data_9GXB
# 
_entry.id   9GXB 
# 
_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   9GXB         pdb_00009gxb 10.2210/pdb9gxb/pdb 
WWPDB D_1292141327 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_software.name' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GXB 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mmedina@unizar.es    Milagros Medina        ? 'principal investigator/group leader' 0000-0001-8743-0182 
3 jmmartin@iqf.csic.es Jose     Martin-Garcia M 'principal investigator/group leader' 0000-0002-4558-3858 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Martinez-Julvez, M.' 1 0000-0001-9047-0046 
'Martin-Garcia, J.M.' 2 0000-0002-4558-3858 
'Medina, M.'          3 0000-0001-8743-0182 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            762 
_citation.language                  ? 
_citation.page_first                110204 
_citation.page_last                 110204 
_citation.title                     
'New insights into the function and molecular mechanisms of Ferredoxin-NADP + reductase from Brucella ovis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2024.110204 
_citation.pdbx_database_id_PubMed   39522858 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Moreno, A.'            1  ? 
primary 'Quereda-Moraleda, I.'  2  ? 
primary 'Lozano-Vallhonrat, C.' 3  ? 
primary 'Bunuel-Escudero, M.'   4  ? 
primary 'Botha, S.'             5  ? 
primary 'Kupitz, C.'            6  ? 
primary 'Lisova, S.'            7  ? 
primary 'Sierra, R.'            8  ? 
primary 'Mariani, V.'           9  ? 
primary 'Schleissner, P.'       10 ? 
primary 'Gee, L.B.'             11 ? 
primary 'Dorner, K.'            12 ? 
primary 'Schmidt, C.'           13 ? 
primary 'Han, H.'               14 ? 
primary 'Kloos, M.'             15 ? 
primary 'Smyth, P.'             16 ? 
primary 'Valerio, J.'           17 ? 
primary 'Schulz, J.'            18 ? 
primary 'de Wijn, R.'           19 ? 
primary 'Melo, D.V.M.'          20 ? 
primary 'Round, A.'             21 ? 
primary 'Trost, F.'             22 ? 
primary 'Sobolev, E.'           23 ? 
primary 'Juncheng, E.'          24 ? 
primary 'Sikorski, M.'          25 ? 
primary 'Bean, R.'              26 ? 
primary 'Martinez-Julvez, M.'   27 ? 
primary 'Martin-Garcia, J.M.'   28 ? 
primary 'Medina, M.'            29 ? 
# 
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 'ferredoxin--NADP(+) reductase' 29937.053 1  1.18.1.2 ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'   785.550   1  ?        ? ? ? 
3 water       nat water                           18.015    64 ?        ? ? ? 
# 
_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       
;GPGSHMSSNFNQETVTDIHHWTDTLFSFRTTRDPGFRFQSGQFIMMGLEVNGKPLTRAYSIASSLYEDGLEFFSIKVPNG
PLTSKLQHLKKGDQIIVSKKPVGTLLYDNLKPGKHLWLLSTGTGLAPFLSIIRDLEVYERFEKVILVHGVRQVAELAYTD
FISNELPQDEFLGEMVKNQLIYYPTVTREPYKTRGRLTDLIRSGQLFKDVGLPEFNHEDDRMMLCGSPEMLAETKQILEE
RGFTEGSQSEPGEFVIEKAFVEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGSHMSSNFNQETVTDIHHWTDTLFSFRTTRDPGFRFQSGQFIMMGLEVNGKPLTRAYSIASSLYEDGLEFFSIKVPNG
PLTSKLQHLKKGDQIIVSKKPVGTLLYDNLKPGKHLWLLSTGTGLAPFLSIIRDLEVYERFEKVILVHGVRQVAELAYTD
FISNELPQDEFLGEMVKNQLIYYPTVTREPYKTRGRLTDLIRSGQLFKDVGLPEFNHEDDRMMLCGSPEMLAETKQILEE
RGFTEGSQSEPGEFVIEKAFVEK
;
_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 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   SER n 
1 5   HIS n 
1 6   MET n 
1 7   SER n 
1 8   SER n 
1 9   ASN n 
1 10  PHE n 
1 11  ASN n 
1 12  GLN n 
1 13  GLU n 
1 14  THR n 
1 15  VAL n 
1 16  THR n 
1 17  ASP n 
1 18  ILE n 
1 19  HIS n 
1 20  HIS n 
1 21  TRP n 
1 22  THR n 
1 23  ASP n 
1 24  THR n 
1 25  LEU n 
1 26  PHE n 
1 27  SER n 
1 28  PHE n 
1 29  ARG n 
1 30  THR n 
1 31  THR n 
1 32  ARG n 
1 33  ASP n 
1 34  PRO n 
1 35  GLY n 
1 36  PHE n 
1 37  ARG n 
1 38  PHE n 
1 39  GLN n 
1 40  SER n 
1 41  GLY n 
1 42  GLN n 
1 43  PHE n 
1 44  ILE n 
1 45  MET n 
1 46  MET n 
1 47  GLY n 
1 48  LEU n 
1 49  GLU n 
1 50  VAL n 
1 51  ASN n 
1 52  GLY n 
1 53  LYS n 
1 54  PRO n 
1 55  LEU n 
1 56  THR n 
1 57  ARG n 
1 58  ALA n 
1 59  TYR n 
1 60  SER n 
1 61  ILE n 
1 62  ALA n 
1 63  SER n 
1 64  SER n 
1 65  LEU n 
1 66  TYR n 
1 67  GLU n 
1 68  ASP n 
1 69  GLY n 
1 70  LEU n 
1 71  GLU n 
1 72  PHE n 
1 73  PHE n 
1 74  SER n 
1 75  ILE n 
1 76  LYS n 
1 77  VAL n 
1 78  PRO n 
1 79  ASN n 
1 80  GLY n 
1 81  PRO n 
1 82  LEU n 
1 83  THR n 
1 84  SER n 
1 85  LYS n 
1 86  LEU n 
1 87  GLN n 
1 88  HIS n 
1 89  LEU n 
1 90  LYS n 
1 91  LYS n 
1 92  GLY n 
1 93  ASP n 
1 94  GLN n 
1 95  ILE n 
1 96  ILE n 
1 97  VAL n 
1 98  SER n 
1 99  LYS n 
1 100 LYS n 
1 101 PRO n 
1 102 VAL n 
1 103 GLY n 
1 104 THR n 
1 105 LEU n 
1 106 LEU n 
1 107 TYR n 
1 108 ASP n 
1 109 ASN n 
1 110 LEU n 
1 111 LYS n 
1 112 PRO n 
1 113 GLY n 
1 114 LYS n 
1 115 HIS n 
1 116 LEU n 
1 117 TRP n 
1 118 LEU n 
1 119 LEU n 
1 120 SER n 
1 121 THR n 
1 122 GLY n 
1 123 THR n 
1 124 GLY n 
1 125 LEU n 
1 126 ALA n 
1 127 PRO n 
1 128 PHE n 
1 129 LEU n 
1 130 SER n 
1 131 ILE n 
1 132 ILE n 
1 133 ARG n 
1 134 ASP n 
1 135 LEU n 
1 136 GLU n 
1 137 VAL n 
1 138 TYR n 
1 139 GLU n 
1 140 ARG n 
1 141 PHE n 
1 142 GLU n 
1 143 LYS n 
1 144 VAL n 
1 145 ILE n 
1 146 LEU n 
1 147 VAL n 
1 148 HIS n 
1 149 GLY n 
1 150 VAL n 
1 151 ARG n 
1 152 GLN n 
1 153 VAL n 
1 154 ALA n 
1 155 GLU n 
1 156 LEU n 
1 157 ALA n 
1 158 TYR n 
1 159 THR n 
1 160 ASP n 
1 161 PHE n 
1 162 ILE n 
1 163 SER n 
1 164 ASN n 
1 165 GLU n 
1 166 LEU n 
1 167 PRO n 
1 168 GLN n 
1 169 ASP n 
1 170 GLU n 
1 171 PHE n 
1 172 LEU n 
1 173 GLY n 
1 174 GLU n 
1 175 MET n 
1 176 VAL n 
1 177 LYS n 
1 178 ASN n 
1 179 GLN n 
1 180 LEU n 
1 181 ILE n 
1 182 TYR n 
1 183 TYR n 
1 184 PRO n 
1 185 THR n 
1 186 VAL n 
1 187 THR n 
1 188 ARG n 
1 189 GLU n 
1 190 PRO n 
1 191 TYR n 
1 192 LYS n 
1 193 THR n 
1 194 ARG n 
1 195 GLY n 
1 196 ARG n 
1 197 LEU n 
1 198 THR n 
1 199 ASP n 
1 200 LEU n 
1 201 ILE n 
1 202 ARG n 
1 203 SER n 
1 204 GLY n 
1 205 GLN n 
1 206 LEU n 
1 207 PHE n 
1 208 LYS n 
1 209 ASP n 
1 210 VAL n 
1 211 GLY n 
1 212 LEU n 
1 213 PRO n 
1 214 GLU n 
1 215 PHE n 
1 216 ASN n 
1 217 HIS n 
1 218 GLU n 
1 219 ASP n 
1 220 ASP n 
1 221 ARG n 
1 222 MET n 
1 223 MET n 
1 224 LEU n 
1 225 CYS n 
1 226 GLY n 
1 227 SER n 
1 228 PRO n 
1 229 GLU n 
1 230 MET n 
1 231 LEU n 
1 232 ALA n 
1 233 GLU n 
1 234 THR n 
1 235 LYS n 
1 236 GLN n 
1 237 ILE n 
1 238 LEU n 
1 239 GLU n 
1 240 GLU n 
1 241 ARG n 
1 242 GLY n 
1 243 PHE n 
1 244 THR n 
1 245 GLU n 
1 246 GLY n 
1 247 SER n 
1 248 GLN n 
1 249 SER n 
1 250 GLU n 
1 251 PRO n 
1 252 GLY n 
1 253 GLU n 
1 254 PHE n 
1 255 VAL n 
1 256 ILE n 
1 257 GLU n 
1 258 LYS n 
1 259 ALA n 
1 260 PHE n 
1 261 VAL n 
1 262 GLU n 
1 263 LYS 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                   263 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'fpr, BOV_0348' 
_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      'Brucella ovis ATCC 25840' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     444178 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
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   GLY 1   -4  ?   ?   ?   A . n 
A 1 2   PRO 2   -3  ?   ?   ?   A . n 
A 1 3   GLY 3   -2  ?   ?   ?   A . n 
A 1 4   SER 4   -1  ?   ?   ?   A . n 
A 1 5   HIS 5   0   ?   ?   ?   A . n 
A 1 6   MET 6   1   ?   ?   ?   A . n 
A 1 7   SER 7   2   2   SER SER A . n 
A 1 8   SER 8   3   3   SER SER A . n 
A 1 9   ASN 9   4   4   ASN ASN A . n 
A 1 10  PHE 10  5   5   PHE PHE A . n 
A 1 11  ASN 11  6   6   ASN ASN A . n 
A 1 12  GLN 12  7   7   GLN GLN A . n 
A 1 13  GLU 13  8   8   GLU GLU A . n 
A 1 14  THR 14  9   9   THR THR A . n 
A 1 15  VAL 15  10  10  VAL VAL A . n 
A 1 16  THR 16  11  11  THR THR A . n 
A 1 17  ASP 17  12  12  ASP ASP A . n 
A 1 18  ILE 18  13  13  ILE ILE A . n 
A 1 19  HIS 19  14  14  HIS HIS A . n 
A 1 20  HIS 20  15  15  HIS HIS A . n 
A 1 21  TRP 21  16  16  TRP TRP A . n 
A 1 22  THR 22  17  17  THR THR A . n 
A 1 23  ASP 23  18  18  ASP ASP A . n 
A 1 24  THR 24  19  19  THR THR A . n 
A 1 25  LEU 25  20  20  LEU LEU A . n 
A 1 26  PHE 26  21  21  PHE PHE A . n 
A 1 27  SER 27  22  22  SER SER A . n 
A 1 28  PHE 28  23  23  PHE PHE A . n 
A 1 29  ARG 29  24  24  ARG ARG A . n 
A 1 30  THR 30  25  25  THR THR A . n 
A 1 31  THR 31  26  26  THR THR A . n 
A 1 32  ARG 32  27  27  ARG ARG A . n 
A 1 33  ASP 33  28  28  ASP ASP A . n 
A 1 34  PRO 34  29  29  PRO PRO A . n 
A 1 35  GLY 35  30  30  GLY GLY A . n 
A 1 36  PHE 36  31  31  PHE PHE A . n 
A 1 37  ARG 37  32  32  ARG ARG A . n 
A 1 38  PHE 38  33  33  PHE PHE A . n 
A 1 39  GLN 39  34  34  GLN GLN A . n 
A 1 40  SER 40  35  35  SER SER A . n 
A 1 41  GLY 41  36  36  GLY GLY A . n 
A 1 42  GLN 42  37  37  GLN GLN A . n 
A 1 43  PHE 43  38  38  PHE PHE A . n 
A 1 44  ILE 44  39  39  ILE ILE A . n 
A 1 45  MET 45  40  40  MET MET A . n 
A 1 46  MET 46  41  41  MET MET A . n 
A 1 47  GLY 47  42  42  GLY GLY A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  GLU 49  44  44  GLU GLU A . n 
A 1 50  VAL 50  45  45  VAL VAL A . n 
A 1 51  ASN 51  46  46  ASN ASN A . n 
A 1 52  GLY 52  47  47  GLY GLY A . n 
A 1 53  LYS 53  48  48  LYS LYS A . n 
A 1 54  PRO 54  49  49  PRO PRO A . n 
A 1 55  LEU 55  50  50  LEU LEU A . n 
A 1 56  THR 56  51  51  THR THR A . n 
A 1 57  ARG 57  52  52  ARG ARG A . n 
A 1 58  ALA 58  53  53  ALA ALA A . n 
A 1 59  TYR 59  54  54  TYR TYR A . n 
A 1 60  SER 60  55  55  SER SER A . n 
A 1 61  ILE 61  56  56  ILE ILE A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  SER 63  58  58  SER SER A . n 
A 1 64  SER 64  59  59  SER SER A . n 
A 1 65  LEU 65  60  60  LEU LEU A . n 
A 1 66  TYR 66  61  61  TYR TYR A . n 
A 1 67  GLU 67  62  62  GLU GLU A . n 
A 1 68  ASP 68  63  63  ASP ASP A . n 
A 1 69  GLY 69  64  64  GLY GLY A . n 
A 1 70  LEU 70  65  65  LEU LEU A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  PHE 72  67  67  PHE PHE A . n 
A 1 73  PHE 73  68  68  PHE PHE A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ILE 75  70  70  ILE ILE A . n 
A 1 76  LYS 76  71  71  LYS LYS A . n 
A 1 77  VAL 77  72  72  VAL VAL A . n 
A 1 78  PRO 78  73  73  PRO PRO A . n 
A 1 79  ASN 79  74  74  ASN ASN A . n 
A 1 80  GLY 80  75  75  GLY GLY A . n 
A 1 81  PRO 81  76  76  PRO PRO A . n 
A 1 82  LEU 82  77  77  LEU LEU A . n 
A 1 83  THR 83  78  78  THR THR A . n 
A 1 84  SER 84  79  79  SER SER A . n 
A 1 85  LYS 85  80  80  LYS LYS A . n 
A 1 86  LEU 86  81  81  LEU LEU A . n 
A 1 87  GLN 87  82  82  GLN GLN A . n 
A 1 88  HIS 88  83  83  HIS HIS A . n 
A 1 89  LEU 89  84  84  LEU LEU A . n 
A 1 90  LYS 90  85  85  LYS LYS A . n 
A 1 91  LYS 91  86  86  LYS LYS A . n 
A 1 92  GLY 92  87  87  GLY GLY A . n 
A 1 93  ASP 93  88  88  ASP ASP A . n 
A 1 94  GLN 94  89  89  GLN GLN A . n 
A 1 95  ILE 95  90  90  ILE ILE A . n 
A 1 96  ILE 96  91  91  ILE ILE A . n 
A 1 97  VAL 97  92  92  VAL VAL A . n 
A 1 98  SER 98  93  93  SER SER A . n 
A 1 99  LYS 99  94  94  LYS LYS A . n 
A 1 100 LYS 100 95  95  LYS LYS A . n 
A 1 101 PRO 101 96  96  PRO PRO A . n 
A 1 102 VAL 102 97  97  VAL VAL A . n 
A 1 103 GLY 103 98  98  GLY GLY A . n 
A 1 104 THR 104 99  99  THR THR A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 LEU 106 101 101 LEU LEU A . n 
A 1 107 TYR 107 102 102 TYR TYR A . n 
A 1 108 ASP 108 103 103 ASP ASP A . n 
A 1 109 ASN 109 104 104 ASN ASN A . n 
A 1 110 LEU 110 105 105 LEU LEU A . n 
A 1 111 LYS 111 106 106 LYS LYS A . n 
A 1 112 PRO 112 107 107 PRO PRO A . n 
A 1 113 GLY 113 108 108 GLY GLY A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 HIS 115 110 110 HIS HIS A . n 
A 1 116 LEU 116 111 111 LEU LEU A . n 
A 1 117 TRP 117 112 112 TRP TRP A . n 
A 1 118 LEU 118 113 113 LEU LEU A . n 
A 1 119 LEU 119 114 114 LEU LEU A . n 
A 1 120 SER 120 115 115 SER SER A . n 
A 1 121 THR 121 116 116 THR THR A . n 
A 1 122 GLY 122 117 117 GLY GLY A . n 
A 1 123 THR 123 118 118 THR THR A . n 
A 1 124 GLY 124 119 119 GLY GLY A . n 
A 1 125 LEU 125 120 120 LEU LEU A . n 
A 1 126 ALA 126 121 121 ALA ALA A . n 
A 1 127 PRO 127 122 122 PRO PRO A . n 
A 1 128 PHE 128 123 123 PHE PHE A . n 
A 1 129 LEU 129 124 124 LEU LEU A . n 
A 1 130 SER 130 125 125 SER SER A . n 
A 1 131 ILE 131 126 126 ILE ILE A . n 
A 1 132 ILE 132 127 127 ILE ILE A . n 
A 1 133 ARG 133 128 128 ARG ARG A . n 
A 1 134 ASP 134 129 129 ASP ASP A . n 
A 1 135 LEU 135 130 130 LEU LEU A . n 
A 1 136 GLU 136 131 131 GLU GLU A . n 
A 1 137 VAL 137 132 132 VAL VAL A . n 
A 1 138 TYR 138 133 133 TYR TYR A . n 
A 1 139 GLU 139 134 134 GLU GLU A . n 
A 1 140 ARG 140 135 135 ARG ARG A . n 
A 1 141 PHE 141 136 136 PHE PHE A . n 
A 1 142 GLU 142 137 137 GLU GLU A . n 
A 1 143 LYS 143 138 138 LYS LYS A . n 
A 1 144 VAL 144 139 139 VAL VAL A . n 
A 1 145 ILE 145 140 140 ILE ILE A . n 
A 1 146 LEU 146 141 141 LEU LEU A . n 
A 1 147 VAL 147 142 142 VAL VAL A . n 
A 1 148 HIS 148 143 143 HIS HIS A . n 
A 1 149 GLY 149 144 144 GLY GLY A . n 
A 1 150 VAL 150 145 145 VAL VAL A . n 
A 1 151 ARG 151 146 146 ARG ARG A . n 
A 1 152 GLN 152 147 147 GLN GLN A . n 
A 1 153 VAL 153 148 148 VAL VAL A . n 
A 1 154 ALA 154 149 149 ALA ALA A . n 
A 1 155 GLU 155 150 150 GLU GLU A . n 
A 1 156 LEU 156 151 151 LEU LEU A . n 
A 1 157 ALA 157 152 152 ALA ALA A . n 
A 1 158 TYR 158 153 153 TYR TYR A . n 
A 1 159 THR 159 154 154 THR THR A . n 
A 1 160 ASP 160 155 155 ASP ASP A . n 
A 1 161 PHE 161 156 156 PHE PHE A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 ASN 164 159 159 ASN ASN A . n 
A 1 165 GLU 165 160 160 GLU GLU A . n 
A 1 166 LEU 166 161 161 LEU LEU A . n 
A 1 167 PRO 167 162 162 PRO PRO A . n 
A 1 168 GLN 168 163 163 GLN GLN A . n 
A 1 169 ASP 169 164 164 ASP ASP A . n 
A 1 170 GLU 170 165 165 GLU GLU A . n 
A 1 171 PHE 171 166 166 PHE PHE A . n 
A 1 172 LEU 172 167 167 LEU LEU A . n 
A 1 173 GLY 173 168 168 GLY GLY A . n 
A 1 174 GLU 174 169 169 GLU GLU A . n 
A 1 175 MET 175 170 170 MET MET A . n 
A 1 176 VAL 176 171 171 VAL VAL A . n 
A 1 177 LYS 177 172 172 LYS LYS A . n 
A 1 178 ASN 178 173 173 ASN ASN A . n 
A 1 179 GLN 179 174 174 GLN GLN A . n 
A 1 180 LEU 180 175 175 LEU LEU A . n 
A 1 181 ILE 181 176 176 ILE ILE A . n 
A 1 182 TYR 182 177 177 TYR TYR A . n 
A 1 183 TYR 183 178 178 TYR TYR A . n 
A 1 184 PRO 184 179 179 PRO PRO A . n 
A 1 185 THR 185 180 180 THR THR A . n 
A 1 186 VAL 186 181 181 VAL VAL A . n 
A 1 187 THR 187 182 182 THR THR A . n 
A 1 188 ARG 188 183 183 ARG ARG A . n 
A 1 189 GLU 189 184 184 GLU GLU A . n 
A 1 190 PRO 190 185 185 PRO PRO A . n 
A 1 191 TYR 191 186 186 TYR TYR A . n 
A 1 192 LYS 192 187 187 LYS LYS A . n 
A 1 193 THR 193 188 188 THR THR A . n 
A 1 194 ARG 194 189 189 ARG ARG A . n 
A 1 195 GLY 195 190 190 GLY GLY A . n 
A 1 196 ARG 196 191 191 ARG ARG A . n 
A 1 197 LEU 197 192 192 LEU LEU A . n 
A 1 198 THR 198 193 193 THR THR A . n 
A 1 199 ASP 199 194 194 ASP ASP A . n 
A 1 200 LEU 200 195 195 LEU LEU A . n 
A 1 201 ILE 201 196 196 ILE ILE A . n 
A 1 202 ARG 202 197 197 ARG ARG A . n 
A 1 203 SER 203 198 198 SER SER A . n 
A 1 204 GLY 204 199 199 GLY GLY A . n 
A 1 205 GLN 205 200 200 GLN GLN A . n 
A 1 206 LEU 206 201 201 LEU LEU A . n 
A 1 207 PHE 207 202 202 PHE PHE A . n 
A 1 208 LYS 208 203 203 LYS LYS A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 VAL 210 205 205 VAL VAL A . n 
A 1 211 GLY 211 206 206 GLY GLY A . n 
A 1 212 LEU 212 207 207 LEU LEU A . n 
A 1 213 PRO 213 208 208 PRO PRO A . n 
A 1 214 GLU 214 209 209 GLU GLU A . n 
A 1 215 PHE 215 210 210 PHE PHE A . n 
A 1 216 ASN 216 211 211 ASN ASN A . n 
A 1 217 HIS 217 212 212 HIS HIS A . n 
A 1 218 GLU 218 213 213 GLU GLU A . n 
A 1 219 ASP 219 214 214 ASP ASP A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 ARG 221 216 216 ARG ARG A . n 
A 1 222 MET 222 217 217 MET MET A . n 
A 1 223 MET 223 218 218 MET MET A . n 
A 1 224 LEU 224 219 219 LEU LEU A . n 
A 1 225 CYS 225 220 220 CYS CYS A . n 
A 1 226 GLY 226 221 221 GLY GLY A . n 
A 1 227 SER 227 222 222 SER SER A . n 
A 1 228 PRO 228 223 223 PRO PRO A . n 
A 1 229 GLU 229 224 224 GLU GLU A . n 
A 1 230 MET 230 225 225 MET MET A . n 
A 1 231 LEU 231 226 226 LEU LEU A . n 
A 1 232 ALA 232 227 227 ALA ALA A . n 
A 1 233 GLU 233 228 228 GLU GLU A . n 
A 1 234 THR 234 229 229 THR THR A . n 
A 1 235 LYS 235 230 230 LYS LYS A . n 
A 1 236 GLN 236 231 231 GLN GLN A . n 
A 1 237 ILE 237 232 232 ILE ILE A . n 
A 1 238 LEU 238 233 233 LEU LEU A . n 
A 1 239 GLU 239 234 234 GLU GLU A . n 
A 1 240 GLU 240 235 235 GLU GLU A . n 
A 1 241 ARG 241 236 236 ARG ARG A . n 
A 1 242 GLY 242 237 237 GLY GLY A . n 
A 1 243 PHE 243 238 238 PHE PHE A . n 
A 1 244 THR 244 239 239 THR THR A . n 
A 1 245 GLU 245 240 240 GLU GLU A . n 
A 1 246 GLY 246 241 241 GLY GLY A . n 
A 1 247 SER 247 242 242 SER SER A . n 
A 1 248 GLN 248 243 243 GLN GLN A . n 
A 1 249 SER 249 244 244 SER SER A . n 
A 1 250 GLU 250 245 245 GLU GLU A . n 
A 1 251 PRO 251 246 246 PRO PRO A . n 
A 1 252 GLY 252 247 247 GLY GLY A . n 
A 1 253 GLU 253 248 248 GLU GLU A . n 
A 1 254 PHE 254 249 249 PHE PHE A . n 
A 1 255 VAL 255 250 250 VAL VAL A . n 
A 1 256 ILE 256 251 251 ILE ILE A . n 
A 1 257 GLU 257 252 252 GLU GLU A . n 
A 1 258 LYS 258 253 253 LYS LYS A . n 
A 1 259 ALA 259 254 254 ALA ALA A . n 
A 1 260 PHE 260 255 255 PHE PHE A . n 
A 1 261 VAL 261 256 256 VAL VAL A . n 
A 1 262 GLU 262 257 257 GLU GLU A . n 
A 1 263 LYS 263 258 258 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 FAD 1  301 301 FAD FAD A . 
C 3 HOH 1  401 1   HOH HOH A . 
C 3 HOH 2  402 42  HOH HOH A . 
C 3 HOH 3  403 24  HOH HOH A . 
C 3 HOH 4  404 11  HOH HOH A . 
C 3 HOH 5  405 57  HOH HOH A . 
C 3 HOH 6  406 30  HOH HOH A . 
C 3 HOH 7  407 18  HOH HOH A . 
C 3 HOH 8  408 36  HOH HOH A . 
C 3 HOH 9  409 47  HOH HOH A . 
C 3 HOH 10 410 53  HOH HOH A . 
C 3 HOH 11 411 55  HOH HOH A . 
C 3 HOH 12 412 33  HOH HOH A . 
C 3 HOH 13 413 25  HOH HOH A . 
C 3 HOH 14 414 22  HOH HOH A . 
C 3 HOH 15 415 50  HOH HOH A . 
C 3 HOH 16 416 8   HOH HOH A . 
C 3 HOH 17 417 54  HOH HOH A . 
C 3 HOH 18 418 13  HOH HOH A . 
C 3 HOH 19 419 7   HOH HOH A . 
C 3 HOH 20 420 32  HOH HOH A . 
C 3 HOH 21 421 43  HOH HOH A . 
C 3 HOH 22 422 9   HOH HOH A . 
C 3 HOH 23 423 16  HOH HOH A . 
C 3 HOH 24 424 64  HOH HOH A . 
C 3 HOH 25 425 17  HOH HOH A . 
C 3 HOH 26 426 35  HOH HOH A . 
C 3 HOH 27 427 15  HOH HOH A . 
C 3 HOH 28 428 23  HOH HOH A . 
C 3 HOH 29 429 48  HOH HOH A . 
C 3 HOH 30 430 37  HOH HOH A . 
C 3 HOH 31 431 60  HOH HOH A . 
C 3 HOH 32 432 40  HOH HOH A . 
C 3 HOH 33 433 26  HOH HOH A . 
C 3 HOH 34 434 3   HOH HOH A . 
C 3 HOH 35 435 27  HOH HOH A . 
C 3 HOH 36 436 52  HOH HOH A . 
C 3 HOH 37 437 21  HOH HOH A . 
C 3 HOH 38 438 31  HOH HOH A . 
C 3 HOH 39 439 45  HOH HOH A . 
C 3 HOH 40 440 51  HOH HOH A . 
C 3 HOH 41 441 28  HOH HOH A . 
C 3 HOH 42 442 34  HOH HOH A . 
C 3 HOH 43 443 61  HOH HOH A . 
C 3 HOH 44 444 56  HOH HOH A . 
C 3 HOH 45 445 29  HOH HOH A . 
C 3 HOH 46 446 46  HOH HOH A . 
C 3 HOH 47 447 2   HOH HOH A . 
C 3 HOH 48 448 41  HOH HOH A . 
C 3 HOH 49 449 12  HOH HOH A . 
C 3 HOH 50 450 59  HOH HOH A . 
C 3 HOH 51 451 63  HOH HOH A . 
C 3 HOH 52 452 19  HOH HOH A . 
C 3 HOH 53 453 39  HOH HOH A . 
C 3 HOH 54 454 44  HOH HOH A . 
C 3 HOH 55 455 62  HOH HOH A . 
C 3 HOH 56 456 4   HOH HOH A . 
C 3 HOH 57 457 14  HOH HOH A . 
C 3 HOH 58 458 49  HOH HOH A . 
C 3 HOH 59 459 5   HOH HOH A . 
C 3 HOH 60 460 6   HOH HOH A . 
C 3 HOH 61 461 58  HOH HOH A . 
C 3 HOH 62 462 20  HOH HOH A . 
C 3 HOH 63 463 38  HOH HOH A . 
C 3 HOH 64 464 10  HOH HOH A . 
# 
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   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GXB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.900 
_cell.length_a_esd                 ? 
_cell.length_b                     39.900 
_cell.length_b_esd                 ? 
_cell.length_c                     168.500 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GXB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GXB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    
;25% PEG 4.000
0.1M MES pH 6.5
0.2M MgCl2
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         AGIPD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-03 
_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   1.319 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'EUROPEAN XFEL BEAMLINE SPB/SFX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.319 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   SPB/SFX 
_diffrn_source.pdbx_synchrotron_site       'European XFEL' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GXB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.9 
_reflns.d_resolution_low                               23 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     20670 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                48 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.8157 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.9 
_reflns_shell.d_res_low                                     2.0 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2013 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.2460 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GXB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.90 
_refine.ls_d_res_low                             22.97 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     20610 
_refine.ls_number_reflns_R_free                  1039 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2243 
_refine.ls_R_factor_R_free                       0.2532 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2170 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          3.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.21 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        22.97 
_refine_hist.number_atoms_solvent             64 
_refine_hist.number_atoms_total               2187 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2123 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.704 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.929 ? 282 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045 ? 320 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 373 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.90 2.00  . . 162 2747 94.00 . . . . 0.3679 . . . . . . . . . . . 0.4406 
'X-RAY DIFFRACTION' 2.00 2.13  . . 155 2788 95.00 . . . . 0.2915 . . . . . . . . . . . 0.3051 
'X-RAY DIFFRACTION' 2.13 2.29  . . 131 2814 96.00 . . . . 0.2613 . . . . . . . . . . . 0.2977 
'X-RAY DIFFRACTION' 2.29 2.52  . . 169 2763 94.00 . . . . 0.2490 . . . . . . . . . . . 0.2822 
'X-RAY DIFFRACTION' 2.52 2.88  . . 135 2830 95.00 . . . . 0.2348 . . . . . . . . . . . 0.2625 
'X-RAY DIFFRACTION' 2.88 3.63  . . 129 2824 96.00 . . . . 0.2115 . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 3.63 22.97 . . 158 2805 95.00 . . . . 0.1713 . . . . . . . . . . . 0.2005 
# 
_struct.entry_id                     9GXB 
_struct.title                        
'Room temperature structure of FAD-containing ferrodoxin-NADP reductase from Brucella ovis at EuXFEL' 
_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        9GXB 
_struct_keywords.text            
;ferredoxin-NADP+ reductase, room temperature X-ray diffraction, electron transfer, oxidative damage protection, serial femtosecond crystallography, XFEL, microcrystals., OXIDOREDUCTASE
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0H3ASL8_BRUO2 
_struct_ref.pdbx_db_accession          A0A0H3ASL8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSSNFNQETVTDIHHWTDTLFSFRTTRDPGFRFQSGQFIMMGLEVNGKPLTRAYSIASSLYEDGLEFFSIKVPNGPLTSK
LQHLKKGDQIIVSKKPVGTLLYDNLKPGKHLWLLSTGTGLAPFLSIIRDLEVYERFEKVILVHGVRQVAELAYTDFISNE
LPQDEFLGEMVKNQLIYYPTVTREPYKTRGRLTDLIRSGQLFKDVGLPEFNHEDDRMMLCGSPEMLAETKQILEERGFTE
GSQSEPGEFVIEKAFVEK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GXB 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 6 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 263 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0H3ASL8 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  258 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       258 
# 
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 9GXB GLY A 1 ? UNP A0A0H3ASL8 ? ? 'expression tag' -4 1 
1 9GXB PRO A 2 ? UNP A0A0H3ASL8 ? ? 'expression tag' -3 2 
1 9GXB GLY A 3 ? UNP A0A0H3ASL8 ? ? 'expression tag' -2 3 
1 9GXB SER A 4 ? UNP A0A0H3ASL8 ? ? 'expression tag' -1 4 
1 9GXB HIS A 5 ? UNP A0A0H3ASL8 ? ? 'expression tag' 0  5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1270  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  11950 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 82  ? GLN A 87  ? LEU A 77  GLN A 82  1 ? 6  
HELX_P HELX_P2  AA2 LEU A 106 ? LEU A 110 ? LEU A 101 LEU A 105 5 ? 5  
HELX_P HELX_P3  AA3 LEU A 125 ? ILE A 132 ? LEU A 120 ILE A 127 1 ? 8  
HELX_P HELX_P4  AA4 ASP A 134 ? PHE A 141 ? ASP A 129 PHE A 136 1 ? 8  
HELX_P HELX_P5  AA5 GLN A 152 ? LEU A 156 ? GLN A 147 LEU A 151 5 ? 5  
HELX_P HELX_P6  AA6 TYR A 158 ? ASN A 164 ? TYR A 153 ASN A 159 1 ? 7  
HELX_P HELX_P7  AA7 GLU A 165 ? ASP A 169 ? GLU A 160 ASP A 164 5 ? 5  
HELX_P HELX_P8  AA8 LEU A 172 ? GLN A 179 ? LEU A 167 GLN A 174 1 ? 8  
HELX_P HELX_P9  AA9 ARG A 196 ? SER A 203 ? ARG A 191 SER A 198 1 ? 8  
HELX_P HELX_P10 AB1 GLY A 204 ? GLY A 211 ? GLY A 199 GLY A 206 1 ? 8  
HELX_P HELX_P11 AB2 SER A 227 ? ARG A 241 ? SER A 222 ARG A 236 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 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 LYS A 53  ? SER A 60  ? LYS A 48  SER A 55  
AA1 2 PHE A 43  ? VAL A 50  ? PHE A 38  VAL A 45  
AA1 3 GLN A 94  ? SER A 98  ? GLN A 89  SER A 93  
AA1 4 PHE A 10  ? HIS A 20  ? PHE A 5   HIS A 15  
AA1 5 LEU A 25  ? THR A 30  ? LEU A 20  THR A 25  
AA1 6 LEU A 70  ? ILE A 75  ? LEU A 65  ILE A 70  
AA2 1 LEU A 180 ? VAL A 186 ? LEU A 175 VAL A 181 
AA2 2 LYS A 143 ? VAL A 150 ? LYS A 138 VAL A 145 
AA2 3 HIS A 115 ? THR A 121 ? HIS A 110 THR A 116 
AA2 4 ASP A 220 ? GLY A 226 ? ASP A 215 GLY A 221 
AA2 5 PHE A 254 ? LYS A 258 ? PHE A 249 LYS A 253 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 55  ? O LEU A 50  N LEU A 48  ? N LEU A 43  
AA1 2 3 N MET A 45  ? N MET A 40  O SER A 98  ? O SER A 93  
AA1 3 4 O VAL A 97  ? O VAL A 92  N ASN A 11  ? N ASN A 6   
AA1 4 5 N HIS A 19  ? N HIS A 14  O SER A 27  ? O SER A 22  
AA1 5 6 N THR A 30  ? N THR A 25  O LEU A 70  ? O LEU A 65  
AA2 1 2 O ILE A 181 ? O ILE A 176 N LEU A 146 ? N LEU A 141 
AA2 2 3 O ILE A 145 ? O ILE A 140 N LEU A 118 ? N LEU A 113 
AA2 3 4 N TRP A 117 ? N TRP A 112 O MET A 223 ? O MET A 218 
AA2 4 5 N LEU A 224 ? N LEU A 219 O VAL A 255 ? O VAL A 250 
# 
_pdbx_entry_details.entry_id                   9GXB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 252 ? ? O A HOH 401 ? ? 2.07 
2 1 O   A HOH 440 ? ? O A HOH 450 ? ? 2.13 
3 1 O   A SER 3   ? ? O A HOH 402 ? ? 2.18 
# 
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 SER A 3  ? ? 71.70   -7.56   
2 1 THR A 17 ? ? -124.17 -163.88 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       464 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.52 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -4 ? A GLY 1 
2 1 Y 1 A PRO -3 ? A PRO 2 
3 1 Y 1 A GLY -2 ? A GLY 3 
4 1 Y 1 A SER -1 ? A SER 4 
5 1 Y 1 A HIS 0  ? A HIS 5 
6 1 Y 1 A MET 1  ? A MET 6 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
VAL N      N N N 458 
VAL CA     C N S 459 
VAL C      C N N 460 
VAL O      O N N 461 
VAL CB     C N N 462 
VAL CG1    C N N 463 
VAL CG2    C N N 464 
VAL OXT    O N N 465 
VAL H      H N N 466 
VAL H2     H N N 467 
VAL HA     H N N 468 
VAL HB     H N N 469 
VAL HG11   H N N 470 
VAL HG12   H N N 471 
VAL HG13   H N N 472 
VAL HG21   H N N 473 
VAL HG22   H N N 474 
VAL HG23   H N N 475 
VAL HXT    H N N 476 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Economy and Competitiveness (MINECO)' Spain PID2022-136369NB-I00           1 
'Other government'                                 ?     LMP13_21                       2 
'Other government'                                 ?     'Biologia Estructural_E35_23R' 3 
'Comunidad de Madrid'                              Spain 2019-T1/BMD-15552              4 
'Agencia Estatal de Investigacion (AEI)'           Spain CNS2022/135713                 5 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6RR3 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   DFFN 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    9GXB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.025063 
_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]   0.025063 
_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]   0.005935 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER A 1 7   ? -2.264 -6.273  13.789  1.00 34.80 ? 2   SER A N     1 
ATOM   2    C CA    . SER A 1 7   ? -0.911 -6.721  13.497  1.00 48.88 ? 2   SER A CA    1 
ATOM   3    C C     . SER A 1 7   ? -0.913 -8.001  12.662  1.00 49.97 ? 2   SER A C     1 
ATOM   4    O O     . SER A 1 7   ? -1.908 -8.310  12.001  1.00 49.88 ? 2   SER A O     1 
ATOM   5    C CB    . SER A 1 7   ? -0.128 -6.932  14.797  1.00 48.00 ? 2   SER A CB    1 
ATOM   6    O OG    . SER A 1 7   ? 0.086  -5.698  15.459  1.00 41.06 ? 2   SER A OG    1 
ATOM   7    N N     . SER A 1 8   ? 0.215  -8.719  12.695  1.00 46.01 ? 3   SER A N     1 
ATOM   8    C CA    . SER A 1 8   ? 0.444  -9.952  11.942  1.00 46.95 ? 3   SER A CA    1 
ATOM   9    C C     . SER A 1 8   ? 0.612  -9.689  10.448  1.00 47.66 ? 3   SER A C     1 
ATOM   10   O O     . SER A 1 8   ? 0.951  -10.606 9.694   1.00 51.13 ? 3   SER A O     1 
ATOM   11   C CB    . SER A 1 8   ? -0.675 -10.973 12.183  1.00 44.27 ? 3   SER A CB    1 
ATOM   12   O OG    . SER A 1 8   ? -0.806 -11.261 13.562  1.00 42.73 ? 3   SER A OG    1 
ATOM   13   N N     . ASN A 1 9   ? 0.382  -8.454  10.007  1.00 50.72 ? 4   ASN A N     1 
ATOM   14   C CA    . ASN A 1 9   ? 0.911  -7.970  8.737   1.00 44.26 ? 4   ASN A CA    1 
ATOM   15   C C     . ASN A 1 9   ? 2.260  -7.291  8.909   1.00 36.06 ? 4   ASN A C     1 
ATOM   16   O O     . ASN A 1 9   ? 2.758  -6.667  7.968   1.00 33.46 ? 4   ASN A O     1 
ATOM   17   C CB    . ASN A 1 9   ? -0.069 -7.001  8.065   1.00 38.34 ? 4   ASN A CB    1 
ATOM   18   C CG    . ASN A 1 9   ? -1.464 -7.563  7.956   1.00 40.83 ? 4   ASN A CG    1 
ATOM   19   O OD1   . ASN A 1 9   ? -2.046 -8.011  8.943   1.00 57.40 ? 4   ASN A OD1   1 
ATOM   20   N ND2   . ASN A 1 9   ? -2.015 -7.543  6.747   1.00 32.64 ? 4   ASN A ND2   1 
ATOM   21   N N     . PHE A 1 10  ? 2.858  -7.406  10.091  1.00 39.86 ? 5   PHE A N     1 
ATOM   22   C CA    . PHE A 1 10  ? 4.109  -6.747  10.415  1.00 35.75 ? 5   PHE A CA    1 
ATOM   23   C C     . PHE A 1 10  ? 5.084  -7.770  10.971  1.00 33.76 ? 5   PHE A C     1 
ATOM   24   O O     . PHE A 1 10  ? 4.705  -8.877  11.362  1.00 38.86 ? 5   PHE A O     1 
ATOM   25   C CB    . PHE A 1 10  ? 3.901  -5.625  11.442  1.00 32.40 ? 5   PHE A CB    1 
ATOM   26   C CG    . PHE A 1 10  ? 3.005  -4.530  10.962  1.00 34.74 ? 5   PHE A CG    1 
ATOM   27   C CD1   . PHE A 1 10  ? 3.518  -3.457  10.252  1.00 33.82 ? 5   PHE A CD1   1 
ATOM   28   C CD2   . PHE A 1 10  ? 1.643  -4.578  11.214  1.00 33.51 ? 5   PHE A CD2   1 
ATOM   29   C CE1   . PHE A 1 10  ? 2.690  -2.449  9.804   1.00 38.05 ? 5   PHE A CE1   1 
ATOM   30   C CE2   . PHE A 1 10  ? 0.809  -3.574  10.771  1.00 36.82 ? 5   PHE A CE2   1 
ATOM   31   C CZ    . PHE A 1 10  ? 1.333  -2.506  10.064  1.00 39.72 ? 5   PHE A CZ    1 
ATOM   32   N N     . ASN A 1 11  ? 6.351  -7.382  10.997  1.00 32.35 ? 6   ASN A N     1 
ATOM   33   C CA    . ASN A 1 11  ? 7.382  -8.119  11.703  1.00 28.36 ? 6   ASN A CA    1 
ATOM   34   C C     . ASN A 1 11  ? 7.818  -7.301  12.907  1.00 30.32 ? 6   ASN A C     1 
ATOM   35   O O     . ASN A 1 11  ? 7.962  -6.077  12.818  1.00 26.70 ? 6   ASN A O     1 
ATOM   36   C CB    . ASN A 1 11  ? 8.583  -8.406  10.802  1.00 28.21 ? 6   ASN A CB    1 
ATOM   37   C CG    . ASN A 1 11  ? 8.271  -9.417  9.722   1.00 29.44 ? 6   ASN A CG    1 
ATOM   38   O OD1   . ASN A 1 11  ? 7.552  -10.389 9.952   1.00 33.60 ? 6   ASN A OD1   1 
ATOM   39   N ND2   . ASN A 1 11  ? 8.809  -9.191  8.530   1.00 28.37 ? 6   ASN A ND2   1 
ATOM   40   N N     . GLN A 1 12  ? 8.005  -7.971  14.039  1.00 32.39 ? 7   GLN A N     1 
ATOM   41   C CA    . GLN A 1 12  ? 8.557  -7.324  15.218  1.00 32.35 ? 7   GLN A CA    1 
ATOM   42   C C     . GLN A 1 12  ? 10.076 -7.416  15.153  1.00 25.49 ? 7   GLN A C     1 
ATOM   43   O O     . GLN A 1 12  ? 10.633 -8.514  15.050  1.00 24.81 ? 7   GLN A O     1 
ATOM   44   C CB    . GLN A 1 12  ? 8.017  -7.947  16.505  1.00 34.15 ? 7   GLN A CB    1 
ATOM   45   C CG    . GLN A 1 12  ? 6.766  -7.252  17.020  1.00 35.09 ? 7   GLN A CG    1 
ATOM   46   C CD    . GLN A 1 12  ? 6.712  -7.181  18.531  1.00 36.19 ? 7   GLN A CD    1 
ATOM   47   O OE1   . GLN A 1 12  ? 7.226  -8.056  19.228  1.00 44.47 ? 7   GLN A OE1   1 
ATOM   48   N NE2   . GLN A 1 12  ? 6.099  -6.124  19.048  1.00 32.23 ? 7   GLN A NE2   1 
ATOM   49   N N     . GLU A 1 13  ? 10.733 -6.257  15.180  1.00 30.36 ? 8   GLU A N     1 
ATOM   50   C CA    . GLU A 1 13  ? 12.182 -6.149  15.170  1.00 25.52 ? 8   GLU A CA    1 
ATOM   51   C C     . GLU A 1 13  ? 12.635 -5.343  16.379  1.00 23.12 ? 8   GLU A C     1 
ATOM   52   O O     . GLU A 1 13  ? 11.945 -4.422  16.829  1.00 23.06 ? 8   GLU A O     1 
ATOM   53   C CB    . GLU A 1 13  ? 12.684 -5.501  13.872  1.00 24.35 ? 8   GLU A CB    1 
ATOM   54   C CG    . GLU A 1 13  ? 12.177 -6.178  12.598  1.00 24.52 ? 8   GLU A CG    1 
ATOM   55   C CD    . GLU A 1 13  ? 12.669 -7.615  12.407  1.00 18.31 ? 8   GLU A CD    1 
ATOM   56   O OE1   . GLU A 1 13  ? 13.405 -8.151  13.260  1.00 18.37 ? 8   GLU A OE1   1 
ATOM   57   O OE2   . GLU A 1 13  ? 12.305 -8.219  11.381  1.00 22.58 ? 8   GLU A OE2   1 
ATOM   58   N N     . THR A 1 14  ? 13.800 -5.707  16.906  1.00 30.39 ? 9   THR A N     1 
ATOM   59   C CA    . THR A 1 14  ? 14.354 -5.092  18.104  1.00 30.19 ? 9   THR A CA    1 
ATOM   60   C C     . THR A 1 14  ? 15.381 -4.040  17.713  1.00 24.29 ? 9   THR A C     1 
ATOM   61   O O     . THR A 1 14  ? 16.234 -4.290  16.856  1.00 22.44 ? 9   THR A O     1 
ATOM   62   C CB    . THR A 1 14  ? 15.001 -6.144  19.004  1.00 22.80 ? 9   THR A CB    1 
ATOM   63   O OG1   . THR A 1 14  ? 14.078 -7.216  19.220  1.00 30.82 ? 9   THR A OG1   1 
ATOM   64   C CG2   . THR A 1 14  ? 15.373 -5.540  20.346  1.00 25.40 ? 9   THR A CG2   1 
ATOM   65   N N     . VAL A 1 15  ? 15.294 -2.868  18.341  1.00 26.28 ? 10  VAL A N     1 
ATOM   66   C CA    . VAL A 1 15  ? 16.293 -1.831  18.119  1.00 29.98 ? 10  VAL A CA    1 
ATOM   67   C C     . VAL A 1 15  ? 17.611 -2.272  18.742  1.00 31.42 ? 10  VAL A C     1 
ATOM   68   O O     . VAL A 1 15  ? 17.680 -2.587  19.937  1.00 28.88 ? 10  VAL A O     1 
ATOM   69   C CB    . VAL A 1 15  ? 15.820 -0.488  18.694  1.00 31.98 ? 10  VAL A CB    1 
ATOM   70   C CG1   . VAL A 1 15  ? 16.727 0.638   18.226  1.00 29.41 ? 10  VAL A CG1   1 
ATOM   71   C CG2   . VAL A 1 15  ? 14.386 -0.207  18.279  1.00 32.91 ? 10  VAL A CG2   1 
ATOM   72   N N     . THR A 1 16  ? 18.663 -2.312  17.924  1.00 34.40 ? 11  THR A N     1 
ATOM   73   C CA    . THR A 1 16  ? 19.984 -2.753  18.354  1.00 30.23 ? 11  THR A CA    1 
ATOM   74   C C     . THR A 1 16  ? 20.963 -1.612  18.566  1.00 27.06 ? 11  THR A C     1 
ATOM   75   O O     . THR A 1 16  ? 21.808 -1.696  19.461  1.00 25.79 ? 11  THR A O     1 
ATOM   76   C CB    . THR A 1 16  ? 20.584 -3.720  17.323  1.00 35.24 ? 11  THR A CB    1 
ATOM   77   O OG1   . THR A 1 16  ? 20.389 -3.193  16.005  1.00 28.17 ? 11  THR A OG1   1 
ATOM   78   C CG2   . THR A 1 16  ? 19.916 -5.087  17.416  1.00 30.51 ? 11  THR A CG2   1 
ATOM   79   N N     . ASP A 1 17  ? 20.870 -0.558  17.759  1.00 26.60 ? 12  ASP A N     1 
ATOM   80   C CA    . ASP A 1 17  ? 21.752 0.591   17.864  1.00 23.30 ? 12  ASP A CA    1 
ATOM   81   C C     . ASP A 1 17  ? 20.958 1.851   17.565  1.00 25.48 ? 12  ASP A C     1 
ATOM   82   O O     . ASP A 1 17  ? 19.994 1.826   16.795  1.00 20.02 ? 12  ASP A O     1 
ATOM   83   C CB    . ASP A 1 17  ? 22.950 0.476   16.908  1.00 29.77 ? 12  ASP A CB    1 
ATOM   84   C CG    . ASP A 1 17  ? 24.187 1.174   17.439  1.00 29.70 ? 12  ASP A CG    1 
ATOM   85   O OD1   . ASP A 1 17  ? 24.065 2.320   17.918  1.00 35.90 ? 12  ASP A OD1   1 
ATOM   86   O OD2   . ASP A 1 17  ? 25.283 0.579   17.379  1.00 33.63 ? 12  ASP A OD2   1 
ATOM   87   N N     . ILE A 1 18  ? 21.358 2.946   18.212  1.00 29.56 ? 13  ILE A N     1 
ATOM   88   C CA    . ILE A 1 18  ? 20.791 4.271   17.988  1.00 21.83 ? 13  ILE A CA    1 
ATOM   89   C C     . ILE A 1 18  ? 21.938 5.269   17.941  1.00 22.35 ? 13  ILE A C     1 
ATOM   90   O O     . ILE A 1 18  ? 22.851 5.216   18.771  1.00 19.71 ? 13  ILE A O     1 
ATOM   91   C CB    . ILE A 1 18  ? 19.779 4.685   19.077  1.00 24.37 ? 13  ILE A CB    1 
ATOM   92   C CG1   . ILE A 1 18  ? 18.778 3.563   19.372  1.00 31.10 ? 13  ILE A CG1   1 
ATOM   93   C CG2   . ILE A 1 18  ? 19.046 5.957   18.673  1.00 24.12 ? 13  ILE A CG2   1 
ATOM   94   C CD1   . ILE A 1 18  ? 19.127 2.745   20.595  1.00 28.42 ? 13  ILE A CD1   1 
ATOM   95   N N     . HIS A 1 19  ? 21.900 6.168   16.962  1.00 24.04 ? 14  HIS A N     1 
ATOM   96   C CA    . HIS A 1 19  ? 22.847 7.273   16.895  1.00 25.93 ? 14  HIS A CA    1 
ATOM   97   C C     . HIS A 1 19  ? 22.103 8.514   16.434  1.00 20.45 ? 14  HIS A C     1 
ATOM   98   O O     . HIS A 1 19  ? 21.613 8.559   15.303  1.00 21.83 ? 14  HIS A O     1 
ATOM   99   C CB    . HIS A 1 19  ? 24.017 6.966   15.956  1.00 20.73 ? 14  HIS A CB    1 
ATOM   100  C CG    . HIS A 1 19  ? 24.932 8.131   15.738  1.00 24.51 ? 14  HIS A CG    1 
ATOM   101  N ND1   . HIS A 1 19  ? 26.169 8.225   16.339  1.00 35.70 ? 14  HIS A ND1   1 
ATOM   102  C CD2   . HIS A 1 19  ? 24.795 9.245   14.982  1.00 22.48 ? 14  HIS A CD2   1 
ATOM   103  C CE1   . HIS A 1 19  ? 26.752 9.350   15.965  1.00 28.93 ? 14  HIS A CE1   1 
ATOM   104  N NE2   . HIS A 1 19  ? 25.939 9.987   15.142  1.00 23.11 ? 14  HIS A NE2   1 
ATOM   105  N N     . HIS A 1 20  ? 22.020 9.511   17.307  1.00 22.17 ? 15  HIS A N     1 
ATOM   106  C CA    . HIS A 1 20  ? 21.439 10.795  16.952  1.00 17.06 ? 15  HIS A CA    1 
ATOM   107  C C     . HIS A 1 20  ? 22.513 11.658  16.310  1.00 16.97 ? 15  HIS A C     1 
ATOM   108  O O     . HIS A 1 20  ? 23.656 11.688  16.770  1.00 17.49 ? 15  HIS A O     1 
ATOM   109  C CB    . HIS A 1 20  ? 20.867 11.495  18.184  1.00 16.88 ? 15  HIS A CB    1 
ATOM   110  C CG    . HIS A 1 20  ? 19.799 10.712  18.881  1.00 16.46 ? 15  HIS A CG    1 
ATOM   111  N ND1   . HIS A 1 20  ? 18.455 10.929  18.672  1.00 18.36 ? 15  HIS A ND1   1 
ATOM   112  C CD2   . HIS A 1 20  ? 19.881 9.722   19.802  1.00 19.25 ? 15  HIS A CD2   1 
ATOM   113  C CE1   . HIS A 1 20  ? 17.755 10.097  19.422  1.00 18.53 ? 15  HIS A CE1   1 
ATOM   114  N NE2   . HIS A 1 20  ? 18.597 9.355   20.119  1.00 18.60 ? 15  HIS A NE2   1 
ATOM   115  N N     . TRP A 1 21  ? 22.144 12.342  15.229  1.00 18.83 ? 16  TRP A N     1 
ATOM   116  C CA    . TRP A 1 21  ? 23.055 13.256  14.551  1.00 20.35 ? 16  TRP A CA    1 
ATOM   117  C C     . TRP A 1 21  ? 22.869 14.675  15.075  1.00 17.79 ? 16  TRP A C     1 
ATOM   118  O O     . TRP A 1 21  ? 23.804 15.280  15.609  1.00 20.20 ? 16  TRP A O     1 
ATOM   119  C CB    . TRP A 1 21  ? 22.823 13.193  13.035  1.00 19.30 ? 16  TRP A CB    1 
ATOM   120  C CG    . TRP A 1 21  ? 23.028 11.825  12.461  1.00 18.18 ? 16  TRP A CG    1 
ATOM   121  C CD1   . TRP A 1 21  ? 22.059 10.924  12.134  1.00 16.32 ? 16  TRP A CD1   1 
ATOM   122  C CD2   . TRP A 1 21  ? 24.280 11.206  12.132  1.00 18.32 ? 16  TRP A CD2   1 
ATOM   123  N NE1   . TRP A 1 21  ? 22.628 9.777   11.637  1.00 19.66 ? 16  TRP A NE1   1 
ATOM   124  C CE2   . TRP A 1 21  ? 23.989 9.925   11.621  1.00 17.59 ? 16  TRP A CE2   1 
ATOM   125  C CE3   . TRP A 1 21  ? 25.617 11.609  12.223  1.00 18.43 ? 16  TRP A CE3   1 
ATOM   126  C CZ2   . TRP A 1 21  ? 24.984 9.044   11.203  1.00 16.16 ? 16  TRP A CZ2   1 
ATOM   127  C CZ3   . TRP A 1 21  ? 26.604 10.732  11.808  1.00 17.46 ? 16  TRP A CZ3   1 
ATOM   128  C CH2   . TRP A 1 21  ? 26.282 9.464   11.304  1.00 17.78 ? 16  TRP A CH2   1 
ATOM   129  N N     . THR A 1 22  ? 21.659 15.206  14.933  1.00 18.01 ? 17  THR A N     1 
ATOM   130  C CA    . THR A 1 22  ? 21.312 16.536  15.410  1.00 19.40 ? 17  THR A CA    1 
ATOM   131  C C     . THR A 1 22  ? 20.115 16.433  16.345  1.00 18.72 ? 17  THR A C     1 
ATOM   132  O O     . THR A 1 22  ? 19.787 15.340  16.817  1.00 19.35 ? 17  THR A O     1 
ATOM   133  C CB    . THR A 1 22  ? 21.002 17.461  14.228  1.00 20.68 ? 17  THR A CB    1 
ATOM   134  O OG1   . THR A 1 22  ? 19.846 16.973  13.531  1.00 21.76 ? 17  THR A OG1   1 
ATOM   135  C CG2   . THR A 1 22  ? 22.183 17.527  13.263  1.00 20.19 ? 17  THR A CG2   1 
ATOM   136  N N     . ASP A 1 23  ? 19.452 17.552  16.620  1.00 18.21 ? 18  ASP A N     1 
ATOM   137  C CA    . ASP A 1 23  ? 18.187 17.516  17.337  1.00 18.09 ? 18  ASP A CA    1 
ATOM   138  C C     . ASP A 1 23  ? 17.001 17.339  16.397  1.00 16.28 ? 18  ASP A C     1 
ATOM   139  O O     . ASP A 1 23  ? 15.853 17.431  16.843  1.00 15.31 ? 18  ASP A O     1 
ATOM   140  C CB    . ASP A 1 23  ? 18.016 18.774  18.201  1.00 15.75 ? 18  ASP A CB    1 
ATOM   141  C CG    . ASP A 1 23  ? 18.059 20.060  17.396  1.00 19.77 ? 18  ASP A CG    1 
ATOM   142  O OD1   . ASP A 1 23  ? 18.336 20.010  16.182  1.00 23.30 ? 18  ASP A OD1   1 
ATOM   143  O OD2   . ASP A 1 23  ? 17.822 21.133  17.991  1.00 24.80 ? 18  ASP A OD2   1 
ATOM   144  N N     . THR A 1 24  ? 17.261 17.070  15.110  1.00 16.52 ? 19  THR A N     1 
ATOM   145  C CA    . THR A 1 24  ? 16.220 16.798  14.128  1.00 19.62 ? 19  THR A CA    1 
ATOM   146  C C     . THR A 1 24  ? 16.481 15.553  13.287  1.00 19.62 ? 19  THR A C     1 
ATOM   147  O O     . THR A 1 24  ? 15.614 15.176  12.489  1.00 19.67 ? 19  THR A O     1 
ATOM   148  C CB    . THR A 1 24  ? 16.041 17.994  13.174  1.00 21.09 ? 19  THR A CB    1 
ATOM   149  O OG1   . THR A 1 24  ? 17.286 18.281  12.519  1.00 22.78 ? 19  THR A OG1   1 
ATOM   150  C CG2   . THR A 1 24  ? 15.546 19.227  13.929  1.00 15.09 ? 19  THR A CG2   1 
ATOM   151  N N     . LEU A 1 25  ? 17.639 14.911  13.432  1.00 19.21 ? 20  LEU A N     1 
ATOM   152  C CA    . LEU A 1 25  ? 18.029 13.808  12.563  1.00 18.46 ? 20  LEU A CA    1 
ATOM   153  C C     . LEU A 1 25  ? 18.725 12.741  13.390  1.00 18.49 ? 20  LEU A C     1 
ATOM   154  O O     . LEU A 1 25  ? 19.757 13.016  14.007  1.00 21.25 ? 20  LEU A O     1 
ATOM   155  C CB    . LEU A 1 25  ? 18.958 14.296  11.442  1.00 18.72 ? 20  LEU A CB    1 
ATOM   156  C CG    . LEU A 1 25  ? 18.368 15.210  10.369  1.00 16.35 ? 20  LEU A CG    1 
ATOM   157  C CD1   . LEU A 1 25  ? 19.467 15.792  9.490   1.00 16.94 ? 20  LEU A CD1   1 
ATOM   158  C CD2   . LEU A 1 25  ? 17.368 14.443  9.533   1.00 15.16 ? 20  LEU A CD2   1 
ATOM   159  N N     . PHE A 1 26  ? 18.176 11.526  13.394  1.00 19.65 ? 21  PHE A N     1 
ATOM   160  C CA    . PHE A 1 26  ? 18.836 10.400  14.040  1.00 19.22 ? 21  PHE A CA    1 
ATOM   161  C C     . PHE A 1 26  ? 18.725 9.162   13.155  1.00 18.31 ? 21  PHE A C     1 
ATOM   162  O O     . PHE A 1 26  ? 18.029 9.152   12.136  1.00 18.06 ? 21  PHE A O     1 
ATOM   163  C CB    . PHE A 1 26  ? 18.281 10.157  15.460  1.00 18.14 ? 21  PHE A CB    1 
ATOM   164  C CG    . PHE A 1 26  ? 17.001 9.361   15.513  1.00 17.43 ? 21  PHE A CG    1 
ATOM   165  C CD1   . PHE A 1 26  ? 15.801 9.910   15.091  1.00 17.40 ? 21  PHE A CD1   1 
ATOM   166  C CD2   . PHE A 1 26  ? 16.994 8.079   16.040  1.00 14.66 ? 21  PHE A CD2   1 
ATOM   167  C CE1   . PHE A 1 26  ? 14.628 9.183   15.160  1.00 19.61 ? 21  PHE A CE1   1 
ATOM   168  C CE2   . PHE A 1 26  ? 15.825 7.347   16.113  1.00 15.63 ? 21  PHE A CE2   1 
ATOM   169  C CZ    . PHE A 1 26  ? 14.642 7.896   15.673  1.00 19.51 ? 21  PHE A CZ    1 
ATOM   170  N N     . SER A 1 27  ? 19.457 8.122   13.548  1.00 20.68 ? 22  SER A N     1 
ATOM   171  C CA    . SER A 1 27  ? 19.503 6.857   12.833  1.00 18.21 ? 22  SER A CA    1 
ATOM   172  C C     . SER A 1 27  ? 19.500 5.717   13.841  1.00 20.92 ? 22  SER A C     1 
ATOM   173  O O     . SER A 1 27  ? 20.198 5.773   14.858  1.00 19.03 ? 22  SER A O     1 
ATOM   174  C CB    . SER A 1 27  ? 20.749 6.755   11.939  1.00 14.90 ? 22  SER A CB    1 
ATOM   175  O OG    . SER A 1 27  ? 20.775 7.778   10.963  1.00 14.88 ? 22  SER A OG    1 
ATOM   176  N N     . PHE A 1 28  ? 18.715 4.683   13.556  1.00 22.01 ? 23  PHE A N     1 
ATOM   177  C CA    . PHE A 1 28  ? 18.674 3.510   14.413  1.00 19.49 ? 23  PHE A CA    1 
ATOM   178  C C     . PHE A 1 28  ? 18.645 2.258   13.552  1.00 19.94 ? 23  PHE A C     1 
ATOM   179  O O     . PHE A 1 28  ? 18.013 2.229   12.492  1.00 19.37 ? 23  PHE A O     1 
ATOM   180  C CB    . PHE A 1 28  ? 17.470 3.554   15.376  1.00 17.18 ? 23  PHE A CB    1 
ATOM   181  C CG    . PHE A 1 28  ? 16.138 3.382   14.705  1.00 21.71 ? 23  PHE A CG    1 
ATOM   182  C CD1   . PHE A 1 28  ? 15.496 4.468   14.124  1.00 19.54 ? 23  PHE A CD1   1 
ATOM   183  C CD2   . PHE A 1 28  ? 15.509 2.144   14.685  1.00 25.39 ? 23  PHE A CD2   1 
ATOM   184  C CE1   . PHE A 1 28  ? 14.268 4.317   13.513  1.00 19.92 ? 23  PHE A CE1   1 
ATOM   185  C CE2   . PHE A 1 28  ? 14.280 1.986   14.076  1.00 21.01 ? 23  PHE A CE2   1 
ATOM   186  C CZ    . PHE A 1 28  ? 13.659 3.075   13.491  1.00 24.47 ? 23  PHE A CZ    1 
ATOM   187  N N     . ARG A 1 29  ? 19.358 1.236   14.010  1.00 25.50 ? 24  ARG A N     1 
ATOM   188  C CA    . ARG A 1 29  ? 19.390 -0.069  13.375  1.00 19.63 ? 24  ARG A CA    1 
ATOM   189  C C     . ARG A 1 29  ? 18.560 -1.060  14.181  1.00 24.93 ? 24  ARG A C     1 
ATOM   190  O O     . ARG A 1 29  ? 18.407 -0.928  15.400  1.00 24.20 ? 24  ARG A O     1 
ATOM   191  C CB    . ARG A 1 29  ? 20.831 -0.564  13.225  1.00 18.45 ? 24  ARG A CB    1 
ATOM   192  C CG    . ARG A 1 29  ? 21.630 0.218   12.195  1.00 17.92 ? 24  ARG A CG    1 
ATOM   193  C CD    . ARG A 1 29  ? 23.119 0.241   12.497  1.00 21.14 ? 24  ARG A CD    1 
ATOM   194  N NE    . ARG A 1 29  ? 23.814 -0.951  12.029  1.00 27.92 ? 24  ARG A NE    1 
ATOM   195  C CZ    . ARG A 1 29  ? 25.067 -1.252  12.342  1.00 24.98 ? 24  ARG A CZ    1 
ATOM   196  N NH1   . ARG A 1 29  ? 25.809 -0.439  13.078  1.00 22.84 ? 24  ARG A NH1   1 
ATOM   197  N NH2   . ARG A 1 29  ? 25.592 -2.391  11.899  1.00 23.60 ? 24  ARG A NH2   1 
ATOM   198  N N     . THR A 1 30  ? 17.996 -2.041  13.478  1.00 27.11 ? 25  THR A N     1 
ATOM   199  C CA    . THR A 1 30  ? 17.188 -3.086  14.087  1.00 23.37 ? 25  THR A CA    1 
ATOM   200  C C     . THR A 1 30  ? 17.595 -4.441  13.524  1.00 21.47 ? 25  THR A C     1 
ATOM   201  O O     . THR A 1 30  ? 18.438 -4.550  12.631  1.00 18.47 ? 25  THR A O     1 
ATOM   202  C CB    . THR A 1 30  ? 15.680 -2.858  13.861  1.00 20.64 ? 25  THR A CB    1 
ATOM   203  O OG1   . THR A 1 30  ? 15.350 -3.112  12.487  1.00 23.12 ? 25  THR A OG1   1 
ATOM   204  C CG2   . THR A 1 30  ? 15.264 -1.442  14.242  1.00 23.59 ? 25  THR A CG2   1 
ATOM   205  N N     . THR A 1 31  ? 16.984 -5.482  14.074  1.00 25.74 ? 26  THR A N     1 
ATOM   206  C CA    . THR A 1 31  ? 17.119 -6.806  13.505  1.00 26.08 ? 26  THR A CA    1 
ATOM   207  C C     . THR A 1 31  ? 16.367 -6.880  12.175  1.00 21.47 ? 26  THR A C     1 
ATOM   208  O O     . THR A 1 31  ? 15.629 -5.969  11.788  1.00 21.79 ? 26  THR A O     1 
ATOM   209  C CB    . THR A 1 31  ? 16.596 -7.858  14.485  1.00 26.22 ? 26  THR A CB    1 
ATOM   210  O OG1   . THR A 1 31  ? 15.200 -7.631  14.733  1.00 22.13 ? 26  THR A OG1   1 
ATOM   211  C CG2   . THR A 1 31  ? 17.354 -7.775  15.806  1.00 26.10 ? 26  THR A CG2   1 
ATOM   212  N N     . ARG A 1 32  ? 16.560 -7.985  11.466  1.00 18.45 ? 27  ARG A N     1 
ATOM   213  C CA    . ARG A 1 32  ? 15.876 -8.214  10.204  1.00 20.29 ? 27  ARG A CA    1 
ATOM   214  C C     . ARG A 1 32  ? 15.307 -9.619  10.202  1.00 20.32 ? 27  ARG A C     1 
ATOM   215  O O     . ARG A 1 32  ? 16.013 -10.579 10.525  1.00 22.93 ? 27  ARG A O     1 
ATOM   216  C CB    . ARG A 1 32  ? 16.820 -8.002  9.020   1.00 25.01 ? 27  ARG A CB    1 
ATOM   217  C CG    . ARG A 1 32  ? 16.252 -8.327  7.661   1.00 20.10 ? 27  ARG A CG    1 
ATOM   218  C CD    . ARG A 1 32  ? 17.337 -8.156  6.620   1.00 18.38 ? 27  ARG A CD    1 
ATOM   219  N NE    . ARG A 1 32  ? 16.892 -8.496  5.276   1.00 21.38 ? 27  ARG A NE    1 
ATOM   220  C CZ    . ARG A 1 32  ? 17.680 -8.484  4.209   1.00 16.81 ? 27  ARG A CZ    1 
ATOM   221  N NH1   . ARG A 1 32  ? 18.952 -8.128  4.293   1.00 17.47 ? 27  ARG A NH1   1 
ATOM   222  N NH2   . ARG A 1 32  ? 17.178 -8.831  3.027   1.00 17.96 ? 27  ARG A NH2   1 
ATOM   223  N N     . ASP A 1 33  ? 14.035 -9.732  9.847   1.00 19.66 ? 28  ASP A N     1 
ATOM   224  C CA    . ASP A 1 33  ? 13.386 -11.027 9.859   1.00 20.70 ? 28  ASP A CA    1 
ATOM   225  C C     . ASP A 1 33  ? 13.955 -11.886 8.736   1.00 20.43 ? 28  ASP A C     1 
ATOM   226  O O     . ASP A 1 33  ? 14.192 -11.383 7.633   1.00 24.19 ? 28  ASP A O     1 
ATOM   227  C CB    . ASP A 1 33  ? 11.874 -10.873 9.693   1.00 26.56 ? 28  ASP A CB    1 
ATOM   228  C CG    . ASP A 1 33  ? 11.133 -12.182 9.843   1.00 18.90 ? 28  ASP A CG    1 
ATOM   229  O OD1   . ASP A 1 33  ? 10.879 -12.576 10.999  1.00 21.39 ? 28  ASP A OD1   1 
ATOM   230  O OD2   . ASP A 1 33  ? 10.796 -12.809 8.818   1.00 19.04 ? 28  ASP A OD2   1 
ATOM   231  N N     . PRO A 1 34  ? 14.228 -13.170 8.996   1.00 23.73 ? 29  PRO A N     1 
ATOM   232  C CA    . PRO A 1 34  ? 14.687 -14.055 7.913   1.00 17.44 ? 29  PRO A CA    1 
ATOM   233  C C     . PRO A 1 34  ? 13.810 -13.997 6.678   1.00 15.63 ? 29  PRO A C     1 
ATOM   234  O O     . PRO A 1 34  ? 14.323 -14.054 5.555   1.00 22.67 ? 29  PRO A O     1 
ATOM   235  C CB    . PRO A 1 34  ? 14.649 -15.433 8.577   1.00 16.49 ? 29  PRO A CB    1 
ATOM   236  C CG    . PRO A 1 34  ? 15.020 -15.133 9.993   1.00 20.51 ? 29  PRO A CG    1 
ATOM   237  C CD    . PRO A 1 34  ? 14.347 -13.818 10.316  1.00 14.64 ? 29  PRO A CD    1 
ATOM   238  N N     . GLY A 1 35  ? 12.501 -13.859 6.855   1.00 18.89 ? 30  GLY A N     1 
ATOM   239  C CA    . GLY A 1 35  ? 11.580 -13.766 5.748   1.00 18.46 ? 30  GLY A CA    1 
ATOM   240  C C     . GLY A 1 35  ? 11.485 -12.419 5.068   1.00 22.84 ? 30  GLY A C     1 
ATOM   241  O O     . GLY A 1 35  ? 10.732 -12.293 4.098   1.00 20.83 ? 30  GLY A O     1 
ATOM   242  N N     . PHE A 1 36  ? 12.222 -11.407 5.529   1.00 20.91 ? 31  PHE A N     1 
ATOM   243  C CA    . PHE A 1 36  ? 12.118 -10.060 4.974   1.00 20.55 ? 31  PHE A CA    1 
ATOM   244  C C     . PHE A 1 36  ? 13.104 -9.908  3.821   1.00 23.87 ? 31  PHE A C     1 
ATOM   245  O O     . PHE A 1 36  ? 14.321 -9.936  4.028   1.00 25.68 ? 31  PHE A O     1 
ATOM   246  C CB    . PHE A 1 36  ? 12.371 -9.001  6.045   1.00 22.63 ? 31  PHE A CB    1 
ATOM   247  C CG    . PHE A 1 36  ? 12.148 -7.594  5.559   1.00 24.70 ? 31  PHE A CG    1 
ATOM   248  C CD1   . PHE A 1 36  ? 10.872 -7.151  5.248   1.00 24.87 ? 31  PHE A CD1   1 
ATOM   249  C CD2   . PHE A 1 36  ? 13.213 -6.720  5.398   1.00 22.39 ? 31  PHE A CD2   1 
ATOM   250  C CE1   . PHE A 1 36  ? 10.655 -5.858  4.794   1.00 29.02 ? 31  PHE A CE1   1 
ATOM   251  C CE2   . PHE A 1 36  ? 13.004 -5.422  4.943   1.00 28.23 ? 31  PHE A CE2   1 
ATOM   252  C CZ    . PHE A 1 36  ? 11.722 -4.992  4.642   1.00 24.17 ? 31  PHE A CZ    1 
ATOM   253  N N     . ARG A 1 37  ? 12.579 -9.730  2.611   1.00 26.00 ? 32  ARG A N     1 
ATOM   254  C CA    . ARG A 1 37  ? 13.388 -9.530  1.418   1.00 23.32 ? 32  ARG A CA    1 
ATOM   255  C C     . ARG A 1 37  ? 12.958 -8.234  0.743   1.00 18.96 ? 32  ARG A C     1 
ATOM   256  O O     . ARG A 1 37  ? 11.763 -7.944  0.647   1.00 20.40 ? 32  ARG A O     1 
ATOM   257  C CB    . ARG A 1 37  ? 13.239 -10.708 0.448   1.00 19.55 ? 32  ARG A CB    1 
ATOM   258  C CG    . ARG A 1 37  ? 13.774 -12.026 0.996   1.00 25.27 ? 32  ARG A CG    1 
ATOM   259  C CD    . ARG A 1 37  ? 15.005 -12.544 0.266   1.00 25.71 ? 32  ARG A CD    1 
ATOM   260  N NE    . ARG A 1 37  ? 16.014 -11.515 0.042   1.00 26.02 ? 32  ARG A NE    1 
ATOM   261  C CZ    . ARG A 1 37  ? 16.534 -11.220 -1.142  1.00 29.48 ? 32  ARG A CZ    1 
ATOM   262  N NH1   . ARG A 1 37  ? 16.169 -11.863 -2.237  1.00 34.01 ? 32  ARG A NH1   1 
ATOM   263  N NH2   . ARG A 1 37  ? 17.451 -10.259 -1.227  1.00 29.94 ? 32  ARG A NH2   1 
ATOM   264  N N     . PHE A 1 38  ? 13.935 -7.454  0.281   1.00 17.42 ? 33  PHE A N     1 
ATOM   265  C CA    . PHE A 1 38  ? 13.658 -6.172  -0.352  1.00 15.65 ? 33  PHE A CA    1 
ATOM   266  C C     . PHE A 1 38  ? 14.734 -5.865  -1.384  1.00 14.40 ? 33  PHE A C     1 
ATOM   267  O O     . PHE A 1 38  ? 15.863 -6.352  -1.302  1.00 16.13 ? 33  PHE A O     1 
ATOM   268  C CB    . PHE A 1 38  ? 13.573 -5.030  0.673   1.00 16.66 ? 33  PHE A CB    1 
ATOM   269  C CG    . PHE A 1 38  ? 14.910 -4.617  1.235   1.00 17.56 ? 33  PHE A CG    1 
ATOM   270  C CD1   . PHE A 1 38  ? 15.419 -5.242  2.363   1.00 15.65 ? 33  PHE A CD1   1 
ATOM   271  C CD2   . PHE A 1 38  ? 15.666 -3.624  0.627   1.00 16.11 ? 33  PHE A CD2   1 
ATOM   272  C CE1   . PHE A 1 38  ? 16.649 -4.880  2.877   1.00 18.31 ? 33  PHE A CE1   1 
ATOM   273  C CE2   . PHE A 1 38  ? 16.900 -3.262  1.131   1.00 16.76 ? 33  PHE A CE2   1 
ATOM   274  C CZ    . PHE A 1 38  ? 17.392 -3.890  2.258   1.00 16.81 ? 33  PHE A CZ    1 
ATOM   275  N N     . GLN A 1 39  ? 14.366 -5.025  -2.347  1.00 17.70 ? 34  GLN A N     1 
ATOM   276  C CA    . GLN A 1 39  ? 15.277 -4.499  -3.351  1.00 14.33 ? 34  GLN A CA    1 
ATOM   277  C C     . GLN A 1 39  ? 15.788 -3.132  -2.913  1.00 13.94 ? 34  GLN A C     1 
ATOM   278  O O     . GLN A 1 39  ? 15.120 -2.414  -2.165  1.00 15.98 ? 34  GLN A O     1 
ATOM   279  C CB    . GLN A 1 39  ? 14.577 -4.390  -4.706  1.00 15.02 ? 34  GLN A CB    1 
ATOM   280  C CG    . GLN A 1 39  ? 13.915 -5.676  -5.178  1.00 15.99 ? 34  GLN A CG    1 
ATOM   281  C CD    . GLN A 1 39  ? 13.080 -5.481  -6.432  1.00 16.28 ? 34  GLN A CD    1 
ATOM   282  O OE1   . GLN A 1 39  ? 13.596 -5.511  -7.549  1.00 19.62 ? 34  GLN A OE1   1 
ATOM   283  N NE2   . GLN A 1 39  ? 11.779 -5.278  -6.250  1.00 16.95 ? 34  GLN A NE2   1 
ATOM   284  N N     . SER A 1 40  ? 16.982 -2.778  -3.387  1.00 19.06 ? 35  SER A N     1 
ATOM   285  C CA    . SER A 1 40  ? 17.594 -1.505  -3.019  1.00 18.57 ? 35  SER A CA    1 
ATOM   286  C C     . SER A 1 40  ? 16.792 -0.333  -3.575  1.00 16.02 ? 35  SER A C     1 
ATOM   287  O O     . SER A 1 40  ? 16.475 -0.290  -4.768  1.00 19.59 ? 35  SER A O     1 
ATOM   288  C CB    . SER A 1 40  ? 19.032 -1.442  -3.525  1.00 14.86 ? 35  SER A CB    1 
ATOM   289  O OG    . SER A 1 40  ? 19.832 -2.408  -2.873  1.00 19.69 ? 35  SER A OG    1 
ATOM   290  N N     . GLY A 1 41  ? 16.473 0.625   -2.707  1.00 15.28 ? 36  GLY A N     1 
ATOM   291  C CA    . GLY A 1 41  ? 15.690 1.781   -3.078  1.00 15.73 ? 36  GLY A CA    1 
ATOM   292  C C     . GLY A 1 41  ? 14.229 1.711   -2.687  1.00 14.71 ? 36  GLY A C     1 
ATOM   293  O O     . GLY A 1 41  ? 13.513 2.706   -2.855  1.00 17.88 ? 36  GLY A O     1 
ATOM   294  N N     . GLN A 1 42  ? 13.765 0.576   -2.173  1.00 18.41 ? 37  GLN A N     1 
ATOM   295  C CA    . GLN A 1 42  ? 12.371 0.449   -1.780  1.00 19.57 ? 37  GLN A CA    1 
ATOM   296  C C     . GLN A 1 42  ? 12.147 1.015   -0.380  1.00 16.65 ? 37  GLN A C     1 
ATOM   297  O O     . GLN A 1 42  ? 13.082 1.297   0.374   1.00 15.26 ? 37  GLN A O     1 
ATOM   298  C CB    . GLN A 1 42  ? 11.922 -1.012  -1.834  1.00 15.60 ? 37  GLN A CB    1 
ATOM   299  C CG    . GLN A 1 42  ? 11.744 -1.563  -3.239  1.00 17.86 ? 37  GLN A CG    1 
ATOM   300  C CD    . GLN A 1 42  ? 11.194 -2.980  -3.249  1.00 18.00 ? 37  GLN A CD    1 
ATOM   301  O OE1   . GLN A 1 42  ? 11.719 -3.867  -2.580  1.00 17.02 ? 37  GLN A OE1   1 
ATOM   302  N NE2   . GLN A 1 42  ? 10.134 -3.197  -4.022  1.00 21.30 ? 37  GLN A NE2   1 
ATOM   303  N N     . PHE A 1 43  ? 10.874 1.180   -0.040  1.00 18.73 ? 38  PHE A N     1 
ATOM   304  C CA    . PHE A 1 43  ? 10.466 1.617   1.282   1.00 17.58 ? 38  PHE A CA    1 
ATOM   305  C C     . PHE A 1 43  ? 9.384  0.688   1.818   1.00 20.48 ? 38  PHE A C     1 
ATOM   306  O O     . PHE A 1 43  ? 8.780  -0.099  1.082   1.00 21.70 ? 38  PHE A O     1 
ATOM   307  C CB    . PHE A 1 43  ? 9.996  3.090   1.272   1.00 15.35 ? 38  PHE A CB    1 
ATOM   308  C CG    . PHE A 1 43  ? 8.694  3.328   0.543   1.00 19.23 ? 38  PHE A CG    1 
ATOM   309  C CD1   . PHE A 1 43  ? 7.477  3.249   1.204   1.00 21.64 ? 38  PHE A CD1   1 
ATOM   310  C CD2   . PHE A 1 43  ? 8.693  3.675   -0.797  1.00 18.12 ? 38  PHE A CD2   1 
ATOM   311  C CE1   . PHE A 1 43  ? 6.287  3.477   0.534   1.00 17.01 ? 38  PHE A CE1   1 
ATOM   312  C CE2   . PHE A 1 43  ? 7.508  3.908   -1.469  1.00 18.22 ? 38  PHE A CE2   1 
ATOM   313  C CZ    . PHE A 1 43  ? 6.304  3.810   -0.801  1.00 17.83 ? 38  PHE A CZ    1 
ATOM   314  N N     . ILE A 1 44  ? 9.175  0.778   3.133   1.00 22.40 ? 39  ILE A N     1 
ATOM   315  C CA    . ILE A 1 44  ? 8.166  0.014   3.853   1.00 18.99 ? 39  ILE A CA    1 
ATOM   316  C C     . ILE A 1 44  ? 7.433  0.946   4.814   1.00 22.12 ? 39  ILE A C     1 
ATOM   317  O O     . ILE A 1 44  ? 7.789  2.113   4.974   1.00 22.48 ? 39  ILE A O     1 
ATOM   318  C CB    . ILE A 1 44  ? 8.769  -1.221  4.575   1.00 17.58 ? 39  ILE A CB    1 
ATOM   319  C CG1   . ILE A 1 44  ? 10.021 -0.899  5.424   1.00 20.11 ? 39  ILE A CG1   1 
ATOM   320  C CG2   . ILE A 1 44  ? 9.075  -2.334  3.582   1.00 21.29 ? 39  ILE A CG2   1 
ATOM   321  C CD1   . ILE A 1 44  ? 9.906  0.164   6.500   1.00 22.76 ? 39  ILE A CD1   1 
ATOM   322  N N     . MET A 1 45  ? 6.389  0.416   5.448   1.00 23.80 ? 40  MET A N     1 
ATOM   323  C CA    . MET A 1 45  ? 5.695  1.125   6.514   1.00 20.03 ? 40  MET A CA    1 
ATOM   324  C C     . MET A 1 45  ? 6.303  0.705   7.846   1.00 21.10 ? 40  MET A C     1 
ATOM   325  O O     . MET A 1 45  ? 6.204  -0.464  8.238   1.00 24.69 ? 40  MET A O     1 
ATOM   326  C CB    . MET A 1 45  ? 4.192  0.846   6.482   1.00 22.27 ? 40  MET A CB    1 
ATOM   327  C CG    . MET A 1 45  ? 3.500  1.248   5.183   1.00 25.55 ? 40  MET A CG    1 
ATOM   328  S SD    . MET A 1 45  ? 3.596  3.019   4.821   1.00 31.69 ? 40  MET A SD    1 
ATOM   329  C CE    . MET A 1 45  ? 2.466  3.697   6.029   1.00 16.05 ? 40  MET A CE    1 
ATOM   330  N N     . MET A 1 46  ? 6.946  1.652   8.530   1.00 23.14 ? 41  MET A N     1 
ATOM   331  C CA    . MET A 1 46  ? 7.659  1.401   9.776   1.00 21.52 ? 41  MET A CA    1 
ATOM   332  C C     . MET A 1 46  ? 7.045  2.244   10.887  1.00 16.78 ? 41  MET A C     1 
ATOM   333  O O     . MET A 1 46  ? 6.670  3.401   10.668  1.00 19.10 ? 41  MET A O     1 
ATOM   334  C CB    . MET A 1 46  ? 9.157  1.730   9.630   1.00 24.59 ? 41  MET A CB    1 
ATOM   335  C CG    . MET A 1 46  ? 10.034 1.380   10.836  1.00 21.58 ? 41  MET A CG    1 
ATOM   336  S SD    . MET A 1 46  ? 10.165 2.631   12.129  1.00 16.32 ? 41  MET A SD    1 
ATOM   337  C CE    . MET A 1 46  ? 11.037 3.924   11.275  1.00 16.15 ? 41  MET A CE    1 
ATOM   338  N N     . GLY A 1 47  ? 6.944  1.669   12.082  1.00 19.57 ? 42  GLY A N     1 
ATOM   339  C CA    . GLY A 1 47  ? 6.390  2.410   13.196  1.00 19.11 ? 42  GLY A CA    1 
ATOM   340  C C     . GLY A 1 47  ? 6.383  1.676   14.519  1.00 18.55 ? 42  GLY A C     1 
ATOM   341  O O     . GLY A 1 47  ? 7.249  0.836   14.778  1.00 19.74 ? 42  GLY A O     1 
ATOM   342  N N     . LEU A 1 48  ? 5.397  1.992   15.360  1.00 25.46 ? 43  LEU A N     1 
ATOM   343  C CA    . LEU A 1 48  ? 5.316  1.490   16.723  1.00 23.66 ? 43  LEU A CA    1 
ATOM   344  C C     . LEU A 1 48  ? 3.927  0.921   16.979  1.00 22.76 ? 43  LEU A C     1 
ATOM   345  O O     . LEU A 1 48  ? 2.952  1.307   16.329  1.00 21.12 ? 43  LEU A O     1 
ATOM   346  C CB    . LEU A 1 48  ? 5.631  2.607   17.741  1.00 17.72 ? 43  LEU A CB    1 
ATOM   347  C CG    . LEU A 1 48  ? 7.029  3.232   17.646  1.00 17.80 ? 43  LEU A CG    1 
ATOM   348  C CD1   . LEU A 1 48  ? 7.161  4.439   18.555  1.00 17.53 ? 43  LEU A CD1   1 
ATOM   349  C CD2   . LEU A 1 48  ? 8.111  2.216   17.960  1.00 21.28 ? 43  LEU A CD2   1 
ATOM   350  N N     . GLU A 1 49  ? 3.849  -0.010  17.930  1.00 24.08 ? 44  GLU A N     1 
ATOM   351  C CA    . GLU A 1 49  ? 2.587  -0.641  18.308  1.00 26.71 ? 44  GLU A CA    1 
ATOM   352  C C     . GLU A 1 49  ? 1.984  0.155   19.462  1.00 30.37 ? 44  GLU A C     1 
ATOM   353  O O     . GLU A 1 49  ? 2.484  0.098   20.591  1.00 25.91 ? 44  GLU A O     1 
ATOM   354  C CB    . GLU A 1 49  ? 2.812  -2.102  18.693  1.00 33.17 ? 44  GLU A CB    1 
ATOM   355  C CG    . GLU A 1 49  ? 2.154  -3.112  17.759  1.00 35.34 ? 44  GLU A CG    1 
ATOM   356  C CD    . GLU A 1 49  ? 2.323  -4.550  18.225  1.00 36.93 ? 44  GLU A CD    1 
ATOM   357  O OE1   . GLU A 1 49  ? 2.206  -4.807  19.443  1.00 34.80 ? 44  GLU A OE1   1 
ATOM   358  O OE2   . GLU A 1 49  ? 2.582  -5.423  17.367  1.00 30.62 ? 44  GLU A OE2   1 
ATOM   359  N N     . VAL A 1 50  ? 0.920  0.903   19.177  1.00 31.04 ? 45  VAL A N     1 
ATOM   360  C CA    . VAL A 1 50  ? 0.320  1.837   20.124  1.00 33.10 ? 45  VAL A CA    1 
ATOM   361  C C     . VAL A 1 50  ? -1.143 1.461   20.304  1.00 32.75 ? 45  VAL A C     1 
ATOM   362  O O     . VAL A 1 50  ? -1.902 1.428   19.327  1.00 36.35 ? 45  VAL A O     1 
ATOM   363  C CB    . VAL A 1 50  ? 0.456  3.292   19.646  1.00 32.19 ? 45  VAL A CB    1 
ATOM   364  C CG1   . VAL A 1 50  ? -0.265 4.233   20.597  1.00 36.55 ? 45  VAL A CG1   1 
ATOM   365  C CG2   . VAL A 1 50  ? 1.923  3.680   19.504  1.00 26.34 ? 45  VAL A CG2   1 
ATOM   366  N N     . ASN A 1 51  ? -1.538 1.191   21.552  1.00 36.79 ? 46  ASN A N     1 
ATOM   367  C CA    . ASN A 1 51  ? -2.900 0.759   21.891  1.00 41.82 ? 46  ASN A CA    1 
ATOM   368  C C     . ASN A 1 51  ? -3.314 -0.488  21.115  1.00 42.37 ? 46  ASN A C     1 
ATOM   369  O O     . ASN A 1 51  ? -4.505 -0.733  20.904  1.00 45.33 ? 46  ASN A O     1 
ATOM   370  C CB    . ASN A 1 51  ? -3.928 1.875   21.668  1.00 45.86 ? 46  ASN A CB    1 
ATOM   371  C CG    . ASN A 1 51  ? -3.664 3.101   22.520  1.00 42.05 ? 46  ASN A CG    1 
ATOM   372  O OD1   . ASN A 1 51  ? -3.728 4.230   22.035  1.00 38.65 ? 46  ASN A OD1   1 
ATOM   373  N ND2   . ASN A 1 51  ? -3.390 2.886   23.803  1.00 43.96 ? 46  ASN A ND2   1 
ATOM   374  N N     . GLY A 1 52  ? -2.338 -1.288  20.693  1.00 42.91 ? 47  GLY A N     1 
ATOM   375  C CA    . GLY A 1 52  ? -2.611 -2.438  19.857  1.00 47.83 ? 47  GLY A CA    1 
ATOM   376  C C     . GLY A 1 52  ? -2.889 -2.120  18.405  1.00 45.06 ? 47  GLY A C     1 
ATOM   377  O O     . GLY A 1 52  ? -3.362 -2.998  17.674  1.00 48.00 ? 47  GLY A O     1 
ATOM   378  N N     . LYS A 1 53  ? -2.611 -0.895  17.962  1.00 44.44 ? 48  LYS A N     1 
ATOM   379  C CA    . LYS A 1 53  ? -2.867 -0.474  16.596  1.00 42.65 ? 48  LYS A CA    1 
ATOM   380  C C     . LYS A 1 53  ? -1.593 0.071   15.966  1.00 37.71 ? 48  LYS A C     1 
ATOM   381  O O     . LYS A 1 53  ? -0.798 0.737   16.640  1.00 34.08 ? 48  LYS A O     1 
ATOM   382  C CB    . LYS A 1 53  ? -3.976 0.587   16.554  1.00 35.07 ? 48  LYS A CB    1 
ATOM   383  C CG    . LYS A 1 53  ? -5.229 0.180   17.310  1.00 45.74 ? 48  LYS A CG    1 
ATOM   384  C CD    . LYS A 1 53  ? -5.656 1.216   18.335  1.00 42.31 ? 48  LYS A CD    1 
ATOM   385  C CE    . LYS A 1 53  ? -7.150 1.118   18.591  1.00 47.19 ? 48  LYS A CE    1 
ATOM   386  N NZ    . LYS A 1 53  ? -7.547 1.803   19.848  1.00 56.20 ? 48  LYS A NZ    1 
ATOM   387  N N     . PRO A 1 54  ? -1.372 -0.193  14.673  1.00 34.38 ? 49  PRO A N     1 
ATOM   388  C CA    . PRO A 1 54  ? -0.114 0.225   14.043  1.00 33.54 ? 49  PRO A CA    1 
ATOM   389  C C     . PRO A 1 54  ? -0.037 1.724   13.800  1.00 23.72 ? 49  PRO A C     1 
ATOM   390  O O     . PRO A 1 54  ? -0.796 2.280   13.002  1.00 25.71 ? 49  PRO A O     1 
ATOM   391  C CB    . PRO A 1 54  ? -0.104 -0.564  12.726  1.00 33.17 ? 49  PRO A CB    1 
ATOM   392  C CG    . PRO A 1 54  ? -1.540 -0.794  12.416  1.00 30.08 ? 49  PRO A CG    1 
ATOM   393  C CD    . PRO A 1 54  ? -2.266 -0.888  13.728  1.00 25.87 ? 49  PRO A CD    1 
ATOM   394  N N     . LEU A 1 55  ? 0.875  2.390   14.497  1.00 23.15 ? 50  LEU A N     1 
ATOM   395  C CA    . LEU A 1 55  ? 1.218  3.780   14.211  1.00 27.42 ? 50  LEU A CA    1 
ATOM   396  C C     . LEU A 1 55  ? 2.511  3.761   13.400  1.00 25.25 ? 50  LEU A C     1 
ATOM   397  O O     . LEU A 1 55  ? 3.604  3.629   13.955  1.00 23.06 ? 50  LEU A O     1 
ATOM   398  C CB    . LEU A 1 55  ? 1.354  4.592   15.495  1.00 21.91 ? 50  LEU A CB    1 
ATOM   399  C CG    . LEU A 1 55  ? 1.607  6.086   15.284  1.00 20.35 ? 50  LEU A CG    1 
ATOM   400  C CD1   . LEU A 1 55  ? 0.454  6.719   14.515  1.00 23.02 ? 50  LEU A CD1   1 
ATOM   401  C CD2   . LEU A 1 55  ? 1.805  6.777   16.614  1.00 23.06 ? 50  LEU A CD2   1 
ATOM   402  N N     . THR A 1 56  ? 2.378  3.878   12.078  1.00 22.57 ? 51  THR A N     1 
ATOM   403  C CA    . THR A 1 56  ? 3.502  3.771   11.161  1.00 22.69 ? 51  THR A CA    1 
ATOM   404  C C     . THR A 1 56  ? 3.483  4.922   10.163  1.00 22.48 ? 51  THR A C     1 
ATOM   405  O O     . THR A 1 56  ? 2.448  5.549   9.924   1.00 25.75 ? 51  THR A O     1 
ATOM   406  C CB    . THR A 1 56  ? 3.494  2.431   10.398  1.00 17.14 ? 51  THR A CB    1 
ATOM   407  O OG1   . THR A 1 56  ? 2.394  2.401   9.479   1.00 23.50 ? 51  THR A OG1   1 
ATOM   408  C CG2   . THR A 1 56  ? 3.370  1.266   11.346  1.00 18.69 ? 51  THR A CG2   1 
ATOM   409  N N     . ARG A 1 57  ? 4.656  5.198   9.592   1.00 24.53 ? 52  ARG A N     1 
ATOM   410  C CA    . ARG A 1 57  ? 4.816  6.087   8.448   1.00 23.33 ? 52  ARG A CA    1 
ATOM   411  C C     . ARG A 1 57  ? 5.685  5.396   7.407   1.00 20.88 ? 52  ARG A C     1 
ATOM   412  O O     . ARG A 1 57  ? 6.243  4.320   7.643   1.00 19.46 ? 52  ARG A O     1 
ATOM   413  C CB    . ARG A 1 57  ? 5.451  7.433   8.833   1.00 20.42 ? 52  ARG A CB    1 
ATOM   414  C CG    . ARG A 1 57  ? 4.679  8.285   9.836   1.00 22.47 ? 52  ARG A CG    1 
ATOM   415  C CD    . ARG A 1 57  ? 3.429  8.900   9.229   1.00 22.14 ? 52  ARG A CD    1 
ATOM   416  N NE    . ARG A 1 57  ? 2.675  9.668   10.213  1.00 22.78 ? 52  ARG A NE    1 
ATOM   417  C CZ    . ARG A 1 57  ? 1.671  9.195   10.940  1.00 23.75 ? 52  ARG A CZ    1 
ATOM   418  N NH1   . ARG A 1 57  ? 1.258  7.944   10.822  1.00 23.95 ? 52  ARG A NH1   1 
ATOM   419  N NH2   . ARG A 1 57  ? 1.069  10.000  11.810  1.00 27.55 ? 52  ARG A NH2   1 
ATOM   420  N N     . ALA A 1 58  ? 5.795  6.027   6.241   1.00 23.68 ? 53  ALA A N     1 
ATOM   421  C CA    . ALA A 1 58  ? 6.659  5.504   5.192   1.00 24.08 ? 53  ALA A CA    1 
ATOM   422  C C     . ALA A 1 58  ? 8.118  5.773   5.542   1.00 21.71 ? 53  ALA A C     1 
ATOM   423  O O     . ALA A 1 58  ? 8.462  6.848   6.044   1.00 18.16 ? 53  ALA A O     1 
ATOM   424  C CB    . ALA A 1 58  ? 6.304  6.127   3.842   1.00 16.48 ? 53  ALA A CB    1 
ATOM   425  N N     . TYR A 1 59  ? 8.970  4.777   5.296   1.00 22.90 ? 54  TYR A N     1 
ATOM   426  C CA    . TYR A 1 59  ? 10.392 4.872   5.612   1.00 18.47 ? 54  TYR A CA    1 
ATOM   427  C C     . TYR A 1 59  ? 11.192 4.095   4.581   1.00 16.05 ? 54  TYR A C     1 
ATOM   428  O O     . TYR A 1 59  ? 10.961 2.897   4.394   1.00 16.99 ? 54  TYR A O     1 
ATOM   429  C CB    . TYR A 1 59  ? 10.691 4.338   7.011   1.00 19.64 ? 54  TYR A CB    1 
ATOM   430  C CG    . TYR A 1 59  ? 10.624 5.373   8.108   1.00 19.77 ? 54  TYR A CG    1 
ATOM   431  C CD1   . TYR A 1 59  ? 9.413  5.763   8.658   1.00 19.22 ? 54  TYR A CD1   1 
ATOM   432  C CD2   . TYR A 1 59  ? 11.785 5.967   8.586   1.00 19.18 ? 54  TYR A CD2   1 
ATOM   433  C CE1   . TYR A 1 59  ? 9.358  6.708   9.660   1.00 21.28 ? 54  TYR A CE1   1 
ATOM   434  C CE2   . TYR A 1 59  ? 11.740 6.910   9.584   1.00 18.10 ? 54  TYR A CE2   1 
ATOM   435  C CZ    . TYR A 1 59  ? 10.528 7.278   10.119  1.00 18.62 ? 54  TYR A CZ    1 
ATOM   436  O OH    . TYR A 1 59  ? 10.494 8.223   11.117  1.00 23.70 ? 54  TYR A OH    1 
ATOM   437  N N     . SER A 1 60  ? 12.133 4.773   3.928   1.00 14.62 ? 55  SER A N     1 
ATOM   438  C CA    . SER A 1 60  ? 13.098 4.084   3.085   1.00 15.11 ? 55  SER A CA    1 
ATOM   439  C C     . SER A 1 60  ? 13.890 3.077   3.909   1.00 17.55 ? 55  SER A C     1 
ATOM   440  O O     . SER A 1 60  ? 14.153 3.280   5.098   1.00 21.19 ? 55  SER A O     1 
ATOM   441  C CB    . SER A 1 60  ? 14.055 5.082   2.434   1.00 11.80 ? 55  SER A CB    1 
ATOM   442  O OG    . SER A 1 60  ? 13.381 5.955   1.552   1.00 16.97 ? 55  SER A OG    1 
ATOM   443  N N     . ILE A 1 61  ? 14.270 1.977   3.270   1.00 20.33 ? 56  ILE A N     1 
ATOM   444  C CA    . ILE A 1 61  ? 15.159 1.001   3.888   1.00 21.29 ? 56  ILE A CA    1 
ATOM   445  C C     . ILE A 1 61  ? 16.590 1.439   3.591   1.00 18.48 ? 56  ILE A C     1 
ATOM   446  O O     . ILE A 1 61  ? 17.027 1.439   2.436   1.00 17.12 ? 56  ILE A O     1 
ATOM   447  C CB    . ILE A 1 61  ? 14.871 -0.420  3.393   1.00 17.43 ? 56  ILE A CB    1 
ATOM   448  C CG1   . ILE A 1 61  ? 13.410 -0.780  3.699   1.00 17.60 ? 56  ILE A CG1   1 
ATOM   449  C CG2   . ILE A 1 61  ? 15.827 -1.405  4.048   1.00 16.65 ? 56  ILE A CG2   1 
ATOM   450  C CD1   . ILE A 1 61  ? 12.802 -1.804  2.780   1.00 18.34 ? 56  ILE A CD1   1 
ATOM   451  N N     . ALA A 1 62  ? 17.308 1.845   4.642   1.00 17.80 ? 57  ALA A N     1 
ATOM   452  C CA    . ALA A 1 62  ? 18.628 2.448   4.529   1.00 16.13 ? 57  ALA A CA    1 
ATOM   453  C C     . ALA A 1 62  ? 19.764 1.451   4.717   1.00 17.92 ? 57  ALA A C     1 
ATOM   454  O O     . ALA A 1 62  ? 20.925 1.804   4.476   1.00 20.14 ? 57  ALA A O     1 
ATOM   455  C CB    . ALA A 1 62  ? 18.771 3.588   5.544   1.00 17.21 ? 57  ALA A CB    1 
ATOM   456  N N     . SER A 1 63  ? 19.466 0.232   5.143   1.00 17.63 ? 58  SER A N     1 
ATOM   457  C CA    . SER A 1 63  ? 20.470 -0.809  5.251   1.00 17.38 ? 58  SER A CA    1 
ATOM   458  C C     . SER A 1 63  ? 20.618 -1.536  3.917   1.00 16.19 ? 58  SER A C     1 
ATOM   459  O O     . SER A 1 63  ? 19.716 -1.537  3.078   1.00 15.87 ? 58  SER A O     1 
ATOM   460  C CB    . SER A 1 63  ? 20.097 -1.798  6.356   1.00 18.04 ? 58  SER A CB    1 
ATOM   461  O OG    . SER A 1 63  ? 18.765 -2.261  6.199   1.00 18.51 ? 58  SER A OG    1 
ATOM   462  N N     . SER A 1 64  ? 21.779 -2.157  3.733   1.00 16.36 ? 59  SER A N     1 
ATOM   463  C CA    . SER A 1 64  ? 22.025 -2.962  2.547   1.00 17.18 ? 59  SER A CA    1 
ATOM   464  C C     . SER A 1 64  ? 21.211 -4.252  2.599   1.00 18.05 ? 59  SER A C     1 
ATOM   465  O O     . SER A 1 64  ? 20.832 -4.731  3.671   1.00 15.64 ? 59  SER A O     1 
ATOM   466  C CB    . SER A 1 64  ? 23.516 -3.281  2.428   1.00 16.37 ? 59  SER A CB    1 
ATOM   467  O OG    . SER A 1 64  ? 23.780 -4.164  1.356   1.00 22.02 ? 59  SER A OG    1 
ATOM   468  N N     . LEU A 1 65  ? 20.927 -4.814  1.418   1.00 18.05 ? 60  LEU A N     1 
ATOM   469  C CA    . LEU A 1 65  ? 20.279 -6.122  1.379   1.00 19.95 ? 60  LEU A CA    1 
ATOM   470  C C     . LEU A 1 65  ? 21.197 -7.226  1.893   1.00 22.16 ? 60  LEU A C     1 
ATOM   471  O O     . LEU A 1 65  ? 20.706 -8.281  2.316   1.00 21.33 ? 60  LEU A O     1 
ATOM   472  C CB    . LEU A 1 65  ? 19.818 -6.457  -0.045  1.00 21.59 ? 60  LEU A CB    1 
ATOM   473  C CG    . LEU A 1 65  ? 20.861 -7.000  -1.034  1.00 26.24 ? 60  LEU A CG    1 
ATOM   474  C CD1   . LEU A 1 65  ? 20.831 -8.533  -1.097  1.00 19.64 ? 60  LEU A CD1   1 
ATOM   475  C CD2   . LEU A 1 65  ? 20.671 -6.404  -2.423  1.00 32.39 ? 60  LEU A CD2   1 
ATOM   476  N N     . TYR A 1 66  ? 22.513 -7.009  1.859   1.00 19.13 ? 61  TYR A N     1 
ATOM   477  C CA    . TYR A 1 66  ? 23.482 -7.996  2.315   1.00 22.16 ? 61  TYR A CA    1 
ATOM   478  C C     . TYR A 1 66  ? 23.626 -8.034  3.831   1.00 22.62 ? 61  TYR A C     1 
ATOM   479  O O     . TYR A 1 66  ? 24.381 -8.866  4.347   1.00 23.37 ? 61  TYR A O     1 
ATOM   480  C CB    . TYR A 1 66  ? 24.848 -7.722  1.680   1.00 18.95 ? 61  TYR A CB    1 
ATOM   481  C CG    . TYR A 1 66  ? 24.883 -7.921  0.185   1.00 21.77 ? 61  TYR A CG    1 
ATOM   482  C CD1   . TYR A 1 66  ? 24.561 -6.882  -0.682  1.00 23.42 ? 61  TYR A CD1   1 
ATOM   483  C CD2   . TYR A 1 66  ? 25.220 -9.155  -0.362  1.00 24.09 ? 61  TYR A CD2   1 
ATOM   484  C CE1   . TYR A 1 66  ? 24.587 -7.059  -2.055  1.00 24.70 ? 61  TYR A CE1   1 
ATOM   485  C CE2   . TYR A 1 66  ? 25.249 -9.345  -1.730  1.00 27.72 ? 61  TYR A CE2   1 
ATOM   486  C CZ    . TYR A 1 66  ? 24.931 -8.292  -2.571  1.00 26.89 ? 61  TYR A CZ    1 
ATOM   487  O OH    . TYR A 1 66  ? 24.955 -8.473  -3.933  1.00 22.45 ? 61  TYR A OH    1 
ATOM   488  N N     . GLU A 1 67  ? 22.923 -7.172  4.553   1.00 19.70 ? 62  GLU A N     1 
ATOM   489  C CA    . GLU A 1 67  ? 23.115 -7.007  5.985   1.00 18.13 ? 62  GLU A CA    1 
ATOM   490  C C     . GLU A 1 67  ? 22.100 -7.836  6.759   1.00 18.35 ? 62  GLU A C     1 
ATOM   491  O O     . GLU A 1 67  ? 20.950 -7.989  6.335   1.00 18.89 ? 62  GLU A O     1 
ATOM   492  C CB    . GLU A 1 67  ? 22.994 -5.529  6.368   1.00 18.65 ? 62  GLU A CB    1 
ATOM   493  C CG    . GLU A 1 67  ? 23.529 -5.164  7.746   1.00 26.29 ? 62  GLU A CG    1 
ATOM   494  C CD    . GLU A 1 67  ? 25.048 -5.094  7.798   1.00 29.47 ? 62  GLU A CD    1 
ATOM   495  O OE1   . GLU A 1 67  ? 25.689 -5.022  6.727   1.00 26.73 ? 62  GLU A OE1   1 
ATOM   496  O OE2   . GLU A 1 67  ? 25.601 -5.109  8.918   1.00 27.07 ? 62  GLU A OE2   1 
ATOM   497  N N     . ASP A 1 68  ? 22.542 -8.373  7.896   1.00 20.79 ? 63  ASP A N     1 
ATOM   498  C CA    . ASP A 1 68  ? 21.663 -9.080  8.827   1.00 21.37 ? 63  ASP A CA    1 
ATOM   499  C C     . ASP A 1 68  ? 21.038 -8.070  9.797   1.00 20.93 ? 63  ASP A C     1 
ATOM   500  O O     . ASP A 1 68  ? 21.345 -8.013  10.991  1.00 16.24 ? 63  ASP A O     1 
ATOM   501  C CB    . ASP A 1 68  ? 22.447 -10.170 9.551   1.00 23.11 ? 63  ASP A CB    1 
ATOM   502  C CG    . ASP A 1 68  ? 21.567 -11.071 10.403  1.00 18.71 ? 63  ASP A CG    1 
ATOM   503  O OD1   . ASP A 1 68  ? 20.339 -11.105 10.187  1.00 26.59 ? 63  ASP A OD1   1 
ATOM   504  O OD2   . ASP A 1 68  ? 22.112 -11.748 11.300  1.00 16.86 ? 63  ASP A OD2   1 
ATOM   505  N N     . GLY A 1 69  ? 20.149 -7.251  9.251   1.00 21.68 ? 64  GLY A N     1 
ATOM   506  C CA    . GLY A 1 69  ? 19.534 -6.182  10.015  1.00 20.56 ? 64  GLY A CA    1 
ATOM   507  C C     . GLY A 1 69  ? 18.947 -5.123  9.112   1.00 15.64 ? 64  GLY A C     1 
ATOM   508  O O     . GLY A 1 69  ? 19.153 -5.114  7.899   1.00 18.10 ? 64  GLY A O     1 
ATOM   509  N N     . LEU A 1 70  ? 18.197 -4.215  9.736   1.00 18.81 ? 65  LEU A N     1 
ATOM   510  C CA    . LEU A 1 70  ? 17.579 -3.081  9.062   1.00 21.80 ? 65  LEU A CA    1 
ATOM   511  C C     . LEU A 1 70  ? 18.055 -1.775  9.686   1.00 20.49 ? 65  LEU A C     1 
ATOM   512  O O     . LEU A 1 70  ? 18.392 -1.721  10.871  1.00 21.67 ? 65  LEU A O     1 
ATOM   513  C CB    . LEU A 1 70  ? 16.046 -3.146  9.128   1.00 21.25 ? 65  LEU A CB    1 
ATOM   514  C CG    . LEU A 1 70  ? 15.365 -4.325  8.431   1.00 22.68 ? 65  LEU A CG    1 
ATOM   515  C CD1   . LEU A 1 70  ? 13.855 -4.258  8.619   1.00 24.07 ? 65  LEU A CD1   1 
ATOM   516  C CD2   . LEU A 1 70  ? 15.729 -4.374  6.956   1.00 17.43 ? 65  LEU A CD2   1 
ATOM   517  N N     . GLU A 1 71  ? 18.072 -0.717  8.879   1.00 20.64 ? 66  GLU A N     1 
ATOM   518  C CA    . GLU A 1 71  ? 18.539 0.590   9.319   1.00 22.13 ? 66  GLU A CA    1 
ATOM   519  C C     . GLU A 1 71  ? 17.628 1.671   8.755   1.00 19.74 ? 66  GLU A C     1 
ATOM   520  O O     . GLU A 1 71  ? 17.221 1.608   7.590   1.00 13.08 ? 66  GLU A O     1 
ATOM   521  C CB    . GLU A 1 71  ? 19.991 0.839   8.880   1.00 22.72 ? 66  GLU A CB    1 
ATOM   522  C CG    . GLU A 1 71  ? 20.594 2.133   9.383   1.00 18.35 ? 66  GLU A CG    1 
ATOM   523  C CD    . GLU A 1 71  ? 22.071 2.237   9.061   1.00 19.55 ? 66  GLU A CD    1 
ATOM   524  O OE1   . GLU A 1 71  ? 22.614 1.295   8.444   1.00 22.17 ? 66  GLU A OE1   1 
ATOM   525  O OE2   . GLU A 1 71  ? 22.694 3.247   9.448   1.00 21.84 ? 66  GLU A OE2   1 
ATOM   526  N N     . PHE A 1 72  ? 17.312 2.660   9.592   1.00 24.26 ? 67  PHE A N     1 
ATOM   527  C CA    . PHE A 1 72  ? 16.423 3.756   9.227   1.00 21.95 ? 67  PHE A CA    1 
ATOM   528  C C     . PHE A 1 72  ? 17.057 5.097   9.583   1.00 19.02 ? 67  PHE A C     1 
ATOM   529  O O     . PHE A 1 72  ? 17.568 5.276   10.694  1.00 16.49 ? 67  PHE A O     1 
ATOM   530  C CB    . PHE A 1 72  ? 15.055 3.597   9.906   1.00 18.70 ? 67  PHE A CB    1 
ATOM   531  C CG    . PHE A 1 72  ? 14.375 2.290   9.592   1.00 21.09 ? 67  PHE A CG    1 
ATOM   532  C CD1   . PHE A 1 72  ? 13.709 2.118   8.383   1.00 18.54 ? 67  PHE A CD1   1 
ATOM   533  C CD2   . PHE A 1 72  ? 14.410 1.234   10.492  1.00 19.80 ? 67  PHE A CD2   1 
ATOM   534  C CE1   . PHE A 1 72  ? 13.086 0.925   8.079   1.00 20.65 ? 67  PHE A CE1   1 
ATOM   535  C CE2   . PHE A 1 72  ? 13.789 0.030   10.197  1.00 21.22 ? 67  PHE A CE2   1 
ATOM   536  C CZ    . PHE A 1 72  ? 13.126 -0.126  8.990   1.00 24.89 ? 67  PHE A CZ    1 
ATOM   537  N N     . PHE A 1 73  ? 17.023 6.029   8.625   1.00 19.29 ? 68  PHE A N     1 
ATOM   538  C CA    . PHE A 1 73  ? 17.513 7.398   8.777   1.00 14.26 ? 68  PHE A CA    1 
ATOM   539  C C     . PHE A 1 73  ? 16.303 8.323   8.882   1.00 16.60 ? 68  PHE A C     1 
ATOM   540  O O     . PHE A 1 73  ? 15.634 8.601   7.882   1.00 17.57 ? 68  PHE A O     1 
ATOM   541  C CB    . PHE A 1 73  ? 18.423 7.761   7.605   1.00 14.35 ? 68  PHE A CB    1 
ATOM   542  C CG    . PHE A 1 73  ? 18.943 9.173   7.639   1.00 17.01 ? 68  PHE A CG    1 
ATOM   543  C CD1   . PHE A 1 73  ? 19.242 9.803   8.840   1.00 16.13 ? 68  PHE A CD1   1 
ATOM   544  C CD2   . PHE A 1 73  ? 19.176 9.857   6.455   1.00 15.76 ? 68  PHE A CD2   1 
ATOM   545  C CE1   . PHE A 1 73  ? 19.733 11.102  8.857   1.00 15.99 ? 68  PHE A CE1   1 
ATOM   546  C CE2   . PHE A 1 73  ? 19.670 11.152  6.466   1.00 15.79 ? 68  PHE A CE2   1 
ATOM   547  C CZ    . PHE A 1 73  ? 19.947 11.775  7.668   1.00 12.86 ? 68  PHE A CZ    1 
ATOM   548  N N     . SER A 1 74  ? 16.036 8.809   10.095  1.00 16.51 ? 69  SER A N     1 
ATOM   549  C CA    . SER A 1 74  ? 14.737 9.355   10.455  1.00 18.48 ? 69  SER A CA    1 
ATOM   550  C C     . SER A 1 74  ? 14.809 10.841  10.787  1.00 17.28 ? 69  SER A C     1 
ATOM   551  O O     . SER A 1 74  ? 15.828 11.346  11.268  1.00 19.06 ? 69  SER A O     1 
ATOM   552  C CB    . SER A 1 74  ? 14.147 8.597   11.650  1.00 14.57 ? 69  SER A CB    1 
ATOM   553  O OG    . SER A 1 74  ? 12.857 9.079   11.969  1.00 18.31 ? 69  SER A OG    1 
ATOM   554  N N     . ILE A 1 75  ? 13.703 11.532  10.521  1.00 20.32 ? 70  ILE A N     1 
ATOM   555  C CA    . ILE A 1 75  ? 13.499 12.901  10.980  1.00 20.27 ? 70  ILE A CA    1 
ATOM   556  C C     . ILE A 1 75  ? 12.995 12.878  12.416  1.00 16.41 ? 70  ILE A C     1 
ATOM   557  O O     . ILE A 1 75  ? 12.379 11.907  12.864  1.00 17.54 ? 70  ILE A O     1 
ATOM   558  C CB    . ILE A 1 75  ? 12.516 13.645  10.048  1.00 17.30 ? 70  ILE A CB    1 
ATOM   559  C CG1   . ILE A 1 75  ? 12.716 15.161  10.124  1.00 16.41 ? 70  ILE A CG1   1 
ATOM   560  C CG2   . ILE A 1 75  ? 11.068 13.288  10.359  1.00 19.12 ? 70  ILE A CG2   1 
ATOM   561  C CD1   . ILE A 1 75  ? 13.996 15.637  9.493   1.00 21.39 ? 70  ILE A CD1   1 
ATOM   562  N N     . LYS A 1 76  ? 13.277 13.951  13.151  1.00 21.44 ? 71  LYS A N     1 
ATOM   563  C CA    . LYS A 1 76  ? 12.697 14.191  14.471  1.00 20.11 ? 71  LYS A CA    1 
ATOM   564  C C     . LYS A 1 76  ? 11.862 15.459  14.386  1.00 18.59 ? 71  LYS A C     1 
ATOM   565  O O     . LYS A 1 76  ? 12.405 16.561  14.259  1.00 17.88 ? 71  LYS A O     1 
ATOM   566  C CB    . LYS A 1 76  ? 13.770 14.311  15.552  1.00 17.41 ? 71  LYS A CB    1 
ATOM   567  C CG    . LYS A 1 76  ? 14.444 12.993  15.890  1.00 19.77 ? 71  LYS A CG    1 
ATOM   568  C CD    . LYS A 1 76  ? 15.435 13.123  17.033  1.00 16.33 ? 71  LYS A CD    1 
ATOM   569  C CE    . LYS A 1 76  ? 16.698 13.816  16.601  1.00 16.37 ? 71  LYS A CE    1 
ATOM   570  N NZ    . LYS A 1 76  ? 17.657 13.942  17.725  1.00 18.16 ? 71  LYS A NZ    1 
ATOM   571  N N     . VAL A 1 77  ? 10.545 15.299  14.437  1.00 19.22 ? 72  VAL A N     1 
ATOM   572  C CA    . VAL A 1 77  ? 9.618  16.426  14.410  1.00 23.68 ? 72  VAL A CA    1 
ATOM   573  C C     . VAL A 1 77  ? 9.031  16.567  15.809  1.00 20.08 ? 72  VAL A C     1 
ATOM   574  O O     . VAL A 1 77  ? 8.733  15.551  16.454  1.00 21.76 ? 72  VAL A O     1 
ATOM   575  C CB    . VAL A 1 77  ? 8.531  16.228  13.339  1.00 31.42 ? 72  VAL A CB    1 
ATOM   576  C CG1   . VAL A 1 77  ? 7.521  17.372  13.361  1.00 24.68 ? 72  VAL A CG1   1 
ATOM   577  C CG2   . VAL A 1 77  ? 9.173  16.110  11.965  1.00 22.24 ? 72  VAL A CG2   1 
ATOM   578  N N     . PRO A 1 78  ? 8.886  17.790  16.329  1.00 22.82 ? 73  PRO A N     1 
ATOM   579  C CA    . PRO A 1 78  ? 8.393  17.939  17.712  1.00 26.25 ? 73  PRO A CA    1 
ATOM   580  C C     . PRO A 1 78  ? 6.987  17.405  17.941  1.00 20.86 ? 73  PRO A C     1 
ATOM   581  O O     . PRO A 1 78  ? 6.781  16.586  18.846  1.00 20.68 ? 73  PRO A O     1 
ATOM   582  C CB    . PRO A 1 78  ? 8.489  19.453  17.929  1.00 23.14 ? 73  PRO A CB    1 
ATOM   583  C CG    . PRO A 1 78  ? 9.646  19.852  17.075  1.00 22.56 ? 73  PRO A CG    1 
ATOM   584  C CD    . PRO A 1 78  ? 9.464  19.044  15.819  1.00 20.67 ? 73  PRO A CD    1 
ATOM   585  N N     . ASN A 1 79  ? 6.010  17.841  17.150  1.00 21.93 ? 74  ASN A N     1 
ATOM   586  C CA    . ASN A 1 79  ? 4.630  17.411  17.324  1.00 22.74 ? 74  ASN A CA    1 
ATOM   587  C C     . ASN A 1 79  ? 4.223  16.332  16.327  1.00 26.64 ? 74  ASN A C     1 
ATOM   588  O O     . ASN A 1 79  ? 3.026  16.151  16.073  1.00 29.76 ? 74  ASN A O     1 
ATOM   589  C CB    . ASN A 1 79  ? 3.689  18.610  17.226  1.00 23.31 ? 74  ASN A CB    1 
ATOM   590  C CG    . ASN A 1 79  ? 3.795  19.519  18.427  1.00 20.55 ? 74  ASN A CG    1 
ATOM   591  O OD1   . ASN A 1 79  ? 3.883  20.737  18.288  1.00 27.06 ? 74  ASN A OD1   1 
ATOM   592  N ND2   . ASN A 1 79  ? 3.792  18.931  19.620  1.00 23.14 ? 74  ASN A ND2   1 
ATOM   593  N N     . GLY A 1 80  ? 5.189  15.611  15.765  1.00 25.29 ? 75  GLY A N     1 
ATOM   594  C CA    . GLY A 1 80  ? 4.901  14.541  14.844  1.00 26.28 ? 75  GLY A CA    1 
ATOM   595  C C     . GLY A 1 80  ? 4.383  13.303  15.549  1.00 22.29 ? 75  GLY A C     1 
ATOM   596  O O     . GLY A 1 80  ? 4.958  12.844  16.539  1.00 25.74 ? 75  GLY A O     1 
ATOM   597  N N     . PRO A 1 81  ? 3.274  12.744  15.050  1.00 20.91 ? 76  PRO A N     1 
ATOM   598  C CA    . PRO A 1 81  ? 2.663  11.589  15.732  1.00 21.15 ? 76  PRO A CA    1 
ATOM   599  C C     . PRO A 1 81  ? 3.604  10.412  15.920  1.00 25.14 ? 76  PRO A C     1 
ATOM   600  O O     . PRO A 1 81  ? 3.543  9.739   16.957  1.00 24.33 ? 76  PRO A O     1 
ATOM   601  C CB    . PRO A 1 81  ? 1.492  11.238  14.807  1.00 21.57 ? 76  PRO A CB    1 
ATOM   602  C CG    . PRO A 1 81  ? 1.104  12.552  14.217  1.00 24.42 ? 76  PRO A CG    1 
ATOM   603  C CD    . PRO A 1 81  ? 2.408  13.271  13.981  1.00 23.38 ? 76  PRO A CD    1 
ATOM   604  N N     . LEU A 1 82  ? 4.480  10.145  14.947  1.00 30.00 ? 77  LEU A N     1 
ATOM   605  C CA    . LEU A 1 82  ? 5.417  9.028   15.036  1.00 25.37 ? 77  LEU A CA    1 
ATOM   606  C C     . LEU A 1 82  ? 6.763  9.441   15.630  1.00 21.43 ? 77  LEU A C     1 
ATOM   607  O O     . LEU A 1 82  ? 7.193  8.887   16.646  1.00 18.17 ? 77  LEU A O     1 
ATOM   608  C CB    . LEU A 1 82  ? 5.627  8.394   13.655  1.00 20.17 ? 77  LEU A CB    1 
ATOM   609  C CG    . LEU A 1 82  ? 6.634  7.236   13.625  1.00 24.20 ? 77  LEU A CG    1 
ATOM   610  C CD1   . LEU A 1 82  ? 6.235  6.109   14.576  1.00 21.58 ? 77  LEU A CD1   1 
ATOM   611  C CD2   . LEU A 1 82  ? 6.812  6.697   12.220  1.00 18.96 ? 77  LEU A CD2   1 
ATOM   612  N N     . THR A 1 83  ? 7.435  10.413  15.008  1.00 21.57 ? 78  THR A N     1 
ATOM   613  C CA    . THR A 1 83  ? 8.827  10.695  15.347  1.00 27.64 ? 78  THR A CA    1 
ATOM   614  C C     . THR A 1 83  ? 8.994  11.416  16.682  1.00 22.58 ? 78  THR A C     1 
ATOM   615  O O     . THR A 1 83  ? 10.135 11.620  17.115  1.00 17.77 ? 78  THR A O     1 
ATOM   616  C CB    . THR A 1 83  ? 9.486  11.506  14.225  1.00 22.94 ? 78  THR A CB    1 
ATOM   617  O OG1   . THR A 1 83  ? 8.768  12.729  14.017  1.00 19.93 ? 78  THR A OG1   1 
ATOM   618  C CG2   . THR A 1 83  ? 9.487  10.702  12.928  1.00 20.75 ? 78  THR A CG2   1 
ATOM   619  N N     . SER A 1 84  ? 7.900  11.813  17.337  1.00 24.73 ? 79  SER A N     1 
ATOM   620  C CA    . SER A 1 84  ? 8.011  12.312  18.705  1.00 27.42 ? 79  SER A CA    1 
ATOM   621  C C     . SER A 1 84  ? 8.223  11.162  19.682  1.00 22.23 ? 79  SER A C     1 
ATOM   622  O O     . SER A 1 84  ? 9.010  11.278  20.628  1.00 18.26 ? 79  SER A O     1 
ATOM   623  C CB    . SER A 1 84  ? 6.767  13.119  19.083  1.00 21.94 ? 79  SER A CB    1 
ATOM   624  O OG    . SER A 1 84  ? 5.611  12.300  19.130  1.00 20.88 ? 79  SER A OG    1 
ATOM   625  N N     . LYS A 1 85  ? 7.529  10.044  19.463  1.00 27.09 ? 80  LYS A N     1 
ATOM   626  C CA    . LYS A 1 85  ? 7.773  8.839   20.247  1.00 29.05 ? 80  LYS A CA    1 
ATOM   627  C C     . LYS A 1 85  ? 9.030  8.120   19.772  1.00 25.63 ? 80  LYS A C     1 
ATOM   628  O O     . LYS A 1 85  ? 9.774  7.559   20.584  1.00 23.86 ? 80  LYS A O     1 
ATOM   629  C CB    . LYS A 1 85  ? 6.568  7.898   20.162  1.00 20.73 ? 80  LYS A CB    1 
ATOM   630  C CG    . LYS A 1 85  ? 5.218  8.591   20.165  1.00 23.28 ? 80  LYS A CG    1 
ATOM   631  C CD    . LYS A 1 85  ? 4.117  7.654   20.641  1.00 29.54 ? 80  LYS A CD    1 
ATOM   632  C CE    . LYS A 1 85  ? 2.755  8.340   20.622  1.00 41.92 ? 80  LYS A CE    1 
ATOM   633  N NZ    . LYS A 1 85  ? 2.378  8.926   21.943  1.00 40.04 ? 80  LYS A NZ    1 
ATOM   634  N N     . LEU A 1 86  ? 9.280  8.140   18.458  1.00 25.05 ? 81  LEU A N     1 
ATOM   635  C CA    . LEU A 1 86  ? 10.369 7.357   17.882  1.00 25.07 ? 81  LEU A CA    1 
ATOM   636  C C     . LEU A 1 86  ? 11.736 7.904   18.278  1.00 24.24 ? 81  LEU A C     1 
ATOM   637  O O     . LEU A 1 86  ? 12.693 7.132   18.403  1.00 26.60 ? 81  LEU A O     1 
ATOM   638  C CB    . LEU A 1 86  ? 10.233 7.313   16.355  1.00 31.46 ? 81  LEU A CB    1 
ATOM   639  C CG    . LEU A 1 86  ? 10.886 6.160   15.579  1.00 27.83 ? 81  LEU A CG    1 
ATOM   640  C CD1   . LEU A 1 86  ? 10.163 4.842   15.832  1.00 23.06 ? 81  LEU A CD1   1 
ATOM   641  C CD2   . LEU A 1 86  ? 10.929 6.467   14.089  1.00 19.11 ? 81  LEU A CD2   1 
ATOM   642  N N     . GLN A 1 87  ? 11.853 9.219   18.482  1.00 25.57 ? 82  GLN A N     1 
ATOM   643  C CA    . GLN A 1 87  ? 13.130 9.794   18.896  1.00 26.37 ? 82  GLN A CA    1 
ATOM   644  C C     . GLN A 1 87  ? 13.578 9.285   20.260  1.00 21.85 ? 82  GLN A C     1 
ATOM   645  O O     . GLN A 1 87  ? 14.771 9.349   20.572  1.00 20.63 ? 82  GLN A O     1 
ATOM   646  C CB    . GLN A 1 87  ? 13.047 11.319  18.934  1.00 21.52 ? 82  GLN A CB    1 
ATOM   647  C CG    . GLN A 1 87  ? 12.116 11.860  20.004  1.00 21.45 ? 82  GLN A CG    1 
ATOM   648  C CD    . GLN A 1 87  ? 12.105 13.370  20.055  1.00 23.16 ? 82  GLN A CD    1 
ATOM   649  O OE1   . GLN A 1 87  ? 13.151 14.012  19.962  1.00 22.46 ? 82  GLN A OE1   1 
ATOM   650  N NE2   . GLN A 1 87  ? 10.915 13.951  20.190  1.00 26.92 ? 82  GLN A NE2   1 
ATOM   651  N N     . HIS A 1 88  ? 12.649 8.786   21.076  1.00 20.18 ? 83  HIS A N     1 
ATOM   652  C CA    . HIS A 1 88  ? 12.959 8.270   22.399  1.00 23.81 ? 83  HIS A CA    1 
ATOM   653  C C     . HIS A 1 88  ? 13.164 6.761   22.400  1.00 30.47 ? 83  HIS A C     1 
ATOM   654  O O     . HIS A 1 88  ? 13.081 6.129   23.460  1.00 34.10 ? 83  HIS A O     1 
ATOM   655  C CB    . HIS A 1 88  ? 11.860 8.671   23.382  1.00 23.18 ? 83  HIS A CB    1 
ATOM   656  C CG    . HIS A 1 88  ? 11.681 10.151  23.505  1.00 23.04 ? 83  HIS A CG    1 
ATOM   657  N ND1   . HIS A 1 88  ? 12.743 11.020  23.626  1.00 23.70 ? 83  HIS A ND1   1 
ATOM   658  C CD2   . HIS A 1 88  ? 10.566 10.918  23.509  1.00 21.63 ? 83  HIS A CD2   1 
ATOM   659  C CE1   . HIS A 1 88  ? 12.291 12.258  23.709  1.00 22.56 ? 83  HIS A CE1   1 
ATOM   660  N NE2   . HIS A 1 88  ? 10.973 12.224  23.642  1.00 21.24 ? 83  HIS A NE2   1 
ATOM   661  N N     . LEU A 1 89  ? 13.424 6.175   21.234  1.00 27.60 ? 84  LEU A N     1 
ATOM   662  C CA    . LEU A 1 89  ? 13.794 4.771   21.163  1.00 23.79 ? 84  LEU A CA    1 
ATOM   663  C C     . LEU A 1 89  ? 15.099 4.536   21.915  1.00 27.92 ? 84  LEU A C     1 
ATOM   664  O O     . LEU A 1 89  ? 15.960 5.416   22.009  1.00 28.38 ? 84  LEU A O     1 
ATOM   665  C CB    . LEU A 1 89  ? 13.953 4.330   19.706  1.00 33.61 ? 84  LEU A CB    1 
ATOM   666  C CG    . LEU A 1 89  ? 12.706 4.047   18.860  1.00 39.49 ? 84  LEU A CG    1 
ATOM   667  C CD1   . LEU A 1 89  ? 13.110 3.527   17.478  1.00 23.00 ? 84  LEU A CD1   1 
ATOM   668  C CD2   . LEU A 1 89  ? 11.751 3.083   19.559  1.00 28.45 ? 84  LEU A CD2   1 
ATOM   669  N N     . LYS A 1 90  ? 15.236 3.330   22.458  1.00 31.79 ? 85  LYS A N     1 
ATOM   670  C CA    . LYS A 1 90  ? 16.441 2.913   23.156  1.00 35.86 ? 85  LYS A CA    1 
ATOM   671  C C     . LYS A 1 90  ? 16.751 1.475   22.759  1.00 32.60 ? 85  LYS A C     1 
ATOM   672  O O     . LYS A 1 90  ? 15.952 0.807   22.095  1.00 30.28 ? 85  LYS A O     1 
ATOM   673  C CB    . LYS A 1 90  ? 16.281 3.072   24.676  1.00 36.15 ? 85  LYS A CB    1 
ATOM   674  C CG    . LYS A 1 90  ? 16.293 4.531   25.132  1.00 32.76 ? 85  LYS A CG    1 
ATOM   675  C CD    . LYS A 1 90  ? 15.166 4.844   26.109  1.00 46.76 ? 85  LYS A CD    1 
ATOM   676  C CE    . LYS A 1 90  ? 15.312 4.073   27.413  1.00 55.86 ? 85  LYS A CE    1 
ATOM   677  N NZ    . LYS A 1 90  ? 14.667 4.799   28.547  1.00 51.54 ? 85  LYS A NZ    1 
ATOM   678  N N     . LYS A 1 91  ? 17.936 1.003   23.143  1.00 30.99 ? 86  LYS A N     1 
ATOM   679  C CA    . LYS A 1 91  ? 18.311 -0.367  22.817  1.00 38.32 ? 86  LYS A CA    1 
ATOM   680  C C     . LYS A 1 91  ? 17.375 -1.346  23.513  1.00 36.70 ? 86  LYS A C     1 
ATOM   681  O O     . LYS A 1 91  ? 17.134 -1.245  24.720  1.00 28.95 ? 86  LYS A O     1 
ATOM   682  C CB    . LYS A 1 91  ? 19.765 -0.648  23.209  1.00 48.62 ? 86  LYS A CB    1 
ATOM   683  C CG    . LYS A 1 91  ? 20.808 0.060   22.349  1.00 34.47 ? 86  LYS A CG    1 
ATOM   684  C CD    . LYS A 1 91  ? 22.222 -0.167  22.874  1.00 29.86 ? 86  LYS A CD    1 
ATOM   685  C CE    . LYS A 1 91  ? 22.380 -1.556  23.483  1.00 35.55 ? 86  LYS A CE    1 
ATOM   686  N NZ    . LYS A 1 91  ? 23.780 -1.837  23.907  1.00 36.55 ? 86  LYS A NZ    1 
ATOM   687  N N     . GLY A 1 92  ? 16.839 -2.287  22.738  1.00 35.80 ? 87  GLY A N     1 
ATOM   688  C CA    . GLY A 1 92  ? 15.900 -3.267  23.232  1.00 30.90 ? 87  GLY A CA    1 
ATOM   689  C C     . GLY A 1 92  ? 14.453 -2.991  22.884  1.00 35.42 ? 87  GLY A C     1 
ATOM   690  O O     . GLY A 1 92  ? 13.608 -3.871  23.089  1.00 42.71 ? 87  GLY A O     1 
ATOM   691  N N     . ASP A 1 93  ? 14.142 -1.808  22.362  1.00 34.10 ? 88  ASP A N     1 
ATOM   692  C CA    . ASP A 1 93  ? 12.761 -1.443  22.093  1.00 34.85 ? 88  ASP A CA    1 
ATOM   693  C C     . ASP A 1 93  ? 12.250 -2.136  20.833  1.00 30.16 ? 88  ASP A C     1 
ATOM   694  O O     . ASP A 1 93  ? 13.017 -2.540  19.955  1.00 28.40 ? 88  ASP A O     1 
ATOM   695  C CB    . ASP A 1 93  ? 12.620 0.072   21.956  1.00 27.21 ? 88  ASP A CB    1 
ATOM   696  C CG    . ASP A 1 93  ? 12.537 0.768   23.297  1.00 30.80 ? 88  ASP A CG    1 
ATOM   697  O OD1   . ASP A 1 93  ? 12.823 0.117   24.326  1.00 36.90 ? 88  ASP A OD1   1 
ATOM   698  O OD2   . ASP A 1 93  ? 12.186 1.965   23.325  1.00 40.53 ? 88  ASP A OD2   1 
ATOM   699  N N     . GLN A 1 94  ? 10.932 -2.271  20.758  1.00 26.28 ? 89  GLN A N     1 
ATOM   700  C CA    . GLN A 1 94  ? 10.278 -2.946  19.647  1.00 29.59 ? 89  GLN A CA    1 
ATOM   701  C C     . GLN A 1 94  ? 9.703  -1.930  18.671  1.00 25.75 ? 89  GLN A C     1 
ATOM   702  O O     . GLN A 1 94  ? 9.208  -0.874  19.074  1.00 30.12 ? 89  GLN A O     1 
ATOM   703  C CB    . GLN A 1 94  ? 9.167  -3.871  20.148  1.00 30.49 ? 89  GLN A CB    1 
ATOM   704  C CG    . GLN A 1 94  ? 9.671  -5.099  20.895  1.00 35.82 ? 89  GLN A CG    1 
ATOM   705  C CD    . GLN A 1 94  ? 10.992 -5.617  20.353  1.00 32.97 ? 89  GLN A CD    1 
ATOM   706  O OE1   . GLN A 1 94  ? 12.051 -5.377  20.933  1.00 31.19 ? 89  GLN A OE1   1 
ATOM   707  N NE2   . GLN A 1 94  ? 10.933 -6.336  19.233  1.00 31.94 ? 89  GLN A NE2   1 
ATOM   708  N N     . ILE A 1 95  ? 9.795  -2.249  17.381  1.00 29.19 ? 90  ILE A N     1 
ATOM   709  C CA    . ILE A 1 95  ? 9.133  -1.503  16.322  1.00 28.64 ? 90  ILE A CA    1 
ATOM   710  C C     . ILE A 1 95  ? 8.448  -2.512  15.410  1.00 23.41 ? 90  ILE A C     1 
ATOM   711  O O     . ILE A 1 95  ? 8.705  -3.714  15.475  1.00 22.47 ? 90  ILE A O     1 
ATOM   712  C CB    . ILE A 1 95  ? 10.103 -0.611  15.515  1.00 24.60 ? 90  ILE A CB    1 
ATOM   713  C CG1   . ILE A 1 95  ? 11.040 -1.473  14.665  1.00 25.24 ? 90  ILE A CG1   1 
ATOM   714  C CG2   . ILE A 1 95  ? 10.895 0.312   16.436  1.00 24.40 ? 90  ILE A CG2   1 
ATOM   715  C CD1   . ILE A 1 95  ? 11.386 -0.863  13.334  1.00 21.72 ? 90  ILE A CD1   1 
ATOM   716  N N     . ILE A 1 96  ? 7.561  -2.009  14.556  1.00 32.87 ? 91  ILE A N     1 
ATOM   717  C CA    . ILE A 1 96  ? 6.882  -2.827  13.559  1.00 31.73 ? 91  ILE A CA    1 
ATOM   718  C C     . ILE A 1 96  ? 7.328  -2.375  12.177  1.00 27.35 ? 91  ILE A C     1 
ATOM   719  O O     . ILE A 1 96  ? 7.552  -1.182  11.941  1.00 23.44 ? 91  ILE A O     1 
ATOM   720  C CB    . ILE A 1 96  ? 5.346  -2.763  13.703  1.00 32.47 ? 91  ILE A CB    1 
ATOM   721  C CG1   . ILE A 1 96  ? 4.819  -1.350  13.444  1.00 26.17 ? 91  ILE A CG1   1 
ATOM   722  C CG2   . ILE A 1 96  ? 4.920  -3.248  15.087  1.00 33.72 ? 91  ILE A CG2   1 
ATOM   723  C CD1   . ILE A 1 96  ? 3.441  -1.093  14.022  1.00 24.06 ? 91  ILE A CD1   1 
ATOM   724  N N     . VAL A 1 97  ? 7.491  -3.339  11.275  1.00 32.78 ? 92  VAL A N     1 
ATOM   725  C CA    . VAL A 1 97  ? 7.893  -3.094  9.896   1.00 30.75 ? 92  VAL A CA    1 
ATOM   726  C C     . VAL A 1 97  ? 6.965  -3.899  8.998   1.00 29.18 ? 92  VAL A C     1 
ATOM   727  O O     . VAL A 1 97  ? 6.785  -5.104  9.210   1.00 32.20 ? 92  VAL A O     1 
ATOM   728  C CB    . VAL A 1 97  ? 9.363  -3.489  9.641   1.00 34.42 ? 92  VAL A CB    1 
ATOM   729  C CG1   . VAL A 1 97  ? 9.784  -3.113  8.233   1.00 30.31 ? 92  VAL A CG1   1 
ATOM   730  C CG2   . VAL A 1 97  ? 10.286 -2.857  10.665  1.00 27.67 ? 92  VAL A CG2   1 
ATOM   731  N N     . SER A 1 98  ? 6.376  -3.241  8.004   1.00 32.14 ? 93  SER A N     1 
ATOM   732  C CA    . SER A 1 98  ? 5.488  -3.946  7.093   1.00 28.59 ? 93  SER A CA    1 
ATOM   733  C C     . SER A 1 98  ? 6.270  -4.957  6.259   1.00 23.37 ? 93  SER A C     1 
ATOM   734  O O     . SER A 1 98  ? 7.496  -4.892  6.137   1.00 27.94 ? 93  SER A O     1 
ATOM   735  C CB    . SER A 1 98  ? 4.751  -2.961  6.189   1.00 31.88 ? 93  SER A CB    1 
ATOM   736  O OG    . SER A 1 98  ? 5.647  -2.259  5.347   1.00 28.75 ? 93  SER A OG    1 
ATOM   737  N N     . LYS A 1 99  ? 5.540  -5.907  5.683   1.00 29.05 ? 94  LYS A N     1 
ATOM   738  C CA    . LYS A 1 99  ? 6.146  -7.064  5.039   1.00 28.87 ? 94  LYS A CA    1 
ATOM   739  C C     . LYS A 1 99  ? 6.122  -6.997  3.517   1.00 28.05 ? 94  LYS A C     1 
ATOM   740  O O     . LYS A 1 99  ? 6.612  -7.922  2.865   1.00 30.18 ? 94  LYS A O     1 
ATOM   741  C CB    . LYS A 1 99  ? 5.450  -8.344  5.512   1.00 26.01 ? 94  LYS A CB    1 
ATOM   742  C CG    . LYS A 1 99  ? 5.647  -8.631  6.989   1.00 30.57 ? 94  LYS A CG    1 
ATOM   743  C CD    . LYS A 1 99  ? 5.649  -10.124 7.283   1.00 34.22 ? 94  LYS A CD    1 
ATOM   744  C CE    . LYS A 1 99  ? 4.254  -10.652 7.559   1.00 35.99 ? 94  LYS A CE    1 
ATOM   745  N NZ    . LYS A 1 99  ? 4.318  -11.911 8.353   1.00 39.45 ? 94  LYS A NZ    1 
ATOM   746  N N     . LYS A 1 100 ? 5.578  -5.926  2.937   1.00 28.28 ? 95  LYS A N     1 
ATOM   747  C CA    . LYS A 1 100 ? 5.415  -5.782  1.490   1.00 25.52 ? 95  LYS A CA    1 
ATOM   748  C C     . LYS A 1 100 ? 6.155  -4.529  1.043   1.00 24.73 ? 95  LYS A C     1 
ATOM   749  O O     . LYS A 1 100 ? 5.609  -3.417  1.108   1.00 24.27 ? 95  LYS A O     1 
ATOM   750  C CB    . LYS A 1 100 ? 3.932  -5.716  1.124   1.00 28.49 ? 95  LYS A CB    1 
ATOM   751  C CG    . LYS A 1 100 ? 3.609  -5.333  -0.312  1.00 21.59 ? 95  LYS A CG    1 
ATOM   752  C CD    . LYS A 1 100 ? 3.556  -6.536  -1.230  1.00 31.08 ? 95  LYS A CD    1 
ATOM   753  C CE    . LYS A 1 100 ? 3.787  -6.124  -2.674  1.00 33.01 ? 95  LYS A CE    1 
ATOM   754  N NZ    . LYS A 1 100 ? 5.216  -5.833  -2.960  1.00 28.37 ? 95  LYS A NZ    1 
ATOM   755  N N     . PRO A 1 101 ? 7.406  -4.654  0.601   1.00 29.23 ? 96  PRO A N     1 
ATOM   756  C CA    . PRO A 1 101 ? 8.146  -3.471  0.150   1.00 17.66 ? 96  PRO A CA    1 
ATOM   757  C C     . PRO A 1 101 ? 7.568  -2.915  -1.141  1.00 23.74 ? 96  PRO A C     1 
ATOM   758  O O     . PRO A 1 101 ? 6.943  -3.627  -1.929  1.00 23.18 ? 96  PRO A O     1 
ATOM   759  C CB    . PRO A 1 101 ? 9.575  -3.992  -0.057  1.00 15.76 ? 96  PRO A CB    1 
ATOM   760  C CG    . PRO A 1 101 ? 9.607  -5.353  0.558   1.00 17.26 ? 96  PRO A CG    1 
ATOM   761  C CD    . PRO A 1 101 ? 8.216  -5.879  0.530   1.00 21.20 ? 96  PRO A CD    1 
ATOM   762  N N     . VAL A 1 102 ? 7.778  -1.616  -1.344  1.00 25.56 ? 97  VAL A N     1 
ATOM   763  C CA    . VAL A 1 102 ? 7.283  -0.927  -2.530  1.00 22.86 ? 97  VAL A CA    1 
ATOM   764  C C     . VAL A 1 102 ? 8.163  0.294   -2.747  1.00 20.02 ? 97  VAL A C     1 
ATOM   765  O O     . VAL A 1 102 ? 8.828  0.768   -1.827  1.00 19.91 ? 97  VAL A O     1 
ATOM   766  C CB    . VAL A 1 102 ? 5.786  -0.554  -2.365  1.00 26.33 ? 97  VAL A CB    1 
ATOM   767  C CG1   . VAL A 1 102 ? 5.594  0.438   -1.221  1.00 20.66 ? 97  VAL A CG1   1 
ATOM   768  C CG2   . VAL A 1 102 ? 5.189  -0.040  -3.679  1.00 21.05 ? 97  VAL A CG2   1 
ATOM   769  N N     . GLY A 1 103 ? 8.200  0.782   -3.978  1.00 20.68 ? 98  GLY A N     1 
ATOM   770  C CA    . GLY A 1 103 ? 8.966  1.967   -4.299  1.00 18.78 ? 98  GLY A CA    1 
ATOM   771  C C     . GLY A 1 103 ? 9.277  2.051   -5.773  1.00 18.85 ? 98  GLY A C     1 
ATOM   772  O O     . GLY A 1 103 ? 9.177  1.077   -6.521  1.00 19.43 ? 98  GLY A O     1 
ATOM   773  N N     . THR A 1 104 ? 9.670  3.256   -6.193  1.00 30.30 ? 99  THR A N     1 
ATOM   774  C CA    . THR A 1 104 ? 10.019 3.546   -7.578  1.00 20.73 ? 99  THR A CA    1 
ATOM   775  C C     . THR A 1 104 ? 11.517 3.552   -7.834  1.00 18.54 ? 99  THR A C     1 
ATOM   776  O O     . THR A 1 104 ? 11.927 3.481   -8.997  1.00 18.70 ? 99  THR A O     1 
ATOM   777  C CB    . THR A 1 104 ? 9.452  4.910   -7.997  1.00 19.24 ? 99  THR A CB    1 
ATOM   778  O OG1   . THR A 1 104 ? 9.976  5.930   -7.136  1.00 18.39 ? 99  THR A OG1   1 
ATOM   779  C CG2   . THR A 1 104 ? 7.939  4.920   -7.906  1.00 17.34 ? 99  THR A CG2   1 
ATOM   780  N N     . LEU A 1 105 ? 12.338 3.635   -6.785  1.00 21.64 ? 100 LEU A N     1 
ATOM   781  C CA    . LEU A 1 105 ? 13.781 3.812   -6.936  1.00 21.04 ? 100 LEU A CA    1 
ATOM   782  C C     . LEU A 1 105 ? 14.481 2.506   -7.294  1.00 15.81 ? 100 LEU A C     1 
ATOM   783  O O     . LEU A 1 105 ? 15.451 2.105   -6.642  1.00 17.63 ? 100 LEU A O     1 
ATOM   784  C CB    . LEU A 1 105 ? 14.364 4.413   -5.655  1.00 19.96 ? 100 LEU A CB    1 
ATOM   785  C CG    . LEU A 1 105 ? 13.830 5.810   -5.351  1.00 17.04 ? 100 LEU A CG    1 
ATOM   786  C CD1   . LEU A 1 105 ? 14.443 6.354   -4.076  1.00 18.44 ? 100 LEU A CD1   1 
ATOM   787  C CD2   . LEU A 1 105 ? 14.127 6.721   -6.522  1.00 17.85 ? 100 LEU A CD2   1 
ATOM   788  N N     . LEU A 1 106 ? 14.010 1.854   -8.353  1.00 22.30 ? 101 LEU A N     1 
ATOM   789  C CA    . LEU A 1 106 ? 14.523 0.561   -8.781  1.00 23.63 ? 101 LEU A CA    1 
ATOM   790  C C     . LEU A 1 106 ? 15.400 0.726   -10.019 1.00 19.44 ? 101 LEU A C     1 
ATOM   791  O O     . LEU A 1 106 ? 15.122 1.569   -10.877 1.00 21.84 ? 101 LEU A O     1 
ATOM   792  C CB    . LEU A 1 106 ? 13.366 -0.405  -9.069  1.00 23.15 ? 101 LEU A CB    1 
ATOM   793  C CG    . LEU A 1 106 ? 12.370 -0.634  -7.923  1.00 18.59 ? 101 LEU A CG    1 
ATOM   794  C CD1   . LEU A 1 106 ? 11.273 -1.585  -8.351  1.00 16.50 ? 101 LEU A CD1   1 
ATOM   795  C CD2   . LEU A 1 106 ? 13.057 -1.158  -6.679  1.00 16.78 ? 101 LEU A CD2   1 
ATOM   796  N N     . TYR A 1 107 ? 16.471 -0.076  -10.098 1.00 24.33 ? 102 TYR A N     1 
ATOM   797  C CA    . TYR A 1 107 ? 17.328 -0.048  -11.283 1.00 24.67 ? 102 TYR A CA    1 
ATOM   798  C C     . TYR A 1 107 ? 16.538 -0.386  -12.539 1.00 24.57 ? 102 TYR A C     1 
ATOM   799  O O     . TYR A 1 107 ? 16.797 0.171   -13.612 1.00 25.02 ? 102 TYR A O     1 
ATOM   800  C CB    . TYR A 1 107 ? 18.496 -1.028  -11.144 1.00 19.57 ? 102 TYR A CB    1 
ATOM   801  C CG    . TYR A 1 107 ? 19.285 -0.936  -9.861  1.00 28.22 ? 102 TYR A CG    1 
ATOM   802  C CD1   . TYR A 1 107 ? 19.781 0.279   -9.405  1.00 24.85 ? 102 TYR A CD1   1 
ATOM   803  C CD2   . TYR A 1 107 ? 19.549 -2.076  -9.110  1.00 30.75 ? 102 TYR A CD2   1 
ATOM   804  C CE1   . TYR A 1 107 ? 20.506 0.359   -8.230  1.00 21.31 ? 102 TYR A CE1   1 
ATOM   805  C CE2   . TYR A 1 107 ? 20.270 -2.007  -7.938  1.00 25.00 ? 102 TYR A CE2   1 
ATOM   806  C CZ    . TYR A 1 107 ? 20.747 -0.788  -7.502  1.00 26.09 ? 102 TYR A CZ    1 
ATOM   807  O OH    . TYR A 1 107 ? 21.466 -0.719  -6.333  1.00 29.14 ? 102 TYR A OH    1 
ATOM   808  N N     . ASP A 1 108 ? 15.574 -1.305  -12.426 1.00 28.00 ? 103 ASP A N     1 
ATOM   809  C CA    . ASP A 1 108 ? 14.864 -1.803  -13.598 1.00 29.59 ? 103 ASP A CA    1 
ATOM   810  C C     . ASP A 1 108 ? 13.916 -0.769  -14.192 1.00 26.73 ? 103 ASP A C     1 
ATOM   811  O O     . ASP A 1 108 ? 13.518 -0.909  -15.354 1.00 28.66 ? 103 ASP A O     1 
ATOM   812  C CB    . ASP A 1 108 ? 14.109 -3.084  -13.237 1.00 30.47 ? 103 ASP A CB    1 
ATOM   813  C CG    . ASP A 1 108 ? 15.044 -4.232  -12.888 1.00 35.53 ? 103 ASP A CG    1 
ATOM   814  O OD1   . ASP A 1 108 ? 16.191 -4.236  -13.386 1.00 35.24 ? 103 ASP A OD1   1 
ATOM   815  O OD2   . ASP A 1 108 ? 14.638 -5.129  -12.118 1.00 30.50 ? 103 ASP A OD2   1 
ATOM   816  N N     . ASN A 1 109 ? 13.549 0.262   -13.430 1.00 26.00 ? 104 ASN A N     1 
ATOM   817  C CA    . ASN A 1 109 ? 12.786 1.380   -13.970 1.00 22.67 ? 104 ASN A CA    1 
ATOM   818  C C     . ASN A 1 109 ? 13.647 2.341   -14.779 1.00 21.36 ? 104 ASN A C     1 
ATOM   819  O O     . ASN A 1 109 ? 13.113 3.311   -15.328 1.00 18.38 ? 104 ASN A O     1 
ATOM   820  C CB    . ASN A 1 109 ? 12.087 2.145   -12.841 1.00 21.45 ? 104 ASN A CB    1 
ATOM   821  C CG    . ASN A 1 109 ? 11.098 1.288   -12.072 1.00 20.22 ? 104 ASN A CG    1 
ATOM   822  O OD1   . ASN A 1 109 ? 10.859 0.130   -12.416 1.00 21.49 ? 104 ASN A OD1   1 
ATOM   823  N ND2   . ASN A 1 109 ? 10.506 1.862   -11.031 1.00 21.89 ? 104 ASN A ND2   1 
ATOM   824  N N     . LEU A 1 110 ? 14.956 2.097   -14.856 1.00 27.57 ? 105 LEU A N     1 
ATOM   825  C CA    . LEU A 1 110 ? 15.898 2.939   -15.583 1.00 25.59 ? 105 LEU A CA    1 
ATOM   826  C C     . LEU A 1 110 ? 16.519 2.158   -16.731 1.00 24.65 ? 105 LEU A C     1 
ATOM   827  O O     . LEU A 1 110 ? 16.771 0.955   -16.613 1.00 31.86 ? 105 LEU A O     1 
ATOM   828  C CB    . LEU A 1 110 ? 17.022 3.455   -14.678 1.00 22.13 ? 105 LEU A CB    1 
ATOM   829  C CG    . LEU A 1 110 ? 16.731 4.423   -13.532 1.00 20.41 ? 105 LEU A CG    1 
ATOM   830  C CD1   . LEU A 1 110 ? 18.022 4.712   -12.800 1.00 19.20 ? 105 LEU A CD1   1 
ATOM   831  C CD2   . LEU A 1 110 ? 16.117 5.710   -14.046 1.00 20.32 ? 105 LEU A CD2   1 
ATOM   832  N N     . LYS A 1 111 ? 16.783 2.854   -17.830 1.00 27.30 ? 106 LYS A N     1 
ATOM   833  C CA    . LYS A 1 111 ? 17.442 2.235   -18.962 1.00 30.32 ? 106 LYS A CA    1 
ATOM   834  C C     . LYS A 1 111 ? 18.918 2.004   -18.641 1.00 29.60 ? 106 LYS A C     1 
ATOM   835  O O     . LYS A 1 111 ? 19.487 2.683   -17.782 1.00 23.46 ? 106 LYS A O     1 
ATOM   836  C CB    . LYS A 1 111 ? 17.288 3.111   -20.202 1.00 24.33 ? 106 LYS A CB    1 
ATOM   837  C CG    . LYS A 1 111 ? 15.859 3.189   -20.707 1.00 20.30 ? 106 LYS A CG    1 
ATOM   838  C CD    . LYS A 1 111 ? 15.797 3.667   -22.142 1.00 30.64 ? 106 LYS A CD    1 
ATOM   839  C CE    . LYS A 1 111 ? 16.449 5.028   -22.281 1.00 29.30 ? 106 LYS A CE    1 
ATOM   840  N NZ    . LYS A 1 111 ? 15.892 5.822   -23.412 1.00 20.57 ? 106 LYS A NZ    1 
ATOM   841  N N     . PRO A 1 112 ? 19.552 1.028   -19.297 1.00 37.37 ? 107 PRO A N     1 
ATOM   842  C CA    . PRO A 1 112 ? 20.990 0.817   -19.083 1.00 30.46 ? 107 PRO A CA    1 
ATOM   843  C C     . PRO A 1 112 ? 21.786 2.057   -19.460 1.00 27.27 ? 107 PRO A C     1 
ATOM   844  O O     . PRO A 1 112 ? 21.504 2.718   -20.462 1.00 23.90 ? 107 PRO A O     1 
ATOM   845  C CB    . PRO A 1 112 ? 21.324 -0.372  -19.994 1.00 29.20 ? 107 PRO A CB    1 
ATOM   846  C CG    . PRO A 1 112 ? 20.167 -0.517  -20.926 1.00 24.16 ? 107 PRO A CG    1 
ATOM   847  C CD    . PRO A 1 112 ? 18.971 0.050   -20.235 1.00 23.19 ? 107 PRO A CD    1 
ATOM   848  N N     . GLY A 1 113 ? 22.780 2.378   -18.632 1.00 31.75 ? 108 GLY A N     1 
ATOM   849  C CA    . GLY A 1 113 ? 23.560 3.581   -18.822 1.00 32.69 ? 108 GLY A CA    1 
ATOM   850  C C     . GLY A 1 113 ? 24.952 3.464   -18.238 1.00 22.93 ? 108 GLY A C     1 
ATOM   851  O O     . GLY A 1 113 ? 25.315 2.463   -17.616 1.00 26.19 ? 108 GLY A O     1 
ATOM   852  N N     . LYS A 1 114 ? 25.732 4.524   -18.447 1.00 26.14 ? 109 LYS A N     1 
ATOM   853  C CA    . LYS A 1 114 ? 27.118 4.594   -18.001 1.00 27.51 ? 109 LYS A CA    1 
ATOM   854  C C     . LYS A 1 114 ? 27.259 5.286   -16.650 1.00 26.21 ? 109 LYS A C     1 
ATOM   855  O O     . LYS A 1 114 ? 28.193 4.981   -15.897 1.00 21.00 ? 109 LYS A O     1 
ATOM   856  C CB    . LYS A 1 114 ? 27.949 5.317   -19.071 1.00 28.58 ? 109 LYS A CB    1 
ATOM   857  C CG    . LYS A 1 114 ? 29.424 5.539   -18.767 1.00 27.31 ? 109 LYS A CG    1 
ATOM   858  C CD    . LYS A 1 114 ? 30.132 6.107   -19.999 1.00 28.90 ? 109 LYS A CD    1 
ATOM   859  C CE    . LYS A 1 114 ? 31.397 6.876   -19.644 1.00 29.18 ? 109 LYS A CE    1 
ATOM   860  N NZ    . LYS A 1 114 ? 31.895 7.694   -20.787 1.00 17.95 ? 109 LYS A NZ    1 
ATOM   861  N N     . HIS A 1 115 ? 26.333 6.190   -16.320 1.00 27.98 ? 110 HIS A N     1 
ATOM   862  C CA    . HIS A 1 115 ? 26.348 6.954   -15.080 1.00 27.49 ? 110 HIS A CA    1 
ATOM   863  C C     . HIS A 1 115 ? 25.029 6.782   -14.336 1.00 20.08 ? 110 HIS A C     1 
ATOM   864  O O     . HIS A 1 115 ? 23.986 6.523   -14.941 1.00 21.49 ? 110 HIS A O     1 
ATOM   865  C CB    . HIS A 1 115 ? 26.591 8.448   -15.348 1.00 24.02 ? 110 HIS A CB    1 
ATOM   866  C CG    . HIS A 1 115 ? 27.934 8.749   -15.942 1.00 21.08 ? 110 HIS A CG    1 
ATOM   867  N ND1   . HIS A 1 115 ? 28.172 9.868   -16.710 1.00 16.91 ? 110 HIS A ND1   1 
ATOM   868  C CD2   . HIS A 1 115 ? 29.114 8.091   -15.862 1.00 20.23 ? 110 HIS A CD2   1 
ATOM   869  C CE1   . HIS A 1 115 ? 29.437 9.879   -17.086 1.00 18.00 ? 110 HIS A CE1   1 
ATOM   870  N NE2   . HIS A 1 115 ? 30.031 8.812   -16.584 1.00 17.66 ? 110 HIS A NE2   1 
ATOM   871  N N     . LEU A 1 116 ? 25.085 6.927   -13.013 1.00 22.46 ? 111 LEU A N     1 
ATOM   872  C CA    . LEU A 1 116 ? 23.884 6.978   -12.181 1.00 22.38 ? 111 LEU A CA    1 
ATOM   873  C C     . LEU A 1 116 ? 24.055 8.085   -11.151 1.00 20.61 ? 111 LEU A C     1 
ATOM   874  O O     . LEU A 1 116 ? 24.905 7.985   -10.260 1.00 17.31 ? 111 LEU A O     1 
ATOM   875  C CB    . LEU A 1 116 ? 23.601 5.645   -11.491 1.00 22.27 ? 111 LEU A CB    1 
ATOM   876  C CG    . LEU A 1 116 ? 22.329 5.696   -10.638 1.00 16.05 ? 111 LEU A CG    1 
ATOM   877  C CD1   . LEU A 1 116 ? 21.125 5.987   -11.509 1.00 16.24 ? 111 LEU A CD1   1 
ATOM   878  C CD2   . LEU A 1 116 ? 22.122 4.416   -9.854  1.00 15.83 ? 111 LEU A CD2   1 
ATOM   879  N N     . TRP A 1 117 ? 23.237 9.125   -11.265 1.00 21.82 ? 112 TRP A N     1 
ATOM   880  C CA    . TRP A 1 117 ? 23.271 10.263  -10.356 1.00 23.40 ? 112 TRP A CA    1 
ATOM   881  C C     . TRP A 1 117 ? 22.198 10.067  -9.287  1.00 20.38 ? 112 TRP A C     1 
ATOM   882  O O     . TRP A 1 117 ? 21.001 10.050  -9.593  1.00 19.65 ? 112 TRP A O     1 
ATOM   883  C CB    . TRP A 1 117 ? 23.074 11.570  -11.123 1.00 20.24 ? 112 TRP A CB    1 
ATOM   884  C CG    . TRP A 1 117 ? 24.129 11.800  -12.176 1.00 24.33 ? 112 TRP A CG    1 
ATOM   885  C CD1   . TRP A 1 117 ? 24.154 11.280  -13.441 1.00 26.11 ? 112 TRP A CD1   1 
ATOM   886  C CD2   . TRP A 1 117 ? 25.310 12.607  -12.055 1.00 22.64 ? 112 TRP A CD2   1 
ATOM   887  N NE1   . TRP A 1 117 ? 25.275 11.711  -14.110 1.00 18.33 ? 112 TRP A NE1   1 
ATOM   888  C CE2   . TRP A 1 117 ? 26.000 12.527  -13.283 1.00 20.06 ? 112 TRP A CE2   1 
ATOM   889  C CE3   . TRP A 1 117 ? 25.851 13.391  -11.029 1.00 20.41 ? 112 TRP A CE3   1 
ATOM   890  C CZ2   . TRP A 1 117 ? 27.202 13.199  -13.511 1.00 22.09 ? 112 TRP A CZ2   1 
ATOM   891  C CZ3   . TRP A 1 117 ? 27.046 14.060  -11.261 1.00 16.95 ? 112 TRP A CZ3   1 
ATOM   892  C CH2   . TRP A 1 117 ? 27.706 13.957  -12.490 1.00 19.79 ? 112 TRP A CH2   1 
ATOM   893  N N     . LEU A 1 118 ? 22.636 9.900   -8.038  1.00 21.17 ? 113 LEU A N     1 
ATOM   894  C CA    . LEU A 1 118 ? 21.749 9.815   -6.877  1.00 18.21 ? 113 LEU A CA    1 
ATOM   895  C C     . LEU A 1 118 ? 21.696 11.195  -6.229  1.00 14.64 ? 113 LEU A C     1 
ATOM   896  O O     . LEU A 1 118 ? 22.632 11.605  -5.538  1.00 17.25 ? 113 LEU A O     1 
ATOM   897  C CB    . LEU A 1 118 ? 22.236 8.756   -5.893  1.00 18.11 ? 113 LEU A CB    1 
ATOM   898  C CG    . LEU A 1 118 ? 22.534 7.353   -6.431  1.00 17.31 ? 113 LEU A CG    1 
ATOM   899  C CD1   . LEU A 1 118 ? 23.144 6.489   -5.344  1.00 15.29 ? 113 LEU A CD1   1 
ATOM   900  C CD2   . LEU A 1 118 ? 21.281 6.696   -6.991  1.00 16.87 ? 113 LEU A CD2   1 
ATOM   901  N N     . LEU A 1 119 ? 20.595 11.909  -6.450  1.00 21.33 ? 114 LEU A N     1 
ATOM   902  C CA    . LEU A 1 119 ? 20.426 13.282  -5.989  1.00 20.35 ? 114 LEU A CA    1 
ATOM   903  C C     . LEU A 1 119 ? 19.470 13.280  -4.807  1.00 13.36 ? 114 LEU A C     1 
ATOM   904  O O     . LEU A 1 119 ? 18.320 12.850  -4.937  1.00 15.66 ? 114 LEU A O     1 
ATOM   905  C CB    . LEU A 1 119 ? 19.897 14.173  -7.115  1.00 20.05 ? 114 LEU A CB    1 
ATOM   906  C CG    . LEU A 1 119 ? 20.606 14.051  -8.469  1.00 15.04 ? 114 LEU A CG    1 
ATOM   907  C CD1   . LEU A 1 119 ? 19.862 14.839  -9.529  1.00 20.60 ? 114 LEU A CD1   1 
ATOM   908  C CD2   . LEU A 1 119 ? 22.053 14.503  -8.378  1.00 14.88 ? 114 LEU A CD2   1 
ATOM   909  N N     . SER A 1 120 ? 19.943 13.758  -3.658  1.00 15.91 ? 115 SER A N     1 
ATOM   910  C CA    . SER A 1 120 ? 19.143 13.724  -2.445  1.00 17.05 ? 115 SER A CA    1 
ATOM   911  C C     . SER A 1 120 ? 19.332 15.003  -1.647  1.00 14.58 ? 115 SER A C     1 
ATOM   912  O O     . SER A 1 120 ? 20.386 15.643  -1.704  1.00 16.35 ? 115 SER A O     1 
ATOM   913  C CB    . SER A 1 120 ? 19.493 12.511  -1.560  1.00 18.81 ? 115 SER A CB    1 
ATOM   914  O OG    . SER A 1 120 ? 20.839 12.549  -1.106  1.00 19.03 ? 115 SER A OG    1 
ATOM   915  N N     . THR A 1 121 ? 18.285 15.369  -0.910  1.00 18.41 ? 116 THR A N     1 
ATOM   916  C CA    . THR A 1 121 ? 18.361 16.339  0.172   1.00 16.14 ? 116 THR A CA    1 
ATOM   917  C C     . THR A 1 121 ? 17.853 15.704  1.459   1.00 13.40 ? 116 THR A C     1 
ATOM   918  O O     . THR A 1 121 ? 16.963 14.847  1.436   1.00 14.12 ? 116 THR A O     1 
ATOM   919  C CB    . THR A 1 121 ? 17.541 17.605  -0.119  1.00 11.84 ? 116 THR A CB    1 
ATOM   920  O OG1   . THR A 1 121 ? 16.149 17.269  -0.167  1.00 15.46 ? 116 THR A OG1   1 
ATOM   921  C CG2   . THR A 1 121 ? 17.973 18.250  -1.427  1.00 12.69 ? 116 THR A CG2   1 
ATOM   922  N N     . GLY A 1 122 ? 18.441 16.126  2.576   1.00 13.24 ? 117 GLY A N     1 
ATOM   923  C CA    . GLY A 1 122 ? 17.944 15.754  3.892   1.00 10.65 ? 117 GLY A CA    1 
ATOM   924  C C     . GLY A 1 122 ? 17.917 14.255  4.109   1.00 11.27 ? 117 GLY A C     1 
ATOM   925  O O     . GLY A 1 122 ? 18.931 13.561  3.983   1.00 14.42 ? 117 GLY A O     1 
ATOM   926  N N     . THR A 1 123 ? 16.740 13.741  4.456   1.00 13.26 ? 118 THR A N     1 
ATOM   927  C CA    . THR A 1 123 ? 16.567 12.315  4.680   1.00 13.61 ? 118 THR A CA    1 
ATOM   928  C C     . THR A 1 123 ? 16.379 11.532  3.387   1.00 17.32 ? 118 THR A C     1 
ATOM   929  O O     . THR A 1 123 ? 16.294 10.300  3.440   1.00 16.75 ? 118 THR A O     1 
ATOM   930  C CB    . THR A 1 123 ? 15.376 12.062  5.617   1.00 20.26 ? 118 THR A CB    1 
ATOM   931  O OG1   . THR A 1 123 ? 14.195 12.690  5.095   1.00 20.04 ? 118 THR A OG1   1 
ATOM   932  C CG2   . THR A 1 123 ? 15.669 12.597  7.017   1.00 16.11 ? 118 THR A CG2   1 
ATOM   933  N N     . GLY A 1 124 ? 16.314 12.210  2.238   1.00 17.02 ? 119 GLY A N     1 
ATOM   934  C CA    . GLY A 1 124 ? 16.284 11.531  0.951   1.00 14.69 ? 119 GLY A CA    1 
ATOM   935  C C     . GLY A 1 124 ? 17.551 10.764  0.628   1.00 13.13 ? 119 GLY A C     1 
ATOM   936  O O     . GLY A 1 124 ? 17.567 10.012  -0.355  1.00 12.74 ? 119 GLY A O     1 
ATOM   937  N N     . LEU A 1 125 ? 18.611 10.951  1.423   1.00 15.56 ? 120 LEU A N     1 
ATOM   938  C CA    . LEU A 1 125 ? 19.803 10.119  1.308   1.00 17.17 ? 120 LEU A CA    1 
ATOM   939  C C     . LEU A 1 125 ? 19.494 8.657   1.616   1.00 12.88 ? 120 LEU A C     1 
ATOM   940  O O     . LEU A 1 125 ? 20.189 7.759   1.127   1.00 10.49 ? 120 LEU A O     1 
ATOM   941  C CB    . LEU A 1 125 ? 20.884 10.645  2.259   1.00 14.83 ? 120 LEU A CB    1 
ATOM   942  C CG    . LEU A 1 125 ? 22.270 9.991   2.358   1.00 10.47 ? 120 LEU A CG    1 
ATOM   943  C CD1   . LEU A 1 125 ? 23.066 10.144  1.071   1.00 10.36 ? 120 LEU A CD1   1 
ATOM   944  C CD2   . LEU A 1 125 ? 23.032 10.538  3.560   1.00 11.85 ? 120 LEU A CD2   1 
ATOM   945  N N     . ALA A 1 126 ? 18.439 8.411   2.400   1.00 14.21 ? 121 ALA A N     1 
ATOM   946  C CA    . ALA A 1 126 ? 18.199 7.094   2.993   1.00 13.70 ? 121 ALA A CA    1 
ATOM   947  C C     . ALA A 1 126 ? 18.032 5.974   1.973   1.00 12.44 ? 121 ALA A C     1 
ATOM   948  O O     . ALA A 1 126 ? 18.657 4.914   2.153   1.00 10.57 ? 121 ALA A O     1 
ATOM   949  C CB    . ALA A 1 126 ? 16.993 7.173   3.937   1.00 12.96 ? 121 ALA A CB    1 
ATOM   950  N N     . PRO A 1 127 ? 17.225 6.106   0.915   1.00 12.78 ? 122 PRO A N     1 
ATOM   951  C CA    . PRO A 1 127 ? 17.162 5.009   -0.064  1.00 17.04 ? 122 PRO A CA    1 
ATOM   952  C C     . PRO A 1 127 ? 18.478 4.773   -0.785  1.00 17.23 ? 122 PRO A C     1 
ATOM   953  O O     . PRO A 1 127 ? 18.753 3.642   -1.205  1.00 15.02 ? 122 PRO A O     1 
ATOM   954  C CB    . PRO A 1 127 ? 16.060 5.466   -1.027  1.00 16.63 ? 122 PRO A CB    1 
ATOM   955  C CG    . PRO A 1 127 ? 16.057 6.946   -0.909  1.00 12.15 ? 122 PRO A CG    1 
ATOM   956  C CD    . PRO A 1 127 ? 16.316 7.205   0.541   1.00 10.57 ? 122 PRO A CD    1 
ATOM   957  N N     . PHE A 1 128 ? 19.308 5.809   -0.928  1.00 18.83 ? 123 PHE A N     1 
ATOM   958  C CA    . PHE A 1 128 ? 20.599 5.684   -1.591  1.00 17.22 ? 123 PHE A CA    1 
ATOM   959  C C     . PHE A 1 128 ? 21.674 5.100   -0.683  1.00 16.62 ? 123 PHE A C     1 
ATOM   960  O O     . PHE A 1 128 ? 22.726 4.688   -1.182  1.00 18.10 ? 123 PHE A O     1 
ATOM   961  C CB    . PHE A 1 128 ? 21.050 7.049   -2.119  1.00 18.78 ? 123 PHE A CB    1 
ATOM   962  C CG    . PHE A 1 128 ? 20.090 7.666   -3.101  1.00 20.92 ? 123 PHE A CG    1 
ATOM   963  C CD1   . PHE A 1 128 ? 19.372 6.874   -3.983  1.00 17.92 ? 123 PHE A CD1   1 
ATOM   964  C CD2   . PHE A 1 128 ? 19.918 9.045   -3.151  1.00 22.12 ? 123 PHE A CD2   1 
ATOM   965  C CE1   . PHE A 1 128 ? 18.486 7.441   -4.887  1.00 19.51 ? 123 PHE A CE1   1 
ATOM   966  C CE2   . PHE A 1 128 ? 19.033 9.620   -4.060  1.00 19.40 ? 123 PHE A CE2   1 
ATOM   967  C CZ    . PHE A 1 128 ? 18.319 8.815   -4.928  1.00 17.36 ? 123 PHE A CZ    1 
ATOM   968  N N     . LEU A 1 129 ? 21.443 5.071   0.632   1.00 19.15 ? 124 LEU A N     1 
ATOM   969  C CA    . LEU A 1 129 ? 22.340 4.352   1.530   1.00 17.45 ? 124 LEU A CA    1 
ATOM   970  C C     . LEU A 1 129 ? 22.267 2.850   1.293   1.00 18.48 ? 124 LEU A C     1 
ATOM   971  O O     . LEU A 1 129 ? 23.268 2.143   1.464   1.00 17.76 ? 124 LEU A O     1 
ATOM   972  C CB    . LEU A 1 129 ? 22.005 4.685   2.985   1.00 17.09 ? 124 LEU A CB    1 
ATOM   973  C CG    . LEU A 1 129 ? 22.386 6.103   3.414   1.00 13.77 ? 124 LEU A CG    1 
ATOM   974  C CD1   . LEU A 1 129 ? 21.769 6.437   4.750   1.00 11.98 ? 124 LEU A CD1   1 
ATOM   975  C CD2   . LEU A 1 129 ? 23.894 6.253   3.469   1.00 11.56 ? 124 LEU A CD2   1 
ATOM   976  N N     . SER A 1 130 ? 21.097 2.355   0.892   1.00 17.19 ? 125 SER A N     1 
ATOM   977  C CA    . SER A 1 130 ? 20.954 0.961   0.496   1.00 17.14 ? 125 SER A CA    1 
ATOM   978  C C     . SER A 1 130 ? 21.573 0.711   -0.875  1.00 15.18 ? 125 SER A C     1 
ATOM   979  O O     . SER A 1 130 ? 22.254 -0.302  -1.079  1.00 18.38 ? 125 SER A O     1 
ATOM   980  C CB    . SER A 1 130 ? 19.472 0.584   0.497   1.00 16.50 ? 125 SER A CB    1 
ATOM   981  O OG    . SER A 1 130 ? 19.274 -0.788  0.235   1.00 17.10 ? 125 SER A OG    1 
ATOM   982  N N     . ILE A 1 131 ? 21.366 1.641   -1.810  1.00 16.87 ? 126 ILE A N     1 
ATOM   983  C CA    . ILE A 1 131 ? 21.773 1.434   -3.196  1.00 19.54 ? 126 ILE A CA    1 
ATOM   984  C C     . ILE A 1 131 ? 23.293 1.429   -3.330  1.00 20.68 ? 126 ILE A C     1 
ATOM   985  O O     . ILE A 1 131 ? 23.861 0.578   -4.026  1.00 23.95 ? 126 ILE A O     1 
ATOM   986  C CB    . ILE A 1 131 ? 21.125 2.504   -4.092  1.00 22.24 ? 126 ILE A CB    1 
ATOM   987  C CG1   . ILE A 1 131 ? 19.612 2.284   -4.168  1.00 15.57 ? 126 ILE A CG1   1 
ATOM   988  C CG2   . ILE A 1 131 ? 21.750 2.500   -5.491  1.00 21.81 ? 126 ILE A CG2   1 
ATOM   989  C CD1   . ILE A 1 131 ? 18.876 3.347   -4.942  1.00 13.79 ? 126 ILE A CD1   1 
ATOM   990  N N     . ILE A 1 132 ? 23.978 2.372   -2.674  1.00 21.39 ? 127 ILE A N     1 
ATOM   991  C CA    . ILE A 1 132 ? 25.436 2.425   -2.772  1.00 19.31 ? 127 ILE A CA    1 
ATOM   992  C C     . ILE A 1 132 ? 26.099 1.263   -2.046  1.00 18.15 ? 127 ILE A C     1 
ATOM   993  O O     . ILE A 1 132 ? 27.290 1.007   -2.253  1.00 22.57 ? 127 ILE A O     1 
ATOM   994  C CB    . ILE A 1 132 ? 25.996 3.759   -2.236  1.00 18.37 ? 127 ILE A CB    1 
ATOM   995  C CG1   . ILE A 1 132 ? 25.792 3.865   -0.719  1.00 21.51 ? 127 ILE A CG1   1 
ATOM   996  C CG2   . ILE A 1 132 ? 25.375 4.935   -2.965  1.00 17.72 ? 127 ILE A CG2   1 
ATOM   997  C CD1   . ILE A 1 132 ? 26.371 5.128   -0.097  1.00 22.07 ? 127 ILE A CD1   1 
ATOM   998  N N     . ARG A 1 133 ? 25.369 0.550   -1.191  1.00 16.63 ? 128 ARG A N     1 
ATOM   999  C CA    . ARG A 1 133 ? 25.895 -0.639  -0.535  1.00 18.26 ? 128 ARG A CA    1 
ATOM   1000 C C     . ARG A 1 133 ? 25.353 -1.919  -1.163  1.00 21.03 ? 128 ARG A C     1 
ATOM   1001 O O     . ARG A 1 133 ? 25.157 -2.924  -0.470  1.00 23.41 ? 128 ARG A O     1 
ATOM   1002 C CB    . ARG A 1 133 ? 25.610 -0.576  0.965   1.00 18.29 ? 128 ARG A CB    1 
ATOM   1003 C CG    . ARG A 1 133 ? 26.439 0.517   1.651   1.00 24.63 ? 128 ARG A CG    1 
ATOM   1004 C CD    . ARG A 1 133 ? 26.356 0.532   3.176   1.00 17.86 ? 128 ARG A CD    1 
ATOM   1005 N NE    . ARG A 1 133 ? 25.015 0.799   3.678   1.00 19.56 ? 128 ARG A NE    1 
ATOM   1006 C CZ    . ARG A 1 133 ? 24.725 1.000   4.956   1.00 17.13 ? 128 ARG A CZ    1 
ATOM   1007 N NH1   . ARG A 1 133 ? 25.664 0.989   5.888   1.00 22.44 ? 128 ARG A NH1   1 
ATOM   1008 N NH2   . ARG A 1 133 ? 23.465 1.229   5.308   1.00 17.21 ? 128 ARG A NH2   1 
ATOM   1009 N N     . ASP A 1 134 ? 25.121 -1.895  -2.477  1.00 23.94 ? 129 ASP A N     1 
ATOM   1010 C CA    . ASP A 1 134 ? 24.634 -3.032  -3.245  1.00 23.59 ? 129 ASP A CA    1 
ATOM   1011 C C     . ASP A 1 134 ? 25.654 -3.380  -4.322  1.00 21.53 ? 129 ASP A C     1 
ATOM   1012 O O     . ASP A 1 134 ? 26.268 -2.492  -4.921  1.00 24.72 ? 129 ASP A O     1 
ATOM   1013 C CB    . ASP A 1 134 ? 23.272 -2.723  -3.895  1.00 19.62 ? 129 ASP A CB    1 
ATOM   1014 C CG    . ASP A 1 134 ? 22.686 -3.915  -4.645  1.00 19.10 ? 129 ASP A CG    1 
ATOM   1015 O OD1   . ASP A 1 134 ? 23.292 -5.006  -4.638  1.00 20.86 ? 129 ASP A OD1   1 
ATOM   1016 O OD2   . ASP A 1 134 ? 21.618 -3.755  -5.270  1.00 22.29 ? 129 ASP A OD2   1 
ATOM   1017 N N     . LEU A 1 135 ? 25.820 -4.681  -4.574  1.00 19.70 ? 130 LEU A N     1 
ATOM   1018 C CA    . LEU A 1 135 ? 26.768 -5.129  -5.590  1.00 21.27 ? 130 LEU A CA    1 
ATOM   1019 C C     . LEU A 1 135 ? 26.294 -4.780  -6.998  1.00 22.28 ? 130 LEU A C     1 
ATOM   1020 O O     . LEU A 1 135 ? 27.110 -4.452  -7.868  1.00 20.75 ? 130 LEU A O     1 
ATOM   1021 C CB    . LEU A 1 135 ? 26.981 -6.638  -5.466  1.00 25.28 ? 130 LEU A CB    1 
ATOM   1022 C CG    . LEU A 1 135 ? 28.017 -7.309  -6.368  1.00 19.80 ? 130 LEU A CG    1 
ATOM   1023 C CD1   . LEU A 1 135 ? 29.420 -6.959  -5.917  1.00 24.90 ? 130 LEU A CD1   1 
ATOM   1024 C CD2   . LEU A 1 135 ? 27.811 -8.815  -6.401  1.00 23.33 ? 130 LEU A CD2   1 
ATOM   1025 N N     . GLU A 1 136 ? 24.980 -4.836  -7.239  1.00 24.29 ? 131 GLU A N     1 
ATOM   1026 C CA    . GLU A 1 136 ? 24.469 -4.785  -8.607  1.00 23.05 ? 131 GLU A CA    1 
ATOM   1027 C C     . GLU A 1 136 ? 24.553 -3.387  -9.216  1.00 23.00 ? 131 GLU A C     1 
ATOM   1028 O O     . GLU A 1 136 ? 24.699 -3.264  -10.436 1.00 20.30 ? 131 GLU A O     1 
ATOM   1029 C CB    . GLU A 1 136 ? 23.032 -5.305  -8.651  1.00 23.11 ? 131 GLU A CB    1 
ATOM   1030 C CG    . GLU A 1 136 ? 22.431 -5.342  -10.050 1.00 22.05 ? 131 GLU A CG    1 
ATOM   1031 C CD    . GLU A 1 136 ? 21.047 -5.955  -10.084 1.00 22.74 ? 131 GLU A CD    1 
ATOM   1032 O OE1   . GLU A 1 136 ? 20.645 -6.574  -9.079  1.00 29.68 ? 131 GLU A OE1   1 
ATOM   1033 O OE2   . GLU A 1 136 ? 20.351 -5.805  -11.109 1.00 25.29 ? 131 GLU A OE2   1 
ATOM   1034 N N     . VAL A 1 137 ? 24.470 -2.326  -8.402  1.00 29.26 ? 132 VAL A N     1 
ATOM   1035 C CA    . VAL A 1 137 ? 24.566 -0.975  -8.960  1.00 28.91 ? 132 VAL A CA    1 
ATOM   1036 C C     . VAL A 1 137 ? 25.933 -0.742  -9.593  1.00 25.45 ? 132 VAL A C     1 
ATOM   1037 O O     . VAL A 1 137 ? 26.047 -0.034  -10.602 1.00 26.14 ? 132 VAL A O     1 
ATOM   1038 C CB    . VAL A 1 137 ? 24.242 0.095   -7.888  1.00 22.79 ? 132 VAL A CB    1 
ATOM   1039 C CG1   . VAL A 1 137 ? 25.390 0.278   -6.901  1.00 21.67 ? 132 VAL A CG1   1 
ATOM   1040 C CG2   . VAL A 1 137 ? 23.910 1.425   -8.551  1.00 22.81 ? 132 VAL A CG2   1 
ATOM   1041 N N     . TYR A 1 138 ? 26.982 -1.344  -9.035  1.00 22.05 ? 133 TYR A N     1 
ATOM   1042 C CA    . TYR A 1 138 ? 28.327 -1.191  -9.565  1.00 21.86 ? 133 TYR A CA    1 
ATOM   1043 C C     . TYR A 1 138 ? 28.628 -2.164  -10.696 1.00 19.29 ? 133 TYR A C     1 
ATOM   1044 O O     . TYR A 1 138 ? 29.646 -2.007  -11.377 1.00 20.76 ? 133 TYR A O     1 
ATOM   1045 C CB    . TYR A 1 138 ? 29.345 -1.352  -8.432  1.00 24.13 ? 133 TYR A CB    1 
ATOM   1046 C CG    . TYR A 1 138 ? 29.138 -0.351  -7.318  1.00 22.30 ? 133 TYR A CG    1 
ATOM   1047 C CD1   . TYR A 1 138 ? 29.397 0.999   -7.516  1.00 22.79 ? 133 TYR A CD1   1 
ATOM   1048 C CD2   . TYR A 1 138 ? 28.681 -0.753  -6.072  1.00 20.91 ? 133 TYR A CD2   1 
ATOM   1049 C CE1   . TYR A 1 138 ? 29.207 1.920   -6.508  1.00 20.57 ? 133 TYR A CE1   1 
ATOM   1050 C CE2   . TYR A 1 138 ? 28.490 0.165   -5.055  1.00 21.43 ? 133 TYR A CE2   1 
ATOM   1051 C CZ    . TYR A 1 138 ? 28.754 1.499   -5.281  1.00 18.71 ? 133 TYR A CZ    1 
ATOM   1052 O OH    . TYR A 1 138 ? 28.566 2.416   -4.275  1.00 18.89 ? 133 TYR A OH    1 
ATOM   1053 N N     . GLU A 1 139 ? 27.767 -3.155  -10.912 1.00 23.24 ? 134 GLU A N     1 
ATOM   1054 C CA    . GLU A 1 139 ? 27.831 -4.006  -12.089 1.00 21.01 ? 134 GLU A CA    1 
ATOM   1055 C C     . GLU A 1 139 ? 27.077 -3.419  -13.275 1.00 21.58 ? 134 GLU A C     1 
ATOM   1056 O O     . GLU A 1 139 ? 27.271 -3.883  -14.404 1.00 27.07 ? 134 GLU A O     1 
ATOM   1057 C CB    . GLU A 1 139 ? 27.268 -5.395  -11.771 1.00 19.71 ? 134 GLU A CB    1 
ATOM   1058 C CG    . GLU A 1 139 ? 28.126 -6.221  -10.826 1.00 20.62 ? 134 GLU A CG    1 
ATOM   1059 C CD    . GLU A 1 139 ? 27.500 -7.562  -10.487 1.00 16.08 ? 134 GLU A CD    1 
ATOM   1060 O OE1   . GLU A 1 139 ? 26.367 -7.577  -9.963  1.00 21.13 ? 134 GLU A OE1   1 
ATOM   1061 O OE2   . GLU A 1 139 ? 28.137 -8.605  -10.741 1.00 22.04 ? 134 GLU A OE2   1 
ATOM   1062 N N     . ARG A 1 140 ? 26.232 -2.409  -13.046 1.00 22.99 ? 135 ARG A N     1 
ATOM   1063 C CA    . ARG A 1 140 ? 25.369 -1.848  -14.076 1.00 26.37 ? 135 ARG A CA    1 
ATOM   1064 C C     . ARG A 1 140 ? 25.759 -0.439  -14.495 1.00 26.17 ? 135 ARG A C     1 
ATOM   1065 O O     . ARG A 1 140 ? 25.384 -0.014  -15.592 1.00 21.84 ? 135 ARG A O     1 
ATOM   1066 C CB    . ARG A 1 140 ? 23.911 -1.823  -13.588 1.00 26.87 ? 135 ARG A CB    1 
ATOM   1067 C CG    . ARG A 1 140 ? 23.318 -3.192  -13.318 1.00 22.43 ? 135 ARG A CG    1 
ATOM   1068 C CD    . ARG A 1 140 ? 21.928 -3.088  -12.712 1.00 19.37 ? 135 ARG A CD    1 
ATOM   1069 N NE    . ARG A 1 140 ? 20.924 -2.665  -13.679 1.00 28.74 ? 135 ARG A NE    1 
ATOM   1070 C CZ    . ARG A 1 140 ? 19.699 -3.169  -13.744 1.00 20.82 ? 135 ARG A CZ    1 
ATOM   1071 N NH1   . ARG A 1 140 ? 19.269 -4.053  -12.862 1.00 29.03 ? 135 ARG A NH1   1 
ATOM   1072 N NH2   . ARG A 1 140 ? 18.885 -2.776  -14.718 1.00 21.20 ? 135 ARG A NH2   1 
ATOM   1073 N N     . PHE A 1 141 ? 26.480 0.292   -13.645 1.00 28.65 ? 136 PHE A N     1 
ATOM   1074 C CA    . PHE A 1 141 ? 26.892 1.664   -13.897 1.00 25.88 ? 136 PHE A CA    1 
ATOM   1075 C C     . PHE A 1 141 ? 28.391 1.784   -13.660 1.00 28.68 ? 136 PHE A C     1 
ATOM   1076 O O     . PHE A 1 141 ? 28.910 1.272   -12.662 1.00 27.66 ? 136 PHE A O     1 
ATOM   1077 C CB    . PHE A 1 141 ? 26.146 2.659   -12.979 1.00 29.22 ? 136 PHE A CB    1 
ATOM   1078 C CG    . PHE A 1 141 ? 24.667 2.781   -13.260 1.00 22.72 ? 136 PHE A CG    1 
ATOM   1079 C CD1   . PHE A 1 141 ? 24.210 3.463   -14.377 1.00 22.43 ? 136 PHE A CD1   1 
ATOM   1080 C CD2   . PHE A 1 141 ? 23.736 2.233   -12.393 1.00 20.44 ? 136 PHE A CD2   1 
ATOM   1081 C CE1   . PHE A 1 141 ? 22.855 3.584   -14.631 1.00 17.20 ? 136 PHE A CE1   1 
ATOM   1082 C CE2   . PHE A 1 141 ? 22.383 2.352   -12.645 1.00 20.61 ? 136 PHE A CE2   1 
ATOM   1083 C CZ    . PHE A 1 141 ? 21.944 3.030   -13.767 1.00 18.07 ? 136 PHE A CZ    1 
ATOM   1084 N N     . GLU A 1 142 ? 29.085 2.477   -14.570 1.00 31.57 ? 137 GLU A N     1 
ATOM   1085 C CA    . GLU A 1 142 ? 30.520 2.688   -14.394 1.00 28.77 ? 137 GLU A CA    1 
ATOM   1086 C C     . GLU A 1 142 ? 30.806 3.635   -13.233 1.00 23.67 ? 137 GLU A C     1 
ATOM   1087 O O     . GLU A 1 142 ? 31.712 3.384   -12.430 1.00 22.50 ? 137 GLU A O     1 
ATOM   1088 C CB    . GLU A 1 142 ? 31.146 3.228   -15.679 1.00 28.69 ? 137 GLU A CB    1 
ATOM   1089 C CG    . GLU A 1 142 ? 31.314 2.215   -16.787 1.00 24.73 ? 137 GLU A CG    1 
ATOM   1090 C CD    . GLU A 1 142 ? 32.189 2.749   -17.904 1.00 32.25 ? 137 GLU A CD    1 
ATOM   1091 O OE1   . GLU A 1 142 ? 32.794 3.826   -17.721 1.00 39.10 ? 137 GLU A OE1   1 
ATOM   1092 O OE2   . GLU A 1 142 ? 32.271 2.101   -18.967 1.00 41.89 ? 137 GLU A OE2   1 
ATOM   1093 N N     . LYS A 1 143 ? 30.056 4.729   -13.134 1.00 24.44 ? 138 LYS A N     1 
ATOM   1094 C CA    . LYS A 1 143 ? 30.188 5.683   -12.042 1.00 25.01 ? 138 LYS A CA    1 
ATOM   1095 C C     . LYS A 1 143 ? 28.872 5.809   -11.290 1.00 23.85 ? 138 LYS A C     1 
ATOM   1096 O O     . LYS A 1 143 ? 27.792 5.750   -11.887 1.00 22.93 ? 138 LYS A O     1 
ATOM   1097 C CB    . LYS A 1 143 ? 30.626 7.063   -12.547 1.00 23.14 ? 138 LYS A CB    1 
ATOM   1098 C CG    . LYS A 1 143 ? 32.013 7.106   -13.145 1.00 19.14 ? 138 LYS A CG    1 
ATOM   1099 C CD    . LYS A 1 143 ? 33.048 6.921   -12.056 1.00 22.84 ? 138 LYS A CD    1 
ATOM   1100 C CE    . LYS A 1 143 ? 34.448 6.859   -12.626 1.00 21.27 ? 138 LYS A CE    1 
ATOM   1101 N NZ    . LYS A 1 143 ? 35.459 6.690   -11.550 1.00 26.61 ? 138 LYS A NZ    1 
ATOM   1102 N N     . VAL A 1 144 ? 28.977 5.980   -9.974  1.00 21.11 ? 139 VAL A N     1 
ATOM   1103 C CA    . VAL A 1 144 ? 27.839 6.249   -9.102  1.00 23.68 ? 139 VAL A CA    1 
ATOM   1104 C C     . VAL A 1 144 ? 28.158 7.534   -8.351  1.00 18.86 ? 139 VAL A C     1 
ATOM   1105 O O     . VAL A 1 144 ? 29.062 7.562   -7.508  1.00 17.83 ? 139 VAL A O     1 
ATOM   1106 C CB    . VAL A 1 144 ? 27.564 5.095   -8.129  1.00 25.41 ? 139 VAL A CB    1 
ATOM   1107 C CG1   . VAL A 1 144 ? 26.393 5.441   -7.217  1.00 18.10 ? 139 VAL A CG1   1 
ATOM   1108 C CG2   . VAL A 1 144 ? 27.306 3.803   -8.892  1.00 29.67 ? 139 VAL A CG2   1 
ATOM   1109 N N     . ILE A 1 145 ? 27.431 8.597   -8.659  1.00 22.53 ? 140 ILE A N     1 
ATOM   1110 C CA    . ILE A 1 145 ? 27.664 9.902   -8.058  1.00 23.58 ? 140 ILE A CA    1 
ATOM   1111 C C     . ILE A 1 145 ? 26.569 10.128  -7.027  1.00 16.78 ? 140 ILE A C     1 
ATOM   1112 O O     . ILE A 1 145 ? 25.388 10.218  -7.376  1.00 17.79 ? 140 ILE A O     1 
ATOM   1113 C CB    . ILE A 1 145 ? 27.688 11.027  -9.105  1.00 22.41 ? 140 ILE A CB    1 
ATOM   1114 C CG1   . ILE A 1 145 ? 28.596 10.683  -10.298 1.00 18.16 ? 140 ILE A CG1   1 
ATOM   1115 C CG2   . ILE A 1 145 ? 28.143 12.333  -8.459  1.00 21.78 ? 140 ILE A CG2   1 
ATOM   1116 C CD1   . ILE A 1 145 ? 27.897 9.953   -11.447 1.00 16.87 ? 140 ILE A CD1   1 
ATOM   1117 N N     . LEU A 1 146 ? 26.959 10.214  -5.758  1.00 17.67 ? 141 LEU A N     1 
ATOM   1118 C CA    . LEU A 1 146 ? 26.039 10.483  -4.660  1.00 14.63 ? 141 LEU A CA    1 
ATOM   1119 C C     . LEU A 1 146 ? 26.173 11.943  -4.244  1.00 11.02 ? 141 LEU A C     1 
ATOM   1120 O O     . LEU A 1 146 ? 27.253 12.377  -3.833  1.00 12.45 ? 141 LEU A O     1 
ATOM   1121 C CB    . LEU A 1 146 ? 26.317 9.559   -3.476  1.00 16.09 ? 141 LEU A CB    1 
ATOM   1122 C CG    . LEU A 1 146 ? 25.509 9.880   -2.221  1.00 16.30 ? 141 LEU A CG    1 
ATOM   1123 C CD1   . LEU A 1 146 ? 24.022 9.787   -2.524  1.00 16.56 ? 141 LEU A CD1   1 
ATOM   1124 C CD2   . LEU A 1 146 ? 25.897 8.967   -1.063  1.00 14.27 ? 141 LEU A CD2   1 
ATOM   1125 N N     . VAL A 1 147 ? 25.081 12.693  -4.360  1.00 14.15 ? 142 VAL A N     1 
ATOM   1126 C CA    . VAL A 1 147 ? 25.037 14.108  -4.006  1.00 15.21 ? 142 VAL A CA    1 
ATOM   1127 C C     . VAL A 1 147 ? 24.030 14.283  -2.880  1.00 13.80 ? 142 VAL A C     1 
ATOM   1128 O O     . VAL A 1 147 ? 22.887 13.830  -2.994  1.00 17.92 ? 142 VAL A O     1 
ATOM   1129 C CB    . VAL A 1 147 ? 24.669 14.990  -5.214  1.00 12.86 ? 142 VAL A CB    1 
ATOM   1130 C CG1   . VAL A 1 147 ? 24.480 16.435  -4.775  1.00 12.94 ? 142 VAL A CG1   1 
ATOM   1131 C CG2   . VAL A 1 147 ? 25.730 14.886  -6.306  1.00 13.07 ? 142 VAL A CG2   1 
ATOM   1132 N N     . HIS A 1 148 ? 24.453 14.943  -1.801  1.00 19.03 ? 143 HIS A N     1 
ATOM   1133 C CA    . HIS A 1 148 ? 23.627 15.117  -0.608  1.00 18.51 ? 143 HIS A CA    1 
ATOM   1134 C C     . HIS A 1 148 ? 23.560 16.590  -0.231  1.00 12.98 ? 143 HIS A C     1 
ATOM   1135 O O     . HIS A 1 148 ? 24.557 17.180  0.187   1.00 16.38 ? 143 HIS A O     1 
ATOM   1136 C CB    . HIS A 1 148 ? 24.170 14.287  0.558   1.00 14.11 ? 143 HIS A CB    1 
ATOM   1137 C CG    . HIS A 1 148 ? 23.229 14.212  1.718   1.00 13.69 ? 143 HIS A CG    1 
ATOM   1138 N ND1   . HIS A 1 148 ? 23.659 14.210  3.026   1.00 15.22 ? 143 HIS A ND1   1 
ATOM   1139 C CD2   . HIS A 1 148 ? 21.876 14.170  1.766   1.00 12.16 ? 143 HIS A CD2   1 
ATOM   1140 C CE1   . HIS A 1 148 ? 22.614 14.145  3.831   1.00 12.48 ? 143 HIS A CE1   1 
ATOM   1141 N NE2   . HIS A 1 148 ? 21.521 14.124  3.091   1.00 14.21 ? 143 HIS A NE2   1 
ATOM   1142 N N     . GLY A 1 149 ? 22.360 17.181  -0.347  1.00 14.20 ? 144 GLY A N     1 
ATOM   1143 C CA    . GLY A 1 149 ? 22.152 18.570  -0.019  1.00 15.34 ? 144 GLY A CA    1 
ATOM   1144 C C     . GLY A 1 149 ? 21.523 18.753  1.347   1.00 14.77 ? 144 GLY A C     1 
ATOM   1145 O O     . GLY A 1 149 ? 20.465 18.194  1.635   1.00 18.16 ? 144 GLY A O     1 
ATOM   1146 N N     . VAL A 1 150 ? 22.179 19.555  2.186   1.00 16.36 ? 145 VAL A N     1 
ATOM   1147 C CA    . VAL A 1 150 ? 21.709 19.854  3.533   1.00 15.66 ? 145 VAL A CA    1 
ATOM   1148 C C     . VAL A 1 150 ? 21.862 21.347  3.796   1.00 16.22 ? 145 VAL A C     1 
ATOM   1149 O O     . VAL A 1 150 ? 22.526 22.072  3.051   1.00 16.69 ? 145 VAL A O     1 
ATOM   1150 C CB    . VAL A 1 150 ? 22.460 19.047  4.614   1.00 13.84 ? 145 VAL A CB    1 
ATOM   1151 C CG1   . VAL A 1 150 ? 22.117 17.567  4.515   1.00 15.86 ? 145 VAL A CG1   1 
ATOM   1152 C CG2   . VAL A 1 150 ? 23.950 19.271  4.507   1.00 15.29 ? 145 VAL A CG2   1 
ATOM   1153 N N     . ARG A 1 151 ? 21.227 21.797  4.883   1.00 17.34 ? 146 ARG A N     1 
ATOM   1154 C CA    . ARG A 1 151 ? 21.321 23.193  5.294   1.00 16.41 ? 146 ARG A CA    1 
ATOM   1155 C C     . ARG A 1 151 ? 22.541 23.455  6.169   1.00 15.62 ? 146 ARG A C     1 
ATOM   1156 O O     . ARG A 1 151 ? 23.171 24.510  6.050   1.00 16.10 ? 146 ARG A O     1 
ATOM   1157 C CB    . ARG A 1 151 ? 20.046 23.614  6.025   1.00 17.88 ? 146 ARG A CB    1 
ATOM   1158 C CG    . ARG A 1 151 ? 18.879 23.935  5.108   1.00 17.84 ? 146 ARG A CG    1 
ATOM   1159 C CD    . ARG A 1 151 ? 17.655 24.372  5.893   1.00 23.78 ? 146 ARG A CD    1 
ATOM   1160 N NE    . ARG A 1 151 ? 17.053 23.279  6.646   1.00 33.58 ? 146 ARG A NE    1 
ATOM   1161 C CZ    . ARG A 1 151 ? 16.232 22.376  6.128   1.00 24.47 ? 146 ARG A CZ    1 
ATOM   1162 N NH1   . ARG A 1 151 ? 15.902 22.400  4.848   1.00 20.35 ? 146 ARG A NH1   1 
ATOM   1163 N NH2   . ARG A 1 151 ? 15.735 21.423  6.912   1.00 23.14 ? 146 ARG A NH2   1 
ATOM   1164 N N     . GLN A 1 152 ? 22.888 22.518  7.051   1.00 23.39 ? 147 GLN A N     1 
ATOM   1165 C CA    . GLN A 1 152 ? 24.017 22.683  7.956   1.00 18.73 ? 147 GLN A CA    1 
ATOM   1166 C C     . GLN A 1 152 ? 24.966 21.506  7.816   1.00 14.76 ? 147 GLN A C     1 
ATOM   1167 O O     . GLN A 1 152 ? 24.565 20.413  7.406   1.00 19.44 ? 147 GLN A O     1 
ATOM   1168 C CB    . GLN A 1 152 ? 23.570 22.803  9.420   1.00 18.75 ? 147 GLN A CB    1 
ATOM   1169 C CG    . GLN A 1 152 ? 22.948 24.142  9.767   1.00 21.25 ? 147 GLN A CG    1 
ATOM   1170 C CD    . GLN A 1 152 ? 21.564 24.005  10.365  1.00 18.46 ? 147 GLN A CD    1 
ATOM   1171 O OE1   . GLN A 1 152 ? 20.649 23.486  9.728   1.00 22.73 ? 147 GLN A OE1   1 
ATOM   1172 N NE2   . GLN A 1 152 ? 21.398 24.500  11.587  1.00 15.05 ? 147 GLN A NE2   1 
ATOM   1173 N N     . VAL A 1 153 ? 26.231 21.744  8.177   1.00 19.57 ? 148 VAL A N     1 
ATOM   1174 C CA    . VAL A 1 153 ? 27.247 20.695  8.113   1.00 19.36 ? 148 VAL A CA    1 
ATOM   1175 C C     . VAL A 1 153 ? 26.852 19.504  8.983   1.00 19.22 ? 148 VAL A C     1 
ATOM   1176 O O     . VAL A 1 153 ? 26.991 18.344  8.573   1.00 21.06 ? 148 VAL A O     1 
ATOM   1177 C CB    . VAL A 1 153 ? 28.619 21.266  8.512   1.00 13.57 ? 148 VAL A CB    1 
ATOM   1178 C CG1   . VAL A 1 153 ? 29.663 20.176  8.530   1.00 13.66 ? 148 VAL A CG1   1 
ATOM   1179 C CG2   . VAL A 1 153 ? 29.024 22.377  7.564   1.00 18.16 ? 148 VAL A CG2   1 
ATOM   1180 N N     . ALA A 1 154 ? 26.337 19.770  10.188  1.00 18.09 ? 149 ALA A N     1 
ATOM   1181 C CA    . ALA A 1 154 ? 25.914 18.695  11.081  1.00 16.41 ? 149 ALA A CA    1 
ATOM   1182 C C     . ALA A 1 154 ? 24.848 17.801  10.460  1.00 18.56 ? 149 ALA A C     1 
ATOM   1183 O O     . ALA A 1 154 ? 24.702 16.647  10.881  1.00 19.78 ? 149 ALA A O     1 
ATOM   1184 C CB    . ALA A 1 154 ? 25.395 19.277  12.397  1.00 14.83 ? 149 ALA A CB    1 
ATOM   1185 N N     . GLU A 1 155 ? 24.106 18.302  9.470   1.00 18.88 ? 150 GLU A N     1 
ATOM   1186 C CA    . GLU A 1 155 ? 23.076 17.516  8.802   1.00 17.29 ? 150 GLU A CA    1 
ATOM   1187 C C     . GLU A 1 155 ? 23.645 16.488  7.827   1.00 15.99 ? 150 GLU A C     1 
ATOM   1188 O O     . GLU A 1 155 ? 22.881 15.672  7.300   1.00 16.44 ? 150 GLU A O     1 
ATOM   1189 C CB    . GLU A 1 155 ? 22.101 18.443  8.068   1.00 18.01 ? 150 GLU A CB    1 
ATOM   1190 C CG    . GLU A 1 155 ? 21.144 19.211  8.978   1.00 19.87 ? 150 GLU A CG    1 
ATOM   1191 C CD    . GLU A 1 155 ? 20.257 20.190  8.218   1.00 15.33 ? 150 GLU A CD    1 
ATOM   1192 O OE1   . GLU A 1 155 ? 20.567 20.515  7.057   1.00 19.35 ? 150 GLU A OE1   1 
ATOM   1193 O OE2   . GLU A 1 155 ? 19.233 20.633  8.775   1.00 22.94 ? 150 GLU A OE2   1 
ATOM   1194 N N     . LEU A 1 156 ? 24.958 16.492  7.585   1.00 18.51 ? 151 LEU A N     1 
ATOM   1195 C CA    . LEU A 1 156 ? 25.594 15.495  6.719   1.00 17.25 ? 151 LEU A CA    1 
ATOM   1196 C C     . LEU A 1 156 ? 25.799 14.187  7.484   1.00 14.93 ? 151 LEU A C     1 
ATOM   1197 O O     . LEU A 1 156 ? 26.915 13.784  7.818   1.00 15.27 ? 151 LEU A O     1 
ATOM   1198 C CB    . LEU A 1 156 ? 26.915 16.015  6.169   1.00 17.17 ? 151 LEU A CB    1 
ATOM   1199 C CG    . LEU A 1 156 ? 26.845 17.096  5.098   1.00 19.15 ? 151 LEU A CG    1 
ATOM   1200 C CD1   . LEU A 1 156 ? 28.212 17.721  4.863   1.00 20.78 ? 151 LEU A CD1   1 
ATOM   1201 C CD2   . LEU A 1 156 ? 26.305 16.484  3.819   1.00 20.63 ? 151 LEU A CD2   1 
ATOM   1202 N N     . ALA A 1 157 ? 24.683 13.514  7.755   1.00 19.23 ? 152 ALA A N     1 
ATOM   1203 C CA    . ALA A 1 157 ? 24.742 12.189  8.353   1.00 15.95 ? 152 ALA A CA    1 
ATOM   1204 C C     . ALA A 1 157 ? 25.563 11.257  7.474   1.00 16.36 ? 152 ALA A C     1 
ATOM   1205 O O     . ALA A 1 157 ? 25.581 11.385  6.247   1.00 20.01 ? 152 ALA A O     1 
ATOM   1206 C CB    . ALA A 1 157 ? 23.335 11.624  8.546   1.00 12.89 ? 152 ALA A CB    1 
ATOM   1207 N N     . TYR A 1 158 ? 26.267 10.326  8.116   1.00 15.81 ? 153 TYR A N     1 
ATOM   1208 C CA    . TYR A 1 158 ? 27.049 9.290   7.441   1.00 20.90 ? 153 TYR A CA    1 
ATOM   1209 C C     . TYR A 1 158 ? 28.192 9.864   6.610   1.00 19.66 ? 153 TYR A C     1 
ATOM   1210 O O     . TYR A 1 158 ? 28.720 9.176   5.732   1.00 20.85 ? 153 TYR A O     1 
ATOM   1211 C CB    . TYR A 1 158 ? 26.173 8.415   6.532   1.00 16.53 ? 153 TYR A CB    1 
ATOM   1212 C CG    . TYR A 1 158 ? 25.028 7.709   7.209   1.00 12.70 ? 153 TYR A CG    1 
ATOM   1213 C CD1   . TYR A 1 158 ? 25.192 6.453   7.766   1.00 13.64 ? 153 TYR A CD1   1 
ATOM   1214 C CD2   . TYR A 1 158 ? 23.771 8.294   7.264   1.00 13.34 ? 153 TYR A CD2   1 
ATOM   1215 C CE1   . TYR A 1 158 ? 24.138 5.806   8.374   1.00 13.90 ? 153 TYR A CE1   1 
ATOM   1216 C CE2   . TYR A 1 158 ? 22.713 7.659   7.870   1.00 11.14 ? 153 TYR A CE2   1 
ATOM   1217 C CZ    . TYR A 1 158 ? 22.900 6.415   8.421   1.00 12.33 ? 153 TYR A CZ    1 
ATOM   1218 O OH    . TYR A 1 158 ? 21.840 5.782   9.023   1.00 14.40 ? 153 TYR A OH    1 
ATOM   1219 N N     . THR A 1 159 ? 28.580 11.121  6.842   1.00 17.18 ? 154 THR A N     1 
ATOM   1220 C CA    . THR A 1 159 ? 29.572 11.736  5.967   1.00 19.77 ? 154 THR A CA    1 
ATOM   1221 C C     . THR A 1 159 ? 30.941 11.077  6.118   1.00 24.20 ? 154 THR A C     1 
ATOM   1222 O O     . THR A 1 159 ? 31.682 10.963  5.134   1.00 25.10 ? 154 THR A O     1 
ATOM   1223 C CB    . THR A 1 159 ? 29.636 13.254  6.213   1.00 18.67 ? 154 THR A CB    1 
ATOM   1224 O OG1   . THR A 1 159 ? 30.240 13.907  5.087   1.00 20.26 ? 154 THR A OG1   1 
ATOM   1225 C CG2   . THR A 1 159 ? 30.407 13.602  7.493   1.00 15.36 ? 154 THR A CG2   1 
ATOM   1226 N N     . ASP A 1 160 ? 31.278 10.597  7.314   1.00 19.01 ? 155 ASP A N     1 
ATOM   1227 C CA    . ASP A 1 160 ? 32.560 9.931   7.501   1.00 23.69 ? 155 ASP A CA    1 
ATOM   1228 C C     . ASP A 1 160 ? 32.496 8.451   7.137   1.00 23.14 ? 155 ASP A C     1 
ATOM   1229 O O     . ASP A 1 160 ? 33.516 7.872   6.744   1.00 21.79 ? 155 ASP A O     1 
ATOM   1230 C CB    . ASP A 1 160 ? 33.031 10.105  8.946   1.00 33.88 ? 155 ASP A CB    1 
ATOM   1231 C CG    . ASP A 1 160 ? 33.666 11.461  9.193   1.00 42.85 ? 155 ASP A CG    1 
ATOM   1232 O OD1   . ASP A 1 160 ? 33.296 12.113  10.193  1.00 50.35 ? 155 ASP A OD1   1 
ATOM   1233 O OD2   . ASP A 1 160 ? 34.539 11.867  8.393   1.00 42.56 ? 155 ASP A OD2   1 
ATOM   1234 N N     . PHE A 1 161 ? 31.321 7.826   7.258   1.00 23.14 ? 156 PHE A N     1 
ATOM   1235 C CA    . PHE A 1 161 ? 31.182 6.428   6.859   1.00 22.74 ? 156 PHE A CA    1 
ATOM   1236 C C     . PHE A 1 161 ? 31.296 6.264   5.346   1.00 22.41 ? 156 PHE A C     1 
ATOM   1237 O O     . PHE A 1 161 ? 31.843 5.264   4.864   1.00 24.10 ? 156 PHE A O     1 
ATOM   1238 C CB    . PHE A 1 161 ? 29.848 5.864   7.355   1.00 21.06 ? 156 PHE A CB    1 
ATOM   1239 C CG    . PHE A 1 161 ? 29.538 4.488   6.826   1.00 21.03 ? 156 PHE A CG    1 
ATOM   1240 C CD1   . PHE A 1 161 ? 30.133 3.366   7.382   1.00 21.56 ? 156 PHE A CD1   1 
ATOM   1241 C CD2   . PHE A 1 161 ? 28.667 4.319   5.760   1.00 20.57 ? 156 PHE A CD2   1 
ATOM   1242 C CE1   . PHE A 1 161 ? 29.855 2.103   6.898   1.00 17.70 ? 156 PHE A CE1   1 
ATOM   1243 C CE2   . PHE A 1 161 ? 28.387 3.059   5.268   1.00 20.42 ? 156 PHE A CE2   1 
ATOM   1244 C CZ    . PHE A 1 161 ? 28.979 1.949   5.837   1.00 20.57 ? 156 PHE A CZ    1 
ATOM   1245 N N     . ILE A 1 162 ? 30.770 7.223   4.582   1.00 21.85 ? 157 ILE A N     1 
ATOM   1246 C CA    . ILE A 1 162 ? 30.827 7.124   3.127   1.00 24.47 ? 157 ILE A CA    1 
ATOM   1247 C C     . ILE A 1 162 ? 32.260 7.272   2.636   1.00 24.86 ? 157 ILE A C     1 
ATOM   1248 O O     . ILE A 1 162 ? 32.703 6.549   1.736   1.00 22.83 ? 157 ILE A O     1 
ATOM   1249 C CB    . ILE A 1 162 ? 29.907 8.176   2.480   1.00 19.02 ? 157 ILE A CB    1 
ATOM   1250 C CG1   . ILE A 1 162 ? 28.451 7.951   2.885   1.00 25.43 ? 157 ILE A CG1   1 
ATOM   1251 C CG2   . ILE A 1 162 ? 30.026 8.128   0.963   1.00 15.65 ? 157 ILE A CG2   1 
ATOM   1252 C CD1   . ILE A 1 162 ? 27.538 9.107   2.533   1.00 19.17 ? 157 ILE A CD1   1 
ATOM   1253 N N     . SER A 1 163 ? 33.008 8.204   3.223   1.00 24.33 ? 158 SER A N     1 
ATOM   1254 C CA    . SER A 1 163 ? 34.297 8.612   2.681   1.00 25.19 ? 158 SER A CA    1 
ATOM   1255 C C     . SER A 1 163 ? 35.463 7.839   3.282   1.00 20.78 ? 158 SER A C     1 
ATOM   1256 O O     . SER A 1 163 ? 36.446 7.563   2.586   1.00 23.24 ? 158 SER A O     1 
ATOM   1257 C CB    . SER A 1 163 ? 34.499 10.113  2.901   1.00 22.63 ? 158 SER A CB    1 
ATOM   1258 O OG    . SER A 1 163 ? 33.590 10.855  2.113   1.00 20.78 ? 158 SER A OG    1 
ATOM   1259 N N     . ASN A 1 164 ? 35.376 7.481   4.559   1.00 21.89 ? 159 ASN A N     1 
ATOM   1260 C CA    . ASN A 1 164 ? 36.480 6.818   5.235   1.00 29.19 ? 159 ASN A CA    1 
ATOM   1261 C C     . ASN A 1 164 ? 36.277 5.312   5.370   1.00 28.07 ? 159 ASN A C     1 
ATOM   1262 O O     . ASN A 1 164 ? 37.188 4.539   5.059   1.00 26.76 ? 159 ASN A O     1 
ATOM   1263 C CB    . ASN A 1 164 ? 36.696 7.461   6.610   1.00 28.12 ? 159 ASN A CB    1 
ATOM   1264 C CG    . ASN A 1 164 ? 36.942 8.960   6.518   1.00 28.35 ? 159 ASN A CG    1 
ATOM   1265 O OD1   . ASN A 1 164 ? 37.667 9.429   5.641   1.00 31.07 ? 159 ASN A OD1   1 
ATOM   1266 N ND2   . ASN A 1 164 ? 36.327 9.717   7.417   1.00 31.31 ? 159 ASN A ND2   1 
ATOM   1267 N N     . GLU A 1 165 ? 35.087 4.874   5.787   1.00 27.11 ? 160 GLU A N     1 
ATOM   1268 C CA    . GLU A 1 165 ? 34.852 3.480   6.151   1.00 28.85 ? 160 GLU A CA    1 
ATOM   1269 C C     . GLU A 1 165 ? 34.255 2.634   5.029   1.00 27.84 ? 160 GLU A C     1 
ATOM   1270 O O     . GLU A 1 165 ? 34.592 1.451   4.917   1.00 26.11 ? 160 GLU A O     1 
ATOM   1271 C CB    . GLU A 1 165 ? 33.947 3.408   7.387   1.00 29.33 ? 160 GLU A CB    1 
ATOM   1272 C CG    . GLU A 1 165 ? 34.372 4.346   8.506   1.00 30.66 ? 160 GLU A CG    1 
ATOM   1273 C CD    . GLU A 1 165 ? 33.960 3.852   9.882   1.00 51.65 ? 160 GLU A CD    1 
ATOM   1274 O OE1   . GLU A 1 165 ? 32.803 3.408   10.040  1.00 50.34 ? 160 GLU A OE1   1 
ATOM   1275 O OE2   . GLU A 1 165 ? 34.799 3.906   10.807  1.00 47.54 ? 160 GLU A OE2   1 
ATOM   1276 N N     . LEU A 1 166 ? 33.376 3.194   4.194   1.00 25.97 ? 161 LEU A N     1 
ATOM   1277 C CA    . LEU A 1 166 ? 32.782 2.427   3.099   1.00 26.20 ? 161 LEU A CA    1 
ATOM   1278 C C     . LEU A 1 166 ? 33.805 1.983   2.047   1.00 24.76 ? 161 LEU A C     1 
ATOM   1279 O O     . LEU A 1 166 ? 33.673 0.876   1.509   1.00 22.53 ? 161 LEU A O     1 
ATOM   1280 C CB    . LEU A 1 166 ? 31.654 3.226   2.435   1.00 27.78 ? 161 LEU A CB    1 
ATOM   1281 C CG    . LEU A 1 166 ? 30.823 2.515   1.356   1.00 25.60 ? 161 LEU A CG    1 
ATOM   1282 C CD1   . LEU A 1 166 ? 30.229 1.206   1.870   1.00 21.78 ? 161 LEU A CD1   1 
ATOM   1283 C CD2   . LEU A 1 166 ? 29.730 3.434   0.821   1.00 21.75 ? 161 LEU A CD2   1 
ATOM   1284 N N     . PRO A 1 167 ? 34.824 2.786   1.703   1.00 28.59 ? 162 PRO A N     1 
ATOM   1285 C CA    . PRO A 1 167 ? 35.855 2.274   0.783   1.00 28.79 ? 162 PRO A CA    1 
ATOM   1286 C C     . PRO A 1 167 ? 36.672 1.129   1.359   1.00 23.80 ? 162 PRO A C     1 
ATOM   1287 O O     . PRO A 1 167 ? 37.325 0.413   0.590   1.00 18.68 ? 162 PRO A O     1 
ATOM   1288 C CB    . PRO A 1 167 ? 36.735 3.503   0.509   1.00 22.45 ? 162 PRO A CB    1 
ATOM   1289 C CG    . PRO A 1 167 ? 35.880 4.658   0.819   1.00 22.42 ? 162 PRO A CG    1 
ATOM   1290 C CD    . PRO A 1 167 ? 35.010 4.226   1.952   1.00 24.65 ? 162 PRO A CD    1 
ATOM   1291 N N     . GLN A 1 168 ? 36.653 0.931   2.675   1.00 25.01 ? 163 GLN A N     1 
ATOM   1292 C CA    . GLN A 1 168 ? 37.388 -0.149  3.321   1.00 24.47 ? 163 GLN A CA    1 
ATOM   1293 C C     . GLN A 1 168 ? 36.606 -1.456  3.378   1.00 25.33 ? 163 GLN A C     1 
ATOM   1294 O O     . GLN A 1 168 ? 37.109 -2.432  3.945   1.00 29.40 ? 163 GLN A O     1 
ATOM   1295 C CB    . GLN A 1 168 ? 37.776 0.250   4.750   1.00 23.10 ? 163 GLN A CB    1 
ATOM   1296 C CG    . GLN A 1 168 ? 38.861 1.303   4.871   1.00 24.56 ? 163 GLN A CG    1 
ATOM   1297 C CD    . GLN A 1 168 ? 39.226 1.586   6.324   1.00 27.31 ? 163 GLN A CD    1 
ATOM   1298 O OE1   . GLN A 1 168 ? 39.720 0.711   7.035   1.00 30.75 ? 163 GLN A OE1   1 
ATOM   1299 N NE2   . GLN A 1 168 ? 38.963 2.808   6.775   1.00 27.26 ? 163 GLN A NE2   1 
ATOM   1300 N N     . ASP A 1 169 ? 35.395 -1.498  2.823   1.00 28.06 ? 164 ASP A N     1 
ATOM   1301 C CA    . ASP A 1 169 ? 34.530 -2.660  2.986   1.00 26.47 ? 164 ASP A CA    1 
ATOM   1302 C C     . ASP A 1 169 ? 35.133 -3.876  2.291   1.00 25.37 ? 164 ASP A C     1 
ATOM   1303 O O     . ASP A 1 169 ? 35.495 -3.818  1.112   1.00 25.51 ? 164 ASP A O     1 
ATOM   1304 C CB    . ASP A 1 169 ? 33.137 -2.373  2.430   1.00 27.72 ? 164 ASP A CB    1 
ATOM   1305 C CG    . ASP A 1 169 ? 32.130 -3.451  2.793   1.00 27.90 ? 164 ASP A CG    1 
ATOM   1306 O OD1   . ASP A 1 169 ? 31.732 -3.523  3.977   1.00 31.75 ? 164 ASP A OD1   1 
ATOM   1307 O OD2   . ASP A 1 169 ? 31.747 -4.235  1.901   1.00 30.96 ? 164 ASP A OD2   1 
ATOM   1308 N N     . GLU A 1 170 ? 35.229 -4.983  3.026   1.00 26.27 ? 165 GLU A N     1 
ATOM   1309 C CA    . GLU A 1 170 ? 35.912 -6.175  2.541   1.00 34.38 ? 165 GLU A CA    1 
ATOM   1310 C C     . GLU A 1 170 ? 35.106 -6.939  1.502   1.00 31.74 ? 165 GLU A C     1 
ATOM   1311 O O     . GLU A 1 170 ? 35.642 -7.867  0.885   1.00 38.22 ? 165 GLU A O     1 
ATOM   1312 C CB    . GLU A 1 170 ? 36.272 -7.078  3.731   1.00 40.35 ? 165 GLU A CB    1 
ATOM   1313 C CG    . GLU A 1 170 ? 35.128 -7.884  4.343   1.00 38.93 ? 165 GLU A CG    1 
ATOM   1314 C CD    . GLU A 1 170 ? 35.050 -9.300  3.807   1.00 32.61 ? 165 GLU A CD    1 
ATOM   1315 O OE1   . GLU A 1 170 ? 36.072 -9.796  3.286   1.00 32.77 ? 165 GLU A OE1   1 
ATOM   1316 O OE2   . GLU A 1 170 ? 33.971 -9.921  3.917   1.00 36.43 ? 165 GLU A OE2   1 
ATOM   1317 N N     . PHE A 1 171 ? 33.848 -6.558  1.280   1.00 30.33 ? 166 PHE A N     1 
ATOM   1318 C CA    . PHE A 1 171 ? 33.014 -7.147  0.242   1.00 27.29 ? 166 PHE A CA    1 
ATOM   1319 C C     . PHE A 1 171 ? 32.723 -6.173  -0.890  1.00 25.13 ? 166 PHE A C     1 
ATOM   1320 O O     . PHE A 1 171 ? 32.424 -6.612  -2.004  1.00 25.55 ? 166 PHE A O     1 
ATOM   1321 C CB    . PHE A 1 171 ? 31.691 -7.638  0.863   1.00 26.41 ? 166 PHE A CB    1 
ATOM   1322 C CG    . PHE A 1 171 ? 30.739 -8.291  -0.109  1.00 23.44 ? 166 PHE A CG    1 
ATOM   1323 C CD1   . PHE A 1 171 ? 31.200 -9.122  -1.118  1.00 31.72 ? 166 PHE A CD1   1 
ATOM   1324 C CD2   . PHE A 1 171 ? 29.377 -8.076  -0.005  1.00 20.11 ? 166 PHE A CD2   1 
ATOM   1325 C CE1   . PHE A 1 171 ? 30.317 -9.716  -2.006  1.00 27.83 ? 166 PHE A CE1   1 
ATOM   1326 C CE2   . PHE A 1 171 ? 28.496 -8.667  -0.889  1.00 22.46 ? 166 PHE A CE2   1 
ATOM   1327 C CZ    . PHE A 1 171 ? 28.966 -9.487  -1.888  1.00 25.20 ? 166 PHE A CZ    1 
ATOM   1328 N N     . LEU A 1 172 ? 32.851 -4.865  -0.643  1.00 26.04 ? 167 LEU A N     1 
ATOM   1329 C CA    . LEU A 1 172 ? 32.418 -3.850  -1.593  1.00 23.18 ? 167 LEU A CA    1 
ATOM   1330 C C     . LEU A 1 172 ? 33.376 -2.673  -1.725  1.00 22.72 ? 167 LEU A C     1 
ATOM   1331 O O     . LEU A 1 172 ? 33.041 -1.710  -2.422  1.00 23.07 ? 167 LEU A O     1 
ATOM   1332 C CB    . LEU A 1 172 ? 31.031 -3.314  -1.191  1.00 26.51 ? 167 LEU A CB    1 
ATOM   1333 C CG    . LEU A 1 172 ? 29.837 -4.263  -1.288  1.00 22.16 ? 167 LEU A CG    1 
ATOM   1334 C CD1   . LEU A 1 172 ? 28.601 -3.606  -0.707  1.00 17.83 ? 167 LEU A CD1   1 
ATOM   1335 C CD2   . LEU A 1 172 ? 29.595 -4.664  -2.729  1.00 21.73 ? 167 LEU A CD2   1 
ATOM   1336 N N     . GLY A 1 173 ? 34.555 -2.723  -1.103  1.00 26.69 ? 168 GLY A N     1 
ATOM   1337 C CA    . GLY A 1 173 ? 35.367 -1.520  -0.980  1.00 23.78 ? 168 GLY A CA    1 
ATOM   1338 C C     . GLY A 1 173 ? 36.003 -1.074  -2.284  1.00 23.67 ? 168 GLY A C     1 
ATOM   1339 O O     . GLY A 1 173 ? 35.938 0.106   -2.644  1.00 21.64 ? 168 GLY A O     1 
ATOM   1340 N N     . GLU A 1 174 ? 36.636 -2.008  -3.004  1.00 31.73 ? 169 GLU A N     1 
ATOM   1341 C CA    . GLU A 1 174 ? 37.370 -1.645  -4.214  1.00 27.85 ? 169 GLU A CA    1 
ATOM   1342 C C     . GLU A 1 174 ? 36.446 -1.059  -5.271  1.00 23.44 ? 169 GLU A C     1 
ATOM   1343 O O     . GLU A 1 174 ? 36.868 -0.202  -6.057  1.00 24.19 ? 169 GLU A O     1 
ATOM   1344 C CB    . GLU A 1 174 ? 38.101 -2.867  -4.772  1.00 27.79 ? 169 GLU A CB    1 
ATOM   1345 C CG    . GLU A 1 174 ? 39.494 -2.594  -5.328  1.00 26.64 ? 169 GLU A CG    1 
ATOM   1346 C CD    . GLU A 1 174 ? 40.429 -1.953  -4.312  1.00 24.70 ? 169 GLU A CD    1 
ATOM   1347 O OE1   . GLU A 1 174 ? 40.372 -2.334  -3.122  1.00 26.33 ? 169 GLU A OE1   1 
ATOM   1348 O OE2   . GLU A 1 174 ? 41.242 -1.094  -4.706  1.00 24.89 ? 169 GLU A OE2   1 
ATOM   1349 N N     . MET A 1 175 ? 35.186 -1.511  -5.305  1.00 25.31 ? 170 MET A N     1 
ATOM   1350 C CA    . MET A 1 175 ? 34.196 -0.926  -6.204  1.00 20.98 ? 170 MET A CA    1 
ATOM   1351 C C     . MET A 1 175 ? 33.822 0.485   -5.772  1.00 19.47 ? 170 MET A C     1 
ATOM   1352 O O     . MET A 1 175 ? 33.575 1.352   -6.615  1.00 17.16 ? 170 MET A O     1 
ATOM   1353 C CB    . MET A 1 175 ? 32.949 -1.804  -6.249  1.00 21.35 ? 170 MET A CB    1 
ATOM   1354 C CG    . MET A 1 175 ? 33.075 -3.030  -7.131  1.00 23.38 ? 170 MET A CG    1 
ATOM   1355 S SD    . MET A 1 175 ? 31.752 -4.197  -6.789  1.00 26.14 ? 170 MET A SD    1 
ATOM   1356 C CE    . MET A 1 175 ? 32.280 -4.818  -5.197  1.00 24.90 ? 170 MET A CE    1 
ATOM   1357 N N     . VAL A 1 176 ? 33.769 0.728   -4.461  1.00 26.14 ? 171 VAL A N     1 
ATOM   1358 C CA    . VAL A 1 176 ? 33.468 2.064   -3.954  1.00 23.53 ? 171 VAL A CA    1 
ATOM   1359 C C     . VAL A 1 176 ? 34.615 3.021   -4.259  1.00 22.07 ? 171 VAL A C     1 
ATOM   1360 O O     . VAL A 1 176 ? 34.401 4.156   -4.702  1.00 19.59 ? 171 VAL A O     1 
ATOM   1361 C CB    . VAL A 1 176 ? 33.161 2.002   -2.446  1.00 19.88 ? 171 VAL A CB    1 
ATOM   1362 C CG1   . VAL A 1 176 ? 33.341 3.367   -1.794  1.00 20.28 ? 171 VAL A CG1   1 
ATOM   1363 C CG2   . VAL A 1 176 ? 31.756 1.469   -2.215  1.00 20.94 ? 171 VAL A CG2   1 
ATOM   1364 N N     . LYS A 1 177 ? 35.852 2.571   -4.034  1.00 23.72 ? 172 LYS A N     1 
ATOM   1365 C CA    . LYS A 1 177 ? 37.013 3.412   -4.308  1.00 24.84 ? 172 LYS A CA    1 
ATOM   1366 C C     . LYS A 1 177 ? 37.067 3.831   -5.773  1.00 23.09 ? 172 LYS A C     1 
ATOM   1367 O O     . LYS A 1 177 ? 37.440 4.968   -6.090  1.00 22.16 ? 172 LYS A O     1 
ATOM   1368 C CB    . LYS A 1 177 ? 38.293 2.671   -3.917  1.00 27.77 ? 172 LYS A CB    1 
ATOM   1369 C CG    . LYS A 1 177 ? 38.564 2.653   -2.420  1.00 23.33 ? 172 LYS A CG    1 
ATOM   1370 C CD    . LYS A 1 177 ? 39.940 2.099   -2.098  1.00 21.75 ? 172 LYS A CD    1 
ATOM   1371 C CE    . LYS A 1 177 ? 40.039 1.727   -0.629  1.00 20.69 ? 172 LYS A CE    1 
ATOM   1372 N NZ    . LYS A 1 177 ? 41.420 1.342   -0.233  1.00 26.56 ? 172 LYS A NZ    1 
ATOM   1373 N N     . ASN A 1 178 ? 36.680 2.937   -6.681  1.00 24.88 ? 173 ASN A N     1 
ATOM   1374 C CA    . ASN A 1 178 ? 36.817 3.206   -8.107  1.00 30.45 ? 173 ASN A CA    1 
ATOM   1375 C C     . ASN A 1 178 ? 35.575 3.828   -8.732  1.00 28.87 ? 173 ASN A C     1 
ATOM   1376 O O     . ASN A 1 178 ? 35.698 4.577   -9.707  1.00 32.00 ? 173 ASN A O     1 
ATOM   1377 C CB    . ASN A 1 178 ? 37.163 1.919   -8.860  1.00 30.57 ? 173 ASN A CB    1 
ATOM   1378 C CG    . ASN A 1 178 ? 38.618 1.526   -8.705  1.00 28.64 ? 173 ASN A CG    1 
ATOM   1379 O OD1   . ASN A 1 178 ? 39.518 2.344   -8.893  1.00 27.42 ? 173 ASN A OD1   1 
ATOM   1380 N ND2   . ASN A 1 178 ? 38.856 0.262   -8.379  1.00 43.82 ? 173 ASN A ND2   1 
ATOM   1381 N N     . GLN A 1 179 ? 34.387 3.549   -8.201  1.00 29.83 ? 174 GLN A N     1 
ATOM   1382 C CA    . GLN A 1 179 ? 33.148 3.911   -8.878  1.00 28.06 ? 174 GLN A CA    1 
ATOM   1383 C C     . GLN A 1 179 ? 32.282 4.908   -8.124  1.00 22.13 ? 174 GLN A C     1 
ATOM   1384 O O     . GLN A 1 179 ? 31.564 5.677   -8.766  1.00 24.60 ? 174 GLN A O     1 
ATOM   1385 C CB    . GLN A 1 179 ? 32.322 2.647   -9.163  1.00 26.70 ? 174 GLN A CB    1 
ATOM   1386 C CG    . GLN A 1 179 ? 33.086 1.609   -9.969  1.00 24.42 ? 174 GLN A CG    1 
ATOM   1387 C CD    . GLN A 1 179 ? 32.263 0.380   -10.280 1.00 21.28 ? 174 GLN A CD    1 
ATOM   1388 O OE1   . GLN A 1 179 ? 32.568 -0.718  -9.810  1.00 20.19 ? 174 GLN A OE1   1 
ATOM   1389 N NE2   . GLN A 1 179 ? 31.213 0.555   -11.076 1.00 27.10 ? 174 GLN A NE2   1 
ATOM   1390 N N     . LEU A 1 180 ? 32.328 4.928   -6.796  1.00 24.93 ? 175 LEU A N     1 
ATOM   1391 C CA    . LEU A 1 180 ? 31.462 5.800   -6.013  1.00 20.38 ? 175 LEU A CA    1 
ATOM   1392 C C     . LEU A 1 180 ? 32.094 7.180   -5.876  1.00 18.79 ? 175 LEU A C     1 
ATOM   1393 O O     . LEU A 1 180 ? 33.221 7.307   -5.389  1.00 19.84 ? 175 LEU A O     1 
ATOM   1394 C CB    . LEU A 1 180 ? 31.181 5.207   -4.633  1.00 18.48 ? 175 LEU A CB    1 
ATOM   1395 C CG    . LEU A 1 180 ? 30.210 6.061   -3.813  1.00 20.69 ? 175 LEU A CG    1 
ATOM   1396 C CD1   . LEU A 1 180 ? 28.838 6.070   -4.467  1.00 24.60 ? 175 LEU A CD1   1 
ATOM   1397 C CD2   . LEU A 1 180 ? 30.116 5.607   -2.361  1.00 17.75 ? 175 LEU A CD2   1 
ATOM   1398 N N     . ILE A 1 181 ? 31.362 8.207   -6.302  1.00 24.74 ? 176 ILE A N     1 
ATOM   1399 C CA    . ILE A 1 181 ? 31.728 9.599   -6.075  1.00 25.47 ? 176 ILE A CA    1 
ATOM   1400 C C     . ILE A 1 181 ? 30.718 10.200  -5.106  1.00 17.66 ? 176 ILE A C     1 
ATOM   1401 O O     . ILE A 1 181 ? 29.505 10.126  -5.336  1.00 16.31 ? 176 ILE A O     1 
ATOM   1402 C CB    . ILE A 1 181 ? 31.793 10.394  -7.392  1.00 23.02 ? 176 ILE A CB    1 
ATOM   1403 C CG1   . ILE A 1 181 ? 32.829 9.776   -8.335  1.00 18.52 ? 176 ILE A CG1   1 
ATOM   1404 C CG2   . ILE A 1 181 ? 32.110 11.864  -7.125  1.00 19.57 ? 176 ILE A CG2   1 
ATOM   1405 C CD1   . ILE A 1 181 ? 32.737 10.266  -9.765  1.00 23.42 ? 176 ILE A CD1   1 
ATOM   1406 N N     . TYR A 1 182 ? 31.222 10.781  -4.023  1.00 15.28 ? 177 TYR A N     1 
ATOM   1407 C CA    . TYR A 1 182 ? 30.407 11.377  -2.976  1.00 15.98 ? 177 TYR A CA    1 
ATOM   1408 C C     . TYR A 1 182 ? 30.547 12.892  -3.055  1.00 13.82 ? 177 TYR A C     1 
ATOM   1409 O O     . TYR A 1 182 ? 31.666 13.413  -3.110  1.00 16.26 ? 177 TYR A O     1 
ATOM   1410 C CB    . TYR A 1 182 ? 30.842 10.852  -1.606  1.00 20.66 ? 177 TYR A CB    1 
ATOM   1411 C CG    . TYR A 1 182 ? 30.239 11.552  -0.413  1.00 15.00 ? 177 TYR A CG    1 
ATOM   1412 C CD1   . TYR A 1 182 ? 28.888 11.871  -0.373  1.00 14.07 ? 177 TYR A CD1   1 
ATOM   1413 C CD2   . TYR A 1 182 ? 31.024 11.888  0.674   1.00 14.86 ? 177 TYR A CD2   1 
ATOM   1414 C CE1   . TYR A 1 182 ? 28.340 12.505  0.724   1.00 17.84 ? 177 TYR A CE1   1 
ATOM   1415 C CE2   . TYR A 1 182 ? 30.490 12.521  1.774   1.00 19.26 ? 177 TYR A CE2   1 
ATOM   1416 C CZ    . TYR A 1 182 ? 29.147 12.829  1.796   1.00 18.84 ? 177 TYR A CZ    1 
ATOM   1417 O OH    . TYR A 1 182 ? 28.618 13.464  2.898   1.00 20.45 ? 177 TYR A OH    1 
ATOM   1418 N N     . TYR A 1 183 ? 29.413 13.593  -3.078  1.00 15.80 ? 178 TYR A N     1 
ATOM   1419 C CA    . TYR A 1 183 ? 29.373 15.042  -3.286  1.00 18.42 ? 178 TYR A CA    1 
ATOM   1420 C C     . TYR A 1 183 ? 28.432 15.689  -2.280  1.00 15.99 ? 178 TYR A C     1 
ATOM   1421 O O     . TYR A 1 183 ? 27.248 15.907  -2.567  1.00 14.74 ? 178 TYR A O     1 
ATOM   1422 C CB    . TYR A 1 183 ? 28.954 15.372  -4.717  1.00 15.97 ? 178 TYR A CB    1 
ATOM   1423 C CG    . TYR A 1 183 ? 29.099 16.828  -5.094  1.00 14.93 ? 178 TYR A CG    1 
ATOM   1424 C CD1   . TYR A 1 183 ? 30.336 17.371  -5.387  1.00 21.57 ? 178 TYR A CD1   1 
ATOM   1425 C CD2   . TYR A 1 183 ? 27.988 17.656  -5.172  1.00 17.06 ? 178 TYR A CD2   1 
ATOM   1426 C CE1   . TYR A 1 183 ? 30.468 18.699  -5.733  1.00 21.74 ? 178 TYR A CE1   1 
ATOM   1427 C CE2   . TYR A 1 183 ? 28.110 18.987  -5.519  1.00 20.67 ? 178 TYR A CE2   1 
ATOM   1428 C CZ    . TYR A 1 183 ? 29.352 19.504  -5.800  1.00 22.97 ? 178 TYR A CZ    1 
ATOM   1429 O OH    . TYR A 1 183 ? 29.476 20.829  -6.151  1.00 26.71 ? 178 TYR A OH    1 
ATOM   1430 N N     . PRO A 1 184 ? 28.923 16.013  -1.089  1.00 16.63 ? 179 PRO A N     1 
ATOM   1431 C CA    . PRO A 1 184 ? 28.092 16.744  -0.129  1.00 15.33 ? 179 PRO A CA    1 
ATOM   1432 C C     . PRO A 1 184 ? 28.123 18.245  -0.380  1.00 18.45 ? 179 PRO A C     1 
ATOM   1433 O O     . PRO A 1 184 ? 29.161 18.827  -0.706  1.00 18.81 ? 179 PRO A O     1 
ATOM   1434 C CB    . PRO A 1 184 ? 28.728 16.389  1.218   1.00 12.92 ? 179 PRO A CB    1 
ATOM   1435 C CG    . PRO A 1 184 ? 30.159 16.147  0.892   1.00 14.32 ? 179 PRO A CG    1 
ATOM   1436 C CD    . PRO A 1 184 ? 30.254 15.702  -0.545  1.00 12.26 ? 179 PRO A CD    1 
ATOM   1437 N N     . THR A 1 185 ? 26.961 18.875  -0.242  1.00 19.41 ? 180 THR A N     1 
ATOM   1438 C CA    . THR A 1 185 ? 26.854 20.319  -0.366  1.00 18.96 ? 180 THR A CA    1 
ATOM   1439 C C     . THR A 1 185 ? 26.006 20.863  0.774   1.00 17.09 ? 180 THR A C     1 
ATOM   1440 O O     . THR A 1 185 ? 25.074 20.208  1.247   1.00 17.38 ? 180 THR A O     1 
ATOM   1441 C CB    . THR A 1 185 ? 26.271 20.736  -1.727  1.00 18.55 ? 180 THR A CB    1 
ATOM   1442 O OG1   . THR A 1 185 ? 26.374 22.158  -1.877  1.00 18.23 ? 180 THR A OG1   1 
ATOM   1443 C CG2   . THR A 1 185 ? 24.821 20.303  -1.860  1.00 17.93 ? 180 THR A CG2   1 
ATOM   1444 N N     . VAL A 1 186 ? 26.363 22.067  1.222   1.00 22.77 ? 181 VAL A N     1 
ATOM   1445 C CA    . VAL A 1 186 ? 25.726 22.732  2.353   1.00 25.73 ? 181 VAL A CA    1 
ATOM   1446 C C     . VAL A 1 186 ? 25.346 24.146  1.927   1.00 21.74 ? 181 VAL A C     1 
ATOM   1447 O O     . VAL A 1 186 ? 26.109 24.815  1.222   1.00 20.18 ? 181 VAL A O     1 
ATOM   1448 C CB    . VAL A 1 186 ? 26.660 22.753  3.586   1.00 22.15 ? 181 VAL A CB    1 
ATOM   1449 C CG1   . VAL A 1 186 ? 26.031 23.515  4.743   1.00 20.80 ? 181 VAL A CG1   1 
ATOM   1450 C CG2   . VAL A 1 186 ? 27.027 21.339  4.002   1.00 16.93 ? 181 VAL A CG2   1 
ATOM   1451 N N     . THR A 1 187 ? 24.165 24.603  2.349   1.00 25.30 ? 182 THR A N     1 
ATOM   1452 C CA    . THR A 1 187 ? 23.660 25.915  1.948   1.00 30.60 ? 182 THR A CA    1 
ATOM   1453 C C     . THR A 1 187 ? 23.940 27.010  2.975   1.00 22.31 ? 182 THR A C     1 
ATOM   1454 O O     . THR A 1 187 ? 24.494 28.057  2.623   1.00 20.16 ? 182 THR A O     1 
ATOM   1455 C CB    . THR A 1 187 ? 22.149 25.849  1.670   1.00 18.23 ? 182 THR A CB    1 
ATOM   1456 O OG1   . THR A 1 187 ? 21.500 25.079  2.688   1.00 15.99 ? 182 THR A OG1   1 
ATOM   1457 C CG2   . THR A 1 187 ? 21.883 25.206  0.323   1.00 18.52 ? 182 THR A CG2   1 
ATOM   1458 N N     . ARG A 1 188 ? 23.584 26.788  4.242   1.00 18.82 ? 183 ARG A N     1 
ATOM   1459 C CA    . ARG A 1 188 ? 23.500 27.858  5.228   1.00 22.36 ? 183 ARG A CA    1 
ATOM   1460 C C     . ARG A 1 188 ? 24.653 27.869  6.227   1.00 24.35 ? 183 ARG A C     1 
ATOM   1461 O O     . ARG A 1 188 ? 24.565 28.558  7.250   1.00 25.86 ? 183 ARG A O     1 
ATOM   1462 C CB    . ARG A 1 188 ? 22.168 27.769  5.974   1.00 17.93 ? 183 ARG A CB    1 
ATOM   1463 C CG    . ARG A 1 188 ? 20.979 27.941  5.065   1.00 16.44 ? 183 ARG A CG    1 
ATOM   1464 C CD    . ARG A 1 188 ? 19.684 28.008  5.835   1.00 16.22 ? 183 ARG A CD    1 
ATOM   1465 N NE    . ARG A 1 188 ? 18.548 27.937  4.927   1.00 19.53 ? 183 ARG A NE    1 
ATOM   1466 C CZ    . ARG A 1 188 ? 17.281 27.883  5.312   1.00 17.52 ? 183 ARG A CZ    1 
ATOM   1467 N NH1   . ARG A 1 188 ? 16.943 27.950  6.590   1.00 18.20 ? 183 ARG A NH1   1 
ATOM   1468 N NH2   . ARG A 1 188 ? 16.330 27.759  4.392   1.00 17.35 ? 183 ARG A NH2   1 
ATOM   1469 N N     . GLU A 1 189 ? 25.725 27.132  5.964   1.00 20.54 ? 184 GLU A N     1 
ATOM   1470 C CA    . GLU A 1 189 ? 26.928 27.184  6.779   1.00 18.68 ? 184 GLU A CA    1 
ATOM   1471 C C     . GLU A 1 189 ? 28.138 27.095  5.866   1.00 17.84 ? 184 GLU A C     1 
ATOM   1472 O O     . GLU A 1 189 ? 28.054 26.509  4.780   1.00 22.54 ? 184 GLU A O     1 
ATOM   1473 C CB    . GLU A 1 189 ? 26.981 26.051  7.817   1.00 22.55 ? 184 GLU A CB    1 
ATOM   1474 C CG    . GLU A 1 189 ? 26.091 26.275  9.028   1.00 23.47 ? 184 GLU A CG    1 
ATOM   1475 C CD    . GLU A 1 189 ? 26.412 25.328  10.170  1.00 21.70 ? 184 GLU A CD    1 
ATOM   1476 O OE1   . GLU A 1 189 ? 26.081 25.659  11.330  1.00 30.94 ? 184 GLU A OE1   1 
ATOM   1477 O OE2   . GLU A 1 189 ? 26.997 24.255  9.910   1.00 17.45 ? 184 GLU A OE2   1 
ATOM   1478 N N     . PRO A 1 190 ? 29.272 27.669  6.272   1.00 22.07 ? 185 PRO A N     1 
ATOM   1479 C CA    . PRO A 1 190 ? 30.473 27.603  5.425   1.00 19.41 ? 185 PRO A CA    1 
ATOM   1480 C C     . PRO A 1 190 ? 30.982 26.172  5.310   1.00 19.81 ? 185 PRO A C     1 
ATOM   1481 O O     . PRO A 1 190 ? 31.111 25.454  6.306   1.00 17.17 ? 185 PRO A O     1 
ATOM   1482 C CB    . PRO A 1 190 ? 31.480 28.505  6.151   1.00 18.21 ? 185 PRO A CB    1 
ATOM   1483 C CG    . PRO A 1 190 ? 30.673 29.315  7.119   1.00 19.12 ? 185 PRO A CG    1 
ATOM   1484 C CD    . PRO A 1 190 ? 29.478 28.495  7.473   1.00 20.87 ? 185 PRO A CD    1 
ATOM   1485 N N     . TYR A 1 191 ? 31.263 25.762  4.079   1.00 19.63 ? 186 TYR A N     1 
ATOM   1486 C CA    . TYR A 1 191 ? 31.673 24.397  3.791   1.00 22.24 ? 186 TYR A CA    1 
ATOM   1487 C C     . TYR A 1 191 ? 32.437 24.434  2.478   1.00 24.59 ? 186 TYR A C     1 
ATOM   1488 O O     . TYR A 1 191 ? 32.399 25.431  1.752   1.00 26.11 ? 186 TYR A O     1 
ATOM   1489 C CB    . TYR A 1 191 ? 30.453 23.465  3.741   1.00 21.40 ? 186 TYR A CB    1 
ATOM   1490 C CG    . TYR A 1 191 ? 30.755 21.982  3.658   1.00 20.82 ? 186 TYR A CG    1 
ATOM   1491 C CD1   . TYR A 1 191 ? 31.336 21.311  4.725   1.00 20.96 ? 186 TYR A CD1   1 
ATOM   1492 C CD2   . TYR A 1 191 ? 30.408 21.244  2.533   1.00 19.71 ? 186 TYR A CD2   1 
ATOM   1493 C CE1   . TYR A 1 191 ? 31.596 19.952  4.660   1.00 24.40 ? 186 TYR A CE1   1 
ATOM   1494 C CE2   . TYR A 1 191 ? 30.660 19.889  2.460   1.00 21.30 ? 186 TYR A CE2   1 
ATOM   1495 C CZ    . TYR A 1 191 ? 31.253 19.246  3.525   1.00 22.44 ? 186 TYR A CZ    1 
ATOM   1496 O OH    . TYR A 1 191 ? 31.503 17.893  3.453   1.00 22.55 ? 186 TYR A OH    1 
ATOM   1497 N N     . LYS A 1 192 ? 33.152 23.344  2.185   1.00 25.11 ? 187 LYS A N     1 
ATOM   1498 C CA    . LYS A 1 192 ? 33.941 23.313  0.956   1.00 21.21 ? 187 LYS A CA    1 
ATOM   1499 C C     . LYS A 1 192 ? 33.059 23.516  -0.269  1.00 19.43 ? 187 LYS A C     1 
ATOM   1500 O O     . LYS A 1 192 ? 33.423 24.261  -1.186  1.00 19.35 ? 187 LYS A O     1 
ATOM   1501 C CB    . LYS A 1 192 ? 34.737 22.008  0.860   1.00 22.86 ? 187 LYS A CB    1 
ATOM   1502 C CG    . LYS A 1 192 ? 33.938 20.720  0.967   1.00 22.98 ? 187 LYS A CG    1 
ATOM   1503 C CD    . LYS A 1 192 ? 34.858 19.520  0.727   1.00 27.37 ? 187 LYS A CD    1 
ATOM   1504 C CE    . LYS A 1 192 ? 34.295 18.222  1.301   1.00 20.02 ? 187 LYS A CE    1 
ATOM   1505 N NZ    . LYS A 1 192 ? 33.013 17.819  0.657   1.00 18.34 ? 187 LYS A NZ    1 
ATOM   1506 N N     . THR A 1 193 ? 31.886 22.890  -0.289  1.00 24.42 ? 188 THR A N     1 
ATOM   1507 C CA    . THR A 1 193 ? 30.888 23.101  -1.328  1.00 25.47 ? 188 THR A CA    1 
ATOM   1508 C C     . THR A 1 193 ? 29.707 23.869  -0.748  1.00 21.87 ? 188 THR A C     1 
ATOM   1509 O O     . THR A 1 193 ? 29.316 23.644  0.400   1.00 22.79 ? 188 THR A O     1 
ATOM   1510 C CB    . THR A 1 193 ? 30.410 21.769  -1.913  1.00 23.23 ? 188 THR A CB    1 
ATOM   1511 O OG1   . THR A 1 193 ? 31.536 20.908  -2.126  1.00 29.66 ? 188 THR A OG1   1 
ATOM   1512 C CG2   . THR A 1 193 ? 29.693 21.995  -3.232  1.00 21.01 ? 188 THR A CG2   1 
ATOM   1513 N N     . ARG A 1 194 ? 29.141 24.775  -1.540  1.00 25.96 ? 189 ARG A N     1 
ATOM   1514 C CA    . ARG A 1 194 ? 28.036 25.605  -1.086  1.00 30.25 ? 189 ARG A CA    1 
ATOM   1515 C C     . ARG A 1 194 ? 26.914 25.604  -2.118  1.00 33.25 ? 189 ARG A C     1 
ATOM   1516 O O     . ARG A 1 194 ? 27.118 25.267  -3.288  1.00 27.36 ? 189 ARG A O     1 
ATOM   1517 C CB    . ARG A 1 194 ? 28.493 27.045  -0.809  1.00 25.38 ? 189 ARG A CB    1 
ATOM   1518 C CG    . ARG A 1 194 ? 29.544 27.165  0.277   1.00 19.78 ? 189 ARG A CG    1 
ATOM   1519 C CD    . ARG A 1 194 ? 28.950 26.796  1.629   1.00 22.68 ? 189 ARG A CD    1 
ATOM   1520 N NE    . ARG A 1 194 ? 27.896 27.715  2.043   1.00 23.21 ? 189 ARG A NE    1 
ATOM   1521 C CZ    . ARG A 1 194 ? 28.097 28.951  2.480   1.00 20.16 ? 189 ARG A CZ    1 
ATOM   1522 N NH1   . ARG A 1 194 ? 29.318 29.439  2.644   1.00 20.83 ? 189 ARG A NH1   1 
ATOM   1523 N NH2   . ARG A 1 194 ? 27.047 29.713  2.769   1.00 24.55 ? 189 ARG A NH2   1 
ATOM   1524 N N     . GLY A 1 195 ? 25.719 25.982  -1.661  1.00 34.75 ? 190 GLY A N     1 
ATOM   1525 C CA    . GLY A 1 195 ? 24.577 26.208  -2.530  1.00 36.29 ? 190 GLY A CA    1 
ATOM   1526 C C     . GLY A 1 195 ? 23.649 25.012  -2.601  1.00 32.11 ? 190 GLY A C     1 
ATOM   1527 O O     . GLY A 1 195 ? 23.901 23.945  -2.033  1.00 31.26 ? 190 GLY A O     1 
ATOM   1528 N N     . ARG A 1 196 ? 22.538 25.218  -3.312  1.00 30.98 ? 191 ARG A N     1 
ATOM   1529 C CA    . ARG A 1 196 ? 21.599 24.144  -3.612  1.00 22.24 ? 191 ARG A CA    1 
ATOM   1530 C C     . ARG A 1 196 ? 22.143 23.254  -4.721  1.00 27.36 ? 191 ARG A C     1 
ATOM   1531 O O     . ARG A 1 196 ? 22.914 23.698  -5.578  1.00 28.41 ? 191 ARG A O     1 
ATOM   1532 C CB    . ARG A 1 196 ? 20.242 24.701  -4.042  1.00 24.34 ? 191 ARG A CB    1 
ATOM   1533 C CG    . ARG A 1 196 ? 19.395 25.273  -2.926  1.00 26.58 ? 191 ARG A CG    1 
ATOM   1534 C CD    . ARG A 1 196 ? 18.019 25.655  -3.454  1.00 32.13 ? 191 ARG A CD    1 
ATOM   1535 N NE    . ARG A 1 196 ? 16.928 25.251  -2.570  1.00 49.78 ? 191 ARG A NE    1 
ATOM   1536 C CZ    . ARG A 1 196 ? 16.594 23.997  -2.288  1.00 38.36 ? 191 ARG A CZ    1 
ATOM   1537 N NH1   . ARG A 1 196 ? 17.227 22.971  -2.831  1.00 29.28 ? 191 ARG A NH1   1 
ATOM   1538 N NH2   . ARG A 1 196 ? 15.592 23.769  -1.442  1.00 40.00 ? 191 ARG A NH2   1 
ATOM   1539 N N     . LEU A 1 197 ? 21.732 21.982  -4.704  1.00 26.39 ? 192 LEU A N     1 
ATOM   1540 C CA    . LEU A 1 197 ? 22.158 21.085  -5.774  1.00 25.64 ? 192 LEU A CA    1 
ATOM   1541 C C     . LEU A 1 197 ? 21.525 21.479  -7.099  1.00 27.00 ? 192 LEU A C     1 
ATOM   1542 O O     . LEU A 1 197 ? 22.102 21.216  -8.161  1.00 28.43 ? 192 LEU A O     1 
ATOM   1543 C CB    . LEU A 1 197 ? 21.829 19.627  -5.436  1.00 23.14 ? 192 LEU A CB    1 
ATOM   1544 C CG    . LEU A 1 197 ? 20.388 19.114  -5.367  1.00 17.12 ? 192 LEU A CG    1 
ATOM   1545 C CD1   . LEU A 1 197 ? 19.891 18.639  -6.727  1.00 16.57 ? 192 LEU A CD1   1 
ATOM   1546 C CD2   . LEU A 1 197 ? 20.300 17.982  -4.354  1.00 19.62 ? 192 LEU A CD2   1 
ATOM   1547 N N     . THR A 1 198 ? 20.346 22.105  -7.055  1.00 27.71 ? 193 THR A N     1 
ATOM   1548 C CA    . THR A 1 198 ? 19.727 22.601  -8.280  1.00 29.23 ? 193 THR A CA    1 
ATOM   1549 C C     . THR A 1 198 ? 20.535 23.750  -8.871  1.00 24.59 ? 193 THR A C     1 
ATOM   1550 O O     . THR A 1 198 ? 20.720 23.823  -10.090 1.00 23.70 ? 193 THR A O     1 
ATOM   1551 C CB    . THR A 1 198 ? 18.287 23.039  -8.005  1.00 27.12 ? 193 THR A CB    1 
ATOM   1552 O OG1   . THR A 1 198 ? 18.274 24.041  -6.980  1.00 26.47 ? 193 THR A OG1   1 
ATOM   1553 C CG2   . THR A 1 198 ? 17.449 21.858  -7.549  1.00 25.86 ? 193 THR A CG2   1 
ATOM   1554 N N     . ASP A 1 199 ? 21.033 24.648  -8.015  1.00 25.13 ? 194 ASP A N     1 
ATOM   1555 C CA    . ASP A 1 199 ? 21.908 25.723  -8.469  1.00 24.19 ? 194 ASP A CA    1 
ATOM   1556 C C     . ASP A 1 199 ? 23.222 25.180  -9.012  1.00 22.12 ? 194 ASP A C     1 
ATOM   1557 O O     . ASP A 1 199 ? 23.805 25.767  -9.932  1.00 21.52 ? 194 ASP A O     1 
ATOM   1558 C CB    . ASP A 1 199 ? 22.179 26.695  -7.318  1.00 23.27 ? 194 ASP A CB    1 
ATOM   1559 C CG    . ASP A 1 199 ? 20.916 27.347  -6.794  1.00 20.56 ? 194 ASP A CG    1 
ATOM   1560 O OD1   . ASP A 1 199 ? 19.895 27.337  -7.513  1.00 34.90 ? 194 ASP A OD1   1 
ATOM   1561 O OD2   . ASP A 1 199 ? 20.943 27.868  -5.662  1.00 19.31 ? 194 ASP A OD2   1 
ATOM   1562 N N     . LEU A 1 200 ? 23.705 24.070  -8.445  1.00 30.02 ? 195 LEU A N     1 
ATOM   1563 C CA    . LEU A 1 200 ? 24.944 23.458  -8.913  1.00 25.01 ? 195 LEU A CA    1 
ATOM   1564 C C     . LEU A 1 200 ? 24.770 22.822  -10.287 1.00 23.62 ? 195 LEU A C     1 
ATOM   1565 O O     . LEU A 1 200 ? 25.709 22.824  -11.092 1.00 23.10 ? 195 LEU A O     1 
ATOM   1566 C CB    . LEU A 1 200 ? 25.419 22.421  -7.893  1.00 27.53 ? 195 LEU A CB    1 
ATOM   1567 C CG    . LEU A 1 200 ? 25.898 22.967  -6.544  1.00 26.00 ? 195 LEU A CG    1 
ATOM   1568 C CD1   . LEU A 1 200 ? 26.017 21.861  -5.507  1.00 19.05 ? 195 LEU A CD1   1 
ATOM   1569 C CD2   . LEU A 1 200 ? 27.229 23.665  -6.711  1.00 25.64 ? 195 LEU A CD2   1 
ATOM   1570 N N     . ILE A 1 201 ? 23.585 22.278  -10.573 1.00 21.36 ? 196 ILE A N     1 
ATOM   1571 C CA    . ILE A 1 201 ? 23.310 21.768  -11.911 1.00 25.05 ? 196 ILE A CA    1 
ATOM   1572 C C     . ILE A 1 201 ? 23.182 22.921  -12.900 1.00 26.97 ? 196 ILE A C     1 
ATOM   1573 O O     . ILE A 1 201 ? 23.674 22.844  -14.032 1.00 33.39 ? 196 ILE A O     1 
ATOM   1574 C CB    . ILE A 1 201 ? 22.050 20.881  -11.898 1.00 27.42 ? 196 ILE A CB    1 
ATOM   1575 C CG1   . ILE A 1 201 ? 22.286 19.620  -11.061 1.00 29.83 ? 196 ILE A CG1   1 
ATOM   1576 C CG2   . ILE A 1 201 ? 21.635 20.502  -13.316 1.00 22.00 ? 196 ILE A CG2   1 
ATOM   1577 C CD1   . ILE A 1 201 ? 21.019 18.861  -10.705 1.00 27.42 ? 196 ILE A CD1   1 
ATOM   1578 N N     . ARG A 1 202 ? 22.539 24.013  -12.481 1.00 26.28 ? 197 ARG A N     1 
ATOM   1579 C CA    . ARG A 1 202 ? 22.369 25.175  -13.350 1.00 27.27 ? 197 ARG A CA    1 
ATOM   1580 C C     . ARG A 1 202 ? 23.708 25.813  -13.703 1.00 32.27 ? 197 ARG A C     1 
ATOM   1581 O O     . ARG A 1 202 ? 24.048 25.963  -14.883 1.00 27.03 ? 197 ARG A O     1 
ATOM   1582 C CB    . ARG A 1 202 ? 21.449 26.194  -12.682 1.00 22.24 ? 197 ARG A CB    1 
ATOM   1583 C CG    . ARG A 1 202 ? 20.058 25.672  -12.432 1.00 28.19 ? 197 ARG A CG    1 
ATOM   1584 C CD    . ARG A 1 202 ? 19.153 26.753  -11.880 1.00 40.11 ? 197 ARG A CD    1 
ATOM   1585 N NE    . ARG A 1 202 ? 17.988 26.177  -11.225 1.00 32.97 ? 197 ARG A NE    1 
ATOM   1586 C CZ    . ARG A 1 202 ? 16.928 25.725  -11.879 1.00 38.37 ? 197 ARG A CZ    1 
ATOM   1587 N NH1   . ARG A 1 202 ? 16.859 25.771  -13.199 1.00 44.98 ? 197 ARG A NH1   1 
ATOM   1588 N NH2   . ARG A 1 202 ? 15.917 25.204  -11.195 1.00 36.72 ? 197 ARG A NH2   1 
ATOM   1589 N N     . SER A 1 203 ? 24.484 26.203  -12.689 1.00 30.30 ? 198 SER A N     1 
ATOM   1590 C CA    . SER A 1 203 ? 25.755 26.871  -12.939 1.00 31.46 ? 198 SER A CA    1 
ATOM   1591 C C     . SER A 1 203 ? 26.781 25.965  -13.607 1.00 36.87 ? 198 SER A C     1 
ATOM   1592 O O     . SER A 1 203 ? 27.836 26.458  -14.025 1.00 43.20 ? 198 SER A O     1 
ATOM   1593 C CB    . SER A 1 203 ? 26.338 27.411  -11.633 1.00 27.09 ? 198 SER A CB    1 
ATOM   1594 O OG    . SER A 1 203 ? 26.691 26.352  -10.766 1.00 28.92 ? 198 SER A OG    1 
ATOM   1595 N N     . GLY A 1 204 ? 26.504 24.668  -13.720 1.00 36.41 ? 199 GLY A N     1 
ATOM   1596 C CA    . GLY A 1 204 ? 27.467 23.731  -14.258 1.00 32.76 ? 199 GLY A CA    1 
ATOM   1597 C C     . GLY A 1 204 ? 28.583 23.350  -13.314 1.00 33.20 ? 199 GLY A C     1 
ATOM   1598 O O     . GLY A 1 204 ? 29.508 22.641  -13.727 1.00 30.69 ? 199 GLY A O     1 
ATOM   1599 N N     . GLN A 1 205 ? 28.527 23.795  -12.055 1.00 38.12 ? 200 GLN A N     1 
ATOM   1600 C CA    . GLN A 1 205 ? 29.590 23.480  -11.106 1.00 33.76 ? 200 GLN A CA    1 
ATOM   1601 C C     . GLN A 1 205 ? 29.561 22.016  -10.686 1.00 25.42 ? 200 GLN A C     1 
ATOM   1602 O O     . GLN A 1 205 ? 30.618 21.438  -10.414 1.00 30.28 ? 200 GLN A O     1 
ATOM   1603 C CB    . GLN A 1 205 ? 29.488 24.392  -9.881  1.00 33.89 ? 200 GLN A CB    1 
ATOM   1604 C CG    . GLN A 1 205 ? 30.684 24.311  -8.947  1.00 33.59 ? 200 GLN A CG    1 
ATOM   1605 C CD    . GLN A 1 205 ? 30.389 24.875  -7.572  1.00 40.78 ? 200 GLN A CD    1 
ATOM   1606 O OE1   . GLN A 1 205 ? 29.847 25.974  -7.446  1.00 41.40 ? 200 GLN A OE1   1 
ATOM   1607 N NE2   . GLN A 1 205 ? 30.733 24.121  -6.534  1.00 39.89 ? 200 GLN A NE2   1 
ATOM   1608 N N     . LEU A 1 206 ? 28.374 21.404  -10.630 1.00 25.78 ? 201 LEU A N     1 
ATOM   1609 C CA    . LEU A 1 206 ? 28.279 19.979  -10.323 1.00 24.17 ? 201 LEU A CA    1 
ATOM   1610 C C     . LEU A 1 206 ? 29.149 19.149  -11.254 1.00 25.14 ? 201 LEU A C     1 
ATOM   1611 O O     . LEU A 1 206 ? 29.858 18.239  -10.809 1.00 21.63 ? 201 LEU A O     1 
ATOM   1612 C CB    . LEU A 1 206 ? 26.827 19.509  -10.416 1.00 34.28 ? 201 LEU A CB    1 
ATOM   1613 C CG    . LEU A 1 206 ? 26.616 17.991  -10.342 1.00 23.62 ? 201 LEU A CG    1 
ATOM   1614 C CD1   . LEU A 1 206 ? 26.990 17.440  -8.970  1.00 20.46 ? 201 LEU A CD1   1 
ATOM   1615 C CD2   . LEU A 1 206 ? 25.194 17.607  -10.723 1.00 21.20 ? 201 LEU A CD2   1 
ATOM   1616 N N     . PHE A 1 207 ? 29.104 19.444  -12.555 1.00 32.60 ? 202 PHE A N     1 
ATOM   1617 C CA    . PHE A 1 207 ? 29.895 18.682  -13.516 1.00 34.27 ? 202 PHE A CA    1 
ATOM   1618 C C     . PHE A 1 207 ? 31.374 19.042  -13.457 1.00 28.83 ? 202 PHE A C     1 
ATOM   1619 O O     . PHE A 1 207 ? 32.224 18.189  -13.734 1.00 25.95 ? 202 PHE A O     1 
ATOM   1620 C CB    . PHE A 1 207 ? 29.348 18.887  -14.929 1.00 29.14 ? 202 PHE A CB    1 
ATOM   1621 C CG    . PHE A 1 207 ? 27.895 18.534  -15.071 1.00 38.17 ? 202 PHE A CG    1 
ATOM   1622 C CD1   . PHE A 1 207 ? 27.471 17.222  -14.928 1.00 34.85 ? 202 PHE A CD1   1 
ATOM   1623 C CD2   . PHE A 1 207 ? 26.953 19.508  -15.358 1.00 42.96 ? 202 PHE A CD2   1 
ATOM   1624 C CE1   . PHE A 1 207 ? 26.133 16.891  -15.061 1.00 35.03 ? 202 PHE A CE1   1 
ATOM   1625 C CE2   . PHE A 1 207 ? 25.614 19.183  -15.495 1.00 37.33 ? 202 PHE A CE2   1 
ATOM   1626 C CZ    . PHE A 1 207 ? 25.204 17.875  -15.347 1.00 34.82 ? 202 PHE A CZ    1 
ATOM   1627 N N     . LYS A 1 208 ? 31.702 20.284  -13.098 1.00 27.07 ? 203 LYS A N     1 
ATOM   1628 C CA    . LYS A 1 208 ? 33.101 20.654  -12.923 1.00 22.30 ? 203 LYS A CA    1 
ATOM   1629 C C     . LYS A 1 208 ? 33.712 19.941  -11.722 1.00 23.15 ? 203 LYS A C     1 
ATOM   1630 O O     . LYS A 1 208 ? 34.874 19.522  -11.766 1.00 28.28 ? 203 LYS A O     1 
ATOM   1631 C CB    . LYS A 1 208 ? 33.221 22.174  -12.787 1.00 28.84 ? 203 LYS A CB    1 
ATOM   1632 C CG    . LYS A 1 208 ? 34.534 22.672  -12.188 1.00 34.26 ? 203 LYS A CG    1 
ATOM   1633 C CD    . LYS A 1 208 ? 34.837 24.125  -12.565 1.00 36.00 ? 203 LYS A CD    1 
ATOM   1634 C CE    . LYS A 1 208 ? 33.593 25.002  -12.614 1.00 27.07 ? 203 LYS A CE    1 
ATOM   1635 N NZ    . LYS A 1 208 ? 32.912 25.132  -11.296 1.00 25.10 ? 203 LYS A NZ    1 
ATOM   1636 N N     . ASP A 1 209 ? 32.936 19.762  -10.655 1.00 26.72 ? 204 ASP A N     1 
ATOM   1637 C CA    . ASP A 1 209 ? 33.485 19.245  -9.407  1.00 27.70 ? 204 ASP A CA    1 
ATOM   1638 C C     . ASP A 1 209 ? 33.645 17.729  -9.412  1.00 23.80 ? 204 ASP A C     1 
ATOM   1639 O O     . ASP A 1 209 ? 34.564 17.212  -8.770  1.00 26.33 ? 204 ASP A O     1 
ATOM   1640 C CB    . ASP A 1 209 ? 32.601 19.673  -8.238  1.00 25.57 ? 204 ASP A CB    1 
ATOM   1641 C CG    . ASP A 1 209 ? 32.562 21.179  -8.057  1.00 25.72 ? 204 ASP A CG    1 
ATOM   1642 O OD1   . ASP A 1 209 ? 33.147 21.903  -8.890  1.00 24.62 ? 204 ASP A OD1   1 
ATOM   1643 O OD2   . ASP A 1 209 ? 31.930 21.639  -7.082  1.00 30.67 ? 204 ASP A OD2   1 
ATOM   1644 N N     . VAL A 1 210 ? 32.771 17.001  -10.114 1.00 33.01 ? 205 VAL A N     1 
ATOM   1645 C CA    . VAL A 1 210 ? 32.847 15.539  -10.124 1.00 32.14 ? 205 VAL A CA    1 
ATOM   1646 C C     . VAL A 1 210 ? 33.670 14.998  -11.281 1.00 25.68 ? 205 VAL A C     1 
ATOM   1647 O O     . VAL A 1 210 ? 33.958 13.791  -11.308 1.00 20.97 ? 205 VAL A O     1 
ATOM   1648 C CB    . VAL A 1 210 ? 31.445 14.894  -10.169 1.00 31.10 ? 205 VAL A CB    1 
ATOM   1649 C CG1   . VAL A 1 210 ? 30.562 15.456  -9.063  1.00 37.34 ? 205 VAL A CG1   1 
ATOM   1650 C CG2   . VAL A 1 210 ? 30.801 15.102  -11.529 1.00 22.72 ? 205 VAL A CG2   1 
ATOM   1651 N N     . GLY A 1 211 ? 34.057 15.844  -12.234 1.00 27.07 ? 206 GLY A N     1 
ATOM   1652 C CA    . GLY A 1 211 ? 34.913 15.430  -13.326 1.00 28.93 ? 206 GLY A CA    1 
ATOM   1653 C C     . GLY A 1 211 ? 34.212 14.756  -14.483 1.00 24.22 ? 206 GLY A C     1 
ATOM   1654 O O     . GLY A 1 211 ? 34.888 14.184  -15.346 1.00 25.07 ? 206 GLY A O     1 
ATOM   1655 N N     . LEU A 1 212 ? 32.885 14.805  -14.534 1.00 32.34 ? 207 LEU A N     1 
ATOM   1656 C CA    . LEU A 1 212 ? 32.106 14.165  -15.580 1.00 32.09 ? 207 LEU A CA    1 
ATOM   1657 C C     . LEU A 1 212 ? 31.350 15.214  -16.386 1.00 35.59 ? 207 LEU A C     1 
ATOM   1658 O O     . LEU A 1 212 ? 31.019 16.284  -15.865 1.00 32.90 ? 207 LEU A O     1 
ATOM   1659 C CB    . LEU A 1 212 ? 31.111 13.159  -14.985 1.00 34.35 ? 207 LEU A CB    1 
ATOM   1660 C CG    . LEU A 1 212 ? 31.677 12.160  -13.974 1.00 29.14 ? 207 LEU A CG    1 
ATOM   1661 C CD1   . LEU A 1 212 ? 30.614 11.167  -13.542 1.00 27.42 ? 207 LEU A CD1   1 
ATOM   1662 C CD2   . LEU A 1 212 ? 32.883 11.433  -14.544 1.00 32.61 ? 207 LEU A CD2   1 
ATOM   1663 N N     . PRO A 1 213 ? 31.065 14.945  -17.657 1.00 41.79 ? 208 PRO A N     1 
ATOM   1664 C CA    . PRO A 1 213 ? 30.369 15.936  -18.485 1.00 41.36 ? 208 PRO A CA    1 
ATOM   1665 C C     . PRO A 1 213 ? 28.885 16.026  -18.148 1.00 38.99 ? 208 PRO A C     1 
ATOM   1666 O O     . PRO A 1 213 ? 28.321 15.217  -17.405 1.00 35.28 ? 208 PRO A O     1 
ATOM   1667 C CB    . PRO A 1 213 ? 30.593 15.434  -19.921 1.00 35.33 ? 208 PRO A CB    1 
ATOM   1668 C CG    . PRO A 1 213 ? 31.642 14.350  -19.810 1.00 40.06 ? 208 PRO A CG    1 
ATOM   1669 C CD    . PRO A 1 213 ? 31.469 13.770  -18.445 1.00 41.33 ? 208 PRO A CD    1 
ATOM   1670 N N     . GLU A 1 214 ? 28.259 17.047  -18.737 1.00 38.52 ? 209 GLU A N     1 
ATOM   1671 C CA    . GLU A 1 214 ? 26.868 17.401  -18.490 1.00 39.50 ? 209 GLU A CA    1 
ATOM   1672 C C     . GLU A 1 214 ? 25.947 16.221  -18.784 1.00 34.20 ? 209 GLU A C     1 
ATOM   1673 O O     . GLU A 1 214 ? 26.312 15.277  -19.492 1.00 36.55 ? 209 GLU A O     1 
ATOM   1674 C CB    . GLU A 1 214 ? 26.464 18.591  -19.365 1.00 47.34 ? 209 GLU A CB    1 
ATOM   1675 C CG    . GLU A 1 214 ? 26.982 19.950  -18.894 1.00 44.35 ? 209 GLU A CG    1 
ATOM   1676 C CD    . GLU A 1 214 ? 25.867 20.882  -18.451 1.00 43.63 ? 209 GLU A CD    1 
ATOM   1677 O OE1   . GLU A 1 214 ? 24.810 20.890  -19.114 1.00 45.87 ? 209 GLU A OE1   1 
ATOM   1678 O OE2   . GLU A 1 214 ? 26.053 21.612  -17.455 1.00 40.06 ? 209 GLU A OE2   1 
ATOM   1679 N N     . PHE A 1 215 ? 24.738 16.278  -18.220 1.00 31.72 ? 210 PHE A N     1 
ATOM   1680 C CA    . PHE A 1 215 ? 23.721 15.278  -18.525 1.00 34.50 ? 210 PHE A CA    1 
ATOM   1681 C C     . PHE A 1 215 ? 23.500 15.162  -20.029 1.00 31.74 ? 210 PHE A C     1 
ATOM   1682 O O     . PHE A 1 215 ? 23.388 16.168  -20.735 1.00 31.95 ? 210 PHE A O     1 
ATOM   1683 C CB    . PHE A 1 215 ? 22.383 15.606  -17.837 1.00 29.65 ? 210 PHE A CB    1 
ATOM   1684 C CG    . PHE A 1 215 ? 22.427 15.594  -16.334 1.00 30.54 ? 210 PHE A CG    1 
ATOM   1685 C CD1   . PHE A 1 215 ? 23.088 14.581  -15.647 1.00 27.19 ? 210 PHE A CD1   1 
ATOM   1686 C CD2   . PHE A 1 215 ? 21.736 16.551  -15.604 1.00 30.75 ? 210 PHE A CD2   1 
ATOM   1687 C CE1   . PHE A 1 215 ? 23.103 14.557  -14.259 1.00 22.90 ? 210 PHE A CE1   1 
ATOM   1688 C CE2   . PHE A 1 215 ? 21.744 16.532  -14.216 1.00 29.70 ? 210 PHE A CE2   1 
ATOM   1689 C CZ    . PHE A 1 215 ? 22.427 15.533  -13.543 1.00 25.87 ? 210 PHE A CZ    1 
ATOM   1690 N N     . ASN A 1 216 ? 23.435 13.922  -20.507 1.00 29.60 ? 211 ASN A N     1 
ATOM   1691 C CA    . ASN A 1 216 ? 23.079 13.621  -21.885 1.00 32.07 ? 211 ASN A CA    1 
ATOM   1692 C C     . ASN A 1 216 ? 22.251 12.342  -21.911 1.00 32.20 ? 211 ASN A C     1 
ATOM   1693 O O     . ASN A 1 216 ? 22.363 11.488  -21.025 1.00 26.36 ? 211 ASN A O     1 
ATOM   1694 C CB    . ASN A 1 216 ? 24.324 13.513  -22.787 1.00 27.70 ? 211 ASN A CB    1 
ATOM   1695 C CG    . ASN A 1 216 ? 25.255 12.395  -22.367 1.00 28.42 ? 211 ASN A CG    1 
ATOM   1696 O OD1   . ASN A 1 216 ? 24.979 11.220  -22.604 1.00 40.53 ? 211 ASN A OD1   1 
ATOM   1697 N ND2   . ASN A 1 216 ? 26.378 12.757  -21.756 1.00 29.35 ? 211 ASN A ND2   1 
ATOM   1698 N N     . HIS A 1 217 ? 21.403 12.230  -22.938 1.00 33.80 ? 212 HIS A N     1 
ATOM   1699 C CA    . HIS A 1 217 ? 20.354 11.216  -22.973 1.00 29.98 ? 212 HIS A CA    1 
ATOM   1700 C C     . HIS A 1 217 ? 20.896 9.802   -23.113 1.00 26.14 ? 212 HIS A C     1 
ATOM   1701 O O     . HIS A 1 217 ? 20.145 8.846   -22.892 1.00 23.73 ? 212 HIS A O     1 
ATOM   1702 C CB    . HIS A 1 217 ? 19.387 11.501  -24.123 1.00 32.12 ? 212 HIS A CB    1 
ATOM   1703 C CG    . HIS A 1 217 ? 18.667 12.806  -23.993 1.00 30.81 ? 212 HIS A CG    1 
ATOM   1704 N ND1   . HIS A 1 217 ? 18.194 13.505  -25.082 1.00 33.51 ? 212 HIS A ND1   1 
ATOM   1705 C CD2   . HIS A 1 217 ? 18.366 13.553  -22.907 1.00 27.64 ? 212 HIS A CD2   1 
ATOM   1706 C CE1   . HIS A 1 217 ? 17.616 14.619  -24.669 1.00 28.98 ? 212 HIS A CE1   1 
ATOM   1707 N NE2   . HIS A 1 217 ? 17.712 14.675  -23.354 1.00 24.79 ? 212 HIS A NE2   1 
ATOM   1708 N N     . GLU A 1 218 ? 22.166 9.645   -23.478 1.00 26.92 ? 213 GLU A N     1 
ATOM   1709 C CA    . GLU A 1 218 ? 22.739 8.319   -23.660 1.00 31.47 ? 213 GLU A CA    1 
ATOM   1710 C C     . GLU A 1 218 ? 23.342 7.760   -22.375 1.00 33.30 ? 213 GLU A C     1 
ATOM   1711 O O     . GLU A 1 218 ? 23.109 6.597   -22.033 1.00 27.00 ? 213 GLU A O     1 
ATOM   1712 C CB    . GLU A 1 218 ? 23.810 8.356   -24.751 1.00 33.87 ? 213 GLU A CB    1 
ATOM   1713 C CG    . GLU A 1 218 ? 24.344 6.984   -25.127 1.00 40.91 ? 213 GLU A CG    1 
ATOM   1714 C CD    . GLU A 1 218 ? 25.686 7.051   -25.823 1.00 41.42 ? 213 GLU A CD    1 
ATOM   1715 O OE1   . GLU A 1 218 ? 25.771 6.614   -26.990 1.00 52.65 ? 213 GLU A OE1   1 
ATOM   1716 O OE2   . GLU A 1 218 ? 26.653 7.542   -25.204 1.00 47.98 ? 213 GLU A OE2   1 
ATOM   1717 N N     . ASP A 1 219 ? 24.115 8.572   -21.655 1.00 31.36 ? 214 ASP A N     1 
ATOM   1718 C CA    . ASP A 1 219 ? 24.990 8.068   -20.604 1.00 27.82 ? 214 ASP A CA    1 
ATOM   1719 C C     . ASP A 1 219 ? 24.445 8.254   -19.196 1.00 25.56 ? 214 ASP A C     1 
ATOM   1720 O O     . ASP A 1 219 ? 24.696 7.402   -18.336 1.00 24.07 ? 214 ASP A O     1 
ATOM   1721 C CB    . ASP A 1 219 ? 26.364 8.745   -20.698 1.00 33.87 ? 214 ASP A CB    1 
ATOM   1722 C CG    . ASP A 1 219 ? 27.056 8.481   -22.024 1.00 37.43 ? 214 ASP A CG    1 
ATOM   1723 O OD1   . ASP A 1 219 ? 27.229 7.298   -22.383 1.00 38.26 ? 214 ASP A OD1   1 
ATOM   1724 O OD2   . ASP A 1 219 ? 27.428 9.460   -22.704 1.00 32.25 ? 214 ASP A OD2   1 
ATOM   1725 N N     . ASP A 1 220 ? 23.715 9.335   -18.928 1.00 26.22 ? 215 ASP A N     1 
ATOM   1726 C CA    . ASP A 1 220 ? 23.360 9.707   -17.564 1.00 23.38 ? 215 ASP A CA    1 
ATOM   1727 C C     . ASP A 1 220 ? 21.948 9.260   -17.208 1.00 20.77 ? 215 ASP A C     1 
ATOM   1728 O O     . ASP A 1 220 ? 20.985 9.577   -17.914 1.00 25.43 ? 215 ASP A O     1 
ATOM   1729 C CB    . ASP A 1 220 ? 23.507 11.213  -17.354 1.00 23.68 ? 215 ASP A CB    1 
ATOM   1730 C CG    . ASP A 1 220 ? 24.923 11.692  -17.577 1.00 20.28 ? 215 ASP A CG    1 
ATOM   1731 O OD1   . ASP A 1 220 ? 25.810 11.304  -16.789 1.00 22.20 ? 215 ASP A OD1   1 
ATOM   1732 O OD2   . ASP A 1 220 ? 25.159 12.443  -18.542 1.00 26.22 ? 215 ASP A OD2   1 
ATOM   1733 N N     . ARG A 1 221 ? 21.846 8.523   -16.107 1.00 17.55 ? 216 ARG A N     1 
ATOM   1734 C CA    . ARG A 1 221 ? 20.594 8.125   -15.491 1.00 18.72 ? 216 ARG A CA    1 
ATOM   1735 C C     . ARG A 1 221 ? 20.570 8.699   -14.080 1.00 21.79 ? 216 ARG A C     1 
ATOM   1736 O O     . ARG A 1 221 ? 21.610 8.796   -13.424 1.00 22.81 ? 216 ARG A O     1 
ATOM   1737 C CB    . ARG A 1 221 ? 20.475 6.601   -15.459 1.00 19.99 ? 216 ARG A CB    1 
ATOM   1738 C CG    . ARG A 1 221 ? 20.761 5.931   -16.799 1.00 21.62 ? 216 ARG A CG    1 
ATOM   1739 C CD    . ARG A 1 221 ? 19.702 6.278   -17.842 1.00 30.02 ? 216 ARG A CD    1 
ATOM   1740 N NE    . ARG A 1 221 ? 20.031 5.753   -19.165 1.00 34.84 ? 216 ARG A NE    1 
ATOM   1741 C CZ    . ARG A 1 221 ? 20.447 6.488   -20.188 1.00 23.98 ? 216 ARG A CZ    1 
ATOM   1742 N NH1   . ARG A 1 221 ? 20.557 7.802   -20.096 1.00 20.92 ? 216 ARG A NH1   1 
ATOM   1743 N NH2   . ARG A 1 221 ? 20.756 5.888   -21.334 1.00 29.62 ? 216 ARG A NH2   1 
ATOM   1744 N N     . MET A 1 222 ? 19.388 9.107   -13.613 1.00 29.03 ? 217 MET A N     1 
ATOM   1745 C CA    . MET A 1 222 ? 19.301 9.854   -12.363 1.00 27.31 ? 217 MET A CA    1 
ATOM   1746 C C     . MET A 1 222 ? 18.215 9.300   -11.451 1.00 20.79 ? 217 MET A C     1 
ATOM   1747 O O     . MET A 1 222 ? 17.176 8.824   -11.911 1.00 18.00 ? 217 MET A O     1 
ATOM   1748 C CB    . MET A 1 222 ? 19.036 11.351  -12.617 1.00 25.46 ? 217 MET A CB    1 
ATOM   1749 C CG    . MET A 1 222 ? 19.897 11.978  -13.707 1.00 23.59 ? 217 MET A CG    1 
ATOM   1750 S SD    . MET A 1 222 ? 19.082 11.944  -15.313 1.00 23.30 ? 217 MET A SD    1 
ATOM   1751 C CE    . MET A 1 222 ? 19.954 13.238  -16.175 1.00 18.37 ? 217 MET A CE    1 
ATOM   1752 N N     . MET A 1 223 ? 18.470 9.369   -10.147 1.00 26.26 ? 218 MET A N     1 
ATOM   1753 C CA    . MET A 1 223 ? 17.478 9.067   -9.123  1.00 22.07 ? 218 MET A CA    1 
ATOM   1754 C C     . MET A 1 223 ? 17.351 10.264  -8.190  1.00 17.88 ? 218 MET A C     1 
ATOM   1755 O O     . MET A 1 223 ? 18.353 10.744  -7.652  1.00 17.29 ? 218 MET A O     1 
ATOM   1756 C CB    . MET A 1 223 ? 17.854 7.811   -8.334  1.00 24.29 ? 218 MET A CB    1 
ATOM   1757 C CG    . MET A 1 223 ? 17.748 6.518   -9.127  1.00 19.06 ? 218 MET A CG    1 
ATOM   1758 S SD    . MET A 1 223 ? 17.767 5.071   -8.063  1.00 20.67 ? 218 MET A SD    1 
ATOM   1759 C CE    . MET A 1 223 ? 17.777 3.755   -9.278  1.00 19.08 ? 218 MET A CE    1 
ATOM   1760 N N     . LEU A 1 224 ? 16.122 10.745  -8.008  1.00 20.63 ? 219 LEU A N     1 
ATOM   1761 C CA    . LEU A 1 224 ? 15.830 11.920  -7.197  1.00 17.32 ? 219 LEU A CA    1 
ATOM   1762 C C     . LEU A 1 224 ? 14.995 11.519  -5.991  1.00 15.78 ? 219 LEU A C     1 
ATOM   1763 O O     . LEU A 1 224 ? 13.937 10.903  -6.142  1.00 19.12 ? 219 LEU A O     1 
ATOM   1764 C CB    . LEU A 1 224 ? 15.087 12.991  -8.011  1.00 16.85 ? 219 LEU A CB    1 
ATOM   1765 C CG    . LEU A 1 224 ? 15.821 13.952  -8.958  1.00 18.33 ? 219 LEU A CG    1 
ATOM   1766 C CD1   . LEU A 1 224 ? 16.762 13.249  -9.926  1.00 19.81 ? 219 LEU A CD1   1 
ATOM   1767 C CD2   . LEU A 1 224 ? 14.801 14.746  -9.742  1.00 20.73 ? 219 LEU A CD2   1 
ATOM   1768 N N     . CYS A 1 225 ? 15.467 11.880  -4.800  1.00 18.09 ? 220 CYS A N     1 
ATOM   1769 C CA    . CYS A 1 225 ? 14.697 11.703  -3.572  1.00 20.57 ? 220 CYS A CA    1 
ATOM   1770 C C     . CYS A 1 225 ? 14.994 12.885  -2.662  1.00 14.46 ? 220 CYS A C     1 
ATOM   1771 O O     . CYS A 1 225 ? 16.130 13.046  -2.206  1.00 14.49 ? 220 CYS A O     1 
ATOM   1772 C CB    . CYS A 1 225 ? 15.035 10.377  -2.886  1.00 17.60 ? 220 CYS A CB    1 
ATOM   1773 S SG    . CYS A 1 225 ? 13.997 9.981   -1.460  1.00 15.78 ? 220 CYS A SG    1 
ATOM   1774 N N     . GLY A 1 226 ? 13.990 13.707  -2.397  1.00 15.37 ? 221 GLY A N     1 
ATOM   1775 C CA    . GLY A 1 226 ? 14.210 14.861  -1.556  1.00 20.40 ? 221 GLY A CA    1 
ATOM   1776 C C     . GLY A 1 226 ? 12.936 15.607  -1.238  1.00 17.65 ? 221 GLY A C     1 
ATOM   1777 O O     . GLY A 1 226 ? 11.841 15.043  -1.255  1.00 22.42 ? 221 GLY A O     1 
ATOM   1778 N N     . SER A 1 227 ? 13.108 16.894  -0.940  1.00 20.68 ? 222 SER A N     1 
ATOM   1779 C CA    . SER A 1 227 ? 12.003 17.760  -0.573  1.00 25.44 ? 222 SER A CA    1 
ATOM   1780 C C     . SER A 1 227 ? 11.112 18.047  -1.781  1.00 22.45 ? 222 SER A C     1 
ATOM   1781 O O     . SER A 1 227 ? 11.538 17.904  -2.929  1.00 20.41 ? 222 SER A O     1 
ATOM   1782 C CB    . SER A 1 227 ? 12.535 19.066  0.009   1.00 20.04 ? 222 SER A CB    1 
ATOM   1783 O OG    . SER A 1 227 ? 13.395 19.721  -0.909  1.00 19.06 ? 222 SER A OG    1 
ATOM   1784 N N     . PRO A 1 228 ? 9.855  18.436  -1.542  1.00 26.13 ? 223 PRO A N     1 
ATOM   1785 C CA    . PRO A 1 228 ? 8.975  18.790  -2.670  1.00 20.88 ? 223 PRO A CA    1 
ATOM   1786 C C     . PRO A 1 228 ? 9.519  19.907  -3.548  1.00 18.84 ? 223 PRO A C     1 
ATOM   1787 O O     . PRO A 1 228 ? 9.420  19.822  -4.779  1.00 20.51 ? 223 PRO A O     1 
ATOM   1788 C CB    . PRO A 1 228 ? 7.678  19.198  -1.961  1.00 22.88 ? 223 PRO A CB    1 
ATOM   1789 C CG    . PRO A 1 228 ? 7.669  18.345  -0.736  1.00 17.93 ? 223 PRO A CG    1 
ATOM   1790 C CD    . PRO A 1 228 ? 9.105  18.342  -0.276  1.00 20.86 ? 223 PRO A CD    1 
ATOM   1791 N N     . GLU A 1 229 ? 10.091 20.957  -2.952  1.00 22.80 ? 224 GLU A N     1 
ATOM   1792 C CA    . GLU A 1 229 ? 10.658 22.044  -3.748  1.00 23.95 ? 224 GLU A CA    1 
ATOM   1793 C C     . GLU A 1 229 ? 11.793 21.552  -4.643  1.00 23.94 ? 224 GLU A C     1 
ATOM   1794 O O     . GLU A 1 229 ? 11.874 21.929  -5.818  1.00 21.96 ? 224 GLU A O     1 
ATOM   1795 C CB    . GLU A 1 229 ? 11.148 23.169  -2.834  1.00 25.25 ? 224 GLU A CB    1 
ATOM   1796 C CG    . GLU A 1 229 ? 10.079 24.190  -2.448  1.00 36.44 ? 224 GLU A CG    1 
ATOM   1797 C CD    . GLU A 1 229 ? 10.626 25.308  -1.571  1.00 42.32 ? 224 GLU A CD    1 
ATOM   1798 O OE1   . GLU A 1 229 ? 11.563 26.007  -2.013  1.00 40.46 ? 224 GLU A OE1   1 
ATOM   1799 O OE2   . GLU A 1 229 ? 10.121 25.491  -0.442  1.00 33.14 ? 224 GLU A OE2   1 
ATOM   1800 N N     . MET A 1 230 ? 12.675 20.705  -4.104  1.00 23.04 ? 225 MET A N     1 
ATOM   1801 C CA    . MET A 1 230 ? 13.814 20.203  -4.869  1.00 23.54 ? 225 MET A CA    1 
ATOM   1802 C C     . MET A 1 230 ? 13.383 19.229  -5.965  1.00 22.45 ? 225 MET A C     1 
ATOM   1803 O O     . MET A 1 230 ? 14.014 19.180  -7.029  1.00 22.90 ? 225 MET A O     1 
ATOM   1804 C CB    . MET A 1 230 ? 14.828 19.576  -3.895  1.00 19.79 ? 225 MET A CB    1 
ATOM   1805 C CG    . MET A 1 230 ? 16.011 18.776  -4.463  1.00 16.60 ? 225 MET A CG    1 
ATOM   1806 S SD    . MET A 1 230 ? 15.575 17.169  -5.154  1.00 28.71 ? 225 MET A SD    1 
ATOM   1807 C CE    . MET A 1 230 ? 17.180 16.438  -5.458  1.00 25.01 ? 225 MET A CE    1 
ATOM   1808 N N     . LEU A 1 231 ? 12.324 18.449  -5.738  1.00 22.67 ? 226 LEU A N     1 
ATOM   1809 C CA    . LEU A 1 231 ? 11.897 17.493  -6.756  1.00 25.83 ? 226 LEU A CA    1 
ATOM   1810 C C     . LEU A 1 231 ? 11.270 18.202  -7.951  1.00 22.06 ? 226 LEU A C     1 
ATOM   1811 O O     . LEU A 1 231 ? 11.656 17.956  -9.100  1.00 25.09 ? 226 LEU A O     1 
ATOM   1812 C CB    . LEU A 1 231 ? 10.922 16.476  -6.163  1.00 19.74 ? 226 LEU A CB    1 
ATOM   1813 C CG    . LEU A 1 231 ? 11.511 15.479  -5.162  1.00 18.52 ? 226 LEU A CG    1 
ATOM   1814 C CD1   . LEU A 1 231 ? 10.449 14.494  -4.701  1.00 17.05 ? 226 LEU A CD1   1 
ATOM   1815 C CD2   . LEU A 1 231 ? 12.718 14.748  -5.739  1.00 19.81 ? 226 LEU A CD2   1 
ATOM   1816 N N     . ALA A 1 232 ? 10.300 19.088  -7.697  1.00 24.95 ? 227 ALA A N     1 
ATOM   1817 C CA    . ALA A 1 232 ? 9.624  19.790  -8.786  1.00 23.08 ? 227 ALA A CA    1 
ATOM   1818 C C     . ALA A 1 232 ? 10.593 20.660  -9.576  1.00 19.78 ? 227 ALA A C     1 
ATOM   1819 O O     . ALA A 1 232 ? 10.469 20.796  -10.799 1.00 22.40 ? 227 ALA A O     1 
ATOM   1820 C CB    . ALA A 1 232 ? 8.483  20.638  -8.230  1.00 27.01 ? 227 ALA A CB    1 
ATOM   1821 N N     . GLU A 1 233 ? 11.560 21.263  -8.888  1.00 25.33 ? 228 GLU A N     1 
ATOM   1822 C CA    . GLU A 1 233 ? 12.551 22.096  -9.556  1.00 20.63 ? 228 GLU A CA    1 
ATOM   1823 C C     . GLU A 1 233 ? 13.470 21.262  -10.442 1.00 23.97 ? 228 GLU A C     1 
ATOM   1824 O O     . GLU A 1 233 ? 13.713 21.610  -11.604 1.00 21.59 ? 228 GLU A O     1 
ATOM   1825 C CB    . GLU A 1 233 ? 13.354 22.858  -8.508  1.00 24.06 ? 228 GLU A CB    1 
ATOM   1826 C CG    . GLU A 1 233 ? 14.177 23.982  -9.057  1.00 27.42 ? 228 GLU A CG    1 
ATOM   1827 C CD    . GLU A 1 233 ? 14.542 25.009  -8.012  1.00 29.60 ? 228 GLU A CD    1 
ATOM   1828 O OE1   . GLU A 1 233 ? 13.971 24.964  -6.902  1.00 29.63 ? 228 GLU A OE1   1 
ATOM   1829 O OE2   . GLU A 1 233 ? 15.416 25.853  -8.299  1.00 39.03 ? 228 GLU A OE2   1 
ATOM   1830 N N     . THR A 1 234 ? 13.992 20.153  -9.907  1.00 21.88 ? 229 THR A N     1 
ATOM   1831 C CA    . THR A 1 234 ? 14.921 19.321  -10.669 1.00 23.86 ? 229 THR A CA    1 
ATOM   1832 C C     . THR A 1 234 ? 14.192 18.532  -11.751 1.00 18.94 ? 229 THR A C     1 
ATOM   1833 O O     . THR A 1 234 ? 14.765 18.260  -12.813 1.00 21.29 ? 229 THR A O     1 
ATOM   1834 C CB    . THR A 1 234 ? 15.678 18.379  -9.722  1.00 24.92 ? 229 THR A CB    1 
ATOM   1835 O OG1   . THR A 1 234 ? 16.276 19.141  -8.666  1.00 22.96 ? 229 THR A OG1   1 
ATOM   1836 C CG2   . THR A 1 234 ? 16.791 17.635  -10.454 1.00 19.65 ? 229 THR A CG2   1 
ATOM   1837 N N     . LYS A 1 235 ? 12.930 18.171  -11.506 1.00 20.43 ? 230 LYS A N     1 
ATOM   1838 C CA    . LYS A 1 235 ? 12.138 17.492  -12.526 1.00 21.20 ? 230 LYS A CA    1 
ATOM   1839 C C     . LYS A 1 235 ? 11.937 18.385  -13.743 1.00 22.55 ? 230 LYS A C     1 
ATOM   1840 O O     . LYS A 1 235 ? 11.927 17.903  -14.882 1.00 19.58 ? 230 LYS A O     1 
ATOM   1841 C CB    . LYS A 1 235 ? 10.799 17.061  -11.929 1.00 21.68 ? 230 LYS A CB    1 
ATOM   1842 C CG    . LYS A 1 235 ? 9.922  16.191  -12.814 1.00 23.04 ? 230 LYS A CG    1 
ATOM   1843 C CD    . LYS A 1 235 ? 8.759  15.636  -11.999 1.00 22.89 ? 230 LYS A CD    1 
ATOM   1844 C CE    . LYS A 1 235 ? 7.811  14.794  -12.828 1.00 21.38 ? 230 LYS A CE    1 
ATOM   1845 N NZ    . LYS A 1 235 ? 6.971  15.642  -13.715 1.00 29.46 ? 230 LYS A NZ    1 
ATOM   1846 N N     . GLN A 1 236 ? 11.787 19.696  -13.521 1.00 28.30 ? 231 GLN A N     1 
ATOM   1847 C CA    . GLN A 1 236 ? 11.698 20.645  -14.628 1.00 24.55 ? 231 GLN A CA    1 
ATOM   1848 C C     . GLN A 1 236 ? 13.035 20.770  -15.348 1.00 24.16 ? 231 GLN A C     1 
ATOM   1849 O O     . GLN A 1 236 ? 13.080 20.853  -16.580 1.00 23.62 ? 231 GLN A O     1 
ATOM   1850 C CB    . GLN A 1 236 ? 11.245 22.011  -14.113 1.00 24.47 ? 231 GLN A CB    1 
ATOM   1851 C CG    . GLN A 1 236 ? 11.045 23.052  -15.206 1.00 22.25 ? 231 GLN A CG    1 
ATOM   1852 C CD    . GLN A 1 236 ? 10.306 24.283  -14.715 1.00 19.75 ? 231 GLN A CD    1 
ATOM   1853 O OE1   . GLN A 1 236 ? 9.130  24.217  -14.365 1.00 25.89 ? 231 GLN A OE1   1 
ATOM   1854 N NE2   . GLN A 1 236 ? 10.993 25.423  -14.707 1.00 18.67 ? 231 GLN A NE2   1 
ATOM   1855 N N     . ILE A 1 237 ? 14.132 20.801  -14.585 1.00 27.01 ? 232 ILE A N     1 
ATOM   1856 C CA    . ILE A 1 237 ? 15.473 20.825  -15.167 1.00 22.26 ? 232 ILE A CA    1 
ATOM   1857 C C     . ILE A 1 237 ? 15.659 19.652  -16.121 1.00 20.28 ? 232 ILE A C     1 
ATOM   1858 O O     . ILE A 1 237 ? 16.089 19.819  -17.269 1.00 17.68 ? 232 ILE A O     1 
ATOM   1859 C CB    . ILE A 1 237 ? 16.533 20.805  -14.049 1.00 24.61 ? 232 ILE A CB    1 
ATOM   1860 C CG1   . ILE A 1 237 ? 16.600 22.153  -13.326 1.00 24.59 ? 232 ILE A CG1   1 
ATOM   1861 C CG2   . ILE A 1 237 ? 17.896 20.406  -14.602 1.00 25.38 ? 232 ILE A CG2   1 
ATOM   1862 C CD1   . ILE A 1 237 ? 17.419 22.116  -12.050 1.00 21.80 ? 232 ILE A CD1   1 
ATOM   1863 N N     . LEU A 1 238 ? 15.320 18.448  -15.654 1.00 19.39 ? 233 LEU A N     1 
ATOM   1864 C CA    . LEU A 1 238 ? 15.623 17.233  -16.401 1.00 20.91 ? 233 LEU A CA    1 
ATOM   1865 C C     . LEU A 1 238 ? 14.698 17.067  -17.601 1.00 20.77 ? 233 LEU A C     1 
ATOM   1866 O O     . LEU A 1 238 ? 15.140 16.648  -18.677 1.00 20.11 ? 233 LEU A O     1 
ATOM   1867 C CB    . LEU A 1 238 ? 15.520 16.018  -15.475 1.00 26.87 ? 233 LEU A CB    1 
ATOM   1868 C CG    . LEU A 1 238 ? 16.550 15.879  -14.344 1.00 22.30 ? 233 LEU A CG    1 
ATOM   1869 C CD1   . LEU A 1 238 ? 16.401 14.540  -13.639 1.00 14.55 ? 233 LEU A CD1   1 
ATOM   1870 C CD2   . LEU A 1 238 ? 17.967 16.064  -14.856 1.00 26.57 ? 233 LEU A CD2   1 
ATOM   1871 N N     . GLU A 1 239 ? 13.411 17.392  -17.436 1.00 21.53 ? 234 GLU A N     1 
ATOM   1872 C CA    . GLU A 1 239 ? 12.444 17.169  -18.509 1.00 23.09 ? 234 GLU A CA    1 
ATOM   1873 C C     . GLU A 1 239 ? 12.564 18.208  -19.621 1.00 22.86 ? 234 GLU A C     1 
ATOM   1874 O O     . GLU A 1 239 ? 12.279 17.897  -20.783 1.00 21.66 ? 234 GLU A O     1 
ATOM   1875 C CB    . GLU A 1 239 ? 11.026 17.152  -17.940 1.00 20.58 ? 234 GLU A CB    1 
ATOM   1876 C CG    . GLU A 1 239 ? 10.711 15.913  -17.122 1.00 26.56 ? 234 GLU A CG    1 
ATOM   1877 C CD    . GLU A 1 239 ? 9.245  15.791  -16.790 1.00 25.70 ? 234 GLU A CD    1 
ATOM   1878 O OE1   . GLU A 1 239 ? 8.601  16.843  -16.601 1.00 24.82 ? 234 GLU A OE1   1 
ATOM   1879 O OE2   . GLU A 1 239 ? 8.741  14.644  -16.731 1.00 26.42 ? 234 GLU A OE2   1 
ATOM   1880 N N     . GLU A 1 240 ? 12.970 19.439  -19.293 1.00 21.10 ? 235 GLU A N     1 
ATOM   1881 C CA    . GLU A 1 240 ? 13.200 20.446  -20.324 1.00 19.07 ? 235 GLU A CA    1 
ATOM   1882 C C     . GLU A 1 240 ? 14.446 20.150  -21.148 1.00 17.08 ? 235 GLU A C     1 
ATOM   1883 O O     . GLU A 1 240 ? 14.590 20.692  -22.247 1.00 15.81 ? 235 GLU A O     1 
ATOM   1884 C CB    . GLU A 1 240 ? 13.316 21.835  -19.692 1.00 21.08 ? 235 GLU A CB    1 
ATOM   1885 C CG    . GLU A 1 240 ? 12.014 22.394  -19.143 1.00 21.76 ? 235 GLU A CG    1 
ATOM   1886 C CD    . GLU A 1 240 ? 12.094 23.888  -18.885 1.00 23.55 ? 235 GLU A CD    1 
ATOM   1887 O OE1   . GLU A 1 240 ? 13.105 24.499  -19.283 1.00 29.15 ? 235 GLU A OE1   1 
ATOM   1888 O OE2   . GLU A 1 240 ? 11.158 24.450  -18.275 1.00 23.26 ? 235 GLU A OE2   1 
ATOM   1889 N N     . ARG A 1 241 ? 15.344 19.307  -20.640 1.00 21.24 ? 236 ARG A N     1 
ATOM   1890 C CA    . ARG A 1 241 ? 16.530 18.878  -21.367 1.00 18.66 ? 236 ARG A CA    1 
ATOM   1891 C C     . ARG A 1 241 ? 16.260 17.698  -22.289 1.00 19.83 ? 236 ARG A C     1 
ATOM   1892 O O     . ARG A 1 241 ? 17.095 17.406  -23.153 1.00 24.91 ? 236 ARG A O     1 
ATOM   1893 C CB    . ARG A 1 241 ? 17.642 18.500  -20.383 1.00 20.37 ? 236 ARG A CB    1 
ATOM   1894 C CG    . ARG A 1 241 ? 18.334 19.687  -19.736 1.00 23.35 ? 236 ARG A CG    1 
ATOM   1895 C CD    . ARG A 1 241 ? 19.303 19.241  -18.647 1.00 22.89 ? 236 ARG A CD    1 
ATOM   1896 N NE    . ARG A 1 241 ? 19.933 20.380  -17.990 1.00 30.97 ? 236 ARG A NE    1 
ATOM   1897 C CZ    . ARG A 1 241 ? 21.240 20.539  -17.826 1.00 31.53 ? 236 ARG A CZ    1 
ATOM   1898 N NH1   . ARG A 1 241 ? 22.111 19.656  -18.292 1.00 31.29 ? 236 ARG A NH1   1 
ATOM   1899 N NH2   . ARG A 1 241 ? 21.685 21.610  -17.172 1.00 22.89 ? 236 ARG A NH2   1 
ATOM   1900 N N     . GLY A 1 242 ? 15.128 17.018  -22.123 1.00 22.52 ? 237 GLY A N     1 
ATOM   1901 C CA    . GLY A 1 242 ? 14.772 15.880  -22.941 1.00 24.25 ? 237 GLY A CA    1 
ATOM   1902 C C     . GLY A 1 242 ? 14.740 14.539  -22.229 1.00 23.35 ? 237 GLY A C     1 
ATOM   1903 O O     . GLY A 1 242 ? 14.574 13.511  -22.895 1.00 24.31 ? 237 GLY A O     1 
ATOM   1904 N N     . PHE A 1 243 ? 14.887 14.510  -20.907 1.00 23.94 ? 238 PHE A N     1 
ATOM   1905 C CA    . PHE A 1 243 ? 14.925 13.256  -20.170 1.00 25.30 ? 238 PHE A CA    1 
ATOM   1906 C C     . PHE A 1 243 ? 13.525 12.906  -19.688 1.00 22.71 ? 238 PHE A C     1 
ATOM   1907 O O     . PHE A 1 243 ? 12.777 13.778  -19.235 1.00 23.62 ? 238 PHE A O     1 
ATOM   1908 C CB    . PHE A 1 243 ? 15.883 13.350  -18.980 1.00 27.47 ? 238 PHE A CB    1 
ATOM   1909 C CG    . PHE A 1 243 ? 17.315 13.601  -19.367 1.00 27.09 ? 238 PHE A CG    1 
ATOM   1910 C CD1   . PHE A 1 243 ? 17.735 14.870  -19.728 1.00 22.06 ? 238 PHE A CD1   1 
ATOM   1911 C CD2   . PHE A 1 243 ? 18.235 12.566  -19.393 1.00 30.97 ? 238 PHE A CD2   1 
ATOM   1912 C CE1   . PHE A 1 243 ? 19.049 15.105  -20.088 1.00 26.89 ? 238 PHE A CE1   1 
ATOM   1913 C CE2   . PHE A 1 243 ? 19.552 12.795  -19.756 1.00 25.29 ? 238 PHE A CE2   1 
ATOM   1914 C CZ    . PHE A 1 243 ? 19.959 14.062  -20.102 1.00 25.22 ? 238 PHE A CZ    1 
ATOM   1915 N N     . THR A 1 244 ? 13.173 11.627  -19.790 1.00 24.64 ? 239 THR A N     1 
ATOM   1916 C CA    . THR A 1 244 ? 11.833 11.158  -19.469 1.00 22.83 ? 239 THR A CA    1 
ATOM   1917 C C     . THR A 1 244 ? 11.851 10.348  -18.179 1.00 17.77 ? 239 THR A C     1 
ATOM   1918 O O     . THR A 1 244 ? 12.868 9.749   -17.816 1.00 19.12 ? 239 THR A O     1 
ATOM   1919 C CB    . THR A 1 244 ? 11.252 10.321  -20.618 1.00 20.66 ? 239 THR A CB    1 
ATOM   1920 O OG1   . THR A 1 244 ? 11.811 9.002   -20.601 1.00 24.57 ? 239 THR A OG1   1 
ATOM   1921 C CG2   . THR A 1 244 ? 11.570 10.972  -21.953 1.00 16.92 ? 239 THR A CG2   1 
ATOM   1922 N N     . GLU A 1 245 ? 10.712 10.339  -17.487 1.00 24.70 ? 240 GLU A N     1 
ATOM   1923 C CA    . GLU A 1 245 ? 10.584 9.648   -16.209 1.00 21.37 ? 240 GLU A CA    1 
ATOM   1924 C C     . GLU A 1 245 ? 10.180 8.193   -16.425 1.00 19.67 ? 240 GLU A C     1 
ATOM   1925 O O     . GLU A 1 245 ? 9.145  7.912   -17.039 1.00 18.45 ? 240 GLU A O     1 
ATOM   1926 C CB    . GLU A 1 245 ? 9.567  10.338  -15.306 1.00 18.94 ? 240 GLU A CB    1 
ATOM   1927 C CG    . GLU A 1 245 ? 9.387  9.599   -13.995 1.00 22.44 ? 240 GLU A CG    1 
ATOM   1928 C CD    . GLU A 1 245 ? 8.565  10.360  -12.983 1.00 22.51 ? 240 GLU A CD    1 
ATOM   1929 O OE1   . GLU A 1 245 ? 8.129  11.489  -13.288 1.00 29.67 ? 240 GLU A OE1   1 
ATOM   1930 O OE2   . GLU A 1 245 ? 8.372  9.822   -11.873 1.00 32.60 ? 240 GLU A OE2   1 
ATOM   1931 N N     . GLY A 1 246 ? 10.983 7.275   -15.886 1.00 19.02 ? 241 GLY A N     1 
ATOM   1932 C CA    . GLY A 1 246 ? 10.711 5.865   -16.031 1.00 18.48 ? 241 GLY A CA    1 
ATOM   1933 C C     . GLY A 1 246 ? 9.685  5.354   -15.042 1.00 23.52 ? 241 GLY A C     1 
ATOM   1934 O O     . GLY A 1 246 ? 9.220  6.057   -14.146 1.00 27.82 ? 241 GLY A O     1 
ATOM   1935 N N     . SER A 1 247 ? 9.328  4.090   -15.229 1.00 23.61 ? 242 SER A N     1 
ATOM   1936 C CA    . SER A 1 247 ? 8.384  3.399   -14.363 1.00 24.99 ? 242 SER A CA    1 
ATOM   1937 C C     . SER A 1 247 ? 8.538  1.905   -14.619 1.00 29.91 ? 242 SER A C     1 
ATOM   1938 O O     . SER A 1 247 ? 9.313  1.480   -15.482 1.00 27.02 ? 242 SER A O     1 
ATOM   1939 C CB    . SER A 1 247 ? 6.946  3.880   -14.602 1.00 29.42 ? 242 SER A CB    1 
ATOM   1940 O OG    . SER A 1 247 ? 6.461  3.490   -15.878 1.00 26.16 ? 242 SER A OG    1 
ATOM   1941 N N     . GLN A 1 248 ? 7.788  1.107   -13.857 1.00 30.89 ? 243 GLN A N     1 
ATOM   1942 C CA    . GLN A 1 248 ? 7.895  -0.344  -13.971 1.00 35.62 ? 243 GLN A CA    1 
ATOM   1943 C C     . GLN A 1 248 ? 7.547  -0.816  -15.379 1.00 39.75 ? 243 GLN A C     1 
ATOM   1944 O O     . GLN A 1 248 ? 8.212  -1.703  -15.928 1.00 39.77 ? 243 GLN A O     1 
ATOM   1945 C CB    . GLN A 1 248 ? 6.990  -1.010  -12.935 1.00 37.31 ? 243 GLN A CB    1 
ATOM   1946 C CG    . GLN A 1 248 ? 7.322  -2.459  -12.632 1.00 42.97 ? 243 GLN A CG    1 
ATOM   1947 C CD    . GLN A 1 248 ? 6.623  -2.957  -11.382 1.00 47.33 ? 243 GLN A CD    1 
ATOM   1948 O OE1   . GLN A 1 248 ? 6.509  -2.234  -10.393 1.00 47.92 ? 243 GLN A OE1   1 
ATOM   1949 N NE2   . GLN A 1 248 ? 6.149  -4.196  -11.422 1.00 51.88 ? 243 GLN A NE2   1 
ATOM   1950 N N     . SER A 1 249 ? 6.524  -0.218  -15.988 1.00 34.27 ? 244 SER A N     1 
ATOM   1951 C CA    . SER A 1 249 ? 6.055  -0.626  -17.303 1.00 30.04 ? 244 SER A CA    1 
ATOM   1952 C C     . SER A 1 249 ? 6.809  0.034   -18.453 1.00 40.71 ? 244 SER A C     1 
ATOM   1953 O O     . SER A 1 249 ? 6.654  -0.402  -19.598 1.00 37.74 ? 244 SER A O     1 
ATOM   1954 C CB    . SER A 1 249 ? 4.558  -0.327  -17.436 1.00 29.40 ? 244 SER A CB    1 
ATOM   1955 O OG    . SER A 1 249 ? 4.240  0.942   -16.898 1.00 33.89 ? 244 SER A OG    1 
ATOM   1956 N N     . GLU A 1 250 ? 7.620  1.064   -18.188 1.00 41.65 ? 245 GLU A N     1 
ATOM   1957 C CA    . GLU A 1 250 ? 8.328  1.758   -19.262 1.00 42.03 ? 245 GLU A CA    1 
ATOM   1958 C C     . GLU A 1 250 ? 9.573  2.461   -18.727 1.00 37.02 ? 245 GLU A C     1 
ATOM   1959 O O     . GLU A 1 250 ? 9.498  3.613   -18.280 1.00 28.77 ? 245 GLU A O     1 
ATOM   1960 C CB    . GLU A 1 250 ? 7.406  2.763   -19.952 1.00 43.37 ? 245 GLU A CB    1 
ATOM   1961 C CG    . GLU A 1 250 ? 8.024  3.464   -21.151 1.00 40.86 ? 245 GLU A CG    1 
ATOM   1962 C CD    . GLU A 1 250 ? 7.037  4.367   -21.860 1.00 53.74 ? 245 GLU A CD    1 
ATOM   1963 O OE1   . GLU A 1 250 ? 6.634  5.388   -21.266 1.00 51.88 ? 245 GLU A OE1   1 
ATOM   1964 O OE2   . GLU A 1 250 ? 6.656  4.050   -23.006 1.00 59.74 ? 245 GLU A OE2   1 
ATOM   1965 N N     . PRO A 1 251 ? 10.733 1.805   -18.765 1.00 39.30 ? 246 PRO A N     1 
ATOM   1966 C CA    . PRO A 1 251 ? 11.948 2.417   -18.213 1.00 27.49 ? 246 PRO A CA    1 
ATOM   1967 C C     . PRO A 1 251 ? 12.313 3.717   -18.918 1.00 26.08 ? 246 PRO A C     1 
ATOM   1968 O O     . PRO A 1 251 ? 11.984 3.938   -20.086 1.00 30.50 ? 246 PRO A O     1 
ATOM   1969 C CB    . PRO A 1 251 ? 13.023 1.346   -18.434 1.00 30.37 ? 246 PRO A CB    1 
ATOM   1970 C CG    . PRO A 1 251 ? 12.289 0.071   -18.597 1.00 37.72 ? 246 PRO A CG    1 
ATOM   1971 C CD    . PRO A 1 251 ? 10.914 0.382   -19.099 1.00 35.37 ? 246 PRO A CD    1 
ATOM   1972 N N     . GLY A 1 252 ? 13.005 4.580   -18.186 1.00 27.49 ? 247 GLY A N     1 
ATOM   1973 C CA    . GLY A 1 252 ? 13.393 5.890   -18.681 1.00 24.51 ? 247 GLY A CA    1 
ATOM   1974 C C     . GLY A 1 252 ? 14.738 6.295   -18.126 1.00 20.43 ? 247 GLY A C     1 
ATOM   1975 O O     . GLY A 1 252 ? 15.570 5.444   -17.803 1.00 25.50 ? 247 GLY A O     1 
ATOM   1976 N N     . GLU A 1 253 ? 14.947 7.610   -18.009 1.00 23.89 ? 248 GLU A N     1 
ATOM   1977 C CA    . GLU A 1 253 ? 16.241 8.127   -17.578 1.00 33.12 ? 248 GLU A CA    1 
ATOM   1978 C C     . GLU A 1 253 ? 16.278 8.523   -16.111 1.00 24.22 ? 248 GLU A C     1 
ATOM   1979 O O     . GLU A 1 253 ? 17.345 8.450   -15.492 1.00 21.78 ? 248 GLU A O     1 
ATOM   1980 C CB    . GLU A 1 253 ? 16.645 9.333   -18.432 1.00 27.13 ? 248 GLU A CB    1 
ATOM   1981 C CG    . GLU A 1 253 ? 17.232 8.950   -19.778 1.00 24.40 ? 248 GLU A CG    1 
ATOM   1982 C CD    . GLU A 1 253 ? 16.195 8.923   -20.879 1.00 21.39 ? 248 GLU A CD    1 
ATOM   1983 O OE1   . GLU A 1 253 ? 15.321 9.804   -20.908 1.00 18.85 ? 248 GLU A OE1   1 
ATOM   1984 O OE2   . GLU A 1 253 ? 16.243 7.993   -21.711 1.00 27.09 ? 248 GLU A OE2   1 
ATOM   1985 N N     . PHE A 1 254 ? 15.153 8.938   -15.533 1.00 23.65 ? 249 PHE A N     1 
ATOM   1986 C CA    . PHE A 1 254 ? 15.122 9.302   -14.125 1.00 23.57 ? 249 PHE A CA    1 
ATOM   1987 C C     . PHE A 1 254 ? 13.833 8.815   -13.474 1.00 23.05 ? 249 PHE A C     1 
ATOM   1988 O O     . PHE A 1 254 ? 12.772 8.771   -14.103 1.00 20.82 ? 249 PHE A O     1 
ATOM   1989 C CB    . PHE A 1 254 ? 15.310 10.825  -13.929 1.00 24.72 ? 249 PHE A CB    1 
ATOM   1990 C CG    . PHE A 1 254 ? 14.164 11.670  -14.426 1.00 23.62 ? 249 PHE A CG    1 
ATOM   1991 C CD1   . PHE A 1 254 ? 13.093 11.977  -13.599 1.00 20.06 ? 249 PHE A CD1   1 
ATOM   1992 C CD2   . PHE A 1 254 ? 14.184 12.193  -15.713 1.00 22.61 ? 249 PHE A CD2   1 
ATOM   1993 C CE1   . PHE A 1 254 ? 12.053 12.759  -14.058 1.00 24.31 ? 249 PHE A CE1   1 
ATOM   1994 C CE2   . PHE A 1 254 ? 13.148 12.978  -16.177 1.00 18.21 ? 249 PHE A CE2   1 
ATOM   1995 C CZ    . PHE A 1 254 ? 12.081 13.260  -15.349 1.00 21.95 ? 249 PHE A CZ    1 
ATOM   1996 N N     . VAL A 1 255 ? 13.954 8.420   -12.204 1.00 24.26 ? 250 VAL A N     1 
ATOM   1997 C CA    . VAL A 1 255 ? 12.814 8.158   -11.337 1.00 23.25 ? 250 VAL A CA    1 
ATOM   1998 C C     . VAL A 1 255 ? 12.923 9.065   -10.117 1.00 21.89 ? 250 VAL A C     1 
ATOM   1999 O O     . VAL A 1 255 ? 13.997 9.564   -9.768  1.00 18.94 ? 250 VAL A O     1 
ATOM   2000 C CB    . VAL A 1 255 ? 12.700 6.673   -10.910 1.00 22.21 ? 250 VAL A CB    1 
ATOM   2001 C CG1   . VAL A 1 255 ? 12.133 5.820   -12.042 1.00 15.97 ? 250 VAL A CG1   1 
ATOM   2002 C CG2   . VAL A 1 255 ? 14.050 6.127   -10.447 1.00 21.11 ? 250 VAL A CG2   1 
ATOM   2003 N N     . ILE A 1 256 ? 11.781 9.281   -9.474  1.00 21.89 ? 251 ILE A N     1 
ATOM   2004 C CA    . ILE A 1 256 ? 11.641 10.238  -8.386  1.00 23.41 ? 251 ILE A CA    1 
ATOM   2005 C C     . ILE A 1 256 ? 10.904 9.564   -7.240  1.00 22.90 ? 251 ILE A C     1 
ATOM   2006 O O     . ILE A 1 256 ? 10.042 8.706   -7.451  1.00 22.78 ? 251 ILE A O     1 
ATOM   2007 C CB    . ILE A 1 256 ? 10.898 11.519  -8.848  1.00 23.26 ? 251 ILE A CB    1 
ATOM   2008 C CG1   . ILE A 1 256 ? 11.748 12.309  -9.843  1.00 21.38 ? 251 ILE A CG1   1 
ATOM   2009 C CG2   . ILE A 1 256 ? 10.457 12.383  -7.678  1.00 14.94 ? 251 ILE A CG2   1 
ATOM   2010 C CD1   . ILE A 1 256 ? 11.048 13.498  -10.423 1.00 22.61 ? 251 ILE A CD1   1 
ATOM   2011 N N     . GLU A 1 257 ? 11.258 9.946   -6.018  1.00 22.20 ? 252 GLU A N     1 
ATOM   2012 C CA    . GLU A 1 257 ? 10.522 9.504   -4.851  1.00 17.57 ? 252 GLU A CA    1 
ATOM   2013 C C     . GLU A 1 257 ? 10.488 10.637  -3.836  1.00 21.65 ? 252 GLU A C     1 
ATOM   2014 O O     . GLU A 1 257 ? 11.481 11.348  -3.648  1.00 18.94 ? 252 GLU A O     1 
ATOM   2015 C CB    . GLU A 1 257 ? 11.154 8.252   -4.249  1.00 16.56 ? 252 GLU A CB    1 
ATOM   2016 C CG    . GLU A 1 257 ? 10.444 7.739   -3.028  1.00 18.23 ? 252 GLU A CG    1 
ATOM   2017 C CD    . GLU A 1 257 ? 10.886 6.348   -2.675  1.00 19.56 ? 252 GLU A CD    1 
ATOM   2018 O OE1   . GLU A 1 257 ? 10.328 5.391   -3.257  1.00 29.03 ? 252 GLU A OE1   1 
ATOM   2019 O OE2   . GLU A 1 257 ? 11.784 6.213   -1.821  1.00 20.24 ? 252 GLU A OE2   1 
ATOM   2020 N N     . LYS A 1 258 ? 9.335  10.807  -3.195  1.00 20.48 ? 253 LYS A N     1 
ATOM   2021 C CA    . LYS A 1 258 ? 9.185  11.847  -2.189  1.00 21.32 ? 253 LYS A CA    1 
ATOM   2022 C C     . LYS A 1 258 ? 9.895  11.450  -0.899  1.00 19.89 ? 253 LYS A C     1 
ATOM   2023 O O     . LYS A 1 258 ? 9.642  10.379  -0.337  1.00 13.55 ? 253 LYS A O     1 
ATOM   2024 C CB    . LYS A 1 258 ? 7.704  12.116  -1.925  1.00 24.98 ? 253 LYS A CB    1 
ATOM   2025 C CG    . LYS A 1 258 ? 6.983  12.775  -3.095  1.00 22.73 ? 253 LYS A CG    1 
ATOM   2026 C CD    . LYS A 1 258 ? 5.476  12.789  -2.902  1.00 30.63 ? 253 LYS A CD    1 
ATOM   2027 C CE    . LYS A 1 258 ? 4.841  14.000  -3.572  1.00 26.65 ? 253 LYS A CE    1 
ATOM   2028 N NZ    . LYS A 1 258 ? 5.080  14.038  -5.043  1.00 23.49 ? 253 LYS A NZ    1 
ATOM   2029 N N     . ALA A 1 259 ? 10.802 12.314  -0.437  1.00 21.01 ? 254 ALA A N     1 
ATOM   2030 C CA    . ALA A 1 259 ? 11.396 12.113  0.877   1.00 16.80 ? 254 ALA A CA    1 
ATOM   2031 C C     . ALA A 1 259 ? 10.391 12.412  1.980   1.00 17.26 ? 254 ALA A C     1 
ATOM   2032 O O     . ALA A 1 259 ? 10.480 11.839  3.073   1.00 20.70 ? 254 ALA A O     1 
ATOM   2033 C CB    . ALA A 1 259 ? 12.644 12.979  1.031   1.00 14.82 ? 254 ALA A CB    1 
ATOM   2034 N N     . PHE A 1 260 ? 9.443  13.306  1.714   1.00 21.68 ? 255 PHE A N     1 
ATOM   2035 C CA    . PHE A 1 260 ? 8.293  13.512  2.584   1.00 24.32 ? 255 PHE A CA    1 
ATOM   2036 C C     . PHE A 1 260 ? 7.242  14.282  1.798   1.00 24.16 ? 255 PHE A C     1 
ATOM   2037 O O     . PHE A 1 260 ? 7.497  14.776  0.696   1.00 21.49 ? 255 PHE A O     1 
ATOM   2038 C CB    . PHE A 1 260 ? 8.667  14.249  3.883   1.00 22.39 ? 255 PHE A CB    1 
ATOM   2039 C CG    . PHE A 1 260 ? 9.308  15.597  3.668   1.00 22.13 ? 255 PHE A CG    1 
ATOM   2040 C CD1   . PHE A 1 260 ? 10.662 15.706  3.393   1.00 19.58 ? 255 PHE A CD1   1 
ATOM   2041 C CD2   . PHE A 1 260 ? 8.551  16.755  3.754   1.00 18.86 ? 255 PHE A CD2   1 
ATOM   2042 C CE1   . PHE A 1 260 ? 11.249 16.943  3.198   1.00 21.60 ? 255 PHE A CE1   1 
ATOM   2043 C CE2   . PHE A 1 260 ? 9.132  17.993  3.560   1.00 21.76 ? 255 PHE A CE2   1 
ATOM   2044 C CZ    . PHE A 1 260 ? 10.483 18.088  3.282   1.00 18.86 ? 255 PHE A CZ    1 
ATOM   2045 N N     . VAL A 1 261 ? 6.046  14.360  2.376   1.00 25.74 ? 256 VAL A N     1 
ATOM   2046 C CA    . VAL A 1 261 ? 4.958  15.180  1.859   1.00 36.11 ? 256 VAL A CA    1 
ATOM   2047 C C     . VAL A 1 261 ? 4.565  16.166  2.949   1.00 41.50 ? 256 VAL A C     1 
ATOM   2048 O O     . VAL A 1 261 ? 4.453  15.792  4.122   1.00 36.35 ? 256 VAL A O     1 
ATOM   2049 C CB    . VAL A 1 261 ? 3.742  14.330  1.432   1.00 30.56 ? 256 VAL A CB    1 
ATOM   2050 C CG1   . VAL A 1 261 ? 2.636  15.216  0.871   1.00 24.81 ? 256 VAL A CG1   1 
ATOM   2051 C CG2   . VAL A 1 261 ? 4.156  13.267  0.427   1.00 27.05 ? 256 VAL A CG2   1 
ATOM   2052 N N     . GLU A 1 262 ? 4.368  17.427  2.567   1.00 37.46 ? 257 GLU A N     1 
ATOM   2053 C CA    . GLU A 1 262 ? 3.957  18.439  3.533   1.00 43.19 ? 257 GLU A CA    1 
ATOM   2054 C C     . GLU A 1 262 ? 2.533  18.171  4.005   1.00 42.64 ? 257 GLU A C     1 
ATOM   2055 O O     . GLU A 1 262 ? 1.613  18.035  3.193   1.00 51.12 ? 257 GLU A O     1 
ATOM   2056 C CB    . GLU A 1 262 ? 4.053  19.838  2.924   1.00 51.94 ? 257 GLU A CB    1 
ATOM   2057 C CG    . GLU A 1 262 ? 5.425  20.487  3.038   1.00 55.62 ? 257 GLU A CG    1 
ATOM   2058 C CD    . GLU A 1 262 ? 5.650  21.151  4.383   1.00 48.25 ? 257 GLU A CD    1 
ATOM   2059 O OE1   . GLU A 1 262 ? 4.890  22.083  4.718   1.00 45.89 ? 257 GLU A OE1   1 
ATOM   2060 O OE2   . GLU A 1 262 ? 6.593  20.753  5.098   1.00 48.96 ? 257 GLU A OE2   1 
ATOM   2061 N N     . LYS A 1 263 ? 2.355  18.088  5.319   1.00 46.56 ? 258 LYS A N     1 
ATOM   2062 C CA    . LYS A 1 263 ? 1.030  17.915  5.904   1.00 53.30 ? 258 LYS A CA    1 
ATOM   2063 C C     . LYS A 1 263 ? 0.581  19.197  6.598   1.00 55.77 ? 258 LYS A C     1 
ATOM   2064 O O     . LYS A 1 263 ? 1.386  20.090  6.871   1.00 46.04 ? 258 LYS A O     1 
ATOM   2065 C CB    . LYS A 1 263 ? 1.016  16.746  6.893   1.00 50.10 ? 258 LYS A CB    1 
ATOM   2066 C CG    . LYS A 1 263 ? 1.273  15.386  6.267   1.00 45.33 ? 258 LYS A CG    1 
ATOM   2067 C CD    . LYS A 1 263 ? 0.991  14.269  7.260   1.00 43.28 ? 258 LYS A CD    1 
ATOM   2068 C CE    . LYS A 1 263 ? 1.268  12.902  6.656   1.00 44.76 ? 258 LYS A CE    1 
ATOM   2069 N NZ    . LYS A 1 263 ? 2.637  12.818  6.076   1.00 45.34 ? 258 LYS A NZ    1 
HETATM 2070 P PA    . FAD B 2 .   ? 4.125  13.857  10.290  1.00 32.50 ? 301 FAD A PA    1 
HETATM 2071 O O1A   . FAD B 2 .   ? 2.852  14.189  10.974  1.00 35.76 ? 301 FAD A O1A   1 
HETATM 2072 O O2A   . FAD B 2 .   ? 4.023  12.752  9.230   1.00 25.74 ? 301 FAD A O2A   1 
HETATM 2073 O O5B   . FAD B 2 .   ? 4.769  15.147  9.646   1.00 34.58 ? 301 FAD A O5B   1 
HETATM 2074 C C5B   . FAD B 2 .   ? 5.181  16.264  10.463  1.00 32.75 ? 301 FAD A C5B   1 
HETATM 2075 C C4B   . FAD B 2 .   ? 5.942  17.269  9.632   1.00 29.90 ? 301 FAD A C4B   1 
HETATM 2076 O O4B   . FAD B 2 .   ? 7.281  16.785  9.383   1.00 32.12 ? 301 FAD A O4B   1 
HETATM 2077 C C3B   . FAD B 2 .   ? 5.329  17.610  8.273   1.00 32.32 ? 301 FAD A C3B   1 
HETATM 2078 O O3B   . FAD B 2 .   ? 5.247  19.018  8.084   1.00 45.09 ? 301 FAD A O3B   1 
HETATM 2079 C C2B   . FAD B 2 .   ? 6.278  16.946  7.268   1.00 31.55 ? 301 FAD A C2B   1 
HETATM 2080 O O2B   . FAD B 2 .   ? 6.391  17.714  6.076   1.00 35.84 ? 301 FAD A O2B   1 
HETATM 2081 C C1B   . FAD B 2 .   ? 7.606  16.960  8.023   1.00 33.85 ? 301 FAD A C1B   1 
HETATM 2082 N N9A   . FAD B 2 .   ? 8.518  15.888  7.627   1.00 26.65 ? 301 FAD A N9A   1 
HETATM 2083 C C8A   . FAD B 2 .   ? 8.221  14.556  7.530   1.00 24.90 ? 301 FAD A C8A   1 
HETATM 2084 N N7A   . FAD B 2 .   ? 9.228  13.808  7.147   1.00 27.28 ? 301 FAD A N7A   1 
HETATM 2085 C C5A   . FAD B 2 .   ? 10.262 14.714  6.979   1.00 23.30 ? 301 FAD A C5A   1 
HETATM 2086 C C6A   . FAD B 2 .   ? 11.605 14.557  6.580   1.00 22.58 ? 301 FAD A C6A   1 
HETATM 2087 N N6A   . FAD B 2 .   ? 12.154 13.379  6.268   1.00 20.53 ? 301 FAD A N6A   1 
HETATM 2088 N N1A   . FAD B 2 .   ? 12.374 15.668  6.515   1.00 20.86 ? 301 FAD A N1A   1 
HETATM 2089 C C2A   . FAD B 2 .   ? 11.829 16.847  6.827   1.00 17.84 ? 301 FAD A C2A   1 
HETATM 2090 N N3A   . FAD B 2 .   ? 10.579 17.116  7.215   1.00 20.82 ? 301 FAD A N3A   1 
HETATM 2091 C C4A   . FAD B 2 .   ? 9.842  16.002  7.270   1.00 20.94 ? 301 FAD A C4A   1 
HETATM 2092 N N1    . FAD B 2 .   ? 11.001 9.951   6.761   1.00 24.98 ? 301 FAD A N1    1 
HETATM 2093 C C2    . FAD B 2 .   ? 12.166 9.611   7.385   1.00 19.76 ? 301 FAD A C2    1 
HETATM 2094 O O2    . FAD B 2 .   ? 12.513 10.145  8.442   1.00 18.48 ? 301 FAD A O2    1 
HETATM 2095 N N3    . FAD B 2 .   ? 12.987 8.647   6.826   1.00 21.25 ? 301 FAD A N3    1 
HETATM 2096 C C4    . FAD B 2 .   ? 12.751 7.957   5.656   1.00 15.10 ? 301 FAD A C4    1 
HETATM 2097 O O4    . FAD B 2 .   ? 13.561 7.122   5.263   1.00 16.87 ? 301 FAD A O4    1 
HETATM 2098 C C4X   . FAD B 2 .   ? 11.510 8.324   4.999   1.00 16.72 ? 301 FAD A C4X   1 
HETATM 2099 N N5    . FAD B 2 .   ? 11.202 7.722   3.880   1.00 19.34 ? 301 FAD A N5    1 
HETATM 2100 C C5X   . FAD B 2 .   ? 10.015 8.077   3.255   1.00 18.12 ? 301 FAD A C5X   1 
HETATM 2101 C C6    . FAD B 2 .   ? 9.665  7.447   2.059   1.00 18.65 ? 301 FAD A C6    1 
HETATM 2102 C C7    . FAD B 2 .   ? 8.483  7.771   1.399   1.00 25.21 ? 301 FAD A C7    1 
HETATM 2103 C C7M   . FAD B 2 .   ? 8.137  7.071   0.110   1.00 13.76 ? 301 FAD A C7M   1 
HETATM 2104 C C8    . FAD B 2 .   ? 7.628  8.748   1.942   1.00 23.37 ? 301 FAD A C8    1 
HETATM 2105 C C8M   . FAD B 2 .   ? 6.342  9.125   1.258   1.00 23.17 ? 301 FAD A C8M   1 
HETATM 2106 C C9    . FAD B 2 .   ? 7.976  9.376   3.134   1.00 19.83 ? 301 FAD A C9    1 
HETATM 2107 C C9A   . FAD B 2 .   ? 9.156  9.050   3.787   1.00 18.88 ? 301 FAD A C9A   1 
HETATM 2108 N N10   . FAD B 2 .   ? 9.534  9.676   4.991   1.00 20.79 ? 301 FAD A N10   1 
HETATM 2109 C C10   . FAD B 2 .   ? 10.699 9.333   5.628   1.00 22.45 ? 301 FAD A C10   1 
HETATM 2110 C "C1'" . FAD B 2 .   ? 8.668  10.682  5.612   1.00 22.05 ? 301 FAD A "C1'" 1 
HETATM 2111 C "C2'" . FAD B 2 .   ? 7.766  10.090  6.690   1.00 24.74 ? 301 FAD A "C2'" 1 
HETATM 2112 O "O2'" . FAD B 2 .   ? 6.390  10.277  6.360   1.00 25.51 ? 301 FAD A "O2'" 1 
HETATM 2113 C "C3'" . FAD B 2 .   ? 8.060  10.774  8.023   1.00 23.55 ? 301 FAD A "C3'" 1 
HETATM 2114 O "O3'" . FAD B 2 .   ? 8.662  9.843   8.914   1.00 23.74 ? 301 FAD A "O3'" 1 
HETATM 2115 C "C4'" . FAD B 2 .   ? 6.817  11.349  8.694   1.00 23.60 ? 301 FAD A "C4'" 1 
HETATM 2116 O "O4'" . FAD B 2 .   ? 6.128  12.206  7.782   1.00 21.18 ? 301 FAD A "O4'" 1 
HETATM 2117 C "C5'" . FAD B 2 .   ? 7.150  12.064  9.985   1.00 26.01 ? 301 FAD A "C5'" 1 
HETATM 2118 O "O5'" . FAD B 2 .   ? 6.563  11.338  11.084  1.00 23.74 ? 301 FAD A "O5'" 1 
HETATM 2119 P P     . FAD B 2 .   ? 5.457  11.990  11.996  1.00 24.20 ? 301 FAD A P     1 
HETATM 2120 O O1P   . FAD B 2 .   ? 6.123  12.181  13.361  1.00 24.44 ? 301 FAD A O1P   1 
HETATM 2121 O O2P   . FAD B 2 .   ? 4.190  11.215  11.989  1.00 27.10 ? 301 FAD A O2P   1 
HETATM 2122 O O3P   . FAD B 2 .   ? 5.223  13.431  11.355  1.00 28.05 ? 301 FAD A O3P   1 
HETATM 2123 O O     . HOH C 3 .   ? 12.688 4.704   -0.726  1.00 14.13 ? 401 HOH A O     1 
HETATM 2124 O O     . HOH C 3 .   ? 0.810  -10.873 7.532   1.00 37.08 ? 402 HOH A O     1 
HETATM 2125 O O     . HOH C 3 .   ? 14.568 11.346  -10.925 1.00 25.14 ? 403 HOH A O     1 
HETATM 2126 O O     . HOH C 3 .   ? 26.003 -2.610  9.733   1.00 20.27 ? 404 HOH A O     1 
HETATM 2127 O O     . HOH C 3 .   ? 33.030 14.860  -4.112  1.00 14.86 ? 405 HOH A O     1 
HETATM 2128 O O     . HOH C 3 .   ? 8.629  -8.911  6.284   1.00 28.08 ? 406 HOH A O     1 
HETATM 2129 O O     . HOH C 3 .   ? 17.291 -8.726  0.751   1.00 19.43 ? 407 HOH A O     1 
HETATM 2130 O O     . HOH C 3 .   ? 29.920 25.990  -14.854 1.00 32.99 ? 408 HOH A O     1 
HETATM 2131 O O     . HOH C 3 .   ? 23.794 24.684  -16.810 1.00 19.26 ? 409 HOH A O     1 
HETATM 2132 O O     . HOH C 3 .   ? 20.287 -5.291  -6.416  1.00 24.21 ? 410 HOH A O     1 
HETATM 2133 O O     . HOH C 3 .   ? 4.587  -3.322  3.209   1.00 33.54 ? 411 HOH A O     1 
HETATM 2134 O O     . HOH C 3 .   ? 19.029 -5.043  5.151   1.00 18.49 ? 412 HOH A O     1 
HETATM 2135 O O     . HOH C 3 .   ? 31.125 26.691  -11.466 1.00 29.75 ? 413 HOH A O     1 
HETATM 2136 O O     . HOH C 3 .   ? 17.221 0.265   -6.966  1.00 20.73 ? 414 HOH A O     1 
HETATM 2137 O O     . HOH C 3 .   ? 22.968 -1.009  7.928   1.00 21.80 ? 415 HOH A O     1 
HETATM 2138 O O     . HOH C 3 .   ? 8.982  12.694  -18.107 1.00 21.34 ? 416 HOH A O     1 
HETATM 2139 O O     . HOH C 3 .   ? 36.950 20.622  -12.388 1.00 26.65 ? 417 HOH A O     1 
HETATM 2140 O O     . HOH C 3 .   ? 0.808  -11.912 15.295  1.00 29.39 ? 418 HOH A O     1 
HETATM 2141 O O     . HOH C 3 .   ? 15.942 1.029   0.264   1.00 17.90 ? 419 HOH A O     1 
HETATM 2142 O O     . HOH C 3 .   ? 43.246 0.419   1.152   1.00 22.72 ? 420 HOH A O     1 
HETATM 2143 O O     . HOH C 3 .   ? 5.603  21.512  8.120   1.00 30.46 ? 421 HOH A O     1 
HETATM 2144 O O     . HOH C 3 .   ? 20.978 -3.262  -0.759  1.00 17.21 ? 422 HOH A O     1 
HETATM 2145 O O     . HOH C 3 .   ? 2.535  11.463  21.559  1.00 20.55 ? 423 HOH A O     1 
HETATM 2146 O O     . HOH C 3 .   ? 36.415 5.884   10.354  1.00 35.40 ? 424 HOH A O     1 
HETATM 2147 O O     . HOH C 3 .   ? 26.888 22.374  11.736  1.00 18.23 ? 425 HOH A O     1 
HETATM 2148 O O     . HOH C 3 .   ? -1.136 4.343   11.390  1.00 24.72 ? 426 HOH A O     1 
HETATM 2149 O O     . HOH C 3 .   ? 23.651 -2.511  5.589   1.00 17.45 ? 427 HOH A O     1 
HETATM 2150 O O     . HOH C 3 .   ? 39.113 5.747   3.675   1.00 21.81 ? 428 HOH A O     1 
HETATM 2151 O O     . HOH C 3 .   ? 25.186 -9.469  -8.421  1.00 24.22 ? 429 HOH A O     1 
HETATM 2152 O O     . HOH C 3 .   ? 13.314 10.557  3.619   1.00 19.11 ? 430 HOH A O     1 
HETATM 2153 O O     . HOH C 3 .   ? 26.115 13.003  3.945   1.00 16.85 ? 431 HOH A O     1 
HETATM 2154 O O     . HOH C 3 .   ? 12.153 18.680  12.509  1.00 16.65 ? 432 HOH A O     1 
HETATM 2155 O O     . HOH C 3 .   ? 11.386 15.369  -21.441 1.00 18.61 ? 433 HOH A O     1 
HETATM 2156 O O     . HOH C 3 .   ? 15.325 5.407   6.525   1.00 15.12 ? 434 HOH A O     1 
HETATM 2157 O O     . HOH C 3 .   ? 24.254 -7.376  9.911   1.00 19.85 ? 435 HOH A O     1 
HETATM 2158 O O     . HOH C 3 .   ? 40.035 9.298   7.184   1.00 17.71 ? 436 HOH A O     1 
HETATM 2159 O O     . HOH C 3 .   ? 18.447 27.245  2.183   1.00 15.19 ? 437 HOH A O     1 
HETATM 2160 O O     . HOH C 3 .   ? 15.611 15.318  19.379  1.00 18.47 ? 438 HOH A O     1 
HETATM 2161 O O     . HOH C 3 .   ? 15.923 22.136  2.010   1.00 22.86 ? 439 HOH A O     1 
HETATM 2162 O O     . HOH C 3 .   ? 24.848 3.040   20.585  1.00 22.21 ? 440 HOH A O     1 
HETATM 2163 O O     . HOH C 3 .   ? 25.635 3.038   15.578  1.00 19.31 ? 441 HOH A O     1 
HETATM 2164 O O     . HOH C 3 .   ? -0.763 -3.052  16.321  1.00 36.61 ? 442 HOH A O     1 
HETATM 2165 O O     . HOH C 3 .   ? 25.175 -4.837  -16.189 1.00 17.39 ? 443 HOH A O     1 
HETATM 2166 O O     . HOH C 3 .   ? 6.212  22.395  17.344  1.00 18.42 ? 444 HOH A O     1 
HETATM 2167 O O     . HOH C 3 .   ? 13.030 8.983   1.669   1.00 15.80 ? 445 HOH A O     1 
HETATM 2168 O O     . HOH C 3 .   ? 0.238  0.627   24.056  1.00 25.00 ? 446 HOH A O     1 
HETATM 2169 O O     . HOH C 3 .   ? 25.801 6.564   18.959  1.00 14.79 ? 447 HOH A O     1 
HETATM 2170 O O     . HOH C 3 .   ? 17.486 -4.566  -16.980 1.00 17.66 ? 448 HOH A O     1 
HETATM 2171 O O     . HOH C 3 .   ? 37.492 19.994  -9.891  1.00 20.88 ? 449 HOH A O     1 
HETATM 2172 O O     . HOH C 3 .   ? 26.715 2.303   19.869  1.00 22.10 ? 450 HOH A O     1 
HETATM 2173 O O     . HOH C 3 .   ? 30.924 -8.703  -8.991  1.00 16.42 ? 451 HOH A O     1 
HETATM 2174 O O     . HOH C 3 .   ? 28.630 25.912  -17.382 1.00 21.11 ? 452 HOH A O     1 
HETATM 2175 O O     . HOH C 3 .   ? 30.304 0.579   -21.494 1.00 19.27 ? 453 HOH A O     1 
HETATM 2176 O O     . HOH C 3 .   ? 34.951 12.767  -4.432  1.00 16.04 ? 454 HOH A O     1 
HETATM 2177 O O     . HOH C 3 .   ? 25.717 -5.859  13.129  1.00 15.49 ? 455 HOH A O     1 
HETATM 2178 O O     . HOH C 3 .   ? 7.444  7.959   23.421  1.00 16.88 ? 456 HOH A O     1 
HETATM 2179 O O     . HOH C 3 .   ? 36.577 -1.209  -10.892 1.00 26.99 ? 457 HOH A O     1 
HETATM 2180 O O     . HOH C 3 .   ? -2.185 17.926  7.428   1.00 20.05 ? 458 HOH A O     1 
HETATM 2181 O O     . HOH C 3 .   ? 30.290 18.106  11.580  1.00 16.28 ? 459 HOH A O     1 
HETATM 2182 O O     . HOH C 3 .   ? 11.711 28.307  -9.781  1.00 24.66 ? 460 HOH A O     1 
HETATM 2183 O O     . HOH C 3 .   ? 24.041 -6.250  15.558  1.00 21.57 ? 461 HOH A O     1 
HETATM 2184 O O     . HOH C 3 .   ? 7.804  -6.842  -16.414 1.00 20.10 ? 462 HOH A O     1 
HETATM 2185 O O     . HOH C 3 .   ? 10.002 29.087  -10.968 1.00 27.22 ? 463 HOH A O     1 
HETATM 2186 O O     . HOH C 3 .   ? 32.692 18.151  12.580  1.00 19.16 ? 464 HOH A O     1 
# 
