ATOM   1217 C  CB  . THR A 1 155 ? 17.225 43.444 11.376 1.00 63.77  ? 177 THR A CB  1 
ATOM   1218 O  OG1 . THR A 1 155 ? 17.371 44.429 10.342 1.00 69.54  ? 177 THR A OG1 1 
ATOM   1219 C  CG2 . THR A 1 155 ? 17.004 42.075 10.753 1.00 49.42  ? 177 THR A CG2 1 
ATOM   1220 N  N   . ILE A 1 156 ? 16.621 44.967 14.331 1.00 67.92  ? 178 ILE A N   1 
ATOM   1221 C  CA  . ILE A 1 156 ? 17.034 46.078 15.175 1.00 69.10  ? 178 ILE A CA  1 
ATOM   1222 C  C   . ILE A 1 156 ? 18.434 45.782 15.694 1.00 65.84  ? 178 ILE A C   1 
ATOM   1223 O  O   . ILE A 1 156 ? 18.745 44.641 16.055 1.00 61.60  ? 178 ILE A O   1 
ATOM   1224 C  CB  . ILE A 1 156 ? 16.046 46.313 16.335 1.00 57.48  ? 178 ILE A CB  1 
ATOM   1225 C  CG1 . ILE A 1 156 ? 14.650 46.616 15.783 1.00 78.29  ? 178 ILE A CG1 1 
ATOM   1226 C  CG2 . ILE A 1 156 ? 16.525 47.452 17.219 1.00 56.87  ? 178 ILE A CG2 1 
ATOM   1227 C  CD1 . ILE A 1 156 ? 13.624 46.983 16.844 1.00 70.77  ? 178 ILE A CD1 1 
ATOM   1228 N  N   . GLN A 1 157 ? 19.281 46.810 15.710 1.00 65.13  ? 179 GLN A N   1 
ATOM   1229 C  CA  . GLN A 1 157 ? 20.676 46.680 16.108 1.00 57.78  ? 179 GLN A CA  1 
ATOM   1230 C  C   . GLN A 1 157 ? 21.059 47.856 16.990 1.00 68.09  ? 179 GLN A C   1 
ATOM   1231 O  O   . GLN A 1 157 ? 20.879 49.013 16.595 1.00 70.08  ? 179 GLN A O   1 
ATOM   1232 C  CB  . GLN A 1 157 ? 21.596 46.630 14.884 1.00 62.02  ? 179 GLN A CB  1 
ATOM   1233 C  CG  . GLN A 1 157 ? 23.065 46.600 15.227 1.00 52.41  ? 179 GLN A CG  1 
ATOM   1234 C  CD  . GLN A 1 157 ? 23.445 45.332 15.947 1.00 71.00  ? 179 GLN A CD  1 
ATOM   1235 O  OE1 . GLN A 1 157 ? 23.236 44.228 15.436 1.00 74.76  ? 179 GLN A OE1 1 
ATOM   1236 N  NE2 . GLN A 1 157 ? 23.993 45.475 17.150 1.00 56.02  ? 179 GLN A NE2 1 
ATOM   1237 N  N   . PHE A 1 158 ? 21.585 47.561 18.178 1.00 67.79  ? 180 PHE A N   1 
ATOM   1238 C  CA  . PHE A 1 158 ? 22.106 48.582 19.075 1.00 61.28  ? 180 PHE A CA  1 
ATOM   1239 C  C   . PHE A 1 158 ? 23.630 48.622 19.007 1.00 63.52  ? 180 PHE A C   1 
ATOM   1240 O  O   . PHE A 1 158 ? 24.289 47.609 18.754 1.00 55.26  ? 180 PHE A O   1 
ATOM   1241 C  CB  . PHE A 1 158 ? 21.670 48.342 20.525 1.00 53.02  ? 180 PHE A CB  1 
ATOM   1242 C  CG  . PHE A 1 158 ? 22.361 49.242 21.517 1.00 61.02  ? 180 PHE A CG  1 
ATOM   1243 C  CD1 . PHE A 1 158 ? 21.966 50.561 21.670 1.00 49.26  ? 180 PHE A CD1 1 
ATOM   1244 C  CD2 . PHE A 1 158 ? 23.420 48.773 22.282 1.00 59.40  ? 180 PHE A CD2 1 
ATOM   1245 C  CE1 . PHE A 1 158 ? 22.607 51.396 22.570 1.00 57.37  ? 180 PHE A CE1 1 
ATOM   1246 C  CE2 . PHE A 1 158 ? 24.065 49.605 23.186 1.00 53.34  ? 180 PHE A CE2 1 
ATOM   1247 C  CZ  . PHE A 1 158 ? 23.658 50.917 23.328 1.00 60.49  ? 180 PHE A CZ  1 
ATOM   1248 N  N   . GLY A 1 159 ? 24.181 49.811 19.236 1.00 57.83  ? 181 GLY A N   1 
ATOM   1249 C  CA  . GLY A 1 159 ? 25.620 49.982 19.278 1.00 59.51  ? 181 GLY A CA  1 
ATOM   1250 C  C   . GLY A 1 159 ? 25.986 51.258 19.996 1.00 70.34  ? 181 GLY A C   1 
ATOM   1251 O  O   . GLY A 1 159 ? 25.205 52.215 20.032 1.00 58.36  ? 181 GLY A O   1 
ATOM   1252 N  N   . VAL A 1 160 ? 27.175 51.270 20.583 1.00 57.32  ? 182 VAL A N   1 
ATOM   1253 C  CA  . VAL A 1 160 ? 27.720 52.477 21.188 1.00 66.84  ? 182 VAL A CA  1 
ATOM   1254 C  C   . VAL A 1 160 ? 28.665 53.116 20.189 1.00 62.77  ? 182 VAL A C   1 
ATOM   1255 O  O   . VAL A 1 160 ? 29.325 52.434 19.394 1.00 64.73  ? 182 VAL A O   1 
ATOM   1256 C  CB  . VAL A 1 160 ? 28.442 52.193 22.520 1.00 68.22  ? 182 VAL A CB  1 
ATOM   1257 C  CG1 . VAL A 1 160 ? 27.484 51.562 23.509 1.00 62.67  ? 182 VAL A CG1 1 
ATOM   1258 C  CG2 . VAL A 1 160 ? 29.652 51.305 22.286 1.00 50.54  ? 182 VAL A CG2 1 
ATOM   1259 N  N   . VAL A 1 161 ? 28.728 54.442 20.212 1.00 55.02  ? 183 VAL A N   1 
ATOM   1260 C  CA  . VAL A 1 161 ? 29.583 55.169 19.288 1.00 73.20  ? 183 VAL A CA  1 
ATOM   1261 C  C   . VAL A 1 161 ? 30.307 56.280 20.029 1.00 66.12  ? 183 VAL A C   1 
ATOM   1262 O  O   . VAL A 1 161 ? 29.816 56.822 21.025 1.00 60.20  ? 183 VAL A O   1 
ATOM   1263 C  CB  . VAL A 1 161 ? 28.793 55.753 18.102 1.00 69.82  ? 183 VAL A CB  1 
ATOM   1264 C  CG1 . VAL A 1 161 ? 28.033 54.660 17.374 1.00 67.32  ? 183 VAL A CG1 1 
ATOM   1265 C  CG2 . VAL A 1 161 ? 27.852 56.819 18.592 1.00 68.99  ? 183 VAL A CG2 1 
ATOM   1266 N  N   . SER A 1 162 ? 31.488 56.613 19.528 1.00 79.85  ? 184 SER A N   1 
ATOM   1267 C  CA  . SER A 1 162 ? 32.264 57.728 20.037 1.00 80.54  ? 184 SER A CA  1 
ATOM   1268 C  C   . SER A 1 162 ? 33.158 58.223 18.908 1.00 97.87  ? 184 SER A C   1 
ATOM   1269 O  O   . SER A 1 162 ? 33.036 57.789 17.758 1.00 98.32  ? 184 SER A O   1 
ATOM   1270 C  CB  . SER A 1 162 ? 33.060 57.312 21.282 1.00 69.39  ? 184 SER A CB  1 
ATOM   1271 O  OG  . SER A 1 162 ? 34.001 56.297 20.979 1.00 78.35  ? 184 SER A OG  1 
ATOM   1272 N  N   . ASP A 1 163 ? 34.055 59.154 19.237 1.00 106.19 ? 185 ASP A N   1 
ATOM   1273 C  CA  . ASP A 1 163 ? 35.092 59.534 18.288 1.00 101.96 ? 185 ASP A CA  1 
ATOM   1274 C  C   . ASP A 1 163 ? 35.983 58.348 17.948 1.00 103.63 ? 185 ASP A C   1 
ATOM   1275 O  O   . ASP A 1 163 ? 36.498 58.255 16.828 1.00 96.45  ? 185 ASP A O   1 
ATOM   1276 C  CB  . ASP A 1 163 ? 35.922 60.688 18.856 1.00 111.64 ? 185 ASP A CB  1 
ATOM   1277 C  CG  . ASP A 1 163 ? 36.247 60.507 20.334 1.00 108.27 ? 185 ASP A CG  1 
ATOM   1278 O  OD1 . ASP A 1 163 ? 36.858 59.479 20.694 1.00 118.26 ? 185 ASP A OD1 1 
ATOM   1279 O  OD2 . ASP A 1 163 ? 35.898 61.400 21.137 1.00 103.01 ? 185 ASP A OD2 1 
ATOM   1280 N  N   . LYS A 1 164 ? 36.151 57.421 18.896 1.00 83.72  ? 186 LYS A N   1 
ATOM   1281 C  CA  . LYS A 1 164 ? 37.025 56.273 18.684 1.00 86.17  ? 186 LYS A CA  1 
ATOM   1282 C  C   . LYS A 1 164 ? 36.437 55.305 17.663 1.00 91.44  ? 186 LYS A C   1 
ATOM   1283 O  O   . LYS A 1 164 ? 37.176 54.696 16.880 1.00 90.16  ? 186 LYS A O   1 
ATOM   1284 C  CB  . LYS A 1 164 ? 37.279 55.568 20.018 1.00 94.16  ? 186 LYS A CB  1 
ATOM   1285 C  CG  . LYS A 1 164 ? 38.276 54.426 19.946 1.00 107.89 ? 186 LYS A CG  1 
ATOM   1286 C  CD  . LYS A 1 164 ? 38.478 53.784 21.309 1.00 103.40 ? 186 LYS A CD  1 
ATOM   1287 C  CE  . LYS A 1 164 ? 39.438 52.607 21.224 1.00 113.01 ? 186 LYS A CE  1 
ATOM   1288 N  NZ  . LYS A 1 164 ? 39.557 51.902 22.528 1.00 111.84 ? 186 LYS A NZ  1 
ATOM   1289 N  N   . GLY A 1 165 ? 35.120 55.150 17.655 1.00 92.23  ? 187 GLY A N   1 
ATOM   1290 C  CA  . GLY A 1 165 ? 34.487 54.282 16.682 1.00 83.83  ? 187 GLY A CA  1 
ATOM   1291 C  C   . GLY A 1 165 ? 33.113 53.849 17.163 1.00 83.69  ? 187 GLY A C   1 
ATOM   1292 O  O   . GLY A 1 165 ? 32.517 54.478 18.035 1.00 73.76  ? 187 GLY A O   1 
ATOM   1293 N  N   . MET A 1 166 ? 32.638 52.762 16.567 1.00 78.89  ? 188 MET A N   1 
ATOM   1294 C  CA  . MET A 1 166 ? 31.326 52.211 16.862 1.00 74.16  ? 188 MET A CA  1 
ATOM   1295 C  C   . MET A 1 166 ? 31.474 50.742 17.232 1.00 80.03  ? 188 MET A C   1 
ATOM   1296 O  O   . MET A 1 166 ? 32.246 50.011 16.605 1.00 58.03  ? 188 MET A O   1 
ATOM   1297 C  CB  . MET A 1 166 ? 30.382 52.368 15.658 1.00 65.81  ? 188 MET A CB  1 
ATOM   1298 C  CG  . MET A 1 166 ? 29.189 51.430 15.692 1.00 77.99  ? 188 MET A CG  1 
ATOM   1299 S  SD  . MET A 1 166 ? 28.235 51.365 14.167 1.00 74.12  ? 188 MET A SD  1 
ATOM   1300 C  CE  . MET A 1 166 ? 27.224 52.826 14.341 1.00 51.13  ? 188 MET A CE  1 
ATOM   1301 N  N   . TRP A 1 167 ? 30.740 50.313 18.259 1.00 62.67  ? 189 TRP A N   1 
ATOM   1302 C  CA  . TRP A 1 167 ? 30.737 48.919 18.696 1.00 66.56  ? 189 TRP A CA  1 
ATOM   1303 C  C   . TRP A 1 167 ? 29.312 48.390 18.643 1.00 64.82  ? 189 TRP A C   1 
ATOM   1304 O  O   . TRP A 1 167 ? 28.461 48.808 19.435 1.00 63.48  ? 189 TRP A O   1 
ATOM   1305 C  CB  . TRP A 1 167 ? 31.316 48.771 20.100 1.00 61.85  ? 189 TRP A CB  1 
ATOM   1306 C  CG  . TRP A 1 167 ? 32.794 48.923 20.133 1.00 73.42  ? 189 TRP A CG  1 
ATOM   1307 C  CD1 . TRP A 1 167 ? 33.725 47.925 20.100 1.00 71.66  ? 189 TRP A CD1 1 
ATOM   1308 C  CD2 . TRP A 1 167 ? 33.523 50.151 20.191 1.00 70.46  ? 189 TRP A CD2 1 
ATOM   1309 N  NE1 . TRP A 1 167 ? 34.990 48.458 20.143 1.00 71.89  ? 189 TRP A NE1 1 
ATOM   1310 C  CE2 . TRP A 1 167 ? 34.893 49.824 20.197 1.00 78.24  ? 189 TRP A CE2 1 
ATOM   1311 C  CE3 . TRP A 1 167 ? 33.148 51.498 20.237 1.00 76.22  ? 189 TRP A CE3 1 
ATOM   1312 C  CZ2 . TRP A 1 167 ? 35.889 50.794 20.248 1.00 82.84  ? 189 TRP A CZ2 1 
ATOM   1313 C  CZ3 . TRP A 1 167 ? 34.137 52.459 20.288 1.00 80.38  ? 189 TRP A CZ3 1 
ATOM   1314 C  CH2 . TRP A 1 167 ? 35.492 52.103 20.294 1.00 92.77  ? 189 TRP A CH2 1 
ATOM   1315 N  N   . LEU A 1 168 ? 29.055 47.471 17.715 1.00 57.02  ? 190 LEU A N   1 
ATOM   1316 C  CA  . LEU A 1 168 ? 27.744 46.846 17.626 1.00 58.66  ? 190 LEU A CA  1 
ATOM   1317 C  C   . LEU A 1 168 ? 27.599 45.798 18.722 1.00 65.68  ? 190 LEU A C   1 
ATOM   1318 O  O   . LEU A 1 168 ? 28.471 44.937 18.894 1.00 60.34  ? 190 LEU A O   1 
ATOM   1319 C  CB  . LEU A 1 168 ? 27.533 46.204 16.253 1.00 60.17  ? 190 LEU A CB  1 
ATOM   1320 C  CG  . LEU A 1 168 ? 27.312 47.129 15.053 1.00 56.43  ? 190 LEU A CG  1 
ATOM   1321 C  CD1 . LEU A 1 168 ? 26.808 46.336 13.863 1.00 48.79  ? 190 LEU A CD1 1 
ATOM   1322 C  CD2 . LEU A 1 168 ? 26.357 48.265 15.390 1.00 44.57  ? 190 LEU A CD2 1 
ATOM   1323 N  N   . HIS A 1 169 ? 26.500 45.876 19.466 1.00 51.38  ? 191 HIS A N   1 
ATOM   1324 C  CA  . HIS A 1 169 ? 26.187 44.891 20.494 1.00 50.34  ? 191 HIS A CA  1 
ATOM   1325 C  C   . HIS A 1 169 ? 25.463 43.720 19.838 1.00 48.63  ? 191 HIS A C   1 
ATOM   1326 O  O   . HIS A 1 169 ? 24.300 43.842 19.436 1.00 60.58  ? 191 HIS A O   1 
ATOM   1327 C  CB  . HIS A 1 169 ? 25.359 45.526 21.603 1.00 46.35  ? 191 HIS A CB  1 
ATOM   1328 C  CG  . HIS A 1 169 ? 26.136 46.485 22.448 1.00 43.48  ? 191 HIS A CG  1 
ATOM   1329 N  ND1 . HIS A 1 169 ? 25.800 46.772 23.753 1.00 64.11  ? 191 HIS A ND1 1 
ATOM   1330 C  CD2 . HIS A 1 169 ? 27.242 47.217 22.174 1.00 63.44  ? 191 HIS A CD2 1 
ATOM   1331 C  CE1 . HIS A 1 169 ? 26.663 47.642 24.246 1.00 56.55  ? 191 HIS A CE1 1 
ATOM   1332 N  NE2 . HIS A 1 169 ? 27.550 47.925 23.309 1.00 64.21  ? 191 HIS A NE2 1 
ATOM   1333 N  N   . SER A 1 170 ? 26.156 42.586 19.725 1.00 39.49  ? 192 SER A N   1 
ATOM   1334 C  CA  . SER A 1 170 ? 25.697 41.404 19.000 1.00 59.89  ? 192 SER A CA  1 
ATOM   1335 C  C   . SER A 1 170 ? 24.559 40.694 19.733 1.00 52.49  ? 192 SER A C   1 
ATOM   1336 O  O   . SER A 1 170 ? 24.168 41.121 20.830 1.00 46.51  ? 192 SER A O   1 
ATOM   1337 C  CB  . SER A 1 170 ? 26.873 40.450 18.791 1.00 51.98  ? 192 SER A CB  1 
ATOM   1338 O  OG  . SER A 1 170 ? 27.260 39.866 20.018 1.00 51.35  ? 192 SER A OG  1 
ATOM   1339 N  N   . PRO A 1 171 ? 23.986 39.625 19.160 1.00 61.32  ? 193 PRO A N   1 
ATOM   1340 C  CA  . PRO A 1 171 ? 22.936 38.892 19.888 1.00 56.56  ? 193 PRO A CA  1 
ATOM   1341 C  C   . PRO A 1 171 ? 23.367 38.371 21.250 1.00 59.02  ? 193 PRO A C   1 
ATOM   1342 O  O   . PRO A 1 171 ? 22.514 38.223 22.134 1.00 64.95  ? 193 PRO A O   1 
ATOM   1343 C  CB  . PRO A 1 171 ? 22.593 37.745 18.930 1.00 64.96  ? 193 PRO A CB  1 
ATOM   1344 C  CG  . PRO A 1 171 ? 22.854 38.310 17.589 1.00 58.69  ? 193 PRO A CG  1 
ATOM   1345 C  CD  . PRO A 1 171 ? 24.055 39.201 17.747 1.00 58.55  ? 193 PRO A CD  1 
ATOM   1346 N  N   . VAL A 1 172 ? 24.662 38.099 21.459 1.00 51.42  ? 194 VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 172 ? 25.122 37.584 22.745 1.00 40.34  ? 194 VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 172 ? 25.495 38.688 23.726 1.00 55.03  ? 194 VAL A C   1 
ATOM   1349 O  O   . VAL A 1 172 ? 25.960 38.387 24.834 1.00 58.90  ? 194 VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 172 ? 26.309 36.616 22.565 1.00 56.28  ? 194 VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 172 ? 25.879 35.412 21.755 1.00 36.98  ? 194 VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 172 ? 27.484 37.318 21.907 1.00 41.48  ? 194 VAL A CG2 1 
ATOM   1353 N  N   . SER A 1 173 ? 25.306 39.952 23.363 1.00 48.55  ? 195 SER A N   1 
ATOM   1354 C  CA  . SER A 1 173 ? 25.420 41.009 24.352 1.00 60.16  ? 195 SER A CA  1 
ATOM   1355 C  C   . SER A 1 173 ? 24.141 41.080 25.182 1.00 60.67  ? 195 SER A C   1 
ATOM   1356 O  O   . SER A 1 173 ? 23.129 40.444 24.870 1.00 56.50  ? 195 SER A O   1 
ATOM   1357 C  CB  . SER A 1 173 ? 25.699 42.354 23.682 1.00 58.26  ? 195 SER A CB  1 
ATOM   1358 O  OG  . SER A 1 173 ? 24.595 42.781 22.905 1.00 55.19  ? 195 SER A OG  1 
ATOM   1359 N  N   . TYR A 1 174 ? 24.193 41.862 26.263 1.00 49.67  ? 196 TYR A N   1 
ATOM   1360 C  CA  . TYR A 1 174 ? 23.002 42.042 27.088 1.00 61.03  ? 196 TYR A CA  1 
ATOM   1361 C  C   . TYR A 1 174 ? 21.863 42.638 26.268 1.00 67.97  ? 196 TYR A C   1 
ATOM   1362 O  O   . TYR A 1 174 ? 20.742 42.117 26.274 1.00 59.97  ? 196 TYR A O   1 
ATOM   1363 C  CB  . TYR A 1 174 ? 23.318 42.915 28.308 1.00 49.22  ? 196 TYR A CB  1 
ATOM   1364 C  CG  . TYR A 1 174 ? 22.081 43.449 29.006 1.00 52.38  ? 196 TYR A CG  1 
ATOM   1365 C  CD1 . TYR A 1 174 ? 21.399 42.689 29.955 1.00 56.68  ? 196 TYR A CD1 1 
ATOM   1366 C  CD2 . TYR A 1 174 ? 21.584 44.710 28.700 1.00 52.07  ? 196 TYR A CD2 1 
ATOM   1367 C  CE1 . TYR A 1 174 ? 20.255 43.185 30.583 1.00 48.96  ? 196 TYR A CE1 1 
ATOM   1368 C  CE2 . TYR A 1 174 ? 20.450 45.208 29.313 1.00 62.58  ? 196 TYR A CE2 1 
ATOM   1369 C  CZ  . TYR A 1 174 ? 19.788 44.447 30.251 1.00 68.68  ? 196 TYR A CZ  1 
ATOM   1370 O  OH  . TYR A 1 174 ? 18.662 44.976 30.848 1.00 65.63  ? 196 TYR A OH  1 
ATOM   1371 N  N   . ALA A 1 175 ? 22.142 43.722 25.534 1.00 61.77  ? 197 ALA A N   1 
ATOM   1372 C  CA  . ALA A 1 175 ? 21.114 44.348 24.705 1.00 61.94  ? 197 ALA A CA  1 
ATOM   1373 C  C   . ALA A 1 175 ? 20.635 43.416 23.601 1.00 69.48  ? 197 ALA A C   1 
ATOM   1374 O  O   . ALA A 1 175 ? 19.450 43.431 23.247 1.00 59.65  ? 197 ALA A O   1 
ATOM   1375 C  CB  . ALA A 1 175 ? 21.641 45.653 24.102 1.00 58.52  ? 197 ALA A CB  1 
ATOM   1376 N  N   . GLY A 1 176 ? 21.538 42.615 23.032 1.00 61.36  ? 198 GLY A N   1 
ATOM   1377 C  CA  . GLY A 1 176 ? 21.120 41.639 22.040 1.00 57.40  ? 198 GLY A CA  1 
ATOM   1378 C  C   . GLY A 1 176 ? 20.200 40.582 22.622 1.00 59.32  ? 198 GLY A C   1 
ATOM   1379 O  O   . GLY A 1 176 ? 19.215 40.190 21.991 1.00 62.17  ? 198 GLY A O   1 
ATOM   1380 N  N   . GLY A 1 177 ? 20.504 40.113 23.833 1.00 56.69  ? 199 GLY A N   1 
ATOM   1381 C  CA  . GLY A 1 177 ? 19.644 39.131 24.471 1.00 49.77  ? 199 GLY A CA  1 
ATOM   1382 C  C   . GLY A 1 177 ? 18.284 39.695 24.834 1.00 52.24  ? 199 GLY A C   1 
ATOM   1383 O  O   . GLY A 1 177 ? 17.268 39.001 24.734 1.00 59.04  ? 199 GLY A O   1 
ATOM   1384 N  N   . VAL A 1 178 ? 18.245 40.958 25.268 1.00 56.83  ? 200 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 178 ? 16.970 41.608 25.555 1.00 52.85  ? 200 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 178 ? 16.103 41.646 24.305 1.00 64.76  ? 200 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 178 ? 14.894 41.384 24.357 1.00 73.93  ? 200 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 178 ? 17.203 43.020 26.123 1.00 58.65  ? 200 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 178 ? 15.883 43.781 26.221 1.00 46.78  ? 200 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 178 ? 17.882 42.942 27.478 1.00 67.04  ? 200 VAL A CG2 1 
ATOM   1391 N  N   . LEU A 1 179 ? 16.705 41.972 23.159 1.00 70.01  ? 201 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 179 ? 15.945 42.013 21.916 1.00 59.24  ? 201 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 179 ? 15.466 40.621 21.515 1.00 67.68  ? 201 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 179 ? 14.321 40.459 21.076 1.00 68.87  ? 201 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 179 ? 16.791 42.648 20.811 1.00 53.53  ? 201 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 179 ? 17.199 44.113 21.027 1.00 72.07  ? 201 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 179 ? 18.303 44.518 20.058 1.00 63.20  ? 201 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 179 ? 16.010 45.065 20.911 1.00 53.71  ? 201 LEU A CD2 1 
ATOM   1399 N  N   . SER A 1 180 ? 16.312 39.599 21.681 1.00 58.00  ? 202 SER A N   1 
ATOM   1400 C  CA  . SER A 1 180 ? 15.891 38.239 21.352 1.00 65.21  ? 202 SER A CA  1 
ATOM   1401 C  C   . SER A 1 180 ? 14.730 37.790 22.230 1.00 76.59  ? 202 SER A C   1 
ATOM   1402 O  O   . SER A 1 180 ? 13.825 37.086 21.766 1.00 69.67  ? 202 SER A O   1 
ATOM   1403 C  CB  . SER A 1 180 ? 17.069 37.279 21.494 1.00 43.66  ? 202 SER A CB  1 
ATOM   1404 O  OG  . SER A 1 180 ? 18.209 37.781 20.823 1.00 75.21  ? 202 SER A OG  1 
ATOM   1405 N  N   . THR A 1 181 ? 14.736 38.193 23.501 1.00 72.34  ? 203 THR A N   1 
ATOM   1406 C  CA  . THR A 1 181 ? 13.653 37.815 24.401 1.00 68.21  ? 203 THR A CA  1 
ATOM   1407 C  C   . THR A 1 181 ? 12.340 38.462 23.977 1.00 75.88  ? 203 THR A C   1 
ATOM   1408 O  O   . THR A 1 181 ? 11.275 37.841 24.063 1.00 82.07  ? 203 THR A O   1 
ATOM   1409 C  CB  . THR A 1 181 ? 14.023 38.192 25.837 1.00 60.30  ? 203 THR A CB  1 
ATOM   1410 O  OG1 . THR A 1 181 ? 15.154 37.412 26.249 1.00 77.01  ? 203 THR A OG1 1 
ATOM   1411 C  CG2 . THR A 1 181 ? 12.861 37.937 26.794 1.00 59.77  ? 203 THR A CG2 1 
ATOM   1412 N  N   . LEU A 1 182 ? 12.400 39.697 23.490 1.00 65.95  ? 204 LEU A N   1 
ATOM   1413 C  CA  . LEU A 1 182 ? 11.221 40.370 22.964 1.00 70.53  ? 204 LEU A CA  1 
ATOM   1414 C  C   . LEU A 1 182 ? 10.798 39.853 21.593 1.00 76.72  ? 204 LEU A C   1 
ATOM   1415 O  O   . LEU A 1 182 ? 9.836  40.381 21.025 1.00 82.06  ? 204 LEU A O   1 
ATOM   1416 C  CB  . LEU A 1 182 ? 11.475 41.875 22.888 1.00 72.30  ? 204 LEU A CB  1 
ATOM   1417 C  CG  . LEU A 1 182 ? 11.715 42.564 24.227 1.00 73.80  ? 204 LEU A CG  1 
ATOM   1418 C  CD1 . LEU A 1 182 ? 11.954 44.047 24.019 1.00 62.35  ? 204 LEU A CD1 1 
ATOM   1419 C  CD2 . LEU A 1 182 ? 10.527 42.329 25.138 1.00 66.09  ? 204 LEU A CD2 1 
ATOM   1420 N  N   . GLY A 1 183 ? 11.482 38.845 21.052 1.00 72.28  ? 205 GLY A N   1 
ATOM   1421 C  CA  . GLY A 1 183 ? 11.164 38.332 19.735 1.00 72.84  ? 205 GLY A CA  1 
ATOM   1422 C  C   . GLY A 1 183 ? 11.596 39.205 18.578 1.00 86.69  ? 205 GLY A C   1 
ATOM   1423 O  O   . GLY A 1 183 ? 11.067 39.053 17.473 1.00 74.07  ? 205 GLY A O   1 
ATOM   1424 N  N   . ILE A 1 184 ? 12.548 40.123 18.795 1.00 81.84  ? 206 ILE A N   1 
ATOM   1425 C  CA  . ILE A 1 184 ? 13.033 41.023 17.753 1.00 73.71  ? 206 ILE A CA  1 
ATOM   1426 C  C   . ILE A 1 184 ? 14.178 40.349 17.011 1.00 79.75  ? 206 ILE A C   1 
ATOM   1427 O  O   . ILE A 1 184 ? 15.051 39.717 17.618 1.00 70.98  ? 206 ILE A O   1 
ATOM   1428 C  CB  . ILE A 1 184 ? 13.474 42.376 18.347 1.00 70.77  ? 206 ILE A CB  1 
ATOM   1429 C  CG1 . ILE A 1 184 ? 12.351 42.996 19.180 1.00 59.89  ? 206 ILE A CG1 1 
ATOM   1430 C  CG2 . ILE A 1 184 ? 13.900 43.339 17.244 1.00 65.59  ? 206 ILE A CG2 1 
ATOM   1431 C  CD1 . ILE A 1 184 ? 11.151 43.428 18.373 1.00 73.92  ? 206 ILE A CD1 1 
ATOM   1432 N  N   . GLN A 1 185 ? 14.174 40.482 15.689 1.00 78.87  ? 207 GLN A N   1 
ATOM   1433 C  CA  . GLN A 1 185 ? 15.188 39.852 14.861 1.00 68.14  ? 207 GLN A CA  1 
ATOM   1434 C  C   . GLN A 1 185 ? 16.474 40.673 14.876 1.00 74.80  ? 207 GLN A C   1 
ATOM   1435 O  O   . GLN A 1 185 ? 16.452 41.900 15.008 1.00 66.89  ? 207 GLN A O   1 
ATOM   1436 C  CB  . GLN A 1 185 ? 14.673 39.691 13.430 1.00 68.56  ? 207 GLN A CB  1 
ATOM   1437 C  CG  . GLN A 1 185 ? 15.501 38.743 12.590 1.00 103.28 ? 207 GLN A CG  1 
ATOM   1438 C  CD  . GLN A 1 185 ? 15.520 37.343 13.160 1.00 106.43 ? 207 GLN A CD  1 
ATOM   1439 O  OE1 . GLN A 1 185 ? 14.480 36.803 13.543 1.00 88.33  ? 207 GLN A OE1 1 
ATOM   1440 N  NE2 . GLN A 1 185 ? 16.707 36.748 13.232 1.00 98.23  ? 207 GLN A NE2 1 
ATOM   1441 N  N   . SER A 1 186 ? 17.613 39.972 14.752 1.00 60.74  ? 208 SER A N   1 
ATOM   1442 C  CA  . SER A 1 186 ? 18.916 40.612 14.725 1.00 58.96  ? 208 SER A CA  1 
ATOM   1443 C  C   . SER A 1 186 ? 19.494 40.585 13.318 1.00 68.48  ? 208 SER A C   1 
ATOM   1444 O  O   . SER A 1 186 ? 19.380 39.572 12.619 1.00 71.68  ? 208 SER A O   1 
ATOM   1445 C  CB  . SER A 1 186 ? 19.906 39.932 15.677 1.00 70.13  ? 208 SER A CB  1 
ATOM   1446 O  OG  . SER A 1 186 ? 21.216 40.441 15.490 1.00 59.78  ? 208 SER A OG  1 
ATOM   1447 N  N   . PRO A 1 187 ? 20.120 41.680 12.877 1.00 72.38  ? 209 PRO A N   1 
ATOM   1448 C  CA  . PRO A 1 187 ? 20.760 41.674 11.555 1.00 58.60  ? 209 PRO A CA  1 
ATOM   1449 C  C   . PRO A 1 187 ? 22.086 40.943 11.527 1.00 53.17  ? 209 PRO A C   1 
ATOM   1450 O  O   . PRO A 1 187 ? 22.551 40.585 10.437 1.00 67.67  ? 209 PRO A O   1 
ATOM   1451 C  CB  . PRO A 1 187 ? 20.948 43.164 11.257 1.00 57.50  ? 209 PRO A CB  1 
ATOM   1452 C  CG  . PRO A 1 187 ? 21.114 43.779 12.608 1.00 58.27  ? 209 PRO A CG  1 
ATOM   1453 C  CD  . PRO A 1 187 ? 20.237 42.987 13.549 1.00 57.84  ? 209 PRO A CD  1 
ATOM   1454 N  N   . LEU A 1 188 ? 22.704 40.710 12.681 1.00 72.94  ? 210 LEU A N   1 
ATOM   1455 C  CA  . LEU A 1 188 ? 23.986 40.032 12.730 1.00 63.43  ? 210 LEU A CA  1 
ATOM   1456 C  C   . LEU A 1 188 ? 23.804 38.523 12.649 1.00 76.37  ? 210 LEU A C   1 
ATOM   1457 O  O   . LEU A 1 188 ? 22.737 37.979 12.947 1.00 64.39  ? 210 LEU A O   1 
ATOM   1458 C  CB  . LEU A 1 188 ? 24.736 40.391 14.007 1.00 67.43  ? 210 LEU A CB  1 
ATOM   1459 C  CG  . LEU A 1 188 ? 25.286 41.811 14.031 1.00 69.06  ? 210 LEU A CG  1 
ATOM   1460 C  CD1 . LEU A 1 188 ? 26.029 42.051 15.324 1.00 67.02  ? 210 LEU A CD1 1 
ATOM   1461 C  CD2 . LEU A 1 188 ? 26.195 42.019 12.828 1.00 53.32  ? 210 LEU A CD2 1 
ATOM   1462 N  N   . ALA A 1 189 ? 24.880 37.851 12.246 1.00 86.52  ? 211 ALA A N   1 
ATOM   1463 C  CA  . ALA A 1 189 ? 24.864 36.407 12.098 1.00 95.92  ? 211 ALA A CA  1 
ATOM   1464 C  C   . ALA A 1 189 ? 24.474 35.740 13.417 1.00 93.78  ? 211 ALA A C   1 
ATOM   1465 O  O   . ALA A 1 189 ? 24.807 36.237 14.498 1.00 89.13  ? 211 ALA A O   1 
ATOM   1466 C  CB  . ALA A 1 189 ? 26.233 35.905 11.641 1.00 91.94  ? 211 ALA A CB  1 
ATOM   1467 N  N   . PRO A 1 190 ? 23.761 34.611 13.357 1.00 110.45 ? 212 PRO A N   1 
ATOM   1468 C  CA  . PRO A 1 190 ? 23.320 33.960 14.601 1.00 106.83 ? 212 PRO A CA  1 
ATOM   1469 C  C   . PRO A 1 190 ? 24.462 33.430 15.448 1.00 105.34 ? 212 PRO A C   1 
ATOM   1470 O  O   . PRO A 1 190 ? 24.266 33.215 16.650 1.00 100.37 ? 212 PRO A O   1 
ATOM   1471 C  CB  . PRO A 1 190 ? 22.419 32.822 14.101 1.00 116.26 ? 212 PRO A CB  1 
ATOM   1472 C  CG  . PRO A 1 190 ? 22.911 32.537 12.718 1.00 109.43 ? 212 PRO A CG  1 
ATOM   1473 C  CD  . PRO A 1 190 ? 23.341 33.863 12.158 1.00 102.71 ? 212 PRO A CD  1 
ATOM   1474 N  N   . SER A 1 191 ? 25.647 33.226 14.868 1.00 110.33 ? 213 SER A N   1 
ATOM   1475 C  CA  . SER A 1 191 ? 26.787 32.656 15.574 1.00 104.00 ? 213 SER A CA  1 
ATOM   1476 C  C   . SER A 1 191 ? 27.872 33.692 15.854 1.00 106.85 ? 213 SER A C   1 
ATOM   1477 O  O   . SER A 1 191 ? 29.052 33.347 15.964 1.00 106.67 ? 213 SER A O   1 
ATOM   1478 C  CB  . SER A 1 191 ? 27.371 31.485 14.787 1.00 96.20  ? 213 SER A CB  1 
ATOM   1479 O  OG  . SER A 1 191 ? 27.903 31.926 13.550 1.00 91.21  ? 213 SER A OG  1 
ATOM   1480 N  N   . GLU A 1 192 ? 27.496 34.965 15.957 1.00 93.11  ? 214 GLU A N   1 
ATOM   1481 C  CA  . GLU A 1 192 ? 28.439 35.975 16.417 1.00 95.59  ? 214 GLU A CA  1 
ATOM   1482 C  C   . GLU A 1 192 ? 28.800 35.704 17.870 1.00 98.62  ? 214 GLU A C   1 
ATOM   1483 O  O   . GLU A 1 192 ? 27.922 35.470 18.706 1.00 104.11 ? 214 GLU A O   1 
ATOM   1484 C  CB  . GLU A 1 192 ? 27.853 37.376 16.264 1.00 87.08  ? 214 GLU A CB  1 
ATOM   1485 C  CG  . GLU A 1 192 ? 28.215 38.045 14.953 1.00 94.52  ? 214 GLU A CG  1 
ATOM   1486 C  CD  . GLU A 1 192 ? 29.713 38.247 14.793 1.00 98.57  ? 214 GLU A CD  1 
ATOM   1487 O  OE1 . GLU A 1 192 ? 30.419 38.380 15.818 1.00 93.11  ? 214 GLU A OE1 1 
ATOM   1488 O  OE2 . GLU A 1 192 ? 30.184 38.271 13.637 1.00 108.90 ? 214 GLU A OE2 1 
ATOM   1489 N  N   . GLN A 1 193 ? 30.097 35.736 18.175 1.00 84.11  ? 215 GLN A N   1 
ATOM   1490 C  CA  . GLN A 1 193 ? 30.590 35.225 19.445 1.00 81.26  ? 215 GLN A CA  1 
ATOM   1491 C  C   . GLN A 1 193 ? 31.125 36.294 20.389 1.00 74.61  ? 215 GLN A C   1 
ATOM   1492 O  O   . GLN A 1 193 ? 31.362 35.988 21.561 1.00 79.03  ? 215 GLN A O   1 
ATOM   1493 C  CB  . GLN A 1 193 ? 31.676 34.169 19.191 1.00 92.43  ? 215 GLN A CB  1 
ATOM   1494 C  CG  . GLN A 1 193 ? 31.179 32.981 18.375 1.00 106.20 ? 215 GLN A CG  1 
ATOM   1495 C  CD  . GLN A 1 193 ? 30.356 32.000 19.192 1.00 106.98 ? 215 GLN A CD  1 
ATOM   1496 O  OE1 . GLN A 1 193 ? 30.549 31.864 20.401 1.00 99.83  ? 215 GLN A OE1 1 
ATOM   1497 N  NE2 . GLN A 1 193 ? 29.431 31.309 18.531 1.00 102.70 ? 215 GLN A NE2 1 
ATOM   1498 N  N   . LYS A 1 194 ? 31.316 37.526 19.932 1.00 73.25  ? 216 LYS A N   1 
ATOM   1499 C  CA  . LYS A 1 194 ? 31.726 38.613 20.811 1.00 73.01  ? 216 LYS A CA  1 
ATOM   1500 C  C   . LYS A 1 194 ? 30.562 39.574 21.007 1.00 54.82  ? 216 LYS A C   1 
ATOM   1501 O  O   . LYS A 1 194 ? 29.791 39.826 20.077 1.00 60.38  ? 216 LYS A O   1 
ATOM   1502 C  CB  . LYS A 1 194 ? 32.954 39.345 20.260 1.00 58.60  ? 216 LYS A CB  1 
ATOM   1503 C  CG  . LYS A 1 194 ? 32.837 39.810 18.825 1.00 83.54  ? 216 LYS A CG  1 
ATOM   1504 C  CD  . LYS A 1 194 ? 34.212 39.916 18.172 1.00 95.84  ? 216 LYS A CD  1 
ATOM   1505 C  CE  . LYS A 1 194 ? 35.245 40.527 19.118 1.00 76.68  ? 216 LYS A CE  1 
ATOM   1506 N  NZ  . LYS A 1 194 ? 34.896 41.912 19.536 1.00 89.14  ? 216 LYS A NZ  1 
ATOM   1507 N  N   . ALA A 1 195 ? 30.425 40.091 22.229 1.00 66.13  ? 217 ALA A N   1 
ATOM   1508 C  CA  . ALA A 1 195 ? 29.263 40.915 22.550 1.00 61.40  ? 217 ALA A CA  1 
ATOM   1509 C  C   . ALA A 1 195 ? 29.394 42.315 21.961 1.00 62.46  ? 217 ALA A C   1 
ATOM   1510 O  O   . ALA A 1 195 ? 28.461 42.820 21.328 1.00 56.05  ? 217 ALA A O   1 
ATOM   1511 C  CB  . ALA A 1 195 ? 29.070 40.980 24.067 1.00 54.50  ? 217 ALA A CB  1 
ATOM   1512 N  N   . TYR A 1 196 ? 30.547 42.956 22.151 1.00 61.04  ? 218 TYR A N   1 
ATOM   1513 C  CA  . TYR A 1 196 ? 30.795 44.306 21.651 1.00 65.15  ? 218 TYR A CA  1 
ATOM   1514 C  C   . TYR A 1 196 ? 31.758 44.209 20.472 1.00 60.32  ? 218 TYR A C   1 
ATOM   1515 O  O   . TYR A 1 196 ? 32.952 43.943 20.654 1.00 74.09  ? 218 TYR A O   1 
ATOM   1516 C  CB  . TYR A 1 196 ? 31.345 45.198 22.761 1.00 65.59  ? 218 TYR A CB  1 
ATOM   1517 C  CG  . TYR A 1 196 ? 30.651 44.983 24.090 1.00 72.56  ? 218 TYR A CG  1 
ATOM   1518 C  CD1 . TYR A 1 196 ? 29.295 45.244 24.235 1.00 64.68  ? 218 TYR A CD1 1 
ATOM   1519 C  CD2 . TYR A 1 196 ? 31.350 44.513 25.198 1.00 75.15  ? 218 TYR A CD2 1 
ATOM   1520 C  CE1 . TYR A 1 196 ? 28.651 45.039 25.444 1.00 64.06  ? 218 TYR A CE1 1 
ATOM   1521 C  CE2 . TYR A 1 196 ? 30.712 44.311 26.417 1.00 68.56  ? 218 TYR A CE2 1 
ATOM   1522 C  CZ  . TYR A 1 196 ? 29.361 44.575 26.530 1.00 64.24  ? 218 TYR A CZ  1 
ATOM   1523 O  OH  . TYR A 1 196 ? 28.706 44.382 27.726 1.00 59.92  ? 218 TYR A OH  1 
ATOM   1524 N  N   . ILE A 1 197 ? 31.236 44.427 19.271 1.00 65.07  ? 219 ILE A N   1 
ATOM   1525 C  CA  . ILE A 1 197 ? 31.957 44.181 18.025 1.00 70.74  ? 219 ILE A CA  1 
ATOM   1526 C  C   . ILE A 1 197 ? 32.494 45.511 17.504 1.00 66.46  ? 219 ILE A C   1 
ATOM   1527 O  O   . ILE A 1 197 ? 31.692 46.400 17.183 1.00 64.25  ? 219 ILE A O   1 
ATOM   1528 C  CB  . ILE A 1 197 ? 31.053 43.520 16.976 1.00 62.23  ? 219 ILE A CB  1 
ATOM   1529 C  CG1 . ILE A 1 197 ? 30.519 42.183 17.492 1.00 59.78  ? 219 ILE A CG1 1 
ATOM   1530 C  CG2 . ILE A 1 197 ? 31.797 43.366 15.653 1.00 49.60  ? 219 ILE A CG2 1 
ATOM   1531 C  CD1 . ILE A 1 197 ? 29.558 41.505 16.539 1.00 50.08  ? 219 ILE A CD1 1 
ATOM   1532 N  N   . PRO A 1 198 ? 33.811 45.688 17.399 1.00 65.67  ? 220 PRO A N   1 
ATOM   1533 C  CA  . PRO A 1 198 ? 34.343 46.868 16.699 1.00 64.49  ? 220 PRO A CA  1 
ATOM   1534 C  C   . PRO A 1 198 ? 33.857 46.876 15.259 1.00 72.14  ? 220 PRO A C   1 
ATOM   1535 O  O   . PRO A 1 198 ? 34.065 45.919 14.507 1.00 64.43  ? 220 PRO A O   1 
ATOM   1536 C  CB  . PRO A 1 198 ? 35.862 46.681 16.789 1.00 51.99  ? 220 PRO A CB  1 
ATOM   1537 C  CG  . PRO A 1 198 ? 36.062 45.772 17.954 1.00 64.99  ? 220 PRO A CG  1 
ATOM   1538 C  CD  . PRO A 1 198 ? 34.884 44.847 17.952 1.00 59.90  ? 220 PRO A CD  1 
ATOM   1539 N  N   . THR A 1 199 ? 33.193 47.962 14.879 1.00 59.99  ? 221 THR A N   1 
ATOM   1540 C  CA  . THR A 1 199 ? 32.436 48.017 13.636 1.00 74.12  ? 221 THR A CA  1 
ATOM   1541 C  C   . THR A 1 199 ? 33.035 49.064 12.711 1.00 61.74  ? 221 THR A C   1 
ATOM   1542 O  O   . THR A 1 199 ? 33.055 50.254 13.046 1.00 70.97  ? 221 THR A O   1 
ATOM   1543 C  CB  . THR A 1 199 ? 30.966 48.331 13.915 1.00 78.90  ? 221 THR A CB  1 
ATOM   1544 O  OG1 . THR A 1 199 ? 30.432 47.341 14.802 1.00 73.13  ? 221 THR A OG1 1 
ATOM   1545 C  CG2 . THR A 1 199 ? 30.172 48.328 12.619 1.00 83.98  ? 221 THR A CG2 1 
ATOM   1546 N  N   . SER A 1 200 ? 33.516 48.621 11.552 1.00 67.20  ? 222 SER A N   1 
ATOM   1547 C  CA  . SER A 1 200 ? 33.935 49.539 10.508 1.00 70.52  ? 222 SER A CA  1 
ATOM   1548 C  C   . SER A 1 200 ? 32.716 50.026 9.734  1.00 72.24  ? 222 SER A C   1 
ATOM   1549 O  O   . SER A 1 200 ? 31.624 49.451 9.812  1.00 67.87  ? 222 SER A O   1 
ATOM   1550 C  CB  . SER A 1 200 ? 34.930 48.868 9.557  1.00 62.38  ? 222 SER A CB  1 
ATOM   1551 O  OG  . SER A 1 200 ? 34.285 47.896 8.751  1.00 55.67  ? 222 SER A OG  1 
ATOM   1552 N  N   . PHE A 1 201 ? 32.908 51.101 8.967  1.00 75.51  ? 223 PHE A N   1 
ATOM   1553 C  CA  . PHE A 1 201 ? 31.805 51.597 8.155  1.00 76.17  ? 223 PHE A CA  1 
ATOM   1554 C  C   . PHE A 1 201 ? 31.350 50.548 7.149  1.00 63.46  ? 223 PHE A C   1 
ATOM   1555 O  O   . PHE A 1 201 ? 30.151 50.415 6.881  1.00 71.06  ? 223 PHE A O   1 
ATOM   1556 C  CB  . PHE A 1 201 ? 32.190 52.889 7.442  1.00 63.50  ? 223 PHE A CB  1 
ATOM   1557 C  CG  . PHE A 1 201 ? 31.094 53.434 6.572  1.00 71.34  ? 223 PHE A CG  1 
ATOM   1558 C  CD1 . PHE A 1 201 ? 29.885 53.833 7.127  1.00 82.79  ? 223 PHE A CD1 1 
ATOM   1559 C  CD2 . PHE A 1 201 ? 31.259 53.535 5.201  1.00 72.45  ? 223 PHE A CD2 1 
ATOM   1560 C  CE1 . PHE A 1 201 ? 28.867 54.328 6.331  1.00 79.10  ? 223 PHE A CE1 1 
ATOM   1561 C  CE2 . PHE A 1 201 ? 30.244 54.030 4.399  1.00 73.82  ? 223 PHE A CE2 1 
ATOM   1562 C  CZ  . PHE A 1 201 ? 29.047 54.426 4.966  1.00 81.36  ? 223 PHE A CZ  1 
ATOM   1563 N  N   . GLU A 1 202 ? 32.288 49.780 6.591  1.00 66.22  ? 224 GLU A N   1 
ATOM   1564 C  CA  . GLU A 1 202 ? 31.889 48.718 5.675  1.00 68.24  ? 224 GLU A CA  1 
ATOM   1565 C  C   . GLU A 1 202 ? 31.104 47.638 6.404  1.00 76.13  ? 224 GLU A C   1 
ATOM   1566 O  O   . GLU A 1 202 ? 30.069 47.176 5.910  1.00 59.80  ? 224 GLU A O   1 
ATOM   1567 C  CB  . GLU A 1 202 ? 33.112 48.113 4.989  1.00 73.57  ? 224 GLU A CB  1 
ATOM   1568 C  CG  . GLU A 1 202 ? 32.758 47.109 3.902  1.00 88.15  ? 224 GLU A CG  1 
ATOM   1569 C  CD  . GLU A 1 202 ? 33.976 46.416 3.329  1.00 98.09  ? 224 GLU A CD  1 
ATOM   1570 O  OE1 . GLU A 1 202 ? 34.997 46.325 4.043  1.00 117.09 ? 224 GLU A OE1 1 
ATOM   1571 O  OE2 . GLU A 1 202 ? 33.913 45.966 2.165  1.00 92.23  ? 224 GLU A OE2 1 
ATOM   1572 N  N   . LEU A 1 203 ? 31.580 47.229 7.582  1.00 77.83  ? 225 LEU A N   1 
ATOM   1573 C  CA  . LEU A 1 203 ? 30.843 46.254 8.376  1.00 67.37  ? 225 LEU A CA  1 
ATOM   1574 C  C   . LEU A 1 203 ? 29.427 46.741 8.663  1.00 73.38  ? 225 LEU A C   1 
ATOM   1575 O  O   . LEU A 1 203 ? 28.470 45.959 8.613  1.00 67.18  ? 225 LEU A O   1 
ATOM   1576 C  CB  . LEU A 1 203 ? 31.595 45.969 9.675  1.00 69.08  ? 225 LEU A CB  1 
ATOM   1577 C  CG  . LEU A 1 203 ? 30.900 45.009 10.638 1.00 53.94  ? 225 LEU A CG  1 
ATOM   1578 C  CD1 . LEU A 1 203 ? 30.644 43.692 9.938  1.00 55.54  ? 225 LEU A CD1 1 
ATOM   1579 C  CD2 . LEU A 1 203 ? 31.727 44.813 11.893 1.00 54.50  ? 225 LEU A CD2 1 
ATOM   1580 N  N   . LEU A 1 204 ? 29.272 48.035 8.947  1.00 66.87  ? 226 LEU A N   1 
ATOM   1581 C  CA  . LEU A 1 204 ? 27.938 48.587 9.148  1.00 64.94  ? 226 LEU A CA  1 
ATOM   1582 C  C   . LEU A 1 204 ? 27.096 48.461 7.885  1.00 70.68  ? 226 LEU A C   1 
ATOM   1583 O  O   . LEU A 1 204 ? 25.891 48.191 7.957  1.00 71.55  ? 226 LEU A O   1 
ATOM   1584 C  CB  . LEU A 1 204 ? 28.042 50.044 9.583  1.00 56.16  ? 226 LEU A CB  1 
ATOM   1585 C  CG  . LEU A 1 204 ? 26.720 50.795 9.696  1.00 70.94  ? 226 LEU A CG  1 
ATOM   1586 C  CD1 . LEU A 1 204 ? 25.769 50.083 10.652 1.00 57.83  ? 226 LEU A CD1 1 
ATOM   1587 C  CD2 . LEU A 1 204 ? 26.999 52.213 10.152 1.00 69.69  ? 226 LEU A CD2 1 
ATOM   1588 N  N   . LEU A 1 205 ? 27.716 48.646 6.718  1.00 72.60  ? 227 LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 205 ? 26.991 48.508 5.459  1.00 76.71  ? 227 LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 205 ? 26.609 47.055 5.195  1.00 71.10  ? 227 LEU A C   1 
ATOM   1591 O  O   . LEU A 1 205 ? 25.513 46.779 4.693  1.00 67.57  ? 227 LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 205 ? 27.831 49.062 4.307  1.00 77.18  ? 227 LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 205 ? 28.148 50.561 4.329  1.00 79.23  ? 227 LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 205 ? 29.111 50.922 3.212  1.00 69.43  ? 227 LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 205 ? 26.883 51.399 4.232  1.00 66.17  ? 227 LEU A CD2 1 
ATOM   1596 N  N   . LYS A 1 206 ? 27.499 46.112 5.521  1.00 61.08  ? 228 LYS A N   1 
ATOM   1597 C  CA  . LYS A 1 206 ? 27.163 44.703 5.359  1.00 69.10  ? 228 LYS A CA  1 
ATOM   1598 C  C   . LYS A 1 206 ? 26.014 44.294 6.274  1.00 67.25  ? 228 LYS A C   1 
ATOM   1599 O  O   . LYS A 1 206 ? 25.212 43.426 5.915  1.00 64.38  ? 228 LYS A O   1 
ATOM   1600 C  CB  . LYS A 1 206 ? 28.384 43.826 5.638  1.00 73.26  ? 228 LYS A CB  1 
ATOM   1601 C  CG  . LYS A 1 206 ? 29.623 44.152 4.824  1.00 75.43  ? 228 LYS A CG  1 
ATOM   1602 C  CD  . LYS A 1 206 ? 30.759 43.208 5.207  1.00 94.80  ? 228 LYS A CD  1 
ATOM   1603 C  CE  . LYS A 1 206 ? 32.101 43.654 4.653  1.00 98.96  ? 228 LYS A CE  1 
ATOM   1604 N  NZ  . LYS A 1 206 ? 33.214 42.791 5.152  1.00 98.68  ? 228 LYS A NZ  1 
ATOM   1605 N  N   . THR A 1 207 ? 25.920 44.900 7.457  1.00 72.92  ? 229 THR A N   1 
ATOM   1606 C  CA  . THR A 1 207 ? 24.864 44.528 8.389  1.00 72.73  ? 229 THR A CA  1 
ATOM   1607 C  C   . THR A 1 207 ? 23.530 45.120 7.960  1.00 68.99  ? 229 THR A C   1 
ATOM   1608 O  O   . THR A 1 207 ? 22.540 44.396 7.807  1.00 75.06  ? 229 THR A O   1 
ATOM   1609 C  CB  . THR A 1 207 ? 25.233 44.985 9.800  1.00 74.18  ? 229 THR A CB  1 
ATOM   1610 O  OG1 . THR A 1 207 ? 26.556 44.534 10.113 1.00 68.80  ? 229 THR A OG1 1 
ATOM   1611 C  CG2 . THR A 1 207 ? 24.257 44.411 10.818 1.00 71.43  ? 229 THR A CG2 1 
ATOM   1612 N  N   . ASN A 1 208 ? 23.497 46.439 7.742  1.00 75.15  ? 230 ASN A N   1 
ATOM   1613 C  CA  . ASN A 1 208 ? 22.340 47.206 7.294  1.00 67.02  ? 230 ASN A CA  1 
ATOM   1614 C  C   . ASN A 1 208 ? 21.111 46.818 8.105  1.00 70.27  ? 230 ASN A C   1 
ATOM   1615 O  O   . ASN A 1 208 ? 20.205 46.156 7.581  1.00 76.82  ? 230 ASN A O   1 
ATOM   1616 C  CB  . ASN A 1 208 ? 22.104 46.988 5.796  1.00 71.54  ? 230 ASN A CB  1 
ATOM   1617 C  CG  . ASN A 1 208 ? 21.046 47.927 5.212  1.00 70.33  ? 230 ASN A CG  1 
ATOM   1618 O  OD1 . ASN A 1 208 ? 20.925 49.084 5.616  1.00 65.76  ? 230 ASN A OD1 1 
ATOM   1619 N  ND2 . ASN A 1 208 ? 20.282 47.424 4.254  1.00 65.09  ? 230 ASN A ND2 1 
ATOM   1620 N  N   . PRO A 1 209 ? 21.052 47.170 9.386  1.00 70.89  ? 231 PRO A N   1 
ATOM   1621 C  CA  . PRO A 1 209 ? 19.829 46.914 10.148 1.00 68.90  ? 231 PRO A CA  1 
ATOM   1622 C  C   . PRO A 1 209 ? 18.720 47.858 9.721  1.00 78.88  ? 231 PRO A C   1 
ATOM   1623 O  O   . PRO A 1 209 ? 18.960 48.990 9.290  1.00 69.52  ? 231 PRO A O   1 
ATOM   1624 C  CB  . PRO A 1 209 ? 20.250 47.169 11.599 1.00 69.73  ? 231 PRO A CB  1 
ATOM   1625 C  CG  . PRO A 1 209 ? 21.380 48.128 11.494 1.00 66.93  ? 231 PRO A CG  1 
ATOM   1626 C  CD  . PRO A 1 209 ? 22.108 47.768 10.225 1.00 52.76  ? 231 PRO A CD  1 
ATOM   1627 N  N   . ASP A 1 210 ? 17.486 47.364 9.830  1.00 67.10  ? 232 ASP A N   1 
ATOM   1628 C  CA  . ASP A 1 210 ? 16.332 48.215 9.575  1.00 65.06  ? 232 ASP A CA  1 
ATOM   1629 C  C   . ASP A 1 210 ? 16.262 49.348 10.592 1.00 70.74  ? 232 ASP A C   1 
ATOM   1630 O  O   . ASP A 1 210 ? 15.929 50.487 10.246 1.00 66.42  ? 232 ASP A O   1 
ATOM   1631 C  CB  . ASP A 1 210 ? 15.056 47.372 9.588  1.00 73.93  ? 232 ASP A CB  1 
ATOM   1632 C  CG  . ASP A 1 210 ? 15.064 46.288 8.515  1.00 87.10  ? 232 ASP A CG  1 
ATOM   1633 O  OD1 . ASP A 1 210 ? 15.571 46.555 7.404  1.00 94.37  ? 232 ASP A OD1 1 
ATOM   1634 O  OD2 . ASP A 1 210 ? 14.572 45.170 8.780  1.00 75.67  ? 232 ASP A OD2 1 
ATOM   1635 N  N   . TRP A 1 211 ? 16.593 49.062 11.846 1.00 73.66  ? 233 TRP A N   1 
ATOM   1636 C  CA  . TRP A 1 211 ? 16.701 50.079 12.879 1.00 66.11  ? 233 TRP A CA  1 
ATOM   1637 C  C   . TRP A 1 211 ? 18.111 50.048 13.443 1.00 67.36  ? 233 TRP A C   1 
ATOM   1638 O  O   . TRP A 1 211 ? 18.644 48.972 13.733 1.00 68.44  ? 233 TRP A O   1 
ATOM   1639 C  CB  . TRP A 1 211 ? 15.686 49.851 13.997 1.00 67.95  ? 233 TRP A CB  1 
ATOM   1640 C  CG  . TRP A 1 211 ? 14.262 50.073 13.605 1.00 67.75  ? 233 TRP A CG  1 
ATOM   1641 C  CD1 . TRP A 1 211 ? 13.456 49.217 12.910 1.00 75.94  ? 233 TRP A CD1 1 
ATOM   1642 C  CD2 . TRP A 1 211 ? 13.463 51.218 13.914 1.00 59.68  ? 233 TRP A CD2 1 
ATOM   1643 N  NE1 . TRP A 1 211 ? 12.205 49.766 12.760 1.00 71.41  ? 233 TRP A NE1 1 
ATOM   1644 C  CE2 . TRP A 1 211 ? 12.183 50.993 13.370 1.00 73.68  ? 233 TRP A CE2 1 
ATOM   1645 C  CE3 . TRP A 1 211 ? 13.706 52.412 14.598 1.00 66.49  ? 233 TRP A CE3 1 
ATOM   1646 C  CZ2 . TRP A 1 211 ? 11.150 51.921 13.485 1.00 74.92  ? 233 TRP A CZ2 1 
ATOM   1647 C  CZ3 . TRP A 1 211 ? 12.680 53.330 14.714 1.00 74.66  ? 233 TRP A CZ3 1 
ATOM   1648 C  CH2 . TRP A 1 211 ? 11.418 53.081 14.158 1.00 66.41  ? 233 TRP A CH2 1 
ATOM   1649 N  N   . LEU A 1 212 ? 18.717 51.218 13.584 1.00 56.25  ? 234 LEU A N   1 
ATOM   1650 C  CA  . LEU A 1 212 ? 20.033 51.338 14.201 1.00 57.44  ? 234 LEU A CA  1 
ATOM   1651 C  C   . LEU A 1 212 ? 19.875 52.262 15.402 1.00 67.64  ? 234 LEU A C   1 
ATOM   1652 O  O   . LEU A 1 212 ? 19.780 53.483 15.247 1.00 66.59  ? 234 LEU A O   1 
ATOM   1653 C  CB  . LEU A 1 212 ? 21.076 51.866 13.222 1.00 59.96  ? 234 LEU A CB  1 
ATOM   1654 C  CG  . LEU A 1 212 ? 22.476 51.874 13.843 1.00 65.50  ? 234 LEU A CG  1 
ATOM   1655 C  CD1 . LEU A 1 212 ? 22.969 50.448 14.028 1.00 57.82  ? 234 LEU A CD1 1 
ATOM   1656 C  CD2 . LEU A 1 212 ? 23.478 52.698 13.039 1.00 53.34  ? 234 LEU A CD2 1 
ATOM   1657 N  N   . LEU A 1 213 ? 19.827 51.679 16.593 1.00 68.44  ? 235 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 213 ? 19.772 52.451 17.823 1.00 63.75  ? 235 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 213 ? 21.196 52.640 18.328 1.00 57.80  ? 235 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 213 ? 21.969 51.680 18.389 1.00 63.29  ? 235 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 213 ? 18.901 51.745 18.862 1.00 70.71  ? 235 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 213 ? 17.575 51.216 18.300 1.00 64.64  ? 235 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 213 ? 16.745 50.497 19.354 1.00 57.90  ? 235 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 213 ? 16.775 52.346 17.667 1.00 67.99  ? 235 LEU A CD2 1 
ATOM   1665 N  N   . VAL A 1 214 ? 21.553 53.879 18.657 1.00 59.48  ? 236 VAL A N   1 
ATOM   1666 C  CA  . VAL A 1 214 ? 22.932 54.228 18.974 1.00 61.35  ? 236 VAL A CA  1 
ATOM   1667 C  C   . VAL A 1 214 ? 22.968 54.980 20.295 1.00 74.49  ? 236 VAL A C   1 
ATOM   1668 O  O   . VAL A 1 214 ? 22.217 55.940 20.494 1.00 62.09  ? 236 VAL A O   1 
ATOM   1669 C  CB  . VAL A 1 214 ? 23.588 55.060 17.851 1.00 72.69  ? 236 VAL A CB  1 
ATOM   1670 C  CG1 . VAL A 1 214 ? 23.848 54.185 16.631 1.00 57.77  ? 236 VAL A CG1 1 
ATOM   1671 C  CG2 . VAL A 1 214 ? 22.716 56.246 17.470 1.00 59.32  ? 236 VAL A CG2 1 
ATOM   1672 N  N   . GLY A 1 215 ? 23.838 54.532 21.204 1.00 68.68  ? 237 GLY A N   1 
ATOM   1673 C  CA  . GLY A 1 215 ? 24.102 55.240 22.432 1.00 58.05  ? 237 GLY A CA  1 
ATOM   1674 C  C   . GLY A 1 215 ? 25.350 56.079 22.264 1.00 62.87  ? 237 GLY A C   1 
ATOM   1675 O  O   . GLY A 1 215 ? 26.437 55.552 22.017 1.00 59.72  ? 237 GLY A O   1 
ATOM   1676 N  N   . LEU A 1 216 ? 25.188 57.395 22.378 1.00 67.49  ? 238 LEU A N   1 
ATOM   1677 C  CA  . LEU A 1 216 ? 26.281 58.320 22.099 1.00 73.59  ? 238 LEU A CA  1 
ATOM   1678 C  C   . LEU A 1 216 ? 27.134 58.514 23.344 1.00 64.10  ? 238 LEU A C   1 
ATOM   1679 O  O   . LEU A 1 216 ? 26.617 58.817 24.425 1.00 62.93  ? 238 LEU A O   1 
ATOM   1680 C  CB  . LEU A 1 216 ? 25.758 59.675 21.627 1.00 75.23  ? 238 LEU A CB  1 
ATOM   1681 C  CG  . LEU A 1 216 ? 24.762 59.769 20.470 1.00 84.77  ? 238 LEU A CG  1 
ATOM   1682 C  CD1 . LEU A 1 216 ? 24.732 61.182 19.906 1.00 84.92  ? 238 LEU A CD1 1 
ATOM   1683 C  CD2 . LEU A 1 216 ? 25.085 58.767 19.386 1.00 76.05  ? 238 LEU A CD2 1 
ATOM   1684 N  N   . TYR A 1 217 ? 28.445 58.349 23.184 1.00 80.29  ? 239 TYR A N   1 
ATOM   1685 C  CA  . TYR A 1 217 ? 29.388 58.669 24.243 1.00 74.95  ? 239 TYR A CA  1 
ATOM   1686 C  C   . TYR A 1 217 ? 30.126 59.978 24.005 1.00 78.27  ? 239 TYR A C   1 
ATOM   1687 O  O   . TYR A 1 217 ? 30.586 60.595 24.973 1.00 82.50  ? 239 TYR A O   1 
ATOM   1688 C  CB  . TYR A 1 217 ? 30.403 57.533 24.411 1.00 84.04  ? 239 TYR A CB  1 
ATOM   1689 C  CG  . TYR A 1 217 ? 29.881 56.355 25.203 1.00 83.15  ? 239 TYR A CG  1 
ATOM   1690 C  CD1 . TYR A 1 217 ? 28.981 56.538 26.246 1.00 77.06  ? 239 TYR A CD1 1 
ATOM   1691 C  CD2 . TYR A 1 217 ? 30.290 55.059 24.907 1.00 72.48  ? 239 TYR A CD2 1 
ATOM   1692 C  CE1 . TYR A 1 217 ? 28.505 55.462 26.978 1.00 70.21  ? 239 TYR A CE1 1 
ATOM   1693 C  CE2 . TYR A 1 217 ? 29.819 53.981 25.628 1.00 74.67  ? 239 TYR A CE2 1 
ATOM   1694 C  CZ  . TYR A 1 217 ? 28.926 54.186 26.661 1.00 77.70  ? 239 TYR A CZ  1 
ATOM   1695 O  OH  . TYR A 1 217 ? 28.459 53.110 27.379 1.00 67.82  ? 239 TYR A OH  1 
ATOM   1696 N  N   . SER A 1 218 ? 30.238 60.417 22.753 1.00 92.77  ? 240 SER A N   1 
ATOM   1697 C  CA  . SER A 1 218 ? 30.892 61.671 22.415 1.00 90.87  ? 240 SER A CA  1 
ATOM   1698 C  C   . SER A 1 218 ? 30.125 62.359 21.297 1.00 102.89 ? 240 SER A C   1 
ATOM   1699 O  O   . SER A 1 218 ? 29.672 61.709 20.350 1.00 90.93  ? 240 SER A O   1 
ATOM   1700 C  CB  . SER A 1 218 ? 32.348 61.451 21.984 1.00 93.67  ? 240 SER A CB  1 
ATOM   1701 O  OG  . SER A 1 218 ? 32.416 60.856 20.700 1.00 88.72  ? 240 SER A OG  1 
ATOM   1702 N  N   . GLN A 1 219 ? 29.982 63.679 21.415 1.00 105.75 ? 241 GLN A N   1 
ATOM   1703 C  CA  . GLN A 1 219 ? 29.355 64.498 20.387 1.00 108.46 ? 241 GLN A CA  1 
ATOM   1704 C  C   . GLN A 1 219 ? 30.395 65.434 19.792 1.00 115.03 ? 241 GLN A C   1 
ATOM   1705 O  O   . GLN A 1 219 ? 30.932 66.287 20.515 1.00 113.93 ? 241 GLN A O   1 
ATOM   1706 C  CB  . GLN A 1 219 ? 28.187 65.296 20.967 1.00 112.83 ? 241 GLN A CB  1 
ATOM   1707 C  CG  . GLN A 1 219 ? 26.883 64.518 21.083 1.00 120.06 ? 241 GLN A CG  1 
ATOM   1708 C  CD  . GLN A 1 219 ? 26.078 64.521 19.794 1.00 124.83 ? 241 GLN A CD  1 
ATOM   1709 O  OE1 . GLN A 1 219 ? 26.636 64.543 18.695 1.00 123.32 ? 241 GLN A OE1 1 
ATOM   1710 N  NE2 . GLN A 1 219 ? 24.755 64.510 19.925 1.00 111.55 ? 241 GLN A NE2 1 
ATOM   1711 N  N   . PRO A 1 220 ? 30.721 65.317 18.496 1.00 107.88 ? 242 PRO A N   1 
ATOM   1712 C  CA  . PRO A 1 220 ? 30.188 64.372 17.508 1.00 94.10  ? 242 PRO A CA  1 
ATOM   1713 C  C   . PRO A 1 220 ? 30.868 63.012 17.616 1.00 91.26  ? 242 PRO A C   1 
ATOM   1714 O  O   . PRO A 1 220 ? 31.600 62.760 18.569 1.00 86.09  ? 242 PRO A O   1 
ATOM   1715 C  CB  . PRO A 1 220 ? 30.499 65.073 16.183 1.00 95.15  ? 242 PRO A CB  1 
ATOM   1716 C  CG  . PRO A 1 220 ? 31.816 65.742 16.453 1.00 94.08  ? 242 PRO A CG  1 
ATOM   1717 C  CD  . PRO A 1 220 ? 31.762 66.176 17.904 1.00 92.95  ? 242 PRO A CD  1 
ATOM   1718 N  N   . ASN A 1 221 ? 30.667 62.117 16.653 1.00 82.62  ? 243 ASN A N   1 
ATOM   1719 C  CA  . ASN A 1 221 ? 31.192 60.764 16.756 1.00 81.67  ? 243 ASN A CA  1 
ATOM   1720 C  C   . ASN A 1 221 ? 31.505 60.235 15.363 1.00 84.82  ? 243 ASN A C   1 
ATOM   1721 O  O   . ASN A 1 221 ? 31.305 60.919 14.354 1.00 76.35  ? 243 ASN A O   1 
ATOM   1722 C  CB  . ASN A 1 221 ? 30.200 59.857 17.482 1.00 89.50  ? 243 ASN A CB  1 
ATOM   1723 C  CG  . ASN A 1 221 ? 28.771 60.143 17.087 1.00 82.55  ? 243 ASN A CG  1 
ATOM   1724 O  OD1 . ASN A 1 221 ? 28.320 59.737 16.018 1.00 80.23  ? 243 ASN A OD1 1 
ATOM   1725 N  ND2 . ASN A 1 221 ? 28.052 60.862 17.942 1.00 77.17  ? 243 ASN A ND2 1 
ATOM   1726 N  N   . ILE A 1 222 ? 31.992 58.992 15.320 1.00 91.35  ? 244 ILE A N   1 
ATOM   1727 C  CA  . ILE A 1 222 ? 32.382 58.364 14.063 1.00 78.79  ? 244 ILE A CA  1 
ATOM   1728 C  C   . ILE A 1 222 ? 31.202 58.226 13.112 1.00 85.96  ? 244 ILE A C   1 
ATOM   1729 O  O   . ILE A 1 222 ? 31.398 58.144 11.894 1.00 81.18  ? 244 ILE A O   1 
ATOM   1730 C  CB  . ILE A 1 222 ? 33.032 56.989 14.339 1.00 95.71  ? 244 ILE A CB  1 
ATOM   1731 C  CG1 . ILE A 1 222 ? 33.849 56.517 13.134 1.00 79.47  ? 244 ILE A CG1 1 
ATOM   1732 C  CG2 . ILE A 1 222 ? 31.974 55.955 14.713 1.00 87.90  ? 244 ILE A CG2 1 
ATOM   1733 C  CD1 . ILE A 1 222 ? 35.316 56.879 13.220 1.00 80.40  ? 244 ILE A CD1 1 
ATOM   1734 N  N   . VAL A 1 223 ? 29.974 58.203 13.638 1.00 86.78  ? 245 VAL A N   1 
ATOM   1735 C  CA  . VAL A 1 223 ? 28.800 58.076 12.779 1.00 85.53  ? 245 VAL A CA  1 
ATOM   1736 C  C   . VAL A 1 223 ? 28.619 59.329 11.937 1.00 89.16  ? 245 VAL A C   1 
ATOM   1737 O  O   . VAL A 1 223 ? 28.306 59.252 10.742 1.00 93.23  ? 245 VAL A O   1 
ATOM   1738 C  CB  . VAL A 1 223 ? 27.546 57.781 13.620 1.00 91.51  ? 245 VAL A CB  1 
ATOM   1739 C  CG1 . VAL A 1 223 ? 26.289 57.983 12.789 1.00 57.51  ? 245 VAL A CG1 1 
ATOM   1740 C  CG2 . VAL A 1 223 ? 27.607 56.372 14.174 1.00 87.46  ? 245 VAL A CG2 1 
ATOM   1741 N  N   . ASP A 1 224 ? 28.803 60.501 12.545 1.00 87.26  ? 246 ASP A N   1 
ATOM   1742 C  CA  . ASP A 1 224 ? 28.748 61.740 11.781 1.00 84.52  ? 246 ASP A CA  1 
ATOM   1743 C  C   . ASP A 1 224 ? 29.808 61.751 10.688 1.00 89.67  ? 246 ASP A C   1 
ATOM   1744 O  O   . ASP A 1 224 ? 29.561 62.240 9.580  1.00 95.04  ? 246 ASP A O   1 
ATOM   1745 C  CB  . ASP A 1 224 ? 28.916 62.932 12.720 1.00 88.01  ? 246 ASP A CB  1 
ATOM   1746 C  CG  . ASP A 1 224 ? 27.878 62.947 13.827 1.00 95.26  ? 246 ASP A CG  1 
ATOM   1747 O  OD1 . ASP A 1 224 ? 26.697 62.649 13.541 1.00 92.56  ? 246 ASP A OD1 1 
ATOM   1748 O  OD2 . ASP A 1 224 ? 28.245 63.240 14.985 1.00 92.44  ? 246 ASP A OD2 1 
ATOM   1749 N  N   . GLU A 1 225 ? 30.991 61.199 10.976 1.00 94.47  ? 247 GLU A N   1 
ATOM   1750 C  CA  . GLU A 1 225 ? 32.032 61.121 9.956  1.00 85.46  ? 247 GLU A CA  1 
ATOM   1751 C  C   . GLU A 1 225 ? 31.658 60.140 8.851  1.00 88.45  ? 247 GLU A C   1 
ATOM   1752 O  O   . GLU A 1 225 ? 32.082 60.310 7.700  1.00 85.48  ? 247 GLU A O   1 
ATOM   1753 C  CB  . GLU A 1 225 ? 33.369 60.733 10.593 1.00 88.11  ? 247 GLU A CB  1 
ATOM   1754 C  CG  . GLU A 1 225 ? 34.575 61.396 9.948  1.00 109.99 ? 247 GLU A CG  1 
ATOM   1755 C  CD  . GLU A 1 225 ? 34.594 62.897 10.174 1.00 113.84 ? 247 GLU A CD  1 
ATOM   1756 O  OE1 . GLU A 1 225 ? 34.259 63.334 11.296 1.00 99.25  ? 247 GLU A OE1 1 
ATOM   1757 O  OE2 . GLU A 1 225 ? 34.935 63.640 9.228  1.00 112.61 ? 247 GLU A OE2 1 
ATOM   1758 N  N   . TRP A 1 226 ? 30.856 59.121 9.175  1.00 96.41  ? 248 TRP A N   1 
ATOM   1759 C  CA  . TRP A 1 226 ? 30.346 58.210 8.159  1.00 84.20  ? 248 TRP A CA  1 
ATOM   1760 C  C   . TRP A 1 226 ? 29.165 58.789 7.390  1.00 84.02  ? 248 TRP A C   1 
ATOM   1761 O  O   . TRP A 1 226 ? 28.916 58.369 6.259  1.00 87.86  ? 248 TRP A O   1 
ATOM   1762 C  CB  . TRP A 1 226 ? 29.945 56.882 8.793  1.00 77.91  ? 248 TRP A CB  1 
ATOM   1763 C  CG  . TRP A 1 226 ? 31.109 56.119 9.365  1.00 86.95  ? 248 TRP A CG  1 
ATOM   1764 C  CD1 . TRP A 1 226 ? 32.434 56.393 9.191  1.00 87.04  ? 248 TRP A CD1 1 
ATOM   1765 C  CD2 . TRP A 1 226 ? 31.046 54.963 10.210 1.00 90.35  ? 248 TRP A CD2 1 
ATOM   1766 N  NE1 . TRP A 1 226 ? 33.200 55.479 9.872  1.00 86.74  ? 248 TRP A NE1 1 
ATOM   1767 C  CE2 . TRP A 1 226 ? 32.373 54.589 10.505 1.00 88.34  ? 248 TRP A CE2 1 
ATOM   1768 C  CE3 . TRP A 1 226 ? 29.996 54.207 10.743 1.00 79.25  ? 248 TRP A CE3 1 
ATOM   1769 C  CZ2 . TRP A 1 226 ? 32.678 53.495 11.307 1.00 84.75  ? 248 TRP A CZ2 1 
ATOM   1770 C  CZ3 . TRP A 1 226 ? 30.300 53.123 11.539 1.00 68.54  ? 248 TRP A CZ3 1 
ATOM   1771 C  CH2 . TRP A 1 226 ? 31.630 52.776 11.814 1.00 87.37  ? 248 TRP A CH2 1 
ATOM   1772 N  N   . ARG A 1 227 ? 28.430 59.740 7.968  1.00 79.60  ? 249 ARG A N   1 
ATOM   1773 C  CA  . ARG A 1 227 ? 27.425 60.459 7.190  1.00 86.37  ? 249 ARG A CA  1 
ATOM   1774 C  C   . ARG A 1 227 ? 28.073 61.318 6.111  1.00 100.96 ? 249 ARG A C   1 
ATOM   1775 O  O   . ARG A 1 227 ? 27.438 61.624 5.094  1.00 81.52  ? 249 ARG A O   1 
ATOM   1776 C  CB  . ARG A 1 227 ? 26.563 61.336 8.106  1.00 87.34  ? 249 ARG A CB  1 
ATOM   1777 C  CG  . ARG A 1 227 ? 25.621 60.576 9.034  1.00 91.01  ? 249 ARG A CG  1 
ATOM   1778 C  CD  . ARG A 1 227 ? 24.970 61.506 10.061 1.00 84.30  ? 249 ARG A CD  1 
ATOM   1779 N  NE  . ARG A 1 227 ? 23.749 60.924 10.603 1.00 82.17  ? 249 ARG A NE  1 
ATOM   1780 C  CZ  . ARG A 1 227 ? 22.564 61.003 10.014 1.00 93.01  ? 249 ARG A CZ  1 
ATOM   1781 N  NH1 . ARG A 1 227 ? 22.408 61.627 8.858  1.00 99.24  ? 249 ARG A NH1 1 
ATOM   1782 N  NH2 . ARG A 1 227 ? 21.508 60.445 10.600 1.00 83.01  ? 249 ARG A NH2 1 
ATOM   1783 N  N   . LYS A 1 228 ? 29.324 61.745 6.327  1.00 125.18 ? 250 LYS A N   1 
ATOM   1784 C  CA  . LYS A 1 228 ? 30.060 62.442 5.275  1.00 106.58 ? 250 LYS A CA  1 
ATOM   1785 C  C   . LYS A 1 228 ? 30.220 61.567 4.039  1.00 97.62  ? 250 LYS A C   1 
ATOM   1786 O  O   . LYS A 1 228 ? 30.309 62.083 2.919  1.00 97.91  ? 250 LYS A O   1 
ATOM   1787 C  CB  . LYS A 1 228 ? 31.435 62.885 5.785  1.00 110.81 ? 250 LYS A CB  1 
ATOM   1788 C  CG  . LYS A 1 228 ? 31.503 64.315 6.317  1.00 101.80 ? 250 LYS A CG  1 
ATOM   1789 C  CD  . LYS A 1 228 ? 30.823 64.454 7.669  1.00 108.49 ? 250 LYS A CD  1 
ATOM   1790 C  CE  . LYS A 1 228 ? 31.810 64.872 8.753  1.00 111.72 ? 250 LYS A CE  1 
ATOM   1791 N  NZ  . LYS A 1 228 ? 31.178 64.893 10.106 1.00 120.84 ? 250 LYS A NZ  1 
ATOM   1792 N  N   . ASN A 1 229 ? 30.256 60.251 4.218  1.00 102.14 ? 251 ASN A N   1 
ATOM   1793 C  CA  . ASN A 1 229 ? 30.375 59.343 3.083  1.00 83.73  ? 251 ASN A CA  1 
ATOM   1794 C  C   . ASN A 1 229 ? 29.062 59.317 2.307  1.00 91.14  ? 251 ASN A C   1 
ATOM   1795 O  O   . ASN A 1 229 ? 27.998 59.148 2.912  1.00 94.95  ? 251 ASN A O   1 
ATOM   1796 C  CB  . ASN A 1 229 ? 30.733 57.941 3.573  1.00 85.15  ? 251 ASN A CB  1 
ATOM   1797 C  CG  . ASN A 1 229 ? 31.368 57.088 2.496  1.00 85.10  ? 251 ASN A CG  1 
ATOM   1798 O  OD1 . ASN A 1 229 ? 30.839 56.960 1.391  1.00 78.88  ? 251 ASN A OD1 1 
ATOM   1799 N  ND2 . ASN A 1 229 ? 32.520 56.502 2.812  1.00 79.24  ? 251 ASN A ND2 1 
ATOM   1800 N  N   . PRO A 1 230 ? 29.085 59.494 0.980  1.00 96.29  ? 252 PRO A N   1 
ATOM   1801 C  CA  . PRO A 1 230 ? 27.827 59.438 0.215  1.00 93.90  ? 252 PRO A CA  1 
ATOM   1802 C  C   . PRO A 1 230 ? 27.214 58.052 0.161  1.00 96.08  ? 252 PRO A C   1 
ATOM   1803 O  O   . PRO A 1 230 ? 26.025 57.930 -0.155 1.00 90.44  ? 252 PRO A O   1 
ATOM   1804 C  CB  . PRO A 1 230 ? 28.246 59.912 -1.182 1.00 77.64  ? 252 PRO A CB  1 
ATOM   1805 C  CG  . PRO A 1 230 ? 29.682 59.536 -1.273 1.00 81.61  ? 252 PRO A CG  1 
ATOM   1806 C  CD  . PRO A 1 230 ? 30.237 59.788 0.109  1.00 90.25  ? 252 PRO A CD  1 
ATOM   1807 N  N   . LEU A 1 231 ? 27.990 57.005 0.449  1.00 89.32  ? 253 LEU A N   1 
ATOM   1808 C  CA  . LEU A 1 231 ? 27.459 55.651 0.544  1.00 85.24  ? 253 LEU A CA  1 
ATOM   1809 C  C   . LEU A 1 231 ? 26.550 55.463 1.751  1.00 77.75  ? 253 LEU A C   1 
ATOM   1810 O  O   . LEU A 1 231 ? 25.872 54.434 1.840  1.00 71.53  ? 253 LEU A O   1 
ATOM   1811 C  CB  . LEU A 1 231 ? 28.611 54.645 0.607  1.00 69.33  ? 253 LEU A CB  1 
ATOM   1812 C  CG  . LEU A 1 231 ? 29.583 54.628 -0.574 1.00 87.92  ? 253 LEU A CG  1 
ATOM   1813 C  CD1 . LEU A 1 231 ? 30.849 53.877 -0.203 1.00 77.09  ? 253 LEU A CD1 1 
ATOM   1814 C  CD2 . LEU A 1 231 ? 28.931 54.009 -1.803 1.00 75.89  ? 253 LEU A CD2 1 
ATOM   1815 N  N   . PHE A 1 232 ? 26.515 56.434 2.666  1.00 78.30  ? 254 PHE A N   1 
ATOM   1816 C  CA  . PHE A 1 232 ? 25.732 56.297 3.888  1.00 80.05  ? 254 PHE A CA  1 
ATOM   1817 C  C   . PHE A 1 232 ? 24.240 56.219 3.598  1.00 78.41  ? 254 PHE A C   1 
ATOM   1818 O  O   . PHE A 1 232 ? 23.484 55.643 4.389  1.00 73.99  ? 254 PHE A O   1 
ATOM   1819 C  CB  . PHE A 1 232 ? 26.038 57.473 4.815  1.00 83.14  ? 254 PHE A CB  1 
ATOM   1820 C  CG  . PHE A 1 232 ? 25.548 57.291 6.218  1.00 81.50  ? 254 PHE A CG  1 
ATOM   1821 C  CD1 . PHE A 1 232 ? 26.344 56.670 7.165  1.00 87.92  ? 254 PHE A CD1 1 
ATOM   1822 C  CD2 . PHE A 1 232 ? 24.303 57.762 6.598  1.00 84.54  ? 254 PHE A CD2 1 
ATOM   1823 C  CE1 . PHE A 1 232 ? 25.902 56.510 8.461  1.00 65.85  ? 254 PHE A CE1 1 
ATOM   1824 C  CE2 . PHE A 1 232 ? 23.855 57.603 7.893  1.00 92.48  ? 254 PHE A CE2 1 
ATOM   1825 C  CZ  . PHE A 1 232 ? 24.656 56.977 8.826  1.00 82.20  ? 254 PHE A CZ  1 
ATOM   1826 N  N   . LYS A 1 233 ? 23.797 56.782 2.471  1.00 85.80  ? 255 LYS A N   1 
ATOM   1827 C  CA  . LYS A 1 233 ? 22.374 56.827 2.162  1.00 80.41  ? 255 LYS A CA  1 
ATOM   1828 C  C   . LYS A 1 233 ? 21.814 55.474 1.740  1.00 77.40  ? 255 LYS A C   1 
ATOM   1829 O  O   . LYS A 1 233 ? 20.594 55.352 1.582  1.00 77.86  ? 255 LYS A O   1 
ATOM   1830 C  CB  . LYS A 1 233 ? 22.108 57.874 1.073  1.00 84.00  ? 255 LYS A CB  1 
ATOM   1831 C  CG  . LYS A 1 233 ? 22.808 57.613 -0.256 1.00 91.73  ? 255 LYS A CG  1 
ATOM   1832 C  CD  . LYS A 1 233 ? 22.791 58.858 -1.135 1.00 88.54  ? 255 LYS A CD  1 
ATOM   1833 C  CE  . LYS A 1 233 ? 23.491 60.021 -0.438 1.00 103.95 ? 255 LYS A CE  1 
ATOM   1834 N  NZ  . LYS A 1 233 ? 23.416 61.297 -1.199 1.00 97.20  ? 255 LYS A NZ  1 
ATOM   1835 N  N   . LEU A 1 234 ? 22.659 54.459 1.559  1.00 74.47  ? 256 LEU A N   1 
ATOM   1836 C  CA  . LEU A 1 234 ? 22.175 53.125 1.225  1.00 81.16  ? 256 LEU A CA  1 
ATOM   1837 C  C   . LEU A 1 234 ? 21.644 52.371 2.434  1.00 78.45  ? 256 LEU A C   1 
ATOM   1838 O  O   . LEU A 1 234 ? 21.058 51.294 2.266  1.00 87.11  ? 256 LEU A O   1 
ATOM   1839 C  CB  . LEU A 1 234 ? 23.290 52.308 0.570  1.00 78.80  ? 256 LEU A CB  1 
ATOM   1840 C  CG  . LEU A 1 234 ? 23.739 52.775 -0.812 1.00 70.87  ? 256 LEU A CG  1 
ATOM   1841 C  CD1 . LEU A 1 234 ? 24.885 51.907 -1.309 1.00 64.79  ? 256 LEU A CD1 1 
ATOM   1842 C  CD2 . LEU A 1 234 ? 22.572 52.736 -1.785 1.00 61.10  ? 256 LEU A CD2 1 
ATOM   1843 N  N   . LEU A 1 235 ? 21.829 52.915 3.635  1.00 76.68  ? 257 LEU A N   1 
ATOM   1844 C  CA  . LEU A 1 235 ? 21.425 52.249 4.865  1.00 74.28  ? 257 LEU A CA  1 
ATOM   1845 C  C   . LEU A 1 235 ? 19.921 52.374 5.068  1.00 73.98  ? 257 LEU A C   1 
ATOM   1846 O  O   . LEU A 1 235 ? 19.362 53.473 4.984  1.00 69.16  ? 257 LEU A O   1 
ATOM   1847 C  CB  . LEU A 1 235 ? 22.172 52.848 6.057  1.00 61.17  ? 257 LEU A CB  1 
ATOM   1848 C  CG  . LEU A 1 235 ? 23.675 52.563 6.085  1.00 63.02  ? 257 LEU A CG  1 
ATOM   1849 C  CD1 . LEU A 1 235 ? 24.395 53.448 7.089  1.00 65.91  ? 257 LEU A CD1 1 
ATOM   1850 C  CD2 . LEU A 1 235 ? 23.922 51.098 6.387  1.00 56.41  ? 257 LEU A CD2 1 
ATOM   1851 N  N   . THR A 1 236 ? 19.272 51.239 5.341  1.00 65.33  ? 258 THR A N   1 
ATOM   1852 C  CA  . THR A 1 236 ? 17.838 51.242 5.608  1.00 60.38  ? 258 THR A CA  1 
ATOM   1853 C  C   . THR A 1 236 ? 17.489 52.173 6.761  1.00 66.96  ? 258 THR A C   1 
ATOM   1854 O  O   . THR A 1 236 ? 16.464 52.863 6.722  1.00 85.82  ? 258 THR A O   1 
ATOM   1855 C  CB  . THR A 1 236 ? 17.360 49.828 5.919  1.00 60.45  ? 258 THR A CB  1 
ATOM   1856 O  OG1 . THR A 1 236 ? 17.707 48.957 4.837  1.00 66.17  ? 258 THR A OG1 1 
ATOM   1857 C  CG2 . THR A 1 236 ? 15.856 49.815 6.123  1.00 68.79  ? 258 THR A CG2 1 
ATOM   1858 N  N   . ALA A 1 237 ? 18.321 52.198 7.805  1.00 72.60  ? 259 ALA A N   1 
ATOM   1859 C  CA  . ALA A 1 237 ? 18.054 53.100 8.919  1.00 83.93  ? 259 ALA A CA  1 
ATOM   1860 C  C   . ALA A 1 237 ? 18.218 54.552 8.501  1.00 76.91  ? 259 ALA A C   1 
ATOM   1861 O  O   . ALA A 1 237 ? 17.618 55.447 9.107  1.00 75.98  ? 259 ALA A O   1 
ATOM   1862 C  CB  . ALA A 1 237 ? 18.969 52.778 10.101 1.00 82.02  ? 259 ALA A CB  1 
ATOM   1863 N  N   . ALA A 1 238 ? 19.034 54.806 7.481  1.00 81.32  ? 260 ALA A N   1 
ATOM   1864 C  CA  . ALA A 1 238 ? 19.135 56.157 6.952  1.00 79.92  ? 260 ALA A CA  1 
ATOM   1865 C  C   . ALA A 1 238 ? 17.961 56.468 6.032  1.00 83.13  ? 260 ALA A C   1 
ATOM   1866 O  O   . ALA A 1 238 ? 17.376 57.554 6.120  1.00 81.39  ? 260 ALA A O   1 
ATOM   1867 C  CB  . ALA A 1 238 ? 20.469 56.337 6.227  1.00 53.65  ? 260 ALA A CB  1 
ATOM   1868 N  N   . LYS A 1 239 ? 17.590 55.518 5.166  1.00 81.06  ? 261 LYS A N   1 
ATOM   1869 C  CA  . LYS A 1 239 ? 16.451 55.709 4.271  1.00 75.39  ? 261 LYS A CA  1 
ATOM   1870 C  C   . LYS A 1 239 ? 15.180 56.021 5.054  1.00 92.79  ? 261 LYS A C   1 
ATOM   1871 O  O   . LYS A 1 239 ? 14.606 57.109 4.929  1.00 96.58  ? 261 LYS A O   1 
ATOM   1872 C  CB  . LYS A 1 239 ? 16.244 54.466 3.398  1.00 69.05  ? 261 LYS A CB  1 
ATOM   1873 C  CG  . LYS A 1 239 ? 17.334 54.192 2.375  1.00 64.19  ? 261 LYS A CG  1 
ATOM   1874 C  CD  . LYS A 1 239 ? 16.942 53.024 1.474  1.00 70.64  ? 261 LYS A CD  1 
ATOM   1875 C  CE  . LYS A 1 239 ? 18.057 52.662 0.507  1.00 80.52  ? 261 LYS A CE  1 
ATOM   1876 N  NZ  . LYS A 1 239 ? 17.629 51.625 -0.474 1.00 95.91  ? 261 LYS A NZ  1 
ATOM   1877 N  N   . LYS A 1 240 ? 14.724 55.074 5.874  1.00 82.74  ? 262 LYS A N   1 
ATOM   1878 C  CA  . LYS A 1 240 ? 13.493 55.246 6.635  1.00 78.34  ? 262 LYS A CA  1 
ATOM   1879 C  C   . LYS A 1 240 ? 13.651 56.178 7.828  1.00 69.40  ? 262 LYS A C   1 
ATOM   1880 O  O   . LYS A 1 240 ? 12.694 56.335 8.594  1.00 75.42  ? 262 LYS A O   1 
ATOM   1881 C  CB  . LYS A 1 240 ? 12.973 53.888 7.117  1.00 73.79  ? 262 LYS A CB  1 
ATOM   1882 C  CG  . LYS A 1 240 ? 12.788 52.858 6.016  1.00 65.92  ? 262 LYS A CG  1 
ATOM   1883 C  CD  . LYS A 1 240 ? 12.083 51.614 6.539  1.00 74.29  ? 262 LYS A CD  1 
ATOM   1884 C  CE  . LYS A 1 240 ? 11.764 50.644 5.410  1.00 98.05  ? 262 LYS A CE  1 
ATOM   1885 N  NZ  . LYS A 1 240 ? 10.963 49.481 5.887  1.00 108.07 ? 262 LYS A NZ  1 
ATOM   1886 N  N   . GLN A 1 241 ? 14.820 56.801 7.996  1.00 76.72  ? 263 GLN A N   1 
ATOM   1887 C  CA  . GLN A 1 241 ? 15.117 57.636 9.161  1.00 93.98  ? 263 GLN A CA  1 
ATOM   1888 C  C   . GLN A 1 241 ? 14.827 56.888 10.462 1.00 94.11  ? 263 GLN A C   1 
ATOM   1889 O  O   . GLN A 1 241 ? 14.263 57.435 11.412 1.00 76.79  ? 263 GLN A O   1 
ATOM   1890 C  CB  . GLN A 1 241 ? 14.354 58.958 9.103  1.00 82.71  ? 263 GLN A CB  1 
ATOM   1891 C  CG  . GLN A 1 241 ? 15.238 60.156 8.803  1.00 90.65  ? 263 GLN A CG  1 
ATOM   1892 C  CD  . GLN A 1 241 ? 14.468 61.458 8.808  1.00 114.34 ? 263 GLN A CD  1 
ATOM   1893 O  OE1 . GLN A 1 241 ? 13.306 61.503 8.406  1.00 122.25 ? 263 GLN A OE1 1 
ATOM   1894 N  NE2 . GLN A 1 241 ? 15.109 62.526 9.273  1.00 113.94 ? 263 GLN A NE2 1 
ATOM   1895 N  N   . GLN A 1 242 ? 15.218 55.613 10.494 1.00 84.13  ? 264 GLN A N   1 
ATOM   1896 C  CA  . GLN A 1 242 ? 15.065 54.760 11.664 1.00 82.19  ? 264 GLN A CA  1 
ATOM   1897 C  C   . GLN A 1 242 ? 16.381 54.568 12.412 1.00 77.67  ? 264 GLN A C   1 
ATOM   1898 O  O   . GLN A 1 242 ? 16.565 53.561 13.105 1.00 78.63  ? 264 GLN A O   1 
ATOM   1899 C  CB  . GLN A 1 242 ? 14.465 53.415 11.254 1.00 73.45  ? 264 GLN A CB  1 
ATOM   1900 C  CG  . GLN A 1 242 ? 13.012 53.529 10.822 1.00 68.69  ? 264 GLN A CG  1 
ATOM   1901 C  CD  . GLN A 1 242 ? 12.460 52.243 10.245 1.00 78.09  ? 264 GLN A CD  1 
ATOM   1902 O  OE1 . GLN A 1 242 ? 13.194 51.280 10.026 1.00 82.98  ? 264 GLN A OE1 1 
ATOM   1903 N  NE2 . GLN A 1 242 ? 11.156 52.222 9.993  1.00 81.20  ? 264 GLN A NE2 1 
ATOM   1904 N  N   . LEU A 1 243 ? 17.301 55.520 12.278 1.00 73.18  ? 265 LEU A N   1 
ATOM   1905 C  CA  . LEU A 1 243 ? 18.526 55.568 13.071 1.00 66.41  ? 265 LEU A CA  1 
ATOM   1906 C  C   . LEU A 1 243 ? 18.250 56.498 14.249 1.00 73.95  ? 265 LEU A C   1 
ATOM   1907 O  O   . LEU A 1 243 ? 18.270 57.724 14.106 1.00 70.92  ? 265 LEU A O   1 
ATOM   1908 C  CB  . LEU A 1 243 ? 19.701 56.042 12.219 1.00 66.77  ? 265 LEU A CB  1 
ATOM   1909 C  CG  . LEU A 1 243 ? 21.111 56.027 12.816 1.00 75.13  ? 265 LEU A CG  1 
ATOM   1910 C  CD1 . LEU A 1 243 ? 22.127 55.873 11.707 1.00 63.08  ? 265 LEU A CD1 1 
ATOM   1911 C  CD2 . LEU A 1 243 ? 21.391 57.299 13.596 1.00 71.62  ? 265 LEU A CD2 1 
ATOM   1912 N  N   . VAL A 1 244 ? 17.989 55.911 15.416 1.00 96.24  ? 266 VAL A N   1 
ATOM   1913 C  CA  . VAL A 1 244 ? 17.507 56.637 16.587 1.00 77.91  ? 266 VAL A CA  1 
ATOM   1914 C  C   . VAL A 1 244 ? 18.604 56.682 17.641 1.00 71.06  ? 266 VAL A C   1 
ATOM   1915 O  O   . VAL A 1 244 ? 19.354 55.714 17.817 1.00 76.88  ? 266 VAL A O   1 
ATOM   1916 C  CB  . VAL A 1 244 ? 16.231 55.992 17.166 1.00 84.64  ? 266 VAL A CB  1 
ATOM   1917 C  CG1 . VAL A 1 244 ? 15.476 56.990 18.030 1.00 77.02  ? 266 VAL A CG1 1 
ATOM   1918 C  CG2 . VAL A 1 244 ? 15.342 55.441 16.053 1.00 75.07  ? 266 VAL A CG2 1 
ATOM   1919 N  N   . GLU A 1 245 ? 18.687 57.807 18.348 1.00 73.24  ? 267 GLU A N   1 
ATOM   1920 C  CA  . GLU A 1 245 ? 19.631 57.974 19.444 1.00 71.99  ? 267 GLU A CA  1 
ATOM   1921 C  C   . GLU A 1 245 ? 18.973 57.532 20.745 1.00 74.26  ? 267 GLU A C   1 
ATOM   1922 O  O   . GLU A 1 245 ? 17.870 57.980 21.073 1.00 74.16  ? 267 GLU A O   1 
ATOM   1923 C  CB  . GLU A 1 245 ? 20.094 59.431 19.538 1.00 66.21  ? 267 GLU A CB  1 
ATOM   1924 C  CG  . GLU A 1 245 ? 20.965 59.740 20.750 1.00 95.75  ? 267 GLU A CG  1 
ATOM   1925 C  CD  . GLU A 1 245 ? 21.432 61.190 20.796 1.00 95.53  ? 267 GLU A CD  1 
ATOM   1926 O  OE1 . GLU A 1 245 ? 21.372 61.880 19.752 1.00 94.48  ? 267 GLU A OE1 1 
ATOM   1927 O  OE2 . GLU A 1 245 ? 21.867 61.637 21.881 1.00 75.31  ? 267 GLU A OE2 1 
ATOM   1928 N  N   . VAL A 1 246 ? 19.647 56.642 21.475 1.00 77.03  ? 268 VAL A N   1 
ATOM   1929 C  CA  . VAL A 1 246 ? 19.121 56.063 22.704 1.00 71.02  ? 268 VAL A CA  1 
ATOM   1930 C  C   . VAL A 1 246 ? 20.136 56.266 23.821 1.00 65.85  ? 268 VAL A C   1 
ATOM   1931 O  O   . VAL A 1 246 ? 21.264 56.710 23.598 1.00 73.74  ? 268 VAL A O   1 
ATOM   1932 C  CB  . VAL A 1 246 ? 18.786 54.566 22.552 1.00 68.91  ? 268 VAL A CB  1 
ATOM   1933 C  CG1 . VAL A 1 246 ? 17.746 54.365 21.463 1.00 56.44  ? 268 VAL A CG1 1 
ATOM   1934 C  CG2 . VAL A 1 246 ? 20.049 53.775 22.247 1.00 66.33  ? 268 VAL A CG2 1 
ATOM   1935 N  N   . SER A 1 247 ? 19.718 55.925 25.035 1.00 63.59  ? 269 SER A N   1 
ATOM   1936 C  CA  . SER A 1 247 ? 20.570 56.090 26.205 1.00 73.20  ? 269 SER A CA  1 
ATOM   1937 C  C   . SER A 1 247 ? 21.594 54.963 26.278 1.00 63.90  ? 269 SER A C   1 
ATOM   1938 O  O   . SER A 1 247 ? 21.206 53.790 26.335 1.00 60.37  ? 269 SER A O   1 
ATOM   1939 C  CB  . SER A 1 247 ? 19.739 56.110 27.480 1.00 55.92  ? 269 SER A CB  1 
ATOM   1940 O  OG  . SER A 1 247 ? 20.576 56.147 28.624 1.00 57.78  ? 269 SER A OG  1 
ATOM   1941 N  N   . PRO A 1 248 ? 22.893 55.265 26.279 1.00 63.28  ? 270 PRO A N   1 
ATOM   1942 C  CA  . PRO A 1 248 ? 23.881 54.194 26.472 1.00 65.16  ? 270 PRO A CA  1 
ATOM   1943 C  C   . PRO A 1 248 ? 23.882 53.651 27.889 1.00 61.99  ? 270 PRO A C   1 
ATOM   1944 O  O   . PRO A 1 248 ? 24.222 52.477 28.091 1.00 61.62  ? 270 PRO A O   1 
ATOM   1945 C  CB  . PRO A 1 248 ? 25.209 54.874 26.118 1.00 55.63  ? 270 PRO A CB  1 
ATOM   1946 C  CG  . PRO A 1 248 ? 24.971 56.324 26.404 1.00 58.49  ? 270 PRO A CG  1 
ATOM   1947 C  CD  . PRO A 1 248 ? 23.519 56.586 26.102 1.00 61.67  ? 270 PRO A CD  1 
ATOM   1948 N  N   . GLU A 1 249 ? 23.519 54.472 28.877 1.00 53.28  ? 271 GLU A N   1 
ATOM   1949 C  CA  . GLU A 1 249 ? 23.373 53.968 30.238 1.00 62.69  ? 271 GLU A CA  1 
ATOM   1950 C  C   . GLU A 1 249 ? 22.300 52.887 30.307 1.00 68.53  ? 271 GLU A C   1 
ATOM   1951 O  O   . GLU A 1 249 ? 22.497 51.838 30.930 1.00 64.72  ? 271 GLU A O   1 
ATOM   1952 C  CB  . GLU A 1 249 ? 23.034 55.118 31.193 1.00 59.06  ? 271 GLU A CB  1 
ATOM   1953 C  CG  . GLU A 1 249 ? 24.068 56.236 31.261 1.00 64.99  ? 271 GLU A CG  1 
ATOM   1954 C  CD  . GLU A 1 249 ? 23.785 57.366 30.281 1.00 81.18  ? 271 GLU A CD  1 
ATOM   1955 O  OE1 . GLU A 1 249 ? 23.043 57.138 29.300 1.00 68.27  ? 271 GLU A OE1 1 
ATOM   1956 O  OE2 . GLU A 1 249 ? 24.304 58.485 30.496 1.00 79.80  ? 271 GLU A OE2 1 
ATOM   1957 N  N   . LEU A 1 250 ? 21.156 53.124 29.661 1.00 53.76  ? 272 LEU A N   1 
ATOM   1958 C  CA  . LEU A 1 250 ? 20.062 52.164 29.730 1.00 66.81  ? 272 LEU A CA  1 
ATOM   1959 C  C   . LEU A 1 250 ? 20.396 50.894 28.964 1.00 52.49  ? 272 LEU A C   1 
ATOM   1960 O  O   . LEU A 1 250 ? 20.118 49.785 29.435 1.00 63.06  ? 272 LEU A O   1 
ATOM   1961 C  CB  . LEU A 1 250 ? 18.779 52.796 29.186 1.00 58.62  ? 272 LEU A CB  1 
ATOM   1962 C  CG  . LEU A 1 250 ? 17.552 51.889 29.039 1.00 65.53  ? 272 LEU A CG  1 
ATOM   1963 C  CD1 . LEU A 1 250 ? 17.009 51.459 30.400 1.00 53.24  ? 272 LEU A CD1 1 
ATOM   1964 C  CD2 . LEU A 1 250 ? 16.473 52.578 28.217 1.00 56.46  ? 272 LEU A CD2 1 
ATOM   1965 N  N   . TRP A 1 251 ? 21.004 51.035 27.790 1.00 45.22  ? 273 TRP A N   1 
ATOM   1966 C  CA  . TRP A 1 251 ? 21.152 49.918 26.872 1.00 59.60  ? 273 TRP A CA  1 
ATOM   1967 C  C   . TRP A 1 251 ? 22.458 49.161 27.041 1.00 58.81  ? 273 TRP A C   1 
ATOM   1968 O  O   . TRP A 1 251 ? 22.526 47.983 26.667 1.00 56.02  ? 273 TRP A O   1 
ATOM   1969 C  CB  . TRP A 1 251 ? 21.060 50.410 25.426 1.00 57.09  ? 273 TRP A CB  1 
ATOM   1970 C  CG  . TRP A 1 251 ? 19.674 50.668 24.931 1.00 69.31  ? 273 TRP A CG  1 
ATOM   1971 C  CD1 . TRP A 1 251 ? 18.905 51.771 25.174 1.00 56.06  ? 273 TRP A CD1 1 
ATOM   1972 C  CD2 . TRP A 1 251 ? 18.893 49.812 24.087 1.00 56.78  ? 273 TRP A CD2 1 
ATOM   1973 N  NE1 . TRP A 1 251 ? 17.694 51.651 24.538 1.00 68.27  ? 273 TRP A NE1 1 
ATOM   1974 C  CE2 . TRP A 1 251 ? 17.660 50.458 23.864 1.00 61.75  ? 273 TRP A CE2 1 
ATOM   1975 C  CE3 . TRP A 1 251 ? 19.118 48.561 23.498 1.00 61.51  ? 273 TRP A CE3 1 
ATOM   1976 C  CZ2 . TRP A 1 251 ? 16.654 49.896 23.080 1.00 56.22  ? 273 TRP A CZ2 1 
ATOM   1977 C  CZ3 . TRP A 1 251 ? 18.115 48.004 22.716 1.00 59.79  ? 273 TRP A CZ3 1 
ATOM   1978 C  CH2 . TRP A 1 251 ? 16.900 48.672 22.515 1.00 63.92  ? 273 TRP A CH2 1 
ATOM   1979 N  N   . SER A 1 252 ? 23.496 49.795 27.576 1.00 47.19  ? 274 SER A N   1 
ATOM   1980 C  CA  . SER A 1 252 ? 24.806 49.164 27.629 1.00 56.92  ? 274 SER A CA  1 
ATOM   1981 C  C   . SER A 1 252 ? 25.334 48.992 29.042 1.00 49.01  ? 274 SER A C   1 
ATOM   1982 O  O   . SER A 1 252 ? 25.867 47.926 29.366 1.00 59.23  ? 274 SER A O   1 
ATOM   1983 C  CB  . SER A 1 252 ? 25.815 49.971 26.801 1.00 50.19  ? 274 SER A CB  1 
ATOM   1984 O  OG  . SER A 1 252 ? 27.076 49.329 26.813 1.00 63.72  ? 274 SER A OG  1 
ATOM   1985 N  N   . LEU A 1 253 ? 25.208 50.009 29.897 1.00 54.24  ? 275 LEU A N   1 
ATOM   1986 C  CA  . LEU A 1 253 ? 25.941 50.003 31.156 1.00 61.59  ? 275 LEU A CA  1 
ATOM   1987 C  C   . LEU A 1 253 ? 25.210 49.232 32.243 1.00 58.30  ? 275 LEU A C   1 
ATOM   1988 O  O   . LEU A 1 253 ? 25.847 48.591 33.084 1.00 54.70  ? 275 LEU A O   1 
ATOM   1989 C  CB  . LEU A 1 253 ? 26.183 51.442 31.630 1.00 48.83  ? 275 LEU A CB  1 
ATOM   1990 C  CG  . LEU A 1 253 ? 26.994 52.378 30.723 1.00 54.97  ? 275 LEU A CG  1 
ATOM   1991 C  CD1 . LEU A 1 253 ? 27.133 53.753 31.368 1.00 45.32  ? 275 LEU A CD1 1 
ATOM   1992 C  CD2 . LEU A 1 253 ? 28.349 51.781 30.426 1.00 47.49  ? 275 LEU A CD2 1 
ATOM   1993 N  N   . ASN A 1 254 ? 23.881 49.285 32.246 1.00 50.71  ? 276 ASN A N   1 
ATOM   1994 C  CA  . ASN A 1 254 ? 23.115 48.928 33.436 1.00 56.22  ? 276 ASN A CA  1 
ATOM   1995 C  C   . ASN A 1 254 ? 22.832 47.425 33.505 1.00 50.83  ? 276 ASN A C   1 
ATOM   1996 O  O   . ASN A 1 254 ? 22.937 46.815 34.573 1.00 57.25  ? 276 ASN A O   1 
ATOM   1997 C  CB  . ASN A 1 254 ? 21.813 49.735 33.456 1.00 59.59  ? 276 ASN A CB  1 
ATOM   1998 C  CG  . ASN A 1 254 ? 21.984 51.105 34.100 1.00 64.17  ? 276 ASN A CG  1 
ATOM   1999 O  OD1 . ASN A 1 254 ? 21.620 51.305 35.261 1.00 49.80  ? 276 ASN A OD1 1 
ATOM   2000 N  ND2 . ASN A 1 254 ? 22.545 52.050 33.355 1.00 58.51  ? 276 ASN A ND2 1 
ATOM   2001 N  N   . ARG A 1 255 ? 22.455 46.815 32.379 1.00 55.78  ? 277 ARG A N   1 
ATOM   2002 C  CA  . ARG A 1 255 ? 22.427 45.351 32.221 1.00 57.92  ? 277 ARG A CA  1 
ATOM   2003 C  C   . ARG A 1 255 ? 21.674 44.656 33.351 1.00 61.47  ? 277 ARG A C   1 
ATOM   2004 O  O   . ARG A 1 255 ? 22.169 43.716 33.973 1.00 59.35  ? 277 ARG A O   1 
ATOM   2005 C  CB  . ARG A 1 255 ? 23.846 44.809 32.109 1.00 51.51  ? 277 ARG A CB  1 
ATOM   2006 C  CG  . ARG A 1 255 ? 24.562 45.236 30.855 1.00 47.60  ? 277 ARG A CG  1 
ATOM   2007 C  CD  . ARG A 1 255 ? 25.826 44.433 30.667 1.00 51.95  ? 277 ARG A CD  1 
ATOM   2008 N  NE  . ARG A 1 255 ? 26.718 44.551 31.813 1.00 45.70  ? 277 ARG A NE  1 
ATOM   2009 C  CZ  . ARG A 1 255 ? 27.658 45.478 31.936 1.00 53.02  ? 277 ARG A CZ  1 
ATOM   2010 N  NH1 . ARG A 1 255 ? 27.843 46.401 31.008 1.00 44.73  ? 277 ARG A NH1 1 
ATOM   2011 N  NH2 . ARG A 1 255 ? 28.431 45.477 33.018 1.00 59.37  ? 277 ARG A NH2 1 
ATOM   2012 N  N   . GLY A 1 256 ? 20.450 45.118 33.611 1.00 69.86  ? 278 GLY A N   1 
ATOM   2013 C  CA  . GLY A 1 256 ? 19.633 44.560 34.666 1.00 70.49  ? 278 GLY A CA  1 
ATOM   2014 C  C   . GLY A 1 256 ? 18.210 44.284 34.210 1.00 72.48  ? 278 GLY A C   1 
ATOM   2015 O  O   . GLY A 1 256 ? 17.834 44.557 33.067 1.00 66.93  ? 278 GLY A O   1 
ATOM   2016 N  N   . MET A 1 257 ? 17.423 43.751 35.151 1.00 68.64  ? 279 MET A N   1 
ATOM   2017 C  CA  . MET A 1 257 ? 16.030 43.406 34.874 1.00 62.99  ? 279 MET A CA  1 
ATOM   2018 C  C   . MET A 1 257 ? 15.198 44.650 34.599 1.00 64.24  ? 279 MET A C   1 
ATOM   2019 O  O   . MET A 1 257 ? 14.461 44.719 33.608 1.00 72.39  ? 279 MET A O   1 
ATOM   2020 C  CB  . MET A 1 257 ? 15.437 42.630 36.052 1.00 59.11  ? 279 MET A CB  1 
ATOM   2021 C  CG  . MET A 1 257 ? 15.923 41.204 36.204 1.00 60.48  ? 279 MET A CG  1 
ATOM   2022 S  SD  . MET A 1 257 ? 15.247 40.396 37.673 1.00 62.82  ? 279 MET A SD  1 
ATOM   2023 C  CE  . MET A 1 257 ? 16.121 41.249 38.982 1.00 61.13  ? 279 MET A CE  1 
ATOM   2024 N  N   . LEU A 1 258 ? 15.297 45.643 35.481 1.00 57.65  ? 280 LEU A N   1 
ATOM   2025 C  CA  . LEU A 1 258 ? 14.519 46.865 35.345 1.00 65.83  ? 280 LEU A CA  1 
ATOM   2026 C  C   . LEU A 1 258 ? 14.897 47.667 34.101 1.00 68.79  ? 280 LEU A C   1 
ATOM   2027 O  O   . LEU A 1 258 ? 14.058 48.414 33.586 1.00 78.05  ? 280 LEU A O   1 
ATOM   2028 C  CB  . LEU A 1 258 ? 14.693 47.702 36.613 1.00 59.89  ? 280 LEU A CB  1 
ATOM   2029 C  CG  . LEU A 1 258 ? 13.564 48.623 37.061 1.00 69.42  ? 280 LEU A CG  1 
ATOM   2030 C  CD1 . LEU A 1 258 ? 12.216 47.935 36.909 1.00 69.36  ? 280 LEU A CD1 1 
ATOM   2031 C  CD2 . LEU A 1 258 ? 13.803 49.024 38.506 1.00 50.39  ? 280 LEU A CD2 1 
ATOM   2032 N  N   . ALA A 1 259 ? 16.131 47.528 33.603 1.00 80.76  ? 281 ALA A N   1 
ATOM   2033 C  CA  . ALA A 1 259 ? 16.511 48.202 32.363 1.00 71.08  ? 281 ALA A CA  1 
ATOM   2034 C  C   . ALA A 1 259 ? 15.962 47.478 31.143 1.00 67.56  ? 281 ALA A C   1 
ATOM   2035 O  O   . ALA A 1 259 ? 15.565 48.119 30.162 1.00 59.47  ? 281 ALA A O   1 
ATOM   2036 C  CB  . ALA A 1 259 ? 18.031 48.312 32.255 1.00 51.65  ? 281 ALA A CB  1 
ATOM   2037 N  N   . ALA A 1 260 ? 15.957 46.145 31.179 1.00 59.38  ? 282 ALA A N   1 
ATOM   2038 C  CA  . ALA A 1 260 ? 15.335 45.380 30.108 1.00 66.83  ? 282 ALA A CA  1 
ATOM   2039 C  C   . ALA A 1 260 ? 13.862 45.733 29.961 1.00 66.91  ? 282 ALA A C   1 
ATOM   2040 O  O   . ALA A 1 260 ? 13.332 45.726 28.844 1.00 68.20  ? 282 ALA A O   1 
ATOM   2041 C  CB  . ALA A 1 260 ? 15.508 43.883 30.366 1.00 47.04  ? 282 ALA A CB  1 
ATOM   2042 N  N   . GLU A 1 261 ? 13.189 46.057 31.069 1.00 57.36  ? 283 GLU A N   1 
ATOM   2043 C  CA  . GLU A 1 261 ? 11.782 46.439 30.993 1.00 74.48  ? 283 GLU A CA  1 
ATOM   2044 C  C   . GLU A 1 261 ? 11.616 47.813 30.361 1.00 72.92  ? 283 GLU A C   1 
ATOM   2045 O  O   . GLU A 1 261 ? 10.720 48.016 29.532 1.00 81.57  ? 283 GLU A O   1 
ATOM   2046 C  CB  . GLU A 1 261 ? 11.151 46.410 32.383 1.00 68.66  ? 283 GLU A CB  1 
ATOM   2047 C  CG  . GLU A 1 261 ? 11.029 45.023 32.983 1.00 72.76  ? 283 GLU A CG  1 
ATOM   2048 C  CD  . GLU A 1 261 ? 10.551 45.062 34.419 1.00 69.73  ? 283 GLU A CD  1 
ATOM   2049 O  OE1 . GLU A 1 261 ? 10.240 46.170 34.912 1.00 76.38  ? 283 GLU A OE1 1 
ATOM   2050 O  OE2 . GLU A 1 261 ? 10.492 43.989 35.054 1.00 68.02  ? 283 GLU A OE2 1 
ATOM   2051 N  N   . GLU A 1 262 ? 12.460 48.772 30.750 1.00 65.36  ? 284 GLU A N   1 
ATOM   2052 C  CA  . GLU A 1 262 ? 12.432 50.087 30.120 1.00 69.21  ? 284 GLU A CA  1 
ATOM   2053 C  C   . GLU A 1 262 ? 12.849 50.014 28.657 1.00 74.82  ? 284 GLU A C   1 
ATOM   2054 O  O   . GLU A 1 262 ? 12.389 50.823 27.845 1.00 79.63  ? 284 GLU A O   1 
ATOM   2055 C  CB  . GLU A 1 262 ? 13.330 51.053 30.894 1.00 68.27  ? 284 GLU A CB  1 
ATOM   2056 C  CG  . GLU A 1 262 ? 12.570 52.111 31.670 1.00 73.35  ? 284 GLU A CG  1 
ATOM   2057 C  CD  . GLU A 1 262 ? 12.185 53.292 30.806 1.00 97.40  ? 284 GLU A CD  1 
ATOM   2058 O  OE1 . GLU A 1 262 ? 12.943 53.604 29.866 1.00 102.31 ? 284 GLU A OE1 1 
ATOM   2059 O  OE2 . GLU A 1 262 ? 11.126 53.905 31.061 1.00 104.20 ? 284 GLU A OE2 1 
ATOM   2060 N  N   . ILE A 1 263 ? 13.709 49.059 28.300 1.00 63.32  ? 285 ILE A N   1 
ATOM   2061 C  CA  . ILE A 1 263 ? 14.042 48.858 26.894 1.00 77.26  ? 285 ILE A CA  1 
ATOM   2062 C  C   . ILE A 1 263 ? 12.814 48.394 26.119 1.00 72.57  ? 285 ILE A C   1 
ATOM   2063 O  O   . ILE A 1 263 ? 12.523 48.903 25.029 1.00 70.45  ? 285 ILE A O   1 
ATOM   2064 C  CB  . ILE A 1 263 ? 15.213 47.868 26.754 1.00 51.99  ? 285 ILE A CB  1 
ATOM   2065 C  CG1 . ILE A 1 263 ? 16.529 48.537 27.147 1.00 62.60  ? 285 ILE A CG1 1 
ATOM   2066 C  CG2 . ILE A 1 263 ? 15.307 47.345 25.334 1.00 41.95  ? 285 ILE A CG2 1 
ATOM   2067 C  CD1 . ILE A 1 263 ? 17.688 47.577 27.210 1.00 62.08  ? 285 ILE A CD1 1 
ATOM   2068 N  N   . ALA A 1 264 ? 12.065 47.436 26.672 1.00 56.52  ? 286 ALA A N   1 
ATOM   2069 C  CA  . ALA A 1 264 ? 10.856 46.970 26.000 1.00 74.74  ? 286 ALA A CA  1 
ATOM   2070 C  C   . ALA A 1 264 ? 9.820  48.085 25.894 1.00 84.33  ? 286 ALA A C   1 
ATOM   2071 O  O   . ALA A 1 264 ? 9.109  48.185 24.888 1.00 73.24  ? 286 ALA A O   1 
ATOM   2072 C  CB  . ALA A 1 264 ? 10.281 45.758 26.733 1.00 49.73  ? 286 ALA A CB  1 
ATOM   2073 N  N   . ARG A 1 265 ? 9.724  48.937 26.920 1.00 73.82  ? 287 ARG A N   1 
ATOM   2074 C  CA  . ARG A 1 265 ? 8.825  50.086 26.845 1.00 82.27  ? 287 ARG A CA  1 
ATOM   2075 C  C   . ARG A 1 265 ? 9.304  51.089 25.801 1.00 86.73  ? 287 ARG A C   1 
ATOM   2076 O  O   . ARG A 1 265 ? 8.510  51.587 24.994 1.00 89.79  ? 287 ARG A O   1 
ATOM   2077 C  CB  . ARG A 1 265 ? 8.699  50.758 28.215 1.00 85.38  ? 287 ARG A CB  1 
ATOM   2078 C  CG  . ARG A 1 265 ? 7.808  50.018 29.211 1.00 89.57  ? 287 ARG A CG  1 
ATOM   2079 C  CD  . ARG A 1 265 ? 7.578  50.833 30.486 1.00 87.33  ? 287 ARG A CD  1 
ATOM   2080 N  NE  . ARG A 1 265 ? 8.756  50.875 31.346 1.00 90.50  ? 287 ARG A NE  1 
ATOM   2081 C  CZ  . ARG A 1 265 ? 9.032  49.979 32.285 1.00 80.97  ? 287 ARG A CZ  1 
ATOM   2082 N  NH1 . ARG A 1 265 ? 8.227  48.955 32.521 1.00 82.72  ? 287 ARG A NH1 1 
ATOM   2083 N  NH2 . ARG A 1 265 ? 10.144 50.111 33.002 1.00 97.24  ? 287 ARG A NH2 1 
ATOM   2084 N  N   . ASN A 1 266 ? 10.603 51.403 25.807 1.00 77.47  ? 288 ASN A N   1 
ATOM   2085 C  CA  . ASN A 1 266 ? 11.139 52.350 24.834 1.00 72.49  ? 288 ASN A CA  1 
ATOM   2086 C  C   . ASN A 1 266 ? 11.037 51.803 23.416 1.00 84.34  ? 288 ASN A C   1 
ATOM   2087 O  O   . ASN A 1 266 ? 10.734 52.548 22.475 1.00 78.66  ? 288 ASN A O   1 
ATOM   2088 C  CB  . ASN A 1 266 ? 12.588 52.690 25.182 1.00 62.93  ? 288 ASN A CB  1 
ATOM   2089 C  CG  . ASN A 1 266 ? 12.702 53.499 26.457 1.00 78.61  ? 288 ASN A CG  1 
ATOM   2090 O  OD1 . ASN A 1 266 ? 11.748 53.592 27.231 1.00 85.55  ? 288 ASN A OD1 1 
ATOM   2091 N  ND2 . ASN A 1 266 ? 13.871 54.092 26.684 1.00 76.85  ? 288 ASN A ND2 1 
ATOM   2092 N  N   . LEU A 1 267 ? 11.277 50.501 23.243 1.00 70.72  ? 289 LEU A N   1 
ATOM   2093 C  CA  . LEU A 1 267 ? 11.169 49.899 21.920 1.00 64.52  ? 289 LEU A CA  1 
ATOM   2094 C  C   . LEU A 1 267 ? 9.736  49.938 21.405 1.00 75.30  ? 289 LEU A C   1 
ATOM   2095 O  O   . LEU A 1 267 ? 9.514  50.022 20.191 1.00 76.23  ? 289 LEU A O   1 
ATOM   2096 C  CB  . LEU A 1 267 ? 11.684 48.461 21.963 1.00 65.10  ? 289 LEU A CB  1 
ATOM   2097 C  CG  . LEU A 1 267 ? 12.109 47.873 20.621 1.00 83.02  ? 289 LEU A CG  1 
ATOM   2098 C  CD1 . LEU A 1 267 ? 13.234 48.712 20.041 1.00 57.74  ? 289 LEU A CD1 1 
ATOM   2099 C  CD2 . LEU A 1 267 ? 12.533 46.422 20.783 1.00 85.59  ? 289 LEU A CD2 1 
ATOM   2100 N  N   . GLU A 1 268 ? 8.755  49.879 22.310 1.00 88.80  ? 290 GLU A N   1 
ATOM   2101 C  CA  . GLU A 1 268 ? 7.356  49.958 21.904 1.00 91.85  ? 290 GLU A CA  1 
ATOM   2102 C  C   . GLU A 1 268 ? 7.018  51.340 21.353 1.00 84.44  ? 290 GLU A C   1 
ATOM   2103 O  O   . GLU A 1 268 ? 6.307  51.456 20.349 1.00 79.25  ? 290 GLU A O   1 
ATOM   2104 C  CB  . GLU A 1 268 ? 6.453  49.603 23.089 1.00 94.32  ? 290 GLU A CB  1 
ATOM   2105 C  CG  . GLU A 1 268 ? 5.013  49.255 22.723 1.00 102.88 ? 290 GLU A CG  1 
ATOM   2106 C  CD  . GLU A 1 268 ? 4.175  48.864 23.936 1.00 122.06 ? 290 GLU A CD  1 
ATOM   2107 O  OE1 . GLU A 1 268 ? 4.304  49.519 24.994 1.00 106.98 ? 290 GLU A OE1 1 
ATOM   2108 O  OE2 . GLU A 1 268 ? 3.391  47.895 23.832 1.00 116.27 ? 290 GLU A OE2 1 
ATOM   2109 N  N   . ALA A 1 269 ? 7.530  52.398 21.988 1.00 83.30  ? 291 ALA A N   1 
ATOM   2110 C  CA  . ALA A 1 269 ? 7.273  53.752 21.512 1.00 74.53  ? 291 ALA A CA  1 
ATOM   2111 C  C   . ALA A 1 269 ? 7.901  54.023 20.153 1.00 83.82  ? 291 ALA A C   1 
ATOM   2112 O  O   . ALA A 1 269 ? 7.430  54.912 19.436 1.00 101.55 ? 291 ALA A O   1 
ATOM   2113 C  CB  . ALA A 1 269 ? 7.782  54.776 22.525 1.00 67.03  ? 291 ALA A CB  1 
ATOM   2114 N  N   . LEU A 1 270 ? 8.951  53.289 19.783 1.00 88.30  ? 292 LEU A N   1 
ATOM   2115 C  CA  . LEU A 1 270 ? 9.556  53.485 18.471 1.00 85.70  ? 292 LEU A CA  1 
ATOM   2116 C  C   . LEU A 1 270 ? 8.714  52.884 17.358 1.00 77.19  ? 292 LEU A C   1 
ATOM   2117 O  O   . LEU A 1 270 ? 8.707  53.407 16.238 1.00 85.85  ? 292 LEU A O   1 
ATOM   2118 C  CB  . LEU A 1 270 ? 10.961 52.882 18.437 1.00 83.94  ? 292 LEU A CB  1 
ATOM   2119 C  CG  . LEU A 1 270 ? 12.051 53.665 19.166 1.00 85.05  ? 292 LEU A CG  1 
ATOM   2120 C  CD1 . LEU A 1 270 ? 13.397 52.977 19.001 1.00 78.95  ? 292 LEU A CD1 1 
ATOM   2121 C  CD2 . LEU A 1 270 ? 12.101 55.097 18.653 1.00 68.24  ? 292 LEU A CD2 1 
ATOM   2122 N  N   . LEU A 1 271 ? 8.001  51.802 17.640 1.00 85.77  ? 293 LEU A N   1 
ATOM   2123 C  CA  . LEU A 1 271 ? 7.277  51.087 16.601 1.00 87.82  ? 293 LEU A CA  1 
ATOM   2124 C  C   . LEU A 1 271 ? 5.798  51.478 16.586 1.00 91.75  ? 293 LEU A C   1 
ATOM   2125 O  O   . LEU A 1 271 ? 5.057  51.209 17.531 1.00 99.66  ? 293 LEU A O   1 
ATOM   2126 C  CB  . LEU A 1 271 ? 7.445  49.576 16.796 1.00 82.95  ? 293 LEU A CB  1 
ATOM   2127 C  CG  . LEU A 1 271 ? 8.878  49.115 17.107 1.00 78.89  ? 293 LEU A CG  1 
ATOM   2128 C  CD1 . LEU A 1 271 ? 8.966  47.597 17.257 1.00 64.97  ? 293 LEU A CD1 1 
ATOM   2129 C  CD2 . LEU A 1 271 ? 9.868  49.605 16.057 1.00 68.42  ? 293 LEU A CD2 1 
HETATM 2130 C  C1  . GOL B 2 .   ? 33.955 51.103 24.706 1.00 88.23  ? 301 GOL A C1  1 
HETATM 2131 O  O1  . GOL B 2 .   ? 33.074 51.881 23.929 1.00 83.94  ? 301 GOL A O1  1 
HETATM 2132 C  C2  . GOL B 2 .   ? 34.955 50.415 23.801 1.00 100.99 ? 301 GOL A C2  1 
HETATM 2133 O  O2  . GOL B 2 .   ? 36.115 51.214 23.735 1.00 118.57 ? 301 GOL A O2  1 
HETATM 2134 C  C3  . GOL B 2 .   ? 35.262 49.016 24.316 1.00 81.46  ? 301 GOL A C3  1 
HETATM 2135 O  O3  . GOL B 2 .   ? 34.174 48.177 23.986 1.00 81.35  ? 301 GOL A O3  1 
HETATM 2136 C  C1  . GOL C 2 .   ? 18.188 47.847 36.247 1.00 92.89  ? 302 GOL A C1  1 
HETATM 2137 O  O1  . GOL C 2 .   ? 17.653 46.676 35.688 1.00 92.50  ? 302 GOL A O1  1 
HETATM 2138 C  C2  . GOL C 2 .   ? 19.471 48.237 35.553 1.00 114.68 ? 302 GOL A C2  1 
HETATM 2139 O  O2  . GOL C 2 .   ? 19.227 49.488 34.957 1.00 135.42 ? 302 GOL A O2  1 
HETATM 2140 C  C3  . GOL C 2 .   ? 20.650 48.319 36.517 1.00 97.36  ? 302 GOL A C3  1 
HETATM 2141 O  O3  . GOL C 2 .   ? 20.678 49.603 37.106 1.00 109.00 ? 302 GOL A O3  1 
HETATM 2142 C  C1  . GOL D 2 .   ? 15.195 56.428 32.587 1.00 87.72  ? 303 GOL A C1  1 
HETATM 2143 O  O1  . GOL D 2 .   ? 14.641 57.186 33.636 1.00 109.89 ? 303 GOL A O1  1 
HETATM 2144 C  C2  . GOL D 2 .   ? 14.636 55.021 32.658 1.00 109.74 ? 303 GOL A C2  1 
HETATM 2145 O  O2  . GOL D 2 .   ? 15.298 54.214 31.708 1.00 103.74 ? 303 GOL A O2  1 
HETATM 2146 C  C3  . GOL D 2 .   ? 14.758 54.459 34.067 1.00 88.96  ? 303 GOL A C3  1 
HETATM 2147 O  O3  . GOL D 2 .   ? 14.101 53.211 34.080 1.00 90.97  ? 303 GOL A O3  1 
HETATM 2148 C  C1  . PEG E 3 .   ? 32.662 37.617 26.292 1.00 85.87  ? 304 PEG A C1  1 
HETATM 2149 O  O1  . PEG E 3 .   ? 33.611 36.983 27.122 1.00 86.91  ? 304 PEG A O1  1 
HETATM 2150 C  C2  . PEG E 3 .   ? 33.342 38.556 25.323 1.00 95.50  ? 304 PEG A C2  1 
HETATM 2151 O  O2  . PEG E 3 .   ? 33.835 39.710 25.963 1.00 95.26  ? 304 PEG A O2  1 
HETATM 2152 C  C3  . PEG E 3 .   ? 35.241 39.733 26.043 1.00 82.71  ? 304 PEG A C3  1 
HETATM 2153 C  C4  . PEG E 3 .   ? 35.677 39.420 27.453 1.00 80.52  ? 304 PEG A C4  1 
HETATM 2154 O  O4  . PEG E 3 .   ? 37.049 39.099 27.497 1.00 73.68  ? 304 PEG A O4  1 
HETATM 2155 C  CA  . FLC F 4 .   ? 30.209 48.114 26.407 1.00 59.87  ? 305 FLC A CA  1 
HETATM 2156 C  CB  . FLC F 4 .   ? 30.540 48.932 27.666 1.00 68.88  ? 305 FLC A CB  1 
HETATM 2157 C  CBC . FLC F 4 .   ? 30.217 50.436 27.443 1.00 79.12  ? 305 FLC A CBC 1 
HETATM 2158 C  CG  . FLC F 4 .   ? 29.759 48.337 28.857 1.00 66.20  ? 305 FLC A CG  1 
HETATM 2159 C  CGC . FLC F 4 .   ? 30.067 48.764 30.308 1.00 57.95  ? 305 FLC A CGC 1 
HETATM 2160 O  OA1 . FLC F 4 .   ? 30.368 48.771 24.111 1.00 60.62  ? 305 FLC A OA1 1 
HETATM 2161 O  OA2 . FLC F 4 .   ? 32.256 48.466 25.238 1.00 78.23  ? 305 FLC A OA2 1 
HETATM 2162 O  OB1 . FLC F 4 .   ? 29.103 50.774 27.011 1.00 66.63  ? 305 FLC A OB1 1 
HETATM 2163 O  OB2 . FLC F 4 .   ? 31.142 51.230 27.730 1.00 91.36  ? 305 FLC A OB2 1 
HETATM 2164 O  OG1 . FLC F 4 .   ? 29.528 48.158 31.255 1.00 69.84  ? 305 FLC A OG1 1 
HETATM 2165 O  OG2 . FLC F 4 .   ? 30.858 49.723 30.445 1.00 65.87  ? 305 FLC A OG2 1 
HETATM 2166 O  OHB . FLC F 4 .   ? 31.935 48.780 27.879 1.00 70.71  ? 305 FLC A OHB 1 
HETATM 2167 C  CAC . FLC G 4 .   ? 34.018 52.560 31.038 1.00 124.12 ? 306 FLC A CAC 1 
HETATM 2168 C  CA  . FLC G 4 .   ? 35.471 52.264 30.616 1.00 137.16 ? 306 FLC A CA  1 
HETATM 2169 C  CB  . FLC G 4 .   ? 35.750 50.993 29.791 1.00 133.94 ? 306 FLC A CB  1 
HETATM 2170 C  CBC . FLC G 4 .   ? 35.395 51.200 28.294 1.00 134.70 ? 306 FLC A CBC 1 
HETATM 2171 C  CG  . FLC G 4 .   ? 37.241 50.670 29.948 1.00 124.08 ? 306 FLC A CG  1 
HETATM 2172 C  CGC . FLC G 4 .   ? 37.682 49.198 29.900 1.00 123.28 ? 306 FLC A CGC 1 
HETATM 2173 O  OA1 . FLC G 4 .   ? 33.161 52.655 30.135 1.00 116.79 ? 306 FLC A OA1 1 
HETATM 2174 O  OA2 . FLC G 4 .   ? 33.792 52.695 32.266 1.00 97.81  ? 306 FLC A OA2 1 
HETATM 2175 O  OB1 . FLC G 4 .   ? 35.090 52.338 27.898 1.00 127.37 ? 306 FLC A OB1 1 
HETATM 2176 O  OB2 . FLC G 4 .   ? 35.452 50.173 27.575 1.00 125.22 ? 306 FLC A OB2 1 
HETATM 2177 O  OG1 . FLC G 4 .   ? 38.232 48.709 30.907 1.00 103.08 ? 306 FLC A OG1 1 
HETATM 2178 O  OG2 . FLC G 4 .   ? 37.450 48.591 28.827 1.00 118.68 ? 306 FLC A OG2 1 
HETATM 2179 O  OHB . FLC G 4 .   ? 34.996 49.916 30.327 1.00 113.11 ? 306 FLC A OHB 1 
HETATM 2180 FE FE  . FE  H 5 .   ? 32.678 50.564 29.114 1.00 106.67 ? 307 FE  A FE  1 
HETATM 2181 O  O   . HOH I 6 .   ? 34.988 52.383 34.714 1.00 65.94  ? 401 HOH A O   1 
HETATM 2182 O  O   . HOH I 6 .   ? 22.554 42.458 16.852 1.00 58.02  ? 402 HOH A O   1 
HETATM 2183 O  O   . HOH I 6 .   ? 24.227 46.912 51.531 1.00 54.19  ? 403 HOH A O   1 
HETATM 2184 O  O   . HOH I 6 .   ? 38.435 54.208 41.216 1.00 49.33  ? 404 HOH A O   1 
HETATM 2185 O  O   . HOH I 6 .   ? 24.691 60.227 33.131 1.00 65.65  ? 405 HOH A O   1 
HETATM 2186 O  O   . HOH I 6 .   ? 26.720 42.223 27.265 1.00 48.24  ? 406 HOH A O   1 
HETATM 2187 O  O   . HOH I 6 .   ? 48.255 42.663 47.268 1.00 63.61  ? 407 HOH A O   1 
HETATM 2188 O  O   . HOH I 6 .   ? 21.752 44.990 19.396 1.00 59.01  ? 408 HOH A O   1 
HETATM 2189 O  O   . HOH I 6 .   ? 40.232 46.396 38.663 1.00 48.84  ? 409 HOH A O   1 
HETATM 2190 O  O   . HOH I 6 .   ? 32.753 41.468 23.667 1.00 43.12  ? 410 HOH A O   1 
HETATM 2191 O  O   . HOH I 6 .   ? 33.443 32.576 50.679 1.00 60.95  ? 411 HOH A O   1 
HETATM 2192 O  O   . HOH I 6 .   ? 43.051 50.764 45.010 1.00 59.78  ? 412 HOH A O   1 
HETATM 2193 O  O   . HOH I 6 .   ? 22.924 48.435 55.583 1.00 63.71  ? 413 HOH A O   1 
HETATM 2194 O  O   . HOH I 6 .   ? 20.224 55.633 45.036 1.00 72.05  ? 414 HOH A O   1 
HETATM 2195 O  O   . HOH I 6 .   ? 23.448 61.727 31.324 1.00 79.85  ? 415 HOH A O   1 
# 
