data_9GXC
# 
_entry.id   9GXC 
# 
_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   9GXC         pdb_00009gxc 10.2210/pdb9gxc/pdb 
WWPDB D_1292141326 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GXC 
_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 
4 mmartine@unizar.es   Marta    Martinez-Julvez ? 'principal investigator/group leader' 0000-0001-9047-0046 
5 mmedina@unizar.es    Milagros Medina          ? 'principal investigator/group leader' 0000-0001-8743-0182 
6 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' 30704.588 1  1.18.1.2 ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'   785.550   1  ?        ? ? ? 
3 water       nat water                           18.015    23 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GPGSHMSSNFNQETVTDIHHWTDTLFSFRTTRDPGFRFQSGQFIMMGLEVNGKPLTRAYSIASSLYEDGLEFFSIKVPNG
PLTSKLQHLKKGDQIIVSKKPVGTLLYDNLKPGKHLWLLSTGTGLAPFLSIIRDLEVYERFEKVILVHGVRQVAELAYTD
FISNELPQDEFLGEMVKNQLIYYPTVTREPYKTRGRLTDLIRSGQLFKDVGLPEFNHEDDRMMLCGSPEMLAETKQILEE
RGFTEGSQSEPGEFVIEKAFVEK(FAD)
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGSHMSSNFNQETVTDIHHWTDTLFSFRTTRDPGFRFQSGQFIMMGLEVNGKPLTRAYSIASSLYEDGLEFFSIKVPNG
PLTSKLQHLKKGDQIIVSKKPVGTLLYDNLKPGKHLWLLSTGTGLAPFLSIIRDLEVYERFEKVILVHGVRQVAELAYTD
FISNELPQDEFLGEMVKNQLIYYPTVTREPYKTRGRLTDLIRSGQLFKDVGLPEFNHEDDRMMLCGSPEMLAETKQILEE
RGFTEGSQSEPGEFVIEKAFVEKX
;
_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 
1 264 FAD 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                   264 
_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 
A 1 264 FAD 264 259 ?   ?   ?   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 6   HOH HOH A . 
C 3 HOH 2  402 10  HOH HOH A . 
C 3 HOH 3  403 17  HOH HOH A . 
C 3 HOH 4  404 14  HOH HOH A . 
C 3 HOH 5  405 13  HOH HOH A . 
C 3 HOH 6  406 8   HOH HOH A . 
C 3 HOH 7  407 20  HOH HOH A . 
C 3 HOH 8  408 15  HOH HOH A . 
C 3 HOH 9  409 16  HOH HOH A . 
C 3 HOH 10 410 11  HOH HOH A . 
C 3 HOH 11 411 7   HOH HOH A . 
C 3 HOH 12 412 21  HOH HOH A . 
C 3 HOH 13 413 23  HOH HOH A . 
C 3 HOH 14 414 12  HOH HOH A . 
C 3 HOH 15 415 18  HOH HOH A . 
C 3 HOH 16 416 9   HOH HOH A . 
C 3 HOH 17 417 5   HOH HOH A . 
C 3 HOH 18 418 4   HOH HOH A . 
C 3 HOH 19 419 2   HOH HOH A . 
C 3 HOH 20 420 3   HOH HOH A . 
C 3 HOH 21 421 19  HOH HOH A . 
C 3 HOH 22 422 22  HOH HOH A . 
C 3 HOH 23 423 1   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 ? ? ? 0.10.2      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                     9GXC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.600 
_cell.length_a_esd                 ? 
_cell.length_b                     39.600 
_cell.length_b_esd                 ? 
_cell.length_c                     167.600 
_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                         9GXC 
_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                   9GXC 
_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          47.00 
_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                         'SLAC ePix10k 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-08 
_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   1.107 
_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                        'SLAC LCLS BEAMLINE MFX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.107 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MFX 
_diffrn_source.pdbx_synchrotron_site       'SLAC LCLS' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GXC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               35.2 
_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                                     28492 
_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                                413 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.3 
_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                                   0.9798 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.1 
_reflns_shell.d_res_low                                     2.2 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2878 
_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                                  0.2043 
_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                                 9GXC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             35.2 
_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                     13025 
_refine.ls_number_reflns_R_free                  628 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1858 
_refine.ls_R_factor_R_free                       0.1967 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1779 
_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                          48.25 
_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                 22.93 
_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.pdbx_number_atoms_protein        2070 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             23 
_refine_hist.number_atoms_total               2146 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        35.2 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.498 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.890 ? 282 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 320 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 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' 2.20 2.42 . . 173 3053 95.00 . . . . 0.7283 . . . . . . . . . . . 0.7729 
'X-RAY DIFFRACTION' 2.42 2.77 . . 133 3125 96.00 . . . . 0.2774 . . . . . . . . . . . 0.3183 
'X-RAY DIFFRACTION' 2.77 3.49 . . 156 3106 95.00 . . . . 0.2060 . . . . . . . . . . . 0.2642 
'X-RAY DIFFRACTION' 3.49 35.2 . . 166 3113 95.00 . . . . 0.1289 . . . . . . . . . . . 0.1419 
# 
_struct.entry_id                     9GXC 
_struct.title                        
'Room temperature structure of FAD-containing ferrodoxin-NADP reductase from Brucella ovis at LCLS' 
_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        9GXC 
_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              9GXC 
_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 9GXC GLY A 1   ? UNP A0A0H3ASL8 ? ? 'expression tag' -4  1 
1 9GXC PRO A 2   ? UNP A0A0H3ASL8 ? ? 'expression tag' -3  2 
1 9GXC GLY A 3   ? UNP A0A0H3ASL8 ? ? 'expression tag' -2  3 
1 9GXC SER A 4   ? UNP A0A0H3ASL8 ? ? 'expression tag' -1  4 
1 9GXC HIS A 5   ? UNP A0A0H3ASL8 ? ? 'expression tag' 0   5 
1 9GXC FAD A 264 ? UNP A0A0H3ASL8 ? ? 'expression tag' 259 6 
# 
_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)' 1260  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  11770 ? 
# 
_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 ? GLU A 165 ? TYR A 153 GLU A 160 1 ? 8  
HELX_P HELX_P7  AA7 LEU A 172 ? GLN A 179 ? LEU A 167 GLN A 174 1 ? 8  
HELX_P HELX_P8  AA8 ARG A 196 ? SER A 203 ? ARG A 191 SER A 198 1 ? 8  
HELX_P HELX_P9  AA9 GLY A 204 ? GLY A 211 ? GLY A 199 GLY A 206 1 ? 8  
HELX_P HELX_P10 AB1 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 ARG A 57  ? O ARG A 52  N MET A 46  ? N MET A 41  
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 PHE A 26  ? N PHE A 21  O SER A 74  ? O SER A 69  
AA2 1 2 O ILE A 181 ? O ILE A 176 N LEU A 146 ? N LEU A 141 
AA2 2 3 O VAL A 147 ? O VAL A 142 N LEU A 118 ? N LEU A 113 
AA2 3 4 N TRP A 117 ? N TRP A 112 O ARG A 221 ? O ARG A 216 
AA2 4 5 N LEU A 224 ? N LEU A 219 O GLU A 257 ? O GLU A 252 
# 
_pdbx_entry_details.entry_id                   9GXC 
_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 OE1 A GLU 66  ? ? O A HOH 401 ? ? 1.95 
2 1 OE1 A GLU 252 ? ? O A HOH 402 ? ? 2.17 
3 1 O   A ARG 135 ? ? O A HOH 403 ? ? 2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     3 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             71.18 
_pdbx_validate_torsion.psi             -15.70 
# 
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   
7 1 Y 1 A FAD 259 ? A FAD 264 
# 
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   MESH 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    9GXC 
_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]   0.025253 
_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]   0.025253 
_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]   0.005967 
_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   ? 22.278  25.610 13.927  1.00 84.49  ? 2   SER A N     1 
ATOM   2    C CA    . SER A 1 7   ? 20.917  26.065 13.674  1.00 86.87  ? 2   SER A CA    1 
ATOM   3    C C     . SER A 1 7   ? 20.914  27.449 13.022  1.00 88.37  ? 2   SER A C     1 
ATOM   4    O O     . SER A 1 7   ? 21.894  27.849 12.391  1.00 87.79  ? 2   SER A O     1 
ATOM   5    C CB    . SER A 1 7   ? 20.106  26.078 14.972  1.00 86.97  ? 2   SER A CB    1 
ATOM   6    O OG    . SER A 1 7   ? 19.943  24.764 15.482  1.00 87.81  ? 2   SER A OG    1 
ATOM   7    N N     . SER A 1 8   ? 19.799  28.164 13.176  1.00 87.94  ? 3   SER A N     1 
ATOM   8    C CA    . SER A 1 8   ? 19.465  29.442 12.558  1.00 88.09  ? 3   SER A CA    1 
ATOM   9    C C     . SER A 1 8   ? 19.181  29.288 11.065  1.00 82.09  ? 3   SER A C     1 
ATOM   10   O O     . SER A 1 8   ? 18.612  30.202 10.466  1.00 84.62  ? 3   SER A O     1 
ATOM   11   C CB    . SER A 1 8   ? 20.542  30.526 12.762  1.00 91.79  ? 3   SER A CB    1 
ATOM   12   O OG    . SER A 1 8   ? 20.187  31.726 12.098  1.00 83.84  ? 3   SER A OG    1 
ATOM   13   N N     . ASN A 1 9   ? 19.557  28.173 10.443  1.00 78.88  ? 4   ASN A N     1 
ATOM   14   C CA    . ASN A 1 9   ? 19.049  27.815 9.129   1.00 76.74  ? 4   ASN A CA    1 
ATOM   15   C C     . ASN A 1 9   ? 17.696  27.118 9.211   1.00 69.93  ? 4   ASN A C     1 
ATOM   16   O O     . ASN A 1 9   ? 17.200  26.626 8.192   1.00 60.77  ? 4   ASN A O     1 
ATOM   17   C CB    . ASN A 1 9   ? 20.058  26.923 8.399   1.00 82.55  ? 4   ASN A CB    1 
ATOM   18   C CG    . ASN A 1 9   ? 21.495  27.354 8.634   1.00 96.61  ? 4   ASN A CG    1 
ATOM   19   O OD1   . ASN A 1 9   ? 21.763  28.507 8.973   1.00 101.91 ? 4   ASN A OD1   1 
ATOM   20   N ND2   . ASN A 1 9   ? 22.427  26.427 8.450   1.00 90.19  ? 4   ASN A ND2   1 
ATOM   21   N N     . PHE A 1 10  ? 17.097  27.069 10.398  1.00 69.34  ? 5   PHE A N     1 
ATOM   22   C CA    . PHE A 1 10  ? 15.842  26.374 10.636  1.00 62.77  ? 5   PHE A CA    1 
ATOM   23   C C     . PHE A 1 10  ? 14.819  27.341 11.219  1.00 66.43  ? 5   PHE A C     1 
ATOM   24   O O     . PHE A 1 10  ? 15.154  28.442 11.661  1.00 70.53  ? 5   PHE A O     1 
ATOM   25   C CB    . PHE A 1 10  ? 16.036  25.187 11.596  1.00 59.92  ? 5   PHE A CB    1 
ATOM   26   C CG    . PHE A 1 10  ? 16.876  24.071 11.035  1.00 64.09  ? 5   PHE A CG    1 
ATOM   27   C CD1   . PHE A 1 10  ? 18.248  24.053 11.230  1.00 68.73  ? 5   PHE A CD1   1 
ATOM   28   C CD2   . PHE A 1 10  ? 16.291  23.026 10.340  1.00 63.97  ? 5   PHE A CD2   1 
ATOM   29   C CE1   . PHE A 1 10  ? 19.023  23.020 10.722  1.00 66.57  ? 5   PHE A CE1   1 
ATOM   30   C CE2   . PHE A 1 10  ? 17.059  21.992 9.832   1.00 59.81  ? 5   PHE A CE2   1 
ATOM   31   C CZ    . PHE A 1 10  ? 18.426  21.989 10.023  1.00 61.65  ? 5   PHE A CZ    1 
ATOM   32   N N     . ASN A 1 11  ? 13.560  26.919 11.198  1.00 61.89  ? 6   ASN A N     1 
ATOM   33   C CA    . ASN A 1 11  ? 12.475  27.630 11.858  1.00 57.77  ? 6   ASN A CA    1 
ATOM   34   C C     . ASN A 1 11  ? 12.061  26.867 13.107  1.00 54.67  ? 6   ASN A C     1 
ATOM   35   O O     . ASN A 1 11  ? 11.918  25.642 13.076  1.00 58.45  ? 6   ASN A O     1 
ATOM   36   C CB    . ASN A 1 11  ? 11.270  27.799 10.924  1.00 60.24  ? 6   ASN A CB    1 
ATOM   37   C CG    . ASN A 1 11  ? 11.477  28.887 9.890   1.00 60.50  ? 6   ASN A CG    1 
ATOM   38   O OD1   . ASN A 1 11  ? 12.189  29.861 10.131  1.00 60.94  ? 6   ASN A OD1   1 
ATOM   39   N ND2   . ASN A 1 11  ? 10.854  28.724 8.728   1.00 61.44  ? 6   ASN A ND2   1 
ATOM   40   N N     . GLN A 1 12  ? 11.887  27.589 14.210  1.00 56.95  ? 7   GLN A N     1 
ATOM   41   C CA    . GLN A 1 12  ? 11.420  26.993 15.457  1.00 59.10  ? 7   GLN A CA    1 
ATOM   42   C C     . GLN A 1 12  ? 9.898   27.050 15.473  1.00 57.09  ? 7   GLN A C     1 
ATOM   43   O O     . GLN A 1 12  ? 9.311   28.133 15.558  1.00 54.80  ? 7   GLN A O     1 
ATOM   44   C CB    . GLN A 1 12  ? 12.015  27.711 16.665  1.00 64.37  ? 7   GLN A CB    1 
ATOM   45   C CG    . GLN A 1 12  ? 13.256  27.042 17.228  1.00 65.99  ? 7   GLN A CG    1 
ATOM   46   C CD    . GLN A 1 12  ? 13.297  27.079 18.744  1.00 73.23  ? 7   GLN A CD    1 
ATOM   47   O OE1   . GLN A 1 12  ? 13.272  26.037 19.401  1.00 65.90  ? 7   GLN A OE1   1 
ATOM   48   N NE2   . GLN A 1 12  ? 13.358  28.279 19.307  1.00 82.07  ? 7   GLN A NE2   1 
ATOM   49   N N     . GLU A 1 13  ? 9.262   25.886 15.381  1.00 53.26  ? 8   GLU A N     1 
ATOM   50   C CA    . GLU A 1 13  ? 7.812   25.783 15.367  1.00 51.71  ? 8   GLU A CA    1 
ATOM   51   C C     . GLU A 1 13  ? 7.334   25.043 16.608  1.00 51.46  ? 8   GLU A C     1 
ATOM   52   O O     . GLU A 1 13  ? 8.060   24.227 17.185  1.00 54.17  ? 8   GLU A O     1 
ATOM   53   C CB    . GLU A 1 13  ? 7.317   25.067 14.101  1.00 53.14  ? 8   GLU A CB    1 
ATOM   54   C CG    . GLU A 1 13  ? 7.977   25.548 12.814  1.00 52.42  ? 8   GLU A CG    1 
ATOM   55   C CD    . GLU A 1 13  ? 7.429   26.877 12.320  1.00 56.42  ? 8   GLU A CD    1 
ATOM   56   O OE1   . GLU A 1 13  ? 6.597   27.491 13.022  1.00 57.80  ? 8   GLU A OE1   1 
ATOM   57   O OE2   . GLU A 1 13  ? 7.839   27.315 11.225  1.00 56.74  ? 8   GLU A OE2   1 
ATOM   58   N N     . THR A 1 14  ? 6.102   25.337 17.012  1.00 54.65  ? 9   THR A N     1 
ATOM   59   C CA    . THR A 1 14  ? 5.513   24.795 18.230  1.00 51.90  ? 9   THR A CA    1 
ATOM   60   C C     . THR A 1 14  ? 4.400   23.826 17.858  1.00 49.89  ? 9   THR A C     1 
ATOM   61   O O     . THR A 1 14  ? 3.475   24.191 17.124  1.00 51.77  ? 9   THR A O     1 
ATOM   62   C CB    . THR A 1 14  ? 4.969   25.915 19.117  1.00 52.09  ? 9   THR A CB    1 
ATOM   63   O OG1   . THR A 1 14  ? 5.816   27.066 19.010  1.00 55.35  ? 9   THR A OG1   1 
ATOM   64   C CG2   . THR A 1 14  ? 4.917   25.464 20.565  1.00 57.89  ? 9   THR A CG2   1 
ATOM   65   N N     . VAL A 1 15  ? 4.488   22.597 18.372  1.00 50.66  ? 10  VAL A N     1 
ATOM   66   C CA    . VAL A 1 15  ? 3.465   21.597 18.093  1.00 52.66  ? 10  VAL A CA    1 
ATOM   67   C C     . VAL A 1 15  ? 2.147   22.034 18.714  1.00 55.25  ? 10  VAL A C     1 
ATOM   68   O O     . VAL A 1 15  ? 2.088   22.405 19.893  1.00 59.04  ? 10  VAL A O     1 
ATOM   69   C CB    . VAL A 1 15  ? 3.907   20.222 18.615  1.00 50.99  ? 10  VAL A CB    1 
ATOM   70   C CG1   . VAL A 1 15  ? 2.800   19.203 18.422  1.00 52.07  ? 10  VAL A CG1   1 
ATOM   71   C CG2   . VAL A 1 15  ? 5.182   19.773 17.915  1.00 51.25  ? 10  VAL A CG2   1 
ATOM   72   N N     . THR A 1 16  ? 1.077   21.997 17.916  1.00 53.45  ? 11  THR A N     1 
ATOM   73   C CA    . THR A 1 16  ? -0.242  22.414 18.369  1.00 52.67  ? 11  THR A CA    1 
ATOM   74   C C     . THR A 1 16  ? -1.232  21.269 18.519  1.00 54.79  ? 11  THR A C     1 
ATOM   75   O O     . THR A 1 16  ? -2.204  21.411 19.267  1.00 51.39  ? 11  THR A O     1 
ATOM   76   C CB    . THR A 1 16  ? -0.837  23.451 17.403  1.00 55.13  ? 11  THR A CB    1 
ATOM   77   O OG1   . THR A 1 16  ? -1.132  22.826 16.148  1.00 56.80  ? 11  THR A OG1   1 
ATOM   78   C CG2   . THR A 1 16  ? 0.141   24.593 17.175  1.00 48.08  ? 11  THR A CG2   1 
ATOM   79   N N     . ASP A 1 17  ? -1.014  20.150 17.834  1.00 56.18  ? 12  ASP A N     1 
ATOM   80   C CA    . ASP A 1 17  ? -1.913  19.007 17.897  1.00 55.45  ? 12  ASP A CA    1 
ATOM   81   C C     . ASP A 1 17  ? -1.116  17.749 17.597  1.00 52.98  ? 12  ASP A C     1 
ATOM   82   O O     . ASP A 1 17  ? -0.208  17.774 16.766  1.00 51.09  ? 12  ASP A O     1 
ATOM   83   C CB    . ASP A 1 17  ? -3.071  19.149 16.900  1.00 58.01  ? 12  ASP A CB    1 
ATOM   84   C CG    . ASP A 1 17  ? -4.375  18.595 17.436  1.00 62.77  ? 12  ASP A CG    1 
ATOM   85   O OD1   . ASP A 1 17  ? -4.387  17.428 17.883  1.00 66.03  ? 12  ASP A OD1   1 
ATOM   86   O OD2   . ASP A 1 17  ? -5.390  19.322 17.405  1.00 65.05  ? 12  ASP A OD2   1 
ATOM   87   N N     . ILE A 1 18  ? -1.445  16.661 18.290  1.00 54.99  ? 13  ILE A N     1 
ATOM   88   C CA    . ILE A 1 18  ? -0.858  15.350 18.036  1.00 54.98  ? 13  ILE A CA    1 
ATOM   89   C C     . ILE A 1 18  ? -1.977  14.320 18.031  1.00 53.67  ? 13  ILE A C     1 
ATOM   90   O O     . ILE A 1 18  ? -2.804  14.292 18.949  1.00 50.00  ? 13  ILE A O     1 
ATOM   91   C CB    . ILE A 1 18  ? 0.208   14.966 19.082  1.00 48.93  ? 13  ILE A CB    1 
ATOM   92   C CG1   . ILE A 1 18  ? 1.228   16.088 19.269  1.00 54.79  ? 13  ILE A CG1   1 
ATOM   93   C CG2   . ILE A 1 18  ? 0.910   13.675 18.680  1.00 46.92  ? 13  ILE A CG2   1 
ATOM   94   C CD1   . ILE A 1 18  ? 1.179   16.719 20.636  1.00 57.00  ? 13  ILE A CD1   1 
ATOM   95   N N     . HIS A 1 19  ? -2.001  13.477 17.002  1.00 53.57  ? 14  HIS A N     1 
ATOM   96   C CA    . HIS A 1 19  ? -2.948  12.372 16.916  1.00 50.33  ? 14  HIS A CA    1 
ATOM   97   C C     . HIS A 1 19  ? -2.186  11.115 16.529  1.00 49.56  ? 14  HIS A C     1 
ATOM   98   O O     . HIS A 1 19  ? -1.554  11.072 15.469  1.00 51.26  ? 14  HIS A O     1 
ATOM   99   C CB    . HIS A 1 19  ? -4.061  12.662 15.904  1.00 48.42  ? 14  HIS A CB    1 
ATOM   100  C CG    . HIS A 1 19  ? -5.170  11.655 15.923  1.00 50.86  ? 14  HIS A CG    1 
ATOM   101  N ND1   . HIS A 1 19  ? -4.991  10.342 15.545  1.00 56.11  ? 14  HIS A ND1   1 
ATOM   102  C CD2   . HIS A 1 19  ? -6.471  11.769 16.281  1.00 60.39  ? 14  HIS A CD2   1 
ATOM   103  C CE1   . HIS A 1 19  ? -6.134  9.691  15.667  1.00 54.87  ? 14  HIS A CE1   1 
ATOM   104  N NE2   . HIS A 1 19  ? -7.048  10.534 16.112  1.00 61.96  ? 14  HIS A NE2   1 
ATOM   105  N N     . HIS A 1 20  ? -2.245  10.101 17.386  1.00 49.33  ? 15  HIS A N     1 
ATOM   106  C CA    . HIS A 1 20  ? -1.605  8.820  17.120  1.00 46.47  ? 15  HIS A CA    1 
ATOM   107  C C     . HIS A 1 20  ? -2.613  7.885  16.463  1.00 47.31  ? 15  HIS A C     1 
ATOM   108  O O     . HIS A 1 20  ? -3.647  7.562  17.057  1.00 49.82  ? 15  HIS A O     1 
ATOM   109  C CB    . HIS A 1 20  ? -1.059  8.206  18.409  1.00 44.51  ? 15  HIS A CB    1 
ATOM   110  C CG    . HIS A 1 20  ? 0.087   8.966  19.002  1.00 42.87  ? 15  HIS A CG    1 
ATOM   111  N ND1   . HIS A 1 20  ? 1.399   8.568  18.856  1.00 45.14  ? 15  HIS A ND1   1 
ATOM   112  C CD2   . HIS A 1 20  ? 0.119   10.098 19.744  1.00 41.32  ? 15  HIS A CD2   1 
ATOM   113  C CE1   . HIS A 1 20  ? 2.189   9.422  19.481  1.00 42.64  ? 15  HIS A CE1   1 
ATOM   114  N NE2   . HIS A 1 20  ? 1.437   10.360 20.029  1.00 44.26  ? 15  HIS A NE2   1 
ATOM   115  N N     . TRP A 1 21  ? -2.315  7.461  15.234  1.00 49.66  ? 16  TRP A N     1 
ATOM   116  C CA    . TRP A 1 21  ? -3.199  6.534  14.536  1.00 51.21  ? 16  TRP A CA    1 
ATOM   117  C C     . TRP A 1 21  ? -2.989  5.105  15.023  1.00 47.16  ? 16  TRP A C     1 
ATOM   118  O O     . TRP A 1 21  ? -3.948  4.422  15.399  1.00 45.32  ? 16  TRP A O     1 
ATOM   119  C CB    . TRP A 1 21  ? -2.972  6.633  13.027  1.00 50.62  ? 16  TRP A CB    1 
ATOM   120  C CG    . TRP A 1 21  ? -2.986  8.041  12.517  1.00 47.20  ? 16  TRP A CG    1 
ATOM   121  C CD1   . TRP A 1 21  ? -1.903  8.816  12.222  1.00 47.58  ? 16  TRP A CD1   1 
ATOM   122  C CD2   . TRP A 1 21  ? -4.141  8.848  12.250  1.00 44.25  ? 16  TRP A CD2   1 
ATOM   123  N NE1   . TRP A 1 21  ? -2.311  10.053 11.785  1.00 47.88  ? 16  TRP A NE1   1 
ATOM   124  C CE2   . TRP A 1 21  ? -3.680  10.098 11.793  1.00 42.60  ? 16  TRP A CE2   1 
ATOM   125  C CE3   . TRP A 1 21  ? -5.519  8.632  12.351  1.00 43.51  ? 16  TRP A CE3   1 
ATOM   126  C CZ2   . TRP A 1 21  ? -4.547  11.129 11.437  1.00 39.73  ? 16  TRP A CZ2   1 
ATOM   127  C CZ3   . TRP A 1 21  ? -6.379  9.658  11.997  1.00 43.32  ? 16  TRP A CZ3   1 
ATOM   128  C CH2   . TRP A 1 21  ? -5.890  10.890 11.546  1.00 42.94  ? 16  TRP A CH2   1 
ATOM   129  N N     . THR A 1 22  ? -1.741  4.639  15.021  1.00 46.25  ? 17  THR A N     1 
ATOM   130  C CA    . THR A 1 22  ? -1.406  3.320  15.544  1.00 45.68  ? 17  THR A CA    1 
ATOM   131  C C     . THR A 1 22  ? -0.206  3.413  16.477  1.00 50.16  ? 17  THR A C     1 
ATOM   132  O O     . THR A 1 22  ? 0.184   4.511  16.888  1.00 49.78  ? 17  THR A O     1 
ATOM   133  C CB    . THR A 1 22  ? -1.106  2.337  14.407  1.00 48.43  ? 17  THR A CB    1 
ATOM   134  O OG1   . THR A 1 22  ? 0.035   2.792  13.668  1.00 51.83  ? 17  THR A OG1   1 
ATOM   135  C CG2   . THR A 1 22  ? -2.298  2.206  13.469  1.00 51.71  ? 17  THR A CG2   1 
ATOM   136  N N     . ASP A 1 23  ? 0.383   2.268  16.819  1.00 51.35  ? 18  ASP A N     1 
ATOM   137  C CA    . ASP A 1 23  ? 1.631   2.255  17.569  1.00 51.02  ? 18  ASP A CA    1 
ATOM   138  C C     . ASP A 1 23  ? 2.835   2.594  16.701  1.00 56.89  ? 18  ASP A C     1 
ATOM   139  O O     . ASP A 1 23  ? 3.937   2.760  17.233  1.00 55.01  ? 18  ASP A O     1 
ATOM   140  C CB    . ASP A 1 23  ? 1.841   0.889  18.227  1.00 53.40  ? 18  ASP A CB    1 
ATOM   141  C CG    . ASP A 1 23  ? 1.703   -0.257 17.245  1.00 54.05  ? 18  ASP A CG    1 
ATOM   142  O OD1   . ASP A 1 23  ? 1.066   -0.063 16.188  1.00 54.46  ? 18  ASP A OD1   1 
ATOM   143  O OD2   . ASP A 1 23  ? 2.231   -1.353 17.530  1.00 55.91  ? 18  ASP A OD2   1 
ATOM   144  N N     . THR A 1 24  ? 2.647   2.696  15.383  1.00 54.36  ? 19  THR A N     1 
ATOM   145  C CA    . THR A 1 24  ? 3.712   3.056  14.461  1.00 50.55  ? 19  THR A CA    1 
ATOM   146  C C     . THR A 1 24  ? 3.417   4.308  13.650  1.00 49.06  ? 19  THR A C     1 
ATOM   147  O O     . THR A 1 24  ? 4.335   4.839  13.015  1.00 49.45  ? 19  THR A O     1 
ATOM   148  C CB    . THR A 1 24  ? 3.997   1.902  13.487  1.00 52.44  ? 19  THR A CB    1 
ATOM   149  O OG1   . THR A 1 24  ? 2.821   1.628  12.715  1.00 58.00  ? 19  THR A OG1   1 
ATOM   150  C CG2   . THR A 1 24  ? 4.400   0.649  14.246  1.00 53.37  ? 19  THR A CG2   1 
ATOM   151  N N     . LEU A 1 25  ? 2.178   4.791  13.648  1.00 52.18  ? 20  LEU A N     1 
ATOM   152  C CA    . LEU A 1 25  ? 1.778   5.942  12.852  1.00 48.59  ? 20  LEU A CA    1 
ATOM   153  C C     . LEU A 1 25  ? 1.194   7.011  13.763  1.00 49.42  ? 20  LEU A C     1 
ATOM   154  O O     . LEU A 1 25  ? 0.357   6.711  14.622  1.00 52.34  ? 20  LEU A O     1 
ATOM   155  C CB    . LEU A 1 25  ? 0.753   5.544  11.785  1.00 48.62  ? 20  LEU A CB    1 
ATOM   156  C CG    . LEU A 1 25  ? 1.272   4.803  10.552  1.00 50.12  ? 20  LEU A CG    1 
ATOM   157  C CD1   . LEU A 1 25  ? 0.113   4.220  9.758   1.00 57.45  ? 20  LEU A CD1   1 
ATOM   158  C CD2   . LEU A 1 25  ? 2.108   5.724  9.684   1.00 47.32  ? 20  LEU A CD2   1 
ATOM   159  N N     . PHE A 1 26  ? 1.641   8.251  13.576  1.00 48.54  ? 21  PHE A N     1 
ATOM   160  C CA    . PHE A 1 26  ? 1.051   9.384  14.270  1.00 44.30  ? 21  PHE A CA    1 
ATOM   161  C C     . PHE A 1 26  ? 1.263   10.637 13.437  1.00 45.04  ? 21  PHE A C     1 
ATOM   162  O O     . PHE A 1 26  ? 2.255   10.761 12.712  1.00 44.81  ? 21  PHE A O     1 
ATOM   163  C CB    . PHE A 1 26  ? 1.640   9.577  15.674  1.00 46.72  ? 21  PHE A CB    1 
ATOM   164  C CG    . PHE A 1 26  ? 2.941   10.329 15.696  1.00 45.35  ? 21  PHE A CG    1 
ATOM   165  C CD1   . PHE A 1 26  ? 4.090   9.773  15.168  1.00 46.89  ? 21  PHE A CD1   1 
ATOM   166  C CD2   . PHE A 1 26  ? 3.012   11.595 16.258  1.00 42.60  ? 21  PHE A CD2   1 
ATOM   167  C CE1   . PHE A 1 26  ? 5.289   10.458 15.196  1.00 43.42  ? 21  PHE A CE1   1 
ATOM   168  C CE2   . PHE A 1 26  ? 4.209   12.288 16.286  1.00 41.73  ? 21  PHE A CE2   1 
ATOM   169  C CZ    . PHE A 1 26  ? 5.348   11.719 15.754  1.00 44.65  ? 21  PHE A CZ    1 
ATOM   170  N N     . SER A 1 27  ? 0.314   11.562 13.549  1.00 48.35  ? 22  SER A N     1 
ATOM   171  C CA    . SER A 1 27  ? 0.366   12.842 12.862  1.00 44.10  ? 22  SER A CA    1 
ATOM   172  C C     . SER A 1 27  ? 0.340   13.958 13.896  1.00 46.28  ? 22  SER A C     1 
ATOM   173  O O     . SER A 1 27  ? -0.323  13.837 14.931  1.00 46.27  ? 22  SER A O     1 
ATOM   174  C CB    . SER A 1 27  ? -0.808  12.994 11.894  1.00 40.28  ? 22  SER A CB    1 
ATOM   175  O OG    . SER A 1 27  ? -0.746  12.029 10.857  1.00 48.16  ? 22  SER A OG    1 
ATOM   176  N N     . PHE A 1 28  ? 1.067   15.039 13.623  1.00 45.23  ? 23  PHE A N     1 
ATOM   177  C CA    . PHE A 1 28  ? 1.076   16.193 14.511  1.00 44.62  ? 23  PHE A CA    1 
ATOM   178  C C     . PHE A 1 28  ? 1.173   17.475 13.700  1.00 47.00  ? 23  PHE A C     1 
ATOM   179  O O     . PHE A 1 28  ? 1.873   17.528 12.683  1.00 46.67  ? 23  PHE A O     1 
ATOM   180  C CB    . PHE A 1 28  ? 2.230   16.127 15.531  1.00 44.04  ? 23  PHE A CB    1 
ATOM   181  C CG    . PHE A 1 28  ? 3.601   16.290 14.927  1.00 44.96  ? 23  PHE A CG    1 
ATOM   182  C CD1   . PHE A 1 28  ? 4.284   15.192 14.435  1.00 43.68  ? 23  PHE A CD1   1 
ATOM   183  C CD2   . PHE A 1 28  ? 4.210   17.536 14.857  1.00 47.02  ? 23  PHE A CD2   1 
ATOM   184  C CE1   . PHE A 1 28  ? 5.547   15.328 13.882  1.00 42.25  ? 23  PHE A CE1   1 
ATOM   185  C CE2   . PHE A 1 28  ? 5.474   17.679 14.306  1.00 47.18  ? 23  PHE A CE2   1 
ATOM   186  C CZ    . PHE A 1 28  ? 6.140   16.574 13.818  1.00 46.77  ? 23  PHE A CZ    1 
ATOM   187  N N     . ARG A 1 29  ? 0.468   18.504 14.165  1.00 49.21  ? 24  ARG A N     1 
ATOM   188  C CA    . ARG A 1 29  ? 0.482   19.824 13.557  1.00 45.41  ? 24  ARG A CA    1 
ATOM   189  C C     . ARG A 1 29  ? 1.323   20.777 14.396  1.00 50.19  ? 24  ARG A C     1 
ATOM   190  O O     . ARG A 1 29  ? 1.441   20.619 15.614  1.00 52.97  ? 24  ARG A O     1 
ATOM   191  C CB    . ARG A 1 29  ? -0.938  20.378 13.406  1.00 46.31  ? 24  ARG A CB    1 
ATOM   192  C CG    . ARG A 1 29  ? -1.910  19.428 12.727  1.00 48.32  ? 24  ARG A CG    1 
ATOM   193  C CD    . ARG A 1 29  ? -3.202  20.133 12.344  1.00 54.14  ? 24  ARG A CD    1 
ATOM   194  N NE    . ARG A 1 29  ? -4.257  19.909 13.326  1.00 67.31  ? 24  ARG A NE    1 
ATOM   195  C CZ    . ARG A 1 29  ? -5.388  19.263 13.078  1.00 70.21  ? 24  ARG A CZ    1 
ATOM   196  N NH1   . ARG A 1 29  ? -5.653  18.765 11.881  1.00 58.71  ? 24  ARG A NH1   1 
ATOM   197  N NH2   . ARG A 1 29  ? -6.277  19.111 14.056  1.00 69.93  ? 24  ARG A NH2   1 
ATOM   198  N N     . THR A 1 30  ? 1.913   21.763 13.729  1.00 50.61  ? 25  THR A N     1 
ATOM   199  C CA    . THR A 1 30  ? 2.753   22.764 14.368  1.00 46.95  ? 25  THR A CA    1 
ATOM   200  C C     . THR A 1 30  ? 2.340   24.145 13.878  1.00 47.05  ? 25  THR A C     1 
ATOM   201  O O     . THR A 1 30  ? 1.424   24.294 13.065  1.00 49.98  ? 25  THR A O     1 
ATOM   202  C CB    . THR A 1 30  ? 4.240   22.530 14.070  1.00 47.38  ? 25  THR A CB    1 
ATOM   203  O OG1   . THR A 1 30  ? 4.464   22.621 12.656  1.00 49.80  ? 25  THR A OG1   1 
ATOM   204  C CG2   . THR A 1 30  ? 4.686   21.165 14.562  1.00 46.81  ? 25  THR A CG2   1 
ATOM   205  N N     . THR A 1 31  ? 3.025   25.163 14.388  1.00 47.68  ? 26  THR A N     1 
ATOM   206  C CA    . THR A 1 31  ? 2.897   26.497 13.831  1.00 47.02  ? 26  THR A CA    1 
ATOM   207  C C     . THR A 1 31  ? 3.647   26.576 12.506  1.00 49.20  ? 26  THR A C     1 
ATOM   208  O O     . THR A 1 31  ? 4.511   25.750 12.199  1.00 52.86  ? 26  THR A O     1 
ATOM   209  C CB    . THR A 1 31  ? 3.437   27.549 14.802  1.00 48.50  ? 26  THR A CB    1 
ATOM   210  O OG1   . THR A 1 31  ? 4.812   27.268 15.094  1.00 48.57  ? 26  THR A OG1   1 
ATOM   211  C CG2   . THR A 1 31  ? 2.640   27.535 16.097  1.00 49.66  ? 26  THR A CG2   1 
ATOM   212  N N     . ARG A 1 32  ? 3.303   27.584 11.713  1.00 46.84  ? 27  ARG A N     1 
ATOM   213  C CA    . ARG A 1 32  ? 3.946   27.825 10.428  1.00 47.45  ? 27  ARG A CA    1 
ATOM   214  C C     . ARG A 1 32  ? 4.533   29.226 10.442  1.00 53.79  ? 27  ARG A C     1 
ATOM   215  O O     . ARG A 1 32  ? 3.810   30.203 10.666  1.00 58.18  ? 27  ARG A O     1 
ATOM   216  C CB    . ARG A 1 32  ? 2.955   27.658 9.276   1.00 46.59  ? 27  ARG A CB    1 
ATOM   217  C CG    . ARG A 1 32  ? 3.535   27.922 7.899   1.00 43.05  ? 27  ARG A CG    1 
ATOM   218  C CD    . ARG A 1 32  ? 2.450   27.868 6.836   1.00 45.30  ? 27  ARG A CD    1 
ATOM   219  N NE    . ARG A 1 32  ? 2.965   28.191 5.511   1.00 45.97  ? 27  ARG A NE    1 
ATOM   220  C CZ    . ARG A 1 32  ? 2.229   28.220 4.409   1.00 49.61  ? 27  ARG A CZ    1 
ATOM   221  N NH1   . ARG A 1 32  ? 0.935   27.944 4.434   1.00 50.67  ? 27  ARG A NH1   1 
ATOM   222  N NH2   . ARG A 1 32  ? 2.806   28.529 3.251   1.00 51.66  ? 27  ARG A NH2   1 
ATOM   223  N N     . ASP A 1 33  ? 5.838   29.318 10.215  1.00 55.77  ? 28  ASP A N     1 
ATOM   224  C CA    . ASP A 1 33  ? 6.498   30.612 10.187  1.00 56.80  ? 28  ASP A CA    1 
ATOM   225  C C     . ASP A 1 33  ? 5.884   31.482 9.092   1.00 53.41  ? 28  ASP A C     1 
ATOM   226  O O     . ASP A 1 33  ? 5.553   30.976 8.013   1.00 52.36  ? 28  ASP A O     1 
ATOM   227  C CB    . ASP A 1 33  ? 7.999   30.439 9.945   1.00 59.79  ? 28  ASP A CB    1 
ATOM   228  C CG    . ASP A 1 33  ? 8.786   31.701 10.239  1.00 53.97  ? 28  ASP A CG    1 
ATOM   229  O OD1   . ASP A 1 33  ? 8.973   32.021 11.431  1.00 55.29  ? 28  ASP A OD1   1 
ATOM   230  O OD2   . ASP A 1 33  ? 9.219   32.371 9.278   1.00 53.69  ? 28  ASP A OD2   1 
ATOM   231  N N     . PRO A 1 34  ? 5.699   32.782 9.339   1.00 58.35  ? 29  PRO A N     1 
ATOM   232  C CA    . PRO A 1 34  ? 5.133   33.649 8.292   1.00 52.99  ? 29  PRO A CA    1 
ATOM   233  C C     . PRO A 1 34  ? 5.930   33.639 7.001   1.00 53.88  ? 29  PRO A C     1 
ATOM   234  O O     . PRO A 1 34  ? 5.347   33.813 5.922   1.00 53.96  ? 29  PRO A O     1 
ATOM   235  C CB    . PRO A 1 34  ? 5.139   35.037 8.948   1.00 50.81  ? 29  PRO A CB    1 
ATOM   236  C CG    . PRO A 1 34  ? 5.093   34.760 10.413  1.00 47.90  ? 29  PRO A CG    1 
ATOM   237  C CD    . PRO A 1 34  ? 5.872   33.492 10.618  1.00 53.59  ? 29  PRO A CD    1 
ATOM   238  N N     . GLY A 1 35  ? 7.244   33.430 7.075   1.00 55.24  ? 30  GLY A N     1 
ATOM   239  C CA    . GLY A 1 35  ? 8.070   33.390 5.886   1.00 53.61  ? 30  GLY A CA    1 
ATOM   240  C C     . GLY A 1 35  ? 8.235   32.031 5.249   1.00 57.85  ? 30  GLY A C     1 
ATOM   241  O O     . GLY A 1 35  ? 8.845   31.931 4.181   1.00 59.13  ? 30  GLY A O     1 
ATOM   242  N N     . PHE A 1 36  ? 7.711   30.978 5.874   1.00 58.21  ? 31  PHE A N     1 
ATOM   243  C CA    . PHE A 1 36  ? 7.815   29.634 5.320   1.00 54.61  ? 31  PHE A CA    1 
ATOM   244  C C     . PHE A 1 36  ? 6.816   29.475 4.181   1.00 50.71  ? 31  PHE A C     1 
ATOM   245  O O     . PHE A 1 36  ? 5.604   29.598 4.385   1.00 50.03  ? 31  PHE A O     1 
ATOM   246  C CB    . PHE A 1 36  ? 7.574   28.578 6.397   1.00 49.14  ? 31  PHE A CB    1 
ATOM   247  C CG    . PHE A 1 36  ? 7.842   27.173 5.934   1.00 50.95  ? 31  PHE A CG    1 
ATOM   248  C CD1   . PHE A 1 36  ? 9.140   26.723 5.759   1.00 48.72  ? 31  PHE A CD1   1 
ATOM   249  C CD2   . PHE A 1 36  ? 6.796   26.309 5.654   1.00 47.70  ? 31  PHE A CD2   1 
ATOM   250  C CE1   . PHE A 1 36  ? 9.391   25.434 5.325   1.00 51.06  ? 31  PHE A CE1   1 
ATOM   251  C CE2   . PHE A 1 36  ? 7.040   25.018 5.218   1.00 49.05  ? 31  PHE A CE2   1 
ATOM   252  C CZ    . PHE A 1 36  ? 8.340   24.581 5.054   1.00 49.16  ? 31  PHE A CZ    1 
ATOM   253  N N     . ARG A 1 37  ? 7.326   29.202 2.983   1.00 50.51  ? 32  ARG A N     1 
ATOM   254  C CA    . ARG A 1 37  ? 6.508   29.030 1.793   1.00 49.48  ? 32  ARG A CA    1 
ATOM   255  C C     . ARG A 1 37  ? 6.923   27.761 1.065   1.00 48.04  ? 32  ARG A C     1 
ATOM   256  O O     . ARG A 1 37  ? 8.113   27.451 0.971   1.00 47.18  ? 32  ARG A O     1 
ATOM   257  C CB    . ARG A 1 37  ? 6.634   30.234 0.862   1.00 54.49  ? 32  ARG A CB    1 
ATOM   258  C CG    . ARG A 1 37  ? 6.268   31.556 1.510   1.00 62.28  ? 32  ARG A CG    1 
ATOM   259  C CD    . ARG A 1 37  ? 4.920   32.049 1.015   1.00 73.62  ? 32  ARG A CD    1 
ATOM   260  N NE    . ARG A 1 37  ? 4.641   31.593 -0.342  1.00 82.74  ? 32  ARG A NE    1 
ATOM   261  C CZ    . ARG A 1 37  ? 5.159   32.126 -1.440  1.00 92.24  ? 32  ARG A CZ    1 
ATOM   262  N NH1   . ARG A 1 37  ? 6.031   33.118 -1.381  1.00 90.93  ? 32  ARG A NH1   1 
ATOM   263  N NH2   . ARG A 1 37  ? 4.800   31.645 -2.627  1.00 91.64  ? 32  ARG A NH2   1 
ATOM   264  N N     . PHE A 1 38  ? 5.934   27.037 0.545   1.00 44.01  ? 33  PHE A N     1 
ATOM   265  C CA    . PHE A 1 38  ? 6.189   25.777 -0.134  1.00 42.79  ? 33  PHE A CA    1 
ATOM   266  C C     . PHE A 1 38  ? 5.103   25.540 -1.172  1.00 46.39  ? 33  PHE A C     1 
ATOM   267  O O     . PHE A 1 38  ? 4.033   26.154 -1.134  1.00 48.02  ? 33  PHE A O     1 
ATOM   268  C CB    . PHE A 1 38  ? 6.245   24.606 0.858   1.00 47.00  ? 33  PHE A CB    1 
ATOM   269  C CG    . PHE A 1 38  ? 4.914   24.261 1.466   1.00 43.38  ? 33  PHE A CG    1 
ATOM   270  C CD1   . PHE A 1 38  ? 4.459   24.926 2.593   1.00 41.59  ? 33  PHE A CD1   1 
ATOM   271  C CD2   . PHE A 1 38  ? 4.121   23.265 0.918   1.00 43.99  ? 33  PHE A CD2   1 
ATOM   272  C CE1   . PHE A 1 38  ? 3.237   24.610 3.155   1.00 39.45  ? 33  PHE A CE1   1 
ATOM   273  C CE2   . PHE A 1 38  ? 2.900   22.946 1.474   1.00 42.61  ? 33  PHE A CE2   1 
ATOM   274  C CZ    . PHE A 1 38  ? 2.457   23.619 2.594   1.00 44.92  ? 33  PHE A CZ    1 
ATOM   275  N N     . GLN A 1 39  ? 5.397   24.643 -2.105  1.00 51.07  ? 34  GLN A N     1 
ATOM   276  C CA    . GLN A 1 39  ? 4.421   24.158 -3.065  1.00 46.27  ? 34  GLN A CA    1 
ATOM   277  C C     . GLN A 1 39  ? 3.928   22.783 -2.633  1.00 44.90  ? 34  GLN A C     1 
ATOM   278  O O     . GLN A 1 39  ? 4.646   22.028 -1.971  1.00 44.75  ? 34  GLN A O     1 
ATOM   279  C CB    . GLN A 1 39  ? 5.019   24.082 -4.471  1.00 46.78  ? 34  GLN A CB    1 
ATOM   280  C CG    . GLN A 1 39  ? 5.813   25.311 -4.880  1.00 46.86  ? 34  GLN A CG    1 
ATOM   281  C CD    . GLN A 1 39  ? 6.481   25.143 -6.230  1.00 51.10  ? 34  GLN A CD    1 
ATOM   282  O OE1   . GLN A 1 39  ? 5.814   24.943 -7.244  1.00 58.11  ? 34  GLN A OE1   1 
ATOM   283  N NE2   . GLN A 1 39  ? 7.807   25.225 -6.249  1.00 47.52  ? 34  GLN A NE2   1 
ATOM   284  N N     . SER A 1 40  ? 2.690   22.467 -3.006  1.00 44.05  ? 35  SER A N     1 
ATOM   285  C CA    . SER A 1 40  ? 2.101   21.195 -2.611  1.00 42.21  ? 35  SER A CA    1 
ATOM   286  C C     . SER A 1 40  ? 2.874   20.035 -3.225  1.00 44.66  ? 35  SER A C     1 
ATOM   287  O O     . SER A 1 40  ? 3.078   19.976 -4.441  1.00 47.66  ? 35  SER A O     1 
ATOM   288  C CB    . SER A 1 40  ? 0.632   21.135 -3.027  1.00 44.92  ? 35  SER A CB    1 
ATOM   289  O OG    . SER A 1 40  ? -0.061  22.302 -2.629  1.00 48.82  ? 35  SER A OG    1 
ATOM   290  N N     . GLY A 1 41  ? 3.308   19.113 -2.367  1.00 44.27  ? 36  GLY A N     1 
ATOM   291  C CA    . GLY A 1 41  ? 4.090   17.963 -2.775  1.00 44.34  ? 36  GLY A CA    1 
ATOM   292  C C     . GLY A 1 41  ? 5.552   18.017 -2.390  1.00 43.60  ? 36  GLY A C     1 
ATOM   293  O O     . GLY A 1 41  ? 6.280   17.056 -2.664  1.00 48.51  ? 36  GLY A O     1 
ATOM   294  N N     . GLN A 1 42  ? 6.008   19.099 -1.772  1.00 47.93  ? 37  GLN A N     1 
ATOM   295  C CA    . GLN A 1 42  ? 7.401   19.252 -1.390  1.00 48.87  ? 37  GLN A CA    1 
ATOM   296  C C     . GLN A 1 42  ? 7.629   18.728 0.021   1.00 45.88  ? 37  GLN A C     1 
ATOM   297  O O     . GLN A 1 42  ? 6.695   18.531 0.801   1.00 48.00  ? 37  GLN A O     1 
ATOM   298  C CB    . GLN A 1 42  ? 7.823   20.718 -1.474  1.00 45.61  ? 37  GLN A CB    1 
ATOM   299  C CG    . GLN A 1 42  ? 7.935   21.243 -2.887  1.00 43.37  ? 37  GLN A CG    1 
ATOM   300  C CD    . GLN A 1 42  ? 8.444   22.667 -2.935  1.00 42.87  ? 37  GLN A CD    1 
ATOM   301  O OE1   . GLN A 1 42  ? 7.948   23.541 -2.223  1.00 48.71  ? 37  GLN A OE1   1 
ATOM   302  N NE2   . GLN A 1 42  ? 9.435   22.910 -3.781  1.00 42.87  ? 37  GLN A NE2   1 
ATOM   303  N N     . PHE A 1 43  ? 8.894   18.504 0.341   1.00 43.86  ? 38  PHE A N     1 
ATOM   304  C CA    . PHE A 1 43  ? 9.299   18.093 1.672   1.00 45.61  ? 38  PHE A CA    1 
ATOM   305  C C     . PHE A 1 43  ? 10.356  19.061 2.192   1.00 48.98  ? 38  PHE A C     1 
ATOM   306  O O     . PHE A 1 43  ? 10.867  19.914 1.460   1.00 51.25  ? 38  PHE A O     1 
ATOM   307  C CB    . PHE A 1 43  ? 9.820   16.646 1.671   1.00 48.17  ? 38  PHE A CB    1 
ATOM   308  C CG    . PHE A 1 43  ? 11.071  16.442 0.858   1.00 49.77  ? 38  PHE A CG    1 
ATOM   309  C CD1   . PHE A 1 43  ? 12.322  16.603 1.436   1.00 48.99  ? 38  PHE A CD1   1 
ATOM   310  C CD2   . PHE A 1 43  ? 11.000  16.052 -0.469  1.00 56.49  ? 38  PHE A CD2   1 
ATOM   311  C CE1   . PHE A 1 43  ? 13.477  16.415 0.696   1.00 47.29  ? 38  PHE A CE1   1 
ATOM   312  C CE2   . PHE A 1 43  ? 12.150  15.860 -1.213  1.00 54.48  ? 38  PHE A CE2   1 
ATOM   313  C CZ    . PHE A 1 43  ? 13.387  16.039 -0.631  1.00 48.99  ? 38  PHE A CZ    1 
ATOM   314  N N     . ILE A 1 44  ? 10.681  18.928 3.478   1.00 51.72  ? 39  ILE A N     1 
ATOM   315  C CA    . ILE A 1 44  ? 11.680  19.755 4.147   1.00 46.08  ? 39  ILE A CA    1 
ATOM   316  C C     . ILE A 1 44  ? 12.451  18.881 5.129   1.00 50.89  ? 39  ILE A C     1 
ATOM   317  O O     . ILE A 1 44  ? 12.149  17.699 5.311   1.00 54.08  ? 39  ILE A O     1 
ATOM   318  C CB    . ILE A 1 44  ? 11.056  20.973 4.868   1.00 44.87  ? 39  ILE A CB    1 
ATOM   319  C CG1   . ILE A 1 44  ? 9.703   20.624 5.503   1.00 45.34  ? 39  ILE A CG1   1 
ATOM   320  C CG2   . ILE A 1 44  ? 10.912  22.157 3.918   1.00 49.07  ? 39  ILE A CG2   1 
ATOM   321  C CD1   . ILE A 1 44  ? 9.791   19.798 6.768   1.00 47.25  ? 39  ILE A CD1   1 
ATOM   322  N N     . MET A 1 45  ? 13.453  19.474 5.774   1.00 52.16  ? 40  MET A N     1 
ATOM   323  C CA    . MET A 1 45  ? 14.199  18.803 6.833   1.00 46.74  ? 40  MET A CA    1 
ATOM   324  C C     . MET A 1 45  ? 13.548  19.144 8.168   1.00 51.64  ? 40  MET A C     1 
ATOM   325  O O     . MET A 1 45  ? 13.628  20.285 8.633   1.00 55.15  ? 40  MET A O     1 
ATOM   326  C CB    . MET A 1 45  ? 15.671  19.211 6.815   1.00 52.23  ? 40  MET A CB    1 
ATOM   327  C CG    . MET A 1 45  ? 16.464  18.641 5.649   1.00 53.13  ? 40  MET A CG    1 
ATOM   328  S SD    . MET A 1 45  ? 15.965  16.961 5.223   1.00 63.96  ? 40  MET A SD    1 
ATOM   329  C CE    . MET A 1 45  ? 17.053  15.999 6.271   1.00 46.94  ? 40  MET A CE    1 
ATOM   330  N N     . MET A 1 46  ? 12.901  18.157 8.779   1.00 52.04  ? 41  MET A N     1 
ATOM   331  C CA    . MET A 1 46  ? 12.188  18.328 10.036  1.00 48.25  ? 41  MET A CA    1 
ATOM   332  C C     . MET A 1 46  ? 12.826  17.445 11.097  1.00 49.77  ? 41  MET A C     1 
ATOM   333  O O     . MET A 1 46  ? 13.247  16.320 10.809  1.00 54.10  ? 41  MET A O     1 
ATOM   334  C CB    . MET A 1 46  ? 10.698  17.989 9.875   1.00 50.94  ? 41  MET A CB    1 
ATOM   335  C CG    . MET A 1 46  ? 9.815   18.335 11.073  1.00 47.67  ? 41  MET A CG    1 
ATOM   336  S SD    . MET A 1 46  ? 9.840   17.088 12.375  1.00 50.56  ? 41  MET A SD    1 
ATOM   337  C CE    . MET A 1 46  ? 8.759   15.854 11.654  1.00 42.89  ? 41  MET A CE    1 
ATOM   338  N N     . GLY A 1 47  ? 12.898  17.959 12.322  1.00 50.38  ? 42  GLY A N     1 
ATOM   339  C CA    . GLY A 1 47  ? 13.493  17.205 13.406  1.00 46.77  ? 42  GLY A CA    1 
ATOM   340  C C     . GLY A 1 47  ? 13.522  17.936 14.732  1.00 46.88  ? 42  GLY A C     1 
ATOM   341  O O     . GLY A 1 47  ? 12.593  18.679 15.062  1.00 48.04  ? 42  GLY A O     1 
ATOM   342  N N     . LEU A 1 48  ? 14.590  17.734 15.499  1.00 51.66  ? 43  LEU A N     1 
ATOM   343  C CA    . LEU A 1 48  ? 14.714  18.276 16.843  1.00 53.26  ? 43  LEU A CA    1 
ATOM   344  C C     . LEU A 1 48  ? 16.076  18.938 17.008  1.00 58.71  ? 43  LEU A C     1 
ATOM   345  O O     . LEU A 1 48  ? 16.986  18.760 16.194  1.00 61.27  ? 43  LEU A O     1 
ATOM   346  C CB    . LEU A 1 48  ? 14.529  17.181 17.905  1.00 50.46  ? 43  LEU A CB    1 
ATOM   347  C CG    . LEU A 1 48  ? 13.178  16.467 17.953  1.00 47.64  ? 43  LEU A CG    1 
ATOM   348  C CD1   . LEU A 1 48  ? 13.299  15.139 18.685  1.00 47.24  ? 43  LEU A CD1   1 
ATOM   349  C CD2   . LEU A 1 48  ? 12.130  17.347 18.613  1.00 44.69  ? 43  LEU A CD2   1 
ATOM   350  N N     . GLU A 1 49  ? 16.204  19.712 18.083  1.00 66.92  ? 44  GLU A N     1 
ATOM   351  C CA    . GLU A 1 49  ? 17.468  20.324 18.478  1.00 67.76  ? 44  GLU A CA    1 
ATOM   352  C C     . GLU A 1 49  ? 18.070  19.471 19.590  1.00 70.13  ? 44  GLU A C     1 
ATOM   353  O O     . GLU A 1 49  ? 17.605  19.512 20.734  1.00 71.88  ? 44  GLU A O     1 
ATOM   354  C CB    . GLU A 1 49  ? 17.257  21.763 18.941  1.00 71.15  ? 44  GLU A CB    1 
ATOM   355  C CG    . GLU A 1 49  ? 18.534  22.486 19.346  1.00 81.67  ? 44  GLU A CG    1 
ATOM   356  C CD    . GLU A 1 49  ? 19.125  23.309 18.218  1.00 88.04  ? 44  GLU A CD    1 
ATOM   357  O OE1   . GLU A 1 49  ? 18.423  24.209 17.710  1.00 88.28  ? 44  GLU A OE1   1 
ATOM   358  O OE2   . GLU A 1 49  ? 20.288  23.056 17.839  1.00 90.14  ? 44  GLU A OE2   1 
ATOM   359  N N     . VAL A 1 50  ? 19.100  18.699 19.255  1.00 70.92  ? 45  VAL A N     1 
ATOM   360  C CA    . VAL A 1 50  ? 19.697  17.732 20.171  1.00 70.40  ? 45  VAL A CA    1 
ATOM   361  C C     . VAL A 1 50  ? 21.129  18.160 20.463  1.00 76.56  ? 45  VAL A C     1 
ATOM   362  O O     . VAL A 1 50  ? 21.974  18.172 19.558  1.00 74.40  ? 45  VAL A O     1 
ATOM   363  C CB    . VAL A 1 50  ? 19.661  16.308 19.596  1.00 65.25  ? 45  VAL A CB    1 
ATOM   364  C CG1   . VAL A 1 50  ? 20.407  15.345 20.506  1.00 69.99  ? 45  VAL A CG1   1 
ATOM   365  C CG2   . VAL A 1 50  ? 18.222  15.854 19.389  1.00 59.81  ? 45  VAL A CG2   1 
ATOM   366  N N     . ASN A 1 51  ? 21.397  18.505 21.725  1.00 80.20  ? 46  ASN A N     1 
ATOM   367  C CA    . ASN A 1 51  ? 22.737  18.882 22.183  1.00 80.39  ? 46  ASN A CA    1 
ATOM   368  C C     . ASN A 1 51  ? 23.296  20.052 21.376  1.00 80.03  ? 46  ASN A C     1 
ATOM   369  O O     . ASN A 1 51  ? 24.484  20.095 21.049  1.00 82.41  ? 46  ASN A O     1 
ATOM   370  C CB    . ASN A 1 51  ? 23.692  17.686 22.144  1.00 82.70  ? 46  ASN A CB    1 
ATOM   371  C CG    . ASN A 1 51  ? 23.465  16.720 23.292  1.00 81.74  ? 46  ASN A CG    1 
ATOM   372  O OD1   . ASN A 1 51  ? 23.623  15.509 23.139  1.00 81.34  ? 46  ASN A OD1   1 
ATOM   373  N ND2   . ASN A 1 51  ? 23.096  17.253 24.451  1.00 82.02  ? 46  ASN A ND2   1 
ATOM   374  N N     . GLY A 1 52  ? 22.433  21.014 21.057  1.00 82.21  ? 47  GLY A N     1 
ATOM   375  C CA    . GLY A 1 52  ? 22.841  22.156 20.265  1.00 87.44  ? 47  GLY A CA    1 
ATOM   376  C C     . GLY A 1 52  ? 23.138  21.858 18.814  1.00 86.85  ? 47  GLY A C     1 
ATOM   377  O O     . GLY A 1 52  ? 23.732  22.700 18.135  1.00 86.13  ? 47  GLY A O     1 
ATOM   378  N N     . LYS A 1 53  ? 22.756  20.683 18.322  1.00 85.72  ? 48  LYS A N     1 
ATOM   379  C CA    . LYS A 1 53  ? 22.941  20.295 16.933  1.00 82.03  ? 48  LYS A CA    1 
ATOM   380  C C     . LYS A 1 53  ? 21.630  19.774 16.367  1.00 77.48  ? 48  LYS A C     1 
ATOM   381  O O     . LYS A 1 53  ? 20.838  19.159 17.088  1.00 76.80  ? 48  LYS A O     1 
ATOM   382  C CB    . LYS A 1 53  ? 24.027  19.218 16.789  1.00 82.63  ? 48  LYS A CB    1 
ATOM   383  C CG    . LYS A 1 53  ? 25.126  19.287 17.838  1.00 87.73  ? 48  LYS A CG    1 
ATOM   384  C CD    . LYS A 1 53  ? 26.087  18.116 17.713  1.00 82.13  ? 48  LYS A CD    1 
ATOM   385  C CE    . LYS A 1 53  ? 26.720  17.780 19.052  1.00 81.30  ? 48  LYS A CE    1 
ATOM   386  N NZ    . LYS A 1 53  ? 28.147  18.200 19.111  1.00 85.06  ? 48  LYS A NZ    1 
ATOM   387  N N     . PRO A 1 54  ? 21.372  20.004 15.078  1.00 76.91  ? 49  PRO A N     1 
ATOM   388  C CA    . PRO A 1 54  ? 20.091  19.583 14.495  1.00 71.19  ? 49  PRO A CA    1 
ATOM   389  C C     . PRO A 1 54  ? 20.086  18.098 14.155  1.00 63.33  ? 49  PRO A C     1 
ATOM   390  O O     . PRO A 1 54  ? 20.983  17.597 13.473  1.00 66.11  ? 49  PRO A O     1 
ATOM   391  C CB    . PRO A 1 54  ? 19.978  20.445 13.232  1.00 67.72  ? 49  PRO A CB    1 
ATOM   392  C CG    . PRO A 1 54  ? 21.391  20.705 12.840  1.00 70.25  ? 49  PRO A CG    1 
ATOM   393  C CD    . PRO A 1 54  ? 22.193  20.769 14.120  1.00 76.03  ? 49  PRO A CD    1 
ATOM   394  N N     . LEU A 1 55  ? 19.066  17.397 14.639  1.00 55.27  ? 50  LEU A N     1 
ATOM   395  C CA    . LEU A 1 55  ? 18.782  16.019 14.245  1.00 53.63  ? 50  LEU A CA    1 
ATOM   396  C C     . LEU A 1 55  ? 17.502  16.066 13.418  1.00 56.75  ? 50  LEU A C     1 
ATOM   397  O O     . LEU A 1 55  ? 16.404  16.202 13.965  1.00 56.68  ? 50  LEU A O     1 
ATOM   398  C CB    . LEU A 1 55  ? 18.642  15.106 15.461  1.00 51.03  ? 50  LEU A CB    1 
ATOM   399  C CG    . LEU A 1 55  ? 17.931  13.767 15.238  1.00 52.62  ? 50  LEU A CG    1 
ATOM   400  C CD1   . LEU A 1 55  ? 18.896  12.718 14.707  1.00 48.35  ? 50  LEU A CD1   1 
ATOM   401  C CD2   . LEU A 1 55  ? 17.264  13.287 16.518  1.00 57.95  ? 50  LEU A CD2   1 
ATOM   402  N N     . THR A 1 56  ? 17.647  15.972 12.099  1.00 53.90  ? 51  THR A N     1 
ATOM   403  C CA    . THR A 1 56  ? 16.531  16.141 11.181  1.00 48.74  ? 51  THR A CA    1 
ATOM   404  C C     . THR A 1 56  ? 16.458  14.974 10.210  1.00 53.27  ? 51  THR A C     1 
ATOM   405  O O     . THR A 1 56  ? 17.462  14.320 9.916   1.00 55.86  ? 51  THR A O     1 
ATOM   406  C CB    . THR A 1 56  ? 16.646  17.450 10.382  1.00 45.50  ? 51  THR A CB    1 
ATOM   407  O OG1   . THR A 1 56  ? 17.878  17.459 9.650   1.00 52.55  ? 51  THR A OG1   1 
ATOM   408  C CG2   . THR A 1 56  ? 16.603  18.650 11.310  1.00 48.34  ? 51  THR A CG2   1 
ATOM   409  N N     . ARG A 1 57  ? 15.248  14.724 9.716   1.00 52.71  ? 52  ARG A N     1 
ATOM   410  C CA    . ARG A 1 57  ? 15.002  13.763 8.653   1.00 49.26  ? 52  ARG A CA    1 
ATOM   411  C C     . ARG A 1 57  ? 14.044  14.383 7.646   1.00 50.68  ? 52  ARG A C     1 
ATOM   412  O O     . ARG A 1 57  ? 13.282  15.299 7.965   1.00 56.78  ? 52  ARG A O     1 
ATOM   413  C CB    . ARG A 1 57  ? 14.425  12.446 9.192   1.00 54.70  ? 52  ARG A CB    1 
ATOM   414  C CG    . ARG A 1 57  ? 15.338  11.709 10.161  1.00 60.81  ? 52  ARG A CG    1 
ATOM   415  C CD    . ARG A 1 57  ? 16.324  10.812 9.432   1.00 62.60  ? 52  ARG A CD    1 
ATOM   416  N NE    . ARG A 1 57  ? 17.096  9.988  10.355  1.00 62.43  ? 52  ARG A NE    1 
ATOM   417  C CZ    . ARG A 1 57  ? 18.112  10.429 11.086  1.00 60.81  ? 52  ARG A CZ    1 
ATOM   418  N NH1   . ARG A 1 57  ? 18.513  11.688 11.026  1.00 59.99  ? 52  ARG A NH1   1 
ATOM   419  N NH2   . ARG A 1 57  ? 18.742  9.584  11.897  1.00 63.21  ? 52  ARG A NH2   1 
ATOM   420  N N     . ALA A 1 58  ? 14.096  13.876 6.417   1.00 53.13  ? 53  ALA A N     1 
ATOM   421  C CA    . ALA A 1 58  ? 13.235  14.389 5.359   1.00 51.14  ? 53  ALA A CA    1 
ATOM   422  C C     . ALA A 1 58  ? 11.775  14.090 5.675   1.00 47.30  ? 53  ALA A C     1 
ATOM   423  O O     . ALA A 1 58  ? 11.423  12.960 6.025   1.00 52.30  ? 53  ALA A O     1 
ATOM   424  C CB    . ALA A 1 58  ? 13.625  13.780 4.014   1.00 48.84  ? 53  ALA A CB    1 
ATOM   425  N N     . TYR A 1 59  ? 10.923  15.107 5.553   1.00 47.14  ? 54  TYR A N     1 
ATOM   426  C CA    . TYR A 1 59  ? 9.508   14.976 5.884   1.00 49.15  ? 54  TYR A CA    1 
ATOM   427  C C     . TYR A 1 59  ? 8.677   15.762 4.884   1.00 46.90  ? 54  TYR A C     1 
ATOM   428  O O     . TYR A 1 59  ? 8.871   16.972 4.729   1.00 48.34  ? 54  TYR A O     1 
ATOM   429  C CB    . TYR A 1 59  ? 9.223   15.466 7.306   1.00 48.39  ? 54  TYR A CB    1 
ATOM   430  C CG    . TYR A 1 59  ? 9.220   14.368 8.339   1.00 49.63  ? 54  TYR A CG    1 
ATOM   431  C CD1   . TYR A 1 59  ? 8.057   13.664 8.625   1.00 48.76  ? 54  TYR A CD1   1 
ATOM   432  C CD2   . TYR A 1 59  ? 10.379  14.025 9.019   1.00 51.08  ? 54  TYR A CD2   1 
ATOM   433  C CE1   . TYR A 1 59  ? 8.048   12.657 9.567   1.00 49.14  ? 54  TYR A CE1   1 
ATOM   434  C CE2   . TYR A 1 59  ? 10.379  13.021 9.966   1.00 48.76  ? 54  TYR A CE2   1 
ATOM   435  C CZ    . TYR A 1 59  ? 9.211   12.338 10.234  1.00 48.74  ? 54  TYR A CZ    1 
ATOM   436  O OH    . TYR A 1 59  ? 9.204   11.334 11.173  1.00 54.89  ? 54  TYR A OH    1 
ATOM   437  N N     . SER A 1 60  ? 7.746   15.079 4.224   1.00 43.57  ? 55  SER A N     1 
ATOM   438  C CA    . SER A 1 60  ? 6.802   15.755 3.348   1.00 42.43  ? 55  SER A CA    1 
ATOM   439  C C     . SER A 1 60  ? 5.868   16.637 4.165   1.00 46.07  ? 55  SER A C     1 
ATOM   440  O O     . SER A 1 60  ? 5.446   16.271 5.266   1.00 50.58  ? 55  SER A O     1 
ATOM   441  C CB    . SER A 1 60  ? 5.994   14.736 2.546   1.00 39.45  ? 55  SER A CB    1 
ATOM   442  O OG    . SER A 1 60  ? 6.805   14.077 1.588   1.00 45.08  ? 55  SER A OG    1 
ATOM   443  N N     . ILE A 1 61  ? 5.551   17.810 3.625   1.00 42.45  ? 56  ILE A N     1 
ATOM   444  C CA    . ILE A 1 61  ? 4.636   18.733 4.287   1.00 39.00  ? 56  ILE A CA    1 
ATOM   445  C C     . ILE A 1 61  ? 3.213   18.269 3.996   1.00 43.14  ? 56  ILE A C     1 
ATOM   446  O O     . ILE A 1 61  ? 2.736   18.373 2.864   1.00 47.50  ? 56  ILE A O     1 
ATOM   447  C CB    . ILE A 1 61  ? 4.855   20.178 3.828   1.00 40.39  ? 56  ILE A CB    1 
ATOM   448  C CG1   . ILE A 1 61  ? 6.298   20.610 4.098   1.00 42.65  ? 56  ILE A CG1   1 
ATOM   449  C CG2   . ILE A 1 61  ? 3.886   21.107 4.535   1.00 40.88  ? 56  ILE A CG2   1 
ATOM   450  C CD1   . ILE A 1 61  ? 6.827   21.624 3.109   1.00 45.07  ? 56  ILE A CD1   1 
ATOM   451  N N     . ALA A 1 62  ? 2.533   17.749 5.019   1.00 41.50  ? 57  ALA A N     1 
ATOM   452  C CA    . ALA A 1 62  ? 1.188   17.221 4.841   1.00 40.80  ? 57  ALA A CA    1 
ATOM   453  C C     . ALA A 1 62  ? 0.110   18.292 4.913   1.00 39.06  ? 57  ALA A C     1 
ATOM   454  O O     . ALA A 1 62  ? -1.030  18.025 4.517   1.00 42.48  ? 57  ALA A O     1 
ATOM   455  C CB    . ALA A 1 62  ? 0.905   16.138 5.886   1.00 41.68  ? 57  ALA A CB    1 
ATOM   456  N N     . SER A 1 63  ? 0.436   19.485 5.400   1.00 41.05  ? 58  SER A N     1 
ATOM   457  C CA    . SER A 1 63  ? -0.541  20.555 5.511   1.00 38.43  ? 58  SER A CA    1 
ATOM   458  C C     . SER A 1 63  ? -0.683  21.296 4.188   1.00 46.61  ? 58  SER A C     1 
ATOM   459  O O     . SER A 1 63  ? 0.245   21.350 3.374   1.00 47.77  ? 58  SER A O     1 
ATOM   460  C CB    . SER A 1 63  ? -0.136  21.545 6.600   1.00 41.12  ? 58  SER A CB    1 
ATOM   461  O OG    . SER A 1 63  ? 1.195   21.988 6.403   1.00 43.66  ? 58  SER A OG    1 
ATOM   462  N N     . SER A 1 64  ? -1.859  21.882 3.986   1.00 49.70  ? 59  SER A N     1 
ATOM   463  C CA    . SER A 1 64  ? -2.094  22.713 2.817   1.00 45.18  ? 59  SER A CA    1 
ATOM   464  C C     . SER A 1 64  ? -1.245  23.975 2.879   1.00 45.39  ? 59  SER A C     1 
ATOM   465  O O     . SER A 1 64  ? -0.954  24.504 3.956   1.00 48.91  ? 59  SER A O     1 
ATOM   466  C CB    . SER A 1 64  ? -3.574  23.083 2.721   1.00 43.98  ? 59  SER A CB    1 
ATOM   467  O OG    . SER A 1 64  ? -3.865  23.730 1.494   1.00 50.49  ? 59  SER A OG    1 
ATOM   468  N N     . LEU A 1 65  ? -0.841  24.459 1.703   1.00 51.12  ? 60  LEU A N     1 
ATOM   469  C CA    . LEU A 1 65  ? -0.137  25.734 1.644   1.00 48.65  ? 60  LEU A CA    1 
ATOM   470  C C     . LEU A 1 65  ? -1.027  26.909 2.027   1.00 49.27  ? 60  LEU A C     1 
ATOM   471  O O     . LEU A 1 65  ? -0.514  28.020 2.209   1.00 52.20  ? 60  LEU A O     1 
ATOM   472  C CB    . LEU A 1 65  ? 0.464   25.948 0.247   1.00 45.76  ? 60  LEU A CB    1 
ATOM   473  C CG    . LEU A 1 65  ? -0.439  26.009 -0.990  1.00 49.96  ? 60  LEU A CG    1 
ATOM   474  C CD1   . LEU A 1 65  ? -0.930  27.428 -1.256  1.00 52.75  ? 60  LEU A CD1   1 
ATOM   475  C CD2   . LEU A 1 65  ? 0.295   25.464 -2.207  1.00 49.63  ? 60  LEU A CD2   1 
ATOM   476  N N     . TYR A 1 66  ? -2.337  26.686 2.147   1.00 49.84  ? 61  TYR A N     1 
ATOM   477  C CA    . TYR A 1 66  ? -3.283  27.678 2.637   1.00 48.66  ? 61  TYR A CA    1 
ATOM   478  C C     . TYR A 1 66  ? -3.457  27.635 4.147   1.00 49.54  ? 61  TYR A C     1 
ATOM   479  O O     . TYR A 1 66  ? -4.185  28.470 4.696   1.00 50.19  ? 61  TYR A O     1 
ATOM   480  C CB    . TYR A 1 66  ? -4.652  27.472 1.982   1.00 49.83  ? 61  TYR A CB    1 
ATOM   481  C CG    . TYR A 1 66  ? -4.659  27.675 0.490   1.00 52.41  ? 61  TYR A CG    1 
ATOM   482  C CD1   . TYR A 1 66  ? -4.877  28.933 -0.051  1.00 53.99  ? 61  TYR A CD1   1 
ATOM   483  C CD2   . TYR A 1 66  ? -4.455  26.611 -0.378  1.00 52.76  ? 61  TYR A CD2   1 
ATOM   484  C CE1   . TYR A 1 66  ? -4.890  29.131 -1.414  1.00 61.18  ? 61  TYR A CE1   1 
ATOM   485  C CE2   . TYR A 1 66  ? -4.466  26.800 -1.743  1.00 58.15  ? 61  TYR A CE2   1 
ATOM   486  C CZ    . TYR A 1 66  ? -4.684  28.060 -2.255  1.00 61.09  ? 61  TYR A CZ    1 
ATOM   487  O OH    . TYR A 1 66  ? -4.694  28.244 -3.616  1.00 60.92  ? 61  TYR A OH    1 
ATOM   488  N N     . GLU A 1 67  ? -2.827  26.680 4.822   1.00 52.71  ? 62  GLU A N     1 
ATOM   489  C CA    . GLU A 1 67  ? -3.011  26.514 6.255   1.00 48.18  ? 62  GLU A CA    1 
ATOM   490  C C     . GLU A 1 67  ? -2.060  27.419 7.027   1.00 50.38  ? 62  GLU A C     1 
ATOM   491  O O     . GLU A 1 67  ? -0.872  27.506 6.701   1.00 48.42  ? 62  GLU A O     1 
ATOM   492  C CB    . GLU A 1 67  ? -2.786  25.055 6.653   1.00 46.53  ? 62  GLU A CB    1 
ATOM   493  C CG    . GLU A 1 67  ? -3.281  24.699 8.047   1.00 48.54  ? 62  GLU A CG    1 
ATOM   494  C CD    . GLU A 1 67  ? -4.790  24.667 8.138   1.00 58.11  ? 62  GLU A CD    1 
ATOM   495  O OE1   . GLU A 1 67  ? -5.432  24.301 7.135   1.00 56.39  ? 62  GLU A OE1   1 
ATOM   496  O OE2   . GLU A 1 67  ? -5.336  25.009 9.206   1.00 64.77  ? 62  GLU A OE2   1 
ATOM   497  N N     . ASP A 1 68  ? -2.586  28.093 8.051   1.00 52.66  ? 63  ASP A N     1 
ATOM   498  C CA    . ASP A 1 68  ? -1.757  28.835 9.001   1.00 53.48  ? 63  ASP A CA    1 
ATOM   499  C C     . ASP A 1 68  ? -1.163  27.865 10.026  1.00 52.12  ? 63  ASP A C     1 
ATOM   500  O O     . ASP A 1 68  ? -1.397  27.944 11.231  1.00 54.83  ? 63  ASP A O     1 
ATOM   501  C CB    . ASP A 1 68  ? -2.568  29.935 9.672   1.00 49.94  ? 63  ASP A CB    1 
ATOM   502  C CG    . ASP A 1 68  ? -1.716  30.841 10.539  1.00 55.87  ? 63  ASP A CG    1 
ATOM   503  O OD1   . ASP A 1 68  ? -0.524  31.026 10.216  1.00 55.29  ? 63  ASP A OD1   1 
ATOM   504  O OD2   . ASP A 1 68  ? -2.239  31.369 11.543  1.00 50.45  ? 63  ASP A OD2   1 
ATOM   505  N N     . GLY A 1 69  ? -0.383  26.923 9.506   1.00 48.07  ? 64  GLY A N     1 
ATOM   506  C CA    . GLY A 1 69  ? 0.175   25.854 10.305  1.00 45.72  ? 64  GLY A CA    1 
ATOM   507  C C     . GLY A 1 69  ? 0.769   24.769 9.433   1.00 45.16  ? 64  GLY A C     1 
ATOM   508  O O     . GLY A 1 69  ? 0.460   24.685 8.240   1.00 49.18  ? 64  GLY A O     1 
ATOM   509  N N     . LEU A 1 70  ? 1.632   23.943 10.010  1.00 44.15  ? 65  LEU A N     1 
ATOM   510  C CA    . LEU A 1 70  ? 2.231   22.816 9.315   1.00 44.47  ? 65  LEU A CA    1 
ATOM   511  C C     . LEU A 1 70  ? 1.646   21.516 9.850   1.00 43.30  ? 65  LEU A C     1 
ATOM   512  O O     . LEU A 1 70  ? 0.986   21.484 10.891  1.00 47.14  ? 65  LEU A O     1 
ATOM   513  C CB    . LEU A 1 70  ? 3.757   22.830 9.470   1.00 45.95  ? 65  LEU A CB    1 
ATOM   514  C CG    . LEU A 1 70  ? 4.480   24.005 8.807   1.00 45.77  ? 65  LEU A CG    1 
ATOM   515  C CD1   . LEU A 1 70  ? 5.969   23.975 9.120   1.00 46.67  ? 65  LEU A CD1   1 
ATOM   516  C CD2   . LEU A 1 70  ? 4.243   24.005 7.304   1.00 42.92  ? 65  LEU A CD2   1 
ATOM   517  N N     . GLU A 1 71  ? 1.888   20.433 9.115   1.00 43.44  ? 66  GLU A N     1 
ATOM   518  C CA    . GLU A 1 71  ? 1.392   19.122 9.509   1.00 38.95  ? 66  GLU A CA    1 
ATOM   519  C C     . GLU A 1 71  ? 2.312   18.056 8.936   1.00 42.23  ? 66  GLU A C     1 
ATOM   520  O O     . GLU A 1 71  ? 2.783   18.178 7.802   1.00 42.41  ? 66  GLU A O     1 
ATOM   521  C CB    . GLU A 1 71  ? -0.047  18.899 9.030   1.00 42.29  ? 66  GLU A CB    1 
ATOM   522  C CG    . GLU A 1 71  ? -0.693  17.641 9.580   1.00 41.30  ? 66  GLU A CG    1 
ATOM   523  C CD    . GLU A 1 71  ? -2.187  17.601 9.335   1.00 46.54  ? 66  GLU A CD    1 
ATOM   524  O OE1   . GLU A 1 71  ? -2.707  18.511 8.656   1.00 47.21  ? 66  GLU A OE1   1 
ATOM   525  O OE2   . GLU A 1 71  ? -2.845  16.666 9.835   1.00 49.60  ? 66  GLU A OE2   1 
ATOM   526  N N     . PHE A 1 72  ? 2.562   17.012 9.724   1.00 45.83  ? 67  PHE A N     1 
ATOM   527  C CA    . PHE A 1 72  ? 3.487   15.952 9.349   1.00 43.77  ? 67  PHE A CA    1 
ATOM   528  C C     . PHE A 1 72  ? 2.874   14.596 9.661   1.00 45.32  ? 67  PHE A C     1 
ATOM   529  O O     . PHE A 1 72  ? 2.480   14.335 10.802  1.00 47.79  ? 67  PHE A O     1 
ATOM   530  C CB    . PHE A 1 72  ? 4.825   16.104 10.079  1.00 42.17  ? 67  PHE A CB    1 
ATOM   531  C CG    . PHE A 1 72  ? 5.530   17.393 9.782   1.00 44.45  ? 67  PHE A CG    1 
ATOM   532  C CD1   . PHE A 1 72  ? 6.234   17.552 8.602   1.00 44.84  ? 67  PHE A CD1   1 
ATOM   533  C CD2   . PHE A 1 72  ? 5.489   18.447 10.681  1.00 42.73  ? 67  PHE A CD2   1 
ATOM   534  C CE1   . PHE A 1 72  ? 6.883   18.735 8.322   1.00 44.18  ? 67  PHE A CE1   1 
ATOM   535  C CE2   . PHE A 1 72  ? 6.139   19.635 10.406  1.00 41.77  ? 67  PHE A CE2   1 
ATOM   536  C CZ    . PHE A 1 72  ? 6.838   19.778 9.224   1.00 47.01  ? 67  PHE A CZ    1 
ATOM   537  N N     . PHE A 1 73  ? 2.793   13.742 8.645   1.00 48.42  ? 68  PHE A N     1 
ATOM   538  C CA    . PHE A 1 73  ? 2.375   12.354 8.811   1.00 42.43  ? 68  PHE A CA    1 
ATOM   539  C C     . PHE A 1 73  ? 3.631   11.519 9.028   1.00 43.66  ? 68  PHE A C     1 
ATOM   540  O O     . PHE A 1 73  ? 4.404   11.295 8.092   1.00 48.07  ? 68  PHE A O     1 
ATOM   541  C CB    . PHE A 1 73  ? 1.587   11.887 7.589   1.00 38.43  ? 68  PHE A CB    1 
ATOM   542  C CG    . PHE A 1 73  ? 0.988   10.517 7.732   1.00 41.03  ? 68  PHE A CG    1 
ATOM   543  C CD1   . PHE A 1 73  ? 0.683   10.000 8.980   1.00 41.49  ? 68  PHE A CD1   1 
ATOM   544  C CD2   . PHE A 1 73  ? 0.727   9.747  6.612   1.00 38.43  ? 68  PHE A CD2   1 
ATOM   545  C CE1   . PHE A 1 73  ? 0.132   8.741  9.106   1.00 44.99  ? 68  PHE A CE1   1 
ATOM   546  C CE2   . PHE A 1 73  ? 0.176   8.489  6.731   1.00 42.35  ? 68  PHE A CE2   1 
ATOM   547  C CZ    . PHE A 1 73  ? -0.121  7.984  7.980   1.00 43.12  ? 68  PHE A CZ    1 
ATOM   548  N N     . SER A 1 74  ? 3.837   11.060 10.260  1.00 44.78  ? 69  SER A N     1 
ATOM   549  C CA    . SER A 1 74  ? 5.121   10.523 10.685  1.00 42.35  ? 69  SER A CA    1 
ATOM   550  C C     . SER A 1 74  ? 5.019   9.050  11.054  1.00 46.10  ? 69  SER A C     1 
ATOM   551  O O     . SER A 1 74  ? 4.006   8.598  11.597  1.00 48.58  ? 69  SER A O     1 
ATOM   552  C CB    . SER A 1 74  ? 5.670   11.310 11.879  1.00 44.46  ? 69  SER A CB    1 
ATOM   553  O OG    . SER A 1 74  ? 7.008   10.938 12.161  1.00 50.14  ? 69  SER A OG    1 
ATOM   554  N N     . ILE A 1 75  ? 6.088   8.312  10.753  1.00 47.33  ? 70  ILE A N     1 
ATOM   555  C CA    . ILE A 1 75  ? 6.229   6.936  11.208  1.00 48.35  ? 70  ILE A CA    1 
ATOM   556  C C     . ILE A 1 75  ? 6.826   6.923  12.613  1.00 51.58  ? 70  ILE A C     1 
ATOM   557  O O     . ILE A 1 75  ? 7.436   7.894  13.068  1.00 54.78  ? 70  ILE A O     1 
ATOM   558  C CB    . ILE A 1 75  ? 7.096   6.131  10.219  1.00 50.63  ? 70  ILE A CB    1 
ATOM   559  C CG1   . ILE A 1 75  ? 6.997   4.623  10.478  1.00 50.04  ? 70  ILE A CG1   1 
ATOM   560  C CG2   . ILE A 1 75  ? 8.546   6.593  10.288  1.00 48.95  ? 70  ILE A CG2   1 
ATOM   561  C CD1   . ILE A 1 75  ? 5.667   4.015  10.095  1.00 50.69  ? 70  ILE A CD1   1 
ATOM   562  N N     . LYS A 1 76  ? 6.632   5.811  13.319  1.00 51.99  ? 71  LYS A N     1 
ATOM   563  C CA    . LYS A 1 76  ? 7.208   5.606  14.645  1.00 48.76  ? 71  LYS A CA    1 
ATOM   564  C C     . LYS A 1 76  ? 8.087   4.364  14.604  1.00 52.34  ? 71  LYS A C     1 
ATOM   565  O O     . LYS A 1 76  ? 7.578   3.239  14.544  1.00 51.21  ? 71  LYS A O     1 
ATOM   566  C CB    . LYS A 1 76  ? 6.119   5.475  15.709  1.00 48.34  ? 71  LYS A CB    1 
ATOM   567  C CG    . LYS A 1 76  ? 5.446   6.787  16.063  1.00 47.73  ? 71  LYS A CG    1 
ATOM   568  C CD    . LYS A 1 76  ? 4.469   6.619  17.214  1.00 47.54  ? 71  LYS A CD    1 
ATOM   569  C CE    . LYS A 1 76  ? 3.133   6.077  16.737  1.00 51.24  ? 71  LYS A CE    1 
ATOM   570  N NZ    . LYS A 1 76  ? 2.238   5.749  17.880  1.00 53.38  ? 71  LYS A NZ    1 
ATOM   571  N N     . VAL A 1 77  ? 9.394   4.568  14.634  1.00 53.60  ? 72  VAL A N     1 
ATOM   572  C CA    . VAL A 1 77  ? 10.377  3.489  14.652  1.00 58.12  ? 72  VAL A CA    1 
ATOM   573  C C     . VAL A 1 77  ? 10.937  3.386  16.064  1.00 60.45  ? 72  VAL A C     1 
ATOM   574  O O     . VAL A 1 77  ? 11.361  4.403  16.623  1.00 56.70  ? 72  VAL A O     1 
ATOM   575  C CB    . VAL A 1 77  ? 11.508  3.727  13.635  1.00 60.21  ? 72  VAL A CB    1 
ATOM   576  C CG1   . VAL A 1 77  ? 12.468  2.548  13.628  1.00 61.25  ? 72  VAL A CG1   1 
ATOM   577  C CG2   . VAL A 1 77  ? 10.929  3.965  12.247  1.00 55.18  ? 72  VAL A CG2   1 
ATOM   578  N N     . PRO A 1 78  ? 10.951  2.196  16.673  1.00 61.35  ? 73  PRO A N     1 
ATOM   579  C CA    . PRO A 1 78  ? 11.411  2.104  18.072  1.00 61.59  ? 73  PRO A CA    1 
ATOM   580  C C     . PRO A 1 78  ? 12.865  2.501  18.263  1.00 60.77  ? 73  PRO A C     1 
ATOM   581  O O     . PRO A 1 78  ? 13.180  3.264  19.185  1.00 59.16  ? 73  PRO A O     1 
ATOM   582  C CB    . PRO A 1 78  ? 11.167  0.627  18.418  1.00 62.43  ? 73  PRO A CB    1 
ATOM   583  C CG    . PRO A 1 78  ? 10.149  0.158  17.431  1.00 56.73  ? 73  PRO A CG    1 
ATOM   584  C CD    . PRO A 1 78  ? 10.427  0.916  16.173  1.00 55.46  ? 73  PRO A CD    1 
ATOM   585  N N     . ASN A 1 79  ? 13.767  2.000  17.419  1.00 56.00  ? 74  ASN A N     1 
ATOM   586  C CA    . ASN A 1 79  ? 15.189  2.291  17.536  1.00 60.29  ? 74  ASN A CA    1 
ATOM   587  C C     . ASN A 1 79  ? 15.659  3.336  16.529  1.00 61.79  ? 74  ASN A C     1 
ATOM   588  O O     . ASN A 1 79  ? 16.858  3.417  16.244  1.00 63.42  ? 74  ASN A O     1 
ATOM   589  C CB    . ASN A 1 79  ? 16.005  1.006  17.387  1.00 64.28  ? 74  ASN A CB    1 
ATOM   590  C CG    . ASN A 1 79  ? 15.959  0.138  18.631  1.00 66.72  ? 74  ASN A CG    1 
ATOM   591  O OD1   . ASN A 1 79  ? 15.958  0.643  19.754  1.00 63.05  ? 74  ASN A OD1   1 
ATOM   592  N ND2   . ASN A 1 79  ? 15.924  -1.175 18.436  1.00 64.57  ? 74  ASN A ND2   1 
ATOM   593  N N     . GLY A 1 80  ? 14.743  4.136  15.988  1.00 60.94  ? 75  GLY A N     1 
ATOM   594  C CA    . GLY A 1 80  ? 15.100  5.186  15.065  1.00 59.18  ? 75  GLY A CA    1 
ATOM   595  C C     . GLY A 1 80  ? 15.586  6.428  15.783  1.00 57.69  ? 75  GLY A C     1 
ATOM   596  O O     . GLY A 1 80  ? 14.977  6.888  16.752  1.00 58.39  ? 75  GLY A O     1 
ATOM   597  N N     . PRO A 1 81  ? 16.704  6.994  15.319  1.00 55.81  ? 76  PRO A N     1 
ATOM   598  C CA    . PRO A 1 81  ? 17.279  8.164  16.008  1.00 52.23  ? 76  PRO A CA    1 
ATOM   599  C C     . PRO A 1 81  ? 16.315  9.325  16.197  1.00 57.56  ? 76  PRO A C     1 
ATOM   600  O O     . PRO A 1 81  ? 16.342  9.970  17.253  1.00 57.76  ? 76  PRO A O     1 
ATOM   601  C CB    . PRO A 1 81  ? 18.452  8.548  15.097  1.00 51.31  ? 76  PRO A CB    1 
ATOM   602  C CG    . PRO A 1 81  ? 18.867  7.264  14.472  1.00 49.19  ? 76  PRO A CG    1 
ATOM   603  C CD    . PRO A 1 81  ? 17.611  6.452  14.293  1.00 54.85  ? 76  PRO A CD    1 
ATOM   604  N N     . LEU A 1 82  ? 15.461  9.615  15.214  1.00 60.48  ? 77  LEU A N     1 
ATOM   605  C CA    . LEU A 1 82  ? 14.557  10.757 15.324  1.00 54.22  ? 77  LEU A CA    1 
ATOM   606  C C     . LEU A 1 82  ? 13.195  10.360 15.887  1.00 51.26  ? 77  LEU A C     1 
ATOM   607  O O     . LEU A 1 82  ? 12.761  10.894 16.913  1.00 52.91  ? 77  LEU A O     1 
ATOM   608  C CB    . LEU A 1 82  ? 14.383  11.436 13.961  1.00 52.60  ? 77  LEU A CB    1 
ATOM   609  C CG    . LEU A 1 82  ? 13.407  12.619 13.982  1.00 49.40  ? 77  LEU A CG    1 
ATOM   610  C CD1   . LEU A 1 82  ? 13.914  13.721 14.904  1.00 51.62  ? 77  LEU A CD1   1 
ATOM   611  C CD2   . LEU A 1 82  ? 13.147  13.163 12.585  1.00 45.81  ? 77  LEU A CD2   1 
ATOM   612  N N     . THR A 1 83  ? 12.511  9.426  15.225  1.00 53.46  ? 78  THR A N     1 
ATOM   613  C CA    . THR A 1 83  ? 11.125  9.124  15.564  1.00 55.69  ? 78  THR A CA    1 
ATOM   614  C C     . THR A 1 83  ? 10.971  8.393  16.892  1.00 56.30  ? 78  THR A C     1 
ATOM   615  O O     . THR A 1 83  ? 9.839   8.250  17.364  1.00 53.36  ? 78  THR A O     1 
ATOM   616  C CB    . THR A 1 83  ? 10.477  8.309  14.445  1.00 53.61  ? 78  THR A CB    1 
ATOM   617  O OG1   . THR A 1 83  ? 11.253  7.131  14.196  1.00 59.68  ? 78  THR A OG1   1 
ATOM   618  C CG2   . THR A 1 83  ? 10.400  9.135  13.172  1.00 49.81  ? 78  THR A CG2   1 
ATOM   619  N N     . SER A 1 84  ? 12.061  7.922  17.502  1.00 59.52  ? 79  SER A N     1 
ATOM   620  C CA    . SER A 1 84  ? 11.954  7.386  18.854  1.00 57.46  ? 79  SER A CA    1 
ATOM   621  C C     . SER A 1 84  ? 11.816  8.498  19.884  1.00 55.11  ? 79  SER A C     1 
ATOM   622  O O     . SER A 1 84  ? 11.119  8.323  20.890  1.00 56.29  ? 79  SER A O     1 
ATOM   623  C CB    . SER A 1 84  ? 13.163  6.509  19.183  1.00 53.50  ? 79  SER A CB    1 
ATOM   624  O OG    . SER A 1 84  ? 14.374  7.222  19.003  1.00 53.32  ? 79  SER A OG    1 
ATOM   625  N N     . LYS A 1 85  ? 12.472  9.636  19.652  1.00 54.23  ? 80  LYS A N     1 
ATOM   626  C CA    . LYS A 1 85  ? 12.241  10.819 20.471  1.00 52.90  ? 80  LYS A CA    1 
ATOM   627  C C     . LYS A 1 85  ? 11.045  11.617 19.971  1.00 50.91  ? 80  LYS A C     1 
ATOM   628  O O     . LYS A 1 85  ? 10.350  12.256 20.769  1.00 53.74  ? 80  LYS A O     1 
ATOM   629  C CB    . LYS A 1 85  ? 13.480  11.715 20.476  1.00 55.79  ? 80  LYS A CB    1 
ATOM   630  C CG    . LYS A 1 85  ? 14.797  10.971 20.562  1.00 61.30  ? 80  LYS A CG    1 
ATOM   631  C CD    . LYS A 1 85  ? 15.905  11.786 19.914  1.00 59.38  ? 80  LYS A CD    1 
ATOM   632  C CE    . LYS A 1 85  ? 17.263  11.500 20.529  1.00 59.63  ? 80  LYS A CE    1 
ATOM   633  N NZ    . LYS A 1 85  ? 17.982  12.761 20.861  1.00 61.65  ? 80  LYS A NZ    1 
ATOM   634  N N     . LEU A 1 86  ? 10.792  11.586 18.660  1.00 52.53  ? 81  LEU A N     1 
ATOM   635  C CA    . LEU A 1 86  ? 9.725   12.393 18.083  1.00 52.33  ? 81  LEU A CA    1 
ATOM   636  C C     . LEU A 1 86  ? 8.349   11.813 18.384  1.00 51.85  ? 81  LEU A C     1 
ATOM   637  O O     . LEU A 1 86  ? 7.357   12.550 18.387  1.00 55.71  ? 81  LEU A O     1 
ATOM   638  C CB    . LEU A 1 86  ? 9.929   12.514 16.575  1.00 54.17  ? 81  LEU A CB    1 
ATOM   639  C CG    . LEU A 1 86  ? 9.335   13.735 15.873  1.00 50.28  ? 81  LEU A CG    1 
ATOM   640  C CD1   . LEU A 1 86  ? 10.072  15.003 16.278  1.00 47.37  ? 81  LEU A CD1   1 
ATOM   641  C CD2   . LEU A 1 86  ? 9.376   13.539 14.369  1.00 48.77  ? 81  LEU A CD2   1 
ATOM   642  N N     . GLN A 1 87  ? 8.264   10.503 18.629  1.00 51.28  ? 82  GLN A N     1 
ATOM   643  C CA    . GLN A 1 87  ? 6.969   9.894  18.907  1.00 50.66  ? 82  GLN A CA    1 
ATOM   644  C C     . GLN A 1 87  ? 6.390   10.382 20.228  1.00 52.90  ? 82  GLN A C     1 
ATOM   645  O O     . GLN A 1 87  ? 5.165   10.428 20.387  1.00 51.48  ? 82  GLN A O     1 
ATOM   646  C CB    . GLN A 1 87  ? 7.092   8.371  18.918  1.00 53.20  ? 82  GLN A CB    1 
ATOM   647  C CG    . GLN A 1 87  ? 7.984   7.822  20.017  1.00 52.30  ? 82  GLN A CG    1 
ATOM   648  C CD    . GLN A 1 87  ? 8.201   6.328  19.896  1.00 48.63  ? 82  GLN A CD    1 
ATOM   649  O OE1   . GLN A 1 87  ? 7.358   5.610  19.360  1.00 52.50  ? 82  GLN A OE1   1 
ATOM   650  N NE2   . GLN A 1 87  ? 9.335   5.851  20.397  1.00 50.92  ? 82  GLN A NE2   1 
ATOM   651  N N     . HIS A 1 88  ? 7.247   10.755 21.178  1.00 56.85  ? 83  HIS A N     1 
ATOM   652  C CA    . HIS A 1 88  ? 6.815   11.216 22.488  1.00 57.39  ? 83  HIS A CA    1 
ATOM   653  C C     . HIS A 1 88  ? 6.550   12.716 22.521  1.00 59.44  ? 83  HIS A C     1 
ATOM   654  O O     . HIS A 1 88  ? 6.602   13.321 23.599  1.00 63.10  ? 83  HIS A O     1 
ATOM   655  C CB    . HIS A 1 88  ? 7.857   10.842 23.542  1.00 52.57  ? 83  HIS A CB    1 
ATOM   656  C CG    . HIS A 1 88  ? 8.176   9.380  23.582  1.00 51.59  ? 83  HIS A CG    1 
ATOM   657  N ND1   . HIS A 1 88  ? 7.215   8.413  23.781  1.00 53.17  ? 83  HIS A ND1   1 
ATOM   658  C CD2   . HIS A 1 88  ? 9.350   8.721  23.442  1.00 53.21  ? 83  HIS A CD2   1 
ATOM   659  C CE1   . HIS A 1 88  ? 7.783   7.220  23.765  1.00 53.15  ? 83  HIS A CE1   1 
ATOM   660  N NE2   . HIS A 1 88  ? 9.078   7.379  23.560  1.00 55.66  ? 83  HIS A NE2   1 
ATOM   661  N N     . LEU A 1 89  ? 6.274   13.326 21.369  1.00 62.10  ? 84  LEU A N     1 
ATOM   662  C CA    . LEU A 1 89  ? 6.004   14.756 21.320  1.00 62.83  ? 84  LEU A CA    1 
ATOM   663  C C     . LEU A 1 89  ? 4.761   15.098 22.132  1.00 64.58  ? 84  LEU A C     1 
ATOM   664  O O     . LEU A 1 89  ? 3.833   14.296 22.262  1.00 63.84  ? 84  LEU A O     1 
ATOM   665  C CB    . LEU A 1 89  ? 5.818   15.218 19.874  1.00 60.55  ? 84  LEU A CB    1 
ATOM   666  C CG    . LEU A 1 89  ? 7.053   15.664 19.088  1.00 57.90  ? 84  LEU A CG    1 
ATOM   667  C CD1   . LEU A 1 89  ? 6.723   15.772 17.608  1.00 51.99  ? 84  LEU A CD1   1 
ATOM   668  C CD2   . LEU A 1 89  ? 7.589   16.984 19.615  1.00 55.11  ? 84  LEU A CD2   1 
ATOM   669  N N     . LYS A 1 90  ? 4.754   16.308 22.683  1.00 61.40  ? 85  LYS A N     1 
ATOM   670  C CA    . LYS A 1 90  ? 3.617   16.826 23.426  1.00 62.05  ? 85  LYS A CA    1 
ATOM   671  C C     . LYS A 1 90  ? 3.278   18.216 22.908  1.00 55.73  ? 85  LYS A C     1 
ATOM   672  O O     . LYS A 1 90  ? 4.071   18.849 22.206  1.00 56.57  ? 85  LYS A O     1 
ATOM   673  C CB    . LYS A 1 90  ? 3.899   16.875 24.934  1.00 62.10  ? 85  LYS A CB    1 
ATOM   674  C CG    . LYS A 1 90  ? 4.050   15.507 25.581  1.00 68.14  ? 85  LYS A CG    1 
ATOM   675  C CD    . LYS A 1 90  ? 4.583   15.619 26.999  1.00 72.47  ? 85  LYS A CD    1 
ATOM   676  C CE    . LYS A 1 90  ? 4.572   14.269 27.698  1.00 78.25  ? 85  LYS A CE    1 
ATOM   677  N NZ    . LYS A 1 90  ? 3.196   13.859 28.091  1.00 76.53  ? 85  LYS A NZ    1 
ATOM   678  N N     . LYS A 1 91  ? 2.079   18.681 23.252  1.00 52.87  ? 86  LYS A N     1 
ATOM   679  C CA    . LYS A 1 91  ? 1.659   20.013 22.842  1.00 54.88  ? 86  LYS A CA    1 
ATOM   680  C C     . LYS A 1 91  ? 2.571   21.066 23.456  1.00 55.31  ? 86  LYS A C     1 
ATOM   681  O O     . LYS A 1 91  ? 2.912   21.004 24.640  1.00 53.50  ? 86  LYS A O     1 
ATOM   682  C CB    . LYS A 1 91  ? 0.207   20.266 23.249  1.00 57.17  ? 86  LYS A CB    1 
ATOM   683  C CG    . LYS A 1 91  ? -0.777  19.211 22.759  1.00 59.37  ? 86  LYS A CG    1 
ATOM   684  C CD    . LYS A 1 91  ? -2.203  19.754 22.687  1.00 64.29  ? 86  LYS A CD    1 
ATOM   685  C CE    . LYS A 1 91  ? -2.421  20.915 23.647  1.00 60.91  ? 86  LYS A CE    1 
ATOM   686  N NZ    . LYS A 1 91  ? -3.687  21.647 23.366  1.00 65.32  ? 86  LYS A NZ    1 
ATOM   687  N N     . GLY A 1 92  ? 2.971   22.037 22.637  1.00 57.04  ? 87  GLY A N     1 
ATOM   688  C CA    . GLY A 1 92  ? 3.893   23.064 23.061  1.00 52.82  ? 87  GLY A CA    1 
ATOM   689  C C     . GLY A 1 92  ? 5.355   22.730 22.865  1.00 58.46  ? 87  GLY A C     1 
ATOM   690  O O     . GLY A 1 92  ? 6.204   23.613 23.044  1.00 64.56  ? 87  GLY A O     1 
ATOM   691  N N     . ASP A 1 93  ? 5.678   21.489 22.510  1.00 57.27  ? 88  ASP A N     1 
ATOM   692  C CA    . ASP A 1 93  ? 7.064   21.113 22.274  1.00 56.60  ? 88  ASP A CA    1 
ATOM   693  C C     . ASP A 1 93  ? 7.611   21.829 21.045  1.00 56.66  ? 88  ASP A C     1 
ATOM   694  O O     . ASP A 1 93  ? 6.868   22.207 20.135  1.00 57.76  ? 88  ASP A O     1 
ATOM   695  C CB    . ASP A 1 93  ? 7.188   19.600 22.096  1.00 58.09  ? 88  ASP A CB    1 
ATOM   696  C CG    . ASP A 1 93  ? 7.303   18.863 23.416  1.00 62.47  ? 88  ASP A CG    1 
ATOM   697  O OD1   . ASP A 1 93  ? 7.613   19.513 24.436  1.00 62.07  ? 88  ASP A OD1   1 
ATOM   698  O OD2   . ASP A 1 93  ? 7.085   17.633 23.433  1.00 65.02  ? 88  ASP A OD2   1 
ATOM   699  N N     . GLN A 1 94  ? 8.927   22.010 21.026  1.00 59.94  ? 89  GLN A N     1 
ATOM   700  C CA    . GLN A 1 94  ? 9.605   22.728 19.957  1.00 58.55  ? 89  GLN A CA    1 
ATOM   701  C C     . GLN A 1 94  ? 10.222  21.746 18.972  1.00 55.79  ? 89  GLN A C     1 
ATOM   702  O O     . GLN A 1 94  ? 10.897  20.791 19.373  1.00 57.70  ? 89  GLN A O     1 
ATOM   703  C CB    . GLN A 1 94  ? 10.686  23.652 20.519  1.00 61.53  ? 89  GLN A CB    1 
ATOM   704  C CG    . GLN A 1 94  ? 10.183  24.633 21.557  1.00 69.39  ? 89  GLN A CG    1 
ATOM   705  C CD    . GLN A 1 94  ? 9.338   25.734 20.949  1.00 66.60  ? 89  GLN A CD    1 
ATOM   706  O OE1   . GLN A 1 94  ? 8.156   25.869 21.262  1.00 67.69  ? 89  GLN A OE1   1 
ATOM   707  N NE2   . GLN A 1 94  ? 9.942   26.526 20.072  1.00 64.81  ? 89  GLN A NE2   1 
ATOM   708  N N     . ILE A 1 95  ? 9.977   21.986 17.683  1.00 54.67  ? 90  ILE A N     1 
ATOM   709  C CA    . ILE A 1 95  ? 10.596  21.253 16.589  1.00 53.13  ? 90  ILE A CA    1 
ATOM   710  C C     . ILE A 1 95  ? 11.194  22.270 15.626  1.00 50.40  ? 90  ILE A C     1 
ATOM   711  O O     . ILE A 1 95  ? 10.825  23.447 15.621  1.00 54.46  ? 90  ILE A O     1 
ATOM   712  C CB    . ILE A 1 95  ? 9.600   20.298 15.874  1.00 53.86  ? 90  ILE A CB    1 
ATOM   713  C CG1   . ILE A 1 95  ? 8.439   21.057 15.217  1.00 48.72  ? 90  ILE A CG1   1 
ATOM   714  C CG2   . ILE A 1 95  ? 9.067   19.257 16.850  1.00 59.83  ? 90  ILE A CG2   1 
ATOM   715  C CD1   . ILE A 1 95  ? 8.668   21.428 13.772  1.00 47.05  ? 90  ILE A CD1   1 
ATOM   716  N N     . ILE A 1 96  ? 12.140  21.808 14.813  1.00 51.39  ? 91  ILE A N     1 
ATOM   717  C CA    . ILE A 1 96  ? 12.848  22.665 13.869  1.00 54.62  ? 91  ILE A CA    1 
ATOM   718  C C     . ILE A 1 96  ? 12.546  22.191 12.454  1.00 54.19  ? 91  ILE A C     1 
ATOM   719  O O     . ILE A 1 96  ? 12.586  20.988 12.171  1.00 55.51  ? 91  ILE A O     1 
ATOM   720  C CB    . ILE A 1 96  ? 14.364  22.688 14.144  1.00 54.91  ? 91  ILE A CB    1 
ATOM   721  C CG1   . ILE A 1 96  ? 14.943  21.274 14.173  1.00 52.46  ? 91  ILE A CG1   1 
ATOM   722  C CG2   . ILE A 1 96  ? 14.655  23.403 15.456  1.00 58.28  ? 91  ILE A CG2   1 
ATOM   723  C CD1   . ILE A 1 96  ? 16.405  21.221 13.804  1.00 54.79  ? 91  ILE A CD1   1 
ATOM   724  N N     . VAL A 1 97  ? 12.225  23.139 11.576  1.00 55.50  ? 92  VAL A N     1 
ATOM   725  C CA    . VAL A 1 97  ? 11.932  22.876 10.172  1.00 52.66  ? 92  VAL A CA    1 
ATOM   726  C C     . VAL A 1 97  ? 12.890  23.695 9.320   1.00 55.61  ? 92  VAL A C     1 
ATOM   727  O O     . VAL A 1 97  ? 13.035  24.906 9.531   1.00 59.98  ? 92  VAL A O     1 
ATOM   728  C CB    . VAL A 1 97  ? 10.470  23.213 9.821   1.00 53.17  ? 92  VAL A CB    1 
ATOM   729  C CG1   . VAL A 1 97  ? 10.281  23.249 8.316   1.00 53.09  ? 92  VAL A CG1   1 
ATOM   730  C CG2   . VAL A 1 97  ? 9.531   22.196 10.439  1.00 51.40  ? 92  VAL A CG2   1 
ATOM   731  N N     . SER A 1 98  ? 13.541  23.038 8.364   1.00 53.74  ? 93  SER A N     1 
ATOM   732  C CA    . SER A 1 98  ? 14.388  23.744 7.416   1.00 50.99  ? 93  SER A CA    1 
ATOM   733  C C     . SER A 1 98  ? 13.545  24.659 6.535   1.00 51.28  ? 93  SER A C     1 
ATOM   734  O O     . SER A 1 98  ? 12.391  24.362 6.212   1.00 52.49  ? 93  SER A O     1 
ATOM   735  C CB    . SER A 1 98  ? 15.171  22.754 6.556   1.00 49.28  ? 93  SER A CB    1 
ATOM   736  O OG    . SER A 1 98  ? 14.366  22.238 5.511   1.00 56.24  ? 93  SER A OG    1 
ATOM   737  N N     . LYS A 1 99  ? 14.136  25.783 6.145   1.00 56.74  ? 94  LYS A N     1 
ATOM   738  C CA    . LYS A 1 99  ? 13.421  26.834 5.436   1.00 57.70  ? 94  LYS A CA    1 
ATOM   739  C C     . LYS A 1 99  ? 13.468  26.680 3.921   1.00 56.25  ? 94  LYS A C     1 
ATOM   740  O O     . LYS A 1 99  ? 12.947  27.546 3.210   1.00 58.53  ? 94  LYS A O     1 
ATOM   741  C CB    . LYS A 1 99  ? 13.989  28.201 5.827   1.00 62.04  ? 94  LYS A CB    1 
ATOM   742  C CG    . LYS A 1 99  ? 13.921  28.490 7.318   1.00 62.76  ? 94  LYS A CG    1 
ATOM   743  C CD    . LYS A 1 99  ? 14.212  29.949 7.610   1.00 62.02  ? 94  LYS A CD    1 
ATOM   744  C CE    . LYS A 1 99  ? 15.607  30.120 8.186   1.00 64.83  ? 94  LYS A CE    1 
ATOM   745  N NZ    . LYS A 1 99  ? 15.612  31.057 9.341   1.00 72.69  ? 94  LYS A NZ    1 
ATOM   746  N N     . LYS A 1 100 ? 14.071  25.607 3.406   1.00 54.08  ? 95  LYS A N     1 
ATOM   747  C CA    . LYS A 1 100 ? 14.267  25.423 1.968   1.00 50.27  ? 95  LYS A CA    1 
ATOM   748  C C     . LYS A 1 100 ? 13.524  24.174 1.513   1.00 53.44  ? 95  LYS A C     1 
ATOM   749  O O     . LYS A 1 100 ? 14.059  23.057 1.596   1.00 54.20  ? 95  LYS A O     1 
ATOM   750  C CB    . LYS A 1 100 ? 15.753  25.330 1.632   1.00 55.31  ? 95  LYS A CB    1 
ATOM   751  C CG    . LYS A 1 100 ? 16.116  25.878 0.263   1.00 64.73  ? 95  LYS A CG    1 
ATOM   752  C CD    . LYS A 1 100 ? 16.416  24.761 -0.721  1.00 74.27  ? 95  LYS A CD    1 
ATOM   753  C CE    . LYS A 1 100 ? 16.590  25.306 -2.129  1.00 74.32  ? 95  LYS A CE    1 
ATOM   754  N NZ    . LYS A 1 100 ? 16.585  24.221 -3.148  1.00 74.13  ? 95  LYS A NZ    1 
ATOM   755  N N     . PRO A 1 101 ? 12.291  24.312 1.030   1.00 50.53  ? 96  PRO A N     1 
ATOM   756  C CA    . PRO A 1 101 ? 11.571  23.147 0.505   1.00 44.52  ? 96  PRO A CA    1 
ATOM   757  C C     . PRO A 1 101 ? 12.204  22.629 -0.776  1.00 50.26  ? 96  PRO A C     1 
ATOM   758  O O     . PRO A 1 101 ? 12.914  23.339 -1.492  1.00 55.48  ? 96  PRO A O     1 
ATOM   759  C CB    . PRO A 1 101 ? 10.159  23.684 0.244   1.00 42.29  ? 96  PRO A CB    1 
ATOM   760  C CG    . PRO A 1 101 ? 10.062  24.940 1.055   1.00 43.01  ? 96  PRO A CG    1 
ATOM   761  C CD    . PRO A 1 101 ? 11.443  25.514 1.070   1.00 49.68  ? 96  PRO A CD    1 
ATOM   762  N N     . VAL A 1 102 ? 11.920  21.358 -1.060  1.00 53.30  ? 97  VAL A N     1 
ATOM   763  C CA    . VAL A 1 102 ? 12.467  20.673 -2.225  1.00 49.42  ? 97  VAL A CA    1 
ATOM   764  C C     . VAL A 1 102 ? 11.610  19.439 -2.469  1.00 45.63  ? 97  VAL A C     1 
ATOM   765  O O     . VAL A 1 102 ? 11.061  18.856 -1.531  1.00 53.68  ? 97  VAL A O     1 
ATOM   766  C CB    . VAL A 1 102 ? 13.963  20.319 -2.007  1.00 55.78  ? 97  VAL A CB    1 
ATOM   767  C CG1   . VAL A 1 102 ? 14.159  19.616 -0.675  1.00 57.21  ? 97  VAL A CG1   1 
ATOM   768  C CG2   . VAL A 1 102 ? 14.519  19.486 -3.164  1.00 53.89  ? 97  VAL A CG2   1 
ATOM   769  N N     . GLY A 1 103 ? 11.471  19.057 -3.738  1.00 47.06  ? 98  GLY A N     1 
ATOM   770  C CA    . GLY A 1 103 ? 10.714  17.865 -4.079  1.00 47.14  ? 98  GLY A CA    1 
ATOM   771  C C     . GLY A 1 103 ? 10.409  17.703 -5.556  1.00 48.13  ? 98  GLY A C     1 
ATOM   772  O O     . GLY A 1 103 ? 10.489  18.667 -6.322  1.00 48.28  ? 98  GLY A O     1 
ATOM   773  N N     . THR A 1 104 ? 10.064  16.484 -5.971  1.00 52.41  ? 99  THR A N     1 
ATOM   774  C CA    . THR A 1 104 ? 9.696   16.216 -7.354  1.00 49.23  ? 99  THR A CA    1 
ATOM   775  C C     . THR A 1 104 ? 8.192   16.100 -7.557  1.00 49.76  ? 99  THR A C     1 
ATOM   776  O O     . THR A 1 104 ? 7.743   16.017 -8.705  1.00 53.76  ? 99  THR A O     1 
ATOM   777  C CB    . THR A 1 104 ? 10.373  14.931 -7.855  1.00 50.34  ? 99  THR A CB    1 
ATOM   778  O OG1   . THR A 1 104 ? 9.706   13.785 -7.314  1.00 52.63  ? 99  THR A OG1   1 
ATOM   779  C CG2   . THR A 1 104 ? 11.835  14.905 -7.444  1.00 54.94  ? 99  THR A CG2   1 
ATOM   780  N N     . LEU A 1 105 ? 7.409   16.102 -6.478  1.00 46.06  ? 100 LEU A N     1 
ATOM   781  C CA    . LEU A 1 105 ? 5.955   15.969 -6.562  1.00 44.55  ? 100 LEU A CA    1 
ATOM   782  C C     . LEU A 1 105 ? 5.304   17.333 -6.806  1.00 46.08  ? 100 LEU A C     1 
ATOM   783  O O     . LEU A 1 105 ? 4.500   17.833 -6.019  1.00 47.36  ? 100 LEU A O     1 
ATOM   784  C CB    . LEU A 1 105 ? 5.417   15.312 -5.297  1.00 45.70  ? 100 LEU A CB    1 
ATOM   785  C CG    . LEU A 1 105 ? 5.993   13.928 -4.996  1.00 44.78  ? 100 LEU A CG    1 
ATOM   786  C CD1   . LEU A 1 105 ? 5.399   13.364 -3.719  1.00 43.97  ? 100 LEU A CD1   1 
ATOM   787  C CD2   . LEU A 1 105 ? 5.757   12.985 -6.165  1.00 40.79  ? 100 LEU A CD2   1 
ATOM   788  N N     . LEU A 1 106 ? 5.672   17.934 -7.932  1.00 47.65  ? 101 LEU A N     1 
ATOM   789  C CA    . LEU A 1 106 ? 5.136   19.217 -8.359  1.00 45.90  ? 101 LEU A CA    1 
ATOM   790  C C     . LEU A 1 106 ? 4.321   19.039 -9.632  1.00 44.32  ? 101 LEU A C     1 
ATOM   791  O O     . LEU A 1 106 ? 4.590   18.146 -10.441 1.00 45.32  ? 101 LEU A O     1 
ATOM   792  C CB    . LEU A 1 106 ? 6.257   20.232 -8.600  1.00 44.00  ? 101 LEU A CB    1 
ATOM   793  C CG    . LEU A 1 106 ? 7.247   20.439 -7.453  1.00 41.30  ? 101 LEU A CG    1 
ATOM   794  C CD1   . LEU A 1 106 ? 8.212   21.566 -7.776  1.00 41.77  ? 101 LEU A CD1   1 
ATOM   795  C CD2   . LEU A 1 106 ? 6.502   20.723 -6.161  1.00 43.18  ? 101 LEU A CD2   1 
ATOM   796  N N     . TYR A 1 107 ? 3.311   19.897 -9.801  1.00 48.25  ? 102 TYR A N     1 
ATOM   797  C CA    . TYR A 1 107 ? 2.516   19.855 -11.023 1.00 45.93  ? 102 TYR A CA    1 
ATOM   798  C C     . TYR A 1 107 ? 3.354   20.243 -12.235 1.00 49.77  ? 102 TYR A C     1 
ATOM   799  O O     . TYR A 1 107 ? 3.180   19.683 -13.323 1.00 54.15  ? 102 TYR A O     1 
ATOM   800  C CB    . TYR A 1 107 ? 1.305   20.780 -10.906 1.00 50.63  ? 102 TYR A CB    1 
ATOM   801  C CG    . TYR A 1 107 ? 0.656   20.812 -9.542  1.00 50.37  ? 102 TYR A CG    1 
ATOM   802  C CD1   . TYR A 1 107 ? 0.055   19.680 -9.007  1.00 50.49  ? 102 TYR A CD1   1 
ATOM   803  C CD2   . TYR A 1 107 ? 0.631   21.982 -8.794  1.00 45.75  ? 102 TYR A CD2   1 
ATOM   804  C CE1   . TYR A 1 107 ? -0.545  19.711 -7.761  1.00 50.47  ? 102 TYR A CE1   1 
ATOM   805  C CE2   . TYR A 1 107 ? 0.035   22.024 -7.549  1.00 43.52  ? 102 TYR A CE2   1 
ATOM   806  C CZ    . TYR A 1 107 ? -0.552  20.886 -7.038  1.00 47.17  ? 102 TYR A CZ    1 
ATOM   807  O OH    . TYR A 1 107 ? -1.146  20.925 -5.798  1.00 51.62  ? 102 TYR A OH    1 
ATOM   808  N N     . ASP A 1 108 ? 4.273   21.198 -12.063 1.00 50.42  ? 103 ASP A N     1 
ATOM   809  C CA    . ASP A 1 108 ? 5.069   21.687 -13.182 1.00 50.41  ? 103 ASP A CA    1 
ATOM   810  C C     . ASP A 1 108 ? 6.039   20.640 -13.711 1.00 53.76  ? 103 ASP A C     1 
ATOM   811  O O     . ASP A 1 108 ? 6.515   20.773 -14.842 1.00 54.13  ? 103 ASP A O     1 
ATOM   812  C CB    . ASP A 1 108 ? 5.828   22.947 -12.768 1.00 51.22  ? 103 ASP A CB    1 
ATOM   813  C CG    . ASP A 1 108 ? 4.905   24.121 -12.512 1.00 55.15  ? 103 ASP A CG    1 
ATOM   814  O OD1   . ASP A 1 108 ? 3.819   24.169 -13.127 1.00 55.26  ? 103 ASP A OD1   1 
ATOM   815  O OD2   . ASP A 1 108 ? 5.262   24.993 -11.692 1.00 56.96  ? 103 ASP A OD2   1 
ATOM   816  N N     . ASN A 1 109 ? 6.347   19.611 -12.924 1.00 52.55  ? 104 ASN A N     1 
ATOM   817  C CA    . ASN A 1 109 ? 7.124   18.482 -13.416 1.00 45.45  ? 104 ASN A CA    1 
ATOM   818  C C     . ASN A 1 109 ? 6.282   17.502 -14.221 1.00 43.71  ? 104 ASN A C     1 
ATOM   819  O O     . ASN A 1 109 ? 6.821   16.507 -14.717 1.00 43.70  ? 104 ASN A O     1 
ATOM   820  C CB    . ASN A 1 109 ? 7.795   17.752 -12.250 1.00 45.31  ? 104 ASN A CB    1 
ATOM   821  C CG    . ASN A 1 109 ? 8.648   18.671 -11.399 1.00 45.71  ? 104 ASN A CG    1 
ATOM   822  O OD1   . ASN A 1 109 ? 8.781   19.859 -11.690 1.00 45.44  ? 104 ASN A OD1   1 
ATOM   823  N ND2   . ASN A 1 109 ? 9.234   18.122 -10.341 1.00 46.56  ? 104 ASN A ND2   1 
ATOM   824  N N     . LEU A 1 110 ? 4.984   17.759 -14.357 1.00 45.48  ? 105 LEU A N     1 
ATOM   825  C CA    . LEU A 1 110 ? 4.081   16.929 -15.137 1.00 48.32  ? 105 LEU A CA    1 
ATOM   826  C C     . LEU A 1 110 ? 3.524   17.735 -16.301 1.00 51.92  ? 105 LEU A C     1 
ATOM   827  O O     . LEU A 1 110 ? 3.385   18.959 -16.220 1.00 51.20  ? 105 LEU A O     1 
ATOM   828  C CB    . LEU A 1 110 ? 2.922   16.406 -14.279 1.00 48.34  ? 105 LEU A CB    1 
ATOM   829  C CG    . LEU A 1 110 ? 3.274   15.484 -13.113 1.00 48.13  ? 105 LEU A CG    1 
ATOM   830  C CD1   . LEU A 1 110 ? 2.029   15.151 -12.309 1.00 40.84  ? 105 LEU A CD1   1 
ATOM   831  C CD2   . LEU A 1 110 ? 3.940   14.219 -13.621 1.00 46.35  ? 105 LEU A CD2   1 
ATOM   832  N N     . LYS A 1 111 ? 3.208   17.039 -17.387 1.00 54.17  ? 106 LYS A N     1 
ATOM   833  C CA    . LYS A 1 111 ? 2.559   17.696 -18.507 1.00 51.44  ? 106 LYS A CA    1 
ATOM   834  C C     . LYS A 1 111 ? 1.068   17.871 -18.219 1.00 53.09  ? 106 LYS A C     1 
ATOM   835  O O     . LYS A 1 111 ? 0.486   17.102 -17.449 1.00 55.80  ? 106 LYS A O     1 
ATOM   836  C CB    . LYS A 1 111 ? 2.752   16.888 -19.786 1.00 52.61  ? 106 LYS A CB    1 
ATOM   837  C CG    . LYS A 1 111 ? 4.206   16.736 -20.204 1.00 53.02  ? 106 LYS A CG    1 
ATOM   838  C CD    . LYS A 1 111 ? 4.332   16.493 -21.700 1.00 55.48  ? 106 LYS A CD    1 
ATOM   839  C CE    . LYS A 1 111 ? 3.820   15.114 -22.080 1.00 53.90  ? 106 LYS A CE    1 
ATOM   840  N NZ    . LYS A 1 111 ? 4.905   14.094 -22.060 1.00 53.69  ? 106 LYS A NZ    1 
ATOM   841  N N     . PRO A 1 112 ? 0.441   18.893 -18.798 1.00 56.43  ? 107 PRO A N     1 
ATOM   842  C CA    . PRO A 1 112 ? -1.002  19.086 -18.598 1.00 49.97  ? 107 PRO A CA    1 
ATOM   843  C C     . PRO A 1 112 ? -1.789  17.837 -18.967 1.00 54.11  ? 107 PRO A C     1 
ATOM   844  O O     . PRO A 1 112 ? -1.667  17.306 -20.073 1.00 55.87  ? 107 PRO A O     1 
ATOM   845  C CB    . PRO A 1 112 ? -1.344  20.259 -19.524 1.00 49.74  ? 107 PRO A CB    1 
ATOM   846  C CG    . PRO A 1 112 ? -0.053  20.890 -19.909 1.00 48.48  ? 107 PRO A CG    1 
ATOM   847  C CD    . PRO A 1 112 ? 1.089   20.045 -19.448 1.00 53.92  ? 107 PRO A CD    1 
ATOM   848  N N     . GLY A 1 113 ? -2.604  17.363 -18.020 1.00 54.89  ? 108 GLY A N     1 
ATOM   849  C CA    . GLY A 1 113 ? -3.362  16.147 -18.219 1.00 50.98  ? 108 GLY A CA    1 
ATOM   850  C C     . GLY A 1 113 ? -4.774  16.281 -17.685 1.00 52.33  ? 108 GLY A C     1 
ATOM   851  O O     . GLY A 1 113 ? -5.132  17.274 -17.048 1.00 51.35  ? 108 GLY A O     1 
ATOM   852  N N     . LYS A 1 114 ? -5.572  15.250 -17.961 1.00 53.88  ? 109 LYS A N     1 
ATOM   853  C CA    . LYS A 1 114 ? -6.961  15.200 -17.525 1.00 55.66  ? 109 LYS A CA    1 
ATOM   854  C C     . LYS A 1 114 ? -7.109  14.606 -16.129 1.00 55.61  ? 109 LYS A C     1 
ATOM   855  O O     . LYS A 1 114 ? -7.965  15.050 -15.355 1.00 57.09  ? 109 LYS A O     1 
ATOM   856  C CB    . LYS A 1 114 ? -7.792  14.389 -18.524 1.00 54.93  ? 109 LYS A CB    1 
ATOM   857  C CG    . LYS A 1 114 ? -9.289  14.425 -18.272 1.00 60.23  ? 109 LYS A CG    1 
ATOM   858  C CD    . LYS A 1 114 ? -10.012 13.402 -19.135 1.00 62.55  ? 109 LYS A CD    1 
ATOM   859  C CE    . LYS A 1 114 ? -10.794 14.070 -20.255 1.00 62.67  ? 109 LYS A CE    1 
ATOM   860  N NZ    . LYS A 1 114 ? -12.258 13.824 -20.134 1.00 60.86  ? 109 LYS A NZ    1 
ATOM   861  N N     . HIS A 1 115 ? -6.293  13.611 -15.791 1.00 53.25  ? 110 HIS A N     1 
ATOM   862  C CA    . HIS A 1 115 ? -6.358  12.940 -14.502 1.00 48.82  ? 110 HIS A CA    1 
ATOM   863  C C     . HIS A 1 115 ? -5.006  13.019 -13.810 1.00 49.99  ? 110 HIS A C     1 
ATOM   864  O O     . HIS A 1 115 ? -3.960  12.898 -14.455 1.00 50.31  ? 110 HIS A O     1 
ATOM   865  C CB    . HIS A 1 115 ? -6.762  11.469 -14.660 1.00 51.93  ? 110 HIS A CB    1 
ATOM   866  C CG    . HIS A 1 115 ? -8.037  11.264 -15.417 1.00 52.45  ? 110 HIS A CG    1 
ATOM   867  N ND1   . HIS A 1 115 ? -8.244  10.179 -16.241 1.00 52.93  ? 110 HIS A ND1   1 
ATOM   868  C CD2   . HIS A 1 115 ? -9.172  12.000 -15.472 1.00 50.71  ? 110 HIS A CD2   1 
ATOM   869  C CE1   . HIS A 1 115 ? -9.451  10.257 -16.774 1.00 51.62  ? 110 HIS A CE1   1 
ATOM   870  N NE2   . HIS A 1 115 ? -10.035 11.353 -16.323 1.00 49.10  ? 110 HIS A NE2   1 
ATOM   871  N N     . LEU A 1 116 ? -5.032  13.223 -12.496 1.00 49.61  ? 111 LEU A N     1 
ATOM   872  C CA    . LEU A 1 116 ? -3.843  13.124 -11.659 1.00 46.89  ? 111 LEU A CA    1 
ATOM   873  C C     . LEU A 1 116 ? -4.015  11.942 -10.717 1.00 43.50  ? 111 LEU A C     1 
ATOM   874  O O     . LEU A 1 116 ? -4.921  11.941 -9.876  1.00 45.49  ? 111 LEU A O     1 
ATOM   875  C CB    . LEU A 1 116 ? -3.596  14.409 -10.869 1.00 43.35  ? 111 LEU A CB    1 
ATOM   876  C CG    . LEU A 1 116 ? -2.309  14.361 -10.039 1.00 38.96  ? 111 LEU A CG    1 
ATOM   877  C CD1   . LEU A 1 116 ? -1.136  13.894 -10.889 1.00 38.92  ? 111 LEU A CD1   1 
ATOM   878  C CD2   . LEU A 1 116 ? -2.000  15.704 -9.408  1.00 41.42  ? 111 LEU A CD2   1 
ATOM   879  N N     . TRP A 1 117 ? -3.151  10.943 -10.861 1.00 46.66  ? 112 TRP A N     1 
ATOM   880  C CA    . TRP A 1 117 ? -3.203  9.730  -10.052 1.00 46.23  ? 112 TRP A CA    1 
ATOM   881  C C     . TRP A 1 117 ? -2.164  9.837  -8.942  1.00 45.80  ? 112 TRP A C     1 
ATOM   882  O O     . TRP A 1 117 ? -0.964  9.681  -9.188  1.00 46.47  ? 112 TRP A O     1 
ATOM   883  C CB    . TRP A 1 117 ? -2.960  8.494  -10.915 1.00 50.12  ? 112 TRP A CB    1 
ATOM   884  C CG    . TRP A 1 117 ? -3.977  8.307  -11.997 1.00 53.61  ? 112 TRP A CG    1 
ATOM   885  C CD1   . TRP A 1 117 ? -3.995  8.913  -13.220 1.00 52.62  ? 112 TRP A CD1   1 
ATOM   886  C CD2   . TRP A 1 117 ? -5.126  7.453  -11.956 1.00 55.83  ? 112 TRP A CD2   1 
ATOM   887  N NE1   . TRP A 1 117 ? -5.085  8.490  -13.942 1.00 51.82  ? 112 TRP A NE1   1 
ATOM   888  C CE2   . TRP A 1 117 ? -5.795  7.593  -13.188 1.00 55.64  ? 112 TRP A CE2   1 
ATOM   889  C CE3   . TRP A 1 117 ? -5.654  6.584  -10.997 1.00 51.87  ? 112 TRP A CE3   1 
ATOM   890  C CZ2   . TRP A 1 117 ? -6.965  6.897  -13.486 1.00 56.86  ? 112 TRP A CZ2   1 
ATOM   891  C CZ3   . TRP A 1 117 ? -6.815  5.893  -11.294 1.00 51.71  ? 112 TRP A CZ3   1 
ATOM   892  C CH2   . TRP A 1 117 ? -7.457  6.054  -12.528 1.00 53.99  ? 112 TRP A CH2   1 
ATOM   893  N N     . LEU A 1 118 ? -2.625  10.103 -7.722  1.00 51.28  ? 113 LEU A N     1 
ATOM   894  C CA    . LEU A 1 118 ? -1.748  10.160 -6.554  1.00 41.62  ? 113 LEU A CA    1 
ATOM   895  C C     . LEU A 1 118 ? -1.698  8.766  -5.941  1.00 40.37  ? 113 LEU A C     1 
ATOM   896  O O     . LEU A 1 118 ? -2.605  8.363  -5.208  1.00 42.93  ? 113 LEU A O     1 
ATOM   897  C CB    . LEU A 1 118 ? -2.240  11.199 -5.554  1.00 38.43  ? 113 LEU A CB    1 
ATOM   898  C CG    . LEU A 1 118 ? -2.471  12.614 -6.088  1.00 38.43  ? 113 LEU A CG    1 
ATOM   899  C CD1   . LEU A 1 118 ? -3.037  13.508 -4.999  1.00 39.33  ? 113 LEU A CD1   1 
ATOM   900  C CD2   . LEU A 1 118 ? -1.187  13.196 -6.648  1.00 38.43  ? 113 LEU A CD2   1 
ATOM   901  N N     . LEU A 1 119 ? -0.636  8.025  -6.245  1.00 43.84  ? 114 LEU A N     1 
ATOM   902  C CA    . LEU A 1 119 ? -0.460  6.660  -5.765  1.00 41.99  ? 114 LEU A CA    1 
ATOM   903  C C     . LEU A 1 119 ? 0.517   6.671  -4.596  1.00 40.42  ? 114 LEU A C     1 
ATOM   904  O O     . LEU A 1 119 ? 1.666   7.101  -4.748  1.00 45.10  ? 114 LEU A O     1 
ATOM   905  C CB    . LEU A 1 119 ? 0.046   5.756  -6.889  1.00 44.95  ? 114 LEU A CB    1 
ATOM   906  C CG    . LEU A 1 119 ? -0.606  5.982  -8.256  1.00 44.94  ? 114 LEU A CG    1 
ATOM   907  C CD1   . LEU A 1 119 ? 0.131   5.212  -9.341  1.00 44.84  ? 114 LEU A CD1   1 
ATOM   908  C CD2   . LEU A 1 119 ? -2.080  5.602  -8.227  1.00 41.53  ? 114 LEU A CD2   1 
ATOM   909  N N     . SER A 1 120 ? 0.065   6.195  -3.436  1.00 45.80  ? 115 SER A N     1 
ATOM   910  C CA    . SER A 1 120 ? 0.856   6.287  -2.217  1.00 43.76  ? 115 SER A CA    1 
ATOM   911  C C     . SER A 1 120 ? 0.657   5.047  -1.357  1.00 44.77  ? 115 SER A C     1 
ATOM   912  O O     . SER A 1 120 ? -0.355  4.347  -1.456  1.00 48.72  ? 115 SER A O     1 
ATOM   913  C CB    . SER A 1 120 ? 0.493   7.540  -1.409  1.00 45.96  ? 115 SER A CB    1 
ATOM   914  O OG    . SER A 1 120 ? -0.806  7.428  -0.853  1.00 43.88  ? 115 SER A OG    1 
ATOM   915  N N     . THR A 1 121 ? 1.653   4.782  -0.510  1.00 49.49  ? 116 THR A N     1 
ATOM   916  C CA    . THR A 1 121 ? 1.575   3.748  0.514   1.00 46.29  ? 116 THR A CA    1 
ATOM   917  C C     . THR A 1 121 ? 2.138   4.295  1.817   1.00 50.21  ? 116 THR A C     1 
ATOM   918  O O     . THR A 1 121 ? 3.105   5.062  1.819   1.00 49.22  ? 116 THR A O     1 
ATOM   919  C CB    . THR A 1 121 ? 2.352   2.471  0.142   1.00 39.03  ? 116 THR A CB    1 
ATOM   920  O OG1   . THR A 1 121 ? 3.760   2.730  0.196   1.00 46.28  ? 116 THR A OG1   1 
ATOM   921  C CG2   . THR A 1 121 ? 1.985   1.983  -1.245  1.00 45.41  ? 116 THR A CG2   1 
ATOM   922  N N     . GLY A 1 122 ? 1.526   3.885  2.927   1.00 48.93  ? 117 GLY A N     1 
ATOM   923  C CA    . GLY A 1 122 ? 2.047   4.248  4.238   1.00 42.45  ? 117 GLY A CA    1 
ATOM   924  C C     . GLY A 1 122 ? 2.074   5.750  4.441   1.00 42.85  ? 117 GLY A C     1 
ATOM   925  O O     . GLY A 1 122 ? 1.087   6.453  4.197   1.00 45.67  ? 117 GLY A O     1 
ATOM   926  N N     . THR A 1 123 ? 3.223   6.257  4.895   1.00 48.88  ? 118 THR A N     1 
ATOM   927  C CA    . THR A 1 123 ? 3.392   7.691  5.101   1.00 43.25  ? 118 THR A CA    1 
ATOM   928  C C     . THR A 1 123 ? 3.565   8.462  3.802   1.00 44.52  ? 118 THR A C     1 
ATOM   929  O O     . THR A 1 123 ? 3.692   9.691  3.851   1.00 49.14  ? 118 THR A O     1 
ATOM   930  C CB    . THR A 1 123 ? 4.588   7.961  6.017   1.00 45.50  ? 118 THR A CB    1 
ATOM   931  O OG1   . THR A 1 123 ? 5.772   7.394  5.443   1.00 50.57  ? 118 THR A OG1   1 
ATOM   932  C CG2   . THR A 1 123 ? 4.354   7.362  7.393   1.00 43.57  ? 118 THR A CG2   1 
ATOM   933  N N     . GLY A 1 124 ? 3.574   7.787  2.652   1.00 44.14  ? 119 GLY A N     1 
ATOM   934  C CA    . GLY A 1 124 ? 3.597   8.482  1.377   1.00 41.52  ? 119 GLY A CA    1 
ATOM   935  C C     . GLY A 1 124 ? 2.345   9.284  1.090   1.00 43.79  ? 119 GLY A C     1 
ATOM   936  O O     . GLY A 1 124 ? 2.300   9.993  0.077   1.00 45.22  ? 119 GLY A O     1 
ATOM   937  N N     . LEU A 1 125 ? 1.328   9.179  1.947   1.00 43.19  ? 120 LEU A N     1 
ATOM   938  C CA    . LEU A 1 125 ? 0.135   10.004 1.825   1.00 38.43  ? 120 LEU A CA    1 
ATOM   939  C C     . LEU A 1 125 ? 0.399   11.456 2.205   1.00 38.47  ? 120 LEU A C     1 
ATOM   940  O O     . LEU A 1 125 ? -0.365  12.338 1.799   1.00 44.62  ? 120 LEU A O     1 
ATOM   941  C CB    . LEU A 1 125 ? -0.979  9.424  2.701   1.00 38.43  ? 120 LEU A CB    1 
ATOM   942  C CG    . LEU A 1 125 ? -2.341  10.119 2.746   1.00 42.95  ? 120 LEU A CG    1 
ATOM   943  C CD1   . LEU A 1 125 ? -3.035  10.045 1.394   1.00 42.00  ? 120 LEU A CD1   1 
ATOM   944  C CD2   . LEU A 1 125 ? -3.207  9.511  3.839   1.00 39.35  ? 120 LEU A CD2   1 
ATOM   945  N N     . ALA A 1 126 ? 1.469   11.720 2.959   1.00 39.67  ? 121 ALA A N     1 
ATOM   946  C CA    . ALA A 1 126 ? 1.777   13.042 3.495   1.00 39.42  ? 121 ALA A CA    1 
ATOM   947  C C     . ALA A 1 126 ? 1.822   14.124 2.415   1.00 43.66  ? 121 ALA A C     1 
ATOM   948  O O     . ALA A 1 126 ? 1.082   15.109 2.523   1.00 46.07  ? 121 ALA A O     1 
ATOM   949  C CB    . ALA A 1 126 ? 3.095   13.007 4.277   1.00 38.43  ? 121 ALA A CB    1 
ATOM   950  N N     . PRO A 1 127 ? 2.643   13.998 1.362   1.00 45.95  ? 122 PRO A N     1 
ATOM   951  C CA    . PRO A 1 127 ? 2.708   15.091 0.377   1.00 40.63  ? 122 PRO A CA    1 
ATOM   952  C C     . PRO A 1 127 ? 1.420   15.272 -0.404  1.00 41.67  ? 122 PRO A C     1 
ATOM   953  O O     . PRO A 1 127 ? 1.174   16.373 -0.913  1.00 44.63  ? 122 PRO A O     1 
ATOM   954  C CB    . PRO A 1 127 ? 3.859   14.672 -0.543  1.00 44.16  ? 122 PRO A CB    1 
ATOM   955  C CG    . PRO A 1 127 ? 3.864   13.200 -0.471  1.00 39.60  ? 122 PRO A CG    1 
ATOM   956  C CD    . PRO A 1 127 ? 3.446   12.839 0.925   1.00 41.52  ? 122 PRO A CD    1 
ATOM   957  N N     . PHE A 1 128 ? 0.590   14.234 -0.512  1.00 42.62  ? 123 PHE A N     1 
ATOM   958  C CA    . PHE A 1 128 ? -0.674  14.354 -1.224  1.00 41.95  ? 123 PHE A CA    1 
ATOM   959  C C     . PHE A 1 128 ? -1.776  14.946 -0.358  1.00 42.49  ? 123 PHE A C     1 
ATOM   960  O O     . PHE A 1 128 ? -2.747  15.482 -0.901  1.00 46.72  ? 123 PHE A O     1 
ATOM   961  C CB    . PHE A 1 128 ? -1.097  12.988 -1.765  1.00 41.28  ? 123 PHE A CB    1 
ATOM   962  C CG    . PHE A 1 128 ? -0.075  12.357 -2.666  1.00 38.91  ? 123 PHE A CG    1 
ATOM   963  C CD1   . PHE A 1 128 ? 0.704   13.140 -3.501  1.00 38.43  ? 123 PHE A CD1   1 
ATOM   964  C CD2   . PHE A 1 128 ? 0.114   10.985 -2.673  1.00 38.43  ? 123 PHE A CD2   1 
ATOM   965  C CE1   . PHE A 1 128 ? 1.649   12.569 -4.329  1.00 38.43  ? 123 PHE A CE1   1 
ATOM   966  C CE2   . PHE A 1 128 ? 1.058   10.408 -3.500  1.00 38.75  ? 123 PHE A CE2   1 
ATOM   967  C CZ    . PHE A 1 128 ? 1.827   11.201 -4.329  1.00 38.43  ? 123 PHE A CZ    1 
ATOM   968  N N     . LEU A 1 129 ? -1.650  14.863 0.970   1.00 42.94  ? 124 LEU A N     1 
ATOM   969  C CA    . LEU A 1 129 ? -2.562  15.597 1.840   1.00 39.50  ? 124 LEU A CA    1 
ATOM   970  C C     . LEU A 1 129 ? -2.448  17.097 1.612   1.00 42.39  ? 124 LEU A C     1 
ATOM   971  O O     . LEU A 1 129 ? -3.418  17.835 1.817   1.00 46.33  ? 124 LEU A O     1 
ATOM   972  C CB    . LEU A 1 129 ? -2.283  15.258 3.304   1.00 39.76  ? 124 LEU A CB    1 
ATOM   973  C CG    . LEU A 1 129 ? -2.579  13.824 3.745   1.00 38.81  ? 124 LEU A CG    1 
ATOM   974  C CD1   . LEU A 1 129 ? -1.887  13.528 5.061   1.00 38.43  ? 124 LEU A CD1   1 
ATOM   975  C CD2   . LEU A 1 129 ? -4.078  13.598 3.864   1.00 40.08  ? 124 LEU A CD2   1 
ATOM   976  N N     . SER A 1 130 ? -1.271  17.563 1.190   1.00 46.41  ? 125 SER A N     1 
ATOM   977  C CA    . SER A 1 130 ? -1.102  18.960 0.810   1.00 41.49  ? 125 SER A CA    1 
ATOM   978  C C     . SER A 1 130 ? -1.629  19.223 -0.595  1.00 43.27  ? 125 SER A C     1 
ATOM   979  O O     . SER A 1 130 ? -2.155  20.307 -0.871  1.00 50.03  ? 125 SER A O     1 
ATOM   980  C CB    . SER A 1 130 ? 0.374   19.350 0.900   1.00 40.04  ? 125 SER A CB    1 
ATOM   981  O OG    . SER A 1 130 ? 0.567   20.707 0.545   1.00 46.05  ? 125 SER A OG    1 
ATOM   982  N N     . ILE A 1 131 ? -1.499  18.243 -1.490  1.00 43.14  ? 126 ILE A N     1 
ATOM   983  C CA    . ILE A 1 131 ? -1.891  18.449 -2.881  1.00 41.88  ? 126 ILE A CA    1 
ATOM   984  C C     . ILE A 1 131 ? -3.409  18.442 -3.017  1.00 44.93  ? 126 ILE A C     1 
ATOM   985  O O     . ILE A 1 131 ? -3.995  19.346 -3.622  1.00 49.86  ? 126 ILE A O     1 
ATOM   986  C CB    . ILE A 1 131 ? -1.232  17.391 -3.783  1.00 39.54  ? 126 ILE A CB    1 
ATOM   987  C CG1   . ILE A 1 131 ? 0.264   17.679 -3.915  1.00 38.43  ? 126 ILE A CG1   1 
ATOM   988  C CG2   . ILE A 1 131 ? -1.894  17.370 -5.151  1.00 42.00  ? 126 ILE A CG2   1 
ATOM   989  C CD1   . ILE A 1 131 ? 1.065   16.533 -4.474  1.00 39.28  ? 126 ILE A CD1   1 
ATOM   990  N N     . ILE A 1 132 ? -4.070  17.428 -2.450  1.00 46.84  ? 127 ILE A N     1 
ATOM   991  C CA    . ILE A 1 132 ? -5.528  17.385 -2.489  1.00 44.89  ? 127 ILE A CA    1 
ATOM   992  C C     . ILE A 1 132 ? -6.137  18.561 -1.742  1.00 46.18  ? 127 ILE A C     1 
ATOM   993  O O     . ILE A 1 132 ? -7.299  18.908 -1.977  1.00 45.30  ? 127 ILE A O     1 
ATOM   994  C CB    . ILE A 1 132 ? -6.059  16.049 -1.926  1.00 45.51  ? 127 ILE A CB    1 
ATOM   995  C CG1   . ILE A 1 132 ? -5.907  16.007 -0.403  1.00 43.50  ? 127 ILE A CG1   1 
ATOM   996  C CG2   . ILE A 1 132 ? -5.360  14.873 -2.585  1.00 46.28  ? 127 ILE A CG2   1 
ATOM   997  C CD1   . ILE A 1 132 ? -6.460  14.753 0.231   1.00 40.06  ? 127 ILE A CD1   1 
ATOM   998  N N     . ARG A 1 133 ? -5.380  19.185 -0.838  1.00 45.95  ? 128 ARG A N     1 
ATOM   999  C CA    . ARG A 1 133 ? -5.794  20.416 -0.180  1.00 41.57  ? 128 ARG A CA    1 
ATOM   1000 C C     . ARG A 1 133 ? -5.190  21.650 -0.842  1.00 47.38  ? 128 ARG A C     1 
ATOM   1001 O O     . ARG A 1 133 ? -4.977  22.672 -0.182  1.00 49.48  ? 128 ARG A O     1 
ATOM   1002 C CB    . ARG A 1 133 ? -5.443  20.373 1.307   1.00 45.73  ? 128 ARG A CB    1 
ATOM   1003 C CG    . ARG A 1 133 ? -6.287  19.392 2.102   1.00 42.69  ? 128 ARG A CG    1 
ATOM   1004 C CD    . ARG A 1 133 ? -6.092  19.570 3.598   1.00 40.75  ? 128 ARG A CD    1 
ATOM   1005 N NE    . ARG A 1 133 ? -4.816  19.029 4.051   1.00 44.93  ? 128 ARG A NE    1 
ATOM   1006 C CZ    . ARG A 1 133 ? -4.471  18.895 5.324   1.00 45.29  ? 128 ARG A CZ    1 
ATOM   1007 N NH1   . ARG A 1 133 ? -5.287  19.252 6.303   1.00 55.46  ? 128 ARG A NH1   1 
ATOM   1008 N NH2   . ARG A 1 133 ? -3.278  18.390 5.623   1.00 44.46  ? 128 ARG A NH2   1 
ATOM   1009 N N     . ASP A 1 134 ? -4.913  21.568 -2.140  1.00 47.89  ? 129 ASP A N     1 
ATOM   1010 C CA    . ASP A 1 134 ? -4.457  22.699 -2.935  1.00 47.88  ? 129 ASP A CA    1 
ATOM   1011 C C     . ASP A 1 134 ? -5.505  22.997 -3.997  1.00 45.96  ? 129 ASP A C     1 
ATOM   1012 O O     . ASP A 1 134 ? -5.986  22.081 -4.672  1.00 47.93  ? 129 ASP A O     1 
ATOM   1013 C CB    . ASP A 1 134 ? -3.103  22.408 -3.589  1.00 45.30  ? 129 ASP A CB    1 
ATOM   1014 C CG    . ASP A 1 134 ? -2.458  23.648 -4.182  1.00 46.19  ? 129 ASP A CG    1 
ATOM   1015 O OD1   . ASP A 1 134 ? -3.062  24.738 -4.101  1.00 50.06  ? 129 ASP A OD1   1 
ATOM   1016 O OD2   . ASP A 1 134 ? -1.343  23.530 -4.734  1.00 47.09  ? 129 ASP A OD2   1 
ATOM   1017 N N     . LEU A 1 135 ? -5.863  24.275 -4.136  1.00 47.07  ? 130 LEU A N     1 
ATOM   1018 C CA    . LEU A 1 135 ? -6.840  24.659 -5.149  1.00 49.48  ? 130 LEU A CA    1 
ATOM   1019 C C     . LEU A 1 135 ? -6.312  24.415 -6.557  1.00 49.45  ? 130 LEU A C     1 
ATOM   1020 O O     . LEU A 1 135 ? -7.088  24.098 -7.466  1.00 51.66  ? 130 LEU A O     1 
ATOM   1021 C CB    . LEU A 1 135 ? -7.225  26.129 -4.965  1.00 53.49  ? 130 LEU A CB    1 
ATOM   1022 C CG    . LEU A 1 135 ? -7.761  26.898 -6.175  1.00 51.56  ? 130 LEU A CG    1 
ATOM   1023 C CD1   . LEU A 1 135 ? -9.168  26.443 -6.538  1.00 53.43  ? 130 LEU A CD1   1 
ATOM   1024 C CD2   . LEU A 1 135 ? -7.723  28.398 -5.923  1.00 54.09  ? 130 LEU A CD2   1 
ATOM   1025 N N     . GLU A 1 136 ? -4.996  24.530 -6.747  1.00 51.10  ? 131 GLU A N     1 
ATOM   1026 C CA    . GLU A 1 136 ? -4.422  24.464 -8.087  1.00 51.25  ? 131 GLU A CA    1 
ATOM   1027 C C     . GLU A 1 136 ? -4.583  23.086 -8.717  1.00 49.86  ? 131 GLU A C     1 
ATOM   1028 O O     . GLU A 1 136 ? -4.759  22.988 -9.937  1.00 52.24  ? 131 GLU A O     1 
ATOM   1029 C CB    . GLU A 1 136 ? -2.945  24.855 -8.036  1.00 49.97  ? 131 GLU A CB    1 
ATOM   1030 C CG    . GLU A 1 136 ? -2.309  25.078 -9.393  1.00 49.56  ? 131 GLU A CG    1 
ATOM   1031 C CD    . GLU A 1 136 ? -0.877  25.566 -9.289  1.00 57.74  ? 131 GLU A CD    1 
ATOM   1032 O OE1   . GLU A 1 136 ? -0.449  25.933 -8.174  1.00 59.41  ? 131 GLU A OE1   1 
ATOM   1033 O OE2   . GLU A 1 136 ? -0.181  25.587 -10.325 1.00 62.77  ? 131 GLU A OE2   1 
ATOM   1034 N N     . VAL A 1 137 ? -4.532  22.016 -7.916  1.00 52.45  ? 132 VAL A N     1 
ATOM   1035 C CA    . VAL A 1 137 ? -4.616  20.670 -8.477  1.00 44.95  ? 132 VAL A CA    1 
ATOM   1036 C C     . VAL A 1 137 ? -5.982  20.428 -9.105  1.00 45.92  ? 132 VAL A C     1 
ATOM   1037 O O     . VAL A 1 137 ? -6.107  19.644 -10.054 1.00 51.91  ? 132 VAL A O     1 
ATOM   1038 C CB    . VAL A 1 137 ? -4.295  19.613 -7.402  1.00 44.74  ? 132 VAL A CB    1 
ATOM   1039 C CG1   . VAL A 1 137 ? -5.442  19.478 -6.414  1.00 47.22  ? 132 VAL A CG1   1 
ATOM   1040 C CG2   . VAL A 1 137 ? -3.997  18.275 -8.053  1.00 42.36  ? 132 VAL A CG2   1 
ATOM   1041 N N     . TYR A 1 138 ? -7.021  21.096 -8.605  1.00 48.64  ? 133 TYR A N     1 
ATOM   1042 C CA    . TYR A 1 138 ? -8.355  20.946 -9.165  1.00 46.81  ? 133 TYR A CA    1 
ATOM   1043 C C     . TYR A 1 138 ? -8.607  21.891 -10.330 1.00 49.76  ? 133 TYR A C     1 
ATOM   1044 O O     . TYR A 1 138 ? -9.541  21.661 -11.107 1.00 46.71  ? 133 TYR A O     1 
ATOM   1045 C CB    . TYR A 1 138 ? -9.408  21.159 -8.074  1.00 47.92  ? 133 TYR A CB    1 
ATOM   1046 C CG    . TYR A 1 138 ? -9.222  20.243 -6.884  1.00 48.54  ? 133 TYR A CG    1 
ATOM   1047 C CD1   . TYR A 1 138 ? -9.288  18.863 -7.029  1.00 46.99  ? 133 TYR A CD1   1 
ATOM   1048 C CD2   . TYR A 1 138 ? -8.964  20.757 -5.620  1.00 45.91  ? 133 TYR A CD2   1 
ATOM   1049 C CE1   . TYR A 1 138 ? -9.113  18.021 -5.947  1.00 42.42  ? 133 TYR A CE1   1 
ATOM   1050 C CE2   . TYR A 1 138 ? -8.787  19.923 -4.533  1.00 46.90  ? 133 TYR A CE2   1 
ATOM   1051 C CZ    . TYR A 1 138 ? -8.862  18.556 -4.702  1.00 46.99  ? 133 TYR A CZ    1 
ATOM   1052 O OH    . TYR A 1 138 ? -8.685  17.723 -3.620  1.00 47.21  ? 133 TYR A OH    1 
ATOM   1053 N N     . GLU A 1 139 ? -7.795  22.940 -10.471 1.00 52.60  ? 134 GLU A N     1 
ATOM   1054 C CA    . GLU A 1 139 ? -7.854  23.778 -11.661 1.00 49.92  ? 134 GLU A CA    1 
ATOM   1055 C C     . GLU A 1 139 ? -7.121  23.142 -12.833 1.00 52.36  ? 134 GLU A C     1 
ATOM   1056 O O     . GLU A 1 139 ? -7.531  23.317 -13.986 1.00 55.86  ? 134 GLU A O     1 
ATOM   1057 C CB    . GLU A 1 139 ? -7.260  25.156 -11.367 1.00 48.64  ? 134 GLU A CB    1 
ATOM   1058 C CG    . GLU A 1 139 ? -8.121  26.039 -10.484 1.00 53.56  ? 134 GLU A CG    1 
ATOM   1059 C CD    . GLU A 1 139 ? -7.517  27.415 -10.281 1.00 57.99  ? 134 GLU A CD    1 
ATOM   1060 O OE1   . GLU A 1 139 ? -6.287  27.556 -10.446 1.00 61.72  ? 134 GLU A OE1   1 
ATOM   1061 O OE2   . GLU A 1 139 ? -8.272  28.356 -9.958  1.00 64.00  ? 134 GLU A OE2   1 
ATOM   1062 N N     . ARG A 1 140 ? -6.045  22.404 -12.560 1.00 49.68  ? 135 ARG A N     1 
ATOM   1063 C CA    . ARG A 1 140 ? -5.245  21.787 -13.610 1.00 51.70  ? 135 ARG A CA    1 
ATOM   1064 C C     . ARG A 1 140 ? -5.749  20.407 -14.006 1.00 53.77  ? 135 ARG A C     1 
ATOM   1065 O O     . ARG A 1 140 ? -5.578  20.003 -15.163 1.00 54.08  ? 135 ARG A O     1 
ATOM   1066 C CB    . ARG A 1 140 ? -3.784  21.679 -13.164 1.00 51.89  ? 135 ARG A CB    1 
ATOM   1067 C CG    . ARG A 1 140 ? -3.173  22.990 -12.700 1.00 47.84  ? 135 ARG A CG    1 
ATOM   1068 C CD    . ARG A 1 140 ? -1.795  22.773 -12.094 1.00 44.93  ? 135 ARG A CD    1 
ATOM   1069 N NE    . ARG A 1 140 ? -0.758  22.655 -13.112 1.00 52.63  ? 135 ARG A NE    1 
ATOM   1070 C CZ    . ARG A 1 140 ? 0.411   23.279 -13.065 1.00 51.36  ? 135 ARG A CZ    1 
ATOM   1071 N NH1   . ARG A 1 140 ? 0.730   24.074 -12.057 1.00 48.04  ? 135 ARG A NH1   1 
ATOM   1072 N NH2   . ARG A 1 140 ? 1.283   23.098 -14.053 1.00 54.34  ? 135 ARG A NH2   1 
ATOM   1073 N N     . PHE A 1 141 ? -6.366  19.672 -13.081 1.00 51.81  ? 136 PHE A N     1 
ATOM   1074 C CA    . PHE A 1 141 ? -6.784  18.299 -13.329 1.00 46.86  ? 136 PHE A CA    1 
ATOM   1075 C C     . PHE A 1 141 ? -8.278  18.167 -13.079 1.00 50.12  ? 136 PHE A C     1 
ATOM   1076 O O     . PHE A 1 141 ? -8.779  18.600 -12.036 1.00 52.56  ? 136 PHE A O     1 
ATOM   1077 C CB    . PHE A 1 141 ? -6.006  17.323 -12.441 1.00 47.15  ? 136 PHE A CB    1 
ATOM   1078 C CG    . PHE A 1 141 ? -4.544  17.236 -12.775 1.00 45.39  ? 136 PHE A CG    1 
ATOM   1079 C CD1   . PHE A 1 141 ? -4.112  16.523 -13.882 1.00 46.31  ? 136 PHE A CD1   1 
ATOM   1080 C CD2   . PHE A 1 141 ? -3.602  17.877 -11.988 1.00 44.36  ? 136 PHE A CD2   1 
ATOM   1081 C CE1   . PHE A 1 141 ? -2.767  16.447 -14.193 1.00 43.22  ? 136 PHE A CE1   1 
ATOM   1082 C CE2   . PHE A 1 141 ? -2.257  17.806 -12.294 1.00 44.28  ? 136 PHE A CE2   1 
ATOM   1083 C CZ    . PHE A 1 141 ? -1.838  17.089 -13.397 1.00 44.67  ? 136 PHE A CZ    1 
ATOM   1084 N N     . GLU A 1 142 ? -8.985  17.570 -14.042 1.00 49.51  ? 137 GLU A N     1 
ATOM   1085 C CA    . GLU A 1 142 ? -10.414 17.331 -13.871 1.00 52.47  ? 137 GLU A CA    1 
ATOM   1086 C C     . GLU A 1 142 ? -10.673 16.338 -12.746 1.00 53.14  ? 137 GLU A C     1 
ATOM   1087 O O     . GLU A 1 142 ? -11.620 16.500 -11.968 1.00 54.64  ? 137 GLU A O     1 
ATOM   1088 C CB    . GLU A 1 142 ? -11.025 16.822 -15.177 1.00 56.35  ? 137 GLU A CB    1 
ATOM   1089 C CG    . GLU A 1 142 ? -10.801 17.727 -16.375 1.00 60.90  ? 137 GLU A CG    1 
ATOM   1090 C CD    . GLU A 1 142 ? -11.477 17.202 -17.626 1.00 69.55  ? 137 GLU A CD    1 
ATOM   1091 O OE1   . GLU A 1 142 ? -12.187 16.177 -17.535 1.00 70.12  ? 137 GLU A OE1   1 
ATOM   1092 O OE2   . GLU A 1 142 ? -11.298 17.812 -18.700 1.00 75.18  ? 137 GLU A OE2   1 
ATOM   1093 N N     . LYS A 1 143 ? -9.842  15.303 -12.645 1.00 52.42  ? 138 LYS A N     1 
ATOM   1094 C CA    . LYS A 1 143 ? -9.991  14.269 -11.632 1.00 45.16  ? 138 LYS A CA    1 
ATOM   1095 C C     . LYS A 1 143 ? -8.675  14.087 -10.893 1.00 49.12  ? 138 LYS A C     1 
ATOM   1096 O O     . LYS A 1 143 ? -7.615  13.985 -11.520 1.00 49.56  ? 138 LYS A O     1 
ATOM   1097 C CB    . LYS A 1 143 ? -10.435 12.942 -12.256 1.00 43.75  ? 138 LYS A CB    1 
ATOM   1098 C CG    . LYS A 1 143 ? -11.853 12.952 -12.803 1.00 50.21  ? 138 LYS A CG    1 
ATOM   1099 C CD    . LYS A 1 143 ? -12.872 12.982 -11.676 1.00 48.41  ? 138 LYS A CD    1 
ATOM   1100 C CE    . LYS A 1 143 ? -14.287 13.111 -12.214 1.00 50.71  ? 138 LYS A CE    1 
ATOM   1101 N NZ    . LYS A 1 143 ? -15.284 13.252 -11.117 1.00 59.11  ? 138 LYS A NZ    1 
ATOM   1102 N N     . VAL A 1 144 ? -8.747  14.052 -9.565  1.00 48.95  ? 139 VAL A N     1 
ATOM   1103 C CA    . VAL A 1 144 ? -7.608  13.741 -8.709  1.00 47.16  ? 139 VAL A CA    1 
ATOM   1104 C C     . VAL A 1 144 ? -7.928  12.448 -7.976  1.00 48.89  ? 139 VAL A C     1 
ATOM   1105 O O     . VAL A 1 144 ? -8.842  12.410 -7.144  1.00 49.82  ? 139 VAL A O     1 
ATOM   1106 C CB    . VAL A 1 144 ? -7.303  14.873 -7.716  1.00 46.47  ? 139 VAL A CB    1 
ATOM   1107 C CG1   . VAL A 1 144 ? -6.078  14.524 -6.886  1.00 45.02  ? 139 VAL A CG1   1 
ATOM   1108 C CG2   . VAL A 1 144 ? -7.098  16.186 -8.454  1.00 46.64  ? 139 VAL A CG2   1 
ATOM   1109 N N     . ILE A 1 145 ? -7.184  11.392 -8.287  1.00 52.14  ? 140 ILE A N     1 
ATOM   1110 C CA    . ILE A 1 145 ? -7.415  10.066 -7.728  1.00 44.93  ? 140 ILE A CA    1 
ATOM   1111 C C     . ILE A 1 145 ? -6.351  9.824  -6.667  1.00 44.39  ? 140 ILE A C     1 
ATOM   1112 O O     . ILE A 1 145 ? -5.165  9.674  -6.985  1.00 47.89  ? 140 ILE A O     1 
ATOM   1113 C CB    . ILE A 1 145 ? -7.387  8.974  -8.806  1.00 44.17  ? 140 ILE A CB    1 
ATOM   1114 C CG1   . ILE A 1 145 ? -8.237  9.383  -10.013 1.00 48.94  ? 140 ILE A CG1   1 
ATOM   1115 C CG2   . ILE A 1 145 ? -7.873  7.652  -8.235  1.00 45.05  ? 140 ILE A CG2   1 
ATOM   1116 C CD1   . ILE A 1 145 ? -7.438  9.972  -11.161 1.00 45.27  ? 140 ILE A CD1   1 
ATOM   1117 N N     . LEU A 1 146 ? -6.771  9.788  -5.404  1.00 45.80  ? 141 LEU A N     1 
ATOM   1118 C CA    . LEU A 1 146 ? -5.869  9.581  -4.277  1.00 42.09  ? 141 LEU A CA    1 
ATOM   1119 C C     . LEU A 1 146 ? -5.950  8.121  -3.846  1.00 42.29  ? 141 LEU A C     1 
ATOM   1120 O O     . LEU A 1 146 ? -6.951  7.692  -3.265  1.00 46.16  ? 141 LEU A O     1 
ATOM   1121 C CB    . LEU A 1 146 ? -6.219  10.514 -3.120  1.00 42.55  ? 141 LEU A CB    1 
ATOM   1122 C CG    . LEU A 1 146 ? -5.310  10.402 -1.895  1.00 41.63  ? 141 LEU A CG    1 
ATOM   1123 C CD1   . LEU A 1 146 ? -3.869  10.704 -2.272  1.00 43.81  ? 141 LEU A CD1   1 
ATOM   1124 C CD2   . LEU A 1 146 ? -5.783  11.329 -0.792  1.00 43.74  ? 141 LEU A CD2   1 
ATOM   1125 N N     . VAL A 1 147 ? -4.894  7.363  -4.131  1.00 43.31  ? 142 VAL A N     1 
ATOM   1126 C CA    . VAL A 1 147 ? -4.807  5.954  -3.767  1.00 41.58  ? 142 VAL A CA    1 
ATOM   1127 C C     . VAL A 1 147 ? -3.873  5.821  -2.573  1.00 42.71  ? 142 VAL A C     1 
ATOM   1128 O O     . VAL A 1 147 ? -2.760  6.362  -2.582  1.00 47.96  ? 142 VAL A O     1 
ATOM   1129 C CB    . VAL A 1 147 ? -4.315  5.101  -4.949  1.00 42.91  ? 142 VAL A CB    1 
ATOM   1130 C CG1   . VAL A 1 147 ? -4.108  3.657  -4.516  1.00 46.24  ? 142 VAL A CG1   1 
ATOM   1131 C CG2   . VAL A 1 147 ? -5.299  5.182  -6.106  1.00 41.83  ? 142 VAL A CG2   1 
ATOM   1132 N N     . HIS A 1 148 ? -4.324  5.107  -1.544  1.00 44.35  ? 143 HIS A N     1 
ATOM   1133 C CA    . HIS A 1 148 ? -3.533  4.871  -0.342  1.00 46.07  ? 143 HIS A CA    1 
ATOM   1134 C C     . HIS A 1 148 ? -3.521  3.379  -0.049  1.00 41.41  ? 143 HIS A C     1 
ATOM   1135 O O     . HIS A 1 148 ? -4.581  2.772  0.129   1.00 46.12  ? 143 HIS A O     1 
ATOM   1136 C CB    . HIS A 1 148 ? -4.090  5.650  0.852   1.00 46.04  ? 143 HIS A CB    1 
ATOM   1137 C CG    . HIS A 1 148 ? -3.172  5.679  2.034   1.00 44.27  ? 143 HIS A CG    1 
ATOM   1138 N ND1   . HIS A 1 148 ? -3.632  5.713  3.333   1.00 46.57  ? 143 HIS A ND1   1 
ATOM   1139 C CD2   . HIS A 1 148 ? -1.821  5.675  2.113   1.00 40.78  ? 143 HIS A CD2   1 
ATOM   1140 C CE1   . HIS A 1 148 ? -2.603  5.731  4.161   1.00 46.12  ? 143 HIS A CE1   1 
ATOM   1141 N NE2   . HIS A 1 148 ? -1.492  5.708  3.447   1.00 44.24  ? 143 HIS A NE2   1 
ATOM   1142 N N     . GLY A 1 149 ? -2.327  2.794  -0.001  1.00 45.05  ? 144 GLY A N     1 
ATOM   1143 C CA    . GLY A 1 149 ? -2.156  1.380  0.283   1.00 41.03  ? 144 GLY A CA    1 
ATOM   1144 C C     . GLY A 1 149 ? -1.528  1.180  1.650   1.00 44.94  ? 144 GLY A C     1 
ATOM   1145 O O     . GLY A 1 149 ? -0.514  1.801  1.976   1.00 47.22  ? 144 GLY A O     1 
ATOM   1146 N N     . VAL A 1 150 ? -2.146  0.305  2.444   1.00 47.95  ? 145 VAL A N     1 
ATOM   1147 C CA    . VAL A 1 150 ? -1.692  0.000  3.795   1.00 48.29  ? 145 VAL A CA    1 
ATOM   1148 C C     . VAL A 1 150 ? -1.829  -1.498 4.033   1.00 48.93  ? 145 VAL A C     1 
ATOM   1149 O O     . VAL A 1 150 ? -2.414  -2.230 3.232   1.00 48.58  ? 145 VAL A O     1 
ATOM   1150 C CB    . VAL A 1 150 ? -2.476  0.785  4.868   1.00 48.93  ? 145 VAL A CB    1 
ATOM   1151 C CG1   . VAL A 1 150 ? -2.077  2.255  4.858   1.00 47.14  ? 145 VAL A CG1   1 
ATOM   1152 C CG2   . VAL A 1 150 ? -3.968  0.625  4.650   1.00 47.45  ? 145 VAL A CG2   1 
ATOM   1153 N N     . ARG A 1 151 ? -1.278  -1.948 5.161   1.00 51.09  ? 146 ARG A N     1 
ATOM   1154 C CA    . ARG A 1 151 ? -1.349  -3.352 5.542   1.00 47.20  ? 146 ARG A CA    1 
ATOM   1155 C C     . ARG A 1 151 ? -2.526  -3.652 6.459   1.00 46.74  ? 146 ARG A C     1 
ATOM   1156 O O     . ARG A 1 151 ? -3.101  -4.744 6.378   1.00 49.49  ? 146 ARG A O     1 
ATOM   1157 C CB    . ARG A 1 151 ? -0.050  -3.779 6.230   1.00 51.91  ? 146 ARG A CB    1 
ATOM   1158 C CG    . ARG A 1 151 ? 1.140   -3.895 5.296   1.00 53.51  ? 146 ARG A CG    1 
ATOM   1159 C CD    . ARG A 1 151 ? 2.403   -4.212 6.072   1.00 57.94  ? 146 ARG A CD    1 
ATOM   1160 N NE    . ARG A 1 151 ? 3.453   -3.233 5.819   1.00 55.12  ? 146 ARG A NE    1 
ATOM   1161 C CZ    . ARG A 1 151 ? 3.803   -2.276 6.667   1.00 56.81  ? 146 ARG A CZ    1 
ATOM   1162 N NH1   . ARG A 1 151 ? 3.196   -2.128 7.834   1.00 61.06  ? 146 ARG A NH1   1 
ATOM   1163 N NH2   . ARG A 1 151 ? 4.788   -1.445 6.337   1.00 62.96  ? 146 ARG A NH2   1 
ATOM   1164 N N     . GLN A 1 152 ? -2.895  -2.712 7.326   1.00 48.26  ? 147 GLN A N     1 
ATOM   1165 C CA    . GLN A 1 152 ? -4.005  -2.885 8.249   1.00 49.07  ? 147 GLN A CA    1 
ATOM   1166 C C     . GLN A 1 152 ? -4.975  -1.722 8.097   1.00 47.41  ? 147 GLN A C     1 
ATOM   1167 O O     . GLN A 1 152 ? -4.619  -0.649 7.606   1.00 51.82  ? 147 GLN A O     1 
ATOM   1168 C CB    . GLN A 1 152 ? -3.520  -2.986 9.701   1.00 47.77  ? 147 GLN A CB    1 
ATOM   1169 C CG    . GLN A 1 152 ? -3.085  -4.381 10.116  1.00 48.76  ? 147 GLN A CG    1 
ATOM   1170 C CD    . GLN A 1 152 ? -1.580  -4.529 10.181  1.00 56.26  ? 147 GLN A CD    1 
ATOM   1171 O OE1   . GLN A 1 152 ? -0.877  -3.643 10.667  1.00 59.05  ? 147 GLN A OE1   1 
ATOM   1172 N NE2   . GLN A 1 152 ? -1.075  -5.654 9.688   1.00 57.64  ? 147 GLN A NE2   1 
ATOM   1173 N N     . VAL A 1 153 ? -6.215  -1.953 8.530   1.00 47.57  ? 148 VAL A N     1 
ATOM   1174 C CA    . VAL A 1 153 ? -7.243  -0.922 8.424   1.00 44.52  ? 148 VAL A CA    1 
ATOM   1175 C C     . VAL A 1 153 ? -6.901  0.266  9.315   1.00 47.39  ? 148 VAL A C     1 
ATOM   1176 O O     . VAL A 1 153 ? -7.152  1.423  8.954   1.00 53.60  ? 148 VAL A O     1 
ATOM   1177 C CB    . VAL A 1 153 ? -8.625  -1.512 8.765   1.00 44.13  ? 148 VAL A CB    1 
ATOM   1178 C CG1   . VAL A 1 153 ? -9.686  -0.421 8.798   1.00 40.46  ? 148 VAL A CG1   1 
ATOM   1179 C CG2   . VAL A 1 153 ? -8.999  -2.597 7.763   1.00 48.70  ? 148 VAL A CG2   1 
ATOM   1180 N N     . ALA A 1 154 ? -6.308  0.006  10.483  1.00 47.33  ? 149 ALA A N     1 
ATOM   1181 C CA    . ALA A 1 154 ? -5.955  1.085  11.399  1.00 42.33  ? 149 ALA A CA    1 
ATOM   1182 C C     . ALA A 1 154 ? -4.882  2.004  10.831  1.00 48.77  ? 149 ALA A C     1 
ATOM   1183 O O     . ALA A 1 154 ? -4.723  3.126  11.322  1.00 48.97  ? 149 ALA A O     1 
ATOM   1184 C CB    . ALA A 1 154 ? -5.493  0.509  12.737  1.00 42.25  ? 149 ALA A CB    1 
ATOM   1185 N N     . GLU A 1 155 ? -4.144  1.558  9.814   1.00 49.39  ? 150 GLU A N     1 
ATOM   1186 C CA    . GLU A 1 155 ? -3.131  2.395  9.184   1.00 47.16  ? 150 GLU A CA    1 
ATOM   1187 C C     . GLU A 1 155 ? -3.719  3.411  8.215   1.00 48.88  ? 150 GLU A C     1 
ATOM   1188 O O     . GLU A 1 155 ? -2.985  4.282  7.737   1.00 50.37  ? 150 GLU A O     1 
ATOM   1189 C CB    . GLU A 1 155 ? -2.108  1.522  8.454   1.00 48.13  ? 150 GLU A CB    1 
ATOM   1190 C CG    . GLU A 1 155 ? -1.304  0.611  9.367   1.00 51.72  ? 150 GLU A CG    1 
ATOM   1191 C CD    . GLU A 1 155 ? -0.206  -0.133 8.632   1.00 53.12  ? 150 GLU A CD    1 
ATOM   1192 O OE1   . GLU A 1 155 ? -0.335  -0.328 7.405   1.00 54.22  ? 150 GLU A OE1   1 
ATOM   1193 O OE2   . GLU A 1 155 ? 0.786   -0.523 9.282   1.00 60.62  ? 150 GLU A OE2   1 
ATOM   1194 N N     . LEU A 1 156 ? -5.015  3.324  7.915   1.00 48.13  ? 151 LEU A N     1 
ATOM   1195 C CA    . LEU A 1 156 ? -5.663  4.291  7.037   1.00 47.85  ? 151 LEU A CA    1 
ATOM   1196 C C     . LEU A 1 156 ? -5.862  5.622  7.749   1.00 45.82  ? 151 LEU A C     1 
ATOM   1197 O O     . LEU A 1 156 ? -6.984  5.965  8.133   1.00 48.01  ? 151 LEU A O     1 
ATOM   1198 C CB    . LEU A 1 156 ? -7.007  3.753  6.542   1.00 52.01  ? 151 LEU A CB    1 
ATOM   1199 C CG    . LEU A 1 156 ? -6.952  2.713  5.426   1.00 51.95  ? 151 LEU A CG    1 
ATOM   1200 C CD1   . LEU A 1 156 ? -8.341  2.167  5.135   1.00 47.53  ? 151 LEU A CD1   1 
ATOM   1201 C CD2   . LEU A 1 156 ? -6.341  3.323  4.177   1.00 49.50  ? 151 LEU A CD2   1 
ATOM   1202 N N     . ALA A 1 157 ? -4.781  6.373  7.933   1.00 47.23  ? 152 ALA A N     1 
ATOM   1203 C CA    . ALA A 1 157 ? -4.880  7.672  8.576   1.00 45.81  ? 152 ALA A CA    1 
ATOM   1204 C C     . ALA A 1 157 ? -5.628  8.655  7.682   1.00 48.96  ? 152 ALA A C     1 
ATOM   1205 O O     . ALA A 1 157 ? -5.658  8.518  6.456   1.00 58.66  ? 152 ALA A O     1 
ATOM   1206 C CB    . ALA A 1 157 ? -3.489  8.213  8.904   1.00 45.80  ? 152 ALA A CB    1 
ATOM   1207 N N     . TYR A 1 158 ? -6.251  9.646  8.318   1.00 47.07  ? 153 TYR A N     1 
ATOM   1208 C CA    . TYR A 1 158 ? -7.006  10.710 7.661   1.00 43.44  ? 153 TYR A CA    1 
ATOM   1209 C C     . TYR A 1 158 ? -8.205  10.195 6.872   1.00 46.62  ? 153 TYR A C     1 
ATOM   1210 O O     . TYR A 1 158 ? -8.822  10.965 6.127   1.00 51.79  ? 153 TYR A O     1 
ATOM   1211 C CB    . TYR A 1 158 ? -6.112  11.543 6.730   1.00 44.06  ? 153 TYR A CB    1 
ATOM   1212 C CG    . TYR A 1 158 ? -4.952  12.242 7.402   1.00 40.59  ? 153 TYR A CG    1 
ATOM   1213 C CD1   . TYR A 1 158 ? -3.745  11.586 7.611   1.00 40.81  ? 153 TYR A CD1   1 
ATOM   1214 C CD2   . TYR A 1 158 ? -5.054  13.568 7.797   1.00 41.64  ? 153 TYR A CD2   1 
ATOM   1215 C CE1   . TYR A 1 158 ? -2.679  12.226 8.215   1.00 40.11  ? 153 TYR A CE1   1 
ATOM   1216 C CE2   . TYR A 1 158 ? -3.995  14.216 8.398   1.00 41.38  ? 153 TYR A CE2   1 
ATOM   1217 C CZ    . TYR A 1 158 ? -2.810  13.542 8.604   1.00 40.92  ? 153 TYR A CZ    1 
ATOM   1218 O OH    . TYR A 1 158 ? -1.755  14.191 9.202   1.00 41.19  ? 153 TYR A OH    1 
ATOM   1219 N N     . THR A 1 159 ? -8.561  8.915  7.016   1.00 48.00  ? 154 THR A N     1 
ATOM   1220 C CA    . THR A 1 159 ? -9.575  8.334  6.140   1.00 47.36  ? 154 THR A CA    1 
ATOM   1221 C C     . THR A 1 159 ? -10.963 8.903  6.414   1.00 51.62  ? 154 THR A C     1 
ATOM   1222 O O     . THR A 1 159 ? -11.807 8.922  5.512   1.00 53.79  ? 154 THR A O     1 
ATOM   1223 C CB    . THR A 1 159 ? -9.578  6.808  6.269   1.00 46.61  ? 154 THR A CB    1 
ATOM   1224 O OG1   . THR A 1 159 ? -10.312 6.237  5.178   1.00 47.04  ? 154 THR A OG1   1 
ATOM   1225 C CG2   . THR A 1 159 ? -10.207 6.367  7.584   1.00 50.23  ? 154 THR A CG2   1 
ATOM   1226 N N     . ASP A 1 160 ? -11.220 9.373  7.636   1.00 53.65  ? 155 ASP A N     1 
ATOM   1227 C CA    . ASP A 1 160 ? -12.482 10.050 7.910   1.00 53.89  ? 155 ASP A CA    1 
ATOM   1228 C C     . ASP A 1 160 ? -12.421 11.523 7.532   1.00 57.97  ? 155 ASP A C     1 
ATOM   1229 O O     . ASP A 1 160 ? -13.453 12.121 7.209   1.00 55.68  ? 155 ASP A O     1 
ATOM   1230 C CB    . ASP A 1 160 ? -12.860 9.898  9.385   1.00 61.84  ? 155 ASP A CB    1 
ATOM   1231 C CG    . ASP A 1 160 ? -13.358 8.506  9.718   1.00 67.91  ? 155 ASP A CG    1 
ATOM   1232 O OD1   . ASP A 1 160 ? -14.511 8.185  9.356   1.00 72.68  ? 155 ASP A OD1   1 
ATOM   1233 O OD2   . ASP A 1 160 ? -12.602 7.734  10.343  1.00 63.89  ? 155 ASP A OD2   1 
ATOM   1234 N N     . PHE A 1 161 ? -11.226 12.116 7.561   1.00 59.79  ? 156 PHE A N     1 
ATOM   1235 C CA    . PHE A 1 161 ? -11.071 13.512 7.168   1.00 54.16  ? 156 PHE A CA    1 
ATOM   1236 C C     . PHE A 1 161 ? -11.277 13.686 5.668   1.00 53.67  ? 156 PHE A C     1 
ATOM   1237 O O     . PHE A 1 161 ? -12.007 14.583 5.230   1.00 57.98  ? 156 PHE A O     1 
ATOM   1238 C CB    . PHE A 1 161 ? -9.689  14.016 7.588   1.00 50.01  ? 156 PHE A CB    1 
ATOM   1239 C CG    . PHE A 1 161 ? -9.298  15.319 6.955   1.00 50.42  ? 156 PHE A CG    1 
ATOM   1240 C CD1   . PHE A 1 161 ? -9.844  16.511 7.396   1.00 47.55  ? 156 PHE A CD1   1 
ATOM   1241 C CD2   . PHE A 1 161 ? -8.380  15.350 5.917   1.00 49.95  ? 156 PHE A CD2   1 
ATOM   1242 C CE1   . PHE A 1 161 ? -9.484  17.711 6.815   1.00 46.74  ? 156 PHE A CE1   1 
ATOM   1243 C CE2   . PHE A 1 161 ? -8.017  16.546 5.332   1.00 47.41  ? 156 PHE A CE2   1 
ATOM   1244 C CZ    . PHE A 1 161 ? -8.569  17.728 5.781   1.00 45.76  ? 156 PHE A CZ    1 
ATOM   1245 N N     . ILE A 1 162 ? -10.639 12.835 4.864   1.00 51.02  ? 157 ILE A N     1 
ATOM   1246 C CA    . ILE A 1 162 ? -10.764 12.940 3.414   1.00 54.46  ? 157 ILE A CA    1 
ATOM   1247 C C     . ILE A 1 162 ? -12.179 12.590 2.970   1.00 55.60  ? 157 ILE A C     1 
ATOM   1248 O O     . ILE A 1 162 ? -12.706 13.171 2.014   1.00 56.24  ? 157 ILE A O     1 
ATOM   1249 C CB    . ILE A 1 162 ? -9.718  12.044 2.725   1.00 50.01  ? 157 ILE A CB    1 
ATOM   1250 C CG1   . ILE A 1 162 ? -8.322  12.324 3.285   1.00 52.28  ? 157 ILE A CG1   1 
ATOM   1251 C CG2   . ILE A 1 162 ? -9.739  12.252 1.218   1.00 48.60  ? 157 ILE A CG2   1 
ATOM   1252 C CD1   . ILE A 1 162 ? -7.218  11.558 2.588   1.00 49.38  ? 157 ILE A CD1   1 
ATOM   1253 N N     . SER A 1 163 ? -12.821 11.646 3.658   1.00 57.39  ? 158 SER A N     1 
ATOM   1254 C CA    . SER A 1 163 ? -14.131 11.174 3.221   1.00 55.90  ? 158 SER A CA    1 
ATOM   1255 C C     . SER A 1 163 ? -15.249 12.105 3.677   1.00 55.09  ? 158 SER A C     1 
ATOM   1256 O O     . SER A 1 163 ? -16.150 12.430 2.896   1.00 56.14  ? 158 SER A O     1 
ATOM   1257 C CB    . SER A 1 163 ? -14.375 9.755  3.739   1.00 59.57  ? 158 SER A CB    1 
ATOM   1258 O OG    . SER A 1 163 ? -13.707 8.795  2.938   1.00 63.88  ? 158 SER A OG    1 
ATOM   1259 N N     . ASN A 1 164 ? -15.208 12.547 4.934   1.00 57.28  ? 159 ASN A N     1 
ATOM   1260 C CA    . ASN A 1 164 ? -16.326 13.264 5.533   1.00 55.88  ? 159 ASN A CA    1 
ATOM   1261 C C     . ASN A 1 164 ? -16.080 14.749 5.747   1.00 52.41  ? 159 ASN A C     1 
ATOM   1262 O O     . ASN A 1 164 ? -17.017 15.537 5.607   1.00 54.01  ? 159 ASN A O     1 
ATOM   1263 C CB    . ASN A 1 164 ? -16.700 12.630 6.879   1.00 57.17  ? 159 ASN A CB    1 
ATOM   1264 C CG    . ASN A 1 164 ? -17.035 11.156 6.757   1.00 57.98  ? 159 ASN A CG    1 
ATOM   1265 O OD1   . ASN A 1 164 ? -17.775 10.747 5.862   1.00 58.16  ? 159 ASN A OD1   1 
ATOM   1266 N ND2   . ASN A 1 164 ? -16.488 10.348 7.658   1.00 57.35  ? 159 ASN A ND2   1 
ATOM   1267 N N     . GLU A 1 165 ? -14.856 15.155 6.083   1.00 54.67  ? 160 GLU A N     1 
ATOM   1268 C CA    . GLU A 1 165 ? -14.594 16.541 6.454   1.00 53.78  ? 160 GLU A CA    1 
ATOM   1269 C C     . GLU A 1 165 ? -13.997 17.376 5.330   1.00 53.81  ? 160 GLU A C     1 
ATOM   1270 O O     . GLU A 1 165 ? -14.264 18.580 5.265   1.00 55.30  ? 160 GLU A O     1 
ATOM   1271 C CB    . GLU A 1 165 ? -13.665 16.596 7.672   1.00 51.61  ? 160 GLU A CB    1 
ATOM   1272 C CG    . GLU A 1 165 ? -14.401 16.498 8.999   1.00 53.43  ? 160 GLU A CG    1 
ATOM   1273 C CD    . GLU A 1 165 ? -13.468 16.302 10.176  1.00 60.91  ? 160 GLU A CD    1 
ATOM   1274 O OE1   . GLU A 1 165 ? -13.907 16.515 11.325  1.00 69.85  ? 160 GLU A OE1   1 
ATOM   1275 O OE2   . GLU A 1 165 ? -12.295 15.935 9.952   1.00 65.65  ? 160 GLU A OE2   1 
ATOM   1276 N N     . LEU A 1 166 ? -13.197 16.780 4.452   1.00 54.59  ? 161 LEU A N     1 
ATOM   1277 C CA    . LEU A 1 166 ? -12.625 17.520 3.333   1.00 53.76  ? 161 LEU A CA    1 
ATOM   1278 C C     . LEU A 1 166 ? -13.693 17.954 2.327   1.00 54.84  ? 161 LEU A C     1 
ATOM   1279 O O     . LEU A 1 166 ? -13.614 19.076 1.811   1.00 58.27  ? 161 LEU A O     1 
ATOM   1280 C CB    . LEU A 1 166 ? -11.537 16.696 2.638   1.00 53.20  ? 161 LEU A CB    1 
ATOM   1281 C CG    . LEU A 1 166 ? -10.699 17.453 1.605   1.00 49.32  ? 161 LEU A CG    1 
ATOM   1282 C CD1   . LEU A 1 166 ? -10.157 18.744 2.199   1.00 47.04  ? 161 LEU A CD1   1 
ATOM   1283 C CD2   . LEU A 1 166 ? -9.565  16.585 1.083   1.00 48.56  ? 161 LEU A CD2   1 
ATOM   1284 N N     . PRO A 1 167 ? -14.691 17.120 2.000   1.00 53.49  ? 162 PRO A N     1 
ATOM   1285 C CA    . PRO A 1 167 ? -15.776 17.610 1.132   1.00 53.49  ? 162 PRO A CA    1 
ATOM   1286 C C     . PRO A 1 167 ? -16.586 18.736 1.746   1.00 54.38  ? 162 PRO A C     1 
ATOM   1287 O O     . PRO A 1 167 ? -17.244 19.479 1.007   1.00 54.03  ? 162 PRO A O     1 
ATOM   1288 C CB    . PRO A 1 167 ? -16.640 16.361 0.908   1.00 49.54  ? 162 PRO A CB    1 
ATOM   1289 C CG    . PRO A 1 167 ? -15.713 15.231 1.099   1.00 51.12  ? 162 PRO A CG    1 
ATOM   1290 C CD    . PRO A 1 167 ? -14.794 15.662 2.199   1.00 52.90  ? 162 PRO A CD    1 
ATOM   1291 N N     . GLN A 1 168 ? -16.571 18.886 3.066   1.00 57.33  ? 163 GLN A N     1 
ATOM   1292 C CA    . GLN A 1 168 ? -17.258 19.993 3.715   1.00 55.29  ? 163 GLN A CA    1 
ATOM   1293 C C     . GLN A 1 168 ? -16.373 21.217 3.905   1.00 57.50  ? 163 GLN A C     1 
ATOM   1294 O O     . GLN A 1 168 ? -16.805 22.175 4.557   1.00 56.74  ? 163 GLN A O     1 
ATOM   1295 C CB    . GLN A 1 168 ? -17.818 19.552 5.071   1.00 53.89  ? 163 GLN A CB    1 
ATOM   1296 C CG    . GLN A 1 168 ? -18.706 18.320 5.007   1.00 55.92  ? 163 GLN A CG    1 
ATOM   1297 C CD    . GLN A 1 168 ? -19.275 17.940 6.359   1.00 61.84  ? 163 GLN A CD    1 
ATOM   1298 O OE1   . GLN A 1 168 ? -20.015 18.711 6.971   1.00 60.20  ? 163 GLN A OE1   1 
ATOM   1299 N NE2   . GLN A 1 168 ? -18.931 16.750 6.832   1.00 58.43  ? 163 GLN A NE2   1 
ATOM   1300 N N     . ASP A 1 169 ? -15.156 21.212 3.366   1.00 60.59  ? 164 ASP A N     1 
ATOM   1301 C CA    . ASP A 1 169 ? -14.309 22.394 3.455   1.00 57.54  ? 164 ASP A CA    1 
ATOM   1302 C C     . ASP A 1 169 ? -15.017 23.584 2.827   1.00 58.37  ? 164 ASP A C     1 
ATOM   1303 O O     . ASP A 1 169 ? -15.374 23.545 1.648   1.00 58.04  ? 164 ASP A O     1 
ATOM   1304 C CB    . ASP A 1 169 ? -12.966 22.141 2.768   1.00 58.82  ? 164 ASP A CB    1 
ATOM   1305 C CG    . ASP A 1 169 ? -11.919 23.174 3.131   1.00 58.43  ? 164 ASP A CG    1 
ATOM   1306 O OD1   . ASP A 1 169 ? -11.264 23.043 4.182   1.00 59.27  ? 164 ASP A OD1   1 
ATOM   1307 O OD2   . ASP A 1 169 ? -11.732 24.120 2.340   1.00 62.02  ? 164 ASP A OD2   1 
ATOM   1308 N N     . GLU A 1 170 ? -15.221 24.643 3.618   1.00 61.26  ? 165 GLU A N     1 
ATOM   1309 C CA    . GLU A 1 170 ? -15.853 25.859 3.116   1.00 60.22  ? 165 GLU A CA    1 
ATOM   1310 C C     . GLU A 1 170 ? -15.172 26.420 1.874   1.00 62.75  ? 165 GLU A C     1 
ATOM   1311 O O     . GLU A 1 170 ? -15.754 27.291 1.225   1.00 62.88  ? 165 GLU A O     1 
ATOM   1312 C CB    . GLU A 1 170 ? -15.876 26.942 4.196   1.00 63.32  ? 165 GLU A CB    1 
ATOM   1313 C CG    . GLU A 1 170 ? -14.495 27.399 4.652   1.00 69.24  ? 165 GLU A CG    1 
ATOM   1314 C CD    . GLU A 1 170 ? -14.004 28.651 3.930   1.00 72.17  ? 165 GLU A CD    1 
ATOM   1315 O OE1   . GLU A 1 170 ? -14.836 29.509 3.576   1.00 72.25  ? 165 GLU A OE1   1 
ATOM   1316 O OE2   . GLU A 1 170 ? -12.781 28.773 3.707   1.00 61.01  ? 165 GLU A OE2   1 
ATOM   1317 N N     . PHE A 1 171 ? -13.969 25.955 1.531   1.00 60.84  ? 166 PHE A N     1 
ATOM   1318 C CA    . PHE A 1 171 ? -13.151 26.559 0.485   1.00 55.28  ? 166 PHE A CA    1 
ATOM   1319 C C     . PHE A 1 171 ? -12.853 25.612 -0.664  1.00 60.09  ? 166 PHE A C     1 
ATOM   1320 O O     . PHE A 1 171 ? -12.964 26.016 -1.824  1.00 63.55  ? 166 PHE A O     1 
ATOM   1321 C CB    . PHE A 1 171 ? -11.845 27.088 1.102   1.00 57.99  ? 166 PHE A CB    1 
ATOM   1322 C CG    . PHE A 1 171 ? -10.818 27.554 0.092   1.00 54.62  ? 166 PHE A CG    1 
ATOM   1323 C CD1   . PHE A 1 171 ? -10.944 28.782 -0.539  1.00 53.39  ? 166 PHE A CD1   1 
ATOM   1324 C CD2   . PHE A 1 171 ? -9.691  26.794 -0.177  1.00 59.64  ? 166 PHE A CD2   1 
ATOM   1325 C CE1   . PHE A 1 171 ? -9.980  29.220 -1.452  1.00 58.25  ? 166 PHE A CE1   1 
ATOM   1326 C CE2   . PHE A 1 171 ? -8.725  27.224 -1.085  1.00 61.15  ? 166 PHE A CE2   1 
ATOM   1327 C CZ    . PHE A 1 171 ? -8.869  28.440 -1.722  1.00 59.59  ? 166 PHE A CZ    1 
ATOM   1328 N N     . LEU A 1 172 ? -12.479 24.367 -0.376  1.00 59.17  ? 167 LEU A N     1 
ATOM   1329 C CA    . LEU A 1 172 ? -12.190 23.363 -1.393  1.00 56.50  ? 167 LEU A CA    1 
ATOM   1330 C C     . LEU A 1 172 ? -13.266 22.289 -1.483  1.00 56.19  ? 167 LEU A C     1 
ATOM   1331 O O     . LEU A 1 172 ? -13.094 21.321 -2.231  1.00 54.80  ? 167 LEU A O     1 
ATOM   1332 C CB    . LEU A 1 172 ? -10.834 22.698 -1.125  1.00 59.94  ? 167 LEU A CB    1 
ATOM   1333 C CG    . LEU A 1 172 ? -9.596  23.571 -1.271  1.00 57.65  ? 167 LEU A CG    1 
ATOM   1334 C CD1   . LEU A 1 172 ? -8.352  22.786 -0.941  1.00 51.16  ? 167 LEU A CD1   1 
ATOM   1335 C CD2   . LEU A 1 172 ? -9.525  24.112 -2.682  1.00 54.56  ? 167 LEU A CD2   1 
ATOM   1336 N N     . GLY A 1 173 ? -14.372 22.450 -0.763  1.00 57.99  ? 168 GLY A N     1 
ATOM   1337 C CA    . GLY A 1 173 ? -15.400 21.432 -0.683  1.00 52.40  ? 168 GLY A CA    1 
ATOM   1338 C C     . GLY A 1 173 ? -16.008 21.011 -2.006  1.00 53.77  ? 168 GLY A C     1 
ATOM   1339 O O     . GLY A 1 173 ? -15.966 19.829 -2.364  1.00 59.43  ? 168 GLY A O     1 
ATOM   1340 N N     . GLU A 1 174 ? -16.576 21.969 -2.743  1.00 55.54  ? 169 GLU A N     1 
ATOM   1341 C CA    . GLU A 1 174 ? -17.254 21.644 -3.992  1.00 55.44  ? 169 GLU A CA    1 
ATOM   1342 C C     . GLU A 1 174 ? -16.304 21.081 -5.041  1.00 56.72  ? 169 GLU A C     1 
ATOM   1343 O O     . GLU A 1 174 ? -16.751 20.358 -5.937  1.00 61.13  ? 169 GLU A O     1 
ATOM   1344 C CB    . GLU A 1 174 ? -17.966 22.882 -4.536  1.00 62.73  ? 169 GLU A CB    1 
ATOM   1345 C CG    . GLU A 1 174 ? -19.417 22.641 -4.925  1.00 72.25  ? 169 GLU A CG    1 
ATOM   1346 C CD    . GLU A 1 174 ? -20.313 22.409 -3.723  1.00 85.60  ? 169 GLU A CD    1 
ATOM   1347 O OE1   . GLU A 1 174 ? -20.990 21.360 -3.681  1.00 85.87  ? 169 GLU A OE1   1 
ATOM   1348 O OE2   . GLU A 1 174 ? -20.342 23.273 -2.822  1.00 88.83  ? 169 GLU A OE2   1 
ATOM   1349 N N     . MET A 1 175 ? -15.010 21.395 -4.955  1.00 55.96  ? 170 MET A N     1 
ATOM   1350 C CA    . MET A 1 175 ? -14.044 20.796 -5.870  1.00 49.74  ? 170 MET A CA    1 
ATOM   1351 C C     . MET A 1 175 ? -13.624 19.407 -5.405  1.00 49.82  ? 170 MET A C     1 
ATOM   1352 O O     . MET A 1 175 ? -13.467 18.497 -6.226  1.00 51.41  ? 170 MET A O     1 
ATOM   1353 C CB    . MET A 1 175 ? -12.824 21.703 -6.020  1.00 52.02  ? 170 MET A CB    1 
ATOM   1354 C CG    . MET A 1 175 ? -13.083 22.945 -6.853  1.00 55.05  ? 170 MET A CG    1 
ATOM   1355 S SD    . MET A 1 175 ? -12.055 24.338 -6.359  1.00 65.43  ? 170 MET A SD    1 
ATOM   1356 C CE    . MET A 1 175 ? -12.822 24.775 -4.802  1.00 56.01  ? 170 MET A CE    1 
ATOM   1357 N N     . VAL A 1 176 ? -13.436 19.226 -4.096  1.00 51.39  ? 171 VAL A N     1 
ATOM   1358 C CA    . VAL A 1 176 ? -13.136 17.898 -3.567  1.00 50.22  ? 171 VAL A CA    1 
ATOM   1359 C C     . VAL A 1 176 ? -14.315 16.961 -3.800  1.00 51.59  ? 171 VAL A C     1 
ATOM   1360 O O     . VAL A 1 176 ? -14.137 15.771 -4.092  1.00 55.11  ? 171 VAL A O     1 
ATOM   1361 C CB    . VAL A 1 176 ? -12.762 17.994 -2.075  1.00 47.92  ? 171 VAL A CB    1 
ATOM   1362 C CG1   . VAL A 1 176 ? -12.843 16.631 -1.401  1.00 48.03  ? 171 VAL A CG1   1 
ATOM   1363 C CG2   . VAL A 1 176 ? -11.369 18.590 -1.917  1.00 46.59  ? 171 VAL A CG2   1 
ATOM   1364 N N     . LYS A 1 177 ? -15.537 17.488 -3.698  1.00 52.06  ? 172 LYS A N     1 
ATOM   1365 C CA    . LYS A 1 177 ? -16.721 16.674 -3.952  1.00 50.50  ? 172 LYS A CA    1 
ATOM   1366 C C     . LYS A 1 177 ? -16.789 16.227 -5.407  1.00 50.92  ? 172 LYS A C     1 
ATOM   1367 O O     . LYS A 1 177 ? -17.181 15.090 -5.695  1.00 49.61  ? 172 LYS A O     1 
ATOM   1368 C CB    . LYS A 1 177 ? -17.981 17.454 -3.578  1.00 56.43  ? 172 LYS A CB    1 
ATOM   1369 C CG    . LYS A 1 177 ? -18.576 17.090 -2.230  1.00 57.56  ? 172 LYS A CG    1 
ATOM   1370 C CD    . LYS A 1 177 ? -19.937 17.744 -2.044  1.00 62.91  ? 172 LYS A CD    1 
ATOM   1371 C CE    . LYS A 1 177 ? -19.804 19.155 -1.493  1.00 62.35  ? 172 LYS A CE    1 
ATOM   1372 N NZ    . LYS A 1 177 ? -20.797 19.432 -0.418  1.00 64.29  ? 172 LYS A NZ    1 
ATOM   1373 N N     . ASN A 1 178 ? -16.408 17.102 -6.338  1.00 54.62  ? 173 ASN A N     1 
ATOM   1374 C CA    . ASN A 1 178 ? -16.562 16.820 -7.760  1.00 51.95  ? 173 ASN A CA    1 
ATOM   1375 C C     . ASN A 1 178 ? -15.324 16.183 -8.381  1.00 53.54  ? 173 ASN A C     1 
ATOM   1376 O O     . ASN A 1 178 ? -15.449 15.337 -9.272  1.00 57.70  ? 173 ASN A O     1 
ATOM   1377 C CB    . ASN A 1 178 ? -16.901 18.106 -8.520  1.00 54.07  ? 173 ASN A CB    1 
ATOM   1378 C CG    . ASN A 1 178 ? -18.204 18.731 -8.064  1.00 57.32  ? 173 ASN A CG    1 
ATOM   1379 O OD1   . ASN A 1 178 ? -19.123 18.036 -7.632  1.00 61.47  ? 173 ASN A OD1   1 
ATOM   1380 N ND2   . ASN A 1 178 ? -18.287 20.053 -8.155  1.00 58.99  ? 173 ASN A ND2   1 
ATOM   1381 N N     . GLN A 1 179 ? -14.128 16.568 -7.934  1.00 53.92  ? 174 GLN A N     1 
ATOM   1382 C CA    . GLN A 1 179 ? -12.904 16.231 -8.646  1.00 52.19  ? 174 GLN A CA    1 
ATOM   1383 C C     . GLN A 1 179 ? -11.997 15.249 -7.918  1.00 49.05  ? 174 GLN A C     1 
ATOM   1384 O O     . GLN A 1 179 ? -11.070 14.720 -8.542  1.00 53.30  ? 174 GLN A O     1 
ATOM   1385 C CB    . GLN A 1 179 ? -12.110 17.509 -8.957  1.00 50.12  ? 174 GLN A CB    1 
ATOM   1386 C CG    . GLN A 1 179 ? -12.913 18.558 -9.708  1.00 46.20  ? 174 GLN A CG    1 
ATOM   1387 C CD    . GLN A 1 179 ? -12.115 19.813 -9.992  1.00 49.07  ? 174 GLN A CD    1 
ATOM   1388 O OE1   . GLN A 1 179 ? -12.470 20.904 -9.547  1.00 54.62  ? 174 GLN A OE1   1 
ATOM   1389 N NE2   . GLN A 1 179 ? -11.028 19.665 -10.742 1.00 49.27  ? 174 GLN A NE2   1 
ATOM   1390 N N     . LEU A 1 180 ? -12.224 14.986 -6.635  1.00 50.86  ? 175 LEU A N     1 
ATOM   1391 C CA    . LEU A 1 180 ? -11.356 14.102 -5.866  1.00 50.55  ? 175 LEU A CA    1 
ATOM   1392 C C     . LEU A 1 180 ? -11.961 12.708 -5.774  1.00 48.89  ? 175 LEU A C     1 
ATOM   1393 O O     . LEU A 1 180 ? -13.140 12.555 -5.441  1.00 50.35  ? 175 LEU A O     1 
ATOM   1394 C CB    . LEU A 1 180 ? -11.105 14.653 -4.461  1.00 46.86  ? 175 LEU A CB    1 
ATOM   1395 C CG    . LEU A 1 180 ? -10.011 13.904 -3.696  1.00 46.20  ? 175 LEU A CG    1 
ATOM   1396 C CD1   . LEU A 1 180 ? -8.630  14.357 -4.149  1.00 46.00  ? 175 LEU A CD1   1 
ATOM   1397 C CD2   . LEU A 1 180 ? -10.168 14.074 -2.192  1.00 54.64  ? 175 LEU A CD2   1 
ATOM   1398 N N     . ILE A 1 181 ? -11.146 11.698 -6.070  1.00 49.62  ? 176 ILE A N     1 
ATOM   1399 C CA    . ILE A 1 181 ? -11.502 10.298 -5.883  1.00 48.90  ? 176 ILE A CA    1 
ATOM   1400 C C     . ILE A 1 181 ? -10.531 9.701  -4.874  1.00 49.49  ? 176 ILE A C     1 
ATOM   1401 O O     . ILE A 1 181 ? -9.311  9.808  -5.040  1.00 53.32  ? 176 ILE A O     1 
ATOM   1402 C CB    . ILE A 1 181 ? -11.468 9.514  -7.208  1.00 49.75  ? 176 ILE A CB    1 
ATOM   1403 C CG1   . ILE A 1 181 ? -12.362 10.187 -8.250  1.00 55.88  ? 176 ILE A CG1   1 
ATOM   1404 C CG2   . ILE A 1 181 ? -11.897 8.072  -6.984  1.00 45.51  ? 176 ILE A CG2   1 
ATOM   1405 C CD1   . ILE A 1 181 ? -12.357 9.495  -9.597  1.00 52.75  ? 176 ILE A CD1   1 
ATOM   1406 N N     . TYR A 1 182 ? -11.073 9.083  -3.830  1.00 47.51  ? 177 TYR A N     1 
ATOM   1407 C CA    . TYR A 1 182 ? -10.282 8.519  -2.743  1.00 47.31  ? 177 TYR A CA    1 
ATOM   1408 C C     . TYR A 1 182 ? -10.419 7.003  -2.774  1.00 47.67  ? 177 TYR A C     1 
ATOM   1409 O O     . TYR A 1 182 ? -11.530 6.475  -2.659  1.00 51.55  ? 177 TYR A O     1 
ATOM   1410 C CB    . TYR A 1 182 ? -10.738 9.088  -1.399  1.00 45.49  ? 177 TYR A CB    1 
ATOM   1411 C CG    . TYR A 1 182 ? -10.039 8.496  -0.198  1.00 45.17  ? 177 TYR A CG    1 
ATOM   1412 C CD1   . TYR A 1 182 ? -8.655  8.385  -0.159  1.00 44.77  ? 177 TYR A CD1   1 
ATOM   1413 C CD2   . TYR A 1 182 ? -10.764 8.059  0.902   1.00 47.07  ? 177 TYR A CD2   1 
ATOM   1414 C CE1   . TYR A 1 182 ? -8.014  7.847  0.940   1.00 44.24  ? 177 TYR A CE1   1 
ATOM   1415 C CE2   . TYR A 1 182 ? -10.133 7.521  2.005   1.00 43.54  ? 177 TYR A CE2   1 
ATOM   1416 C CZ    . TYR A 1 182 ? -8.759  7.418  2.019   1.00 46.13  ? 177 TYR A CZ    1 
ATOM   1417 O OH    . TYR A 1 182 ? -8.129  6.882  3.117   1.00 54.42  ? 177 TYR A OH    1 
ATOM   1418 N N     . TYR A 1 183 ? -9.291  6.308  -2.929  1.00 46.77  ? 178 TYR A N     1 
ATOM   1419 C CA    . TYR A 1 183 ? -9.272  4.860  -3.134  1.00 45.80  ? 178 TYR A CA    1 
ATOM   1420 C C     . TYR A 1 183 ? -8.312  4.210  -2.148  1.00 46.68  ? 178 TYR A C     1 
ATOM   1421 O O     . TYR A 1 183 ? -7.122  4.036  -2.443  1.00 50.49  ? 178 TYR A O     1 
ATOM   1422 C CB    . TYR A 1 183 ? -8.885  4.520  -4.572  1.00 48.92  ? 178 TYR A CB    1 
ATOM   1423 C CG    . TYR A 1 183 ? -9.094  3.070  -4.944  1.00 50.12  ? 178 TYR A CG    1 
ATOM   1424 C CD1   . TYR A 1 183 ? -10.372 2.532  -5.021  1.00 47.84  ? 178 TYR A CD1   1 
ATOM   1425 C CD2   . TYR A 1 183 ? -8.016  2.243  -5.231  1.00 55.15  ? 178 TYR A CD2   1 
ATOM   1426 C CE1   . TYR A 1 183 ? -10.570 1.210  -5.364  1.00 47.97  ? 178 TYR A CE1   1 
ATOM   1427 C CE2   . TYR A 1 183 ? -8.204  0.918  -5.577  1.00 56.79  ? 178 TYR A CE2   1 
ATOM   1428 C CZ    . TYR A 1 183 ? -9.484  0.407  -5.642  1.00 54.19  ? 178 TYR A CZ    1 
ATOM   1429 O OH    . TYR A 1 183 ? -9.680  -0.910 -5.986  1.00 60.36  ? 178 TYR A OH    1 
ATOM   1430 N N     . PRO A 1 184 ? -8.794  3.837  -0.962  1.00 46.21  ? 179 PRO A N     1 
ATOM   1431 C CA    . PRO A 1 184 ? -7.939  3.132  -0.001  1.00 44.53  ? 179 PRO A CA    1 
ATOM   1432 C C     . PRO A 1 184 ? -7.984  1.623  -0.187  1.00 50.63  ? 179 PRO A C     1 
ATOM   1433 O O     . PRO A 1 184 ? -9.015  1.038  -0.525  1.00 56.71  ? 179 PRO A O     1 
ATOM   1434 C CB    . PRO A 1 184 ? -8.549  3.538  1.347   1.00 44.93  ? 179 PRO A CB    1 
ATOM   1435 C CG    . PRO A 1 184 ? -10.003 3.709  1.046   1.00 45.95  ? 179 PRO A CG    1 
ATOM   1436 C CD    . PRO A 1 184 ? -10.112 4.171  -0.392  1.00 48.50  ? 179 PRO A CD    1 
ATOM   1437 N N     . THR A 1 185 ? -6.837  0.984  0.037   1.00 48.67  ? 180 THR A N     1 
ATOM   1438 C CA    . THR A 1 185 ? -6.724  -0.462 -0.087  1.00 49.52  ? 180 THR A CA    1 
ATOM   1439 C C     . THR A 1 185 ? -5.898  -1.015 1.065   1.00 48.75  ? 180 THR A C     1 
ATOM   1440 O O     . THR A 1 185 ? -4.964  -0.372 1.551   1.00 52.00  ? 180 THR A O     1 
ATOM   1441 C CB    . THR A 1 185 ? -6.107  -0.873 -1.438  1.00 52.30  ? 180 THR A CB    1 
ATOM   1442 O OG1   . THR A 1 185 ? -6.091  -2.303 -1.545  1.00 57.14  ? 180 THR A OG1   1 
ATOM   1443 C CG2   . THR A 1 185 ? -4.693  -0.329 -1.588  1.00 46.05  ? 180 THR A CG2   1 
ATOM   1444 N N     . VAL A 1 186 ? -6.271  -2.215 1.508   1.00 49.07  ? 181 VAL A N     1 
ATOM   1445 C CA    . VAL A 1 186 ? -5.631  -2.893 2.629   1.00 49.57  ? 181 VAL A CA    1 
ATOM   1446 C C     . VAL A 1 186 ? -5.269  -4.304 2.188   1.00 51.00  ? 181 VAL A C     1 
ATOM   1447 O O     . VAL A 1 186 ? -6.040  -4.956 1.478   1.00 51.61  ? 181 VAL A O     1 
ATOM   1448 C CB    . VAL A 1 186 ? -6.546  -2.926 3.872   1.00 47.49  ? 181 VAL A CB    1 
ATOM   1449 C CG1   . VAL A 1 186 ? -5.852  -3.607 5.040   1.00 53.27  ? 181 VAL A CG1   1 
ATOM   1450 C CG2   . VAL A 1 186 ? -6.982  -1.518 4.253   1.00 48.24  ? 181 VAL A CG2   1 
ATOM   1451 N N     . THR A 1 187 ? -4.098  -4.781 2.613   1.00 52.31  ? 182 THR A N     1 
ATOM   1452 C CA    . THR A 1 187 ? -3.582  -6.069 2.162   1.00 51.04  ? 182 THR A CA    1 
ATOM   1453 C C     . THR A 1 187 ? -3.852  -7.205 3.142   1.00 51.41  ? 182 THR A C     1 
ATOM   1454 O O     . THR A 1 187 ? -4.310  -8.276 2.733   1.00 52.04  ? 182 THR A O     1 
ATOM   1455 C CB    . THR A 1 187 ? -2.074  -5.970 1.898   1.00 50.92  ? 182 THR A CB    1 
ATOM   1456 O OG1   . THR A 1 187 ? -1.416  -5.447 3.059   1.00 57.18  ? 182 THR A OG1   1 
ATOM   1457 C CG2   . THR A 1 187 ? -1.797  -5.059 0.712   1.00 50.58  ? 182 THR A CG2   1 
ATOM   1458 N N     . ARG A 1 188 ? -3.583  -6.999 4.433   1.00 50.85  ? 183 ARG A N     1 
ATOM   1459 C CA    . ARG A 1 188 ? -3.532  -8.096 5.391   1.00 48.74  ? 183 ARG A CA    1 
ATOM   1460 C C     . ARG A 1 188 ? -4.685  -8.085 6.390   1.00 50.83  ? 183 ARG A C     1 
ATOM   1461 O O     . ARG A 1 188 ? -4.606  -8.756 7.423   1.00 54.43  ? 183 ARG A O     1 
ATOM   1462 C CB    . ARG A 1 188 ? -2.192  -8.081 6.128   1.00 46.47  ? 183 ARG A CB    1 
ATOM   1463 C CG    . ARG A 1 188 ? -0.995  -8.214 5.203   1.00 49.10  ? 183 ARG A CG    1 
ATOM   1464 C CD    . ARG A 1 188 ? 0.308   -8.299 5.974   1.00 47.22  ? 183 ARG A CD    1 
ATOM   1465 N NE    . ARG A 1 188 ? 1.451   -7.946 5.141   1.00 45.11  ? 183 ARG A NE    1 
ATOM   1466 C CZ    . ARG A 1 188 ? 2.691   -7.813 5.590   1.00 53.75  ? 183 ARG A CZ    1 
ATOM   1467 N NH1   . ARG A 1 188 ? 2.989   -8.012 6.863   1.00 57.27  ? 183 ARG A NH1   1 
ATOM   1468 N NH2   . ARG A 1 188 ? 3.656   -7.476 4.739   1.00 57.31  ? 183 ARG A NH2   1 
ATOM   1469 N N     . GLU A 1 189 ? -5.757  -7.353 6.107   1.00 50.48  ? 184 GLU A N     1 
ATOM   1470 C CA    . GLU A 1 189 ? -6.940  -7.364 6.954   1.00 50.74  ? 184 GLU A CA    1 
ATOM   1471 C C     . GLU A 1 189 ? -8.186  -7.265 6.088   1.00 53.22  ? 184 GLU A C     1 
ATOM   1472 O O     . GLU A 1 189 ? -8.152  -6.649 5.016   1.00 52.72  ? 184 GLU A O     1 
ATOM   1473 C CB    . GLU A 1 189 ? -6.932  -6.216 7.977   1.00 53.24  ? 184 GLU A CB    1 
ATOM   1474 C CG    . GLU A 1 189 ? -5.984  -6.432 9.148   1.00 57.23  ? 184 GLU A CG    1 
ATOM   1475 C CD    . GLU A 1 189 ? -6.308  -5.547 10.337  1.00 56.46  ? 184 GLU A CD    1 
ATOM   1476 O OE1   . GLU A 1 189 ? -7.053  -4.560 10.163  1.00 55.24  ? 184 GLU A OE1   1 
ATOM   1477 O OE2   . GLU A 1 189 ? -5.822  -5.844 11.449  1.00 60.12  ? 184 GLU A OE2   1 
ATOM   1478 N N     . PRO A 1 190 ? -9.293  -7.870 6.520   1.00 55.38  ? 185 PRO A N     1 
ATOM   1479 C CA    . PRO A 1 190 ? -10.542 -7.782 5.747   1.00 51.83  ? 185 PRO A CA    1 
ATOM   1480 C C     . PRO A 1 190 ? -10.982 -6.337 5.565   1.00 54.25  ? 185 PRO A C     1 
ATOM   1481 O O     . PRO A 1 190 ? -11.295 -5.635 6.530   1.00 55.64  ? 185 PRO A O     1 
ATOM   1482 C CB    . PRO A 1 190 ? -11.538 -8.579 6.596   1.00 50.45  ? 185 PRO A CB    1 
ATOM   1483 C CG    . PRO A 1 190 ? -10.690 -9.529 7.373   1.00 53.34  ? 185 PRO A CG    1 
ATOM   1484 C CD    . PRO A 1 190 ? -9.413  -8.794 7.661   1.00 55.61  ? 185 PRO A CD    1 
ATOM   1485 N N     . TYR A 1 191 ? -10.996 -5.896 4.310   1.00 52.41  ? 186 TYR A N     1 
ATOM   1486 C CA    . TYR A 1 191 ? -11.388 -4.542 3.951   1.00 50.88  ? 186 TYR A CA    1 
ATOM   1487 C C     . TYR A 1 191 ? -12.156 -4.602 2.638   1.00 55.36  ? 186 TYR A C     1 
ATOM   1488 O O     . TYR A 1 191 ? -12.125 -5.607 1.923   1.00 60.14  ? 186 TYR A O     1 
ATOM   1489 C CB    . TYR A 1 191 ? -10.165 -3.621 3.838   1.00 55.08  ? 186 TYR A CB    1 
ATOM   1490 C CG    . TYR A 1 191 ? -10.490 -2.146 3.743   1.00 56.79  ? 186 TYR A CG    1 
ATOM   1491 C CD1   . TYR A 1 191 ? -11.035 -1.463 4.822   1.00 56.53  ? 186 TYR A CD1   1 
ATOM   1492 C CD2   . TYR A 1 191 ? -10.241 -1.436 2.576   1.00 55.55  ? 186 TYR A CD2   1 
ATOM   1493 C CE1   . TYR A 1 191 ? -11.329 -0.115 4.739   1.00 58.87  ? 186 TYR A CE1   1 
ATOM   1494 C CE2   . TYR A 1 191 ? -10.531 -0.088 2.484   1.00 54.68  ? 186 TYR A CE2   1 
ATOM   1495 C CZ    . TYR A 1 191 ? -11.075 0.567  3.568   1.00 57.44  ? 186 TYR A CZ    1 
ATOM   1496 O OH    . TYR A 1 191 ? -11.366 1.909  3.480   1.00 55.56  ? 186 TYR A OH    1 
ATOM   1497 N N     . LYS A 1 192 ? -12.859 -3.511 2.320   1.00 57.28  ? 187 LYS A N     1 
ATOM   1498 C CA    . LYS A 1 192 ? -13.651 -3.483 1.095   1.00 56.06  ? 187 LYS A CA    1 
ATOM   1499 C C     . LYS A 1 192 ? -12.782 -3.464 -0.157  1.00 59.33  ? 187 LYS A C     1 
ATOM   1500 O O     . LYS A 1 192 ? -13.288 -3.742 -1.249  1.00 63.88  ? 187 LYS A O     1 
ATOM   1501 C CB    . LYS A 1 192 ? -14.599 -2.282 1.103   1.00 55.89  ? 187 LYS A CB    1 
ATOM   1502 C CG    . LYS A 1 192 ? -13.917 -0.925 1.065   1.00 57.39  ? 187 LYS A CG    1 
ATOM   1503 C CD    . LYS A 1 192 ? -14.850 0.165  1.574   1.00 64.09  ? 187 LYS A CD    1 
ATOM   1504 C CE    . LYS A 1 192 ? -14.182 1.530  1.555   1.00 64.85  ? 187 LYS A CE    1 
ATOM   1505 N NZ    . LYS A 1 192 ? -14.281 2.170  0.214   1.00 64.54  ? 187 LYS A NZ    1 
ATOM   1506 N N     . THR A 1 193 ? -11.495 -3.150 -0.024  1.00 58.99  ? 188 THR A N     1 
ATOM   1507 C CA    . THR A 1 193 ? -10.543 -3.215 -1.127  1.00 56.91  ? 188 THR A CA    1 
ATOM   1508 C C     . THR A 1 193 ? -9.298  -3.940 -0.641  1.00 56.09  ? 188 THR A C     1 
ATOM   1509 O O     . THR A 1 193 ? -8.623  -3.468 0.280   1.00 57.33  ? 188 THR A O     1 
ATOM   1510 C CB    . THR A 1 193 ? -10.185 -1.818 -1.644  1.00 57.48  ? 188 THR A CB    1 
ATOM   1511 O OG1   . THR A 1 193 ? -11.385 -1.074 -1.886  1.00 56.18  ? 188 THR A OG1   1 
ATOM   1512 C CG2   . THR A 1 193 ? -9.383  -1.916 -2.934  1.00 53.22  ? 188 THR A CG2   1 
ATOM   1513 N N     . ARG A 1 194 ? -8.996  -5.079 -1.257  1.00 55.62  ? 189 ARG A N     1 
ATOM   1514 C CA    . ARG A 1 194 ? -7.892  -5.928 -0.838  1.00 55.13  ? 189 ARG A CA    1 
ATOM   1515 C C     . ARG A 1 194 ? -6.796  -5.961 -1.895  1.00 59.02  ? 189 ARG A C     1 
ATOM   1516 O O     . ARG A 1 194 ? -7.052  -5.770 -3.088  1.00 61.30  ? 189 ARG A O     1 
ATOM   1517 C CB    . ARG A 1 194 ? -8.374  -7.355 -0.555  1.00 55.95  ? 189 ARG A CB    1 
ATOM   1518 C CG    . ARG A 1 194 ? -9.416  -7.460 0.545   1.00 50.80  ? 189 ARG A CG    1 
ATOM   1519 C CD    . ARG A 1 194 ? -8.826  -7.104 1.897   1.00 57.52  ? 189 ARG A CD    1 
ATOM   1520 N NE    . ARG A 1 194 ? -7.735  -7.996 2.269   1.00 53.86  ? 189 ARG A NE    1 
ATOM   1521 C CZ    . ARG A 1 194 ? -7.896  -9.191 2.822   1.00 52.86  ? 189 ARG A CZ    1 
ATOM   1522 N NH1   . ARG A 1 194 ? -9.099  -9.679 3.075   1.00 56.92  ? 189 ARG A NH1   1 
ATOM   1523 N NH2   . ARG A 1 194 ? -6.822  -9.912 3.132   1.00 55.73  ? 189 ARG A NH2   1 
ATOM   1524 N N     . GLY A 1 195 ? -5.570  -6.198 -1.439  1.00 57.97  ? 190 GLY A N     1 
ATOM   1525 C CA    . GLY A 1 195 ? -4.445  -6.411 -2.323  1.00 58.31  ? 190 GLY A CA    1 
ATOM   1526 C C     . GLY A 1 195 ? -3.560  -5.179 -2.458  1.00 55.39  ? 190 GLY A C     1 
ATOM   1527 O O     . GLY A 1 195 ? -3.926  -4.058 -2.091  1.00 53.56  ? 190 GLY A O     1 
ATOM   1528 N N     . ARG A 1 196 ? -2.365  -5.406 -2.999  1.00 61.78  ? 191 ARG A N     1 
ATOM   1529 C CA    . ARG A 1 196 ? -1.451  -4.314 -3.298  1.00 55.84  ? 191 ARG A CA    1 
ATOM   1530 C C     . ARG A 1 196 ? -2.039  -3.420 -4.382  1.00 54.67  ? 191 ARG A C     1 
ATOM   1531 O O     . ARG A 1 196 ? -2.849  -3.857 -5.204  1.00 62.15  ? 191 ARG A O     1 
ATOM   1532 C CB    . ARG A 1 196 ? -0.104  -4.865 -3.764  1.00 60.90  ? 191 ARG A CB    1 
ATOM   1533 C CG    . ARG A 1 196 ? 0.303   -6.158 -3.081  1.00 61.81  ? 191 ARG A CG    1 
ATOM   1534 C CD    . ARG A 1 196 ? 1.533   -5.923 -2.238  1.00 73.19  ? 191 ARG A CD    1 
ATOM   1535 N NE    . ARG A 1 196 ? 2.598   -5.343 -3.044  1.00 77.56  ? 191 ARG A NE    1 
ATOM   1536 C CZ    . ARG A 1 196 ? 3.657   -4.720 -2.549  1.00 83.95  ? 191 ARG A CZ    1 
ATOM   1537 N NH1   . ARG A 1 196 ? 3.783   -4.498 -1.251  1.00 86.13  ? 191 ARG A NH1   1 
ATOM   1538 N NH2   . ARG A 1 196 ? 4.609   -4.302 -3.377  1.00 78.14  ? 191 ARG A NH2   1 
ATOM   1539 N N     . LEU A 1 197 ? -1.621  -2.151 -4.389  1.00 55.19  ? 192 LEU A N     1 
ATOM   1540 C CA    . LEU A 1 197 ? -2.069  -1.257 -5.450  1.00 57.07  ? 192 LEU A CA    1 
ATOM   1541 C C     . LEU A 1 197 ? -1.472  -1.633 -6.799  1.00 60.05  ? 192 LEU A C     1 
ATOM   1542 O O     . LEU A 1 197 ? -2.056  -1.301 -7.835  1.00 59.81  ? 192 LEU A O     1 
ATOM   1543 C CB    . LEU A 1 197 ? -1.742  0.199  -5.107  1.00 53.74  ? 192 LEU A CB    1 
ATOM   1544 C CG    . LEU A 1 197 ? -0.303  0.716  -5.133  1.00 53.50  ? 192 LEU A CG    1 
ATOM   1545 C CD1   . LEU A 1 197 ? 0.058   1.309  -6.488  1.00 50.59  ? 192 LEU A CD1   1 
ATOM   1546 C CD2   . LEU A 1 197 ? -0.141  1.756  -4.047  1.00 51.01  ? 192 LEU A CD2   1 
ATOM   1547 N N     . THR A 1 198 ? -0.325  -2.316 -6.810  1.00 63.97  ? 193 THR A N     1 
ATOM   1548 C CA    . THR A 1 198 ? 0.202   -2.840 -8.064  1.00 58.99  ? 193 THR A CA    1 
ATOM   1549 C C     . THR A 1 198 ? -0.658  -3.986 -8.578  1.00 62.09  ? 193 THR A C     1 
ATOM   1550 O O     . THR A 1 198 ? -0.977  -4.043 -9.770  1.00 66.60  ? 193 THR A O     1 
ATOM   1551 C CB    . THR A 1 198 ? 1.649   -3.299 -7.884  1.00 59.79  ? 193 THR A CB    1 
ATOM   1552 O OG1   . THR A 1 198 ? 1.721   -4.255 -6.820  1.00 67.22  ? 193 THR A OG1   1 
ATOM   1553 C CG2   . THR A 1 198 ? 2.548   -2.117 -7.560  1.00 56.70  ? 193 THR A CG2   1 
ATOM   1554 N N     . ASP A 1 199 ? -1.051  -4.903 -7.689  1.00 63.67  ? 194 ASP A N     1 
ATOM   1555 C CA    . ASP A 1 199 ? -1.886  -6.028 -8.099  1.00 59.16  ? 194 ASP A CA    1 
ATOM   1556 C C     . ASP A 1 199 ? -3.245  -5.566 -8.606  1.00 61.10  ? 194 ASP A C     1 
ATOM   1557 O O     . ASP A 1 199 ? -3.862  -6.248 -9.433  1.00 67.23  ? 194 ASP A O     1 
ATOM   1558 C CB    . ASP A 1 199 ? -2.058  -7.007 -6.938  1.00 59.68  ? 194 ASP A CB    1 
ATOM   1559 C CG    . ASP A 1 199 ? -0.803  -7.812 -6.664  1.00 67.40  ? 194 ASP A CG    1 
ATOM   1560 O OD1   . ASP A 1 199 ? -0.038  -8.061 -7.618  1.00 71.87  ? 194 ASP A OD1   1 
ATOM   1561 O OD2   . ASP A 1 199 ? -0.583  -8.194 -5.495  1.00 68.65  ? 194 ASP A OD2   1 
ATOM   1562 N N     . LEU A 1 200 ? -3.730  -4.421 -8.126  1.00 60.18  ? 195 LEU A N     1 
ATOM   1563 C CA    . LEU A 1 200 ? -4.970  -3.864 -8.648  1.00 58.54  ? 195 LEU A CA    1 
ATOM   1564 C C     . LEU A 1 200 ? -4.784  -3.203 -10.006 1.00 58.28  ? 195 LEU A C     1 
ATOM   1565 O O     . LEU A 1 200 ? -5.767  -3.020 -10.731 1.00 59.66  ? 195 LEU A O     1 
ATOM   1566 C CB    . LEU A 1 200 ? -5.559  -2.858 -7.656  1.00 59.52  ? 195 LEU A CB    1 
ATOM   1567 C CG    . LEU A 1 200 ? -5.818  -3.375 -6.240  1.00 55.57  ? 195 LEU A CG    1 
ATOM   1568 C CD1   . LEU A 1 200 ? -6.138  -2.224 -5.298  1.00 54.87  ? 195 LEU A CD1   1 
ATOM   1569 C CD2   . LEU A 1 200 ? -6.936  -4.406 -6.235  1.00 58.67  ? 195 LEU A CD2   1 
ATOM   1570 N N     . ILE A 1 201 ? -3.551  -2.842 -10.363 1.00 63.61  ? 196 ILE A N     1 
ATOM   1571 C CA    . ILE A 1 201 ? -3.296  -2.273 -11.682 1.00 63.10  ? 196 ILE A CA    1 
ATOM   1572 C C     . ILE A 1 201 ? -3.206  -3.371 -12.735 1.00 68.25  ? 196 ILE A C     1 
ATOM   1573 O O     . ILE A 1 201 ? -3.760  -3.236 -13.832 1.00 69.59  ? 196 ILE A O     1 
ATOM   1574 C CB    . ILE A 1 201 ? -2.023  -1.405 -11.653 1.00 64.44  ? 196 ILE A CB    1 
ATOM   1575 C CG1   . ILE A 1 201 ? -2.282  -0.099 -10.899 1.00 64.25  ? 196 ILE A CG1   1 
ATOM   1576 C CG2   . ILE A 1 201 ? -1.540  -1.107 -13.063 1.00 68.87  ? 196 ILE A CG2   1 
ATOM   1577 C CD1   . ILE A 1 201 ? -1.034  0.525  -10.312 1.00 63.42  ? 196 ILE A CD1   1 
ATOM   1578 N N     . ARG A 1 202 ? -2.517  -4.473 -12.421 1.00 65.60  ? 197 ARG A N     1 
ATOM   1579 C CA    . ARG A 1 202 ? -2.410  -5.579 -13.369 1.00 66.45  ? 197 ARG A CA    1 
ATOM   1580 C C     . ARG A 1 202 ? -3.783  -6.148 -13.704 1.00 69.23  ? 197 ARG A C     1 
ATOM   1581 O O     . ARG A 1 202 ? -4.148  -6.276 -14.878 1.00 72.01  ? 197 ARG A O     1 
ATOM   1582 C CB    . ARG A 1 202 ? -1.506  -6.676 -12.805 1.00 63.81  ? 197 ARG A CB    1 
ATOM   1583 C CG    . ARG A 1 202 ? -0.354  -6.184 -11.951 1.00 64.72  ? 197 ARG A CG    1 
ATOM   1584 C CD    . ARG A 1 202 ? 0.608   -7.319 -11.646 1.00 65.94  ? 197 ARG A CD    1 
ATOM   1585 N NE    . ARG A 1 202 ? 1.806   -6.865 -10.951 1.00 64.44  ? 197 ARG A NE    1 
ATOM   1586 C CZ    . ARG A 1 202 ? 2.946   -6.553 -11.552 1.00 67.88  ? 197 ARG A CZ    1 
ATOM   1587 N NH1   . ARG A 1 202 ? 3.074   -6.617 -12.867 1.00 77.66  ? 197 ARG A NH1   1 
ATOM   1588 N NH2   . ARG A 1 202 ? 3.983   -6.169 -10.814 1.00 67.26  ? 197 ARG A NH2   1 
ATOM   1589 N N     . SER A 1 203 ? -4.561  -6.497 -12.677 1.00 68.75  ? 198 SER A N     1 
ATOM   1590 C CA    . SER A 1 203 ? -5.891  -7.056 -12.887 1.00 68.61  ? 198 SER A CA    1 
ATOM   1591 C C     . SER A 1 203 ? -6.887  -6.036 -13.420 1.00 65.75  ? 198 SER A C     1 
ATOM   1592 O O     . SER A 1 203 ? -7.995  -6.424 -13.804 1.00 69.77  ? 198 SER A O     1 
ATOM   1593 C CB    . SER A 1 203 ? -6.418  -7.653 -11.581 1.00 66.67  ? 198 SER A CB    1 
ATOM   1594 O OG    . SER A 1 203 ? -6.660  -6.640 -10.619 1.00 64.31  ? 198 SER A OG    1 
ATOM   1595 N N     . GLY A 1 204 ? -6.527  -4.754 -13.455 1.00 63.65  ? 199 GLY A N     1 
ATOM   1596 C CA    . GLY A 1 204 ? -7.437  -3.722 -13.903 1.00 60.91  ? 199 GLY A CA    1 
ATOM   1597 C C     . GLY A 1 204 ? -8.550  -3.384 -12.938 1.00 66.45  ? 199 GLY A C     1 
ATOM   1598 O O     . GLY A 1 204 ? -9.426  -2.585 -13.287 1.00 69.34  ? 199 GLY A O     1 
ATOM   1599 N N     . GLN A 1 205 ? -8.546  -3.965 -11.734 1.00 68.18  ? 200 GLN A N     1 
ATOM   1600 C CA    . GLN A 1 205 ? -9.599  -3.682 -10.765 1.00 64.29  ? 200 GLN A CA    1 
ATOM   1601 C C     . GLN A 1 205 ? -9.568  -2.227 -10.315 1.00 60.72  ? 200 GLN A C     1 
ATOM   1602 O O     . GLN A 1 205 ? -10.603 -1.677 -9.919  1.00 63.99  ? 200 GLN A O     1 
ATOM   1603 C CB    . GLN A 1 205 ? -9.463  -4.624 -9.566  1.00 62.58  ? 200 GLN A CB    1 
ATOM   1604 C CG    . GLN A 1 205 ? -10.493 -4.417 -8.467  1.00 61.88  ? 200 GLN A CG    1 
ATOM   1605 C CD    . GLN A 1 205 ? -10.204 -5.253 -7.235  1.00 67.18  ? 200 GLN A CD    1 
ATOM   1606 O OE1   . GLN A 1 205 ? -9.645  -6.346 -7.331  1.00 68.90  ? 200 GLN A OE1   1 
ATOM   1607 N NE2   . GLN A 1 205 ? -10.586 -4.744 -6.070  1.00 62.01  ? 200 GLN A NE2   1 
ATOM   1608 N N     . LEU A 1 206 ? -8.397  -1.586 -10.379 1.00 59.98  ? 201 LEU A N     1 
ATOM   1609 C CA    . LEU A 1 206 ? -8.299  -0.179 -10.006 1.00 60.33  ? 201 LEU A CA    1 
ATOM   1610 C C     . LEU A 1 206 ? -9.172  0.692  -10.902 1.00 65.46  ? 201 LEU A C     1 
ATOM   1611 O O     . LEU A 1 206 ? -9.885  1.577  -10.416 1.00 64.47  ? 201 LEU A O     1 
ATOM   1612 C CB    . LEU A 1 206 ? -6.842  0.279  -10.072 1.00 61.82  ? 201 LEU A CB    1 
ATOM   1613 C CG    . LEU A 1 206 ? -6.593  1.789  -10.034 1.00 60.09  ? 201 LEU A CG    1 
ATOM   1614 C CD1   . LEU A 1 206 ? -7.082  2.390  -8.721  1.00 55.94  ? 201 LEU A CD1   1 
ATOM   1615 C CD2   . LEU A 1 206 ? -5.122  2.100  -10.260 1.00 58.33  ? 201 LEU A CD2   1 
ATOM   1616 N N     . PHE A 1 207 ? -9.136  0.450  -12.214 1.00 66.60  ? 202 PHE A N     1 
ATOM   1617 C CA    . PHE A 1 207 ? -9.908  1.265  -13.144 1.00 64.11  ? 202 PHE A CA    1 
ATOM   1618 C C     . PHE A 1 207 ? -11.389 0.909  -13.129 1.00 65.57  ? 202 PHE A C     1 
ATOM   1619 O O     . PHE A 1 207 ? -12.233 1.781  -13.367 1.00 70.08  ? 202 PHE A O     1 
ATOM   1620 C CB    . PHE A 1 207 ? -9.336  1.121  -14.554 1.00 64.83  ? 202 PHE A CB    1 
ATOM   1621 C CG    . PHE A 1 207 ? -7.852  1.332  -14.623 1.00 66.52  ? 202 PHE A CG    1 
ATOM   1622 C CD1   . PHE A 1 207 ? -7.313  2.600  -14.481 1.00 62.61  ? 202 PHE A CD1   1 
ATOM   1623 C CD2   . PHE A 1 207 ? -6.995  0.262  -14.814 1.00 67.50  ? 202 PHE A CD2   1 
ATOM   1624 C CE1   . PHE A 1 207 ? -5.948  2.798  -14.538 1.00 61.14  ? 202 PHE A CE1   1 
ATOM   1625 C CE2   . PHE A 1 207 ? -5.628  0.454  -14.872 1.00 66.75  ? 202 PHE A CE2   1 
ATOM   1626 C CZ    . PHE A 1 207 ? -5.104  1.724  -14.734 1.00 65.01  ? 202 PHE A CZ    1 
ATOM   1627 N N     . LYS A 1 208 ? -11.723 -0.356 -12.858 1.00 69.16  ? 203 LYS A N     1 
ATOM   1628 C CA    . LYS A 1 208 ? -13.125 -0.734 -12.722 1.00 65.97  ? 203 LYS A CA    1 
ATOM   1629 C C     . LYS A 1 208 ? -13.750 -0.106 -11.482 1.00 66.15  ? 203 LYS A C     1 
ATOM   1630 O O     . LYS A 1 208 ? -14.932 0.260  -11.501 1.00 68.87  ? 203 LYS A O     1 
ATOM   1631 C CB    . LYS A 1 208 ? -13.254 -2.258 -12.675 1.00 64.17  ? 203 LYS A CB    1 
ATOM   1632 C CG    . LYS A 1 208 ? -14.267 -2.780 -11.663 1.00 66.02  ? 203 LYS A CG    1 
ATOM   1633 C CD    . LYS A 1 208 ? -14.195 -4.293 -11.527 1.00 71.68  ? 203 LYS A CD    1 
ATOM   1634 C CE    . LYS A 1 208 ? -13.750 -4.696 -10.130 1.00 78.43  ? 203 LYS A CE    1 
ATOM   1635 N NZ    . LYS A 1 208 ? -13.771 -6.172 -9.940  1.00 73.73  ? 203 LYS A NZ    1 
ATOM   1636 N N     . ASP A 1 209 ? -12.971 0.048  -10.409 1.00 65.99  ? 204 ASP A N     1 
ATOM   1637 C CA    . ASP A 1 209 ? -13.511 0.570  -9.159  1.00 64.20  ? 204 ASP A CA    1 
ATOM   1638 C C     . ASP A 1 209 ? -13.669 2.085  -9.196  1.00 62.22  ? 204 ASP A C     1 
ATOM   1639 O O     . ASP A 1 209 ? -14.677 2.615  -8.717  1.00 67.63  ? 204 ASP A O     1 
ATOM   1640 C CB    . ASP A 1 209 ? -12.612 0.156  -7.996  1.00 66.54  ? 204 ASP A CB    1 
ATOM   1641 C CG    . ASP A 1 209 ? -12.854 -1.271 -7.551  1.00 61.55  ? 204 ASP A CG    1 
ATOM   1642 O OD1   . ASP A 1 209 ? -13.818 -1.893 -8.039  1.00 61.04  ? 204 ASP A OD1   1 
ATOM   1643 O OD2   . ASP A 1 209 ? -12.072 -1.772 -6.714  1.00 64.68  ? 204 ASP A OD2   1 
ATOM   1644 N N     . VAL A 1 210 ? -12.688 2.799  -9.754  1.00 62.98  ? 205 VAL A N     1 
ATOM   1645 C CA    . VAL A 1 210 ? -12.747 4.260  -9.781  1.00 63.53  ? 205 VAL A CA    1 
ATOM   1646 C C     . VAL A 1 210 ? -13.553 4.801  -10.949 1.00 65.02  ? 205 VAL A C     1 
ATOM   1647 O O     . VAL A 1 210 ? -13.810 6.010  -11.001 1.00 62.24  ? 205 VAL A O     1 
ATOM   1648 C CB    . VAL A 1 210 ? -11.336 4.876  -9.827  1.00 61.60  ? 205 VAL A CB    1 
ATOM   1649 C CG1   . VAL A 1 210 ? -10.478 4.329  -8.695  1.00 63.85  ? 205 VAL A CG1   1 
ATOM   1650 C CG2   . VAL A 1 210 ? -10.686 4.620  -11.176 1.00 64.44  ? 205 VAL A CG2   1 
ATOM   1651 N N     . GLY A 1 211 ? -13.956 3.948  -11.888 1.00 66.42  ? 206 GLY A N     1 
ATOM   1652 C CA    . GLY A 1 211 ? -14.789 4.394  -12.987 1.00 67.07  ? 206 GLY A CA    1 
ATOM   1653 C C     . GLY A 1 211 ? -14.077 5.188  -14.056 1.00 69.47  ? 206 GLY A C     1 
ATOM   1654 O O     . GLY A 1 211 ? -14.729 5.915  -14.809 1.00 73.62  ? 206 GLY A O     1 
ATOM   1655 N N     . LEU A 1 212 ? -12.754 5.073  -14.148 1.00 71.38  ? 207 LEU A N     1 
ATOM   1656 C CA    . LEU A 1 212 ? -11.988 5.762  -15.170 1.00 67.84  ? 207 LEU A CA    1 
ATOM   1657 C C     . LEU A 1 212 ? -11.320 4.755  -16.099 1.00 68.02  ? 207 LEU A C     1 
ATOM   1658 O O     . LEU A 1 212 ? -10.991 3.642  -15.678 1.00 68.73  ? 207 LEU A O     1 
ATOM   1659 C CB    . LEU A 1 212 ? -10.918 6.669  -14.548 1.00 62.79  ? 207 LEU A CB    1 
ATOM   1660 C CG    . LEU A 1 212 ? -11.423 7.875  -13.753 1.00 62.90  ? 207 LEU A CG    1 
ATOM   1661 C CD1   . LEU A 1 212 ? -10.266 8.593  -13.078 1.00 60.42  ? 207 LEU A CD1   1 
ATOM   1662 C CD2   . LEU A 1 212 ? -12.196 8.827  -14.653 1.00 63.80  ? 207 LEU A CD2   1 
ATOM   1663 N N     . PRO A 1 213 ? -11.116 5.111  -17.367 1.00 69.72  ? 208 PRO A N     1 
ATOM   1664 C CA    . PRO A 1 213 ? -10.437 4.197  -18.293 1.00 72.25  ? 208 PRO A CA    1 
ATOM   1665 C C     . PRO A 1 213 ? -8.996  3.950  -17.873 1.00 69.39  ? 208 PRO A C     1 
ATOM   1666 O O     . PRO A 1 213 ? -8.450  4.594  -16.973 1.00 66.76  ? 208 PRO A O     1 
ATOM   1667 C CB    . PRO A 1 213 ? -10.512 4.930  -19.638 1.00 73.24  ? 208 PRO A CB    1 
ATOM   1668 C CG    . PRO A 1 213 ? -11.657 5.879  -19.486 1.00 69.01  ? 208 PRO A CG    1 
ATOM   1669 C CD    . PRO A 1 213 ? -11.616 6.314  -18.053 1.00 67.81  ? 208 PRO A CD    1 
ATOM   1670 N N     . GLU A 1 214 ? -8.371  2.989  -18.550 1.00 66.90  ? 209 GLU A N     1 
ATOM   1671 C CA    . GLU A 1 214 ? -6.994  2.631  -18.254 1.00 64.79  ? 209 GLU A CA    1 
ATOM   1672 C C     . GLU A 1 214 ? -6.058  3.803  -18.549 1.00 63.02  ? 209 GLU A C     1 
ATOM   1673 O O     . GLU A 1 214 ? -6.428  4.789  -19.189 1.00 68.31  ? 209 GLU A O     1 
ATOM   1674 C CB    . GLU A 1 214 ? -6.576  1.402  -19.061 1.00 66.97  ? 209 GLU A CB    1 
ATOM   1675 C CG    . GLU A 1 214 ? -6.750  0.083  -18.327 1.00 70.21  ? 209 GLU A CG    1 
ATOM   1676 C CD    . GLU A 1 214 ? -5.608  -0.882 -18.584 1.00 73.64  ? 209 GLU A CD    1 
ATOM   1677 O OE1   . GLU A 1 214 ? -4.830  -0.644 -19.531 1.00 67.61  ? 209 GLU A OE1   1 
ATOM   1678 O OE2   . GLU A 1 214 ? -5.488  -1.877 -17.838 1.00 71.60  ? 209 GLU A OE2   1 
ATOM   1679 N N     . PHE A 1 215 ? -4.824  3.679  -18.064 1.00 62.76  ? 210 PHE A N     1 
ATOM   1680 C CA    . PHE A 1 215 ? -3.825  4.717  -18.281 1.00 63.90  ? 210 PHE A CA    1 
ATOM   1681 C C     . PHE A 1 215 ? -3.552  4.903  -19.768 1.00 63.18  ? 210 PHE A C     1 
ATOM   1682 O O     . PHE A 1 215 ? -3.296  3.937  -20.491 1.00 67.89  ? 210 PHE A O     1 
ATOM   1683 C CB    . PHE A 1 215 ? -2.524  4.365  -17.557 1.00 65.79  ? 210 PHE A CB    1 
ATOM   1684 C CG    . PHE A 1 215 ? -2.635  4.353  -16.059 1.00 65.28  ? 210 PHE A CG    1 
ATOM   1685 C CD1   . PHE A 1 215 ? -3.508  5.203  -15.404 1.00 63.74  ? 210 PHE A CD1   1 
ATOM   1686 C CD2   . PHE A 1 215 ? -1.849  3.496  -15.306 1.00 68.71  ? 210 PHE A CD2   1 
ATOM   1687 C CE1   . PHE A 1 215 ? -3.600  5.194  -14.023 1.00 62.57  ? 210 PHE A CE1   1 
ATOM   1688 C CE2   . PHE A 1 215 ? -1.937  3.481  -13.927 1.00 70.35  ? 210 PHE A CE2   1 
ATOM   1689 C CZ    . PHE A 1 215 ? -2.814  4.330  -13.285 1.00 65.38  ? 210 PHE A CZ    1 
ATOM   1690 N N     . ASN A 1 216 ? -3.611  6.152  -20.223 1.00 60.46  ? 211 ASN A N     1 
ATOM   1691 C CA    . ASN A 1 216 ? -3.200  6.512  -21.570 1.00 62.99  ? 211 ASN A CA    1 
ATOM   1692 C C     . ASN A 1 216 ? -2.299  7.738  -21.498 1.00 61.69  ? 211 ASN A C     1 
ATOM   1693 O O     . ASN A 1 216 ? -2.357  8.523  -20.548 1.00 62.13  ? 211 ASN A O     1 
ATOM   1694 C CB    . ASN A 1 216 ? -4.405  6.769  -22.493 1.00 59.36  ? 211 ASN A CB    1 
ATOM   1695 C CG    . ASN A 1 216 ? -5.198  8.000  -22.101 1.00 60.21  ? 211 ASN A CG    1 
ATOM   1696 O OD1   . ASN A 1 216 ? -4.761  9.132  -22.309 1.00 62.24  ? 211 ASN A OD1   1 
ATOM   1697 N ND2   . ASN A 1 216 ? -6.380  7.783  -21.535 1.00 60.86  ? 211 ASN A ND2   1 
ATOM   1698 N N     . HIS A 1 217 ? -1.460  7.893  -22.522 1.00 61.88  ? 212 HIS A N     1 
ATOM   1699 C CA    . HIS A 1 217 ? -0.423  8.918  -22.508 1.00 61.55  ? 212 HIS A CA    1 
ATOM   1700 C C     . HIS A 1 217 ? -0.973  10.334 -22.620 1.00 57.63  ? 212 HIS A C     1 
ATOM   1701 O O     . HIS A 1 217 ? -0.216  11.288 -22.409 1.00 55.46  ? 212 HIS A O     1 
ATOM   1702 C CB    . HIS A 1 217 ? 0.571   8.663  -23.642 1.00 62.06  ? 212 HIS A CB    1 
ATOM   1703 C CG    . HIS A 1 217 ? 1.167   7.291  -23.623 1.00 57.88  ? 212 HIS A CG    1 
ATOM   1704 N ND1   . HIS A 1 217 ? 1.757   6.721  -24.731 1.00 62.73  ? 212 HIS A ND1   1 
ATOM   1705 C CD2   . HIS A 1 217 ? 1.267   6.374  -22.631 1.00 53.48  ? 212 HIS A CD2   1 
ATOM   1706 C CE1   . HIS A 1 217 ? 2.193   5.513  -24.423 1.00 61.84  ? 212 HIS A CE1   1 
ATOM   1707 N NE2   . HIS A 1 217 ? 1.908   5.278  -23.155 1.00 57.12  ? 212 HIS A NE2   1 
ATOM   1708 N N     . GLU A 1 218 ? -2.254  10.500 -22.940 1.00 57.90  ? 213 GLU A N     1 
ATOM   1709 C CA    . GLU A 1 218 ? -2.826  11.823 -23.160 1.00 64.78  ? 213 GLU A CA    1 
ATOM   1710 C C     . GLU A 1 218 ? -3.551  12.375 -21.939 1.00 66.16  ? 213 GLU A C     1 
ATOM   1711 O O     . GLU A 1 218 ? -3.433  13.568 -21.643 1.00 65.11  ? 213 GLU A O     1 
ATOM   1712 C CB    . GLU A 1 218 ? -3.786  11.783 -24.356 1.00 71.89  ? 213 GLU A CB    1 
ATOM   1713 C CG    . GLU A 1 218 ? -4.995  12.699 -24.233 1.00 79.18  ? 213 GLU A CG    1 
ATOM   1714 C CD    . GLU A 1 218 ? -5.895  12.653 -25.453 1.00 83.48  ? 213 GLU A CD    1 
ATOM   1715 O OE1   . GLU A 1 218 ? -5.485  12.064 -26.475 1.00 89.22  ? 213 GLU A OE1   1 
ATOM   1716 O OE2   . GLU A 1 218 ? -7.015  13.202 -25.387 1.00 84.27  ? 213 GLU A OE2   1 
ATOM   1717 N N     . ASP A 1 219 ? -4.283  11.533 -21.211 1.00 63.63  ? 214 ASP A N     1 
ATOM   1718 C CA    . ASP A 1 219 ? -5.142  12.002 -20.130 1.00 64.98  ? 214 ASP A CA    1 
ATOM   1719 C C     . ASP A 1 219 ? -4.464  11.941 -18.763 1.00 60.10  ? 214 ASP A C     1 
ATOM   1720 O O     . ASP A 1 219 ? -4.529  12.905 -17.993 1.00 58.00  ? 214 ASP A O     1 
ATOM   1721 C CB    . ASP A 1 219 ? -6.434  11.178 -20.098 1.00 62.77  ? 214 ASP A CB    1 
ATOM   1722 C CG    . ASP A 1 219 ? -7.329  11.445 -21.291 1.00 65.48  ? 214 ASP A CG    1 
ATOM   1723 O OD1   . ASP A 1 219 ? -7.196  12.525 -21.904 1.00 70.84  ? 214 ASP A OD1   1 
ATOM   1724 O OD2   . ASP A 1 219 ? -8.167  10.576 -21.615 1.00 64.13  ? 214 ASP A OD2   1 
ATOM   1725 N N     . ASP A 1 220 ? -3.808  10.827 -18.453 1.00 56.41  ? 215 ASP A N     1 
ATOM   1726 C CA    . ASP A 1 220 ? -3.466  10.475 -17.081 1.00 50.85  ? 215 ASP A CA    1 
ATOM   1727 C C     . ASP A 1 220 ? -2.048  10.905 -16.729 1.00 50.94  ? 215 ASP A C     1 
ATOM   1728 O O     . ASP A 1 220 ? -1.094  10.578 -17.443 1.00 52.15  ? 215 ASP A O     1 
ATOM   1729 C CB    . ASP A 1 220 ? -3.628  8.970  -16.870 1.00 52.56  ? 215 ASP A CB    1 
ATOM   1730 C CG    . ASP A 1 220 ? -5.008  8.477  -17.255 1.00 54.63  ? 215 ASP A CG    1 
ATOM   1731 O OD1   . ASP A 1 220 ? -5.986  8.863  -16.581 1.00 55.99  ? 215 ASP A OD1   1 
ATOM   1732 O OD2   . ASP A 1 220 ? -5.118  7.717  -18.240 1.00 57.59  ? 215 ASP A OD2   1 
ATOM   1733 N N     . ARG A 1 221 ? -1.922  11.635 -15.623 1.00 51.30  ? 216 ARG A N     1 
ATOM   1734 C CA    . ARG A 1 221 ? -0.647  11.930 -14.991 1.00 49.72  ? 216 ARG A CA    1 
ATOM   1735 C C     . ARG A 1 221 ? -0.636  11.299 -13.605 1.00 50.64  ? 216 ARG A C     1 
ATOM   1736 O O     . ARG A 1 221 ? -1.685  11.138 -12.975 1.00 51.81  ? 216 ARG A O     1 
ATOM   1737 C CB    . ARG A 1 221 ? -0.400  13.439 -14.887 1.00 48.01  ? 216 ARG A CB    1 
ATOM   1738 C CG    . ARG A 1 221 ? -0.663  14.202 -16.173 1.00 51.71  ? 216 ARG A CG    1 
ATOM   1739 C CD    . ARG A 1 221 ? 0.359   13.853 -17.245 1.00 54.33  ? 216 ARG A CD    1 
ATOM   1740 N NE    . ARG A 1 221 ? 0.005   14.425 -18.538 1.00 57.50  ? 216 ARG A NE    1 
ATOM   1741 C CZ    . ARG A 1 221 ? -0.388  13.717 -19.589 1.00 56.34  ? 216 ARG A CZ    1 
ATOM   1742 N NH1   . ARG A 1 221 ? -0.488  12.399 -19.536 1.00 56.84  ? 216 ARG A NH1   1 
ATOM   1743 N NH2   . ARG A 1 221 ? -0.687  14.348 -20.721 1.00 58.51  ? 216 ARG A NH2   1 
ATOM   1744 N N     . MET A 1 222 ? 0.553   10.937 -13.134 1.00 49.68  ? 217 MET A N     1 
ATOM   1745 C CA    . MET A 1 222 ? 0.686   10.201 -11.886 1.00 46.60  ? 217 MET A CA    1 
ATOM   1746 C C     . MET A 1 222 ? 1.717   10.854 -10.980 1.00 48.09  ? 217 MET A C     1 
ATOM   1747 O O     . MET A 1 222 ? 2.677   11.475 -11.442 1.00 49.30  ? 217 MET A O     1 
ATOM   1748 C CB    . MET A 1 222 ? 1.082   8.738  -12.133 1.00 48.64  ? 217 MET A CB    1 
ATOM   1749 C CG    . MET A 1 222 ? 0.176   7.996  -13.100 1.00 50.09  ? 217 MET A CG    1 
ATOM   1750 S SD    . MET A 1 222 ? 0.601   8.299  -14.824 1.00 61.59  ? 217 MET A SD    1 
ATOM   1751 C CE    . MET A 1 222 ? -0.518  7.172  -15.648 1.00 47.33  ? 217 MET A CE    1 
ATOM   1752 N N     . MET A 1 223 ? 1.500   10.702 -9.676  1.00 48.57  ? 218 MET A N     1 
ATOM   1753 C CA    . MET A 1 223 ? 2.475   11.066 -8.656  1.00 42.49  ? 218 MET A CA    1 
ATOM   1754 C C     . MET A 1 223 ? 2.615   9.890  -7.703  1.00 43.88  ? 218 MET A C     1 
ATOM   1755 O O     . MET A 1 223 ? 1.630   9.466  -7.089  1.00 46.48  ? 218 MET A O     1 
ATOM   1756 C CB    . MET A 1 223 ? 2.058   12.328 -7.900  1.00 45.61  ? 218 MET A CB    1 
ATOM   1757 C CG    . MET A 1 223 ? 2.665   13.602 -8.446  1.00 40.02  ? 218 MET A CG    1 
ATOM   1758 S SD    . MET A 1 223 ? 2.197   15.031 -7.461  1.00 49.11  ? 218 MET A SD    1 
ATOM   1759 C CE    . MET A 1 223 ? 2.171   16.313 -8.707  1.00 41.44  ? 218 MET A CE    1 
ATOM   1760 N N     . LEU A 1 224 ? 3.829   9.362  -7.591  1.00 45.42  ? 219 LEU A N     1 
ATOM   1761 C CA    . LEU A 1 224 ? 4.094   8.146  -6.835  1.00 42.07  ? 219 LEU A CA    1 
ATOM   1762 C C     . LEU A 1 224 ? 4.933   8.476  -5.609  1.00 42.32  ? 219 LEU A C     1 
ATOM   1763 O O     . LEU A 1 224 ? 6.003   9.083  -5.728  1.00 46.18  ? 219 LEU A O     1 
ATOM   1764 C CB    . LEU A 1 224 ? 4.813   7.107  -7.701  1.00 46.60  ? 219 LEU A CB    1 
ATOM   1765 C CG    . LEU A 1 224 ? 4.024   6.257  -8.707  1.00 44.04  ? 219 LEU A CG    1 
ATOM   1766 C CD1   . LEU A 1 224 ? 3.287   7.104  -9.735  1.00 46.95  ? 219 LEU A CD1   1 
ATOM   1767 C CD2   . LEU A 1 224 ? 4.950   5.258  -9.391  1.00 42.34  ? 219 LEU A CD2   1 
ATOM   1768 N N     . CYS A 1 225 ? 4.450   8.067  -4.436  1.00 42.87  ? 220 CYS A N     1 
ATOM   1769 C CA    . CYS A 1 225 ? 5.168   8.304  -3.185  1.00 43.28  ? 220 CYS A CA    1 
ATOM   1770 C C     . CYS A 1 225 ? 4.799   7.181  -2.219  1.00 45.69  ? 220 CYS A C     1 
ATOM   1771 O O     . CYS A 1 225 ? 3.767   7.256  -1.548  1.00 48.98  ? 220 CYS A O     1 
ATOM   1772 C CB    . CYS A 1 225 ? 4.831   9.672  -2.610  1.00 42.50  ? 220 CYS A CB    1 
ATOM   1773 S SG    . CYS A 1 225 ? 5.892   10.187 -1.242  1.00 45.39  ? 220 CYS A SG    1 
ATOM   1774 N N     . GLY A 1 226 ? 5.636   6.163  -2.151  1.00 45.70  ? 221 GLY A N     1 
ATOM   1775 C CA    . GLY A 1 226 ? 5.379   5.026  -1.288  1.00 44.12  ? 221 GLY A CA    1 
ATOM   1776 C C     . GLY A 1 226 ? 6.636   4.247  -0.973  1.00 48.61  ? 221 GLY A C     1 
ATOM   1777 O O     . GLY A 1 226 ? 7.744   4.787  -0.998  1.00 52.11  ? 221 GLY A O     1 
ATOM   1778 N N     . SER A 1 227 ? 6.455   2.962  -0.674  1.00 52.18  ? 222 SER A N     1 
ATOM   1779 C CA    . SER A 1 227 ? 7.566   2.094  -0.327  1.00 52.35  ? 222 SER A CA    1 
ATOM   1780 C C     . SER A 1 227 ? 8.458   1.849  -1.542  1.00 52.06  ? 222 SER A C     1 
ATOM   1781 O O     . SER A 1 227 ? 8.018   1.983  -2.687  1.00 52.53  ? 222 SER A O     1 
ATOM   1782 C CB    . SER A 1 227 ? 7.046   0.767  0.220   1.00 50.90  ? 222 SER A CB    1 
ATOM   1783 O OG    . SER A 1 227 ? 6.261   0.093  -0.747  1.00 49.65  ? 222 SER A OG    1 
ATOM   1784 N N     . PRO A 1 228 ? 9.728   1.501  -1.316  1.00 55.93  ? 223 PRO A N     1 
ATOM   1785 C CA    . PRO A 1 228 ? 10.618  1.221  -2.455  1.00 58.93  ? 223 PRO A CA    1 
ATOM   1786 C C     . PRO A 1 228 ? 10.153  0.056  -3.310  1.00 59.55  ? 223 PRO A C     1 
ATOM   1787 O O     . PRO A 1 228 ? 10.398  0.053  -4.523  1.00 59.14  ? 223 PRO A O     1 
ATOM   1788 C CB    . PRO A 1 228 ? 11.965  0.926  -1.779  1.00 61.02  ? 223 PRO A CB    1 
ATOM   1789 C CG    . PRO A 1 228 ? 11.888  1.646  -0.468  1.00 58.49  ? 223 PRO A CG    1 
ATOM   1790 C CD    . PRO A 1 228 ? 10.458  1.533  -0.037  1.00 57.66  ? 223 PRO A CD    1 
ATOM   1791 N N     . GLU A 1 229 ? 9.479   -0.932 -2.717  1.00 62.14  ? 224 GLU A N     1 
ATOM   1792 C CA    . GLU A 1 229 ? 9.013   -2.076 -3.490  1.00 63.85  ? 224 GLU A CA    1 
ATOM   1793 C C     . GLU A 1 229 ? 7.756   -1.748 -4.286  1.00 59.08  ? 224 GLU A C     1 
ATOM   1794 O O     . GLU A 1 229 ? 7.510   -2.368 -5.326  1.00 61.42  ? 224 GLU A O     1 
ATOM   1795 C CB    . GLU A 1 229 ? 8.759   -3.272 -2.570  1.00 71.12  ? 224 GLU A CB    1 
ATOM   1796 C CG    . GLU A 1 229 ? 9.251   -4.594 -3.150  1.00 85.88  ? 224 GLU A CG    1 
ATOM   1797 C CD    . GLU A 1 229 ? 8.825   -5.805 -2.337  1.00 89.68  ? 224 GLU A CD    1 
ATOM   1798 O OE1   . GLU A 1 229 ? 7.802   -6.426 -2.697  1.00 86.29  ? 224 GLU A OE1   1 
ATOM   1799 O OE2   . GLU A 1 229 ? 9.505   -6.136 -1.341  1.00 86.76  ? 224 GLU A OE2   1 
ATOM   1800 N N     . MET A 1 230 ? 6.948   -0.791 -3.819  1.00 56.82  ? 225 MET A N     1 
ATOM   1801 C CA    . MET A 1 230 ? 5.823   -0.322 -4.621  1.00 54.28  ? 225 MET A CA    1 
ATOM   1802 C C     . MET A 1 230 ? 6.288   0.618  -5.724  1.00 54.28  ? 225 MET A C     1 
ATOM   1803 O O     . MET A 1 230 ? 5.779   0.561  -6.849  1.00 59.87  ? 225 MET A O     1 
ATOM   1804 C CB    . MET A 1 230 ? 4.782   0.355  -3.724  1.00 53.05  ? 225 MET A CB    1 
ATOM   1805 C CG    . MET A 1 230 ? 3.810   1.299  -4.441  1.00 43.02  ? 225 MET A CG    1 
ATOM   1806 S SD    . MET A 1 230 ? 4.387   3.002  -4.645  1.00 53.01  ? 225 MET A SD    1 
ATOM   1807 C CE    . MET A 1 230 ? 2.834   3.897  -4.692  1.00 46.59  ? 225 MET A CE    1 
ATOM   1808 N N     . LEU A 1 231 ? 7.253   1.486  -5.416  1.00 51.59  ? 226 LEU A N     1 
ATOM   1809 C CA    . LEU A 1 231 ? 7.758   2.427  -6.411  1.00 50.83  ? 226 LEU A CA    1 
ATOM   1810 C C     . LEU A 1 231 ? 8.419   1.696  -7.573  1.00 56.46  ? 226 LEU A C     1 
ATOM   1811 O O     . LEU A 1 231 ? 8.099   1.944  -8.741  1.00 56.20  ? 226 LEU A O     1 
ATOM   1812 C CB    . LEU A 1 231 ? 8.743   3.399  -5.759  1.00 47.97  ? 226 LEU A CB    1 
ATOM   1813 C CG    . LEU A 1 231 ? 8.151   4.510  -4.891  1.00 50.41  ? 226 LEU A CG    1 
ATOM   1814 C CD1   . LEU A 1 231 ? 9.244   5.436  -4.381  1.00 46.59  ? 226 LEU A CD1   1 
ATOM   1815 C CD2   . LEU A 1 231 ? 7.106   5.287  -5.667  1.00 46.01  ? 226 LEU A CD2   1 
ATOM   1816 N N     . ALA A 1 232 ? 9.345   0.781  -7.270  1.00 59.98  ? 227 ALA A N     1 
ATOM   1817 C CA    . ALA A 1 232 ? 10.046  0.055  -8.325  1.00 56.00  ? 227 ALA A CA    1 
ATOM   1818 C C     . ALA A 1 232 ? 9.106   -0.853 -9.108  1.00 53.57  ? 227 ALA A C     1 
ATOM   1819 O O     . ALA A 1 232 ? 9.365   -1.146 -10.281 1.00 53.59  ? 227 ALA A O     1 
ATOM   1820 C CB    . ALA A 1 232 ? 11.193  -0.759 -7.728  1.00 58.81  ? 227 ALA A CB    1 
ATOM   1821 N N     . GLU A 1 233 ? 8.018   -1.305 -8.485  1.00 56.74  ? 228 GLU A N     1 
ATOM   1822 C CA    . GLU A 1 233 ? 7.077   -2.177 -9.179  1.00 53.83  ? 228 GLU A CA    1 
ATOM   1823 C C     . GLU A 1 233 ? 6.101   -1.379 -10.036 1.00 55.88  ? 228 GLU A C     1 
ATOM   1824 O O     . GLU A 1 233 ? 5.741   -1.811 -11.137 1.00 56.60  ? 228 GLU A O     1 
ATOM   1825 C CB    . GLU A 1 233 ? 6.324   -3.042 -8.169  1.00 58.30  ? 228 GLU A CB    1 
ATOM   1826 C CG    . GLU A 1 233 ? 5.517   -4.161 -8.793  1.00 61.00  ? 228 GLU A CG    1 
ATOM   1827 C CD    . GLU A 1 233 ? 5.131   -5.233 -7.794  1.00 64.28  ? 228 GLU A CD    1 
ATOM   1828 O OE1   . GLU A 1 233 ? 5.791   -5.331 -6.738  1.00 61.07  ? 228 GLU A OE1   1 
ATOM   1829 O OE2   . GLU A 1 233 ? 4.170   -5.982 -8.068  1.00 69.63  ? 228 GLU A OE2   1 
ATOM   1830 N N     . THR A 1 234 ? 5.666   -0.213 -9.551  1.00 56.88  ? 229 THR A N     1 
ATOM   1831 C CA    . THR A 1 234 ? 4.782   0.638  -10.339 1.00 53.52  ? 229 THR A CA    1 
ATOM   1832 C C     . THR A 1 234 ? 5.544   1.416  -11.406 1.00 51.40  ? 229 THR A C     1 
ATOM   1833 O O     . THR A 1 234 ? 4.967   1.761  -12.444 1.00 55.58  ? 229 THR A O     1 
ATOM   1834 C CB    . THR A 1 234 ? 4.027   1.607  -9.426  1.00 51.40  ? 229 THR A CB    1 
ATOM   1835 O OG1   . THR A 1 234 ? 3.662   0.935  -8.214  1.00 47.82  ? 229 THR A OG1   1 
ATOM   1836 C CG2   . THR A 1 234 ? 2.767   2.115  -10.111 1.00 50.83  ? 229 THR A CG2   1 
ATOM   1837 N N     . LYS A 1 235 ? 6.828   1.701  -11.173 1.00 49.99  ? 230 LYS A N     1 
ATOM   1838 C CA    . LYS A 1 235 ? 7.627   2.384  -12.186 1.00 51.30  ? 230 LYS A CA    1 
ATOM   1839 C C     . LYS A 1 235 ? 7.860   1.491  -13.397 1.00 57.06  ? 230 LYS A C     1 
ATOM   1840 O O     . LYS A 1 235 ? 7.837   1.965  -14.539 1.00 56.02  ? 230 LYS A O     1 
ATOM   1841 C CB    . LYS A 1 235 ? 8.959   2.839  -11.589 1.00 50.44  ? 230 LYS A CB    1 
ATOM   1842 C CG    . LYS A 1 235 ? 9.847   3.617  -12.544 1.00 54.79  ? 230 LYS A CG    1 
ATOM   1843 C CD    . LYS A 1 235 ? 10.990  4.281  -11.793 1.00 56.48  ? 230 LYS A CD    1 
ATOM   1844 C CE    . LYS A 1 235 ? 11.847  5.130  -12.715 1.00 60.11  ? 230 LYS A CE    1 
ATOM   1845 N NZ    . LYS A 1 235 ? 12.881  4.322  -13.413 1.00 70.83  ? 230 LYS A NZ    1 
ATOM   1846 N N     . GLN A 1 236 ? 8.091   0.196  -13.169 1.00 62.13  ? 231 GLN A N     1 
ATOM   1847 C CA    . GLN A 1 236 ? 8.198   -0.741 -14.282 1.00 54.53  ? 231 GLN A CA    1 
ATOM   1848 C C     . GLN A 1 236 ? 6.869   -0.875 -15.013 1.00 54.78  ? 231 GLN A C     1 
ATOM   1849 O O     . GLN A 1 236 ? 6.837   -0.950 -16.247 1.00 58.29  ? 231 GLN A O     1 
ATOM   1850 C CB    . GLN A 1 236 ? 8.679   -2.104 -13.780 1.00 52.90  ? 231 GLN A CB    1 
ATOM   1851 C CG    . GLN A 1 236 ? 8.265   -3.275 -14.660 1.00 59.41  ? 231 GLN A CG    1 
ATOM   1852 C CD    . GLN A 1 236 ? 9.248   -4.428 -14.607 1.00 67.30  ? 231 GLN A CD    1 
ATOM   1853 O OE1   . GLN A 1 236 ? 10.462  -4.225 -14.631 1.00 69.92  ? 231 GLN A OE1   1 
ATOM   1854 N NE2   . GLN A 1 236 ? 8.727   -5.648 -14.540 1.00 61.10  ? 231 GLN A NE2   1 
ATOM   1855 N N     . ILE A 1 237 ? 5.762   -0.897 -14.268 1.00 56.51  ? 232 ILE A N     1 
ATOM   1856 C CA    . ILE A 1 237 ? 4.445   -0.977 -14.892 1.00 52.22  ? 232 ILE A CA    1 
ATOM   1857 C C     . ILE A 1 237 ? 4.194   0.247  -15.764 1.00 51.92  ? 232 ILE A C     1 
ATOM   1858 O O     . ILE A 1 237 ? 3.711   0.130  -16.896 1.00 54.42  ? 232 ILE A O     1 
ATOM   1859 C CB    . ILE A 1 237 ? 3.355   -1.142 -13.817 1.00 57.37  ? 232 ILE A CB    1 
ATOM   1860 C CG1   . ILE A 1 237 ? 3.339   -2.579 -13.290 1.00 59.87  ? 232 ILE A CG1   1 
ATOM   1861 C CG2   . ILE A 1 237 ? 1.989   -0.761 -14.369 1.00 54.92  ? 232 ILE A CG2   1 
ATOM   1862 C CD1   . ILE A 1 237 ? 2.484   -2.767 -12.057 1.00 57.39  ? 232 ILE A CD1   1 
ATOM   1863 N N     . LEU A 1 238 ? 4.536   1.435  -15.264 1.00 53.08  ? 233 LEU A N     1 
ATOM   1864 C CA    . LEU A 1 238 ? 4.252   2.658  -16.010 1.00 49.81  ? 233 LEU A CA    1 
ATOM   1865 C C     . LEU A 1 238 ? 5.181   2.815  -17.209 1.00 49.80  ? 233 LEU A C     1 
ATOM   1866 O O     . LEU A 1 238 ? 4.744   3.239  -18.285 1.00 53.23  ? 233 LEU A O     1 
ATOM   1867 C CB    . LEU A 1 238 ? 4.362   3.871  -15.087 1.00 52.31  ? 233 LEU A CB    1 
ATOM   1868 C CG    . LEU A 1 238 ? 3.261   4.036  -14.038 1.00 49.79  ? 233 LEU A CG    1 
ATOM   1869 C CD1   . LEU A 1 238 ? 3.412   5.364  -13.315 1.00 50.04  ? 233 LEU A CD1   1 
ATOM   1870 C CD2   . LEU A 1 238 ? 1.886   3.923  -14.677 1.00 53.50  ? 233 LEU A CD2   1 
ATOM   1871 N N     . GLU A 1 239 ? 6.463   2.480  -17.047 1.00 54.32  ? 234 GLU A N     1 
ATOM   1872 C CA    . GLU A 1 239 ? 7.424   2.719  -18.119 1.00 49.09  ? 234 GLU A CA    1 
ATOM   1873 C C     . GLU A 1 239 ? 7.238   1.753  -19.285 1.00 48.41  ? 234 GLU A C     1 
ATOM   1874 O O     . GLU A 1 239 ? 7.555   2.101  -20.428 1.00 55.22  ? 234 GLU A O     1 
ATOM   1875 C CB    . GLU A 1 239 ? 8.851   2.629  -17.578 1.00 50.81  ? 234 GLU A CB    1 
ATOM   1876 C CG    . GLU A 1 239 ? 9.298   3.859  -16.802 1.00 54.34  ? 234 GLU A CG    1 
ATOM   1877 C CD    . GLU A 1 239 ? 10.772  3.823  -16.446 1.00 51.22  ? 234 GLU A CD    1 
ATOM   1878 O OE1   . GLU A 1 239 ? 11.301  2.717  -16.208 1.00 52.73  ? 234 GLU A OE1   1 
ATOM   1879 O OE2   . GLU A 1 239 ? 11.401  4.901  -16.406 1.00 50.81  ? 234 GLU A OE2   1 
ATOM   1880 N N     . GLU A 1 240 ? 6.733   0.546  -19.025 1.00 45.50  ? 235 GLU A N     1 
ATOM   1881 C CA    . GLU A 1 240 ? 6.545   -0.432 -20.090 1.00 43.25  ? 235 GLU A CA    1 
ATOM   1882 C C     . GLU A 1 240 ? 5.315   -0.155 -20.943 1.00 48.99  ? 235 GLU A C     1 
ATOM   1883 O O     . GLU A 1 240 ? 5.176   -0.758 -22.013 1.00 51.83  ? 235 GLU A O     1 
ATOM   1884 C CB    . GLU A 1 240 ? 6.464   -1.844 -19.504 1.00 43.02  ? 235 GLU A CB    1 
ATOM   1885 C CG    . GLU A 1 240 ? 7.785   -2.348 -18.944 1.00 41.98  ? 235 GLU A CG    1 
ATOM   1886 C CD    . GLU A 1 240 ? 7.724   -3.797 -18.504 1.00 49.65  ? 235 GLU A CD    1 
ATOM   1887 O OE1   . GLU A 1 240 ? 6.740   -4.484 -18.849 1.00 55.22  ? 235 GLU A OE1   1 
ATOM   1888 O OE2   . GLU A 1 240 ? 8.664   -4.249 -17.818 1.00 53.30  ? 235 GLU A OE2   1 
ATOM   1889 N N     . ARG A 1 241 ? 4.427   0.730  -20.502 1.00 49.94  ? 236 ARG A N     1 
ATOM   1890 C CA    . ARG A 1 241 ? 3.291   1.160  -21.304 1.00 46.28  ? 236 ARG A CA    1 
ATOM   1891 C C     . ARG A 1 241 ? 3.585   2.426  -22.097 1.00 45.55  ? 236 ARG A C     1 
ATOM   1892 O O     . ARG A 1 241 ? 2.742   2.852  -22.893 1.00 46.21  ? 236 ARG A O     1 
ATOM   1893 C CB    . ARG A 1 241 ? 2.066   1.376  -20.409 1.00 48.11  ? 236 ARG A CB    1 
ATOM   1894 C CG    . ARG A 1 241 ? 1.917   0.324  -19.324 1.00 48.91  ? 236 ARG A CG    1 
ATOM   1895 C CD    . ARG A 1 241 ? 0.489   0.228  -18.824 1.00 64.45  ? 236 ARG A CD    1 
ATOM   1896 N NE    . ARG A 1 241 ? 0.213   -1.040 -18.159 1.00 76.52  ? 236 ARG A NE    1 
ATOM   1897 C CZ    . ARG A 1 241 ? -0.925  -1.322 -17.540 1.00 71.77  ? 236 ARG A CZ    1 
ATOM   1898 N NH1   . ARG A 1 241 ? -1.916  -0.448 -17.485 1.00 70.85  ? 236 ARG A NH1   1 
ATOM   1899 N NH2   . ARG A 1 241 ? -1.071  -2.509 -16.957 1.00 63.54  ? 236 ARG A NH2   1 
ATOM   1900 N N     . GLY A 1 242 ? 4.757   3.030  -21.904 1.00 46.85  ? 237 GLY A N     1 
ATOM   1901 C CA    . GLY A 1 242 ? 5.174   4.201  -22.649 1.00 45.92  ? 237 GLY A CA    1 
ATOM   1902 C C     . GLY A 1 242 ? 5.305   5.463  -21.828 1.00 52.51  ? 237 GLY A C     1 
ATOM   1903 O O     . GLY A 1 242 ? 5.835   6.460  -22.337 1.00 50.82  ? 237 GLY A O     1 
ATOM   1904 N N     . PHE A 1 243 ? 4.846   5.458  -20.579 1.00 56.18  ? 238 PHE A N     1 
ATOM   1905 C CA    . PHE A 1 243 ? 4.884   6.662  -19.763 1.00 53.12  ? 238 PHE A CA    1 
ATOM   1906 C C     . PHE A 1 243 ? 6.315   6.996  -19.360 1.00 50.73  ? 238 PHE A C     1 
ATOM   1907 O O     . PHE A 1 243 ? 7.090   6.120  -18.965 1.00 51.70  ? 238 PHE A O     1 
ATOM   1908 C CB    . PHE A 1 243 ? 4.012   6.486  -18.521 1.00 53.22  ? 238 PHE A CB    1 
ATOM   1909 C CG    . PHE A 1 243 ? 2.544   6.384  -18.824 1.00 50.55  ? 238 PHE A CG    1 
ATOM   1910 C CD1   . PHE A 1 243 ? 1.785   7.524  -19.027 1.00 55.92  ? 238 PHE A CD1   1 
ATOM   1911 C CD2   . PHE A 1 243 ? 1.925   5.148  -18.912 1.00 48.95  ? 238 PHE A CD2   1 
ATOM   1912 C CE1   . PHE A 1 243 ? 0.436   7.434  -19.307 1.00 54.52  ? 238 PHE A CE1   1 
ATOM   1913 C CE2   . PHE A 1 243 ? 0.576   5.052  -19.193 1.00 53.81  ? 238 PHE A CE2   1 
ATOM   1914 C CZ    . PHE A 1 243 ? -0.169  6.197  -19.391 1.00 54.83  ? 238 PHE A CZ    1 
ATOM   1915 N N     . THR A 1 244 ? 6.662   8.275  -19.465 1.00 55.34  ? 239 THR A N     1 
ATOM   1916 C CA    . THR A 1 244 ? 7.994   8.766  -19.150 1.00 53.29  ? 239 THR A CA    1 
ATOM   1917 C C     . THR A 1 244 ? 7.974   9.537  -17.836 1.00 50.85  ? 239 THR A C     1 
ATOM   1918 O O     . THR A 1 244 ? 6.956   10.120 -17.454 1.00 49.99  ? 239 THR A O     1 
ATOM   1919 C CB    . THR A 1 244 ? 8.529   9.668  -20.267 1.00 52.84  ? 239 THR A CB    1 
ATOM   1920 O OG1   . THR A 1 244 ? 7.759   10.875 -20.318 1.00 58.65  ? 239 THR A OG1   1 
ATOM   1921 C CG2   . THR A 1 244 ? 8.440   8.961  -21.610 1.00 54.49  ? 239 THR A CG2   1 
ATOM   1922 N N     . GLU A 1 245 ? 9.114   9.535  -17.150 1.00 55.85  ? 240 GLU A N     1 
ATOM   1923 C CA    . GLU A 1 245 ? 9.240   10.247 -15.886 1.00 52.21  ? 240 GLU A CA    1 
ATOM   1924 C C     . GLU A 1 245 ? 9.566   11.712 -16.139 1.00 51.11  ? 240 GLU A C     1 
ATOM   1925 O O     . GLU A 1 245 ? 10.492  12.031 -16.892 1.00 54.16  ? 240 GLU A O     1 
ATOM   1926 C CB    . GLU A 1 245 ? 10.321  9.610  -15.013 1.00 50.73  ? 240 GLU A CB    1 
ATOM   1927 C CG    . GLU A 1 245 ? 10.531  10.323 -13.685 1.00 55.47  ? 240 GLU A CG    1 
ATOM   1928 C CD    . GLU A 1 245 ? 11.310  9.489  -12.688 1.00 56.66  ? 240 GLU A CD    1 
ATOM   1929 O OE1   . GLU A 1 245 ? 11.678  8.345  -13.027 1.00 64.26  ? 240 GLU A OE1   1 
ATOM   1930 O OE2   . GLU A 1 245 ? 11.557  9.978  -11.566 1.00 54.38  ? 240 GLU A OE2   1 
ATOM   1931 N N     . GLY A 1 246 ? 8.806   12.602 -15.505 1.00 48.26  ? 241 GLY A N     1 
ATOM   1932 C CA    . GLY A 1 246 ? 9.043   14.019 -15.652 1.00 47.70  ? 241 GLY A CA    1 
ATOM   1933 C C     . GLY A 1 246 ? 10.040  14.559 -14.645 1.00 50.30  ? 241 GLY A C     1 
ATOM   1934 O O     . GLY A 1 246 ? 10.341  13.934 -13.630 1.00 53.82  ? 241 GLY A O     1 
ATOM   1935 N N     . SER A 1 247 ? 10.560  15.744 -14.947 1.00 48.35  ? 242 SER A N     1 
ATOM   1936 C CA    . SER A 1 247 ? 11.518  16.409 -14.079 1.00 49.56  ? 242 SER A CA    1 
ATOM   1937 C C     . SER A 1 247 ? 11.323  17.913 -14.209 1.00 54.63  ? 242 SER A C     1 
ATOM   1938 O O     . SER A 1 247 ? 10.456  18.386 -14.950 1.00 53.74  ? 242 SER A O     1 
ATOM   1939 C CB    . SER A 1 247 ? 12.954  15.998 -14.424 1.00 54.87  ? 242 SER A CB    1 
ATOM   1940 O OG    . SER A 1 247 ? 13.273  16.330 -15.764 1.00 59.39  ? 242 SER A OG    1 
ATOM   1941 N N     . GLN A 1 248 ? 12.140  18.668 -13.471 1.00 58.16  ? 243 GLN A N     1 
ATOM   1942 C CA    . GLN A 1 248 ? 12.084  20.122 -13.562 1.00 58.21  ? 243 GLN A CA    1 
ATOM   1943 C C     . GLN A 1 248 ? 12.449  20.599 -14.962 1.00 65.17  ? 243 GLN A C     1 
ATOM   1944 O O     . GLN A 1 248 ? 11.827  21.527 -15.493 1.00 64.45  ? 243 GLN A O     1 
ATOM   1945 C CB    . GLN A 1 248 ? 13.018  20.749 -12.527 1.00 53.96  ? 243 GLN A CB    1 
ATOM   1946 C CG    . GLN A 1 248 ? 12.759  22.224 -12.266 1.00 54.52  ? 243 GLN A CG    1 
ATOM   1947 C CD    . GLN A 1 248 ? 12.864  22.585 -10.796 1.00 57.36  ? 243 GLN A CD    1 
ATOM   1948 O OE1   . GLN A 1 248 ? 11.926  22.388 -10.025 1.00 58.86  ? 243 GLN A OE1   1 
ATOM   1949 N NE2   . GLN A 1 248 ? 14.016  23.118 -10.402 1.00 56.38  ? 243 GLN A NE2   1 
ATOM   1950 N N     . SER A 1 249 ? 13.455  19.975 -15.577 1.00 68.60  ? 244 SER A N     1 
ATOM   1951 C CA    . SER A 1 249 ? 13.900  20.408 -16.894 1.00 63.47  ? 244 SER A CA    1 
ATOM   1952 C C     . SER A 1 249 ? 13.007  19.877 -18.006 1.00 66.85  ? 244 SER A C     1 
ATOM   1953 O O     . SER A 1 249 ? 12.921  20.494 -19.073 1.00 68.61  ? 244 SER A O     1 
ATOM   1954 C CB    . SER A 1 249 ? 15.344  19.965 -17.134 1.00 66.20  ? 244 SER A CB    1 
ATOM   1955 O OG    . SER A 1 249 ? 16.141  20.164 -15.979 1.00 67.01  ? 244 SER A OG    1 
ATOM   1956 N N     . GLU A 1 250 ? 12.337  18.748 -17.782 1.00 65.96  ? 245 GLU A N     1 
ATOM   1957 C CA    . GLU A 1 250 ? 11.563  18.082 -18.827 1.00 60.73  ? 245 GLU A CA    1 
ATOM   1958 C C     . GLU A 1 250 ? 10.296  17.498 -18.215 1.00 58.34  ? 245 GLU A C     1 
ATOM   1959 O O     . GLU A 1 250 ? 10.343  16.439 -17.568 1.00 58.83  ? 245 GLU A O     1 
ATOM   1960 C CB    . GLU A 1 250 ? 12.392  16.999 -19.513 1.00 63.70  ? 245 GLU A CB    1 
ATOM   1961 C CG    . GLU A 1 250 ? 11.978  16.705 -20.944 1.00 70.61  ? 245 GLU A CG    1 
ATOM   1962 C CD    . GLU A 1 250 ? 13.039  15.941 -21.710 1.00 80.92  ? 245 GLU A CD    1 
ATOM   1963 O OE1   . GLU A 1 250 ? 13.938  15.358 -21.068 1.00 80.11  ? 245 GLU A OE1   1 
ATOM   1964 O OE2   . GLU A 1 250 ? 12.980  15.929 -22.956 1.00 84.56  ? 245 GLU A OE2   1 
ATOM   1965 N N     . PRO A 1 251 ? 9.152   18.161 -18.386 1.00 53.24  ? 246 PRO A N     1 
ATOM   1966 C CA    . PRO A 1 251 ? 7.895   17.604 -17.873 1.00 47.97  ? 246 PRO A CA    1 
ATOM   1967 C C     . PRO A 1 251 ? 7.572   16.268 -18.526 1.00 50.40  ? 246 PRO A C     1 
ATOM   1968 O O     . PRO A 1 251 ? 7.917   16.015 -19.683 1.00 57.13  ? 246 PRO A O     1 
ATOM   1969 C CB    . PRO A 1 251 ? 6.857   18.669 -18.244 1.00 47.62  ? 246 PRO A CB    1 
ATOM   1970 C CG    . PRO A 1 251 ? 7.632   19.928 -18.379 1.00 53.44  ? 246 PRO A CG    1 
ATOM   1971 C CD    . PRO A 1 251 ? 8.988   19.535 -18.891 1.00 55.56  ? 246 PRO A CD    1 
ATOM   1972 N N     . GLY A 1 252 ? 6.897   15.409 -17.767 1.00 50.58  ? 247 GLY A N     1 
ATOM   1973 C CA    . GLY A 1 252 ? 6.523   14.098 -18.261 1.00 45.91  ? 247 GLY A CA    1 
ATOM   1974 C C     . GLY A 1 252 ? 5.143   13.663 -17.812 1.00 43.53  ? 247 GLY A C     1 
ATOM   1975 O O     . GLY A 1 252 ? 4.259   14.499 -17.606 1.00 46.81  ? 247 GLY A O     1 
ATOM   1976 N N     . GLU A 1 253 ? 4.947   12.355 -17.650 1.00 44.12  ? 248 GLU A N     1 
ATOM   1977 C CA    . GLU A 1 253 ? 3.653   11.816 -17.253 1.00 50.66  ? 248 GLU A CA    1 
ATOM   1978 C C     . GLU A 1 253 ? 3.576   11.433 -15.783 1.00 52.75  ? 248 GLU A C     1 
ATOM   1979 O O     . GLU A 1 253 ? 2.497   11.529 -15.190 1.00 52.82  ? 248 GLU A O     1 
ATOM   1980 C CB    . GLU A 1 253 ? 3.300   10.595 -18.109 1.00 51.49  ? 248 GLU A CB    1 
ATOM   1981 C CG    . GLU A 1 253 ? 2.702   10.944 -19.464 1.00 51.94  ? 248 GLU A CG    1 
ATOM   1982 C CD    . GLU A 1 253 ? 3.740   10.984 -20.569 1.00 55.80  ? 248 GLU A CD    1 
ATOM   1983 O OE1   . GLU A 1 253 ? 4.572   10.055 -20.639 1.00 55.92  ? 248 GLU A OE1   1 
ATOM   1984 O OE2   . GLU A 1 253 ? 3.722   11.942 -21.369 1.00 57.98  ? 248 GLU A OE2   1 
ATOM   1985 N N     . PHE A 1 254 ? 4.679   11.005 -15.174 1.00 50.13  ? 249 PHE A N     1 
ATOM   1986 C CA    . PHE A 1 254 ? 4.669   10.637 -13.766 1.00 48.21  ? 249 PHE A CA    1 
ATOM   1987 C C     . PHE A 1 254 ? 5.962   11.085 -13.101 1.00 48.97  ? 249 PHE A C     1 
ATOM   1988 O O     . PHE A 1 254 ? 7.039   11.000 -13.696 1.00 49.57  ? 249 PHE A O     1 
ATOM   1989 C CB    . PHE A 1 254 ? 4.466   9.120  -13.580 1.00 50.81  ? 249 PHE A CB    1 
ATOM   1990 C CG    . PHE A 1 254 ? 5.624   8.281  -14.050 1.00 49.51  ? 249 PHE A CG    1 
ATOM   1991 C CD1   . PHE A 1 254 ? 5.688   7.837  -15.361 1.00 51.39  ? 249 PHE A CD1   1 
ATOM   1992 C CD2   . PHE A 1 254 ? 6.644   7.931  -13.179 1.00 50.06  ? 249 PHE A CD2   1 
ATOM   1993 C CE1   . PHE A 1 254 ? 6.752   7.065  -15.795 1.00 51.82  ? 249 PHE A CE1   1 
ATOM   1994 C CE2   . PHE A 1 254 ? 7.708   7.162  -13.608 1.00 51.77  ? 249 PHE A CE2   1 
ATOM   1995 C CZ    . PHE A 1 254 ? 7.762   6.728  -14.916 1.00 51.01  ? 249 PHE A CZ    1 
ATOM   1996 N N     . VAL A 1 255 ? 5.841   11.577 -11.872 1.00 47.49  ? 250 VAL A N     1 
ATOM   1997 C CA    . VAL A 1 255 ? 6.985   11.871 -11.021 1.00 45.09  ? 250 VAL A CA    1 
ATOM   1998 C C     . VAL A 1 255 ? 6.934   10.943 -9.815  1.00 45.24  ? 250 VAL A C     1 
ATOM   1999 O O     . VAL A 1 255 ? 5.885   10.402 -9.456  1.00 45.31  ? 250 VAL A O     1 
ATOM   2000 C CB    . VAL A 1 255 ? 7.025   13.349 -10.581 1.00 46.03  ? 250 VAL A CB    1 
ATOM   2001 C CG1   . VAL A 1 255 ? 7.723   14.192 -11.636 1.00 44.52  ? 250 VAL A CG1   1 
ATOM   2002 C CG2   . VAL A 1 255 ? 5.616   13.860 -10.322 1.00 49.03  ? 250 VAL A CG2   1 
ATOM   2003 N N     . ILE A 1 256 ? 8.090   10.760 -9.183  1.00 49.02  ? 251 ILE A N     1 
ATOM   2004 C CA    . ILE A 1 256 ? 8.249   9.762  -8.131  1.00 46.67  ? 251 ILE A CA    1 
ATOM   2005 C C     . ILE A 1 256 ? 9.048   10.362 -6.983  1.00 51.29  ? 251 ILE A C     1 
ATOM   2006 O O     . ILE A 1 256 ? 10.040  11.065 -7.200  1.00 55.05  ? 251 ILE A O     1 
ATOM   2007 C CB    . ILE A 1 256 ? 8.933   8.488  -8.673  1.00 48.06  ? 251 ILE A CB    1 
ATOM   2008 C CG1   . ILE A 1 256 ? 7.939   7.654  -9.482  1.00 46.19  ? 251 ILE A CG1   1 
ATOM   2009 C CG2   . ILE A 1 256 ? 9.529   7.659  -7.543  1.00 47.38  ? 251 ILE A CG2   1 
ATOM   2010 C CD1   . ILE A 1 256 ? 8.572   6.501  -10.220 1.00 50.24  ? 251 ILE A CD1   1 
ATOM   2011 N N     . GLU A 1 257 ? 8.604   10.090 -5.757  1.00 50.06  ? 252 GLU A N     1 
ATOM   2012 C CA    . GLU A 1 257 ? 9.340   10.456 -4.557  1.00 48.59  ? 252 GLU A CA    1 
ATOM   2013 C C     . GLU A 1 257 ? 9.290   9.296  -3.576  1.00 51.93  ? 252 GLU A C     1 
ATOM   2014 O O     . GLU A 1 257 ? 8.263   8.624  -3.453  1.00 49.75  ? 252 GLU A O     1 
ATOM   2015 C CB    . GLU A 1 257 ? 8.769   11.715 -3.900  1.00 47.65  ? 252 GLU A CB    1 
ATOM   2016 C CG    . GLU A 1 257 ? 9.648   12.277 -2.799  1.00 44.46  ? 252 GLU A CG    1 
ATOM   2017 C CD    . GLU A 1 257 ? 9.269   13.691 -2.423  1.00 50.82  ? 252 GLU A CD    1 
ATOM   2018 O OE1   . GLU A 1 257 ? 8.421   13.854 -1.520  1.00 56.68  ? 252 GLU A OE1   1 
ATOM   2019 O OE2   . GLU A 1 257 ? 9.813   14.637 -3.028  1.00 53.75  ? 252 GLU A OE2   1 
ATOM   2020 N N     . LYS A 1 258 ? 10.397  9.063  -2.879  1.00 54.52  ? 253 LYS A N     1 
ATOM   2021 C CA    . LYS A 1 258 ? 10.432  7.996  -1.888  1.00 53.37  ? 253 LYS A CA    1 
ATOM   2022 C C     . LYS A 1 258 ? 9.713   8.432  -0.619  1.00 51.92  ? 253 LYS A C     1 
ATOM   2023 O O     . LYS A 1 258 ? 9.952   9.528  -0.102  1.00 55.18  ? 253 LYS A O     1 
ATOM   2024 C CB    . LYS A 1 258 ? 11.875  7.611  -1.565  1.00 62.56  ? 253 LYS A CB    1 
ATOM   2025 C CG    . LYS A 1 258 ? 12.684  7.117  -2.749  1.00 67.85  ? 253 LYS A CG    1 
ATOM   2026 C CD    . LYS A 1 258 ? 14.137  6.904  -2.353  1.00 69.85  ? 253 LYS A CD    1 
ATOM   2027 C CE    . LYS A 1 258 ? 14.792  5.819  -3.192  1.00 70.72  ? 253 LYS A CE    1 
ATOM   2028 N NZ    . LYS A 1 258 ? 14.486  5.967  -4.640  1.00 72.00  ? 253 LYS A NZ    1 
ATOM   2029 N N     . ALA A 1 259 ? 8.821   7.576  -0.115  1.00 48.59  ? 254 ALA A N     1 
ATOM   2030 C CA    . ALA A 1 259 ? 8.249   7.831  1.200   1.00 49.62  ? 254 ALA A CA    1 
ATOM   2031 C C     . ALA A 1 259 ? 9.267   7.595  2.304   1.00 54.77  ? 254 ALA A C     1 
ATOM   2032 O O     . ALA A 1 259 ? 9.122   8.150  3.398   1.00 57.33  ? 254 ALA A O     1 
ATOM   2033 C CB    . ALA A 1 259 ? 7.012   6.961  1.423   1.00 47.42  ? 254 ALA A CB    1 
ATOM   2034 N N     . PHE A 1 260 ? 10.291  6.794  2.030   1.00 58.37  ? 255 PHE A N     1 
ATOM   2035 C CA    . PHE A 1 260 ? 11.400  6.542  2.944   1.00 62.37  ? 255 PHE A CA    1 
ATOM   2036 C C     . PHE A 1 260 ? 12.463  5.773  2.171   1.00 68.63  ? 255 PHE A C     1 
ATOM   2037 O O     . PHE A 1 260 ? 12.262  5.391  1.014   1.00 71.07  ? 255 PHE A O     1 
ATOM   2038 C CB    . PHE A 1 260 ? 10.953  5.769  4.187   1.00 66.17  ? 255 PHE A CB    1 
ATOM   2039 C CG    . PHE A 1 260 ? 10.387  4.404  3.891   1.00 62.78  ? 255 PHE A CG    1 
ATOM   2040 C CD1   . PHE A 1 260 ? 11.208  3.286  3.845   1.00 63.02  ? 255 PHE A CD1   1 
ATOM   2041 C CD2   . PHE A 1 260 ? 9.032   4.242  3.658   1.00 60.69  ? 255 PHE A CD2   1 
ATOM   2042 C CE1   . PHE A 1 260 ? 10.684  2.034  3.573   1.00 59.78  ? 255 PHE A CE1   1 
ATOM   2043 C CE2   . PHE A 1 260 ? 8.503   2.992  3.386   1.00 57.90  ? 255 PHE A CE2   1 
ATOM   2044 C CZ    . PHE A 1 260 ? 9.330   1.887  3.344   1.00 55.70  ? 255 PHE A CZ    1 
ATOM   2045 N N     . VAL A 1 261 ? 13.600  5.544  2.822   1.00 76.42  ? 256 VAL A N     1 
ATOM   2046 C CA    . VAL A 1 261 ? 14.649  4.694  2.278   1.00 80.91  ? 256 VAL A CA    1 
ATOM   2047 C C     . VAL A 1 261 ? 14.969  3.613  3.301   1.00 84.40  ? 256 VAL A C     1 
ATOM   2048 O O     . VAL A 1 261 ? 14.806  3.804  4.511   1.00 85.28  ? 256 VAL A O     1 
ATOM   2049 C CB    . VAL A 1 261 ? 15.918  5.494  1.894   1.00 83.97  ? 256 VAL A CB    1 
ATOM   2050 C CG1   . VAL A 1 261 ? 15.542  6.776  1.167   1.00 83.30  ? 256 VAL A CG1   1 
ATOM   2051 C CG2   . VAL A 1 261 ? 16.758  5.803  3.119   1.00 87.20  ? 256 VAL A CG2   1 
ATOM   2052 N N     . GLU A 1 262 ? 15.397  2.456  2.802   1.00 82.17  ? 257 GLU A N     1 
ATOM   2053 C CA    . GLU A 1 262 ? 15.737  1.327  3.661   1.00 91.28  ? 257 GLU A CA    1 
ATOM   2054 C C     . GLU A 1 262 ? 17.183  1.476  4.118   1.00 95.31  ? 257 GLU A C     1 
ATOM   2055 O O     . GLU A 1 262 ? 18.113  1.326  3.319   1.00 92.90  ? 257 GLU A O     1 
ATOM   2056 C CB    . GLU A 1 262 ? 15.523  0.008  2.925   1.00 93.56  ? 257 GLU A CB    1 
ATOM   2057 C CG    . GLU A 1 262 ? 14.263  -0.739 3.334   1.00 91.03  ? 257 GLU A CG    1 
ATOM   2058 C CD    . GLU A 1 262 ? 14.075  -0.792 4.838   1.00 90.45  ? 257 GLU A CD    1 
ATOM   2059 O OE1   . GLU A 1 262 ? 15.007  -1.231 5.546   1.00 90.44  ? 257 GLU A OE1   1 
ATOM   2060 O OE2   . GLU A 1 262 ? 12.991  -0.396 5.313   1.00 85.46  ? 257 GLU A OE2   1 
ATOM   2061 N N     . LYS A 1 263 ? 17.372  1.776  5.398   1.00 95.70  ? 258 LYS A N     1 
ATOM   2062 C CA    . LYS A 1 263 ? 18.705  1.957  5.958   1.00 96.59  ? 258 LYS A CA    1 
ATOM   2063 C C     . LYS A 1 263 ? 19.152  0.718  6.726   1.00 99.77  ? 258 LYS A C     1 
ATOM   2064 O O     . LYS A 1 263 ? 18.403  -0.250 6.864   1.00 91.45  ? 258 LYS A O     1 
ATOM   2065 C CB    . LYS A 1 263 ? 18.738  3.184  6.871   1.00 93.38  ? 258 LYS A CB    1 
ATOM   2066 C CG    . LYS A 1 263 ? 17.995  4.386  6.312   1.00 92.65  ? 258 LYS A CG    1 
ATOM   2067 C CD    . LYS A 1 263 ? 17.863  5.490  7.348   1.00 88.92  ? 258 LYS A CD    1 
ATOM   2068 C CE    . LYS A 1 263 ? 17.219  6.731  6.750   1.00 80.77  ? 258 LYS A CE    1 
ATOM   2069 N NZ    . LYS A 1 263 ? 17.989  7.966  7.069   1.00 82.69  ? 258 LYS A NZ    1 
HETATM 2070 P PA    . FAD B 2 .   ? 15.581  6.022  10.623  1.00 92.55  ? 301 FAD A PA    1 
HETATM 2071 O O1A   . FAD B 2 .   ? 16.799  5.672  11.389  1.00 74.65  ? 301 FAD A O1A   1 
HETATM 2072 O O2A   . FAD B 2 .   ? 15.771  7.142  9.595   1.00 74.48  ? 301 FAD A O2A   1 
HETATM 2073 O O5B   . FAD B 2 .   ? 14.968  4.735  9.953   1.00 68.20  ? 301 FAD A O5B   1 
HETATM 2074 C C5B   . FAD B 2 .   ? 14.210  3.784  10.729  1.00 69.82  ? 301 FAD A C5B   1 
HETATM 2075 C C4B   . FAD B 2 .   ? 13.790  2.600  9.891   1.00 69.16  ? 301 FAD A C4B   1 
HETATM 2076 O O4B   . FAD B 2 .   ? 12.411  2.751  9.487   1.00 67.84  ? 301 FAD A O4B   1 
HETATM 2077 C C3B   . FAD B 2 .   ? 14.580  2.370  8.607   1.00 72.12  ? 301 FAD A C3B   1 
HETATM 2078 O O3B   . FAD B 2 .   ? 14.704  0.981  8.325   1.00 78.08  ? 301 FAD A O3B   1 
HETATM 2079 C C2B   . FAD B 2 .   ? 13.740  3.098  7.554   1.00 68.44  ? 301 FAD A C2B   1 
HETATM 2080 O O2B   . FAD B 2 .   ? 13.878  2.498  6.271   1.00 72.68  ? 301 FAD A O2B   1 
HETATM 2081 C C1B   . FAD B 2 .   ? 12.317  2.902  8.082   1.00 66.71  ? 301 FAD A C1B   1 
HETATM 2082 N N9A   . FAD B 2 .   ? 11.429  4.028  7.806   1.00 61.75  ? 301 FAD A N9A   1 
HETATM 2083 C C8A   . FAD B 2 .   ? 11.757  5.356  7.839   1.00 60.26  ? 301 FAD A C8A   1 
HETATM 2084 N N7A   . FAD B 2 .   ? 10.762  6.161  7.548   1.00 58.78  ? 301 FAD A N7A   1 
HETATM 2085 C C5A   . FAD B 2 .   ? 9.706   5.300  7.307   1.00 56.93  ? 301 FAD A C5A   1 
HETATM 2086 C C6A   . FAD B 2 .   ? 8.361   5.523  6.946   1.00 55.84  ? 301 FAD A C6A   1 
HETATM 2087 N N6A   . FAD B 2 .   ? 7.834   6.737  6.761   1.00 52.47  ? 301 FAD A N6A   1 
HETATM 2088 N N1A   . FAD B 2 .   ? 7.567   4.442  6.782   1.00 60.64  ? 301 FAD A N1A   1 
HETATM 2089 C C2A   . FAD B 2 .   ? 8.089   3.226  6.966   1.00 56.42  ? 301 FAD A C2A   1 
HETATM 2090 N N3A   . FAD B 2 .   ? 9.337   2.893  7.305   1.00 55.71  ? 301 FAD A N3A   1 
HETATM 2091 C C4A   . FAD B 2 .   ? 10.098  3.980  7.461   1.00 57.87  ? 301 FAD A C4A   1 
HETATM 2092 N N1    . FAD B 2 .   ? 8.871   9.750  6.872   1.00 55.94  ? 301 FAD A N1    1 
HETATM 2093 C C2    . FAD B 2 .   ? 7.660   10.020 7.440   1.00 53.24  ? 301 FAD A C2    1 
HETATM 2094 O O2    . FAD B 2 .   ? 7.312   9.496  8.504   1.00 54.81  ? 301 FAD A O2    1 
HETATM 2095 N N3    . FAD B 2 .   ? 6.792   10.899 6.816   1.00 51.93  ? 301 FAD A N3    1 
HETATM 2096 C C4    . FAD B 2 .   ? 7.023   11.566 5.630   1.00 51.39  ? 301 FAD A C4    1 
HETATM 2097 O O4    . FAD B 2 .   ? 6.172   12.327 5.171   1.00 52.17  ? 301 FAD A O4    1 
HETATM 2098 C C4X   . FAD B 2 .   ? 8.314   11.273 5.036   1.00 54.85  ? 301 FAD A C4X   1 
HETATM 2099 N N5    . FAD B 2 .   ? 8.620   11.860 3.912   1.00 58.62  ? 301 FAD A N5    1 
HETATM 2100 C C5X   . FAD B 2 .   ? 9.853   11.578 3.345   1.00 50.34  ? 301 FAD A C5X   1 
HETATM 2101 C C6    . FAD B 2 .   ? 10.198  12.195 2.144   1.00 49.75  ? 301 FAD A C6    1 
HETATM 2102 C C7    . FAD B 2 .   ? 11.425  11.944 1.537   1.00 51.33  ? 301 FAD A C7    1 
HETATM 2103 C C7M   . FAD B 2 .   ? 11.763  12.629 0.239   1.00 51.36  ? 301 FAD A C7M   1 
HETATM 2104 C C8    . FAD B 2 .   ? 12.330  11.057 2.143   1.00 50.06  ? 301 FAD A C8    1 
HETATM 2105 C C8M   . FAD B 2 .   ? 13.666  10.764 1.513   1.00 47.24  ? 301 FAD A C8M   1 
HETATM 2106 C C9    . FAD B 2 .   ? 11.989  10.440 3.342   1.00 54.88  ? 301 FAD A C9    1 
HETATM 2107 C C9A   . FAD B 2 .   ? 10.762  10.694 3.944   1.00 53.46  ? 301 FAD A C9A   1 
HETATM 2108 N N10   . FAD B 2 .   ? 10.390  10.085 5.159   1.00 55.32  ? 301 FAD A N10   1 
HETATM 2109 C C10   . FAD B 2 .   ? 9.171   10.351 5.733   1.00 55.95  ? 301 FAD A C10   1 
HETATM 2110 C "C1'" . FAD B 2 .   ? 11.295  9.148  5.836   1.00 56.07  ? 301 FAD A "C1'" 1 
HETATM 2111 C "C2'" . FAD B 2 .   ? 12.160  9.816  6.899   1.00 55.19  ? 301 FAD A "C2'" 1 
HETATM 2112 O "O2'" . FAD B 2 .   ? 13.544  9.592  6.626   1.00 53.83  ? 301 FAD A "O2'" 1 
HETATM 2113 C "C3'" . FAD B 2 .   ? 11.811  9.232  8.267   1.00 55.21  ? 301 FAD A "C3'" 1 
HETATM 2114 O "O3'" . FAD B 2 .   ? 11.290  10.264 9.095   1.00 59.03  ? 301 FAD A "O3'" 1 
HETATM 2115 C "C4'" . FAD B 2 .   ? 12.988  8.576  8.988   1.00 59.58  ? 301 FAD A "C4'" 1 
HETATM 2116 O "O4'" . FAD B 2 .   ? 13.670  7.700  8.090   1.00 66.90  ? 301 FAD A "O4'" 1 
HETATM 2117 C "C5'" . FAD B 2 .   ? 12.556  7.834  10.234  1.00 62.63  ? 301 FAD A "C5'" 1 
HETATM 2118 O "O5'" . FAD B 2 .   ? 13.078  8.520  11.391  1.00 62.04  ? 301 FAD A "O5'" 1 
HETATM 2119 P P     . FAD B 2 .   ? 14.250  7.906  12.244  1.00 79.13  ? 301 FAD A P     1 
HETATM 2120 O O1P   . FAD B 2 .   ? 13.750  7.733  13.681  1.00 60.93  ? 301 FAD A O1P   1 
HETATM 2121 O O2P   . FAD B 2 .   ? 15.501  8.684  12.083  1.00 63.95  ? 301 FAD A O2P   1 
HETATM 2122 O O3P   . FAD B 2 .   ? 14.422  6.462  11.612  1.00 67.42  ? 301 FAD A O3P   1 
HETATM 2123 O O     . HOH C 3 .   ? -3.126  20.410 8.550   1.00 44.84  ? 401 HOH A O     1 
HETATM 2124 O O     . HOH C 3 .   ? 7.592   15.361 -0.199  1.00 50.74  ? 402 HOH A O     1 
HETATM 2125 O O     . HOH C 3 .   ? -3.597  19.750 -16.019 1.00 49.61  ? 403 HOH A O     1 
HETATM 2126 O O     . HOH C 3 .   ? 3.385   12.188 21.766  1.00 55.28  ? 404 HOH A O     1 
HETATM 2127 O O     . HOH C 3 .   ? 1.123   -3.415 9.741   1.00 52.35  ? 405 HOH A O     1 
HETATM 2128 O O     . HOH C 3 .   ? -6.240  6.887  4.319   1.00 49.14  ? 406 HOH A O     1 
HETATM 2129 O O     . HOH C 3 .   ? -2.070  2.160  -19.788 1.00 59.27  ? 407 HOH A O     1 
HETATM 2130 O O     . HOH C 3 .   ? 1.066   24.230 6.068   1.00 45.47  ? 408 HOH A O     1 
HETATM 2131 O O     . HOH C 3 .   ? 7.602   1.499  12.986  1.00 55.52  ? 409 HOH A O     1 
HETATM 2132 O O     . HOH C 3 .   ? 4.446   18.946 0.264   1.00 43.48  ? 410 HOH A O     1 
HETATM 2133 O O     . HOH C 3 .   ? 4.957   14.425 6.719   1.00 42.39  ? 411 HOH A O     1 
HETATM 2134 O O     . HOH C 3 .   ? 1.601   30.929 9.038   1.00 53.09  ? 412 HOH A O     1 
HETATM 2135 O O     . HOH C 3 .   ? 23.516  29.006 13.808  1.00 57.27  ? 413 HOH A O     1 
HETATM 2136 O O     . HOH C 3 .   ? -1.400  22.815 -0.642  1.00 46.08  ? 414 HOH A O     1 
HETATM 2137 O O     . HOH C 3 .   ? -1.284  24.482 14.324  1.00 55.20  ? 415 HOH A O     1 
HETATM 2138 O O     . HOH C 3 .   ? -4.301  22.201 6.075   1.00 50.67  ? 416 HOH A O     1 
HETATM 2139 O O     . HOH C 3 .   ? 9.046   4.156  -21.261 1.00 47.81  ? 417 HOH A O     1 
HETATM 2140 O O     . HOH C 3 .   ? -7.824  19.968 -16.888 1.00 50.50  ? 418 HOH A O     1 
HETATM 2141 O O     . HOH C 3 .   ? -0.670  27.568 13.949  1.00 48.06  ? 419 HOH A O     1 
HETATM 2142 O O     . HOH C 3 .   ? 6.359   11.046 2.242   1.00 50.14  ? 420 HOH A O     1 
HETATM 2143 O O     . HOH C 3 .   ? 30.680  16.681 19.317  1.00 47.61  ? 421 HOH A O     1 
HETATM 2144 O O     . HOH C 3 .   ? -10.858 20.389 5.470   1.00 57.14  ? 422 HOH A O     1 
HETATM 2145 O O     . HOH C 3 .   ? -5.934  -8.072 -7.995  1.00 61.14  ? 423 HOH A O     1 
# 
