data_9GCA
# 
_entry.id   9GCA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9GCA         pdb_00009gca 10.2210/pdb9gca/pdb 
WWPDB D_1292140757 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9GCA 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-01 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              franck.borel@ibs.fr 
_pdbx_contact_author.name_first         Franck 
_pdbx_contact_author.name_last          Borel 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8905-5336 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Borel, F.'   1 0000-0002-8905-5336 
;D'Auria, L.
;
2 ?                   
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? GE ? ? primary Angew.Chem.Int.Ed.Engl.                          ACIEAY 0179 1521-3773 ? ? 64 ? e202414615 e202414615 
'Fragment Discovery by X-Ray Crystallographic Screening Targeting the CTP Binding Site of Pseudomonas Aeruginosa IspD.' 2025 ? 
10.1002/anie.202414615    39676054 ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861        877        
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix'            2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Willocx, D.'       1  ?                   
primary 
;D'Auria, L.
;
2  ?                   
primary 'Walsh, D.'         3  ?                   
primary 'Scherer, H.'       4  ?                   
primary 'Alhayek, A.'       5  ?                   
primary 'Hamed, M.M.'       6  ?                   
primary 'Borel, F.'         7  ?                   
primary 'Diamanti, E.'      8  ?                   
primary 'Hirsch, A.K.H.'    9  0000-0001-8734-4663 
1       'Liebschner, D.'    10 0000-0003-3921-3209 
1       'Afonine, P.V.'     11 0000-0002-5052-991X 
1       'Baker, M.L.'       12 ?                   
1       'Bunkoczi, G.'      13 ?                   
1       'Chen, V.B.'        14 0000-0003-2492-979X 
1       'Croll, T.I.'       15 ?                   
1       'Hintze, B.'        16 0000-0002-4871-2096 
1       'Hung, L.W.'        17 0000-0001-6690-8458 
1       'Jain, S.'          18 ?                   
1       'McCoy, A.J.'       19 ?                   
1       'Moriarty, N.W.'    20 0000-0001-8857-9464 
1       'Oeffner, R.D.'     21 0000-0003-3107-2202 
1       'Poon, B.K.'        22 0000-0001-9633-6067 
1       'Prisant, M.G.'     23 ?                   
1       'Read, R.J.'        24 0000-0001-8273-0047 
1       'Richardson, J.S.'  25 0000-0002-3311-2944 
1       'Richardson, D.C.'  26 ?                   
1       'Sammito, M.D.'     27 0000-0002-8346-9247 
1       'Sobolev, O.V.'     28 0000-0002-0623-3214 
1       'Stockwell, D.H.'   29 ?                   
1       'Terwilliger, T.C.' 30 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  31 ?                   
1       'Videau, L.L.'      32 ?                   
1       'Williams, C.J.'    33 ?                   
1       'Adams, P.D.'       34 0000-0001-9333-8219 
# 
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 '2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase' 28058.889 1  2.7.7.60 ? ? ? 
2 non-polymer syn '6-methyl-5~{H}-pyrrolo[3,4-b]pyridin-7-one'               148.162   1  ?        ? ? ? 
3 water       nat water                                                      18.015    50 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '4-diphosphocytidyl-2C-methyl-D-erythritol synthase,MEP cytidylyltransferase,MCT' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSSGLVPRGSHMTTSDLPAFWTVIPAAGVGSRMRADRPKQYLDLAGRTVIERTLDCFLEHPMLRGLVVCLA
EDDPYWPGLDCAASRHVQRAAGGAERAGSVLNGLLRLLELGAQADDWVLVHDAARPNLTRGDLDRLLEELAEDPVGGLLA
VPARDTLKRSDRDGRVSETIDRSVVWLAYTPQMFRLGALHRALADALVAGVAITDEASAMEWAGYAPKLVEGRADNLKIT
TPEDLLRLQRSFPHLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMTTSDLPAFWTVIPAAGVGSRMRADRPKQYLDLAGRTVIERTLDCFLEHPMLRGLVVCLA
EDDPYWPGLDCAASRHVQRAAGGAERAGSVLNGLLRLLELGAQADDWVLVHDAARPNLTRGDLDRLLEELAEDPVGGLLA
VPARDTLKRSDRDGRVSETIDRSVVWLAYTPQMFRLGALHRALADALVAGVAITDEASAMEWAGYAPKLVEGRADNLKIT
TPEDLLRLQRSFPHLE
;
_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 '6-methyl-5~{H}-pyrrolo[3,4-b]pyridin-7-one' A1IJT 
3 water                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  THR n 
1 23  THR n 
1 24  SER n 
1 25  ASP n 
1 26  LEU n 
1 27  PRO n 
1 28  ALA n 
1 29  PHE n 
1 30  TRP n 
1 31  THR n 
1 32  VAL n 
1 33  ILE n 
1 34  PRO n 
1 35  ALA n 
1 36  ALA n 
1 37  GLY n 
1 38  VAL n 
1 39  GLY n 
1 40  SER n 
1 41  ARG n 
1 42  MET n 
1 43  ARG n 
1 44  ALA n 
1 45  ASP n 
1 46  ARG n 
1 47  PRO n 
1 48  LYS n 
1 49  GLN n 
1 50  TYR n 
1 51  LEU n 
1 52  ASP n 
1 53  LEU n 
1 54  ALA n 
1 55  GLY n 
1 56  ARG n 
1 57  THR n 
1 58  VAL n 
1 59  ILE n 
1 60  GLU n 
1 61  ARG n 
1 62  THR n 
1 63  LEU n 
1 64  ASP n 
1 65  CYS n 
1 66  PHE n 
1 67  LEU n 
1 68  GLU n 
1 69  HIS n 
1 70  PRO n 
1 71  MET n 
1 72  LEU n 
1 73  ARG n 
1 74  GLY n 
1 75  LEU n 
1 76  VAL n 
1 77  VAL n 
1 78  CYS n 
1 79  LEU n 
1 80  ALA n 
1 81  GLU n 
1 82  ASP n 
1 83  ASP n 
1 84  PRO n 
1 85  TYR n 
1 86  TRP n 
1 87  PRO n 
1 88  GLY n 
1 89  LEU n 
1 90  ASP n 
1 91  CYS n 
1 92  ALA n 
1 93  ALA n 
1 94  SER n 
1 95  ARG n 
1 96  HIS n 
1 97  VAL n 
1 98  GLN n 
1 99  ARG n 
1 100 ALA n 
1 101 ALA n 
1 102 GLY n 
1 103 GLY n 
1 104 ALA n 
1 105 GLU n 
1 106 ARG n 
1 107 ALA n 
1 108 GLY n 
1 109 SER n 
1 110 VAL n 
1 111 LEU n 
1 112 ASN n 
1 113 GLY n 
1 114 LEU n 
1 115 LEU n 
1 116 ARG n 
1 117 LEU n 
1 118 LEU n 
1 119 GLU n 
1 120 LEU n 
1 121 GLY n 
1 122 ALA n 
1 123 GLN n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 TRP n 
1 128 VAL n 
1 129 LEU n 
1 130 VAL n 
1 131 HIS n 
1 132 ASP n 
1 133 ALA n 
1 134 ALA n 
1 135 ARG n 
1 136 PRO n 
1 137 ASN n 
1 138 LEU n 
1 139 THR n 
1 140 ARG n 
1 141 GLY n 
1 142 ASP n 
1 143 LEU n 
1 144 ASP n 
1 145 ARG n 
1 146 LEU n 
1 147 LEU n 
1 148 GLU n 
1 149 GLU n 
1 150 LEU n 
1 151 ALA n 
1 152 GLU n 
1 153 ASP n 
1 154 PRO n 
1 155 VAL n 
1 156 GLY n 
1 157 GLY n 
1 158 LEU n 
1 159 LEU n 
1 160 ALA n 
1 161 VAL n 
1 162 PRO n 
1 163 ALA n 
1 164 ARG n 
1 165 ASP n 
1 166 THR n 
1 167 LEU n 
1 168 LYS n 
1 169 ARG n 
1 170 SER n 
1 171 ASP n 
1 172 ARG n 
1 173 ASP n 
1 174 GLY n 
1 175 ARG n 
1 176 VAL n 
1 177 SER n 
1 178 GLU n 
1 179 THR n 
1 180 ILE n 
1 181 ASP n 
1 182 ARG n 
1 183 SER n 
1 184 VAL n 
1 185 VAL n 
1 186 TRP n 
1 187 LEU n 
1 188 ALA n 
1 189 TYR n 
1 190 THR n 
1 191 PRO n 
1 192 GLN n 
1 193 MET n 
1 194 PHE n 
1 195 ARG n 
1 196 LEU n 
1 197 GLY n 
1 198 ALA n 
1 199 LEU n 
1 200 HIS n 
1 201 ARG n 
1 202 ALA n 
1 203 LEU n 
1 204 ALA n 
1 205 ASP n 
1 206 ALA n 
1 207 LEU n 
1 208 VAL n 
1 209 ALA n 
1 210 GLY n 
1 211 VAL n 
1 212 ALA n 
1 213 ILE n 
1 214 THR n 
1 215 ASP n 
1 216 GLU n 
1 217 ALA n 
1 218 SER n 
1 219 ALA n 
1 220 MET n 
1 221 GLU n 
1 222 TRP n 
1 223 ALA n 
1 224 GLY n 
1 225 TYR n 
1 226 ALA n 
1 227 PRO n 
1 228 LYS n 
1 229 LEU n 
1 230 VAL n 
1 231 GLU n 
1 232 GLY n 
1 233 ARG n 
1 234 ALA n 
1 235 ASP n 
1 236 ASN n 
1 237 LEU n 
1 238 LYS n 
1 239 ILE n 
1 240 THR n 
1 241 THR n 
1 242 PRO n 
1 243 GLU n 
1 244 ASP n 
1 245 LEU n 
1 246 LEU n 
1 247 ARG n 
1 248 LEU n 
1 249 GLN n 
1 250 ARG n 
1 251 SER n 
1 252 PHE n 
1 253 PRO n 
1 254 HIS n 
1 255 LEU n 
1 256 GLU 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                   256 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ispD, PA3633' 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1IJT non-polymer         . '6-methyl-5~{H}-pyrrolo[3,4-b]pyridin-7-one' ? 'C8 H8 N2 O'     148.162 
ALA   'L-peptide linking' y ALANINE                                      ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                     ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                   ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                              ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                     ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                    ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                              ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                      ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                    ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                        ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                   ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                      ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                       ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                   ? 'C5 H11 N O2 S'  149.211 
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   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  THR 22  2   ?   ?   ?   A . n 
A 1 23  THR 23  3   ?   ?   ?   A . n 
A 1 24  SER 24  4   ?   ?   ?   A . n 
A 1 25  ASP 25  5   5   ASP ASP A . n 
A 1 26  LEU 26  6   6   LEU LEU A . n 
A 1 27  PRO 27  7   7   PRO PRO A . n 
A 1 28  ALA 28  8   8   ALA ALA A . n 
A 1 29  PHE 29  9   9   PHE PHE A . n 
A 1 30  TRP 30  10  10  TRP TRP A . n 
A 1 31  THR 31  11  11  THR THR A . n 
A 1 32  VAL 32  12  12  VAL VAL A . n 
A 1 33  ILE 33  13  13  ILE ILE A . n 
A 1 34  PRO 34  14  14  PRO PRO A . n 
A 1 35  ALA 35  15  15  ALA ALA A . n 
A 1 36  ALA 36  16  16  ALA ALA A . n 
A 1 37  GLY 37  17  17  GLY GLY A . n 
A 1 38  VAL 38  18  18  VAL VAL A . n 
A 1 39  GLY 39  19  19  GLY GLY A . n 
A 1 40  SER 40  20  20  SER SER A . n 
A 1 41  ARG 41  21  21  ARG ARG A . n 
A 1 42  MET 42  22  22  MET MET A . n 
A 1 43  ARG 43  23  23  ARG ARG A . n 
A 1 44  ALA 44  24  24  ALA ALA A . n 
A 1 45  ASP 45  25  25  ASP ASP A . n 
A 1 46  ARG 46  26  26  ARG ARG A . n 
A 1 47  PRO 47  27  27  PRO PRO A . n 
A 1 48  LYS 48  28  28  LYS LYS A . n 
A 1 49  GLN 49  29  29  GLN GLN A . n 
A 1 50  TYR 50  30  30  TYR TYR A . n 
A 1 51  LEU 51  31  31  LEU LEU A . n 
A 1 52  ASP 52  32  32  ASP ASP A . n 
A 1 53  LEU 53  33  33  LEU LEU A . n 
A 1 54  ALA 54  34  34  ALA ALA A . n 
A 1 55  GLY 55  35  35  GLY GLY A . n 
A 1 56  ARG 56  36  36  ARG ARG A . n 
A 1 57  THR 57  37  37  THR THR A . n 
A 1 58  VAL 58  38  38  VAL VAL A . n 
A 1 59  ILE 59  39  39  ILE ILE A . n 
A 1 60  GLU 60  40  40  GLU GLU A . n 
A 1 61  ARG 61  41  41  ARG ARG A . n 
A 1 62  THR 62  42  42  THR THR A . n 
A 1 63  LEU 63  43  43  LEU LEU A . n 
A 1 64  ASP 64  44  44  ASP ASP A . n 
A 1 65  CYS 65  45  45  CYS CYS A . n 
A 1 66  PHE 66  46  46  PHE PHE A . n 
A 1 67  LEU 67  47  47  LEU LEU A . n 
A 1 68  GLU 68  48  48  GLU GLU A . n 
A 1 69  HIS 69  49  49  HIS HIS A . n 
A 1 70  PRO 70  50  50  PRO PRO A . n 
A 1 71  MET 71  51  51  MET MET A . n 
A 1 72  LEU 72  52  52  LEU LEU A . n 
A 1 73  ARG 73  53  53  ARG ARG A . n 
A 1 74  GLY 74  54  54  GLY GLY A . n 
A 1 75  LEU 75  55  55  LEU LEU A . n 
A 1 76  VAL 76  56  56  VAL VAL A . n 
A 1 77  VAL 77  57  57  VAL VAL A . n 
A 1 78  CYS 78  58  58  CYS CYS A . n 
A 1 79  LEU 79  59  59  LEU LEU A . n 
A 1 80  ALA 80  60  60  ALA ALA A . n 
A 1 81  GLU 81  61  61  GLU GLU A . n 
A 1 82  ASP 82  62  62  ASP ASP A . n 
A 1 83  ASP 83  63  63  ASP ASP A . n 
A 1 84  PRO 84  64  64  PRO PRO A . n 
A 1 85  TYR 85  65  65  TYR TYR A . n 
A 1 86  TRP 86  66  66  TRP TRP A . n 
A 1 87  PRO 87  67  67  PRO PRO A . n 
A 1 88  GLY 88  68  68  GLY GLY A . n 
A 1 89  LEU 89  69  69  LEU LEU A . n 
A 1 90  ASP 90  70  70  ASP ASP A . n 
A 1 91  CYS 91  71  71  CYS CYS A . n 
A 1 92  ALA 92  72  72  ALA ALA A . n 
A 1 93  ALA 93  73  73  ALA ALA A . n 
A 1 94  SER 94  74  74  SER SER A . n 
A 1 95  ARG 95  75  75  ARG ARG A . n 
A 1 96  HIS 96  76  76  HIS HIS A . n 
A 1 97  VAL 97  77  77  VAL VAL A . n 
A 1 98  GLN 98  78  78  GLN GLN A . n 
A 1 99  ARG 99  79  79  ARG ARG A . n 
A 1 100 ALA 100 80  80  ALA ALA A . n 
A 1 101 ALA 101 81  81  ALA ALA A . n 
A 1 102 GLY 102 82  82  GLY GLY A . n 
A 1 103 GLY 103 83  83  GLY GLY A . n 
A 1 104 ALA 104 84  84  ALA ALA A . n 
A 1 105 GLU 105 85  85  GLU GLU A . n 
A 1 106 ARG 106 86  86  ARG ARG A . n 
A 1 107 ALA 107 87  87  ALA ALA A . n 
A 1 108 GLY 108 88  88  GLY GLY A . n 
A 1 109 SER 109 89  89  SER SER A . n 
A 1 110 VAL 110 90  90  VAL VAL A . n 
A 1 111 LEU 111 91  91  LEU LEU A . n 
A 1 112 ASN 112 92  92  ASN ASN A . n 
A 1 113 GLY 113 93  93  GLY GLY A . n 
A 1 114 LEU 114 94  94  LEU LEU A . n 
A 1 115 LEU 115 95  95  LEU LEU A . n 
A 1 116 ARG 116 96  96  ARG ARG A . n 
A 1 117 LEU 117 97  97  LEU LEU A . n 
A 1 118 LEU 118 98  98  LEU LEU A . n 
A 1 119 GLU 119 99  99  GLU GLU A . n 
A 1 120 LEU 120 100 100 LEU LEU A . n 
A 1 121 GLY 121 101 101 GLY GLY A . n 
A 1 122 ALA 122 102 102 ALA ALA A . n 
A 1 123 GLN 123 103 103 GLN GLN A . n 
A 1 124 ALA 124 104 104 ALA ALA A . n 
A 1 125 ASP 125 105 105 ASP ASP A . n 
A 1 126 ASP 126 106 106 ASP ASP A . n 
A 1 127 TRP 127 107 107 TRP TRP A . n 
A 1 128 VAL 128 108 108 VAL VAL A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 VAL 130 110 110 VAL VAL A . n 
A 1 131 HIS 131 111 111 HIS HIS A . n 
A 1 132 ASP 132 112 112 ASP ASP A . n 
A 1 133 ALA 133 113 113 ALA ALA A . n 
A 1 134 ALA 134 114 114 ALA ALA A . n 
A 1 135 ARG 135 115 115 ARG ARG A . n 
A 1 136 PRO 136 116 116 PRO PRO A . n 
A 1 137 ASN 137 117 117 ASN ASN A . n 
A 1 138 LEU 138 118 118 LEU LEU A . n 
A 1 139 THR 139 119 119 THR THR A . n 
A 1 140 ARG 140 120 120 ARG ARG A . n 
A 1 141 GLY 141 121 121 GLY GLY A . n 
A 1 142 ASP 142 122 122 ASP ASP A . n 
A 1 143 LEU 143 123 123 LEU LEU A . n 
A 1 144 ASP 144 124 124 ASP ASP A . n 
A 1 145 ARG 145 125 125 ARG ARG A . n 
A 1 146 LEU 146 126 126 LEU LEU A . n 
A 1 147 LEU 147 127 127 LEU LEU A . n 
A 1 148 GLU 148 128 128 GLU GLU A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 LEU 150 130 130 LEU LEU A . n 
A 1 151 ALA 151 131 131 ALA ALA A . n 
A 1 152 GLU 152 132 132 GLU GLU A . n 
A 1 153 ASP 153 133 133 ASP ASP A . n 
A 1 154 PRO 154 134 134 PRO PRO A . n 
A 1 155 VAL 155 135 135 VAL VAL A . n 
A 1 156 GLY 156 136 136 GLY GLY A . n 
A 1 157 GLY 157 137 137 GLY GLY A . n 
A 1 158 LEU 158 138 138 LEU LEU A . n 
A 1 159 LEU 159 139 139 LEU LEU A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 VAL 161 141 141 VAL VAL A . n 
A 1 162 PRO 162 142 142 PRO PRO A . n 
A 1 163 ALA 163 143 143 ALA ALA A . n 
A 1 164 ARG 164 144 144 ARG ARG A . n 
A 1 165 ASP 165 145 145 ASP ASP A . n 
A 1 166 THR 166 146 146 THR THR A . n 
A 1 167 LEU 167 147 147 LEU LEU A . n 
A 1 168 LYS 168 148 148 LYS LYS A . n 
A 1 169 ARG 169 149 149 ARG ARG A . n 
A 1 170 SER 170 150 150 SER SER A . n 
A 1 171 ASP 171 151 151 ASP ASP A . n 
A 1 172 ARG 172 152 152 ARG ARG A . n 
A 1 173 ASP 173 153 153 ASP ASP A . n 
A 1 174 GLY 174 154 154 GLY GLY A . n 
A 1 175 ARG 175 155 155 ARG ARG A . n 
A 1 176 VAL 176 156 156 VAL VAL A . n 
A 1 177 SER 177 157 157 SER SER A . n 
A 1 178 GLU 178 158 158 GLU GLU A . n 
A 1 179 THR 179 159 159 THR THR A . n 
A 1 180 ILE 180 160 160 ILE ILE A . n 
A 1 181 ASP 181 161 161 ASP ASP A . n 
A 1 182 ARG 182 162 162 ARG ARG A . n 
A 1 183 SER 183 163 163 SER SER A . n 
A 1 184 VAL 184 164 164 VAL VAL A . n 
A 1 185 VAL 185 165 165 VAL VAL A . n 
A 1 186 TRP 186 166 166 TRP TRP A . n 
A 1 187 LEU 187 167 167 LEU LEU A . n 
A 1 188 ALA 188 168 168 ALA ALA A . n 
A 1 189 TYR 189 169 169 TYR TYR A . n 
A 1 190 THR 190 170 170 THR THR A . n 
A 1 191 PRO 191 171 171 PRO PRO A . n 
A 1 192 GLN 192 172 172 GLN GLN A . n 
A 1 193 MET 193 173 173 MET MET A . n 
A 1 194 PHE 194 174 174 PHE PHE A . n 
A 1 195 ARG 195 175 175 ARG ARG A . n 
A 1 196 LEU 196 176 176 LEU LEU A . n 
A 1 197 GLY 197 177 177 GLY GLY A . n 
A 1 198 ALA 198 178 178 ALA ALA A . n 
A 1 199 LEU 199 179 179 LEU LEU A . n 
A 1 200 HIS 200 180 180 HIS HIS A . n 
A 1 201 ARG 201 181 181 ARG ARG A . n 
A 1 202 ALA 202 182 182 ALA ALA A . n 
A 1 203 LEU 203 183 183 LEU LEU A . n 
A 1 204 ALA 204 184 184 ALA ALA A . n 
A 1 205 ASP 205 185 185 ASP ASP A . n 
A 1 206 ALA 206 186 186 ALA ALA A . n 
A 1 207 LEU 207 187 187 LEU LEU A . n 
A 1 208 VAL 208 188 188 VAL VAL A . n 
A 1 209 ALA 209 189 189 ALA ALA A . n 
A 1 210 GLY 210 190 190 GLY GLY A . n 
A 1 211 VAL 211 191 191 VAL VAL A . n 
A 1 212 ALA 212 192 192 ALA ALA A . n 
A 1 213 ILE 213 193 193 ILE ILE A . n 
A 1 214 THR 214 194 194 THR THR A . n 
A 1 215 ASP 215 195 195 ASP ASP A . n 
A 1 216 GLU 216 196 196 GLU GLU A . n 
A 1 217 ALA 217 197 197 ALA ALA A . n 
A 1 218 SER 218 198 198 SER SER A . n 
A 1 219 ALA 219 199 199 ALA ALA A . n 
A 1 220 MET 220 200 200 MET MET A . n 
A 1 221 GLU 221 201 201 GLU GLU A . n 
A 1 222 TRP 222 202 202 TRP TRP A . n 
A 1 223 ALA 223 203 203 ALA ALA A . n 
A 1 224 GLY 224 204 204 GLY GLY A . n 
A 1 225 TYR 225 205 205 TYR TYR A . n 
A 1 226 ALA 226 206 206 ALA ALA A . n 
A 1 227 PRO 227 207 207 PRO PRO A . n 
A 1 228 LYS 228 208 208 LYS LYS A . n 
A 1 229 LEU 229 209 209 LEU LEU A . n 
A 1 230 VAL 230 210 210 VAL VAL A . n 
A 1 231 GLU 231 211 211 GLU GLU A . n 
A 1 232 GLY 232 212 212 GLY GLY A . n 
A 1 233 ARG 233 213 213 ARG ARG A . n 
A 1 234 ALA 234 214 214 ALA ALA A . n 
A 1 235 ASP 235 215 215 ASP ASP A . n 
A 1 236 ASN 236 216 216 ASN ASN A . n 
A 1 237 LEU 237 217 217 LEU LEU A . n 
A 1 238 LYS 238 218 218 LYS LYS A . n 
A 1 239 ILE 239 219 219 ILE ILE A . n 
A 1 240 THR 240 220 220 THR THR A . n 
A 1 241 THR 241 221 221 THR THR A . n 
A 1 242 PRO 242 222 222 PRO PRO A . n 
A 1 243 GLU 243 223 223 GLU GLU A . n 
A 1 244 ASP 244 224 224 ASP ASP A . n 
A 1 245 LEU 245 225 225 LEU LEU A . n 
A 1 246 LEU 246 226 226 LEU LEU A . n 
A 1 247 ARG 247 227 227 ARG ARG A . n 
A 1 248 LEU 248 228 228 LEU LEU A . n 
A 1 249 GLN 249 229 229 GLN GLN A . n 
A 1 250 ARG 250 230 230 ARG ARG A . n 
A 1 251 SER 251 231 231 SER SER A . n 
A 1 252 PHE 252 232 232 PHE PHE A . n 
A 1 253 PRO 253 233 233 PRO PRO A . n 
A 1 254 HIS 254 234 ?   ?   ?   A . n 
A 1 255 LEU 255 235 ?   ?   ?   A . n 
A 1 256 GLU 256 236 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IJT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IJT 
_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 A1IJT 1  301 301 A1IJT 083 A . 
C 3 HOH   1  401 8   HOH   HOH A . 
C 3 HOH   2  402 29  HOH   HOH A . 
C 3 HOH   3  403 17  HOH   HOH A . 
C 3 HOH   4  404 10  HOH   HOH A . 
C 3 HOH   5  405 18  HOH   HOH A . 
C 3 HOH   6  406 19  HOH   HOH A . 
C 3 HOH   7  407 7   HOH   HOH A . 
C 3 HOH   8  408 2   HOH   HOH A . 
C 3 HOH   9  409 48  HOH   HOH A . 
C 3 HOH   10 410 25  HOH   HOH A . 
C 3 HOH   11 411 36  HOH   HOH A . 
C 3 HOH   12 412 1   HOH   HOH A . 
C 3 HOH   13 413 33  HOH   HOH A . 
C 3 HOH   14 414 3   HOH   HOH A . 
C 3 HOH   15 415 22  HOH   HOH A . 
C 3 HOH   16 416 14  HOH   HOH A . 
C 3 HOH   17 417 12  HOH   HOH A . 
C 3 HOH   18 418 13  HOH   HOH A . 
C 3 HOH   19 419 15  HOH   HOH A . 
C 3 HOH   20 420 11  HOH   HOH A . 
C 3 HOH   21 421 34  HOH   HOH A . 
C 3 HOH   22 422 9   HOH   HOH A . 
C 3 HOH   23 423 4   HOH   HOH A . 
C 3 HOH   24 424 35  HOH   HOH A . 
C 3 HOH   25 425 24  HOH   HOH A . 
C 3 HOH   26 426 40  HOH   HOH A . 
C 3 HOH   27 427 21  HOH   HOH A . 
C 3 HOH   28 428 20  HOH   HOH A . 
C 3 HOH   29 429 16  HOH   HOH A . 
C 3 HOH   30 430 47  HOH   HOH A . 
C 3 HOH   31 431 37  HOH   HOH A . 
C 3 HOH   32 432 42  HOH   HOH A . 
C 3 HOH   33 433 5   HOH   HOH A . 
C 3 HOH   34 434 28  HOH   HOH A . 
C 3 HOH   35 435 27  HOH   HOH A . 
C 3 HOH   36 436 30  HOH   HOH A . 
C 3 HOH   37 437 23  HOH   HOH A . 
C 3 HOH   38 438 32  HOH   HOH A . 
C 3 HOH   39 439 31  HOH   HOH A . 
C 3 HOH   40 440 38  HOH   HOH A . 
C 3 HOH   41 441 50  HOH   HOH A . 
C 3 HOH   42 442 51  HOH   HOH A . 
C 3 HOH   43 443 39  HOH   HOH A . 
C 3 HOH   44 444 49  HOH   HOH A . 
C 3 HOH   45 445 26  HOH   HOH A . 
C 3 HOH   46 446 45  HOH   HOH A . 
C 3 HOH   47 447 41  HOH   HOH A . 
C 3 HOH   48 448 44  HOH   HOH A . 
C 3 HOH   49 449 43  HOH   HOH A . 
C 3 HOH   50 450 46  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 28  ? NZ  ? A LYS 48  NZ  
2  1 Y 1 A GLU 223 ? CD  ? A GLU 243 CD  
3  1 Y 1 A GLU 223 ? OE1 ? A GLU 243 OE1 
4  1 Y 1 A GLU 223 ? OE2 ? A GLU 243 OE2 
5  1 Y 1 A ARG 227 ? NE  ? A ARG 247 NE  
6  1 Y 1 A ARG 227 ? CZ  ? A ARG 247 CZ  
7  1 Y 1 A ARG 227 ? NH1 ? A ARG 247 NH1 
8  1 Y 1 A ARG 227 ? NH2 ? A ARG 247 NH2 
9  1 Y 1 A ARG 230 ? CZ  ? A ARG 250 CZ  
10 1 Y 1 A ARG 230 ? NH1 ? A ARG 250 NH1 
11 1 Y 1 A ARG 230 ? NH2 ? A ARG 250 NH2 
# 
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 ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.761 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GCA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.410 
_cell.length_a_esd                 ? 
_cell.length_b                     75.590 
_cell.length_b_esd                 ? 
_cell.length_c                     37.800 
_cell.length_c_esd                 ? 
_cell.volume                       252566.066 
_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                         9GCA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GCA 
_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             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.13 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;26% PEG 500MME
100 mM MES pH 6.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9677 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9677 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          59.23 
_reflns.entry_id                                       9GCA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.17 
_reflns.d_resolution_low                               44.2 
_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                                     12788 
_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                           96.00 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.01 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.07204 
_reflns.pdbx_Rpim_I_all                                0.03746 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.06137 
_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                                    2.17 
_reflns_shell.d_res_low                                     2.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2965 
_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                               3.3 
_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                               0.7483 
_reflns_shell.pdbx_Rpim_I_all                               0.4111 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.843 
_reflns_shell.pdbx_CC_star                                  0.956 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          88.62 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.6201 
_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                               58.85 
_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                                 9GCA 
_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                            2.17 
_refine.ls_d_res_low                             44.20 
_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                     12711 
_refine.ls_number_reflns_R_free                  599 
_refine.ls_number_reflns_R_work                  12112 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.98 
_refine.ls_percent_reflns_R_free                 4.71 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1996 
_refine.ls_R_factor_R_free                       0.2354 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1979 
_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                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.7461 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4068 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.17 
_refine_hist.d_res_low                        44.20 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               1812 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1751 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0021  ? 1813 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4806  ? 2471 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0388  ? 279  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0044  ? 325  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 20.1074 ? 666  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.17 2.39  . . 124 2810 88.61 . . . . 0.4069 . . . . . . . . . . . 0.4580 
'X-RAY DIFFRACTION' 2.39 2.73  . . 152 3024 96.74 . . . . 0.2801 . . . . . . . . . . . 0.3416 
'X-RAY DIFFRACTION' 2.73 3.44  . . 161 3129 99.40 . . . . 0.2230 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 3.44 44.20 . . 162 3149 99.19 . . . . 0.1595 . . . . . . . . . . . 0.1880 
# 
_struct.entry_id                     9GCA 
_struct.title                        'Crystal structure of Pseudomonas aeruginosa IspD in complex with C8H8N2O' 
_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        9GCA 
_struct_keywords.text            'TRANSFERASE, CYTIDYLYLTRANSFERASE, MEP, ISOPRENOID BIOSYNTHESYS, ISPD, PSEUDOMONAS AERUGINOSA' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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                    ISPD_PSEAE 
_struct_ref.pdbx_db_accession          P57707 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTTSDLPAFWTVIPAAGVGSRMRADRPKQYLDLAGRTVIERTLDCFLEHPMLRGLVVCLAEDDPYWPGLDCAASRHVQRA
AGGAERAGSVLNGLLRLLELGAQADDWVLVHDAARPNLTRGDLDRLLEELAEDPVGGLLAVPARDTLKRSDRDGRVSETI
DRSVVWLAYTPQMFRLGALHRALADALVAGVAITDEASAMEWAGYAPKLVEGRADNLKITTPEDLLRLQRSFPH
;
_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              9GCA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 254 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P57707 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  234 
_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       234 
# 
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 9GCA MET A 1   ? UNP P57707 ? ? 'initiating methionine' -19 1  
1 9GCA GLY A 2   ? UNP P57707 ? ? 'expression tag'        -18 2  
1 9GCA SER A 3   ? UNP P57707 ? ? 'expression tag'        -17 3  
1 9GCA SER A 4   ? UNP P57707 ? ? 'expression tag'        -16 4  
1 9GCA HIS A 5   ? UNP P57707 ? ? 'expression tag'        -15 5  
1 9GCA HIS A 6   ? UNP P57707 ? ? 'expression tag'        -14 6  
1 9GCA HIS A 7   ? UNP P57707 ? ? 'expression tag'        -13 7  
1 9GCA HIS A 8   ? UNP P57707 ? ? 'expression tag'        -12 8  
1 9GCA HIS A 9   ? UNP P57707 ? ? 'expression tag'        -11 9  
1 9GCA HIS A 10  ? UNP P57707 ? ? 'expression tag'        -10 10 
1 9GCA SER A 11  ? UNP P57707 ? ? 'expression tag'        -9  11 
1 9GCA SER A 12  ? UNP P57707 ? ? 'expression tag'        -8  12 
1 9GCA GLY A 13  ? UNP P57707 ? ? 'expression tag'        -7  13 
1 9GCA LEU A 14  ? UNP P57707 ? ? 'expression tag'        -6  14 
1 9GCA VAL A 15  ? UNP P57707 ? ? 'expression tag'        -5  15 
1 9GCA PRO A 16  ? UNP P57707 ? ? 'expression tag'        -4  16 
1 9GCA ARG A 17  ? UNP P57707 ? ? 'expression tag'        -3  17 
1 9GCA GLY A 18  ? UNP P57707 ? ? 'expression tag'        -2  18 
1 9GCA SER A 19  ? UNP P57707 ? ? 'expression tag'        -1  19 
1 9GCA HIS A 20  ? UNP P57707 ? ? 'expression tag'        0   20 
1 9GCA LEU A 255 ? UNP P57707 ? ? 'expression tag'        235 21 
1 9GCA GLU A 256 ? UNP P57707 ? ? 'expression tag'        236 22 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3070  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  20060 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 -9.6309713936 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 36.5524881508 
# 
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 PRO A 47  ? LEU A 51  ? PRO A 27  LEU A 31  5 ? 5  
HELX_P HELX_P2 AA2 THR A 57  ? GLU A 68  ? THR A 37  GLU A 48  1 ? 12 
HELX_P HELX_P3 AA3 TYR A 85  ? SER A 94  ? TYR A 65  SER A 74  5 ? 10 
HELX_P HELX_P4 AA4 GLU A 105 ? LEU A 120 ? GLU A 85  LEU A 100 1 ? 16 
HELX_P HELX_P5 AA5 THR A 139 ? ALA A 151 ? THR A 119 ALA A 131 1 ? 13 
HELX_P HELX_P6 AA6 ASP A 181 ? VAL A 184 ? ASP A 161 VAL A 164 5 ? 4  
HELX_P HELX_P7 AA7 LEU A 196 ? GLY A 210 ? LEU A 176 GLY A 190 1 ? 15 
HELX_P HELX_P8 AA8 ASP A 215 ? ALA A 223 ? ASP A 195 ALA A 203 1 ? 9  
HELX_P HELX_P9 AA9 THR A 241 ? GLN A 249 ? THR A 221 GLN A 229 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 190 A . ? THR 170 A PRO 191 A ? PRO 171 A 1 4.55 
2 PHE 252 A . ? PHE 232 A PRO 253 A ? PRO 233 A 1 3.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 97  ? ALA A 101 ? VAL A 77  ALA A 81  
AA1 2 LEU A 72  ? LEU A 79  ? LEU A 52  LEU A 59  
AA1 3 PHE A 29  ? PRO A 34  ? PHE A 9   PRO A 14  
AA1 4 TRP A 127 ? VAL A 130 ? TRP A 107 VAL A 110 
AA1 5 TRP A 186 ? ARG A 195 ? TRP A 166 ARG A 175 
AA1 6 GLY A 156 ? PRO A 162 ? GLY A 136 PRO A 142 
AA1 7 LYS A 228 ? GLU A 231 ? LYS A 208 GLU A 211 
AA2 1 LEU A 167 ? SER A 170 ? LEU A 147 SER A 150 
AA2 2 VAL A 176 ? ILE A 180 ? VAL A 156 ILE A 160 
# 
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 GLN A 98  ? O GLN A 78  N VAL A 77  ? N VAL A 57  
AA1 2 3 O VAL A 76  ? O VAL A 56  N ILE A 33  ? N ILE A 13  
AA1 3 4 N VAL A 32  ? N VAL A 12  O LEU A 129 ? O LEU A 109 
AA1 4 5 N VAL A 128 ? N VAL A 108 O PHE A 194 ? O PHE A 174 
AA1 5 6 O LEU A 187 ? O LEU A 167 N VAL A 161 ? N VAL A 141 
AA1 6 7 N GLY A 156 ? N GLY A 136 O LYS A 228 ? O LYS A 208 
AA2 1 2 N ARG A 169 ? N ARG A 149 O GLU A 178 ? O GLU A 158 
# 
_pdbx_entry_details.entry_id                   9GCA 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 161 ? ? -67.91 98.22  
2 1 THR A 194 ? ? -99.83 -68.41 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A THR 2   ? A THR 22  
23 1 Y 1 A THR 3   ? A THR 23  
24 1 Y 1 A SER 4   ? A SER 24  
25 1 Y 1 A HIS 234 ? A HIS 254 
26 1 Y 1 A LEU 235 ? A LEU 255 
27 1 Y 1 A GLU 236 ? A GLU 256 
# 
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 
A1IJT C10  C N N 1   
A1IJT C01  C N N 2   
A1IJT C03  C N N 3   
A1IJT C04  C Y N 4   
A1IJT C06  C Y N 5   
A1IJT C07  C Y N 6   
A1IJT C08  C Y N 7   
A1IJT C09  C Y N 8   
A1IJT N02  N N N 9   
A1IJT N05  N Y N 10  
A1IJT O11  O N N 11  
A1IJT H101 H N N 12  
A1IJT H102 H N N 13  
A1IJT H012 H N N 14  
A1IJT H011 H N N 15  
A1IJT H013 H N N 16  
A1IJT H061 H N N 17  
A1IJT H071 H N N 18  
A1IJT H081 H N N 19  
ALA   N    N N N 20  
ALA   CA   C N S 21  
ALA   C    C N N 22  
ALA   O    O N N 23  
ALA   CB   C N N 24  
ALA   OXT  O N N 25  
ALA   H    H N N 26  
ALA   H2   H N N 27  
ALA   HA   H N N 28  
ALA   HB1  H N N 29  
ALA   HB2  H N N 30  
ALA   HB3  H N N 31  
ALA   HXT  H N N 32  
ARG   N    N N N 33  
ARG   CA   C N S 34  
ARG   C    C N N 35  
ARG   O    O N N 36  
ARG   CB   C N N 37  
ARG   CG   C N N 38  
ARG   CD   C N N 39  
ARG   NE   N N N 40  
ARG   CZ   C N N 41  
ARG   NH1  N N N 42  
ARG   NH2  N N N 43  
ARG   OXT  O N N 44  
ARG   H    H N N 45  
ARG   H2   H N N 46  
ARG   HA   H N N 47  
ARG   HB2  H N N 48  
ARG   HB3  H N N 49  
ARG   HG2  H N N 50  
ARG   HG3  H N N 51  
ARG   HD2  H N N 52  
ARG   HD3  H N N 53  
ARG   HE   H N N 54  
ARG   HH11 H N N 55  
ARG   HH12 H N N 56  
ARG   HH21 H N N 57  
ARG   HH22 H N N 58  
ARG   HXT  H N N 59  
ASN   N    N N N 60  
ASN   CA   C N S 61  
ASN   C    C N N 62  
ASN   O    O N N 63  
ASN   CB   C N N 64  
ASN   CG   C N N 65  
ASN   OD1  O N N 66  
ASN   ND2  N N N 67  
ASN   OXT  O N N 68  
ASN   H    H N N 69  
ASN   H2   H N N 70  
ASN   HA   H N N 71  
ASN   HB2  H N N 72  
ASN   HB3  H N N 73  
ASN   HD21 H N N 74  
ASN   HD22 H N N 75  
ASN   HXT  H N N 76  
ASP   N    N N N 77  
ASP   CA   C N S 78  
ASP   C    C N N 79  
ASP   O    O N N 80  
ASP   CB   C N N 81  
ASP   CG   C N N 82  
ASP   OD1  O N N 83  
ASP   OD2  O N N 84  
ASP   OXT  O N N 85  
ASP   H    H N N 86  
ASP   H2   H N N 87  
ASP   HA   H N N 88  
ASP   HB2  H N N 89  
ASP   HB3  H N N 90  
ASP   HD2  H N N 91  
ASP   HXT  H N N 92  
CYS   N    N N N 93  
CYS   CA   C N R 94  
CYS   C    C N N 95  
CYS   O    O N N 96  
CYS   CB   C N N 97  
CYS   SG   S N N 98  
CYS   OXT  O N N 99  
CYS   H    H N N 100 
CYS   H2   H N N 101 
CYS   HA   H N N 102 
CYS   HB2  H N N 103 
CYS   HB3  H N N 104 
CYS   HG   H N N 105 
CYS   HXT  H N N 106 
GLN   N    N N N 107 
GLN   CA   C N S 108 
GLN   C    C N N 109 
GLN   O    O N N 110 
GLN   CB   C N N 111 
GLN   CG   C N N 112 
GLN   CD   C N N 113 
GLN   OE1  O N N 114 
GLN   NE2  N N N 115 
GLN   OXT  O N N 116 
GLN   H    H N N 117 
GLN   H2   H N N 118 
GLN   HA   H N N 119 
GLN   HB2  H N N 120 
GLN   HB3  H N N 121 
GLN   HG2  H N N 122 
GLN   HG3  H N N 123 
GLN   HE21 H N N 124 
GLN   HE22 H N N 125 
GLN   HXT  H N N 126 
GLU   N    N N N 127 
GLU   CA   C N S 128 
GLU   C    C N N 129 
GLU   O    O N N 130 
GLU   CB   C N N 131 
GLU   CG   C N N 132 
GLU   CD   C N N 133 
GLU   OE1  O N N 134 
GLU   OE2  O N N 135 
GLU   OXT  O N N 136 
GLU   H    H N N 137 
GLU   H2   H N N 138 
GLU   HA   H N N 139 
GLU   HB2  H N N 140 
GLU   HB3  H N N 141 
GLU   HG2  H N N 142 
GLU   HG3  H N N 143 
GLU   HE2  H N N 144 
GLU   HXT  H N N 145 
GLY   N    N N N 146 
GLY   CA   C N N 147 
GLY   C    C N N 148 
GLY   O    O N N 149 
GLY   OXT  O N N 150 
GLY   H    H N N 151 
GLY   H2   H N N 152 
GLY   HA2  H N N 153 
GLY   HA3  H N N 154 
GLY   HXT  H N N 155 
HIS   N    N N N 156 
HIS   CA   C N S 157 
HIS   C    C N N 158 
HIS   O    O N N 159 
HIS   CB   C N N 160 
HIS   CG   C Y N 161 
HIS   ND1  N Y N 162 
HIS   CD2  C Y N 163 
HIS   CE1  C Y N 164 
HIS   NE2  N Y N 165 
HIS   OXT  O N N 166 
HIS   H    H N N 167 
HIS   H2   H N N 168 
HIS   HA   H N N 169 
HIS   HB2  H N N 170 
HIS   HB3  H N N 171 
HIS   HD1  H N N 172 
HIS   HD2  H N N 173 
HIS   HE1  H N N 174 
HIS   HE2  H N N 175 
HIS   HXT  H N N 176 
HOH   O    O N N 177 
HOH   H1   H N N 178 
HOH   H2   H N N 179 
ILE   N    N N N 180 
ILE   CA   C N S 181 
ILE   C    C N N 182 
ILE   O    O N N 183 
ILE   CB   C N S 184 
ILE   CG1  C N N 185 
ILE   CG2  C N N 186 
ILE   CD1  C N N 187 
ILE   OXT  O N N 188 
ILE   H    H N N 189 
ILE   H2   H N N 190 
ILE   HA   H N N 191 
ILE   HB   H N N 192 
ILE   HG12 H N N 193 
ILE   HG13 H N N 194 
ILE   HG21 H N N 195 
ILE   HG22 H N N 196 
ILE   HG23 H N N 197 
ILE   HD11 H N N 198 
ILE   HD12 H N N 199 
ILE   HD13 H N N 200 
ILE   HXT  H N N 201 
LEU   N    N N N 202 
LEU   CA   C N S 203 
LEU   C    C N N 204 
LEU   O    O N N 205 
LEU   CB   C N N 206 
LEU   CG   C N N 207 
LEU   CD1  C N N 208 
LEU   CD2  C N N 209 
LEU   OXT  O N N 210 
LEU   H    H N N 211 
LEU   H2   H N N 212 
LEU   HA   H N N 213 
LEU   HB2  H N N 214 
LEU   HB3  H N N 215 
LEU   HG   H N N 216 
LEU   HD11 H N N 217 
LEU   HD12 H N N 218 
LEU   HD13 H N N 219 
LEU   HD21 H N N 220 
LEU   HD22 H N N 221 
LEU   HD23 H N N 222 
LEU   HXT  H N N 223 
LYS   N    N N N 224 
LYS   CA   C N S 225 
LYS   C    C N N 226 
LYS   O    O N N 227 
LYS   CB   C N N 228 
LYS   CG   C N N 229 
LYS   CD   C N N 230 
LYS   CE   C N N 231 
LYS   NZ   N N N 232 
LYS   OXT  O N N 233 
LYS   H    H N N 234 
LYS   H2   H N N 235 
LYS   HA   H N N 236 
LYS   HB2  H N N 237 
LYS   HB3  H N N 238 
LYS   HG2  H N N 239 
LYS   HG3  H N N 240 
LYS   HD2  H N N 241 
LYS   HD3  H N N 242 
LYS   HE2  H N N 243 
LYS   HE3  H N N 244 
LYS   HZ1  H N N 245 
LYS   HZ2  H N N 246 
LYS   HZ3  H N N 247 
LYS   HXT  H N N 248 
MET   N    N N N 249 
MET   CA   C N S 250 
MET   C    C N N 251 
MET   O    O N N 252 
MET   CB   C N N 253 
MET   CG   C N N 254 
MET   SD   S N N 255 
MET   CE   C N N 256 
MET   OXT  O N N 257 
MET   H    H N N 258 
MET   H2   H N N 259 
MET   HA   H N N 260 
MET   HB2  H N N 261 
MET   HB3  H N N 262 
MET   HG2  H N N 263 
MET   HG3  H N N 264 
MET   HE1  H N N 265 
MET   HE2  H N N 266 
MET   HE3  H N N 267 
MET   HXT  H N N 268 
PHE   N    N N N 269 
PHE   CA   C N S 270 
PHE   C    C N N 271 
PHE   O    O N N 272 
PHE   CB   C N N 273 
PHE   CG   C Y N 274 
PHE   CD1  C Y N 275 
PHE   CD2  C Y N 276 
PHE   CE1  C Y N 277 
PHE   CE2  C Y N 278 
PHE   CZ   C Y N 279 
PHE   OXT  O N N 280 
PHE   H    H N N 281 
PHE   H2   H N N 282 
PHE   HA   H N N 283 
PHE   HB2  H N N 284 
PHE   HB3  H N N 285 
PHE   HD1  H N N 286 
PHE   HD2  H N N 287 
PHE   HE1  H N N 288 
PHE   HE2  H N N 289 
PHE   HZ   H N N 290 
PHE   HXT  H N N 291 
PRO   N    N N N 292 
PRO   CA   C N S 293 
PRO   C    C N N 294 
PRO   O    O N N 295 
PRO   CB   C N N 296 
PRO   CG   C N N 297 
PRO   CD   C N N 298 
PRO   OXT  O N N 299 
PRO   H    H N N 300 
PRO   HA   H N N 301 
PRO   HB2  H N N 302 
PRO   HB3  H N N 303 
PRO   HG2  H N N 304 
PRO   HG3  H N N 305 
PRO   HD2  H N N 306 
PRO   HD3  H N N 307 
PRO   HXT  H N N 308 
SER   N    N N N 309 
SER   CA   C N S 310 
SER   C    C N N 311 
SER   O    O N N 312 
SER   CB   C N N 313 
SER   OG   O N N 314 
SER   OXT  O N N 315 
SER   H    H N N 316 
SER   H2   H N N 317 
SER   HA   H N N 318 
SER   HB2  H N N 319 
SER   HB3  H N N 320 
SER   HG   H N N 321 
SER   HXT  H N N 322 
THR   N    N N N 323 
THR   CA   C N S 324 
THR   C    C N N 325 
THR   O    O N N 326 
THR   CB   C N R 327 
THR   OG1  O N N 328 
THR   CG2  C N N 329 
THR   OXT  O N N 330 
THR   H    H N N 331 
THR   H2   H N N 332 
THR   HA   H N N 333 
THR   HB   H N N 334 
THR   HG1  H N N 335 
THR   HG21 H N N 336 
THR   HG22 H N N 337 
THR   HG23 H N N 338 
THR   HXT  H N N 339 
TRP   N    N N N 340 
TRP   CA   C N S 341 
TRP   C    C N N 342 
TRP   O    O N N 343 
TRP   CB   C N N 344 
TRP   CG   C Y N 345 
TRP   CD1  C Y N 346 
TRP   CD2  C Y N 347 
TRP   NE1  N Y N 348 
TRP   CE2  C Y N 349 
TRP   CE3  C Y N 350 
TRP   CZ2  C Y N 351 
TRP   CZ3  C Y N 352 
TRP   CH2  C Y N 353 
TRP   OXT  O N N 354 
TRP   H    H N N 355 
TRP   H2   H N N 356 
TRP   HA   H N N 357 
TRP   HB2  H N N 358 
TRP   HB3  H N N 359 
TRP   HD1  H N N 360 
TRP   HE1  H N N 361 
TRP   HE3  H N N 362 
TRP   HZ2  H N N 363 
TRP   HZ3  H N N 364 
TRP   HH2  H N N 365 
TRP   HXT  H N N 366 
TYR   N    N N N 367 
TYR   CA   C N S 368 
TYR   C    C N N 369 
TYR   O    O N N 370 
TYR   CB   C N N 371 
TYR   CG   C Y N 372 
TYR   CD1  C Y N 373 
TYR   CD2  C Y N 374 
TYR   CE1  C Y N 375 
TYR   CE2  C Y N 376 
TYR   CZ   C Y N 377 
TYR   OH   O N N 378 
TYR   OXT  O N N 379 
TYR   H    H N N 380 
TYR   H2   H N N 381 
TYR   HA   H N N 382 
TYR   HB2  H N N 383 
TYR   HB3  H N N 384 
TYR   HD1  H N N 385 
TYR   HD2  H N N 386 
TYR   HE1  H N N 387 
TYR   HE2  H N N 388 
TYR   HH   H N N 389 
TYR   HXT  H N N 390 
VAL   N    N N N 391 
VAL   CA   C N S 392 
VAL   C    C N N 393 
VAL   O    O N N 394 
VAL   CB   C N N 395 
VAL   CG1  C N N 396 
VAL   CG2  C N N 397 
VAL   OXT  O N N 398 
VAL   H    H N N 399 
VAL   H2   H N N 400 
VAL   HA   H N N 401 
VAL   HB   H N N 402 
VAL   HG11 H N N 403 
VAL   HG12 H N N 404 
VAL   HG13 H N N 405 
VAL   HG21 H N N 406 
VAL   HG22 H N N 407 
VAL   HG23 H N N 408 
VAL   HXT  H N N 409 
# 
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 
A1IJT N02 C01  sing N N 1   
A1IJT C03 N02  sing N N 2   
A1IJT N05 C04  doub Y N 3   
A1IJT C06 N05  sing Y N 4   
A1IJT C07 C06  doub Y N 5   
A1IJT C08 C07  sing Y N 6   
A1IJT C09 C08  doub Y N 7   
A1IJT C10 C09  sing N N 8   
A1IJT C04 C03  sing N N 9   
A1IJT O11 C03  doub N N 10  
A1IJT N02 C10  sing N N 11  
A1IJT C04 C09  sing Y N 12  
A1IJT C10 H101 sing N N 13  
A1IJT C10 H102 sing N N 14  
A1IJT C01 H012 sing N N 15  
A1IJT C01 H011 sing N N 16  
A1IJT C01 H013 sing N N 17  
A1IJT C06 H061 sing N N 18  
A1IJT C07 H071 sing N N 19  
A1IJT C08 H081 sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
CYS   N   CA   sing N N 90  
CYS   N   H    sing N N 91  
CYS   N   H2   sing N N 92  
CYS   CA  C    sing N N 93  
CYS   CA  CB   sing N N 94  
CYS   CA  HA   sing N N 95  
CYS   C   O    doub N N 96  
CYS   C   OXT  sing N N 97  
CYS   CB  SG   sing N N 98  
CYS   CB  HB2  sing N N 99  
CYS   CB  HB3  sing N N 100 
CYS   SG  HG   sing N N 101 
CYS   OXT HXT  sing N N 102 
GLN   N   CA   sing N N 103 
GLN   N   H    sing N N 104 
GLN   N   H2   sing N N 105 
GLN   CA  C    sing N N 106 
GLN   CA  CB   sing N N 107 
GLN   CA  HA   sing N N 108 
GLN   C   O    doub N N 109 
GLN   C   OXT  sing N N 110 
GLN   CB  CG   sing N N 111 
GLN   CB  HB2  sing N N 112 
GLN   CB  HB3  sing N N 113 
GLN   CG  CD   sing N N 114 
GLN   CG  HG2  sing N N 115 
GLN   CG  HG3  sing N N 116 
GLN   CD  OE1  doub N N 117 
GLN   CD  NE2  sing N N 118 
GLN   NE2 HE21 sing N N 119 
GLN   NE2 HE22 sing N N 120 
GLN   OXT HXT  sing N N 121 
GLU   N   CA   sing N N 122 
GLU   N   H    sing N N 123 
GLU   N   H2   sing N N 124 
GLU   CA  C    sing N N 125 
GLU   CA  CB   sing N N 126 
GLU   CA  HA   sing N N 127 
GLU   C   O    doub N N 128 
GLU   C   OXT  sing N N 129 
GLU   CB  CG   sing N N 130 
GLU   CB  HB2  sing N N 131 
GLU   CB  HB3  sing N N 132 
GLU   CG  CD   sing N N 133 
GLU   CG  HG2  sing N N 134 
GLU   CG  HG3  sing N N 135 
GLU   CD  OE1  doub N N 136 
GLU   CD  OE2  sing N N 137 
GLU   OE2 HE2  sing N N 138 
GLU   OXT HXT  sing N N 139 
GLY   N   CA   sing N N 140 
GLY   N   H    sing N N 141 
GLY   N   H2   sing N N 142 
GLY   CA  C    sing N N 143 
GLY   CA  HA2  sing N N 144 
GLY   CA  HA3  sing N N 145 
GLY   C   O    doub N N 146 
GLY   C   OXT  sing N N 147 
GLY   OXT HXT  sing N N 148 
HIS   N   CA   sing N N 149 
HIS   N   H    sing N N 150 
HIS   N   H2   sing N N 151 
HIS   CA  C    sing N N 152 
HIS   CA  CB   sing N N 153 
HIS   CA  HA   sing N N 154 
HIS   C   O    doub N N 155 
HIS   C   OXT  sing N N 156 
HIS   CB  CG   sing N N 157 
HIS   CB  HB2  sing N N 158 
HIS   CB  HB3  sing N N 159 
HIS   CG  ND1  sing Y N 160 
HIS   CG  CD2  doub Y N 161 
HIS   ND1 CE1  doub Y N 162 
HIS   ND1 HD1  sing N N 163 
HIS   CD2 NE2  sing Y N 164 
HIS   CD2 HD2  sing N N 165 
HIS   CE1 NE2  sing Y N 166 
HIS   CE1 HE1  sing N N 167 
HIS   NE2 HE2  sing N N 168 
HIS   OXT HXT  sing N N 169 
HOH   O   H1   sing N N 170 
HOH   O   H2   sing N N 171 
ILE   N   CA   sing N N 172 
ILE   N   H    sing N N 173 
ILE   N   H2   sing N N 174 
ILE   CA  C    sing N N 175 
ILE   CA  CB   sing N N 176 
ILE   CA  HA   sing N N 177 
ILE   C   O    doub N N 178 
ILE   C   OXT  sing N N 179 
ILE   CB  CG1  sing N N 180 
ILE   CB  CG2  sing N N 181 
ILE   CB  HB   sing N N 182 
ILE   CG1 CD1  sing N N 183 
ILE   CG1 HG12 sing N N 184 
ILE   CG1 HG13 sing N N 185 
ILE   CG2 HG21 sing N N 186 
ILE   CG2 HG22 sing N N 187 
ILE   CG2 HG23 sing N N 188 
ILE   CD1 HD11 sing N N 189 
ILE   CD1 HD12 sing N N 190 
ILE   CD1 HD13 sing N N 191 
ILE   OXT HXT  sing N N 192 
LEU   N   CA   sing N N 193 
LEU   N   H    sing N N 194 
LEU   N   H2   sing N N 195 
LEU   CA  C    sing N N 196 
LEU   CA  CB   sing N N 197 
LEU   CA  HA   sing N N 198 
LEU   C   O    doub N N 199 
LEU   C   OXT  sing N N 200 
LEU   CB  CG   sing N N 201 
LEU   CB  HB2  sing N N 202 
LEU   CB  HB3  sing N N 203 
LEU   CG  CD1  sing N N 204 
LEU   CG  CD2  sing N N 205 
LEU   CG  HG   sing N N 206 
LEU   CD1 HD11 sing N N 207 
LEU   CD1 HD12 sing N N 208 
LEU   CD1 HD13 sing N N 209 
LEU   CD2 HD21 sing N N 210 
LEU   CD2 HD22 sing N N 211 
LEU   CD2 HD23 sing N N 212 
LEU   OXT HXT  sing N N 213 
LYS   N   CA   sing N N 214 
LYS   N   H    sing N N 215 
LYS   N   H2   sing N N 216 
LYS   CA  C    sing N N 217 
LYS   CA  CB   sing N N 218 
LYS   CA  HA   sing N N 219 
LYS   C   O    doub N N 220 
LYS   C   OXT  sing N N 221 
LYS   CB  CG   sing N N 222 
LYS   CB  HB2  sing N N 223 
LYS   CB  HB3  sing N N 224 
LYS   CG  CD   sing N N 225 
LYS   CG  HG2  sing N N 226 
LYS   CG  HG3  sing N N 227 
LYS   CD  CE   sing N N 228 
LYS   CD  HD2  sing N N 229 
LYS   CD  HD3  sing N N 230 
LYS   CE  NZ   sing N N 231 
LYS   CE  HE2  sing N N 232 
LYS   CE  HE3  sing N N 233 
LYS   NZ  HZ1  sing N N 234 
LYS   NZ  HZ2  sing N N 235 
LYS   NZ  HZ3  sing N N 236 
LYS   OXT HXT  sing N N 237 
MET   N   CA   sing N N 238 
MET   N   H    sing N N 239 
MET   N   H2   sing N N 240 
MET   CA  C    sing N N 241 
MET   CA  CB   sing N N 242 
MET   CA  HA   sing N N 243 
MET   C   O    doub N N 244 
MET   C   OXT  sing N N 245 
MET   CB  CG   sing N N 246 
MET   CB  HB2  sing N N 247 
MET   CB  HB3  sing N N 248 
MET   CG  SD   sing N N 249 
MET   CG  HG2  sing N N 250 
MET   CG  HG3  sing N N 251 
MET   SD  CE   sing N N 252 
MET   CE  HE1  sing N N 253 
MET   CE  HE2  sing N N 254 
MET   CE  HE3  sing N N 255 
MET   OXT HXT  sing N N 256 
PHE   N   CA   sing N N 257 
PHE   N   H    sing N N 258 
PHE   N   H2   sing N N 259 
PHE   CA  C    sing N N 260 
PHE   CA  CB   sing N N 261 
PHE   CA  HA   sing N N 262 
PHE   C   O    doub N N 263 
PHE   C   OXT  sing N N 264 
PHE   CB  CG   sing N N 265 
PHE   CB  HB2  sing N N 266 
PHE   CB  HB3  sing N N 267 
PHE   CG  CD1  doub Y N 268 
PHE   CG  CD2  sing Y N 269 
PHE   CD1 CE1  sing Y N 270 
PHE   CD1 HD1  sing N N 271 
PHE   CD2 CE2  doub Y N 272 
PHE   CD2 HD2  sing N N 273 
PHE   CE1 CZ   doub Y N 274 
PHE   CE1 HE1  sing N N 275 
PHE   CE2 CZ   sing Y N 276 
PHE   CE2 HE2  sing N N 277 
PHE   CZ  HZ   sing N N 278 
PHE   OXT HXT  sing N N 279 
PRO   N   CA   sing N N 280 
PRO   N   CD   sing N N 281 
PRO   N   H    sing N N 282 
PRO   CA  C    sing N N 283 
PRO   CA  CB   sing N N 284 
PRO   CA  HA   sing N N 285 
PRO   C   O    doub N N 286 
PRO   C   OXT  sing N N 287 
PRO   CB  CG   sing N N 288 
PRO   CB  HB2  sing N N 289 
PRO   CB  HB3  sing N N 290 
PRO   CG  CD   sing N N 291 
PRO   CG  HG2  sing N N 292 
PRO   CG  HG3  sing N N 293 
PRO   CD  HD2  sing N N 294 
PRO   CD  HD3  sing N N 295 
PRO   OXT HXT  sing N N 296 
SER   N   CA   sing N N 297 
SER   N   H    sing N N 298 
SER   N   H2   sing N N 299 
SER   CA  C    sing N N 300 
SER   CA  CB   sing N N 301 
SER   CA  HA   sing N N 302 
SER   C   O    doub N N 303 
SER   C   OXT  sing N N 304 
SER   CB  OG   sing N N 305 
SER   CB  HB2  sing N N 306 
SER   CB  HB3  sing N N 307 
SER   OG  HG   sing N N 308 
SER   OXT HXT  sing N N 309 
THR   N   CA   sing N N 310 
THR   N   H    sing N N 311 
THR   N   H2   sing N N 312 
THR   CA  C    sing N N 313 
THR   CA  CB   sing N N 314 
THR   CA  HA   sing N N 315 
THR   C   O    doub N N 316 
THR   C   OXT  sing N N 317 
THR   CB  OG1  sing N N 318 
THR   CB  CG2  sing N N 319 
THR   CB  HB   sing N N 320 
THR   OG1 HG1  sing N N 321 
THR   CG2 HG21 sing N N 322 
THR   CG2 HG22 sing N N 323 
THR   CG2 HG23 sing N N 324 
THR   OXT HXT  sing N N 325 
TRP   N   CA   sing N N 326 
TRP   N   H    sing N N 327 
TRP   N   H2   sing N N 328 
TRP   CA  C    sing N N 329 
TRP   CA  CB   sing N N 330 
TRP   CA  HA   sing N N 331 
TRP   C   O    doub N N 332 
TRP   C   OXT  sing N N 333 
TRP   CB  CG   sing N N 334 
TRP   CB  HB2  sing N N 335 
TRP   CB  HB3  sing N N 336 
TRP   CG  CD1  doub Y N 337 
TRP   CG  CD2  sing Y N 338 
TRP   CD1 NE1  sing Y N 339 
TRP   CD1 HD1  sing N N 340 
TRP   CD2 CE2  doub Y N 341 
TRP   CD2 CE3  sing Y N 342 
TRP   NE1 CE2  sing Y N 343 
TRP   NE1 HE1  sing N N 344 
TRP   CE2 CZ2  sing Y N 345 
TRP   CE3 CZ3  doub Y N 346 
TRP   CE3 HE3  sing N N 347 
TRP   CZ2 CH2  doub Y N 348 
TRP   CZ2 HZ2  sing N N 349 
TRP   CZ3 CH2  sing Y N 350 
TRP   CZ3 HZ3  sing N N 351 
TRP   CH2 HH2  sing N N 352 
TRP   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_pdbx_audit_support.funding_organization   'H2020 Marie Curie Actions of the European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1INJ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9GCA 
_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]   0.010940 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002882 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013229 
_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]   0.027358 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 25  ? -10.25881 22.47074 -14.86727 1.000 85.24708  ? 5   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 25  ? -11.70585 22.64299 -14.92963 1.000 89.54592  ? 5   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 25  ? -12.35277 22.26939 -13.59883 1.000 88.06439  ? 5   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 25  ? -12.63963 21.09907 -13.34390 1.000 81.82851  ? 5   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 25  ? -12.29797 21.80279 -16.06307 1.000 92.10673  ? 5   ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 25  ? -11.66985 22.11452 -17.40844 1.000 110.09939 ? 5   ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 25  ? -10.50224 21.72329 -17.62486 1.000 109.73168 ? 5   ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 25  ? -12.34264 22.75143 -18.24766 1.000 98.41577  ? 5   ASP   A OD2 1 
ATOM   9    N N   . LEU   A 1 26  ? -12.58085 23.27397 -12.75731 1.000 79.45546  ? 6   LEU   A N   1 
ATOM   10   C CA  . LEU   A 1 26  ? -13.14613 23.02755 -11.43926 1.000 62.50985  ? 6   LEU   A CA  1 
ATOM   11   C C   . LEU   A 1 26  ? -14.61887 22.63821 -11.55766 1.000 62.36791  ? 6   LEU   A C   1 
ATOM   12   O O   . LEU   A 1 26  ? -15.33197 23.15204 -12.42566 1.000 59.51294  ? 6   LEU   A O   1 
ATOM   13   C CB  . LEU   A 1 26  ? -12.99721 24.26538 -10.55545 1.000 62.14326  ? 6   LEU   A CB  1 
ATOM   14   C CG  . LEU   A 1 26  ? -11.56008 24.62667 -10.17310 1.000 70.20384  ? 6   LEU   A CG  1 
ATOM   15   C CD1 . LEU   A 1 26  ? -11.51344 25.93888 -9.40535  1.000 55.80390  ? 6   LEU   A CD1 1 
ATOM   16   C CD2 . LEU   A 1 26  ? -10.92988 23.50356 -9.36189  1.000 64.22395  ? 6   LEU   A CD2 1 
ATOM   17   N N   . PRO   A 1 27  ? -15.10199 21.73756 -10.70678 1.000 60.77070  ? 7   PRO   A N   1 
ATOM   18   C CA  . PRO   A 1 27  ? -16.49571 21.29769 -10.80788 1.000 53.49790  ? 7   PRO   A CA  1 
ATOM   19   C C   . PRO   A 1 27  ? -17.46544 22.31579 -10.22893 1.000 60.55092  ? 7   PRO   A C   1 
ATOM   20   O O   . PRO   A 1 27  ? -17.11284 23.14583 -9.38716  1.000 54.14680  ? 7   PRO   A O   1 
ATOM   21   C CB  . PRO   A 1 27  ? -16.51046 20.00049 -9.99020  1.000 62.29329  ? 7   PRO   A CB  1 
ATOM   22   C CG  . PRO   A 1 27  ? -15.44065 20.20565 -8.96609  1.000 56.45775  ? 7   PRO   A CG  1 
ATOM   23   C CD  . PRO   A 1 27  ? -14.37080 21.03403 -9.63652  1.000 57.55747  ? 7   PRO   A CD  1 
ATOM   24   N N   . ALA   A 1 28  ? -18.70670 22.24289 -10.70514 1.000 52.59826  ? 8   ALA   A N   1 
ATOM   25   C CA  . ALA   A 1 28  ? -19.77843 23.04085 -10.12806 1.000 58.54138  ? 8   ALA   A CA  1 
ATOM   26   C C   . ALA   A 1 28  ? -20.17644 22.46904 -8.77264  1.000 62.72624  ? 8   ALA   A C   1 
ATOM   27   O O   . ALA   A 1 28  ? -20.11391 21.25730 -8.54546  1.000 59.16931  ? 8   ALA   A O   1 
ATOM   28   C CB  . ALA   A 1 28  ? -20.98711 23.07654 -11.06367 1.000 54.07465  ? 8   ALA   A CB  1 
ATOM   29   N N   . PHE   A 1 29  ? -20.58530 23.35195 -7.86194  1.000 51.90273  ? 9   PHE   A N   1 
ATOM   30   C CA  . PHE   A 1 29  ? -20.83270 22.92912 -6.49185  1.000 52.82047  ? 9   PHE   A CA  1 
ATOM   31   C C   . PHE   A 1 29  ? -21.86634 23.82796 -5.83182  1.000 55.59972  ? 9   PHE   A C   1 
ATOM   32   O O   . PHE   A 1 29  ? -21.93412 25.03115 -6.09977  1.000 50.01083  ? 9   PHE   A O   1 
ATOM   33   C CB  . PHE   A 1 29  ? -19.53930 22.93323 -5.66431  1.000 52.67727  ? 9   PHE   A CB  1 
ATOM   34   C CG  . PHE   A 1 29  ? -18.94892 24.30186 -5.46072  1.000 49.73582  ? 9   PHE   A CG  1 
ATOM   35   C CD1 . PHE   A 1 29  ? -18.13913 24.87238 -6.42908  1.000 55.28588  ? 9   PHE   A CD1 1 
ATOM   36   C CD2 . PHE   A 1 29  ? -19.19679 25.01420 -4.29634  1.000 49.78086  ? 9   PHE   A CD2 1 
ATOM   37   C CE1 . PHE   A 1 29  ? -17.59241 26.13038 -6.24476  1.000 51.81181  ? 9   PHE   A CE1 1 
ATOM   38   C CE2 . PHE   A 1 29  ? -18.65342 26.27273 -4.10507  1.000 57.47240  ? 9   PHE   A CE2 1 
ATOM   39   C CZ  . PHE   A 1 29  ? -17.84971 26.83126 -5.08103  1.000 53.83243  ? 9   PHE   A CZ  1 
ATOM   40   N N   . TRP   A 1 30  ? -22.66711 23.22422 -4.96091  1.000 51.28459  ? 10  TRP   A N   1 
ATOM   41   C CA  . TRP   A 1 30  ? -23.51724 23.96766 -4.04725  1.000 49.08110  ? 10  TRP   A CA  1 
ATOM   42   C C   . TRP   A 1 30  ? -22.80052 24.13754 -2.71183  1.000 52.66443  ? 10  TRP   A C   1 
ATOM   43   O O   . TRP   A 1 30  ? -21.85766 23.41209 -2.38934  1.000 60.20261  ? 10  TRP   A O   1 
ATOM   44   C CB  . TRP   A 1 30  ? -24.85658 23.25769 -3.84221  1.000 51.38138  ? 10  TRP   A CB  1 
ATOM   45   C CG  . TRP   A 1 30  ? -25.52501 22.84700 -5.12035  1.000 64.70325  ? 10  TRP   A CG  1 
ATOM   46   C CD1 . TRP   A 1 30  ? -25.28140 21.71661 -5.84274  1.000 52.31273  ? 10  TRP   A CD1 1 
ATOM   47   C CD2 . TRP   A 1 30  ? -26.54935 23.56224 -5.82650  1.000 70.20869  ? 10  TRP   A CD2 1 
ATOM   48   N NE1 . TRP   A 1 30  ? -26.08668 21.68374 -6.95454  1.000 60.58836  ? 10  TRP   A NE1 1 
ATOM   49   C CE2 . TRP   A 1 30  ? -26.87422 22.80412 -6.96828  1.000 70.85108  ? 10  TRP   A CE2 1 
ATOM   50   C CE3 . TRP   A 1 30  ? -27.22088 24.76936 -5.60422  1.000 57.75096  ? 10  TRP   A CE3 1 
ATOM   51   C CZ2 . TRP   A 1 30  ? -27.84020 23.21008 -7.88425  1.000 71.26820  ? 10  TRP   A CZ2 1 
ATOM   52   C CZ3 . TRP   A 1 30  ? -28.18052 25.17203 -6.51625  1.000 63.40046  ? 10  TRP   A CZ3 1 
ATOM   53   C CH2 . TRP   A 1 30  ? -28.47982 24.39397 -7.64348  1.000 67.10510  ? 10  TRP   A CH2 1 
ATOM   54   N N   . THR   A 1 31  ? -23.25456 25.11556 -1.93398  1.000 53.58475  ? 11  THR   A N   1 
ATOM   55   C CA  . THR   A 1 31  ? -22.65575 25.41297 -0.64093  1.000 44.35053  ? 11  THR   A CA  1 
ATOM   56   C C   . THR   A 1 31  ? -23.74934 25.49373 0.41067   1.000 48.27687  ? 11  THR   A C   1 
ATOM   57   O O   . THR   A 1 31  ? -24.78382 26.12971 0.18725   1.000 49.76990  ? 11  THR   A O   1 
ATOM   58   C CB  . THR   A 1 31  ? -21.86176 26.72425 -0.68069  1.000 50.17710  ? 11  THR   A CB  1 
ATOM   59   O OG1 . THR   A 1 31  ? -20.74940 26.58716 -1.57398  1.000 55.95946  ? 11  THR   A OG1 1 
ATOM   60   C CG2 . THR   A 1 31  ? -21.34407 27.08203 0.70683   1.000 49.43096  ? 11  THR   A CG2 1 
ATOM   61   N N   . VAL   A 1 32  ? -23.52248 24.83982 1.54684   1.000 46.75314  ? 12  VAL   A N   1 
ATOM   62   C CA  . VAL   A 1 32  ? -24.40766 24.91504 2.70180   1.000 49.81207  ? 12  VAL   A CA  1 
ATOM   63   C C   . VAL   A 1 32  ? -23.61204 25.47369 3.87163   1.000 48.73553  ? 12  VAL   A C   1 
ATOM   64   O O   . VAL   A 1 32  ? -22.53999 24.95457 4.20343   1.000 51.41660  ? 12  VAL   A O   1 
ATOM   65   C CB  . VAL   A 1 32  ? -25.00504 23.54219 3.05844   1.000 45.43182  ? 12  VAL   A CB  1 
ATOM   66   C CG1 . VAL   A 1 32  ? -25.81979 23.64186 4.33991   1.000 44.93295  ? 12  VAL   A CG1 1 
ATOM   67   C CG2 . VAL   A 1 32  ? -25.85962 23.02086 1.91614   1.000 42.33405  ? 12  VAL   A CG2 1 
ATOM   68   N N   . ILE   A 1 33  ? -24.13046 26.53169 4.48641   1.000 45.30863  ? 13  ILE   A N   1 
ATOM   69   C CA  . ILE   A 1 33  ? -23.50478 27.12342 5.66515   1.000 48.17383  ? 13  ILE   A CA  1 
ATOM   70   C C   . ILE   A 1 33  ? -24.42689 26.90168 6.85865   1.000 49.71904  ? 13  ILE   A C   1 
ATOM   71   O O   . ILE   A 1 33  ? -25.39282 27.65739 7.04076   1.000 44.29271  ? 13  ILE   A O   1 
ATOM   72   C CB  . ILE   A 1 33  ? -23.21235 28.61864 5.45864   1.000 48.80031  ? 13  ILE   A CB  1 
ATOM   73   C CG1 . ILE   A 1 33  ? -22.37241 28.83808 4.19736   1.000 40.46993  ? 13  ILE   A CG1 1 
ATOM   74   C CG2 . ILE   A 1 33  ? -22.49765 29.19107 6.67477   1.000 43.95105  ? 13  ILE   A CG2 1 
ATOM   75   C CD1 . ILE   A 1 33  ? -20.94733 28.34881 4.31866   1.000 47.37626  ? 13  ILE   A CD1 1 
ATOM   76   N N   . PRO   A 1 34  ? -24.18818 25.87940 7.68216   1.000 50.50683  ? 14  PRO   A N   1 
ATOM   77   C CA  . PRO   A 1 34  ? -25.02649 25.67494 8.87455   1.000 48.58487  ? 14  PRO   A CA  1 
ATOM   78   C C   . PRO   A 1 34  ? -24.74099 26.74746 9.91649   1.000 45.05719  ? 14  PRO   A C   1 
ATOM   79   O O   . PRO   A 1 34  ? -23.62441 26.85221 10.42954  1.000 50.25869  ? 14  PRO   A O   1 
ATOM   80   C CB  . PRO   A 1 34  ? -24.61859 24.27927 9.36115   1.000 49.78189  ? 14  PRO   A CB  1 
ATOM   81   C CG  . PRO   A 1 34  ? -23.23457 24.08514 8.83360   1.000 46.64946  ? 14  PRO   A CG  1 
ATOM   82   C CD  . PRO   A 1 34  ? -23.17175 24.82424 7.52567   1.000 41.60924  ? 14  PRO   A CD  1 
ATOM   83   N N   . ALA   A 1 35  ? -25.76152 27.55385 10.22273  1.000 42.96825  ? 15  ALA   A N   1 
ATOM   84   C CA  . ALA   A 1 35  ? -25.60307 28.67717 11.13840  1.000 52.90815  ? 15  ALA   A CA  1 
ATOM   85   C C   . ALA   A 1 35  ? -26.80558 28.82195 12.06414  1.000 52.98179  ? 15  ALA   A C   1 
ATOM   86   O O   . ALA   A 1 35  ? -27.13442 29.93507 12.48977  1.000 52.43887  ? 15  ALA   A O   1 
ATOM   87   C CB  . ALA   A 1 35  ? -25.37673 29.98371 10.37167  1.000 42.11866  ? 15  ALA   A CB  1 
ATOM   88   N N   . ALA   A 1 36  ? -27.47319 27.71667 12.38099  1.000 57.60407  ? 16  ALA   A N   1 
ATOM   89   C CA  . ALA   A 1 36  ? -28.63166 27.74162 13.26178  1.000 48.62617  ? 16  ALA   A CA  1 
ATOM   90   C C   . ALA   A 1 36  ? -28.16227 27.59539 14.71103  1.000 46.99885  ? 16  ALA   A C   1 
ATOM   91   O O   . ALA   A 1 36  ? -26.99026 27.82071 15.02453  1.000 54.00557  ? 16  ALA   A O   1 
ATOM   92   C CB  . ALA   A 1 36  ? -29.62914 26.65779 12.84232  1.000 50.48456  ? 16  ALA   A CB  1 
ATOM   93   N N   . GLY   A 1 37  ? -29.06619 27.21318 15.61101  1.000 53.46158  ? 17  GLY   A N   1 
ATOM   94   C CA  . GLY   A 1 37  ? -28.76358 27.18309 17.02451  1.000 60.13075  ? 17  GLY   A CA  1 
ATOM   95   C C   . GLY   A 1 37  ? -28.75873 28.53591 17.69892  1.000 67.23513  ? 17  GLY   A C   1 
ATOM   96   O O   . GLY   A 1 37  ? -28.64155 28.59611 18.92965  1.000 69.86318  ? 17  GLY   A O   1 
ATOM   97   N N   . VAL   A 1 38  ? -28.87619 29.62380 16.93792  1.000 64.73363  ? 18  VAL   A N   1 
ATOM   98   C CA  . VAL   A 1 38  ? -28.96406 30.95379 17.52535  1.000 67.57243  ? 18  VAL   A CA  1 
ATOM   99   C C   . VAL   A 1 38  ? -30.32765 31.12356 18.18092  1.000 73.99861  ? 18  VAL   A C   1 
ATOM   100  O O   . VAL   A 1 38  ? -31.36719 30.82650 17.57713  1.000 76.91894  ? 18  VAL   A O   1 
ATOM   101  C CB  . VAL   A 1 38  ? -28.71954 32.02847 16.45476  1.000 59.19848  ? 18  VAL   A CB  1 
ATOM   102  C CG1 . VAL   A 1 38  ? -28.93792 33.41824 17.02955  1.000 61.72883  ? 18  VAL   A CG1 1 
ATOM   103  C CG2 . VAL   A 1 38  ? -27.31351 31.89888 15.88390  1.000 56.66254  ? 18  VAL   A CG2 1 
ATOM   104  N N   . GLY   A 1 39  ? -30.33069 31.59179 19.42516  1.000 67.34425  ? 19  GLY   A N   1 
ATOM   105  C CA  . GLY   A 1 39  ? -31.57554 31.86384 20.10980  1.000 70.02720  ? 19  GLY   A CA  1 
ATOM   106  C C   . GLY   A 1 39  ? -32.32248 33.02968 19.48912  1.000 72.61847  ? 19  GLY   A C   1 
ATOM   107  O O   . GLY   A 1 39  ? -31.82834 33.74528 18.61700  1.000 80.72230  ? 19  GLY   A O   1 
ATOM   108  N N   . SER   A 1 40  ? -33.55630 33.21906 19.95292  1.000 76.57867  ? 20  SER   A N   1 
ATOM   109  C CA  . SER   A 1 40  ? -34.37106 34.33119 19.48184  1.000 76.24560  ? 20  SER   A CA  1 
ATOM   110  C C   . SER   A 1 40  ? -34.01783 35.64860 20.15324  1.000 73.01553  ? 20  SER   A C   1 
ATOM   111  O O   . SER   A 1 40  ? -34.49173 36.69964 19.70631  1.000 67.50845  ? 20  SER   A O   1 
ATOM   112  C CB  . SER   A 1 40  ? -35.85446 34.03254 19.70872  1.000 77.52553  ? 20  SER   A CB  1 
ATOM   113  O OG  . SER   A 1 40  ? -36.10027 33.66193 21.05346  1.000 82.57332  ? 20  SER   A OG  1 
ATOM   114  N N   . ARG   A 1 41  ? -33.19936 35.61914 21.19897  1.000 68.19270  ? 21  ARG   A N   1 
ATOM   115  C CA  . ARG   A 1 41  ? -32.94519 36.78204 22.03392  1.000 66.91971  ? 21  ARG   A CA  1 
ATOM   116  C C   . ARG   A 1 41  ? -31.52878 37.28565 21.80899  1.000 60.69338  ? 21  ARG   A C   1 
ATOM   117  O O   . ARG   A 1 41  ? -30.56886 36.51134 21.89040  1.000 64.32883  ? 21  ARG   A O   1 
ATOM   118  C CB  . ARG   A 1 41  ? -33.14889 36.43714 23.50989  1.000 65.81502  ? 21  ARG   A CB  1 
ATOM   119  C CG  . ARG   A 1 41  ? -33.74094 37.55247 24.34649  1.000 78.45372  ? 21  ARG   A CG  1 
ATOM   120  C CD  . ARG   A 1 41  ? -34.25710 36.99436 25.66324  1.000 89.16475  ? 21  ARG   A CD  1 
ATOM   121  N NE  . ARG   A 1 41  ? -33.19068 36.70674 26.61587  1.000 85.41737  ? 21  ARG   A NE  1 
ATOM   122  C CZ  . ARG   A 1 41  ? -33.21749 35.71087 27.49267  1.000 90.07422  ? 21  ARG   A CZ  1 
ATOM   123  N NH1 . ARG   A 1 41  ? -34.20122 34.82453 27.50491  1.000 88.58340  ? 21  ARG   A NH1 1 
ATOM   124  N NH2 . ARG   A 1 41  ? -32.23205 35.60087 28.37940  1.000 73.70277  ? 21  ARG   A NH2 1 
ATOM   125  N N   A MET   A 1 42  ? -31.40492 38.57826 21.51635  0.550 60.21566  ? 22  MET   A N   1 
ATOM   126  N N   B MET   A 1 42  ? -31.40170 38.57698 21.52259  0.450 60.22666  ? 22  MET   A N   1 
ATOM   127  C CA  A MET   A 1 42  ? -30.09395 39.20886 21.47193  0.550 58.40160  ? 22  MET   A CA  1 
ATOM   128  C CA  B MET   A 1 42  ? -30.08525 39.19189 21.45697  0.450 58.31497  ? 22  MET   A CA  1 
ATOM   129  C C   A MET   A 1 42  ? -29.45084 39.16394 22.85230  0.550 56.18419  ? 22  MET   A C   1 
ATOM   130  C C   B MET   A 1 42  ? -29.44405 39.19339 22.83954  0.450 56.26819  ? 22  MET   A C   1 
ATOM   131  O O   A MET   A 1 42  ? -30.11694 39.36380 23.87149  0.550 59.50414  ? 22  MET   A O   1 
ATOM   132  O O   B MET   A 1 42  ? -30.10613 39.45132 23.84809  0.450 59.52976  ? 22  MET   A O   1 
ATOM   133  C CB  A MET   A 1 42  ? -30.21582 40.65739 20.99171  0.550 54.63322  ? 22  MET   A CB  1 
ATOM   134  C CB  B MET   A 1 42  ? -30.19055 40.61585 20.91177  0.450 54.67101  ? 22  MET   A CB  1 
ATOM   135  C CG  A MET   A 1 42  ? -30.48703 40.80996 19.50016  0.550 56.35156  ? 22  MET   A CG  1 
ATOM   136  C CG  B MET   A 1 42  ? -30.34917 40.68505 19.39952  0.450 56.44828  ? 22  MET   A CG  1 
ATOM   137  S SD  A MET   A 1 42  ? -30.70221 42.53264 19.00424  0.550 60.90646  ? 22  MET   A SD  1 
ATOM   138  S SD  B MET   A 1 42  ? -30.72645 42.33991 18.79079  0.450 60.97601  ? 22  MET   A SD  1 
ATOM   139  C CE  A MET   A 1 42  ? -30.28413 42.44852 17.26294  0.550 58.05963  ? 22  MET   A CE  1 
ATOM   140  C CE  B MET   A 1 42  ? -32.40662 42.54859 19.37832  0.450 54.41603  ? 22  MET   A CE  1 
ATOM   141  N N   . ARG   A 1 43  ? -28.14879 38.88871 22.88717  1.000 49.49209  ? 23  ARG   A N   1 
ATOM   142  C CA  . ARG   A 1 43  ? -27.41917 38.82920 24.14605  1.000 61.82354  ? 23  ARG   A CA  1 
ATOM   143  C C   . ARG   A 1 43  ? -26.07633 39.52886 24.00330  1.000 58.54585  ? 23  ARG   A C   1 
ATOM   144  O O   . ARG   A 1 43  ? -25.53979 39.66085 22.89937  1.000 58.05285  ? 23  ARG   A O   1 
ATOM   145  C CB  . ARG   A 1 43  ? -27.21407 37.38290 24.61909  1.000 61.90444  ? 23  ARG   A CB  1 
ATOM   146  C CG  . ARG   A 1 43  ? -28.50764 36.67405 24.98632  1.000 63.85897  ? 23  ARG   A CG  1 
ATOM   147  C CD  . ARG   A 1 43  ? -28.24363 35.36459 25.71400  1.000 74.84611  ? 23  ARG   A CD  1 
ATOM   148  N NE  . ARG   A 1 43  ? -29.46219 34.57325 25.83692  1.000 69.59972  ? 23  ARG   A NE  1 
ATOM   149  C CZ  . ARG   A 1 43  ? -29.90917 33.74207 24.90501  1.000 80.96102  ? 23  ARG   A CZ  1 
ATOM   150  N NH1 . ARG   A 1 43  ? -29.23020 33.52638 23.78915  1.000 76.64425  ? 23  ARG   A NH1 1 
ATOM   151  N NH2 . ARG   A 1 43  ? -31.06349 33.10757 25.09982  1.000 82.24965  ? 23  ARG   A NH2 1 
ATOM   152  N N   . ALA   A 1 44  ? -25.55009 39.99370 25.14228  1.000 59.47158  ? 24  ALA   A N   1 
ATOM   153  C CA  . ALA   A 1 44  ? -24.26730 40.69096 25.14521  1.000 62.71088  ? 24  ALA   A CA  1 
ATOM   154  C C   . ALA   A 1 44  ? -23.14082 39.76882 24.70116  1.000 62.49227  ? 24  ALA   A C   1 
ATOM   155  O O   . ALA   A 1 44  ? -22.18510 40.21051 24.05201  1.000 69.52987  ? 24  ALA   A O   1 
ATOM   156  C CB  . ALA   A 1 44  ? -23.98270 41.26508 26.53401  1.000 51.95277  ? 24  ALA   A CB  1 
ATOM   157  N N   . ASP   A 1 45  ? -23.23472 38.48367 25.04421  1.000 74.67146  ? 25  ASP   A N   1 
ATOM   158  C CA  . ASP   A 1 45  ? -22.31434 37.47153 24.53156  1.000 62.54960  ? 25  ASP   A CA  1 
ATOM   159  C C   . ASP   A 1 45  ? -22.90543 36.95193 23.22395  1.000 53.02334  ? 25  ASP   A C   1 
ATOM   160  O O   . ASP   A 1 45  ? -23.55315 35.90459 23.16185  1.000 65.54675  ? 25  ASP   A O   1 
ATOM   161  C CB  . ASP   A 1 45  ? -22.10257 36.36872 25.56166  1.000 77.17818  ? 25  ASP   A CB  1 
ATOM   162  C CG  . ASP   A 1 45  ? -20.83058 35.57540 25.31838  1.000 90.76489  ? 25  ASP   A CG  1 
ATOM   163  O OD1 . ASP   A 1 45  ? -20.92967 34.38579 24.94654  1.000 89.07897  ? 25  ASP   A OD1 1 
ATOM   164  O OD2 . ASP   A 1 45  ? -19.72938 36.14574 25.48862  1.000 83.91665  ? 25  ASP   A OD2 1 
ATOM   165  N N   . ARG   A 1 46  ? -22.68594 37.72718 22.16199  1.000 53.66326  ? 26  ARG   A N   1 
ATOM   166  C CA  . ARG   A 1 46  ? -23.30321 37.44656 20.87514  1.000 63.96777  ? 26  ARG   A CA  1 
ATOM   167  C C   . ARG   A 1 46  ? -22.85336 36.08326 20.35102  1.000 51.32622  ? 26  ARG   A C   1 
ATOM   168  O O   . ARG   A 1 46  ? -21.76611 35.60589 20.69182  1.000 55.30114  ? 26  ARG   A O   1 
ATOM   169  C CB  . ARG   A 1 46  ? -22.94066 38.53281 19.86096  1.000 50.71101  ? 26  ARG   A CB  1 
ATOM   170  C CG  . ARG   A 1 46  ? -23.20242 39.95510 20.32861  1.000 58.31456  ? 26  ARG   A CG  1 
ATOM   171  C CD  . ARG   A 1 46  ? -22.40759 40.95845 19.50041  1.000 66.26373  ? 26  ARG   A CD  1 
ATOM   172  N NE  . ARG   A 1 46  ? -22.91081 41.09074 18.13838  1.000 59.51292  ? 26  ARG   A NE  1 
ATOM   173  C CZ  . ARG   A 1 46  ? -23.59916 42.13320 17.69413  1.000 65.12729  ? 26  ARG   A CZ  1 
ATOM   174  N NH1 . ARG   A 1 46  ? -23.88710 43.15714 18.48108  1.000 67.18984  ? 26  ARG   A NH1 1 
ATOM   175  N NH2 . ARG   A 1 46  ? -24.00654 42.15029 16.42798  1.000 64.76670  ? 26  ARG   A NH2 1 
ATOM   176  N N   . PRO   A 1 47  ? -23.68262 35.42492 19.54170  1.000 52.24074  ? 27  PRO   A N   1 
ATOM   177  C CA  . PRO   A 1 47  ? -23.21614 34.23686 18.81842  1.000 56.35638  ? 27  PRO   A CA  1 
ATOM   178  C C   . PRO   A 1 47  ? -21.96845 34.56601 18.01095  1.000 50.96374  ? 27  PRO   A C   1 
ATOM   179  O O   . PRO   A 1 47  ? -21.87044 35.63085 17.39665  1.000 53.65371  ? 27  PRO   A O   1 
ATOM   180  C CB  . PRO   A 1 47  ? -24.40278 33.88312 17.91567  1.000 52.40500  ? 27  PRO   A CB  1 
ATOM   181  C CG  . PRO   A 1 47  ? -25.59460 34.45940 18.61243  1.000 49.63020  ? 27  PRO   A CG  1 
ATOM   182  C CD  . PRO   A 1 47  ? -25.11057 35.70267 19.30469  1.000 51.53433  ? 27  PRO   A CD  1 
ATOM   183  N N   . LYS   A 1 48  ? -21.00430 33.63979 18.02346  1.000 48.57772  ? 28  LYS   A N   1 
ATOM   184  C CA  . LYS   A 1 48  ? -19.69181 33.92151 17.44500  1.000 54.00780  ? 28  LYS   A CA  1 
ATOM   185  C C   . LYS   A 1 48  ? -19.78214 34.32646 15.97921  1.000 53.91912  ? 28  LYS   A C   1 
ATOM   186  O O   . LYS   A 1 48  ? -18.93781 35.08815 15.49543  1.000 47.22043  ? 28  LYS   A O   1 
ATOM   187  C CB  . LYS   A 1 48  ? -18.77158 32.70868 17.59722  1.000 52.15173  ? 28  LYS   A CB  1 
ATOM   188  C CG  . LYS   A 1 48  ? -17.94997 32.70329 18.87703  1.000 55.13386  ? 28  LYS   A CG  1 
ATOM   189  C CD  . LYS   A 1 48  ? -18.80160 32.38799 20.09716  1.000 68.08826  ? 28  LYS   A CD  1 
ATOM   190  C CE  . LYS   A 1 48  ? -18.02805 32.67857 21.37495  1.000 65.93897  ? 28  LYS   A CE  1 
ATOM   191  N N   . GLN   A 1 49  ? -20.79209 33.83643 15.25927  1.000 51.06491  ? 29  GLN   A N   1 
ATOM   192  C CA  . GLN   A 1 49  ? -20.94745 34.18228 13.85326  1.000 54.32325  ? 29  GLN   A CA  1 
ATOM   193  C C   . GLN   A 1 49  ? -21.35498 35.63536 13.64282  1.000 44.04189  ? 29  GLN   A C   1 
ATOM   194  O O   . GLN   A 1 49  ? -21.26683 36.12616 12.51208  1.000 45.31708  ? 29  GLN   A O   1 
ATOM   195  C CB  . GLN   A 1 49  ? -21.97374 33.25388 13.20292  1.000 44.59677  ? 29  GLN   A CB  1 
ATOM   196  C CG  . GLN   A 1 49  ? -23.38726 33.43250 13.73004  1.000 53.48754  ? 29  GLN   A CG  1 
ATOM   197  C CD  . GLN   A 1 49  ? -24.27663 32.23865 13.43562  1.000 46.60919  ? 29  GLN   A CD  1 
ATOM   198  O OE1 . GLN   A 1 49  ? -25.32232 32.36967 12.79902  1.000 44.94777  ? 29  GLN   A OE1 1 
ATOM   199  N NE2 . GLN   A 1 49  ? -23.86810 31.06676 13.90760  1.000 49.63234  ? 29  GLN   A NE2 1 
ATOM   200  N N   . TYR   A 1 50  ? -21.78918 36.33290 14.69195  1.000 49.06279  ? 30  TYR   A N   1 
ATOM   201  C CA  . TYR   A 1 50  ? -22.22890 37.71718 14.58038  1.000 50.56887  ? 30  TYR   A CA  1 
ATOM   202  C C   . TYR   A 1 50  ? -21.26899 38.69442 15.24490  1.000 46.97591  ? 30  TYR   A C   1 
ATOM   203  O O   . TYR   A 1 50  ? -21.61011 39.86996 15.40703  1.000 50.24639  ? 30  TYR   A O   1 
ATOM   204  C CB  . TYR   A 1 50  ? -23.63704 37.86804 15.16104  1.000 48.20224  ? 30  TYR   A CB  1 
ATOM   205  C CG  . TYR   A 1 50  ? -24.67475 37.10557 14.37116  1.000 43.73800  ? 30  TYR   A CG  1 
ATOM   206  C CD1 . TYR   A 1 50  ? -24.78387 37.27224 12.99660  1.000 46.56539  ? 30  TYR   A CD1 1 
ATOM   207  C CD2 . TYR   A 1 50  ? -25.52212 36.19645 14.99069  1.000 43.75178  ? 30  TYR   A CD2 1 
ATOM   208  C CE1 . TYR   A 1 50  ? -25.72073 36.57023 12.26243  1.000 48.88440  ? 30  TYR   A CE1 1 
ATOM   209  C CE2 . TYR   A 1 50  ? -26.46304 35.48871 14.26391  1.000 50.20457  ? 30  TYR   A CE2 1 
ATOM   210  C CZ  . TYR   A 1 50  ? -26.55641 35.67998 12.89993  1.000 42.88821  ? 30  TYR   A CZ  1 
ATOM   211  O OH  . TYR   A 1 50  ? -27.48817 34.98089 12.16766  1.000 43.56028  ? 30  TYR   A OH  1 
ATOM   212  N N   . LEU   A 1 51  ? -20.07947 38.24210 15.62691  1.000 53.24168  ? 31  LEU   A N   1 
ATOM   213  C CA  . LEU   A 1 51  ? -19.07378 39.13948 16.16816  1.000 50.96104  ? 31  LEU   A CA  1 
ATOM   214  C C   . LEU   A 1 51  ? -18.43644 39.95823 15.04991  1.000 49.92163  ? 31  LEU   A C   1 
ATOM   215  O O   . LEU   A 1 51  ? -18.46247 39.58255 13.87441  1.000 43.87765  ? 31  LEU   A O   1 
ATOM   216  C CB  . LEU   A 1 51  ? -18.00358 38.35498 16.92480  1.000 48.83073  ? 31  LEU   A CB  1 
ATOM   217  C CG  . LEU   A 1 51  ? -18.47675 37.69590 18.21993  1.000 50.16699  ? 31  LEU   A CG  1 
ATOM   218  C CD1 . LEU   A 1 51  ? -17.40031 36.78455 18.78346  1.000 56.15244  ? 31  LEU   A CD1 1 
ATOM   219  C CD2 . LEU   A 1 51  ? -18.87025 38.75622 19.23662  1.000 53.84126  ? 31  LEU   A CD2 1 
ATOM   220  N N   . ASP   A 1 52  ? -17.85865 41.09422 15.43105  1.000 49.59867  ? 32  ASP   A N   1 
ATOM   221  C CA  . ASP   A 1 52  ? -17.25736 42.00632 14.46883  1.000 53.19629  ? 32  ASP   A CA  1 
ATOM   222  C C   . ASP   A 1 52  ? -15.82651 41.58546 14.16722  1.000 53.90219  ? 32  ASP   A C   1 
ATOM   223  O O   . ASP   A 1 52  ? -15.03669 41.33652 15.08399  1.000 58.96824  ? 32  ASP   A O   1 
ATOM   224  C CB  . ASP   A 1 52  ? -17.27576 43.44506 14.98294  1.000 56.16552  ? 32  ASP   A CB  1 
ATOM   225  C CG  . ASP   A 1 52  ? -16.69000 44.42053 13.98069  1.000 64.11080  ? 32  ASP   A CG  1 
ATOM   226  O OD1 . ASP   A 1 52  ? -17.32923 44.64352 12.93036  1.000 68.81466  ? 32  ASP   A OD1 1 
ATOM   227  O OD2 . ASP   A 1 52  ? -15.58765 44.95249 14.23339  1.000 72.59848  ? 32  ASP   A OD2 1 
ATOM   228  N N   . LEU   A 1 53  ? -15.49620 41.52248 12.87848  1.000 50.36923  ? 33  LEU   A N   1 
ATOM   229  C CA  . LEU   A 1 53  ? -14.15840 41.16871 12.40918  1.000 54.44392  ? 33  LEU   A CA  1 
ATOM   230  C C   . LEU   A 1 53  ? -13.73636 42.23102 11.39758  1.000 58.83474  ? 33  LEU   A C   1 
ATOM   231  O O   . LEU   A 1 53  ? -13.97818 42.08310 10.19609  1.000 56.70783  ? 33  LEU   A O   1 
ATOM   232  C CB  . LEU   A 1 53  ? -14.14344 39.76555 11.81295  1.000 55.40559  ? 33  LEU   A CB  1 
ATOM   233  C CG  . LEU   A 1 53  ? -12.79601 39.20303 11.36247  1.000 65.55894  ? 33  LEU   A CG  1 
ATOM   234  C CD1 . LEU   A 1 53  ? -11.70665 39.54361 12.36488  1.000 66.29698  ? 33  LEU   A CD1 1 
ATOM   235  C CD2 . LEU   A 1 53  ? -12.90068 37.69769 11.18582  1.000 67.80213  ? 33  LEU   A CD2 1 
ATOM   236  N N   . ALA   A 1 54  ? -13.11659 43.30328 11.89970  1.000 63.98299  ? 34  ALA   A N   1 
ATOM   237  C CA  . ALA   A 1 54  ? -12.61056 44.40224 11.07347  1.000 58.24855  ? 34  ALA   A CA  1 
ATOM   238  C C   . ALA   A 1 54  ? -13.73156 45.06056 10.26868  1.000 57.71824  ? 34  ALA   A C   1 
ATOM   239  O O   . ALA   A 1 54  ? -13.64424 45.22195 9.04945   1.000 66.55062  ? 34  ALA   A O   1 
ATOM   240  C CB  . ALA   A 1 54  ? -11.48074 43.92872 10.15517  1.000 60.09203  ? 34  ALA   A CB  1 
ATOM   241  N N   . GLY   A 1 55  ? -14.79860 45.44243 10.96553  1.000 57.17686  ? 35  GLY   A N   1 
ATOM   242  C CA  . GLY   A 1 55  ? -15.87783 46.18643 10.35342  1.000 52.88740  ? 35  GLY   A CA  1 
ATOM   243  C C   . GLY   A 1 55  ? -16.98795 45.36042 9.74029   1.000 65.20476  ? 35  GLY   A C   1 
ATOM   244  O O   . GLY   A 1 55  ? -17.90324 45.93769 9.13971   1.000 63.71443  ? 35  GLY   A O   1 
ATOM   245  N N   . ARG   A 1 56  ? -16.94265 44.03569 9.86218   1.000 58.03055  ? 36  ARG   A N   1 
ATOM   246  C CA  . ARG   A 1 56  ? -18.00432 43.18770 9.33822   1.000 63.50838  ? 36  ARG   A CA  1 
ATOM   247  C C   . ARG   A 1 56  ? -18.13715 41.95280 10.21444  1.000 50.18725  ? 36  ARG   A C   1 
ATOM   248  O O   . ARG   A 1 56  ? -17.19777 41.55583 10.90807  1.000 54.82427  ? 36  ARG   A O   1 
ATOM   249  C CB  . ARG   A 1 56  ? -17.74863 42.78043 7.88215   1.000 58.63711  ? 36  ARG   A CB  1 
ATOM   250  C CG  . ARG   A 1 56  ? -18.32293 43.74573 6.86074   1.000 70.96998  ? 36  ARG   A CG  1 
ATOM   251  C CD  . ARG   A 1 56  ? -18.50373 43.07542 5.51099   1.000 63.45772  ? 36  ARG   A CD  1 
ATOM   252  N NE  . ARG   A 1 56  ? -17.23276 42.79899 4.85341   1.000 73.66427  ? 36  ARG   A NE  1 
ATOM   253  C CZ  . ARG   A 1 56  ? -17.11580 42.15639 3.69927   1.000 76.38705  ? 36  ARG   A CZ  1 
ATOM   254  N NH1 . ARG   A 1 56  ? -18.17495 41.69071 3.05766   1.000 74.72001  ? 36  ARG   A NH1 1 
ATOM   255  N NH2 . ARG   A 1 56  ? -15.90639 41.97673 3.17524   1.000 72.55798  ? 36  ARG   A NH2 1 
ATOM   256  N N   . THR   A 1 57  ? -19.32080 41.34779 10.17219  1.000 47.12365  ? 37  THR   A N   1 
ATOM   257  C CA  . THR   A 1 57  ? -19.57538 40.16860 10.98003  1.000 55.51106  ? 37  THR   A CA  1 
ATOM   258  C C   . THR   A 1 57  ? -18.81797 38.96489 10.42598  1.000 46.58982  ? 37  THR   A C   1 
ATOM   259  O O   . THR   A 1 57  ? -18.44292 38.91281 9.24949   1.000 41.13871  ? 37  THR   A O   1 
ATOM   260  C CB  . THR   A 1 57  ? -21.07139 39.86391 11.04138  1.000 49.88865  ? 37  THR   A CB  1 
ATOM   261  O OG1 . THR   A 1 57  ? -21.51216 39.35709 9.77597   1.000 47.03159  ? 37  THR   A OG1 1 
ATOM   262  C CG2 . THR   A 1 57  ? -21.85201 41.12215 11.38430  1.000 53.94704  ? 37  THR   A CG2 1 
ATOM   263  N N   . VAL   A 1 58  ? -18.59209 37.98766 11.30676  1.000 45.93178  ? 38  VAL   A N   1 
ATOM   264  C CA  . VAL   A 1 58  ? -17.84431 36.79168 10.92850  1.000 50.60044  ? 38  VAL   A CA  1 
ATOM   265  C C   . VAL   A 1 58  ? -18.53192 36.06800 9.77800   1.000 40.28247  ? 38  VAL   A C   1 
ATOM   266  O O   . VAL   A 1 58  ? -17.88247 35.64990 8.81037   1.000 46.24404  ? 38  VAL   A O   1 
ATOM   267  C CB  . VAL   A 1 58  ? -17.66374 35.87153 12.15027  1.000 47.95308  ? 38  VAL   A CB  1 
ATOM   268  C CG1 . VAL   A 1 58  ? -17.05815 34.53747 11.73314  1.000 48.43877  ? 38  VAL   A CG1 1 
ATOM   269  C CG2 . VAL   A 1 58  ? -16.80804 36.55825 13.20136  1.000 39.10957  ? 38  VAL   A CG2 1 
ATOM   270  N N   . ILE   A 1 59  ? -19.85610 35.91649 9.85654   1.000 37.81182  ? 39  ILE   A N   1 
ATOM   271  C CA  . ILE   A 1 59  ? -20.55809 35.13125 8.84714   1.000 47.19538  ? 39  ILE   A CA  1 
ATOM   272  C C   . ILE   A 1 59  ? -20.56081 35.84806 7.50360   1.000 48.07094  ? 39  ILE   A C   1 
ATOM   273  O O   . ILE   A 1 59  ? -20.54802 35.19963 6.44902   1.000 44.69877  ? 39  ILE   A O   1 
ATOM   274  C CB  . ILE   A 1 59  ? -21.98573 34.79022 9.31702   1.000 46.40705  ? 39  ILE   A CB  1 
ATOM   275  C CG1 . ILE   A 1 59  ? -22.66022 33.84691 8.31586   1.000 50.18847  ? 39  ILE   A CG1 1 
ATOM   276  C CG2 . ILE   A 1 59  ? -22.81203 36.05385 9.52137   1.000 37.38302  ? 39  ILE   A CG2 1 
ATOM   277  C CD1 . ILE   A 1 59  ? -23.82507 33.06782 8.88939   1.000 40.19301  ? 39  ILE   A CD1 1 
ATOM   278  N N   . GLU   A 1 60  ? -20.56380 37.18374 7.50573   1.000 50.99586  ? 40  GLU   A N   1 
ATOM   279  C CA  . GLU   A 1 60  ? -20.46195 37.90669 6.24240   1.000 46.67163  ? 40  GLU   A CA  1 
ATOM   280  C C   . GLU   A 1 60  ? -19.12549 37.63524 5.56595   1.000 42.93327  ? 40  GLU   A C   1 
ATOM   281  O O   . GLU   A 1 60  ? -19.07562 37.39154 4.35479   1.000 50.23783  ? 40  GLU   A O   1 
ATOM   282  C CB  . GLU   A 1 60  ? -20.65937 39.40667 6.46484   1.000 53.47719  ? 40  GLU   A CB  1 
ATOM   283  C CG  . GLU   A 1 60  ? -22.10058 39.80734 6.74267   1.000 58.85086  ? 40  GLU   A CG  1 
ATOM   284  C CD  . GLU   A 1 60  ? -22.23907 41.27136 7.11558   1.000 71.48319  ? 40  GLU   A CD  1 
ATOM   285  O OE1 . GLU   A 1 60  ? -22.93026 42.01264 6.38318   1.000 64.78422  ? 40  GLU   A OE1 1 
ATOM   286  O OE2 . GLU   A 1 60  ? -21.65008 41.68146 8.13876   1.000 73.62637  ? 40  GLU   A OE2 1 
ATOM   287  N N   . ARG   A 1 61  ? -18.03273 37.65502 6.33343   1.000 44.58555  ? 41  ARG   A N   1 
ATOM   288  C CA  . ARG   A 1 61  ? -16.73245 37.33140 5.75787   1.000 48.56204  ? 41  ARG   A CA  1 
ATOM   289  C C   . ARG   A 1 61  ? -16.65093 35.86726 5.34620   1.000 52.59033  ? 41  ARG   A C   1 
ATOM   290  O O   . ARG   A 1 61  ? -15.92640 35.53198 4.40263   1.000 52.16725  ? 41  ARG   A O   1 
ATOM   291  C CB  . ARG   A 1 61  ? -15.61515 37.67520 6.74316   1.000 45.30310  ? 41  ARG   A CB  1 
ATOM   292  C CG  . ARG   A 1 61  ? -15.51737 39.15704 7.07323   1.000 52.76129  ? 41  ARG   A CG  1 
ATOM   293  C CD  . ARG   A 1 61  ? -14.17119 39.50060 7.68757   1.000 58.63535  ? 41  ARG   A CD  1 
ATOM   294  N NE  . ARG   A 1 61  ? -14.02154 40.93289 7.91525   1.000 69.32465  ? 41  ARG   A NE  1 
ATOM   295  C CZ  . ARG   A 1 61  ? -13.69613 41.80987 6.97513   1.000 63.90359  ? 41  ARG   A CZ  1 
ATOM   296  N NH1 . ARG   A 1 61  ? -13.49905 41.43760 5.72111   1.000 57.70129  ? 41  ARG   A NH1 1 
ATOM   297  N NH2 . ARG   A 1 61  ? -13.56770 43.09275 7.30083   1.000 57.08374  ? 41  ARG   A NH2 1 
ATOM   298  N N   . THR   A 1 62  ? -17.38166 34.98490 6.03283   1.000 46.10604  ? 42  THR   A N   1 
ATOM   299  C CA  . THR   A 1 62  ? -17.40491 33.58315 5.62928   1.000 53.22111  ? 42  THR   A CA  1 
ATOM   300  C C   . THR   A 1 62  ? -18.10156 33.41413 4.28462   1.000 45.19824  ? 42  THR   A C   1 
ATOM   301  O O   . THR   A 1 62  ? -17.63639 32.65159 3.42955   1.000 45.87276  ? 42  THR   A O   1 
ATOM   302  C CB  . THR   A 1 62  ? -18.08877 32.73501 6.70351   1.000 41.67479  ? 42  THR   A CB  1 
ATOM   303  O OG1 . THR   A 1 62  ? -17.38369 32.87158 7.94412   1.000 46.48254  ? 42  THR   A OG1 1 
ATOM   304  C CG2 . THR   A 1 62  ? -18.10389 31.26961 6.29609   1.000 42.75220  ? 42  THR   A CG2 1 
ATOM   305  N N   . LEU   A 1 63  ? -19.20922 34.13067 4.07314   1.000 45.16896  ? 43  LEU   A N   1 
ATOM   306  C CA  . LEU   A 1 63  ? -19.91839 34.03800 2.80112   1.000 56.97407  ? 43  LEU   A CA  1 
ATOM   307  C C   . LEU   A 1 63  ? -19.09339 34.59422 1.64578   1.000 52.22493  ? 43  LEU   A C   1 
ATOM   308  O O   . LEU   A 1 63  ? -19.23731 34.12737 0.50942   1.000 50.12057  ? 43  LEU   A O   1 
ATOM   309  C CB  . LEU   A 1 63  ? -21.26044 34.76625 2.88785   1.000 49.50078  ? 43  LEU   A CB  1 
ATOM   310  C CG  . LEU   A 1 63  ? -22.27369 34.23007 3.90306   1.000 55.91773  ? 43  LEU   A CG  1 
ATOM   311  C CD1 . LEU   A 1 63  ? -23.57881 35.00706 3.82475   1.000 55.17765  ? 43  LEU   A CD1 1 
ATOM   312  C CD2 . LEU   A 1 63  ? -22.51926 32.74485 3.70059   1.000 59.05134  ? 43  LEU   A CD2 1 
ATOM   313  N N   . ASP   A 1 64  ? -18.22497 35.57841 1.90791   1.000 54.31033  ? 44  ASP   A N   1 
ATOM   314  C CA  . ASP   A 1 64  ? -17.43395 36.16035 0.82642   1.000 58.01801  ? 44  ASP   A CA  1 
ATOM   315  C C   . ASP   A 1 64  ? -16.47119 35.14760 0.22440   1.000 55.94796  ? 44  ASP   A C   1 
ATOM   316  O O   . ASP   A 1 64  ? -16.08269 35.28084 -0.94118  1.000 65.71230  ? 44  ASP   A O   1 
ATOM   317  C CB  . ASP   A 1 64  ? -16.65895 37.38433 1.31621   1.000 65.46968  ? 44  ASP   A CB  1 
ATOM   318  C CG  . ASP   A 1 64  ? -17.56255 38.47161 1.85713   1.000 75.28974  ? 44  ASP   A CG  1 
ATOM   319  O OD1 . ASP   A 1 64  ? -17.10917 39.23072 2.73921   1.000 68.29866  ? 44  ASP   A OD1 1 
ATOM   320  O OD2 . ASP   A 1 64  ? -18.72800 38.56152 1.41309   1.000 80.34976  ? 44  ASP   A OD2 1 
ATOM   321  N N   . CYS   A 1 65  ? -16.07863 34.12935 0.99296   1.000 60.33862  ? 45  CYS   A N   1 
ATOM   322  C CA  . CYS   A 1 65  ? -15.17694 33.11304 0.46517   1.000 59.91009  ? 45  CYS   A CA  1 
ATOM   323  C C   . CYS   A 1 65  ? -15.82911 32.27207 -0.62584  1.000 48.64107  ? 45  CYS   A C   1 
ATOM   324  O O   . CYS   A 1 65  ? -15.11638 31.63633 -1.40947  1.000 61.26374  ? 45  CYS   A O   1 
ATOM   325  C CB  . CYS   A 1 65  ? -14.68500 32.20473 1.59598   1.000 59.64598  ? 45  CYS   A CB  1 
ATOM   326  S SG  . CYS   A 1 65  ? -14.08434 33.08069 3.06739   1.000 60.71203  ? 45  CYS   A SG  1 
ATOM   327  N N   . PHE   A 1 66  ? -17.15858 32.25891 -0.69984  1.000 43.88777  ? 46  PHE   A N   1 
ATOM   328  C CA  . PHE   A 1 66  ? -17.88939 31.42109 -1.64434  1.000 51.21601  ? 46  PHE   A CA  1 
ATOM   329  C C   . PHE   A 1 66  ? -18.66255 32.20142 -2.69443  1.000 58.54969  ? 46  PHE   A C   1 
ATOM   330  O O   . PHE   A 1 66  ? -18.73376 31.76363 -3.84599  1.000 53.65980  ? 46  PHE   A O   1 
ATOM   331  C CB  . PHE   A 1 66  ? -18.87659 30.51663 -0.89781  1.000 55.45954  ? 46  PHE   A CB  1 
ATOM   332  C CG  . PHE   A 1 66  ? -18.23421 29.59440 0.09338   1.000 53.07107  ? 46  PHE   A CG  1 
ATOM   333  C CD1 . PHE   A 1 66  ? -17.75115 28.35697 -0.30375  1.000 57.85047  ? 46  PHE   A CD1 1 
ATOM   334  C CD2 . PHE   A 1 66  ? -18.13042 29.95430 1.42589   1.000 49.75491  ? 46  PHE   A CD2 1 
ATOM   335  C CE1 . PHE   A 1 66  ? -17.16585 27.49906 0.60773   1.000 50.82314  ? 46  PHE   A CE1 1 
ATOM   336  C CE2 . PHE   A 1 66  ? -17.54654 29.10118 2.34331   1.000 61.17786  ? 46  PHE   A CE2 1 
ATOM   337  C CZ  . PHE   A 1 66  ? -17.06416 27.87036 1.93317   1.000 45.39907  ? 46  PHE   A CZ  1 
ATOM   338  N N   . LEU   A 1 67  ? -19.24593 33.34671 -2.32401  1.000 55.78298  ? 47  LEU   A N   1 
ATOM   339  C CA  . LEU   A 1 67  ? -20.23915 33.99645 -3.17719  1.000 58.26918  ? 47  LEU   A CA  1 
ATOM   340  C C   . LEU   A 1 67  ? -19.66824 34.41542 -4.52674  1.000 60.81803  ? 47  LEU   A C   1 
ATOM   341  O O   . LEU   A 1 67  ? -20.40704 34.48021 -5.51677  1.000 52.32185  ? 47  LEU   A O   1 
ATOM   342  C CB  . LEU   A 1 67  ? -20.83231 35.20679 -2.45680  1.000 61.04480  ? 47  LEU   A CB  1 
ATOM   343  C CG  . LEU   A 1 67  ? -21.84466 34.87844 -1.36004  1.000 56.90239  ? 47  LEU   A CG  1 
ATOM   344  C CD1 . LEU   A 1 67  ? -22.36807 36.14633 -0.70552  1.000 53.00253  ? 47  LEU   A CD1 1 
ATOM   345  C CD2 . LEU   A 1 67  ? -22.98777 34.05583 -1.93414  1.000 52.16918  ? 47  LEU   A CD2 1 
ATOM   346  N N   . GLU   A 1 68  ? -18.36851 34.68633 -4.59538  1.000 63.68895  ? 48  GLU   A N   1 
ATOM   347  C CA  . GLU   A 1 68  ? -17.74360 35.17854 -5.81563  1.000 65.20919  ? 48  GLU   A CA  1 
ATOM   348  C C   . GLU   A 1 68  ? -17.20351 34.06815 -6.71187  1.000 69.42717  ? 48  GLU   A C   1 
ATOM   349  O O   . GLU   A 1 68  ? -16.62480 34.37007 -7.76123  1.000 57.53828  ? 48  GLU   A O   1 
ATOM   350  C CB  . GLU   A 1 68  ? -16.60595 36.14467 -5.46475  1.000 75.61470  ? 48  GLU   A CB  1 
ATOM   351  C CG  . GLU   A 1 68  ? -16.83804 36.94978 -4.18943  1.000 93.16795  ? 48  GLU   A CG  1 
ATOM   352  C CD  . GLU   A 1 68  ? -17.95540 37.96919 -4.32232  1.000 106.82135 ? 48  GLU   A CD  1 
ATOM   353  O OE1 . GLU   A 1 68  ? -18.29614 38.34222 -5.46587  1.000 108.42438 ? 48  GLU   A OE1 1 
ATOM   354  O OE2 . GLU   A 1 68  ? -18.49219 38.39799 -3.27813  1.000 100.15481 ? 48  GLU   A OE2 1 
ATOM   355  N N   . HIS   A 1 69  ? -17.37418 32.80306 -6.33948  1.000 51.63363  ? 49  HIS   A N   1 
ATOM   356  C CA  . HIS   A 1 69  ? -16.75090 31.72974 -7.10916  1.000 57.66088  ? 49  HIS   A CA  1 
ATOM   357  C C   . HIS   A 1 69  ? -17.56918 31.43655 -8.36261  1.000 57.64308  ? 49  HIS   A C   1 
ATOM   358  O O   . HIS   A 1 69  ? -18.79065 31.27233 -8.27399  1.000 53.20191  ? 49  HIS   A O   1 
ATOM   359  C CB  . HIS   A 1 69  ? -16.61216 30.46450 -6.26852  1.000 55.75860  ? 49  HIS   A CB  1 
ATOM   360  C CG  . HIS   A 1 69  ? -15.56208 29.52335 -6.77132  1.000 55.54646  ? 49  HIS   A CG  1 
ATOM   361  N ND1 . HIS   A 1 69  ? -15.73779 28.74115 -7.89289  1.000 48.47066  ? 49  HIS   A ND1 1 
ATOM   362  C CD2 . HIS   A 1 69  ? -14.31768 29.24907 -6.31248  1.000 54.71493  ? 49  HIS   A CD2 1 
ATOM   363  C CE1 . HIS   A 1 69  ? -14.64898 28.02242 -8.10032  1.000 54.99496  ? 49  HIS   A CE1 1 
ATOM   364  N NE2 . HIS   A 1 69  ? -13.77226 28.31155 -7.15530  1.000 55.16491  ? 49  HIS   A NE2 1 
ATOM   365  N N   . PRO   A 1 70  ? -16.93631 31.35723 -9.53728  1.000 60.07122  ? 50  PRO   A N   1 
ATOM   366  C CA  . PRO   A 1 70  ? -17.71270 31.14546 -10.77028 1.000 63.42425  ? 50  PRO   A CA  1 
ATOM   367  C C   . PRO   A 1 70  ? -18.42006 29.80196 -10.82665 1.000 60.56406  ? 50  PRO   A C   1 
ATOM   368  O O   . PRO   A 1 70  ? -19.45101 29.69085 -11.50170 1.000 60.23429  ? 50  PRO   A O   1 
ATOM   369  C CB  . PRO   A 1 70  ? -16.65581 31.27649 -11.87762 1.000 60.13027  ? 50  PRO   A CB  1 
ATOM   370  C CG  . PRO   A 1 70  ? -15.34906 30.99654 -11.19990 1.000 58.26241  ? 50  PRO   A CG  1 
ATOM   371  C CD  . PRO   A 1 70  ? -15.49562 31.51637 -9.80132  1.000 49.43542  ? 50  PRO   A CD  1 
ATOM   372  N N   . MET   A 1 71  ? -17.91303 28.78114 -10.13905 1.000 54.52759  ? 51  MET   A N   1 
ATOM   373  C CA  . MET   A 1 71  ? -18.52607 27.46009 -10.16432 1.000 62.09622  ? 51  MET   A CA  1 
ATOM   374  C C   . MET   A 1 71  ? -19.60057 27.27982 -9.09675  1.000 63.00063  ? 51  MET   A C   1 
ATOM   375  O O   . MET   A 1 71  ? -20.07949 26.15726 -8.90195  1.000 61.61945  ? 51  MET   A O   1 
ATOM   376  C CB  . MET   A 1 71  ? -17.45508 26.37492 -10.01073 1.000 66.09436  ? 51  MET   A CB  1 
ATOM   377  C CG  . MET   A 1 71  ? -16.33658 26.44583 -11.04397 1.000 72.19315  ? 51  MET   A CG  1 
ATOM   378  S SD  . MET   A 1 71  ? -16.92213 26.65285 -12.74127 1.000 81.05226  ? 51  MET   A SD  1 
ATOM   379  C CE  . MET   A 1 71  ? -17.92055 25.17999 -12.95523 1.000 67.25845  ? 51  MET   A CE  1 
ATOM   380  N N   . LEU   A 1 72  ? -19.99448 28.35099 -8.41159  1.000 57.51168  ? 52  LEU   A N   1 
ATOM   381  C CA  . LEU   A 1 72  ? -21.01137 28.26403 -7.37008  1.000 53.38916  ? 52  LEU   A CA  1 
ATOM   382  C C   . LEU   A 1 72  ? -22.39920 28.26314 -8.00217  1.000 48.07022  ? 52  LEU   A C   1 
ATOM   383  O O   . LEU   A 1 72  ? -22.76971 29.21000 -8.70407  1.000 62.02867  ? 52  LEU   A O   1 
ATOM   384  C CB  . LEU   A 1 72  ? -20.86759 29.42402 -6.38667  1.000 52.57716  ? 52  LEU   A CB  1 
ATOM   385  C CG  . LEU   A 1 72  ? -21.90703 29.50057 -5.26509  1.000 58.58428  ? 52  LEU   A CG  1 
ATOM   386  C CD1 . LEU   A 1 72  ? -21.79375 28.30120 -4.33695  1.000 49.98594  ? 52  LEU   A CD1 1 
ATOM   387  C CD2 . LEU   A 1 72  ? -21.77001 30.80033 -4.48685  1.000 46.35341  ? 52  LEU   A CD2 1 
ATOM   388  N N   . ARG   A 1 73  ? -23.16573 27.19969 -7.75292  1.000 57.68475  ? 53  ARG   A N   1 
ATOM   389  C CA  . ARG   A 1 73  ? -24.52817 27.11985 -8.27013  1.000 54.51958  ? 53  ARG   A CA  1 
ATOM   390  C C   . ARG   A 1 73  ? -25.51681 27.81180 -7.34096  1.000 51.82168  ? 53  ARG   A C   1 
ATOM   391  O O   . ARG   A 1 73  ? -26.49531 28.40984 -7.80161  1.000 68.61368  ? 53  ARG   A O   1 
ATOM   392  C CB  . ARG   A 1 73  ? -24.92765 25.65732 -8.47287  1.000 61.47868  ? 53  ARG   A CB  1 
ATOM   393  C CG  . ARG   A 1 73  ? -24.02487 24.89621 -9.42869  1.000 74.06241  ? 53  ARG   A CG  1 
ATOM   394  C CD  . ARG   A 1 73  ? -24.60104 24.85058 -10.83615 1.000 76.80972  ? 53  ARG   A CD  1 
ATOM   395  N NE  . ARG   A 1 73  ? -25.30115 23.59691 -11.09168 1.000 89.66113  ? 53  ARG   A NE  1 
ATOM   396  C CZ  . ARG   A 1 73  ? -26.61983 23.45524 -11.08828 1.000 90.35480  ? 53  ARG   A CZ  1 
ATOM   397  N NH1 . ARG   A 1 73  ? -27.42532 24.48135 -10.86691 1.000 85.37600  ? 53  ARG   A NH1 1 
ATOM   398  N NH2 . ARG   A 1 73  ? -27.14365 22.25358 -11.31596 1.000 79.95569  ? 53  ARG   A NH2 1 
ATOM   399  N N   . GLY   A 1 74  ? -25.27773 27.73923 -6.03631  1.000 51.93314  ? 54  GLY   A N   1 
ATOM   400  C CA  . GLY   A 1 74  ? -26.14861 28.36258 -5.06222  1.000 50.46295  ? 54  GLY   A CA  1 
ATOM   401  C C   . GLY   A 1 74  ? -25.66484 28.12432 -3.64871  1.000 53.97677  ? 54  GLY   A C   1 
ATOM   402  O O   . GLY   A 1 74  ? -25.10359 27.06648 -3.34879  1.000 52.99877  ? 54  GLY   A O   1 
ATOM   403  N N   . LEU   A 1 75  ? -25.86485 29.10383 -2.77431  1.000 54.68386  ? 55  LEU   A N   1 
ATOM   404  C CA  . LEU   A 1 75  ? -25.46610 29.00837 -1.37950  1.000 53.45596  ? 55  LEU   A CA  1 
ATOM   405  C C   . LEU   A 1 75  ? -26.70576 29.09536 -0.50275  1.000 48.60905  ? 55  LEU   A C   1 
ATOM   406  O O   . LEU   A 1 75  ? -27.59579 29.91688 -0.74617  1.000 55.35244  ? 55  LEU   A O   1 
ATOM   407  C CB  . LEU   A 1 75  ? -24.46527 30.11149 -1.01039  1.000 51.97894  ? 55  LEU   A CB  1 
ATOM   408  C CG  . LEU   A 1 75  ? -23.79190 30.03312 0.36194   1.000 50.42576  ? 55  LEU   A CG  1 
ATOM   409  C CD1 . LEU   A 1 75  ? -22.37105 30.56669 0.28667   1.000 55.24001  ? 55  LEU   A CD1 1 
ATOM   410  C CD2 . LEU   A 1 75  ? -24.58884 30.81026 1.39402   1.000 45.77367  ? 55  LEU   A CD2 1 
ATOM   411  N N   . VAL   A 1 76  ? -26.75896 28.24212 0.51625   1.000 56.98877  ? 56  VAL   A N   1 
ATOM   412  C CA  . VAL   A 1 76  ? -27.89085 28.17568 1.43225   1.000 49.92713  ? 56  VAL   A CA  1 
ATOM   413  C C   . VAL   A 1 76  ? -27.36288 28.30676 2.85094   1.000 46.76743  ? 56  VAL   A C   1 
ATOM   414  O O   . VAL   A 1 76  ? -26.48269 27.54134 3.26160   1.000 48.21795  ? 56  VAL   A O   1 
ATOM   415  C CB  . VAL   A 1 76  ? -28.68720 26.86953 1.27551   1.000 54.90086  ? 56  VAL   A CB  1 
ATOM   416  C CG1 . VAL   A 1 76  ? -29.68291 26.71391 2.41310   1.000 51.37282  ? 56  VAL   A CG1 1 
ATOM   417  C CG2 . VAL   A 1 76  ? -29.40088 26.84519 -0.06551  1.000 56.57000  ? 56  VAL   A CG2 1 
ATOM   418  N N   . VAL   A 1 77  ? -27.88943 29.27563 3.59333   1.000 50.34504  ? 57  VAL   A N   1 
ATOM   419  C CA  . VAL   A 1 77  ? -27.58502 29.43431 5.00912   1.000 44.90223  ? 57  VAL   A CA  1 
ATOM   420  C C   . VAL   A 1 77  ? -28.72821 28.82734 5.80784   1.000 47.01294  ? 57  VAL   A C   1 
ATOM   421  O O   . VAL   A 1 77  ? -29.90292 29.09510 5.52585   1.000 51.96697  ? 57  VAL   A O   1 
ATOM   422  C CB  . VAL   A 1 77  ? -27.37337 30.91324 5.37815   1.000 47.03756  ? 57  VAL   A CB  1 
ATOM   423  C CG1 . VAL   A 1 77  ? -26.94288 31.04277 6.82991   1.000 36.47014  ? 57  VAL   A CG1 1 
ATOM   424  C CG2 . VAL   A 1 77  ? -26.34003 31.54426 4.46804   1.000 48.37862  ? 57  VAL   A CG2 1 
ATOM   425  N N   . CYS   A 1 78  ? -28.38883 27.99314 6.78758   1.000 41.84224  ? 58  CYS   A N   1 
ATOM   426  C CA  . CYS   A 1 78  ? -29.37346 27.39595 7.68070   1.000 43.61683  ? 58  CYS   A CA  1 
ATOM   427  C C   . CYS   A 1 78  ? -29.47197 28.25651 8.93315   1.000 44.41299  ? 58  CYS   A C   1 
ATOM   428  O O   . CYS   A 1 78  ? -28.47115 28.46352 9.62702   1.000 43.77041  ? 58  CYS   A O   1 
ATOM   429  C CB  . CYS   A 1 78  ? -28.98386 25.96168 8.03664   1.000 42.07949  ? 58  CYS   A CB  1 
ATOM   430  S SG  . CYS   A 1 78  ? -28.46236 24.96871 6.61783   1.000 52.55095  ? 58  CYS   A SG  1 
ATOM   431  N N   . LEU   A 1 79  ? -30.67182 28.75626 9.21825   1.000 43.47345  ? 59  LEU   A N   1 
ATOM   432  C CA  . LEU   A 1 79  ? -30.87348 29.72116 10.28704  1.000 53.79135  ? 59  LEU   A CA  1 
ATOM   433  C C   . LEU   A 1 79  ? -32.12890 29.37547 11.06887  1.000 49.94764  ? 59  LEU   A C   1 
ATOM   434  O O   . LEU   A 1 79  ? -33.08990 28.82448 10.52432  1.000 56.29506  ? 59  LEU   A O   1 
ATOM   435  C CB  . LEU   A 1 79  ? -31.00515 31.14946 9.74181   1.000 40.61246  ? 59  LEU   A CB  1 
ATOM   436  C CG  . LEU   A 1 79  ? -29.83823 31.73195 8.94886   1.000 49.52843  ? 59  LEU   A CG  1 
ATOM   437  C CD1 . LEU   A 1 79  ? -30.30966 32.92748 8.14095   1.000 50.95456  ? 59  LEU   A CD1 1 
ATOM   438  C CD2 . LEU   A 1 79  ? -28.70608 32.12578 9.88360   1.000 45.43750  ? 59  LEU   A CD2 1 
ATOM   439  N N   . ALA   A 1 80  ? -32.11001 29.70876 12.35493  1.000 54.62331  ? 60  ALA   A N   1 
ATOM   440  C CA  . ALA   A 1 80  ? -33.33529 29.68641 13.13601  1.000 53.20656  ? 60  ALA   A CA  1 
ATOM   441  C C   . ALA   A 1 80  ? -34.29828 30.73485 12.59522  1.000 61.27029  ? 60  ALA   A C   1 
ATOM   442  O O   . ALA   A 1 80  ? -33.88709 31.81709 12.16644  1.000 63.41603  ? 60  ALA   A O   1 
ATOM   443  C CB  . ALA   A 1 80  ? -33.03700 29.94333 14.61191  1.000 54.09325  ? 60  ALA   A CB  1 
ATOM   444  N N   . GLU   A 1 81  ? -35.58886 30.40221 12.60115  1.000 63.80309  ? 61  GLU   A N   1 
ATOM   445  C CA  . GLU   A 1 81  ? -36.59793 31.29021 12.04061  1.000 65.70368  ? 61  GLU   A CA  1 
ATOM   446  C C   . GLU   A 1 81  ? -36.79741 32.55313 12.87297  1.000 67.78436  ? 61  GLU   A C   1 
ATOM   447  O O   . GLU   A 1 81  ? -37.46738 33.48182 12.40890  1.000 72.55066  ? 61  GLU   A O   1 
ATOM   448  C CB  . GLU   A 1 81  ? -37.92054 30.53235 11.89849  1.000 73.79167  ? 61  GLU   A CB  1 
ATOM   449  C CG  . GLU   A 1 81  ? -37.80997 29.24845 11.09324  1.000 76.08895  ? 61  GLU   A CG  1 
ATOM   450  C CD  . GLU   A 1 81  ? -37.55643 29.51731 9.62122   1.000 88.65219  ? 61  GLU   A CD  1 
ATOM   451  O OE1 . GLU   A 1 81  ? -36.41812 29.91040 9.27816   1.000 85.98837  ? 61  GLU   A OE1 1 
ATOM   452  O OE2 . GLU   A 1 81  ? -38.49559 29.34650 8.81093   1.000 94.77487  ? 61  GLU   A OE2 1 
ATOM   453  N N   . ASP   A 1 82  ? -36.23701 32.61244 14.08413  1.000 64.58021  ? 62  ASP   A N   1 
ATOM   454  C CA  . ASP   A 1 82  ? -36.34574 33.77534 14.95838  1.000 70.58511  ? 62  ASP   A CA  1 
ATOM   455  C C   . ASP   A 1 82  ? -34.99925 34.45169 15.20104  1.000 71.83723  ? 62  ASP   A C   1 
ATOM   456  O O   . ASP   A 1 82  ? -34.84199 35.17191 16.19240  1.000 68.73529  ? 62  ASP   A O   1 
ATOM   457  C CB  . ASP   A 1 82  ? -36.98876 33.36597 16.28365  1.000 71.24059  ? 62  ASP   A CB  1 
ATOM   458  C CG  . ASP   A 1 82  ? -36.47007 32.03419 16.79470  1.000 79.61447  ? 62  ASP   A CG  1 
ATOM   459  O OD1 . ASP   A 1 82  ? -36.70742 31.71096 17.97752  1.000 91.62041  ? 62  ASP   A OD1 1 
ATOM   460  O OD2 . ASP   A 1 82  ? -35.81773 31.31110 16.01478  1.000 84.16819  ? 62  ASP   A OD2 1 
ATOM   461  N N   . ASP   A 1 83  ? -34.02476 34.22822 14.31435  1.000 65.39757  ? 63  ASP   A N   1 
ATOM   462  C CA  . ASP   A 1 83  ? -32.68195 34.78407 14.43920  1.000 60.22632  ? 63  ASP   A CA  1 
ATOM   463  C C   . ASP   A 1 83  ? -32.74442 36.30712 14.41989  1.000 55.52851  ? 63  ASP   A C   1 
ATOM   464  O O   . ASP   A 1 83  ? -33.07759 36.90339 13.38769  1.000 50.11579  ? 63  ASP   A O   1 
ATOM   465  C CB  . ASP   A 1 83  ? -31.77917 34.26067 13.31733  1.000 44.68997  ? 63  ASP   A CB  1 
ATOM   466  C CG  . ASP   A 1 83  ? -30.32418 34.66440 13.49481  1.000 52.90790  ? 63  ASP   A CG  1 
ATOM   467  O OD1 . ASP   A 1 83  ? -30.02417 35.87954 13.51598  1.000 52.44141  ? 63  ASP   A OD1 1 
ATOM   468  O OD2 . ASP   A 1 83  ? -29.47438 33.75840 13.61385  1.000 59.63214  ? 63  ASP   A OD2 1 
ATOM   469  N N   . PRO   A 1 84  ? -32.42699 36.97287 15.53492  1.000 52.92835  ? 64  PRO   A N   1 
ATOM   470  C CA  . PRO   A 1 84  ? -32.58836 38.43214 15.59416  1.000 55.19822  ? 64  PRO   A CA  1 
ATOM   471  C C   . PRO   A 1 84  ? -31.46430 39.21739 14.93915  1.000 57.30773  ? 64  PRO   A C   1 
ATOM   472  O O   . PRO   A 1 84  ? -31.63033 40.42538 14.71856  1.000 62.97569  ? 64  PRO   A O   1 
ATOM   473  C CB  . PRO   A 1 84  ? -32.63798 38.70820 17.10176  1.000 54.67471  ? 64  PRO   A CB  1 
ATOM   474  C CG  . PRO   A 1 84  ? -31.77169 37.64344 17.68289  1.000 56.09534  ? 64  PRO   A CG  1 
ATOM   475  C CD  . PRO   A 1 84  ? -31.96811 36.41627 16.82073  1.000 59.14417  ? 64  PRO   A CD  1 
ATOM   476  N N   . TYR   A 1 85  ? -30.33352 38.58514 14.62527  1.000 53.15111  ? 65  TYR   A N   1 
ATOM   477  C CA  . TYR   A 1 85  ? -29.20397 39.30240 14.04609  1.000 51.60905  ? 65  TYR   A CA  1 
ATOM   478  C C   . TYR   A 1 85  ? -29.19224 39.26947 12.52525  1.000 53.71759  ? 65  TYR   A C   1 
ATOM   479  O O   . TYR   A 1 85  ? -28.75091 40.23983 11.89748  1.000 54.14333  ? 65  TYR   A O   1 
ATOM   480  C CB  . TYR   A 1 85  ? -27.88421 38.72648 14.56788  1.000 44.96594  ? 65  TYR   A CB  1 
ATOM   481  C CG  . TYR   A 1 85  ? -27.65981 38.92977 16.04771  1.000 44.21665  ? 65  TYR   A CG  1 
ATOM   482  C CD1 . TYR   A 1 85  ? -27.14907 40.12753 16.53323  1.000 57.18697  ? 65  TYR   A CD1 1 
ATOM   483  C CD2 . TYR   A 1 85  ? -27.95105 37.92342 16.95950  1.000 51.36596  ? 65  TYR   A CD2 1 
ATOM   484  C CE1 . TYR   A 1 85  ? -26.93976 40.32029 17.88510  1.000 56.45758  ? 65  TYR   A CE1 1 
ATOM   485  C CE2 . TYR   A 1 85  ? -27.74490 38.10573 18.31600  1.000 55.93660  ? 65  TYR   A CE2 1 
ATOM   486  C CZ  . TYR   A 1 85  ? -27.23809 39.30658 18.77204  1.000 55.25702  ? 65  TYR   A CZ  1 
ATOM   487  O OH  . TYR   A 1 85  ? -27.02954 39.49902 20.11792  1.000 68.97393  ? 65  TYR   A OH  1 
ATOM   488  N N   . TRP   A 1 86  ? -29.66512 38.17701 11.92432  1.000 54.36842  ? 66  TRP   A N   1 
ATOM   489  C CA  . TRP   A 1 86  ? -29.59130 38.02820 10.47153  1.000 46.21146  ? 66  TRP   A CA  1 
ATOM   490  C C   . TRP   A 1 86  ? -30.33234 39.11938 9.70577   1.000 54.21968  ? 66  TRP   A C   1 
ATOM   491  O O   . TRP   A 1 86  ? -29.74488 39.67956 8.76337   1.000 44.54134  ? 66  TRP   A O   1 
ATOM   492  C CB  . TRP   A 1 86  ? -30.09104 36.63478 10.07863  1.000 46.18529  ? 66  TRP   A CB  1 
ATOM   493  C CG  . TRP   A 1 86  ? -30.04031 36.36491 8.60850   1.000 53.27384  ? 66  TRP   A CG  1 
ATOM   494  C CD1 . TRP   A 1 86  ? -31.08913 36.38645 7.73590   1.000 46.75590  ? 66  TRP   A CD1 1 
ATOM   495  C CD2 . TRP   A 1 86  ? -28.88083 36.02608 7.83504   1.000 48.54141  ? 66  TRP   A CD2 1 
ATOM   496  N NE1 . TRP   A 1 86  ? -30.65600 36.08091 6.46758   1.000 52.64567  ? 66  TRP   A NE1 1 
ATOM   497  C CE2 . TRP   A 1 86  ? -29.30436 35.85596 6.50132   1.000 50.13800  ? 66  TRP   A CE2 1 
ATOM   498  C CE3 . TRP   A 1 86  ? -27.52725 35.84827 8.14097   1.000 45.51579  ? 66  TRP   A CE3 1 
ATOM   499  C CZ2 . TRP   A 1 86  ? -28.42221 35.51881 5.47394   1.000 47.52041  ? 66  TRP   A CZ2 1 
ATOM   500  C CZ3 . TRP   A 1 86  ? -26.65201 35.51344 7.11804   1.000 48.17398  ? 66  TRP   A CZ3 1 
ATOM   501  C CH2 . TRP   A 1 86  ? -27.10418 35.35190 5.80212   1.000 51.49441  ? 66  TRP   A CH2 1 
ATOM   502  N N   . PRO   A 1 87  ? -31.58558 39.47176 10.02518  1.000 55.21151  ? 67  PRO   A N   1 
ATOM   503  C CA  . PRO   A 1 87  ? -32.27912 40.49659 9.22361   1.000 60.33640  ? 67  PRO   A CA  1 
ATOM   504  C C   . PRO   A 1 87  ? -31.57554 41.84571 9.19715   1.000 55.64396  ? 67  PRO   A C   1 
ATOM   505  O O   . PRO   A 1 87  ? -31.90502 42.67380 8.34042   1.000 65.04657  ? 67  PRO   A O   1 
ATOM   506  C CB  . PRO   A 1 87  ? -33.65865 40.60102 9.89207   1.000 64.02601  ? 67  PRO   A CB  1 
ATOM   507  C CG  . PRO   A 1 87  ? -33.48337 40.00123 11.24733  1.000 51.81679  ? 67  PRO   A CG  1 
ATOM   508  C CD  . PRO   A 1 87  ? -32.47268 38.92141 11.06537  1.000 50.71462  ? 67  PRO   A CD  1 
ATOM   509  N N   . GLY   A 1 88  ? -30.61656 42.09057 10.08831  1.000 53.54556  ? 68  GLY   A N   1 
ATOM   510  C CA  . GLY   A 1 88  ? -29.85724 43.32496 10.05467  1.000 50.16019  ? 68  GLY   A CA  1 
ATOM   511  C C   . GLY   A 1 88  ? -28.71349 43.35639 9.06211   1.000 61.13309  ? 68  GLY   A C   1 
ATOM   512  O O   . GLY   A 1 88  ? -28.19992 44.44070 8.76813   1.000 62.00878  ? 68  GLY   A O   1 
ATOM   513  N N   . LEU   A 1 89  ? -28.30454 42.20213 8.53963   1.000 54.14523  ? 69  LEU   A N   1 
ATOM   514  C CA  . LEU   A 1 89  ? -27.17458 42.11765 7.62404   1.000 62.55629  ? 69  LEU   A CA  1 
ATOM   515  C C   . LEU   A 1 89  ? -27.63239 42.28247 6.17880   1.000 54.74393  ? 69  LEU   A C   1 
ATOM   516  O O   . LEU   A 1 89  ? -28.74848 41.90228 5.81462   1.000 53.23360  ? 69  LEU   A O   1 
ATOM   517  C CB  . LEU   A 1 89  ? -26.45061 40.77987 7.78419   1.000 60.37046  ? 69  LEU   A CB  1 
ATOM   518  C CG  . LEU   A 1 89  ? -26.14969 40.32622 9.21388   1.000 58.49682  ? 69  LEU   A CG  1 
ATOM   519  C CD1 . LEU   A 1 89  ? -25.46036 38.96801 9.20671   1.000 52.95121  ? 69  LEU   A CD1 1 
ATOM   520  C CD2 . LEU   A 1 89  ? -25.30095 41.35608 9.93874   1.000 61.89242  ? 69  LEU   A CD2 1 
ATOM   521  N N   . ASP   A 1 90  ? -26.74550 42.84268 5.34682   1.000 55.40509  ? 70  ASP   A N   1 
ATOM   522  C CA  . ASP   A 1 90  ? -27.09566 43.08506 3.95008   1.000 57.73072  ? 70  ASP   A CA  1 
ATOM   523  C C   . ASP   A 1 90  ? -27.22935 41.79095 3.15621   1.000 64.55888  ? 70  ASP   A C   1 
ATOM   524  O O   . ASP   A 1 90  ? -27.87585 41.78950 2.10453   1.000 55.53188  ? 70  ASP   A O   1 
ATOM   525  C CB  . ASP   A 1 90  ? -26.06959 44.02057 3.28860   1.000 55.73748  ? 70  ASP   A CB  1 
ATOM   526  C CG  . ASP   A 1 90  ? -24.64404 43.48665 3.35780   1.000 70.20998  ? 70  ASP   A CG  1 
ATOM   527  O OD1 . ASP   A 1 90  ? -24.44941 42.31166 3.73925   1.000 67.26255  ? 70  ASP   A OD1 1 
ATOM   528  O OD2 . ASP   A 1 90  ? -23.71139 44.24977 3.02655   1.000 71.05391  ? 70  ASP   A OD2 1 
ATOM   529  N N   A CYS   A 1 91  ? -26.63969 40.69195 3.63108   0.660 61.90213  ? 71  CYS   A N   1 
ATOM   530  N N   B CYS   A 1 91  ? -26.61673 40.69957 3.62351   0.340 61.84258  ? 71  CYS   A N   1 
ATOM   531  C CA  A CYS   A 1 91  ? -26.81053 39.41460 2.95139   0.660 57.36353  ? 71  CYS   A CA  1 
ATOM   532  C CA  B CYS   A 1 91  ? -26.79358 39.40893 2.97052   0.340 57.42544  ? 71  CYS   A CA  1 
ATOM   533  C C   A CYS   A 1 91  ? -28.21361 38.84944 3.12633   0.660 57.12667  ? 71  CYS   A C   1 
ATOM   534  C C   B CYS   A 1 91  ? -28.21961 38.88611 3.09445   0.340 57.15812  ? 71  CYS   A C   1 
ATOM   535  O O   A CYS   A 1 91  ? -28.58870 37.92040 2.40386   0.660 60.35456  ? 71  CYS   A O   1 
ATOM   536  O O   B CYS   A 1 91  ? -28.60656 37.99860 2.32678   0.340 60.30498  ? 71  CYS   A O   1 
ATOM   537  C CB  A CYS   A 1 91  ? -25.76542 38.41794 3.44941   0.660 59.27731  ? 71  CYS   A CB  1 
ATOM   538  C CB  B CYS   A 1 91  ? -25.81499 38.38781 3.55160   0.340 59.33043  ? 71  CYS   A CB  1 
ATOM   539  S SG  A CYS   A 1 91  ? -25.48788 38.44066 5.24131   0.660 64.66245  ? 71  CYS   A SG  1 
ATOM   540  S SG  B CYS   A 1 91  ? -24.07424 38.76832 3.26438   0.340 48.53208  ? 71  CYS   A SG  1 
ATOM   541  N N   . ALA   A 1 92  ? -29.00179 39.39979 4.04987   1.000 57.86497  ? 72  ALA   A N   1 
ATOM   542  C CA  . ALA   A 1 92  ? -30.38935 38.97746 4.18479   1.000 55.15110  ? 72  ALA   A CA  1 
ATOM   543  C C   . ALA   A 1 92  ? -31.26185 39.54587 3.07568   1.000 57.02821  ? 72  ALA   A C   1 
ATOM   544  O O   . ALA   A 1 92  ? -32.35310 39.02075 2.82979   1.000 61.67629  ? 72  ALA   A O   1 
ATOM   545  C CB  . ALA   A 1 92  ? -30.93567 39.38777 5.55378   1.000 56.98556  ? 72  ALA   A CB  1 
ATOM   546  N N   . ALA   A 1 93  ? -30.80613 40.60686 2.40776   1.000 60.06059  ? 73  ALA   A N   1 
ATOM   547  C CA  . ALA   A 1 93  ? -31.47893 41.16599 1.24381   1.000 54.21322  ? 73  ALA   A CA  1 
ATOM   548  C C   . ALA   A 1 93  ? -30.69557 40.89288 -0.03757  1.000 55.10177  ? 73  ALA   A C   1 
ATOM   549  O O   . ALA   A 1 93  ? -30.68304 41.71778 -0.95479  1.000 58.40926  ? 73  ALA   A O   1 
ATOM   550  C CB  . ALA   A 1 93  ? -31.70783 42.66573 1.42746   1.000 51.77402  ? 73  ALA   A CB  1 
ATOM   551  N N   . SER   A 1 94  ? -30.03400 39.74014 -0.10929  1.000 53.50209  ? 74  SER   A N   1 
ATOM   552  C CA  . SER   A 1 94  ? -29.20840 39.36507 -1.24991  1.000 55.64521  ? 74  SER   A CA  1 
ATOM   553  C C   . SER   A 1 94  ? -29.83493 38.17800 -1.96753  1.000 56.62237  ? 74  SER   A C   1 
ATOM   554  O O   . SER   A 1 94  ? -30.13476 37.15584 -1.34072  1.000 52.59336  ? 74  SER   A O   1 
ATOM   555  C CB  . SER   A 1 94  ? -27.78242 39.02193 -0.80594  1.000 56.64323  ? 74  SER   A CB  1 
ATOM   556  O OG  . SER   A 1 94  ? -27.00380 38.53408 -1.88904  1.000 59.90208  ? 74  SER   A OG  1 
ATOM   557  N N   . ARG   A 1 95  ? -30.02955 38.31706 -3.28164  1.000 57.13796  ? 75  ARG   A N   1 
ATOM   558  C CA  . ARG   A 1 95  ? -30.54472 37.21294 -4.08200  1.000 59.41576  ? 75  ARG   A CA  1 
ATOM   559  C C   . ARG   A 1 95  ? -29.54427 36.07301 -4.20120  1.000 60.49183  ? 75  ARG   A C   1 
ATOM   560  O O   . ARG   A 1 95  ? -29.93401 34.95796 -4.56267  1.000 60.92726  ? 75  ARG   A O   1 
ATOM   561  C CB  . ARG   A 1 95  ? -30.91855 37.69440 -5.48398  1.000 65.06546  ? 75  ARG   A CB  1 
ATOM   562  C CG  . ARG   A 1 95  ? -31.82809 38.90650 -5.53385  1.000 67.96692  ? 75  ARG   A CG  1 
ATOM   563  C CD  . ARG   A 1 95  ? -32.07836 39.30480 -6.98118  1.000 70.71088  ? 75  ARG   A CD  1 
ATOM   564  N NE  . ARG   A 1 95  ? -30.84928 39.24996 -7.76578  1.000 88.72116  ? 75  ARG   A NE  1 
ATOM   565  C CZ  . ARG   A 1 95  ? -30.10761 40.30430 -8.07956  1.000 74.74182  ? 75  ARG   A CZ  1 
ATOM   566  N NH1 . ARG   A 1 95  ? -30.44702 41.52625 -7.70257  1.000 64.75640  ? 75  ARG   A NH1 1 
ATOM   567  N NH2 . ARG   A 1 95  ? -28.99667 40.12780 -8.78996  1.000 61.98388  ? 75  ARG   A NH2 1 
ATOM   568  N N   . HIS   A 1 96  ? -28.26859 36.32904 -3.91805  1.000 59.28846  ? 76  HIS   A N   1 
ATOM   569  C CA  . HIS   A 1 96  ? -27.23113 35.31304 -4.02734  1.000 65.21520  ? 76  HIS   A CA  1 
ATOM   570  C C   . HIS   A 1 96  ? -27.16390 34.39850 -2.81072  1.000 56.88748  ? 76  HIS   A C   1 
ATOM   571  O O   . HIS   A 1 96  ? -26.32380 33.49276 -2.78469  1.000 61.30188  ? 76  HIS   A O   1 
ATOM   572  C CB  . HIS   A 1 96  ? -25.86914 35.97912 -4.24742  1.000 58.88090  ? 76  HIS   A CB  1 
ATOM   573  C CG  . HIS   A 1 96  ? -25.81260 36.85722 -5.46012  1.000 77.33203  ? 76  HIS   A CG  1 
ATOM   574  N ND1 . HIS   A 1 96  ? -24.75759 37.70737 -5.71470  1.000 70.80164  ? 76  HIS   A ND1 1 
ATOM   575  C CD2 . HIS   A 1 96  ? -26.67909 37.01530 -6.48933  1.000 74.66269  ? 76  HIS   A CD2 1 
ATOM   576  C CE1 . HIS   A 1 96  ? -24.97675 38.35139 -6.84747  1.000 69.99023  ? 76  HIS   A CE1 1 
ATOM   577  N NE2 . HIS   A 1 96  ? -26.13639 37.95061 -7.33700  1.000 74.04893  ? 76  HIS   A NE2 1 
ATOM   578  N N   . VAL   A 1 97  ? -28.01960 34.60727 -1.81264  1.000 51.29313  ? 77  VAL   A N   1 
ATOM   579  C CA  . VAL   A 1 97  ? -27.99814 33.84084 -0.57234  1.000 58.76990  ? 77  VAL   A CA  1 
ATOM   580  C C   . VAL   A 1 97  ? -29.40877 33.33694 -0.30141  1.000 60.74113  ? 77  VAL   A C   1 
ATOM   581  O O   . VAL   A 1 97  ? -30.33775 34.13859 -0.14752  1.000 54.24304  ? 77  VAL   A O   1 
ATOM   582  C CB  . VAL   A 1 97  ? -27.48556 34.67671 0.61315   1.000 56.17293  ? 77  VAL   A CB  1 
ATOM   583  C CG1 . VAL   A 1 97  ? -27.57969 33.87720 1.90154   1.000 49.58895  ? 77  VAL   A CG1 1 
ATOM   584  C CG2 . VAL   A 1 97  ? -26.05471 35.13483 0.36320   1.000 56.78314  ? 77  VAL   A CG2 1 
ATOM   585  N N   . GLN   A 1 98  ? -29.56886 32.01831 -0.25162  1.000 53.22469  ? 78  GLN   A N   1 
ATOM   586  C CA  . GLN   A 1 98  ? -30.83001 31.37907 0.09085   1.000 53.99839  ? 78  GLN   A CA  1 
ATOM   587  C C   . GLN   A 1 98  ? -30.81114 30.92622 1.54710   1.000 47.28141  ? 78  GLN   A C   1 
ATOM   588  O O   . GLN   A 1 98  ? -29.75361 30.75397 2.15771   1.000 49.68352  ? 78  GLN   A O   1 
ATOM   589  C CB  . GLN   A 1 98  ? -31.10800 30.18510 -0.82948  1.000 61.45802  ? 78  GLN   A CB  1 
ATOM   590  C CG  . GLN   A 1 98  ? -31.90644 30.52303 -2.08121  1.000 60.38347  ? 78  GLN   A CG  1 
ATOM   591  C CD  . GLN   A 1 98  ? -31.11515 31.35922 -3.05785  1.000 64.61410  ? 78  GLN   A CD  1 
ATOM   592  O OE1 . GLN   A 1 98  ? -29.96895 31.04084 -3.37870  1.000 70.46684  ? 78  GLN   A OE1 1 
ATOM   593  N NE2 . GLN   A 1 98  ? -31.71706 32.44283 -3.53151  1.000 82.43388  ? 78  GLN   A NE2 1 
ATOM   594  N N   . ARG   A 1 99  ? -32.00713 30.71532 2.09174   1.000 49.47888  ? 79  ARG   A N   1 
ATOM   595  C CA  . ARG   A 1 99  ? -32.20303 30.46823 3.51317   1.000 47.57601  ? 79  ARG   A CA  1 
ATOM   596  C C   . ARG   A 1 99  ? -32.99077 29.18388 3.72352   1.000 59.51563  ? 79  ARG   A C   1 
ATOM   597  O O   . ARG   A 1 99  ? -33.97182 28.92529 3.01956   1.000 64.63867  ? 79  ARG   A O   1 
ATOM   598  C CB  . ARG   A 1 99  ? -32.94332 31.64296 4.16899   1.000 42.29011  ? 79  ARG   A CB  1 
ATOM   599  C CG  . ARG   A 1 99  ? -33.27105 31.45864 5.63556   1.000 45.68270  ? 79  ARG   A CG  1 
ATOM   600  C CD  . ARG   A 1 99  ? -33.92111 32.70788 6.19260   1.000 53.66545  ? 79  ARG   A CD  1 
ATOM   601  N NE  . ARG   A 1 99  ? -34.01276 32.66543 7.64532   1.000 48.82258  ? 79  ARG   A NE  1 
ATOM   602  C CZ  . ARG   A 1 99  ? -34.34157 33.70164 8.40372   1.000 59.94631  ? 79  ARG   A CZ  1 
ATOM   603  N NH1 . ARG   A 1 99  ? -34.62450 34.88229 7.87722   1.000 60.93315  ? 79  ARG   A NH1 1 
ATOM   604  N NH2 . ARG   A 1 99  ? -34.38320 33.55099 9.72386   1.000 54.68570  ? 79  ARG   A NH2 1 
ATOM   605  N N   . ALA   A 1 100 ? -32.55660 28.38268 4.69678   1.000 50.96338  ? 80  ALA   A N   1 
ATOM   606  C CA  . ALA   A 1 100 ? -33.24923 27.16208 5.08214   1.000 54.27097  ? 80  ALA   A CA  1 
ATOM   607  C C   . ALA   A 1 100 ? -33.50862 27.18882 6.58063   1.000 54.11166  ? 80  ALA   A C   1 
ATOM   608  O O   . ALA   A 1 100 ? -32.79326 27.85086 7.33727   1.000 59.69870  ? 80  ALA   A O   1 
ATOM   609  C CB  . ALA   A 1 100 ? -32.44793 25.90400 4.70878   1.000 47.20179  ? 80  ALA   A CB  1 
ATOM   610  N N   . ALA   A 1 101 ? -34.53942 26.46052 7.00285   1.000 63.37539  ? 81  ALA   A N   1 
ATOM   611  C CA  . ALA   A 1 101 ? -34.91941 26.42868 8.40736   1.000 58.72435  ? 81  ALA   A CA  1 
ATOM   612  C C   . ALA   A 1 101 ? -33.97748 25.52984 9.19640   1.000 60.84056  ? 81  ALA   A C   1 
ATOM   613  O O   . ALA   A 1 101 ? -33.61465 24.43843 8.74872   1.000 63.19972  ? 81  ALA   A O   1 
ATOM   614  C CB  . ALA   A 1 101 ? -36.36036 25.94107 8.56140   1.000 57.88703  ? 81  ALA   A CB  1 
ATOM   615  N N   . GLY   A 1 102 ? -33.58183 25.99651 10.37809  1.000 60.28300  ? 82  GLY   A N   1 
ATOM   616  C CA  . GLY   A 1 102 ? -32.70548 25.21271 11.22052  1.000 60.30741  ? 82  GLY   A CA  1 
ATOM   617  C C   . GLY   A 1 102 ? -33.41194 24.02736 11.84868  1.000 55.92413  ? 82  GLY   A C   1 
ATOM   618  O O   . GLY   A 1 102 ? -34.63944 23.96260 11.93358  1.000 60.79235  ? 82  GLY   A O   1 
ATOM   619  N N   . GLY   A 1 103 ? -32.60540 23.06203 12.29384  1.000 61.37078  ? 83  GLY   A N   1 
ATOM   620  C CA  . GLY   A 1 103 ? -33.09528 21.87853 12.95292  1.000 59.33160  ? 83  GLY   A CA  1 
ATOM   621  C C   . GLY   A 1 103 ? -32.78428 21.86714 14.43857  1.000 62.57159  ? 83  GLY   A C   1 
ATOM   622  O O   . GLY   A 1 103 ? -32.38278 22.87019 15.03239  1.000 67.96801  ? 83  GLY   A O   1 
ATOM   623  N N   . ALA   A 1 104 ? -32.97990 20.69253 15.04073  1.000 69.94631  ? 84  ALA   A N   1 
ATOM   624  C CA  . ALA   A 1 104 ? -32.70753 20.52945 16.46452  1.000 67.17609  ? 84  ALA   A CA  1 
ATOM   625  C C   . ALA   A 1 104 ? -31.21539 20.43536 16.75809  1.000 62.71222  ? 84  ALA   A C   1 
ATOM   626  O O   . ALA   A 1 104 ? -30.76878 20.88030 17.82105  1.000 64.65476  ? 84  ALA   A O   1 
ATOM   627  C CB  . ALA   A 1 104 ? -33.42640 19.29013 16.99824  1.000 73.62004  ? 84  ALA   A CB  1 
ATOM   628  N N   . GLU   A 1 105 ? -30.43942 19.85446 15.84695  1.000 61.45304  ? 85  GLU   A N   1 
ATOM   629  C CA  . GLU   A 1 105 ? -28.99018 19.78781 15.95707  1.000 59.39866  ? 85  GLU   A CA  1 
ATOM   630  C C   . GLU   A 1 105 ? -28.37966 20.28829 14.65588  1.000 56.82098  ? 85  GLU   A C   1 
ATOM   631  O O   . GLU   A 1 105 ? -29.08437 20.57129 13.68278  1.000 54.12266  ? 85  GLU   A O   1 
ATOM   632  C CB  . GLU   A 1 105 ? -28.50357 18.36318 16.26270  1.000 62.15689  ? 85  GLU   A CB  1 
ATOM   633  C CG  . GLU   A 1 105 ? -28.82385 17.34320 15.17552  1.000 64.78671  ? 85  GLU   A CG  1 
ATOM   634  C CD  . GLU   A 1 105 ? -30.25848 16.85053 15.23626  1.000 80.06272  ? 85  GLU   A CD  1 
ATOM   635  O OE1 . GLU   A 1 105 ? -30.67818 16.37502 16.31358  1.000 89.37297  ? 85  GLU   A OE1 1 
ATOM   636  O OE2 . GLU   A 1 105 ? -30.96799 16.94717 14.21075  1.000 77.13552  ? 85  GLU   A OE2 1 
ATOM   637  N N   . ARG   A 1 106 ? -27.04894 20.39674 14.64519  1.000 55.11575  ? 86  ARG   A N   1 
ATOM   638  C CA  . ARG   A 1 106 ? -26.36286 20.88124 13.45156  1.000 56.73955  ? 86  ARG   A CA  1 
ATOM   639  C C   . ARG   A 1 106 ? -26.61424 19.96466 12.26017  1.000 47.31910  ? 86  ARG   A C   1 
ATOM   640  O O   . ARG   A 1 106 ? -26.84420 20.43874 11.14116  1.000 47.76540  ? 86  ARG   A O   1 
ATOM   641  C CB  . ARG   A 1 106 ? -24.86391 21.01369 13.72287  1.000 54.27874  ? 86  ARG   A CB  1 
ATOM   642  C CG  . ARG   A 1 106 ? -24.05391 21.43507 12.50799  1.000 53.51668  ? 86  ARG   A CG  1 
ATOM   643  C CD  . ARG   A 1 106 ? -22.57362 21.16630 12.71183  1.000 57.42060  ? 86  ARG   A CD  1 
ATOM   644  N NE  . ARG   A 1 106 ? -21.90861 20.82648 11.45964  1.000 61.19495  ? 86  ARG   A NE  1 
ATOM   645  C CZ  . ARG   A 1 106 ? -21.14002 21.65438 10.76663  1.000 52.43562  ? 86  ARG   A CZ  1 
ATOM   646  N NH1 . ARG   A 1 106 ? -20.90299 22.88860 11.18109  1.000 73.28990  ? 86  ARG   A NH1 1 
ATOM   647  N NH2 . ARG   A 1 106 ? -20.59024 21.23114 9.63193   1.000 57.46794  ? 86  ARG   A NH2 1 
ATOM   648  N N   . ALA   A 1 107 ? -26.58779 18.64737 12.48433  1.000 58.79544  ? 87  ALA   A N   1 
ATOM   649  C CA  . ALA   A 1 107 ? -26.81589 17.70231 11.39412  1.000 57.56213  ? 87  ALA   A CA  1 
ATOM   650  C C   . ALA   A 1 107 ? -28.20287 17.87717 10.78872  1.000 53.50529  ? 87  ALA   A C   1 
ATOM   651  O O   . ALA   A 1 107 ? -28.36601 17.81992 9.56366   1.000 53.20010  ? 87  ALA   A O   1 
ATOM   652  C CB  . ALA   A 1 107 ? -26.62650 16.26929 11.89164  1.000 60.87853  ? 87  ALA   A CB  1 
ATOM   653  N N   . GLY   A 1 108 ? -29.21490 18.08950 11.63209  1.000 51.21726  ? 88  GLY   A N   1 
ATOM   654  C CA  . GLY   A 1 108 ? -30.55098 18.34032 11.11835  1.000 50.85619  ? 88  GLY   A CA  1 
ATOM   655  C C   . GLY   A 1 108 ? -30.62929 19.60996 10.29223  1.000 62.81980  ? 88  GLY   A C   1 
ATOM   656  O O   . GLY   A 1 108 ? -31.30866 19.65053 9.26326   1.000 58.41041  ? 88  GLY   A O   1 
ATOM   657  N N   . SER   A 1 109 ? -29.93312 20.66405 10.72930  1.000 54.35444  ? 89  SER   A N   1 
ATOM   658  C CA  . SER   A 1 109 ? -29.89930 21.90031 9.95257   1.000 55.90986  ? 89  SER   A CA  1 
ATOM   659  C C   . SER   A 1 109 ? -29.22275 21.68363 8.60490   1.000 49.29406  ? 89  SER   A C   1 
ATOM   660  O O   . SER   A 1 109 ? -29.68286 22.20233 7.57993   1.000 50.62425  ? 89  SER   A O   1 
ATOM   661  C CB  . SER   A 1 109 ? -29.18655 22.99858 10.74127  1.000 46.11560  ? 89  SER   A CB  1 
ATOM   662  O OG  . SER   A 1 109 ? -29.86575 23.26853 11.95575  1.000 54.74109  ? 89  SER   A OG  1 
ATOM   663  N N   . VAL   A 1 110 ? -28.12667 20.91881 8.58761   1.000 50.77900  ? 90  VAL   A N   1 
ATOM   664  C CA  . VAL   A 1 110 ? -27.48236 20.56445 7.32499   1.000 56.37073  ? 90  VAL   A CA  1 
ATOM   665  C C   . VAL   A 1 110 ? -28.44648 19.78542 6.44139   1.000 48.75036  ? 90  VAL   A C   1 
ATOM   666  O O   . VAL   A 1 110 ? -28.49367 19.98314 5.22025   1.000 48.58138  ? 90  VAL   A O   1 
ATOM   667  C CB  . VAL   A 1 110 ? -26.18699 19.77265 7.58877   1.000 56.41241  ? 90  VAL   A CB  1 
ATOM   668  C CG1 . VAL   A 1 110 ? -25.54777 19.33576 6.28197   1.000 41.07358  ? 90  VAL   A CG1 1 
ATOM   669  C CG2 . VAL   A 1 110 ? -25.21366 20.60896 8.39203   1.000 47.30339  ? 90  VAL   A CG2 1 
ATOM   670  N N   . LEU   A 1 111 ? -29.24269 18.90109 7.04787   1.000 52.59550  ? 91  LEU   A N   1 
ATOM   671  C CA  . LEU   A 1 111 ? -30.22439 18.13391 6.28791   1.000 60.86455  ? 91  LEU   A CA  1 
ATOM   672  C C   . LEU   A 1 111 ? -31.24589 19.04867 5.62381   1.000 54.70490  ? 91  LEU   A C   1 
ATOM   673  O O   . LEU   A 1 111 ? -31.56189 18.88650 4.43967   1.000 59.15512  ? 91  LEU   A O   1 
ATOM   674  C CB  . LEU   A 1 111 ? -30.92109 17.12294 7.19806   1.000 59.76063  ? 91  LEU   A CB  1 
ATOM   675  C CG  . LEU   A 1 111 ? -30.66170 15.65311 6.86647   1.000 60.50853  ? 91  LEU   A CG  1 
ATOM   676  C CD1 . LEU   A 1 111 ? -31.60874 14.75242 7.64494   1.000 68.21889  ? 91  LEU   A CD1 1 
ATOM   677  C CD2 . LEU   A 1 111 ? -30.78305 15.40535 5.36803   1.000 63.02578  ? 91  LEU   A CD2 1 
ATOM   678  N N   . ASN   A 1 112 ? -31.77500 20.01982 6.37302   1.000 57.12620  ? 92  ASN   A N   1 
ATOM   679  C CA  . ASN   A 1 112 ? -32.72827 20.95854 5.79090   1.000 52.35903  ? 92  ASN   A CA  1 
ATOM   680  C C   . ASN   A 1 112 ? -32.08677 21.80168 4.69732   1.000 48.57548  ? 92  ASN   A C   1 
ATOM   681  O O   . ASN   A 1 112 ? -32.76884 22.21382 3.75241   1.000 56.95512  ? 92  ASN   A O   1 
ATOM   682  C CB  . ASN   A 1 112 ? -33.31769 21.85324 6.87957   1.000 51.79429  ? 92  ASN   A CB  1 
ATOM   683  C CG  . ASN   A 1 112 ? -34.09225 21.06974 7.92073   1.000 64.15278  ? 92  ASN   A CG  1 
ATOM   684  O OD1 . ASN   A 1 112 ? -34.52259 19.94267 7.67313   1.000 61.17254  ? 92  ASN   A OD1 1 
ATOM   685  N ND2 . ASN   A 1 112 ? -34.27856 21.66640 9.09259   1.000 57.52541  ? 92  ASN   A ND2 1 
ATOM   686  N N   . GLY   A 1 113 ? -30.78350 22.06775 4.80453   1.000 51.76017  ? 93  GLY   A N   1 
ATOM   687  C CA  . GLY   A 1 113 ? -30.09242 22.75820 3.72871   1.000 50.43927  ? 93  GLY   A CA  1 
ATOM   688  C C   . GLY   A 1 113 ? -30.02541 21.92749 2.46187   1.000 50.32391  ? 93  GLY   A C   1 
ATOM   689  O O   . GLY   A 1 113 ? -30.12945 22.46008 1.35328   1.000 51.64930  ? 93  GLY   A O   1 
ATOM   690  N N   . LEU   A 1 114 ? -29.85368 20.61059 2.60794   1.000 52.07421  ? 94  LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 114 ? -29.86995 19.72451 1.44752   1.000 51.87093  ? 94  LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 114 ? -31.25150 19.68362 0.80599   1.000 55.74373  ? 94  LEU   A C   1 
ATOM   693  O O   . LEU   A 1 114 ? -31.37134 19.64902 -0.42459  1.000 57.14446  ? 94  LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 114 ? -29.42499 18.32084 1.85450   1.000 46.50337  ? 94  LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 114 ? -28.03557 18.22042 2.48736   1.000 49.82191  ? 94  LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 114 ? -27.69598 16.77500 2.80380   1.000 53.05076  ? 94  LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 114 ? -26.98147 18.83364 1.57887   1.000 45.49579  ? 94  LEU   A CD2 1 
ATOM   698  N N   . LEU   A 1 115 ? -32.30715 19.68500 1.62415   1.000 56.80122  ? 95  LEU   A N   1 
ATOM   699  C CA  . LEU   A 1 115 ? -33.66147 19.75542 1.08332   1.000 56.18124  ? 95  LEU   A CA  1 
ATOM   700  C C   . LEU   A 1 115 ? -33.89407 21.08188 0.37100   1.000 57.48232  ? 95  LEU   A C   1 
ATOM   701  O O   . LEU   A 1 115 ? -34.54504 21.13043 -0.68045  1.000 58.08960  ? 95  LEU   A O   1 
ATOM   702  C CB  . LEU   A 1 115 ? -34.68542 19.56606 2.20367   1.000 56.03370  ? 95  LEU   A CB  1 
ATOM   703  C CG  . LEU   A 1 115 ? -34.54142 18.31938 3.07923   1.000 67.31300  ? 95  LEU   A CG  1 
ATOM   704  C CD1 . LEU   A 1 115 ? -35.57996 18.32048 4.19496   1.000 67.44293  ? 95  LEU   A CD1 1 
ATOM   705  C CD2 . LEU   A 1 115 ? -34.65148 17.05722 2.24017   1.000 68.20725  ? 95  LEU   A CD2 1 
ATOM   706  N N   . ARG   A 1 116 ? -33.36730 22.17128 0.93454   1.000 56.09743  ? 96  ARG   A N   1 
ATOM   707  C CA  . ARG   A 1 116 ? -33.50776 23.48006 0.30512   1.000 58.89059  ? 96  ARG   A CA  1 
ATOM   708  C C   . ARG   A 1 116 ? -32.79074 23.52152 -1.03947  1.000 56.50017  ? 96  ARG   A C   1 
ATOM   709  O O   . ARG   A 1 116 ? -33.26907 24.15467 -1.98904  1.000 60.98311  ? 96  ARG   A O   1 
ATOM   710  C CB  . ARG   A 1 116 ? -32.97073 24.56399 1.24142   1.000 52.45963  ? 96  ARG   A CB  1 
ATOM   711  C CG  . ARG   A 1 116 ? -33.25298 25.98662 0.79070   1.000 63.28759  ? 96  ARG   A CG  1 
ATOM   712  C CD  . ARG   A 1 116 ? -34.72552 26.33637 0.94010   1.000 63.34471  ? 96  ARG   A CD  1 
ATOM   713  N NE  . ARG   A 1 116 ? -35.05260 27.62388 0.33814   1.000 67.74705  ? 96  ARG   A NE  1 
ATOM   714  C CZ  . ARG   A 1 116 ? -35.39705 27.79067 -0.93161  1.000 71.49592  ? 96  ARG   A CZ  1 
ATOM   715  N NH1 . ARG   A 1 116 ? -35.46984 26.76804 -1.76825  1.000 76.00374  ? 96  ARG   A NH1 1 
ATOM   716  N NH2 . ARG   A 1 116 ? -35.67540 29.01408 -1.37327  1.000 72.43352  ? 96  ARG   A NH2 1 
ATOM   717  N N   . LEU   A 1 117 ? -31.64131 22.84698 -1.13963  1.000 48.18989  ? 97  LEU   A N   1 
ATOM   718  C CA  . LEU   A 1 117 ? -30.92966 22.77533 -2.41236  1.000 55.37710  ? 97  LEU   A CA  1 
ATOM   719  C C   . LEU   A 1 117 ? -31.74987 22.03754 -3.46415  1.000 60.01533  ? 97  LEU   A C   1 
ATOM   720  O O   . LEU   A 1 117 ? -31.77036 22.43304 -4.63608  1.000 59.28742  ? 97  LEU   A O   1 
ATOM   721  C CB  . LEU   A 1 117 ? -29.57346 22.09459 -2.22141  1.000 63.14205  ? 97  LEU   A CB  1 
ATOM   722  C CG  . LEU   A 1 117 ? -28.49068 22.85967 -1.45891  1.000 59.77213  ? 97  LEU   A CG  1 
ATOM   723  C CD1 . LEU   A 1 117 ? -27.24920 21.99654 -1.30890  1.000 52.01236  ? 97  LEU   A CD1 1 
ATOM   724  C CD2 . LEU   A 1 117 ? -28.15216 24.16723 -2.15885  1.000 56.08876  ? 97  LEU   A CD2 1 
ATOM   725  N N   . LEU   A 1 118 ? -32.43364 20.96111 -3.06482  1.000 54.31821  ? 98  LEU   A N   1 
ATOM   726  C CA  . LEU   A 1 118 ? -33.26384 20.22078 -4.01023  1.000 58.76373  ? 98  LEU   A CA  1 
ATOM   727  C C   . LEU   A 1 118 ? -34.40744 21.07415 -4.54247  1.000 68.36005  ? 98  LEU   A C   1 
ATOM   728  O O   . LEU   A 1 118 ? -34.86286 20.86514 -5.67288  1.000 68.20046  ? 98  LEU   A O   1 
ATOM   729  C CB  . LEU   A 1 118 ? -33.80281 18.94943 -3.35339  1.000 64.30629  ? 98  LEU   A CB  1 
ATOM   730  C CG  . LEU   A 1 118 ? -32.75829 17.86030 -3.09247  1.000 59.47194  ? 98  LEU   A CG  1 
ATOM   731  C CD1 . LEU   A 1 118 ? -33.38723 16.64635 -2.42517  1.000 60.93930  ? 98  LEU   A CD1 1 
ATOM   732  C CD2 . LEU   A 1 118 ? -32.05061 17.45883 -4.38426  1.000 63.54338  ? 98  LEU   A CD2 1 
ATOM   733  N N   . GLU   A 1 119 ? -34.87943 22.04092 -3.75142  1.000 66.50393  ? 99  GLU   A N   1 
ATOM   734  C CA  . GLU   A 1 119 ? -35.91661 22.94615 -4.23287  1.000 67.78580  ? 99  GLU   A CA  1 
ATOM   735  C C   . GLU   A 1 119 ? -35.37428 23.91196 -5.27594  1.000 64.86402  ? 99  GLU   A C   1 
ATOM   736  O O   . GLU   A 1 119 ? -36.11139 24.33187 -6.17542  1.000 75.35982  ? 99  GLU   A O   1 
ATOM   737  C CB  . GLU   A 1 119 ? -36.51959 23.72199 -3.06501  1.000 64.72830  ? 99  GLU   A CB  1 
ATOM   738  C CG  . GLU   A 1 119 ? -37.09816 22.84593 -1.97193  1.000 69.58177  ? 99  GLU   A CG  1 
ATOM   739  C CD  . GLU   A 1 119 ? -37.57623 23.65536 -0.78575  1.000 80.78906  ? 99  GLU   A CD  1 
ATOM   740  O OE1 . GLU   A 1 119 ? -37.09710 24.79676 -0.61912  1.000 72.98391  ? 99  GLU   A OE1 1 
ATOM   741  O OE2 . GLU   A 1 119 ? -38.43248 23.15639 -0.02475  1.000 95.44889  ? 99  GLU   A OE2 1 
ATOM   742  N N   . LEU   A 1 120 ? -34.09884 24.27311 -5.17291  1.000 60.17421  ? 100 LEU   A N   1 
ATOM   743  C CA  . LEU   A 1 120 ? -33.46503 25.19024 -6.10880  1.000 60.98898  ? 100 LEU   A CA  1 
ATOM   744  C C   . LEU   A 1 120 ? -32.97807 24.50023 -7.37605  1.000 63.04980  ? 100 LEU   A C   1 
ATOM   745  O O   . LEU   A 1 120 ? -32.31250 25.14368 -8.19720  1.000 71.93456  ? 100 LEU   A O   1 
ATOM   746  C CB  . LEU   A 1 120 ? -32.29891 25.90785 -5.42292  1.000 64.03380  ? 100 LEU   A CB  1 
ATOM   747  C CG  . LEU   A 1 120 ? -32.65136 26.68549 -4.15136  1.000 62.15267  ? 100 LEU   A CG  1 
ATOM   748  C CD1 . LEU   A 1 120 ? -31.39268 27.20338 -3.46856  1.000 59.76286  ? 100 LEU   A CD1 1 
ATOM   749  C CD2 . LEU   A 1 120 ? -33.60840 27.82530 -4.47212  1.000 60.11818  ? 100 LEU   A CD2 1 
ATOM   750  N N   . GLY   A 1 121 ? -33.28699 23.22092 -7.55122  1.000 70.10507  ? 101 GLY   A N   1 
ATOM   751  C CA  . GLY   A 1 121 ? -32.90217 22.50063 -8.74296  1.000 68.04232  ? 101 GLY   A CA  1 
ATOM   752  C C   . GLY   A 1 121 ? -31.63403 21.68521 -8.63577  1.000 62.12257  ? 101 GLY   A C   1 
ATOM   753  O O   . GLY   A 1 121 ? -31.01852 21.39902 -9.66947  1.000 73.89438  ? 101 GLY   A O   1 
ATOM   754  N N   . ALA   A 1 122 ? -31.22072 21.30664 -7.43051  1.000 64.92412  ? 102 ALA   A N   1 
ATOM   755  C CA  . ALA   A 1 122 ? -30.02105 20.50009 -7.27222  1.000 68.62805  ? 102 ALA   A CA  1 
ATOM   756  C C   . ALA   A 1 122 ? -30.30699 19.04244 -7.61356  1.000 60.51436  ? 102 ALA   A C   1 
ATOM   757  O O   . ALA   A 1 122 ? -31.42608 18.54960 -7.44583  1.000 65.51324  ? 102 ALA   A O   1 
ATOM   758  C CB  . ALA   A 1 122 ? -29.48067 20.60643 -5.84661  1.000 62.49572  ? 102 ALA   A CB  1 
ATOM   759  N N   . GLN   A 1 123 ? -29.27998 18.35359 -8.10067  1.000 54.18079  ? 103 GLN   A N   1 
ATOM   760  C CA  . GLN   A 1 123 ? -29.38236 16.95015 -8.46719  1.000 72.57650  ? 103 GLN   A CA  1 
ATOM   761  C C   . GLN   A 1 123 ? -28.61025 16.09199 -7.47252  1.000 58.28736  ? 103 GLN   A C   1 
ATOM   762  O O   . GLN   A 1 123 ? -27.73856 16.57590 -6.74422  1.000 61.22324  ? 103 GLN   A O   1 
ATOM   763  C CB  . GLN   A 1 123 ? -28.86182 16.71533 -9.88982  1.000 74.47621  ? 103 GLN   A CB  1 
ATOM   764  C CG  . GLN   A 1 123 ? -29.66008 15.68534 -10.68037 1.000 77.55721  ? 103 GLN   A CG  1 
ATOM   765  C CD  . GLN   A 1 123 ? -31.03416 16.19124 -11.09482 1.000 80.33582  ? 103 GLN   A CD  1 
ATOM   766  O OE1 . GLN   A 1 123 ? -31.34802 17.37312 -10.94507 1.000 61.52111  ? 103 GLN   A OE1 1 
ATOM   767  N NE2 . GLN   A 1 123 ? -31.85940 15.29339 -11.62292 1.000 77.73242  ? 103 GLN   A NE2 1 
ATOM   768  N N   . ALA   A 1 124 ? -28.94089 14.79692 -7.45856  1.000 59.47301  ? 104 ALA   A N   1 
ATOM   769  C CA  . ALA   A 1 124 ? -28.38104 13.89464 -6.45501  1.000 56.48803  ? 104 ALA   A CA  1 
ATOM   770  C C   . ALA   A 1 124 ? -26.87248 13.74287 -6.59867  1.000 52.52157  ? 104 ALA   A C   1 
ATOM   771  O O   . ALA   A 1 124 ? -26.18251 13.44598 -5.61592  1.000 55.21038  ? 104 ALA   A O   1 
ATOM   772  C CB  . ALA   A 1 124 ? -29.05821 12.52738 -6.54196  1.000 54.11673  ? 104 ALA   A CB  1 
ATOM   773  N N   . ASP   A 1 125 ? -26.34290 13.94362 -7.80302  1.000 58.86329  ? 105 ASP   A N   1 
ATOM   774  C CA  . ASP   A 1 125 ? -24.92219 13.77687 -8.07293  1.000 56.72755  ? 105 ASP   A CA  1 
ATOM   775  C C   . ASP   A 1 125 ? -24.15718 15.09211 -8.04085  1.000 52.50425  ? 105 ASP   A C   1 
ATOM   776  O O   . ASP   A 1 125 ? -22.97041 15.11570 -8.38212  1.000 66.95347  ? 105 ASP   A O   1 
ATOM   777  C CB  . ASP   A 1 125 ? -24.72456 13.08402 -9.42206  1.000 68.36943  ? 105 ASP   A CB  1 
ATOM   778  C CG  . ASP   A 1 125 ? -24.77160 11.56936 -9.31206  1.000 91.73469  ? 105 ASP   A CG  1 
ATOM   779  O OD1 . ASP   A 1 125 ? -25.72903 11.03910 -8.70481  1.000 76.15756  ? 105 ASP   A OD1 1 
ATOM   780  O OD2 . ASP   A 1 125 ? -23.84873 10.91108 -9.83948  1.000 88.03844  ? 105 ASP   A OD2 1 
ATOM   781  N N   . ASP   A 1 126 ? -24.80672 16.18018 -7.63785  1.000 58.04865  ? 106 ASP   A N   1 
ATOM   782  C CA  . ASP   A 1 126 ? -24.14922 17.47442 -7.53566  1.000 56.58059  ? 106 ASP   A CA  1 
ATOM   783  C C   . ASP   A 1 126 ? -23.24753 17.51666 -6.30768  1.000 60.81898  ? 106 ASP   A C   1 
ATOM   784  O O   . ASP   A 1 126 ? -23.57466 16.95028 -5.26004  1.000 59.42709  ? 106 ASP   A O   1 
ATOM   785  C CB  . ASP   A 1 126 ? -25.19024 18.59456 -7.45609  1.000 68.61056  ? 106 ASP   A CB  1 
ATOM   786  C CG  . ASP   A 1 126 ? -25.97195 18.76775 -8.75063  1.000 71.61907  ? 106 ASP   A CG  1 
ATOM   787  O OD1 . ASP   A 1 126 ? -25.44068 18.39709 -9.81730  1.000 66.78973  ? 106 ASP   A OD1 1 
ATOM   788  O OD2 . ASP   A 1 126 ? -27.11086 19.28444 -8.70435  1.000 61.89823  ? 106 ASP   A OD2 1 
ATOM   789  N N   . TRP   A 1 127 ? -22.10751 18.19204 -6.43989  1.000 54.63159  ? 107 TRP   A N   1 
ATOM   790  C CA  . TRP   A 1 127 ? -21.21699 18.37483 -5.30109  1.000 60.72378  ? 107 TRP   A CA  1 
ATOM   791  C C   . TRP   A 1 127 ? -21.79575 19.39652 -4.33024  1.000 50.79170  ? 107 TRP   A C   1 
ATOM   792  O O   . TRP   A 1 127 ? -22.31844 20.43710 -4.73712  1.000 52.12280  ? 107 TRP   A O   1 
ATOM   793  C CB  . TRP   A 1 127 ? -19.83186 18.82610 -5.76505  1.000 51.41759  ? 107 TRP   A CB  1 
ATOM   794  C CG  . TRP   A 1 127 ? -19.00020 17.72791 -6.34910  1.000 65.96258  ? 107 TRP   A CG  1 
ATOM   795  C CD1 . TRP   A 1 127 ? -18.53067 17.64696 -7.62825  1.000 54.90326  ? 107 TRP   A CD1 1 
ATOM   796  C CD2 . TRP   A 1 127 ? -18.53729 16.54800 -5.67583  1.000 61.04337  ? 107 TRP   A CD2 1 
ATOM   797  N NE1 . TRP   A 1 127 ? -17.80151 16.49275 -7.79275  1.000 61.74319  ? 107 TRP   A NE1 1 
ATOM   798  C CE2 . TRP   A 1 127 ? -17.79147 15.80044 -6.60984  1.000 67.91461  ? 107 TRP   A CE2 1 
ATOM   799  C CE3 . TRP   A 1 127 ? -18.68040 16.05227 -4.37532  1.000 50.56002  ? 107 TRP   A CE3 1 
ATOM   800  C CZ2 . TRP   A 1 127 ? -17.19027 14.58488 -6.28484  1.000 55.36420  ? 107 TRP   A CZ2 1 
ATOM   801  C CZ3 . TRP   A 1 127 ? -18.08269 14.84346 -4.05497  1.000 55.70956  ? 107 TRP   A CZ3 1 
ATOM   802  C CH2 . TRP   A 1 127 ? -17.34767 14.12446 -5.00655  1.000 64.58427  ? 107 TRP   A CH2 1 
ATOM   803  N N   . VAL   A 1 128 ? -21.70355 19.09386 -3.03776  1.000 55.74575  ? 108 VAL   A N   1 
ATOM   804  C CA  . VAL   A 1 128 ? -22.16059 19.98709 -1.97964  1.000 46.79647  ? 108 VAL   A CA  1 
ATOM   805  C C   . VAL   A 1 128 ? -20.99584 20.24242 -1.03622  1.000 48.02588  ? 108 VAL   A C   1 
ATOM   806  O O   . VAL   A 1 128 ? -20.28212 19.30719 -0.65667  1.000 45.30298  ? 108 VAL   A O   1 
ATOM   807  C CB  . VAL   A 1 128 ? -23.36315 19.40310 -1.21545  1.000 43.98263  ? 108 VAL   A CB  1 
ATOM   808  C CG1 . VAL   A 1 128 ? -23.81694 20.35776 -0.12571  1.000 41.37445  ? 108 VAL   A CG1 1 
ATOM   809  C CG2 . VAL   A 1 128 ? -24.50228 19.11145 -2.16681  1.000 54.16644  ? 108 VAL   A CG2 1 
ATOM   810  N N   . LEU   A 1 129 ? -20.80496 21.50535 -0.66510  1.000 55.09854  ? 109 LEU   A N   1 
ATOM   811  C CA  . LEU   A 1 129 ? -19.78771 21.91153 0.29452   1.000 44.83112  ? 109 LEU   A CA  1 
ATOM   812  C C   . LEU   A 1 129 ? -20.46398 22.42597 1.55755   1.000 50.90959  ? 109 LEU   A C   1 
ATOM   813  O O   . LEU   A 1 129 ? -21.32145 23.31223 1.48911   1.000 51.17996  ? 109 LEU   A O   1 
ATOM   814  C CB  . LEU   A 1 129 ? -18.87649 22.99521 -0.28931  1.000 56.90615  ? 109 LEU   A CB  1 
ATOM   815  C CG  . LEU   A 1 129 ? -17.61752 22.55722 -1.04249  1.000 63.55527  ? 109 LEU   A CG  1 
ATOM   816  C CD1 . LEU   A 1 129 ? -17.96097 21.77326 -2.29846  1.000 54.53946  ? 109 LEU   A CD1 1 
ATOM   817  C CD2 . LEU   A 1 129 ? -16.76460 23.76541 -1.38483  1.000 39.82788  ? 109 LEU   A CD2 1 
ATOM   818  N N   . VAL   A 1 130 ? -20.08282 21.86765 2.70364   1.000 52.48676  ? 110 VAL   A N   1 
ATOM   819  C CA  . VAL   A 1 130 ? -20.55730 22.32034 4.00625   1.000 38.12934  ? 110 VAL   A CA  1 
ATOM   820  C C   . VAL   A 1 130 ? -19.38426 22.96791 4.72731   1.000 47.47237  ? 110 VAL   A C   1 
ATOM   821  O O   . VAL   A 1 130 ? -18.29703 22.38364 4.80173   1.000 48.56206  ? 110 VAL   A O   1 
ATOM   822  C CB  . VAL   A 1 130 ? -21.14918 21.16273 4.82914   1.000 45.11128  ? 110 VAL   A CB  1 
ATOM   823  C CG1 . VAL   A 1 130 ? -21.81619 21.69434 6.09016   1.000 41.87663  ? 110 VAL   A CG1 1 
ATOM   824  C CG2 . VAL   A 1 130 ? -22.13804 20.36503 3.99029   1.000 43.16394  ? 110 VAL   A CG2 1 
ATOM   825  N N   . HIS   A 1 131 ? -19.59968 24.17409 5.25000   1.000 39.74319  ? 111 HIS   A N   1 
ATOM   826  C CA  . HIS   A 1 131 ? -18.52737 24.96510 5.83414   1.000 45.99817  ? 111 HIS   A CA  1 
ATOM   827  C C   . HIS   A 1 131 ? -19.02651 25.66084 7.09208   1.000 40.22968  ? 111 HIS   A C   1 
ATOM   828  O O   . HIS   A 1 131 ? -20.18097 26.09323 7.15349   1.000 42.47859  ? 111 HIS   A O   1 
ATOM   829  C CB  . HIS   A 1 131 ? -18.00405 25.99868 4.82794   1.000 41.01471  ? 111 HIS   A CB  1 
ATOM   830  C CG  . HIS   A 1 131 ? -16.80972 26.76189 5.30751   1.000 48.00513  ? 111 HIS   A CG  1 
ATOM   831  N ND1 . HIS   A 1 131 ? -15.54834 26.20976 5.36581   1.000 49.58737  ? 111 HIS   A ND1 1 
ATOM   832  C CD2 . HIS   A 1 131 ? -16.68334 28.03637 5.74784   1.000 46.33939  ? 111 HIS   A CD2 1 
ATOM   833  C CE1 . HIS   A 1 131 ? -14.69623 27.11110 5.82136   1.000 54.80975  ? 111 HIS   A CE1 1 
ATOM   834  N NE2 . HIS   A 1 131 ? -15.35966 28.22718 6.06241   1.000 42.35884  ? 111 HIS   A NE2 1 
ATOM   835  N N   . ASP   A 1 132 ? -18.14813 25.76884 8.08823   1.000 41.45102  ? 112 ASP   A N   1 
ATOM   836  C CA  . ASP   A 1 132 ? -18.51500 26.38662 9.35734   1.000 51.78155  ? 112 ASP   A CA  1 
ATOM   837  C C   . ASP   A 1 132 ? -18.77432 27.87907 9.18878   1.000 44.54879  ? 112 ASP   A C   1 
ATOM   838  O O   . ASP   A 1 132 ? -18.05537 28.57707 8.46739   1.000 46.87798  ? 112 ASP   A O   1 
ATOM   839  C CB  . ASP   A 1 132 ? -17.41511 26.17150 10.39838  1.000 52.73013  ? 112 ASP   A CB  1 
ATOM   840  C CG  . ASP   A 1 132 ? -17.22032 24.71126 10.74936  1.000 61.80574  ? 112 ASP   A CG  1 
ATOM   841  O OD1 . ASP   A 1 132 ? -18.20015 23.94008 10.66457  1.000 67.40399  ? 112 ASP   A OD1 1 
ATOM   842  O OD2 . ASP   A 1 132 ? -16.08490 24.33214 11.10990  1.000 64.05200  ? 112 ASP   A OD2 1 
ATOM   843  N N   . ALA   A 1 133 ? -19.81282 28.36802 9.87119   1.000 45.21588  ? 113 ALA   A N   1 
ATOM   844  C CA  . ALA   A 1 133 ? -20.13856 29.78589 9.81712   1.000 54.34378  ? 113 ALA   A CA  1 
ATOM   845  C C   . ALA   A 1 133 ? -19.06880 30.64133 10.48076  1.000 56.38716  ? 113 ALA   A C   1 
ATOM   846  O O   . ALA   A 1 133 ? -18.92959 31.81859 10.13313  1.000 47.68444  ? 113 ALA   A O   1 
ATOM   847  C CB  . ALA   A 1 133 ? -21.50258 30.03867 10.47056  1.000 42.02269  ? 113 ALA   A CB  1 
ATOM   848  N N   . ALA   A 1 134 ? -18.31266 30.08070 11.42577  1.000 52.72024  ? 114 ALA   A N   1 
ATOM   849  C CA  . ALA   A 1 134 ? -17.28877 30.82308 12.14813  1.000 49.92414  ? 114 ALA   A CA  1 
ATOM   850  C C   . ALA   A 1 134 ? -15.87846 30.51982 11.64358  1.000 48.12543  ? 114 ALA   A C   1 
ATOM   851  O O   . ALA   A 1 134 ? -14.91563 30.58690 12.41456  1.000 52.05157  ? 114 ALA   A O   1 
ATOM   852  C CB  . ALA   A 1 134 ? -17.40029 30.54494 13.64683  1.000 49.29683  ? 114 ALA   A CB  1 
ATOM   853  N N   . ARG   A 1 135 ? -15.73613 30.17730 10.35992  1.000 45.21228  ? 115 ARG   A N   1 
ATOM   854  C CA  . ARG   A 1 135 ? -14.43568 30.01689 9.71089   1.000 47.69803  ? 115 ARG   A CA  1 
ATOM   855  C C   . ARG   A 1 135 ? -14.35043 31.02290 8.56552   1.000 44.92686  ? 115 ARG   A C   1 
ATOM   856  O O   . ARG   A 1 135 ? -14.55323 30.66532 7.39566   1.000 45.31114  ? 115 ARG   A O   1 
ATOM   857  C CB  . ARG   A 1 135 ? -14.22419 28.59146 9.20260   1.000 43.16502  ? 115 ARG   A CB  1 
ATOM   858  C CG  . ARG   A 1 135 ? -13.97480 27.55559 10.28957  1.000 51.37422  ? 115 ARG   A CG  1 
ATOM   859  C CD  . ARG   A 1 135 ? -13.45878 26.25090 9.69140   1.000 59.34001  ? 115 ARG   A CD  1 
ATOM   860  N NE  . ARG   A 1 135 ? -13.51914 25.14033 10.63487  1.000 47.59658  ? 115 ARG   A NE  1 
ATOM   861  C CZ  . ARG   A 1 135 ? -12.51240 24.75530 11.40689  1.000 53.42848  ? 115 ARG   A CZ  1 
ATOM   862  N NH1 . ARG   A 1 135 ? -11.33769 25.36283 11.36569  1.000 51.76984  ? 115 ARG   A NH1 1 
ATOM   863  N NH2 . ARG   A 1 135 ? -12.68888 23.73521 12.24176  1.000 52.65113  ? 115 ARG   A NH2 1 
ATOM   864  N N   . PRO   A 1 136 ? -14.04176 32.28780 8.86533   1.000 44.37513  ? 116 PRO   A N   1 
ATOM   865  C CA  . PRO   A 1 136 ? -14.03422 33.32061 7.82087   1.000 49.01272  ? 116 PRO   A CA  1 
ATOM   866  C C   . PRO   A 1 136 ? -12.71976 33.48976 7.07317   1.000 46.18757  ? 116 PRO   A C   1 
ATOM   867  O O   . PRO   A 1 136 ? -12.68145 34.26875 6.10995   1.000 52.80903  ? 116 PRO   A O   1 
ATOM   868  C CB  . PRO   A 1 136 ? -14.36305 34.59272 8.61920   1.000 41.57122  ? 116 PRO   A CB  1 
ATOM   869  C CG  . PRO   A 1 136 ? -13.73531 34.34834 9.95347   1.000 42.42104  ? 116 PRO   A CG  1 
ATOM   870  C CD  . PRO   A 1 136 ? -13.80352 32.85532 10.20604  1.000 43.56311  ? 116 PRO   A CD  1 
ATOM   871  N N   . ASN   A 1 137 ? -11.65266 32.79544 7.46992   1.000 51.59350  ? 117 ASN   A N   1 
ATOM   872  C CA  . ASN   A 1 137 ? -10.34258 32.95665 6.85192   1.000 49.80231  ? 117 ASN   A CA  1 
ATOM   873  C C   . ASN   A 1 137 ? -10.07360 31.90925 5.77454   1.000 47.60298  ? 117 ASN   A C   1 
ATOM   874  O O   . ASN   A 1 137 ? -8.91374  31.57625 5.50821   1.000 54.62036  ? 117 ASN   A O   1 
ATOM   875  C CB  . ASN   A 1 137 ? -9.24982  32.91877 7.91968   1.000 51.09920  ? 117 ASN   A CB  1 
ATOM   876  C CG  . ASN   A 1 137 ? -7.97015  33.59945 7.46951   1.000 59.64861  ? 117 ASN   A CG  1 
ATOM   877  O OD1 . ASN   A 1 137 ? -8.00395  34.63803 6.80805   1.000 72.86635  ? 117 ASN   A OD1 1 
ATOM   878  N ND2 . ASN   A 1 137 ? -6.83304  33.01129 7.82065   1.000 58.07806  ? 117 ASN   A ND2 1 
ATOM   879  N N   . LEU   A 1 138 ? -11.12292 31.38007 5.14908   1.000 47.56319  ? 118 LEU   A N   1 
ATOM   880  C CA  . LEU   A 1 138 ? -10.94314 30.43200 4.05624   1.000 55.02259  ? 118 LEU   A CA  1 
ATOM   881  C C   . LEU   A 1 138 ? -10.43359 31.16261 2.82008   1.000 60.49408  ? 118 LEU   A C   1 
ATOM   882  O O   . LEU   A 1 138 ? -11.09763 32.06873 2.30570   1.000 63.94551  ? 118 LEU   A O   1 
ATOM   883  C CB  . LEU   A 1 138 ? -12.25386 29.71527 3.74790   1.000 49.12961  ? 118 LEU   A CB  1 
ATOM   884  C CG  . LEU   A 1 138 ? -12.18255 28.71671 2.59056   1.000 51.40910  ? 118 LEU   A CG  1 
ATOM   885  C CD1 . LEU   A 1 138 ? -11.34273 27.50418 2.97283   1.000 46.23281  ? 118 LEU   A CD1 1 
ATOM   886  C CD2 . LEU   A 1 138 ? -13.57342 28.29961 2.14269   1.000 50.98380  ? 118 LEU   A CD2 1 
ATOM   887  N N   . THR   A 1 139 ? -9.25941  30.77129 2.34343   1.000 61.03424  ? 119 THR   A N   1 
ATOM   888  C CA  . THR   A 1 139 ? -8.66533  31.40324 1.17717   1.000 60.99227  ? 119 THR   A CA  1 
ATOM   889  C C   . THR   A 1 139 ? -9.18085  30.75823 -0.10474  1.000 64.44235  ? 119 THR   A C   1 
ATOM   890  O O   . THR   A 1 139 ? -9.67744  29.62865 -0.10883  1.000 55.21303  ? 119 THR   A O   1 
ATOM   891  C CB  . THR   A 1 139 ? -7.14092  31.30866 1.22905   1.000 59.82037  ? 119 THR   A CB  1 
ATOM   892  O OG1 . THR   A 1 139 ? -6.75204  29.92899 1.26223   1.000 66.76453  ? 119 THR   A OG1 1 
ATOM   893  C CG2 . THR   A 1 139 ? -6.60943  32.01403 2.46866   1.000 48.72345  ? 119 THR   A CG2 1 
ATOM   894  N N   . ARG   A 1 140 ? -9.05158  31.50209 -1.20590  1.000 53.21775  ? 120 ARG   A N   1 
ATOM   895  C CA  . ARG   A 1 140 ? -9.44887  30.97973 -2.50787  1.000 51.69575  ? 120 ARG   A CA  1 
ATOM   896  C C   . ARG   A 1 140 ? -8.60263  29.78066 -2.90659  1.000 52.13467  ? 120 ARG   A C   1 
ATOM   897  O O   . ARG   A 1 140 ? -9.08411  28.88059 -3.60537  1.000 58.72067  ? 120 ARG   A O   1 
ATOM   898  C CB  . ARG   A 1 140 ? -9.33700  32.07961 -3.56207  1.000 54.29560  ? 120 ARG   A CB  1 
ATOM   899  C CG  . ARG   A 1 140 ? -9.63631  31.61273 -4.96682  1.000 59.43425  ? 120 ARG   A CG  1 
ATOM   900  C CD  . ARG   A 1 140 ? -11.06092 31.10134 -5.04562  1.000 66.00138  ? 120 ARG   A CD  1 
ATOM   901  N NE  . ARG   A 1 140 ? -11.49728 30.88840 -6.41908  1.000 74.19966  ? 120 ARG   A NE  1 
ATOM   902  C CZ  . ARG   A 1 140 ? -12.04874 31.82389 -7.18021  1.000 77.91851  ? 120 ARG   A CZ  1 
ATOM   903  N NH1 . ARG   A 1 140 ? -12.28406 33.04095 -6.71786  1.000 61.51860  ? 120 ARG   A NH1 1 
ATOM   904  N NH2 . ARG   A 1 140 ? -12.36609 31.53299 -8.43878  1.000 74.46832  ? 120 ARG   A NH2 1 
ATOM   905  N N   . GLY   A 1 141 ? -7.34256  29.75173 -2.47280  1.000 52.82687  ? 121 GLY   A N   1 
ATOM   906  C CA  . GLY   A 1 141 ? -6.48188  28.63021 -2.80944  1.000 55.91118  ? 121 GLY   A CA  1 
ATOM   907  C C   . GLY   A 1 141 ? -6.98176  27.32094 -2.23164  1.000 55.85970  ? 121 GLY   A C   1 
ATOM   908  O O   . GLY   A 1 141 ? -7.12813  26.32671 -2.94877  1.000 58.17365  ? 121 GLY   A O   1 
ATOM   909  N N   . ASP   A 1 142 ? -7.24300  27.30213 -0.91953  1.000 53.46262  ? 122 ASP   A N   1 
ATOM   910  C CA  . ASP   A 1 142 ? -7.75715  26.09276 -0.27982  1.000 58.75980  ? 122 ASP   A CA  1 
ATOM   911  C C   . ASP   A 1 142 ? -9.05629  25.63026 -0.92811  1.000 59.01702  ? 122 ASP   A C   1 
ATOM   912  O O   . ASP   A 1 142 ? -9.26038  24.42864 -1.14391  1.000 50.25933  ? 122 ASP   A O   1 
ATOM   913  C CB  . ASP   A 1 142 ? -7.97424  26.32790 1.21694   1.000 52.36441  ? 122 ASP   A CB  1 
ATOM   914  C CG  . ASP   A 1 142 ? -6.68676  26.26961 2.01208   1.000 61.75589  ? 122 ASP   A CG  1 
ATOM   915  O OD1 . ASP   A 1 142 ? -6.73665  26.47566 3.24466   1.000 61.20016  ? 122 ASP   A OD1 1 
ATOM   916  O OD2 . ASP   A 1 142 ? -5.62328  26.02584 1.40265   1.000 72.87906  ? 122 ASP   A OD2 1 
ATOM   917  N N   . LEU   A 1 143 ? -9.94292  26.57352 -1.25058  1.000 51.25183  ? 123 LEU   A N   1 
ATOM   918  C CA  . LEU   A 1 143 ? -11.23140 26.22311 -1.83818  1.000 47.66557  ? 123 LEU   A CA  1 
ATOM   919  C C   . LEU   A 1 143 ? -11.05137 25.51258 -3.17525  1.000 56.22028  ? 123 LEU   A C   1 
ATOM   920  O O   . LEU   A 1 143 ? -11.62948 24.44440 -3.40713  1.000 53.62909  ? 123 LEU   A O   1 
ATOM   921  C CB  . LEU   A 1 143 ? -12.08363 27.48429 -1.99461  1.000 50.29231  ? 123 LEU   A CB  1 
ATOM   922  C CG  . LEU   A 1 143 ? -13.45093 27.34769 -2.66485  1.000 52.38619  ? 123 LEU   A CG  1 
ATOM   923  C CD1 . LEU   A 1 143 ? -14.28342 26.29140 -1.96705  1.000 54.97006  ? 123 LEU   A CD1 1 
ATOM   924  C CD2 . LEU   A 1 143 ? -14.17639 28.68474 -2.66776  1.000 50.52870  ? 123 LEU   A CD2 1 
ATOM   925  N N   . ASP   A 1 144 ? -10.23976 26.08653 -4.06602  1.000 59.55201  ? 124 ASP   A N   1 
ATOM   926  C CA  . ASP   A 1 144 ? -10.02478 25.46666 -5.36957  1.000 55.18370  ? 124 ASP   A CA  1 
ATOM   927  C C   . ASP   A 1 144 ? -9.19551  24.19564 -5.24655  1.000 59.32787  ? 124 ASP   A C   1 
ATOM   928  O O   . ASP   A 1 144 ? -9.42337  23.22578 -5.97928  1.000 58.59426  ? 124 ASP   A O   1 
ATOM   929  C CB  . ASP   A 1 144 ? -9.35422  26.45864 -6.31761  1.000 59.88401  ? 124 ASP   A CB  1 
ATOM   930  C CG  . ASP   A 1 144 ? -10.21877 27.67295 -6.59468  1.000 71.65886  ? 124 ASP   A CG  1 
ATOM   931  O OD1 . ASP   A 1 144 ? -11.45751 27.56107 -6.48000  1.000 72.27701  ? 124 ASP   A OD1 1 
ATOM   932  O OD2 . ASP   A 1 144 ? -9.66054  28.73926 -6.92795  1.000 69.42951  ? 124 ASP   A OD2 1 
ATOM   933  N N   . ARG   A 1 145 ? -8.22680  24.18393 -4.32817  1.000 63.52998  ? 125 ARG   A N   1 
ATOM   934  C CA  . ARG   A 1 145 ? -7.44935  22.97364 -4.08642  1.000 56.46324  ? 125 ARG   A CA  1 
ATOM   935  C C   . ARG   A 1 145 ? -8.35077  21.82511 -3.65293  1.000 61.45398  ? 125 ARG   A C   1 
ATOM   936  O O   . ARG   A 1 145 ? -8.19929  20.69088 -4.12298  1.000 52.19702  ? 125 ARG   A O   1 
ATOM   937  C CB  . ARG   A 1 145 ? -6.37668  23.25161 -3.03465  1.000 53.98328  ? 125 ARG   A CB  1 
ATOM   938  C CG  . ARG   A 1 145 ? -5.62824  22.02593 -2.56607  1.000 54.38298  ? 125 ARG   A CG  1 
ATOM   939  C CD  . ARG   A 1 145 ? -4.44269  22.41963 -1.70446  1.000 63.85120  ? 125 ARG   A CD  1 
ATOM   940  N NE  . ARG   A 1 145 ? -3.73490  21.25253 -1.19352  1.000 78.31210  ? 125 ARG   A NE  1 
ATOM   941  C CZ  . ARG   A 1 145 ? -2.84167  20.55777 -1.88462  1.000 78.16237  ? 125 ARG   A CZ  1 
ATOM   942  N NH1 . ARG   A 1 145 ? -2.51553  20.89002 -3.12292  1.000 71.10042  ? 125 ARG   A NH1 1 
ATOM   943  N NH2 . ARG   A 1 145 ? -2.26310  19.50137 -1.32017  1.000 71.02135  ? 125 ARG   A NH2 1 
ATOM   944  N N   . LEU   A 1 146 ? -9.30550  22.10607 -2.76421  1.000 57.21166  ? 126 LEU   A N   1 
ATOM   945  C CA  . LEU   A 1 146 ? -10.28770 21.09732 -2.38405  1.000 56.25482  ? 126 LEU   A CA  1 
ATOM   946  C C   . LEU   A 1 146 ? -11.14016 20.68040 -3.57730  1.000 63.83665  ? 126 LEU   A C   1 
ATOM   947  O O   . LEU   A 1 146 ? -11.49585 19.50318 -3.71691  1.000 54.19546  ? 126 LEU   A O   1 
ATOM   948  C CB  . LEU   A 1 146 ? -11.17051 21.63351 -1.25661  1.000 54.54601  ? 126 LEU   A CB  1 
ATOM   949  C CG  . LEU   A 1 146 ? -12.18738 20.67323 -0.63938  1.000 55.51341  ? 126 LEU   A CG  1 
ATOM   950  C CD1 . LEU   A 1 146 ? -11.49601 19.70768 0.30811   1.000 48.33130  ? 126 LEU   A CD1 1 
ATOM   951  C CD2 . LEU   A 1 146 ? -13.28984 21.43929 0.07646   1.000 52.11909  ? 126 LEU   A CD2 1 
ATOM   952  N N   . LEU   A 1 147 ? -11.47066 21.63250 -4.45396  1.000 58.73751  ? 127 LEU   A N   1 
ATOM   953  C CA  . LEU   A 1 147 ? -12.36012 21.33718 -5.57316  1.000 59.03671  ? 127 LEU   A CA  1 
ATOM   954  C C   . LEU   A 1 147 ? -11.64918 20.54046 -6.66179  1.000 51.89728  ? 127 LEU   A C   1 
ATOM   955  O O   . LEU   A 1 147 ? -12.23805 19.62731 -7.25117  1.000 51.84165  ? 127 LEU   A O   1 
ATOM   956  C CB  . LEU   A 1 147 ? -12.93139 22.63691 -6.14253  1.000 55.63437  ? 127 LEU   A CB  1 
ATOM   957  C CG  . LEU   A 1 147 ? -13.99476 23.35393 -5.30716  1.000 54.64023  ? 127 LEU   A CG  1 
ATOM   958  C CD1 . LEU   A 1 147 ? -14.12762 24.81152 -5.72884  1.000 62.33554  ? 127 LEU   A CD1 1 
ATOM   959  C CD2 . LEU   A 1 147 ? -15.33559 22.64244 -5.41470  1.000 51.82947  ? 127 LEU   A CD2 1 
ATOM   960  N N   . GLU   A 1 148 ? -10.38664 20.86933 -6.94531  1.000 54.75689  ? 128 GLU   A N   1 
ATOM   961  C CA  . GLU   A 1 148 ? -9.67035  20.19739 -8.02287  1.000 55.48694  ? 128 GLU   A CA  1 
ATOM   962  C C   . GLU   A 1 148 ? -9.22284  18.79710 -7.62580  1.000 56.78084  ? 128 GLU   A C   1 
ATOM   963  O O   . GLU   A 1 148 ? -9.11629  17.91808 -8.48807  1.000 57.22222  ? 128 GLU   A O   1 
ATOM   964  C CB  . GLU   A 1 148 ? -8.45988  21.03247 -8.45364  1.000 52.80648  ? 128 GLU   A CB  1 
ATOM   965  C CG  . GLU   A 1 148 ? -7.35547  21.13289 -7.40998  1.000 63.86748  ? 128 GLU   A CG  1 
ATOM   966  C CD  . GLU   A 1 148 ? -6.24398  22.08068 -7.82651  1.000 78.28056  ? 128 GLU   A CD  1 
ATOM   967  O OE1 . GLU   A 1 148 ? -5.16877  22.05904 -7.18831  1.000 75.12960  ? 128 GLU   A OE1 1 
ATOM   968  O OE2 . GLU   A 1 148 ? -6.44495  22.84581 -8.79454  1.000 74.68394  ? 128 GLU   A OE2 1 
ATOM   969  N N   . GLU   A 1 149 ? -8.95857  18.57111 -6.33790  1.000 56.55324  ? 129 GLU   A N   1 
ATOM   970  C CA  . GLU   A 1 149 ? -8.43380  17.29085 -5.88390  1.000 54.81330  ? 129 GLU   A CA  1 
ATOM   971  C C   . GLU   A 1 149 ? -9.53028  16.25633 -5.66249  1.000 46.16725  ? 129 GLU   A C   1 
ATOM   972  O O   . GLU   A 1 149 ? -9.24307  15.05395 -5.67480  1.000 63.47253  ? 129 GLU   A O   1 
ATOM   973  C CB  . GLU   A 1 149 ? -7.62841  17.49842 -4.59646  1.000 50.58594  ? 129 GLU   A CB  1 
ATOM   974  C CG  . GLU   A 1 149 ? -6.40496  16.60955 -4.45940  1.000 74.61553  ? 129 GLU   A CG  1 
ATOM   975  C CD  . GLU   A 1 149 ? -5.33873  17.22567 -3.56687  1.000 72.85730  ? 129 GLU   A CD  1 
ATOM   976  O OE1 . GLU   A 1 149 ? -4.89512  18.35572 -3.86341  1.000 79.26626  ? 129 GLU   A OE1 1 
ATOM   977  O OE2 . GLU   A 1 149 ? -4.95342  16.59039 -2.56169  1.000 71.94652  ? 129 GLU   A OE2 1 
ATOM   978  N N   . LEU   A 1 150 ? -10.77302 16.69365 -5.46151  1.000 56.20901  ? 130 LEU   A N   1 
ATOM   979  C CA  . LEU   A 1 150 ? -11.89138 15.79476 -5.21584  1.000 56.66579  ? 130 LEU   A CA  1 
ATOM   980  C C   . LEU   A 1 150 ? -12.84602 15.68453 -6.39504  1.000 51.38577  ? 130 LEU   A C   1 
ATOM   981  O O   . LEU   A 1 150 ? -13.82034 14.92654 -6.31323  1.000 49.25507  ? 130 LEU   A O   1 
ATOM   982  C CB  . LEU   A 1 150 ? -12.66584 16.25362 -3.97492  1.000 46.05928  ? 130 LEU   A CB  1 
ATOM   983  C CG  . LEU   A 1 150 ? -11.89637 16.25553 -2.65570  1.000 50.16419  ? 130 LEU   A CG  1 
ATOM   984  C CD1 . LEU   A 1 150 ? -12.73645 16.87944 -1.55934  1.000 50.98280  ? 130 LEU   A CD1 1 
ATOM   985  C CD2 . LEU   A 1 150 ? -11.49373 14.83735 -2.28949  1.000 54.94324  ? 130 LEU   A CD2 1 
ATOM   986  N N   . ALA   A 1 151 ? -12.59185 16.41695 -7.48412  1.000 54.50292  ? 131 ALA   A N   1 
ATOM   987  C CA  . ALA   A 1 151 ? -13.54284 16.47862 -8.58909  1.000 55.27977  ? 131 ALA   A CA  1 
ATOM   988  C C   . ALA   A 1 151 ? -13.83561 15.10269 -9.17396  1.000 57.62505  ? 131 ALA   A C   1 
ATOM   989  O O   . ALA   A 1 151 ? -14.95011 14.86015 -9.65077  1.000 57.66183  ? 131 ALA   A O   1 
ATOM   990  C CB  . ALA   A 1 151 ? -13.01722 17.41677 -9.67448  1.000 50.53190  ? 131 ALA   A CB  1 
ATOM   991  N N   . GLU   A 1 152 ? -12.86001 14.19442 -9.14899  1.000 54.05371  ? 132 GLU   A N   1 
ATOM   992  C CA  . GLU   A 1 152 ? -13.03843 12.83881 -9.65393  1.000 67.42037  ? 132 GLU   A CA  1 
ATOM   993  C C   . GLU   A 1 152 ? -13.05092 11.79696 -8.54173  1.000 62.14632  ? 132 GLU   A C   1 
ATOM   994  O O   . GLU   A 1 152 ? -12.94068 10.59941 -8.82793  1.000 68.09833  ? 132 GLU   A O   1 
ATOM   995  C CB  . GLU   A 1 152 ? -11.93860 12.49748 -10.66374 1.000 65.90292  ? 132 GLU   A CB  1 
ATOM   996  C CG  . GLU   A 1 152 ? -11.82356 13.44883 -11.84215 1.000 86.21372  ? 132 GLU   A CG  1 
ATOM   997  C CD  . GLU   A 1 152 ? -12.76831 13.09730 -12.97730 1.000 95.31763  ? 132 GLU   A CD  1 
ATOM   998  O OE1 . GLU   A 1 152 ? -13.89890 13.63184 -13.00599 1.000 91.28543  ? 132 GLU   A OE1 1 
ATOM   999  O OE2 . GLU   A 1 152 ? -12.37754 12.28026 -13.84029 1.000 102.67218 ? 132 GLU   A OE2 1 
ATOM   1000 N N   . ASP   A 1 153 ? -13.16769 12.21700 -7.28522  1.000 61.50581  ? 133 ASP   A N   1 
ATOM   1001 C CA  . ASP   A 1 153 ? -13.12741 11.26230 -6.18773  1.000 49.77668  ? 133 ASP   A CA  1 
ATOM   1002 C C   . ASP   A 1 153 ? -14.44924 10.50184 -6.10577  1.000 59.05664  ? 133 ASP   A C   1 
ATOM   1003 O O   . ASP   A 1 153 ? -15.51284 11.07477 -6.36705  1.000 56.60278  ? 133 ASP   A O   1 
ATOM   1004 C CB  . ASP   A 1 153 ? -12.85485 11.97190 -4.86407  1.000 52.87141  ? 133 ASP   A CB  1 
ATOM   1005 C CG  . ASP   A 1 153 ? -12.44841 11.01066 -3.76556  1.000 53.35249  ? 133 ASP   A CG  1 
ATOM   1006 O OD1 . ASP   A 1 153 ? -11.24486 10.69010 -3.67438  1.000 53.65020  ? 133 ASP   A OD1 1 
ATOM   1007 O OD2 . ASP   A 1 153 ? -13.33027 10.55652 -3.00422  1.000 45.93718  ? 133 ASP   A OD2 1 
ATOM   1008 N N   . PRO   A 1 154 ? -14.42213 9.21303  -5.75033  1.000 53.33745  ? 134 PRO   A N   1 
ATOM   1009 C CA  . PRO   A 1 154 ? -15.68200 8.45668  -5.67814  1.000 57.32508  ? 134 PRO   A CA  1 
ATOM   1010 C C   . PRO   A 1 154 ? -16.59739 8.87284  -4.53576  1.000 57.68301  ? 134 PRO   A C   1 
ATOM   1011 O O   . PRO   A 1 154 ? -17.79966 8.60409  -4.61634  1.000 56.62623  ? 134 PRO   A O   1 
ATOM   1012 C CB  . PRO   A 1 154 ? -15.21570 7.00334  -5.51542  1.000 57.71259  ? 134 PRO   A CB  1 
ATOM   1013 C CG  . PRO   A 1 154 ? -13.83443 7.10530  -4.95896  1.000 51.48423  ? 134 PRO   A CG  1 
ATOM   1014 C CD  . PRO   A 1 154 ? -13.24466 8.34521  -5.55765  1.000 50.93053  ? 134 PRO   A CD  1 
ATOM   1015 N N   . VAL   A 1 155 ? -16.09341 9.50603  -3.47483  1.000 60.67181  ? 135 VAL   A N   1 
ATOM   1016 C CA  . VAL   A 1 155 ? -16.95403 9.84100  -2.33938  1.000 58.06542  ? 135 VAL   A CA  1 
ATOM   1017 C C   . VAL   A 1 155 ? -16.84557 11.32184 -1.98431  1.000 47.72320  ? 135 VAL   A C   1 
ATOM   1018 O O   . VAL   A 1 155 ? -17.83759 11.95411 -1.60860  1.000 46.16261  ? 135 VAL   A O   1 
ATOM   1019 C CB  . VAL   A 1 155 ? -16.64363 8.95767  -1.11011  1.000 55.36677  ? 135 VAL   A CB  1 
ATOM   1020 C CG1 . VAL   A 1 155 ? -16.61330 7.48819  -1.50362  1.000 65.55970  ? 135 VAL   A CG1 1 
ATOM   1021 C CG2 . VAL   A 1 155 ? -15.35183 9.35861  -0.43463  1.000 55.40377  ? 135 VAL   A CG2 1 
ATOM   1022 N N   . GLY   A 1 156 ? -15.65390 11.88627 -2.09878  1.000 50.46118  ? 136 GLY   A N   1 
ATOM   1023 C CA  . GLY   A 1 156 ? -15.38392 13.22860 -1.64790  1.000 45.64394  ? 136 GLY   A CA  1 
ATOM   1024 C C   . GLY   A 1 156 ? -14.29323 13.28194 -0.59695  1.000 50.73412  ? 136 GLY   A C   1 
ATOM   1025 O O   . GLY   A 1 156 ? -13.46311 12.37634 -0.45937  1.000 49.69345  ? 136 GLY   A O   1 
ATOM   1026 N N   . GLY   A 1 157 ? -14.27841 14.39231 0.12449   1.000 54.93756  ? 137 GLY   A N   1 
ATOM   1027 C CA  . GLY   A 1 157 ? -13.29037 14.58642 1.15932   1.000 45.07092  ? 137 GLY   A CA  1 
ATOM   1028 C C   . GLY   A 1 157 ? -13.51107 15.87661 1.90606   1.000 39.98182  ? 137 GLY   A C   1 
ATOM   1029 O O   . GLY   A 1 157 ? -14.61474 16.41678 1.93542   1.000 39.18768  ? 137 GLY   A O   1 
ATOM   1030 N N   . LEU   A 1 158 ? -12.43921 16.36282 2.51267   1.000 41.64174  ? 138 LEU   A N   1 
ATOM   1031 C CA  . LEU   A 1 158 ? -12.52922 17.51797 3.38519   1.000 52.10258  ? 138 LEU   A CA  1 
ATOM   1032 C C   . LEU   A 1 158 ? -11.14117 18.12014 3.52646   1.000 48.40815  ? 138 LEU   A C   1 
ATOM   1033 O O   . LEU   A 1 158 ? -10.12874 17.45435 3.28656   1.000 45.40922  ? 138 LEU   A O   1 
ATOM   1034 C CB  . LEU   A 1 158 ? -13.09193 17.13087 4.75573   1.000 47.93588  ? 138 LEU   A CB  1 
ATOM   1035 C CG  . LEU   A 1 158 ? -12.15710 16.28184 5.62084   1.000 45.76759  ? 138 LEU   A CG  1 
ATOM   1036 C CD1 . LEU   A 1 158 ? -12.38918 16.55671 7.09768   1.000 44.86868  ? 138 LEU   A CD1 1 
ATOM   1037 C CD2 . LEU   A 1 158 ? -12.31245 14.79124 5.32136   1.000 46.17448  ? 138 LEU   A CD2 1 
ATOM   1038 N N   . LEU   A 1 159 ? -11.10875 19.39111 3.92301   1.000 51.48785  ? 139 LEU   A N   1 
ATOM   1039 C CA  . LEU   A 1 159 ? -9.85270  20.05765 4.23053   1.000 47.74714  ? 139 LEU   A CA  1 
ATOM   1040 C C   . LEU   A 1 159 ? -9.38117  19.65788 5.62011   1.000 49.07603  ? 139 LEU   A C   1 
ATOM   1041 O O   . LEU   A 1 159 ? -10.18785 19.48641 6.53890   1.000 47.52520  ? 139 LEU   A O   1 
ATOM   1042 C CB  . LEU   A 1 159 ? -10.00530 21.57537 4.15745   1.000 42.02469  ? 139 LEU   A CB  1 
ATOM   1043 C CG  . LEU   A 1 159 ? -10.00203 22.24972 2.78944   1.000 57.73228  ? 139 LEU   A CG  1 
ATOM   1044 C CD1 . LEU   A 1 159 ? -9.94869  23.75063 2.98528   1.000 50.41057  ? 139 LEU   A CD1 1 
ATOM   1045 C CD2 . LEU   A 1 159 ? -8.82663  21.76390 1.95881   1.000 45.65958  ? 139 LEU   A CD2 1 
ATOM   1046 N N   . ALA   A 1 160 ? -8.06548  19.52063 5.77208   1.000 47.16911  ? 140 ALA   A N   1 
ATOM   1047 C CA  . ALA   A 1 160 ? -7.47892  19.09484 7.03695   1.000 51.02788  ? 140 ALA   A CA  1 
ATOM   1048 C C   . ALA   A 1 160 ? -6.03505  19.57190 7.10133   1.000 46.09897  ? 140 ALA   A C   1 
ATOM   1049 O O   . ALA   A 1 160 ? -5.40993  19.84802 6.07572   1.000 47.04776  ? 140 ALA   A O   1 
ATOM   1050 C CB  . ALA   A 1 160 ? -7.54654  17.57081 7.21379   1.000 46.26541  ? 140 ALA   A CB  1 
ATOM   1051 N N   . VAL   A 1 161 ? -5.51421  19.66886 8.32224   1.000 45.94485  ? 141 VAL   A N   1 
ATOM   1052 C CA  . VAL   A 1 161 ? -4.12623  20.07158 8.55280   1.000 60.24850  ? 141 VAL   A CA  1 
ATOM   1053 C C   . VAL   A 1 161 ? -3.46819  19.04224 9.46758   1.000 60.00784  ? 141 VAL   A C   1 
ATOM   1054 O O   . VAL   A 1 161 ? -4.16003  18.41732 10.28525  1.000 55.71573  ? 141 VAL   A O   1 
ATOM   1055 C CB  . VAL   A 1 161 ? -4.04339  21.48995 9.14504   1.000 48.31866  ? 141 VAL   A CB  1 
ATOM   1056 C CG1 . VAL   A 1 161 ? -4.53195  22.51894 8.13380   1.000 54.40342  ? 141 VAL   A CG1 1 
ATOM   1057 C CG2 . VAL   A 1 161 ? -4.84747  21.58098 10.43198  1.000 53.43293  ? 141 VAL   A CG2 1 
ATOM   1058 N N   . PRO   A 1 162 ? -2.15370  18.82415 9.37043   1.000 67.57759  ? 142 PRO   A N   1 
ATOM   1059 C CA  . PRO   A 1 162 ? -1.50759  17.84023 10.25022  1.000 62.57752  ? 142 PRO   A CA  1 
ATOM   1060 C C   . PRO   A 1 162 ? -1.41512  18.34936 11.68084  1.000 57.37178  ? 142 PRO   A C   1 
ATOM   1061 O O   . PRO   A 1 162 ? -1.19225  19.53760 11.92392  1.000 68.17405  ? 142 PRO   A O   1 
ATOM   1062 C CB  . PRO   A 1 162 ? -0.10985  17.66460 9.63715   1.000 71.13547  ? 142 PRO   A CB  1 
ATOM   1063 C CG  . PRO   A 1 162 ? -0.09940  18.46480 8.36347   1.000 76.66822  ? 142 PRO   A CG  1 
ATOM   1064 C CD  . PRO   A 1 162 ? -1.18654  19.48030 8.47563   1.000 66.62966  ? 142 PRO   A CD  1 
ATOM   1065 N N   . ALA   A 1 163 ? -1.57933  17.43221 12.63150  1.000 55.29908  ? 143 ALA   A N   1 
ATOM   1066 C CA  . ALA   A 1 163 ? -1.43361  17.77868 14.03905  1.000 63.23397  ? 143 ALA   A CA  1 
ATOM   1067 C C   . ALA   A 1 163 ? 0.01985   18.11786 14.35057  1.000 63.99999  ? 143 ALA   A C   1 
ATOM   1068 O O   . ALA   A 1 163 ? 0.92822   17.33223 14.06260  1.000 72.64237  ? 143 ALA   A O   1 
ATOM   1069 C CB  . ALA   A 1 163 ? -1.91194  16.62588 14.91987  1.000 65.35696  ? 143 ALA   A CB  1 
ATOM   1070 N N   . ARG   A 1 164 ? 0.23994   19.29340 14.94080  1.000 60.12185  ? 144 ARG   A N   1 
ATOM   1071 C CA  . ARG   A 1 164 ? 1.58250   19.75854 15.25817  1.000 67.07530  ? 144 ARG   A CA  1 
ATOM   1072 C C   . ARG   A 1 164 ? 1.88822   19.77250 16.74926  1.000 65.22431  ? 144 ARG   A C   1 
ATOM   1073 O O   . ARG   A 1 164 ? 3.04192   20.00919 17.12143  1.000 79.52616  ? 144 ARG   A O   1 
ATOM   1074 C CB  . ARG   A 1 164 ? 1.80954   21.16444 14.67860  1.000 62.68678  ? 144 ARG   A CB  1 
ATOM   1075 C CG  . ARG   A 1 164 ? 1.65119   21.22708 13.16768  1.000 64.58255  ? 144 ARG   A CG  1 
ATOM   1076 C CD  . ARG   A 1 164 ? 1.73323   22.65001 12.64153  1.000 77.33936  ? 144 ARG   A CD  1 
ATOM   1077 N NE  . ARG   A 1 164 ? 1.17770   22.74845 11.29673  1.000 93.38287  ? 144 ARG   A NE  1 
ATOM   1078 C CZ  . ARG   A 1 164 ? 1.87557   22.58422 10.18109  1.000 90.48474  ? 144 ARG   A CZ  1 
ATOM   1079 N NH1 . ARG   A 1 164 ? 3.17626   22.34362 10.20827  1.000 74.13185  ? 144 ARG   A NH1 1 
ATOM   1080 N NH2 . ARG   A 1 164 ? 1.25181   22.66045 9.00837   1.000 89.77352  ? 144 ARG   A NH2 1 
ATOM   1081 N N   . ASP   A 1 165 ? 0.90151   19.53114 17.60605  1.000 58.09147  ? 145 ASP   A N   1 
ATOM   1082 C CA  . ASP   A 1 165 ? 1.11744   19.43062 19.04089  1.000 60.29864  ? 145 ASP   A CA  1 
ATOM   1083 C C   . ASP   A 1 165 ? 1.30864   17.97349 19.44059  1.000 64.06450  ? 145 ASP   A C   1 
ATOM   1084 O O   . ASP   A 1 165 ? 0.77261   17.06019 18.80750  1.000 67.60132  ? 145 ASP   A O   1 
ATOM   1085 C CB  . ASP   A 1 165 ? -0.05702  20.02460 19.81882  1.000 70.70099  ? 145 ASP   A CB  1 
ATOM   1086 C CG  . ASP   A 1 165 ? -0.24271  21.50400 19.55636  1.000 82.02651  ? 145 ASP   A CG  1 
ATOM   1087 O OD1 . ASP   A 1 165 ? -0.30383  21.89680 18.37158  1.000 76.56265  ? 145 ASP   A OD1 1 
ATOM   1088 O OD2 . ASP   A 1 165 ? -0.34182  22.27173 20.53692  1.000 89.70254  ? 145 ASP   A OD2 1 
ATOM   1089 N N   . THR   A 1 166 ? 2.08296   17.76603 20.50187  1.000 59.88811  ? 146 THR   A N   1 
ATOM   1090 C CA  . THR   A 1 166 ? 2.31787   16.42039 21.00655  1.000 59.03235  ? 146 THR   A CA  1 
ATOM   1091 C C   . THR   A 1 166 ? 1.03296   15.84466 21.58980  1.000 58.27302  ? 146 THR   A C   1 
ATOM   1092 O O   . THR   A 1 166 ? 0.41727   16.44147 22.47905  1.000 56.42846  ? 146 THR   A O   1 
ATOM   1093 C CB  . THR   A 1 166 ? 3.42570   16.43408 22.05940  1.000 61.60267  ? 146 THR   A CB  1 
ATOM   1094 O OG1 . THR   A 1 166 ? 4.68717   16.66880 21.42035  1.000 65.29041  ? 146 THR   A OG1 1 
ATOM   1095 C CG2 . THR   A 1 166 ? 3.47996   15.10303 22.80572  1.000 58.83089  ? 146 THR   A CG2 1 
ATOM   1096 N N   . LEU   A 1 167 ? 0.63255   14.68050 21.08547  1.000 55.92953  ? 147 LEU   A N   1 
ATOM   1097 C CA  . LEU   A 1 167 ? -0.60119  14.02126 21.49178  1.000 55.24653  ? 147 LEU   A CA  1 
ATOM   1098 C C   . LEU   A 1 167 ? -0.28194  12.88399 22.45281  1.000 56.85305  ? 147 LEU   A C   1 
ATOM   1099 O O   . LEU   A 1 167 ? 0.61940   12.07950 22.19461  1.000 56.29258  ? 147 LEU   A O   1 
ATOM   1100 C CB  . LEU   A 1 167 ? -1.35489  13.48463 20.27435  1.000 50.82150  ? 147 LEU   A CB  1 
ATOM   1101 C CG  . LEU   A 1 167 ? -1.53992  14.46402 19.11412  1.000 55.11515  ? 147 LEU   A CG  1 
ATOM   1102 C CD1 . LEU   A 1 167 ? -2.02851  13.73295 17.86938  1.000 61.57212  ? 147 LEU   A CD1 1 
ATOM   1103 C CD2 . LEU   A 1 167 ? -2.49164  15.58748 19.50029  1.000 53.08639  ? 147 LEU   A CD2 1 
ATOM   1104 N N   . LYS   A 1 168 ? -1.02486  12.81640 23.55363  1.000 50.69539  ? 148 LYS   A N   1 
ATOM   1105 C CA  . LYS   A 1 168 ? -0.82677  11.79391 24.57117  1.000 48.61590  ? 148 LYS   A CA  1 
ATOM   1106 C C   . LYS   A 1 168 ? -2.15509  11.11153 24.85663  1.000 58.40616  ? 148 LYS   A C   1 
ATOM   1107 O O   . LYS   A 1 168 ? -3.17348  11.78515 25.03769  1.000 58.69252  ? 148 LYS   A O   1 
ATOM   1108 C CB  . LYS   A 1 168 ? -0.25372  12.39989 25.85684  1.000 47.27981  ? 148 LYS   A CB  1 
ATOM   1109 C CG  . LYS   A 1 168 ? 1.06024   13.14158 25.66194  1.000 53.90896  ? 148 LYS   A CG  1 
ATOM   1110 C CD  . LYS   A 1 168 ? 2.20143   12.43353 26.37124  1.000 51.71483  ? 148 LYS   A CD  1 
ATOM   1111 C CE  . LYS   A 1 168 ? 3.49333   13.22953 26.28692  1.000 45.99284  ? 148 LYS   A CE  1 
ATOM   1112 N NZ  . LYS   A 1 168 ? 4.46475   12.62032 25.33996  1.000 56.19401  ? 148 LYS   A NZ  1 
ATOM   1113 N N   . ARG   A 1 169 ? -2.14564  9.78190  24.89181  1.000 60.81041  ? 149 ARG   A N   1 
ATOM   1114 C CA  . ARG   A 1 169 ? -3.33639  9.01327  25.22404  1.000 59.23680  ? 149 ARG   A CA  1 
ATOM   1115 C C   . ARG   A 1 169 ? -3.35681  8.71957  26.71883  1.000 56.87721  ? 149 ARG   A C   1 
ATOM   1116 O O   . ARG   A 1 169 ? -2.32498  8.39778  27.31418  1.000 51.38186  ? 149 ARG   A O   1 
ATOM   1117 C CB  . ARG   A 1 169 ? -3.37822  7.70780  24.42743  1.000 57.67141  ? 149 ARG   A CB  1 
ATOM   1118 C CG  . ARG   A 1 169 ? -4.64830  6.89630  24.63357  1.000 60.44981  ? 149 ARG   A CG  1 
ATOM   1119 C CD  . ARG   A 1 169 ? -4.60110  5.57829  23.87924  1.000 65.79977  ? 149 ARG   A CD  1 
ATOM   1120 N NE  . ARG   A 1 169 ? -4.39531  5.76918  22.44861  1.000 61.34537  ? 149 ARG   A NE  1 
ATOM   1121 C CZ  . ARG   A 1 169 ? -5.37110  5.93939  21.56695  1.000 66.86377  ? 149 ARG   A CZ  1 
ATOM   1122 N NH1 . ARG   A 1 169 ? -6.64170  5.95204  21.93569  1.000 63.56766  ? 149 ARG   A NH1 1 
ATOM   1123 N NH2 . ARG   A 1 169 ? -5.06441  6.09933  20.28261  1.000 68.02339  ? 149 ARG   A NH2 1 
ATOM   1124 N N   . SER   A 1 170 ? -4.53530  8.83383  27.32190  1.000 47.49946  ? 150 SER   A N   1 
ATOM   1125 C CA  . SER   A 1 170 ? -4.69718  8.64840  28.75640  1.000 60.72603  ? 150 SER   A CA  1 
ATOM   1126 C C   . SER   A 1 170 ? -5.31124  7.28784  29.06298  1.000 53.06136  ? 150 SER   A C   1 
ATOM   1127 O O   . SER   A 1 170 ? -6.22489  6.83650  28.36686  1.000 57.52349  ? 150 SER   A O   1 
ATOM   1128 C CB  . SER   A 1 170 ? -5.57500  9.75290  29.34447  1.000 51.49455  ? 150 SER   A CB  1 
ATOM   1129 O OG  . SER   A 1 170 ? -5.89342  9.47103  30.69531  1.000 62.92085  ? 150 SER   A OG  1 
ATOM   1130 N N   . ASP   A 1 171 ? -4.80819  6.63884  30.11242  1.000 53.32999  ? 151 ASP   A N   1 
ATOM   1131 C CA  . ASP   A 1 171 ? -5.42861  5.41871  30.61420  1.000 61.09564  ? 151 ASP   A CA  1 
ATOM   1132 C C   . ASP   A 1 171 ? -6.59794  5.81240  31.51709  1.000 66.80578  ? 151 ASP   A C   1 
ATOM   1133 O O   . ASP   A 1 171 ? -6.99530  6.97902  31.58157  1.000 68.44753  ? 151 ASP   A O   1 
ATOM   1134 C CB  . ASP   A 1 171 ? -4.38908  4.52382  31.30037  1.000 55.82640  ? 151 ASP   A CB  1 
ATOM   1135 C CG  . ASP   A 1 171 ? -3.70740  5.19390  32.50074  1.000 67.79884  ? 151 ASP   A CG  1 
ATOM   1136 O OD1 . ASP   A 1 171 ? -2.74366  4.60986  33.05067  1.000 72.23201  ? 151 ASP   A OD1 1 
ATOM   1137 O OD2 . ASP   A 1 171 ? -4.13910  6.29071  32.91200  1.000 69.28840  ? 151 ASP   A OD2 1 
ATOM   1138 N N   . ARG   A 1 172 ? -7.18794  4.84302  32.20988  1.000 63.23514  ? 152 ARG   A N   1 
ATOM   1139 C CA  . ARG   A 1 172 ? -8.29213  5.17748  33.09806  1.000 78.87021  ? 152 ARG   A CA  1 
ATOM   1140 C C   . ARG   A 1 172 ? -7.82601  5.80695  34.40515  1.000 73.22797  ? 152 ARG   A C   1 
ATOM   1141 O O   . ARG   A 1 172 ? -8.65345  6.35443  35.14289  1.000 70.62257  ? 152 ARG   A O   1 
ATOM   1142 C CB  . ARG   A 1 172 ? -9.13879  3.93518  33.38868  1.000 76.74384  ? 152 ARG   A CB  1 
ATOM   1143 C CG  . ARG   A 1 172 ? -8.37546  2.77590  33.99961  1.000 75.37228  ? 152 ARG   A CG  1 
ATOM   1144 C CD  . ARG   A 1 172 ? -9.32699  1.87355  34.76366  1.000 84.07964  ? 152 ARG   A CD  1 
ATOM   1145 N NE  . ARG   A 1 172 ? -10.62306 1.77938  34.10303  1.000 88.53848  ? 152 ARG   A NE  1 
ATOM   1146 C CZ  . ARG   A 1 172 ? -11.69707 1.21267  34.63545  1.000 87.86745  ? 152 ARG   A CZ  1 
ATOM   1147 N NH1 . ARG   A 1 172 ? -11.66990 0.67973  35.84549  1.000 78.00772  ? 152 ARG   A NH1 1 
ATOM   1148 N NH2 . ARG   A 1 172 ? -12.82853 1.18365  33.93771  1.000 91.21375  ? 152 ARG   A NH2 1 
ATOM   1149 N N   . ASP   A 1 173 ? -6.52899  5.76305  34.69924  1.000 71.59244  ? 153 ASP   A N   1 
ATOM   1150 C CA  . ASP   A 1 173 ? -5.98127  6.34430  35.91554  1.000 66.89935  ? 153 ASP   A CA  1 
ATOM   1151 C C   . ASP   A 1 173 ? -5.40506  7.73773  35.69197  1.000 71.63555  ? 153 ASP   A C   1 
ATOM   1152 O O   . ASP   A 1 173 ? -4.74077  8.27452  36.58617  1.000 68.14731  ? 153 ASP   A O   1 
ATOM   1153 C CB  . ASP   A 1 173 ? -4.91471  5.41656  36.49991  1.000 70.67514  ? 153 ASP   A CB  1 
ATOM   1154 C CG  . ASP   A 1 173 ? -5.44363  4.01871  36.76431  1.000 84.12263  ? 153 ASP   A CG  1 
ATOM   1155 O OD1 . ASP   A 1 173 ? -6.50686  3.89580  37.40951  1.000 86.14471  ? 153 ASP   A OD1 1 
ATOM   1156 O OD2 . ASP   A 1 173 ? -4.80337  3.04471  36.31419  1.000 82.53801  ? 153 ASP   A OD2 1 
ATOM   1157 N N   . GLY   A 1 174 ? -5.64651  8.33554  34.52574  1.000 67.44609  ? 154 GLY   A N   1 
ATOM   1158 C CA  . GLY   A 1 174 ? -5.14637  9.66758  34.25747  1.000 70.48848  ? 154 GLY   A CA  1 
ATOM   1159 C C   . GLY   A 1 174 ? -3.66225  9.74677  33.98383  1.000 65.53842  ? 154 GLY   A C   1 
ATOM   1160 O O   . GLY   A 1 174 ? -3.09738  10.84239 34.01080  1.000 58.57268  ? 154 GLY   A O   1 
ATOM   1161 N N   . ARG   A 1 175 ? -3.00738  8.62202  33.72563  1.000 55.19279  ? 155 ARG   A N   1 
ATOM   1162 C CA  . ARG   A 1 175 ? -1.59172  8.59127  33.40006  1.000 57.86395  ? 155 ARG   A CA  1 
ATOM   1163 C C   . ARG   A 1 175 ? -1.41871  8.32368  31.91058  1.000 55.14903  ? 155 ARG   A C   1 
ATOM   1164 O O   . ARG   A 1 175 ? -2.28032  7.71920  31.26433  1.000 55.28038  ? 155 ARG   A O   1 
ATOM   1165 C CB  . ARG   A 1 175 ? -0.86439  7.52504  34.22435  1.000 56.04307  ? 155 ARG   A CB  1 
ATOM   1166 C CG  . ARG   A 1 175 ? -1.23788  7.53826  35.69843  1.000 49.61962  ? 155 ARG   A CG  1 
ATOM   1167 C CD  . ARG   A 1 175 ? -0.25622  6.73407  36.53335  1.000 51.17236  ? 155 ARG   A CD  1 
ATOM   1168 N NE  . ARG   A 1 175 ? 1.03983   7.39604  36.62350  1.000 60.42254  ? 155 ARG   A NE  1 
ATOM   1169 C CZ  . ARG   A 1 175 ? 1.42674   8.15307  37.64181  1.000 56.63359  ? 155 ARG   A CZ  1 
ATOM   1170 N NH1 . ARG   A 1 175 ? 0.64241   8.35803  38.68858  1.000 55.15706  ? 155 ARG   A NH1 1 
ATOM   1171 N NH2 . ARG   A 1 175 ? 2.62864   8.72264  37.60700  1.000 49.35899  ? 155 ARG   A NH2 1 
ATOM   1172 N N   . VAL   A 1 176 ? -0.29860  8.79430  31.36834  1.000 53.69019  ? 156 VAL   A N   1 
ATOM   1173 C CA  . VAL   A 1 176 ? -0.03965  8.66015  29.93966  1.000 57.25985  ? 156 VAL   A CA  1 
ATOM   1174 C C   . VAL   A 1 176 ? 0.18580   7.19080  29.60740  1.000 56.41371  ? 156 VAL   A C   1 
ATOM   1175 O O   . VAL   A 1 176 ? 1.09336   6.54757  30.14780  1.000 50.04902  ? 156 VAL   A O   1 
ATOM   1176 C CB  . VAL   A 1 176 ? 1.16124   9.51552  29.51668  1.000 57.49849  ? 156 VAL   A CB  1 
ATOM   1177 C CG1 . VAL   A 1 176 ? 1.53708   9.22063  28.07071  1.000 54.53673  ? 156 VAL   A CG1 1 
ATOM   1178 C CG2 . VAL   A 1 176 ? 0.85290   10.99573 29.69511  1.000 41.59555  ? 156 VAL   A CG2 1 
ATOM   1179 N N   . SER   A 1 177 ? -0.64701  6.65143  28.71774  1.000 57.74163  ? 157 SER   A N   1 
ATOM   1180 C CA  . SER   A 1 177 ? -0.46763  5.28676  28.23937  1.000 63.64511  ? 157 SER   A CA  1 
ATOM   1181 C C   . SER   A 1 177 ? 0.43436   5.21847  27.01442  1.000 61.45443  ? 157 SER   A C   1 
ATOM   1182 O O   . SER   A 1 177 ? 1.16682   4.23581  26.84760  1.000 62.45656  ? 157 SER   A O   1 
ATOM   1183 C CB  . SER   A 1 177 ? -1.82681  4.64949  27.92328  1.000 53.78411  ? 157 SER   A CB  1 
ATOM   1184 O OG  . SER   A 1 177 ? -2.61111  5.48358  27.08826  1.000 57.99047  ? 157 SER   A OG  1 
ATOM   1185 N N   . GLU   A 1 178 ? 0.40661   6.24167  26.16236  1.000 54.03424  ? 158 GLU   A N   1 
ATOM   1186 C CA  . GLU   A 1 178 ? 1.27686   6.30413  24.99430  1.000 65.60881  ? 158 GLU   A CA  1 
ATOM   1187 C C   . GLU   A 1 178 ? 1.27123   7.72317  24.44098  1.000 59.46816  ? 158 GLU   A C   1 
ATOM   1188 O O   . GLU   A 1 178 ? 0.33940   8.49857  24.67612  1.000 58.35525  ? 158 GLU   A O   1 
ATOM   1189 C CB  . GLU   A 1 178 ? 0.83642   5.32103  23.90455  1.000 56.45313  ? 158 GLU   A CB  1 
ATOM   1190 C CG  . GLU   A 1 178 ? -0.16919  5.91275  22.92523  1.000 71.58415  ? 158 GLU   A CG  1 
ATOM   1191 C CD  . GLU   A 1 178 ? -0.46148  4.99900  21.75250  1.000 81.82337  ? 158 GLU   A CD  1 
ATOM   1192 O OE1 . GLU   A 1 178 ? -1.18235  3.99727  21.94355  1.000 88.84740  ? 158 GLU   A OE1 1 
ATOM   1193 O OE2 . GLU   A 1 178 ? 0.03057   5.28406  20.63927  1.000 83.07624  ? 158 GLU   A OE2 1 
ATOM   1194 N N   . THR   A 1 179 ? 2.32969   8.05087  23.70243  1.000 61.07958  ? 159 THR   A N   1 
ATOM   1195 C CA  . THR   A 1 179 ? 2.37432   9.25188  22.87592  1.000 61.41718  ? 159 THR   A CA  1 
ATOM   1196 C C   . THR   A 1 179 ? 1.93407   8.87318  21.46720  1.000 67.98007  ? 159 THR   A C   1 
ATOM   1197 O O   . THR   A 1 179 ? 2.60636   8.08492  20.79183  1.000 60.76410  ? 159 THR   A O   1 
ATOM   1198 C CB  . THR   A 1 179 ? 3.77122   9.87314  22.84848  1.000 58.57042  ? 159 THR   A CB  1 
ATOM   1199 O OG1 . THR   A 1 179 ? 4.06981   10.44258 24.12812  1.000 60.16084  ? 159 THR   A OG1 1 
ATOM   1200 C CG2 . THR   A 1 179 ? 3.85125   10.96091 21.78528  1.000 57.07719  ? 159 THR   A CG2 1 
ATOM   1201 N N   . ILE   A 1 180 ? 0.81028   9.43812  21.02794  1.000 65.30375  ? 160 ILE   A N   1 
ATOM   1202 C CA  . ILE   A 1 180 ? 0.21644   9.04878  19.75533  1.000 64.10372  ? 160 ILE   A CA  1 
ATOM   1203 C C   . ILE   A 1 180 ? 1.09913   9.52420  18.60997  1.000 53.08337  ? 160 ILE   A C   1 
ATOM   1204 O O   . ILE   A 1 180 ? 1.57971   10.66565 18.60430  1.000 57.88651  ? 160 ILE   A O   1 
ATOM   1205 C CB  . ILE   A 1 180 ? -1.20840  9.60959  19.64025  1.000 61.71520  ? 160 ILE   A CB  1 
ATOM   1206 C CG1 . ILE   A 1 180 ? -2.06150  9.10926  20.80906  1.000 63.52539  ? 160 ILE   A CG1 1 
ATOM   1207 C CG2 . ILE   A 1 180 ? -1.83088  9.22690  18.30313  1.000 56.34680  ? 160 ILE   A CG2 1 
ATOM   1208 C CD1 . ILE   A 1 180 ? -3.36536  9.84794  20.97702  1.000 53.13568  ? 160 ILE   A CD1 1 
ATOM   1209 N N   . ASP   A 1 181 ? 1.32917   8.64096  17.64015  1.000 57.76526  ? 161 ASP   A N   1 
ATOM   1210 C CA  . ASP   A 1 181 ? 2.08952   8.98346  16.44065  1.000 58.66023  ? 161 ASP   A CA  1 
ATOM   1211 C C   . ASP   A 1 181 ? 1.27744   9.97689  15.62166  1.000 57.19699  ? 161 ASP   A C   1 
ATOM   1212 O O   . ASP   A 1 181 ? 0.37875   9.59608  14.86688  1.000 62.74867  ? 161 ASP   A O   1 
ATOM   1213 C CB  . ASP   A 1 181 ? 2.41154   7.73245  15.63074  1.000 57.66504  ? 161 ASP   A CB  1 
ATOM   1214 C CG  . ASP   A 1 181 ? 3.27840   8.02890  14.41720  1.000 69.40337  ? 161 ASP   A CG  1 
ATOM   1215 O OD1 . ASP   A 1 181 ? 3.86424   9.13042  14.35055  1.000 77.43186  ? 161 ASP   A OD1 1 
ATOM   1216 O OD2 . ASP   A 1 181 ? 3.37081   7.16072  13.52561  1.000 75.14134  ? 161 ASP   A OD2 1 
ATOM   1217 N N   . ARG   A 1 182 ? 1.59721   11.26154 15.76625  1.000 61.29003  ? 162 ARG   A N   1 
ATOM   1218 C CA  . ARG   A 1 182 ? 0.84195   12.31163 15.09820  1.000 66.55943  ? 162 ARG   A CA  1 
ATOM   1219 C C   . ARG   A 1 182 ? 1.18425   12.45225 13.62071  1.000 66.96940  ? 162 ARG   A C   1 
ATOM   1220 O O   . ARG   A 1 182 ? 0.61640   13.32602 12.95581  1.000 68.37872  ? 162 ARG   A O   1 
ATOM   1221 C CB  . ARG   A 1 182 ? 1.05388   13.64786 15.81477  1.000 62.04221  ? 162 ARG   A CB  1 
ATOM   1222 C CG  . ARG   A 1 182 ? 2.47643   13.89067 16.29377  1.000 67.52361  ? 162 ARG   A CG  1 
ATOM   1223 C CD  . ARG   A 1 182 ? 2.62360   15.30785 16.79033  1.000 67.86918  ? 162 ARG   A CD  1 
ATOM   1224 N NE  . ARG   A 1 182 ? 4.00264   15.78055 16.75117  1.000 67.72962  ? 162 ARG   A NE  1 
ATOM   1225 C CZ  . ARG   A 1 182 ? 4.54258   16.44923 15.74070  1.000 62.94523  ? 162 ARG   A CZ  1 
ATOM   1226 N NH1 . ARG   A 1 182 ? 3.84528   16.75014 14.65769  1.000 72.43180  ? 162 ARG   A NH1 1 
ATOM   1227 N NH2 . ARG   A 1 182 ? 5.81333   16.83528 15.82513  1.000 75.84918  ? 162 ARG   A NH2 1 
ATOM   1228 N N   . SER   A 1 183 ? 2.08176   11.61769 13.08887  1.000 67.12851  ? 163 SER   A N   1 
ATOM   1229 C CA  . SER   A 1 183 ? 2.36363   11.65340 11.66002  1.000 66.05334  ? 163 SER   A CA  1 
ATOM   1230 C C   . SER   A 1 183 ? 1.18417   11.16231 10.83242  1.000 63.00654  ? 163 SER   A C   1 
ATOM   1231 O O   . SER   A 1 183 ? 1.13419   11.43106 9.62809   1.000 72.77695  ? 163 SER   A O   1 
ATOM   1232 C CB  . SER   A 1 183 ? 3.60859   10.82216 11.34475  1.000 63.74831  ? 163 SER   A CB  1 
ATOM   1233 O OG  . SER   A 1 183 ? 3.40719   9.45231  11.65111  1.000 76.90159  ? 163 SER   A OG  1 
ATOM   1234 N N   . VAL   A 1 184 ? 0.24055   10.44950 11.44673  1.000 64.43104  ? 164 VAL   A N   1 
ATOM   1235 C CA  . VAL   A 1 184 ? -0.96867  9.98938  10.77401  1.000 65.77121  ? 164 VAL   A CA  1 
ATOM   1236 C C   . VAL   A 1 184 ? -2.21528  10.69565 11.27555  1.000 57.10616  ? 164 VAL   A C   1 
ATOM   1237 O O   . VAL   A 1 184 ? -3.32706  10.33749 10.85722  1.000 62.65215  ? 164 VAL   A O   1 
ATOM   1238 C CB  . VAL   A 1 184 ? -1.13692  8.46310  10.90348  1.000 66.82617  ? 164 VAL   A CB  1 
ATOM   1239 C CG1 . VAL   A 1 184 ? -0.11520  7.73518  10.03983  1.000 71.50272  ? 164 VAL   A CG1 1 
ATOM   1240 C CG2 . VAL   A 1 184 ? -1.02062  8.03685  12.36230  1.000 63.68304  ? 164 VAL   A CG2 1 
ATOM   1241 N N   . VAL   A 1 185 ? -2.07323  11.68748 12.15183  1.000 53.27515  ? 165 VAL   A N   1 
ATOM   1242 C CA  . VAL   A 1 185 ? -3.20544  12.37917 12.75837  1.000 56.97058  ? 165 VAL   A CA  1 
ATOM   1243 C C   . VAL   A 1 185 ? -3.38039  13.72988 12.07918  1.000 52.12224  ? 165 VAL   A C   1 
ATOM   1244 O O   . VAL   A 1 185 ? -2.42350  14.50595 11.96331  1.000 58.52639  ? 165 VAL   A O   1 
ATOM   1245 C CB  . VAL   A 1 185 ? -3.00710  12.54754 14.27449  1.000 53.31095  ? 165 VAL   A CB  1 
ATOM   1246 C CG1 . VAL   A 1 185 ? -4.21468  13.23853 14.89527  1.000 43.43714  ? 165 VAL   A CG1 1 
ATOM   1247 C CG2 . VAL   A 1 185 ? -2.75411  11.19559 14.92724  1.000 56.79016  ? 165 VAL   A CG2 1 
ATOM   1248 N N   . TRP   A 1 186 ? -4.60269  14.01391 11.63762  1.000 53.32796  ? 166 TRP   A N   1 
ATOM   1249 C CA  . TRP   A 1 186 ? -4.94473  15.27114 10.99056  1.000 55.30216  ? 166 TRP   A CA  1 
ATOM   1250 C C   . TRP   A 1 186 ? -6.09890  15.92721 11.73373  1.000 50.74080  ? 166 TRP   A C   1 
ATOM   1251 O O   . TRP   A 1 186 ? -7.01814  15.24510 12.19983  1.000 54.51909  ? 166 TRP   A O   1 
ATOM   1252 C CB  . TRP   A 1 186 ? -5.33095  15.05260 9.52245   1.000 54.42311  ? 166 TRP   A CB  1 
ATOM   1253 C CG  . TRP   A 1 186 ? -4.23077  14.50002 8.67981   1.000 61.94946  ? 166 TRP   A CG  1 
ATOM   1254 C CD1 . TRP   A 1 186 ? -3.77019  13.21791 8.67402   1.000 67.74548  ? 166 TRP   A CD1 1 
ATOM   1255 C CD2 . TRP   A 1 186 ? -3.45746  15.21089 7.70571   1.000 65.35043  ? 166 TRP   A CD2 1 
ATOM   1256 N NE1 . TRP   A 1 186 ? -2.75200  13.08624 7.76222   1.000 77.05471  ? 166 TRP   A NE1 1 
ATOM   1257 C CE2 . TRP   A 1 186 ? -2.54086  14.29581 7.15359   1.000 69.17065  ? 166 TRP   A CE2 1 
ATOM   1258 C CE3 . TRP   A 1 186 ? -3.44902  16.53379 7.25024   1.000 70.88241  ? 166 TRP   A CE3 1 
ATOM   1259 C CZ2 . TRP   A 1 186 ? -1.62455  14.65926 6.16854   1.000 72.87409  ? 166 TRP   A CZ2 1 
ATOM   1260 C CZ3 . TRP   A 1 186 ? -2.53701  16.89486 6.27593   1.000 64.04059  ? 166 TRP   A CZ3 1 
ATOM   1261 C CH2 . TRP   A 1 186 ? -1.63900  15.95998 5.74282   1.000 74.78925  ? 166 TRP   A CH2 1 
ATOM   1262 N N   . LEU   A 1 187 ? -6.04568  17.25002 11.85202  1.000 55.98416  ? 167 LEU   A N   1 
ATOM   1263 C CA  . LEU   A 1 187 ? -7.17383  17.99367 12.39167  1.000 50.39090  ? 167 LEU   A CA  1 
ATOM   1264 C C   . LEU   A 1 187 ? -8.19495  18.23552 11.28684  1.000 51.64686  ? 167 LEU   A C   1 
ATOM   1265 O O   . LEU   A 1 187 ? -7.84695  18.70976 10.20100  1.000 54.54575  ? 167 LEU   A O   1 
ATOM   1266 C CB  . LEU   A 1 187 ? -6.71625  19.32264 12.99043  1.000 51.65312  ? 167 LEU   A CB  1 
ATOM   1267 C CG  . LEU   A 1 187 ? -5.61764  19.28463 14.05302  1.000 60.05151  ? 167 LEU   A CG  1 
ATOM   1268 C CD1 . LEU   A 1 187 ? -5.39351  20.68170 14.63532  1.000 64.25127  ? 167 LEU   A CD1 1 
ATOM   1269 C CD2 . LEU   A 1 187 ? -5.92212  18.27201 15.15185  1.000 58.71407  ? 167 LEU   A CD2 1 
ATOM   1270 N N   . ALA   A 1 188 ? -9.45492  17.91495 11.56569  1.000 48.25230  ? 168 ALA   A N   1 
ATOM   1271 C CA  . ALA   A 1 188 ? -10.51488 18.06147 10.57728  1.000 47.15573  ? 168 ALA   A CA  1 
ATOM   1272 C C   . ALA   A 1 188 ? -10.95742 19.51764 10.50631  1.000 55.14363  ? 168 ALA   A C   1 
ATOM   1273 O O   . ALA   A 1 188 ? -11.37457 20.09579 11.51616  1.000 54.03391  ? 168 ALA   A O   1 
ATOM   1274 C CB  . ALA   A 1 188 ? -11.69363 17.15649 10.92444  1.000 43.02470  ? 168 ALA   A CB  1 
ATOM   1275 N N   . TYR   A 1 189 ? -10.86634 20.10576 9.31586   1.000 49.52698  ? 169 TYR   A N   1 
ATOM   1276 C CA  . TYR   A 1 189 ? -11.33940 21.45254 9.03978   1.000 52.00982  ? 169 TYR   A CA  1 
ATOM   1277 C C   . TYR   A 1 189 ? -12.52317 21.39028 8.07507   1.000 49.79442  ? 169 TYR   A C   1 
ATOM   1278 O O   . TYR   A 1 189 ? -13.02939 20.31334 7.74161   1.000 49.95290  ? 169 TYR   A O   1 
ATOM   1279 C CB  . TYR   A 1 189 ? -10.20919 22.31842 8.47228   1.000 47.03864  ? 169 TYR   A CB  1 
ATOM   1280 C CG  . TYR   A 1 189 ? -9.24158  22.86819 9.50000   1.000 58.55997  ? 169 TYR   A CG  1 
ATOM   1281 C CD1 . TYR   A 1 189 ? -9.12877  22.29615 10.76094  1.000 55.77918  ? 169 TYR   A CD1 1 
ATOM   1282 C CD2 . TYR   A 1 189 ? -8.44989  23.97402 9.20966   1.000 54.41835  ? 169 TYR   A CD2 1 
ATOM   1283 C CE1 . TYR   A 1 189 ? -8.24713  22.80096 11.69922  1.000 56.78309  ? 169 TYR   A CE1 1 
ATOM   1284 C CE2 . TYR   A 1 189 ? -7.56676  24.48690 10.14086  1.000 53.22868  ? 169 TYR   A CE2 1 
ATOM   1285 C CZ  . TYR   A 1 189 ? -7.46925  23.89612 11.38404  1.000 56.31131  ? 169 TYR   A CZ  1 
ATOM   1286 O OH  . TYR   A 1 189 ? -6.59176  24.40162 12.31478  1.000 61.17897  ? 169 TYR   A OH  1 
ATOM   1287 N N   . THR   A 1 190 ? -12.96388 22.55576 7.62654   1.000 52.32683  ? 170 THR   A N   1 
ATOM   1288 C CA  . THR   A 1 190 ? -13.99250 22.70546 6.60804   1.000 45.23925  ? 170 THR   A CA  1 
ATOM   1289 C C   . THR   A 1 190 ? -13.44976 23.62799 5.52627   1.000 45.72880  ? 170 THR   A C   1 
ATOM   1290 O O   . THR   A 1 190 ? -12.49368 24.37237 5.76511   1.000 53.14308  ? 170 THR   A O   1 
ATOM   1291 C CB  . THR   A 1 190 ? -15.29351 23.27266 7.20119   1.000 48.28925  ? 170 THR   A CB  1 
ATOM   1292 O OG1 . THR   A 1 190 ? -15.10973 24.64784 7.55615   1.000 58.00082  ? 170 THR   A OG1 1 
ATOM   1293 C CG2 . THR   A 1 190 ? -15.71448 22.48295 8.43179   1.000 46.90368  ? 170 THR   A CG2 1 
ATOM   1294 N N   . PRO   A 1 191 ? -14.03775 23.60916 4.31326   1.000 41.72885  ? 171 PRO   A N   1 
ATOM   1295 C CA  . PRO   A 1 191 ? -15.22991 22.87526 3.85017   1.000 49.96304  ? 171 PRO   A CA  1 
ATOM   1296 C C   . PRO   A 1 191 ? -15.05529 21.36375 3.76376   1.000 53.20238  ? 171 PRO   A C   1 
ATOM   1297 O O   . PRO   A 1 191 ? -13.94894 20.82887 3.76514   1.000 44.07316  ? 171 PRO   A O   1 
ATOM   1298 C CB  . PRO   A 1 191 ? -15.48557 23.46763 2.45022   1.000 49.63733  ? 171 PRO   A CB  1 
ATOM   1299 C CG  . PRO   A 1 191 ? -14.72300 24.75507 2.40991   1.000 41.27493  ? 171 PRO   A CG  1 
ATOM   1300 C CD  . PRO   A 1 191 ? -13.51754 24.48998 3.25523   1.000 47.12123  ? 171 PRO   A CD  1 
ATOM   1301 N N   . GLN   A 1 192 ? -16.17976 20.65998 3.70566   1.000 46.47865  ? 172 GLN   A N   1 
ATOM   1302 C CA  . GLN   A 1 192 ? -16.22133 19.23518 3.42514   1.000 50.11240  ? 172 GLN   A CA  1 
ATOM   1303 C C   . GLN   A 1 192 ? -17.08812 19.02909 2.19282   1.000 51.71626  ? 172 GLN   A C   1 
ATOM   1304 O O   . GLN   A 1 192 ? -18.12753 19.67904 2.04241   1.000 47.99213  ? 172 GLN   A O   1 
ATOM   1305 C CB  . GLN   A 1 192 ? -16.76329 18.45422 4.62558   1.000 47.16644  ? 172 GLN   A CB  1 
ATOM   1306 C CG  . GLN   A 1 192 ? -16.07256 18.83012 5.93063   1.000 40.62820  ? 172 GLN   A CG  1 
ATOM   1307 C CD  . GLN   A 1 192 ? -16.44583 17.92066 7.08152   1.000 50.55181  ? 172 GLN   A CD  1 
ATOM   1308 O OE1 . GLN   A 1 192 ? -17.40306 17.15178 6.99732   1.000 54.94959  ? 172 GLN   A OE1 1 
ATOM   1309 N NE2 . GLN   A 1 192 ? -15.68406 18.00013 8.16585   1.000 43.17042  ? 172 GLN   A NE2 1 
ATOM   1310 N N   . MET   A 1 193 ? -16.65262 18.13274 1.30929   1.000 57.96380  ? 173 MET   A N   1 
ATOM   1311 C CA  . MET   A 1 193 ? -17.17484 18.03878 -0.05121  1.000 49.30404  ? 173 MET   A CA  1 
ATOM   1312 C C   . MET   A 1 193 ? -17.68306 16.62307 -0.30193  1.000 46.76648  ? 173 MET   A C   1 
ATOM   1313 O O   . MET   A 1 193 ? -16.89413 15.67192 -0.34226  1.000 42.93767  ? 173 MET   A O   1 
ATOM   1314 C CB  . MET   A 1 193 ? -16.08571 18.43235 -1.04840  1.000 49.95489  ? 173 MET   A CB  1 
ATOM   1315 C CG  . MET   A 1 193 ? -16.45884 18.36229 -2.51149  1.000 49.24387  ? 173 MET   A CG  1 
ATOM   1316 S SD  . MET   A 1 193 ? -15.10708 19.03080 -3.50898  1.000 55.38537  ? 173 MET   A SD  1 
ATOM   1317 C CE  . MET   A 1 193 ? -15.59610 18.49769 -5.15125  1.000 59.99188  ? 173 MET   A CE  1 
ATOM   1318 N N   . PHE   A 1 194 ? -18.99878 16.48732 -0.47051  1.000 39.33445  ? 174 PHE   A N   1 
ATOM   1319 C CA  . PHE   A 1 194 ? -19.62738 15.19745 -0.71494  1.000 55.39819  ? 174 PHE   A CA  1 
ATOM   1320 C C   . PHE   A 1 194 ? -20.74720 15.36247 -1.73265  1.000 53.39864  ? 174 PHE   A C   1 
ATOM   1321 O O   . PHE   A 1 194 ? -21.25169 16.46591 -1.95689  1.000 58.45912  ? 174 PHE   A O   1 
ATOM   1322 C CB  . PHE   A 1 194 ? -20.18038 14.57897 0.57894   1.000 49.05488  ? 174 PHE   A CB  1 
ATOM   1323 C CG  . PHE   A 1 194 ? -19.13640 14.34224 1.63048   1.000 54.88018  ? 174 PHE   A CG  1 
ATOM   1324 C CD1 . PHE   A 1 194 ? -18.17856 13.35723 1.46224   1.000 46.69275  ? 174 PHE   A CD1 1 
ATOM   1325 C CD2 . PHE   A 1 194 ? -19.11350 15.10299 2.78743   1.000 48.77805  ? 174 PHE   A CD2 1 
ATOM   1326 C CE1 . PHE   A 1 194 ? -17.21357 13.13541 2.42660   1.000 48.51296  ? 174 PHE   A CE1 1 
ATOM   1327 C CE2 . PHE   A 1 194 ? -18.15205 14.88523 3.75727   1.000 52.04588  ? 174 PHE   A CE2 1 
ATOM   1328 C CZ  . PHE   A 1 194 ? -17.20102 13.90025 3.57683   1.000 47.50246  ? 174 PHE   A CZ  1 
ATOM   1329 N N   . ARG   A 1 195 ? -21.12592 14.24490 -2.35155  1.000 43.93686  ? 175 ARG   A N   1 
ATOM   1330 C CA  . ARG   A 1 195 ? -22.25020 14.22920 -3.27657  1.000 46.97039  ? 175 ARG   A CA  1 
ATOM   1331 C C   . ARG   A 1 195 ? -23.56073 14.41679 -2.52155  1.000 50.21072  ? 175 ARG   A C   1 
ATOM   1332 O O   . ARG   A 1 195 ? -23.74875 13.89391 -1.41931  1.000 50.93725  ? 175 ARG   A O   1 
ATOM   1333 C CB  . ARG   A 1 195 ? -22.28620 12.91329 -4.05561  1.000 52.60858  ? 175 ARG   A CB  1 
ATOM   1334 C CG  . ARG   A 1 195 ? -21.04502 12.62587 -4.89822  1.000 55.35977  ? 175 ARG   A CG  1 
ATOM   1335 C CD  . ARG   A 1 195 ? -21.11805 13.30899 -6.25778  1.000 58.20913  ? 175 ARG   A CD  1 
ATOM   1336 N NE  . ARG   A 1 195 ? -19.94202 13.03586 -7.07647  1.000 62.61827  ? 175 ARG   A NE  1 
ATOM   1337 C CZ  . ARG   A 1 195 ? -19.75492 13.50796 -8.30209  1.000 71.64683  ? 175 ARG   A CZ  1 
ATOM   1338 N NH1 . ARG   A 1 195 ? -20.65814 14.27225 -8.89469  1.000 69.38139  ? 175 ARG   A NH1 1 
ATOM   1339 N NH2 . ARG   A 1 195 ? -18.63265 13.20697 -8.94917  1.000 61.58893  ? 175 ARG   A NH2 1 
ATOM   1340 N N   . LEU   A 1 196 ? -24.48021 15.16310 -3.13842  1.000 54.18076  ? 176 LEU   A N   1 
ATOM   1341 C CA  . LEU   A 1 196 ? -25.71954 15.52954 -2.45682  1.000 54.25166  ? 176 LEU   A CA  1 
ATOM   1342 C C   . LEU   A 1 196 ? -26.51929 14.29837 -2.04767  1.000 54.28189  ? 176 LEU   A C   1 
ATOM   1343 O O   . LEU   A 1 196 ? -27.00174 14.20861 -0.91253  1.000 48.65087  ? 176 LEU   A O   1 
ATOM   1344 C CB  . LEU   A 1 196 ? -26.56354 16.44143 -3.34729  1.000 57.45913  ? 176 LEU   A CB  1 
ATOM   1345 C CG  . LEU   A 1 196 ? -27.76943 17.12322 -2.68413  1.000 59.89056  ? 176 LEU   A CG  1 
ATOM   1346 C CD1 . LEU   A 1 196 ? -28.00504 18.49494 -3.29281  1.000 53.16241  ? 176 LEU   A CD1 1 
ATOM   1347 C CD2 . LEU   A 1 196 ? -29.02913 16.27569 -2.81005  1.000 51.68881  ? 176 LEU   A CD2 1 
ATOM   1348 N N   . GLY   A 1 197 ? -26.68145 13.34269 -2.96393  1.000 50.92062  ? 177 GLY   A N   1 
ATOM   1349 C CA  . GLY   A 1 197 ? -27.49326 12.17544 -2.65758  1.000 51.43170  ? 177 GLY   A CA  1 
ATOM   1350 C C   . GLY   A 1 197 ? -26.90582 11.32659 -1.54562  1.000 46.14588  ? 177 GLY   A C   1 
ATOM   1351 O O   . GLY   A 1 197 ? -27.60561 10.95271 -0.60046  1.000 51.83679  ? 177 GLY   A O   1 
ATOM   1352 N N   . ALA   A 1 198 ? -25.60782 11.01987 -1.64046  1.000 45.87833  ? 178 ALA   A N   1 
ATOM   1353 C CA  . ALA   A 1 198 ? -24.96218 10.16781 -0.64530  1.000 50.85904  ? 178 ALA   A CA  1 
ATOM   1354 C C   . ALA   A 1 198 ? -24.96833 10.81551 0.73470   1.000 55.59232  ? 178 ALA   A C   1 
ATOM   1355 O O   . ALA   A 1 198 ? -25.27365 10.15794 1.73547   1.000 44.27666  ? 178 ALA   A O   1 
ATOM   1356 C CB  . ALA   A 1 198 ? -23.52997 9.85036  -1.07729  1.000 44.55737  ? 178 ALA   A CB  1 
ATOM   1357 N N   . LEU   A 1 199 ? -24.62324 12.10252 0.81220   1.000 54.22964  ? 179 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 199 ? -24.63077 12.78683 2.10094   1.000 41.57893  ? 179 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 199 ? -26.03683 12.83335 2.68051   1.000 43.22674  ? 179 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 199 ? -26.22696 12.64572 3.88649   1.000 44.24633  ? 179 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 199 ? -24.05844 14.19552 1.94576   1.000 51.94649  ? 179 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 199 ? -23.93733 15.05260 3.20349   1.000 51.08978  ? 179 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 199 ? -23.02609 14.38959 4.22670   1.000 38.05957  ? 179 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 199 ? -23.43088 16.44028 2.84365   1.000 42.09277  ? 179 LEU   A CD2 1 
ATOM   1365 N N   . HIS   A 1 200 ? -27.03811 13.05814 1.82950   1.000 46.51444  ? 180 HIS   A N   1 
ATOM   1366 C CA  . HIS   A 1 200 ? -28.42140 13.07722 2.29459   1.000 48.20021  ? 180 HIS   A CA  1 
ATOM   1367 C C   . HIS   A 1 200 ? -28.79895 11.75506 2.95349   1.000 53.26635  ? 180 HIS   A C   1 
ATOM   1368 O O   . HIS   A 1 200 ? -29.40053 11.73413 4.03406   1.000 53.72605  ? 180 HIS   A O   1 
ATOM   1369 C CB  . HIS   A 1 200 ? -29.35479 13.38175 1.12462   1.000 46.87381  ? 180 HIS   A CB  1 
ATOM   1370 C CG  . HIS   A 1 200 ? -30.79903 13.48958 1.50920   1.000 59.01453  ? 180 HIS   A CG  1 
ATOM   1371 N ND1 . HIS   A 1 200 ? -31.79836 13.68711 0.58129   1.000 72.72780  ? 180 HIS   A ND1 1 
ATOM   1372 C CD2 . HIS   A 1 200 ? -31.41458 13.42667 2.71443   1.000 64.41922  ? 180 HIS   A CD2 1 
ATOM   1373 C CE1 . HIS   A 1 200 ? -32.96626 13.73913 1.19696   1.000 69.57427  ? 180 HIS   A CE1 1 
ATOM   1374 N NE2 . HIS   A 1 200 ? -32.76135 13.58268 2.49227   1.000 67.01814  ? 180 HIS   A NE2 1 
ATOM   1375 N N   . ARG   A 1 201 ? -28.44221 10.63599 2.31942   1.000 51.24666  ? 181 ARG   A N   1 
ATOM   1376 C CA  . ARG   A 1 201 ? -28.76598 9.33183  2.89061   1.000 53.84745  ? 181 ARG   A CA  1 
ATOM   1377 C C   . ARG   A 1 201 ? -27.94857 9.06696  4.14834   1.000 50.24432  ? 181 ARG   A C   1 
ATOM   1378 O O   . ARG   A 1 201 ? -28.47380 8.56068  5.14907   1.000 59.15292  ? 181 ARG   A O   1 
ATOM   1379 C CB  . ARG   A 1 201 ? -28.52748 8.22584  1.85649   1.000 55.27375  ? 181 ARG   A CB  1 
ATOM   1380 C CG  . ARG   A 1 201 ? -29.42719 8.29542  0.61938   1.000 57.75152  ? 181 ARG   A CG  1 
ATOM   1381 C CD  . ARG   A 1 201 ? -29.25461 7.05978  -0.27012  1.000 65.27701  ? 181 ARG   A CD  1 
ATOM   1382 N NE  . ARG   A 1 201 ? -27.96088 7.05890  -0.94077  1.000 66.45464  ? 181 ARG   A NE  1 
ATOM   1383 C CZ  . ARG   A 1 201 ? -27.70809 7.69981  -2.07305  1.000 63.64179  ? 181 ARG   A CZ  1 
ATOM   1384 N NH1 . ARG   A 1 201 ? -28.64899 8.38580  -2.70358  1.000 68.88644  ? 181 ARG   A NH1 1 
ATOM   1385 N NH2 . ARG   A 1 201 ? -26.47813 7.66228  -2.57819  1.000 65.16127  ? 181 ARG   A NH2 1 
ATOM   1386 N N   . ALA   A 1 202 ? -26.66000 9.41107  4.11627   1.000 43.96957  ? 182 ALA   A N   1 
ATOM   1387 C CA  . ALA   A 1 202 ? -25.79737 9.16340  5.26778   1.000 49.64184  ? 182 ALA   A CA  1 
ATOM   1388 C C   . ALA   A 1 202 ? -26.24707 9.96236  6.48566   1.000 50.83260  ? 182 ALA   A C   1 
ATOM   1389 O O   . ALA   A 1 202 ? -26.32776 9.42088  7.59552   1.000 51.37967  ? 182 ALA   A O   1 
ATOM   1390 C CB  . ALA   A 1 202 ? -24.34504 9.49255  4.92129   1.000 45.69176  ? 182 ALA   A CB  1 
ATOM   1391 N N   . LEU   A 1 203 ? -26.55241 11.24868 6.29614   1.000 50.86515  ? 183 LEU   A N   1 
ATOM   1392 C CA  . LEU   A 1 203 ? -26.95968 12.08916 7.41674   1.000 49.55685  ? 183 LEU   A CA  1 
ATOM   1393 C C   . LEU   A 1 203 ? -28.30119 11.64692 7.98330   1.000 52.50224  ? 183 LEU   A C   1 
ATOM   1394 O O   . LEU   A 1 203 ? -28.47933 11.60618 9.20586   1.000 57.30958  ? 183 LEU   A O   1 
ATOM   1395 C CB  . LEU   A 1 203 ? -27.01812 13.55474 6.98057   1.000 50.92545  ? 183 LEU   A CB  1 
ATOM   1396 C CG  . LEU   A 1 203 ? -25.70745 14.34123 7.00611   1.000 54.17239  ? 183 LEU   A CG  1 
ATOM   1397 C CD1 . LEU   A 1 203 ? -25.91074 15.71873 6.39910   1.000 56.69356  ? 183 LEU   A CD1 1 
ATOM   1398 C CD2 . LEU   A 1 203 ? -25.19010 14.45184 8.43120   1.000 57.79082  ? 183 LEU   A CD2 1 
ATOM   1399 N N   . ALA   A 1 204 ? -29.25706 11.31467 7.11306   1.000 48.55686  ? 184 ALA   A N   1 
ATOM   1400 C CA  . ALA   A 1 204 ? -30.58727 10.94819 7.58685   1.000 54.82393  ? 184 ALA   A CA  1 
ATOM   1401 C C   . ALA   A 1 204 ? -30.57301 9.60293  8.30168   1.000 57.67744  ? 184 ALA   A C   1 
ATOM   1402 O O   . ALA   A 1 204 ? -31.22105 9.44218  9.34239   1.000 61.31638  ? 184 ALA   A O   1 
ATOM   1403 C CB  . ALA   A 1 204 ? -31.57080 10.92763 6.41869   1.000 46.53550  ? 184 ALA   A CB  1 
ATOM   1404 N N   . ASP   A 1 205 ? -29.83832 8.62651  7.76235   1.000 56.27199  ? 185 ASP   A N   1 
ATOM   1405 C CA  . ASP   A 1 205 ? -29.79714 7.30579  8.38293   1.000 61.49297  ? 185 ASP   A CA  1 
ATOM   1406 C C   . ASP   A 1 205 ? -29.03602 7.33694  9.70156   1.000 57.53174  ? 185 ASP   A C   1 
ATOM   1407 O O   . ASP   A 1 205 ? -29.42402 6.66279  10.66306  1.000 54.81582  ? 185 ASP   A O   1 
ATOM   1408 C CB  . ASP   A 1 205 ? -29.16966 6.29212  7.42575   1.000 55.91266  ? 185 ASP   A CB  1 
ATOM   1409 C CG  . ASP   A 1 205 ? -29.98983 6.09470  6.16639   1.000 67.83523  ? 185 ASP   A CG  1 
ATOM   1410 O OD1 . ASP   A 1 205 ? -31.11388 6.63680  6.09733   1.000 63.71212  ? 185 ASP   A OD1 1 
ATOM   1411 O OD2 . ASP   A 1 205 ? -29.50700 5.40278  5.24400   1.000 64.63428  ? 185 ASP   A OD2 1 
ATOM   1412 N N   . ALA   A 1 206 ? -27.95220 8.11584  9.76798   1.000 53.36524  ? 186 ALA   A N   1 
ATOM   1413 C CA  . ALA   A 1 206 ? -27.17204 8.18865  10.99824  1.000 57.42053  ? 186 ALA   A CA  1 
ATOM   1414 C C   . ALA   A 1 206 ? -27.94900 8.86878  12.11752  1.000 60.52153  ? 186 ALA   A C   1 
ATOM   1415 O O   . ALA   A 1 206 ? -27.77779 8.51721  13.29097  1.000 66.96974  ? 186 ALA   A O   1 
ATOM   1416 C CB  . ALA   A 1 206 ? -25.85410 8.91656  10.74283  1.000 52.97985  ? 186 ALA   A CB  1 
ATOM   1417 N N   . LEU   A 1 207 ? -28.79912 9.84144  11.77976  1.000 59.01943  ? 187 LEU   A N   1 
ATOM   1418 C CA  . LEU   A 1 207 ? -29.66309 10.44590 12.78791  1.000 60.62672  ? 187 LEU   A CA  1 
ATOM   1419 C C   . LEU   A 1 207 ? -30.70234 9.45222  13.28865  1.000 66.68351  ? 187 LEU   A C   1 
ATOM   1420 O O   . LEU   A 1 207 ? -31.00741 9.41591  14.48638  1.000 73.34968  ? 187 LEU   A O   1 
ATOM   1421 C CB  . LEU   A 1 207 ? -30.33989 11.69200 12.22195  1.000 58.67134  ? 187 LEU   A CB  1 
ATOM   1422 C CG  . LEU   A 1 207 ? -29.57639 13.00273 12.40851  1.000 66.06337  ? 187 LEU   A CG  1 
ATOM   1423 C CD1 . LEU   A 1 207 ? -30.24309 14.12711 11.63369  1.000 70.26467  ? 187 LEU   A CD1 1 
ATOM   1424 C CD2 . LEU   A 1 207 ? -29.48447 13.34774 13.88739  1.000 62.30880  ? 187 LEU   A CD2 1 
ATOM   1425 N N   . VAL   A 1 208 ? -31.26011 8.64181  12.38670  1.000 70.62829  ? 188 VAL   A N   1 
ATOM   1426 C CA  . VAL   A 1 208 ? -32.19061 7.59864  12.80368  1.000 62.12752  ? 188 VAL   A CA  1 
ATOM   1427 C C   . VAL   A 1 208 ? -31.47661 6.56559  13.66508  1.000 59.77492  ? 188 VAL   A C   1 
ATOM   1428 O O   . VAL   A 1 208 ? -32.01869 6.09384  14.67171  1.000 59.33234  ? 188 VAL   A O   1 
ATOM   1429 C CB  . VAL   A 1 208 ? -32.85473 6.95370  11.57282  1.000 67.90233  ? 188 VAL   A CB  1 
ATOM   1430 C CG1 . VAL   A 1 208 ? -33.68306 5.74408  11.98350  1.000 58.56952  ? 188 VAL   A CG1 1 
ATOM   1431 C CG2 . VAL   A 1 208 ? -33.72195 7.96897  10.84355  1.000 62.44558  ? 188 VAL   A CG2 1 
ATOM   1432 N N   . ALA   A 1 209 ? -30.24368 6.21154  13.29607  1.000 58.79566  ? 189 ALA   A N   1 
ATOM   1433 C CA  . ALA   A 1 209 ? -29.48825 5.22053  14.05136  1.000 58.22714  ? 189 ALA   A CA  1 
ATOM   1434 C C   . ALA   A 1 209 ? -29.09398 5.71176  15.43822  1.000 65.14106  ? 189 ALA   A C   1 
ATOM   1435 O O   . ALA   A 1 209 ? -28.82251 4.88712  16.31813  1.000 64.15766  ? 189 ALA   A O   1 
ATOM   1436 C CB  . ALA   A 1 209 ? -28.23502 4.81594  13.27521  1.000 55.51748  ? 189 ALA   A CB  1 
ATOM   1437 N N   . GLY   A 1 210 ? -29.05534 7.02356  15.65503  1.000 65.06429  ? 190 GLY   A N   1 
ATOM   1438 C CA  . GLY   A 1 210 ? -28.59041 7.55974  16.91649  1.000 56.47867  ? 190 GLY   A CA  1 
ATOM   1439 C C   . GLY   A 1 210 ? -27.09970 7.79393  16.98354  1.000 59.92416  ? 190 GLY   A C   1 
ATOM   1440 O O   . GLY   A 1 210 ? -26.52563 7.76266  18.07829  1.000 56.72268  ? 190 GLY   A O   1 
ATOM   1441 N N   . VAL   A 1 211 ? -26.45239 8.02775  15.84526  1.000 57.39936  ? 191 VAL   A N   1 
ATOM   1442 C CA  . VAL   A 1 211 ? -25.01013 8.23795  15.79587  1.000 54.73050  ? 191 VAL   A CA  1 
ATOM   1443 C C   . VAL   A 1 211 ? -24.68347 9.63965  16.29110  1.000 60.59532  ? 191 VAL   A C   1 
ATOM   1444 O O   . VAL   A 1 211 ? -25.39724 10.60489 15.99110  1.000 66.57795  ? 191 VAL   A O   1 
ATOM   1445 C CB  . VAL   A 1 211 ? -24.48847 8.01166  14.36452  1.000 61.10409  ? 191 VAL   A CB  1 
ATOM   1446 C CG1 . VAL   A 1 211 ? -23.03505 8.45259  14.23445  1.000 55.25512  ? 191 VAL   A CG1 1 
ATOM   1447 C CG2 . VAL   A 1 211 ? -24.64642 6.55026  13.96768  1.000 60.02475  ? 191 VAL   A CG2 1 
ATOM   1448 N N   . ALA   A 1 212 ? -23.60045 9.75527  17.06318  1.000 55.37996  ? 192 ALA   A N   1 
ATOM   1449 C CA  . ALA   A 1 212 ? -23.10290 11.05112 17.52634  1.000 69.61606  ? 192 ALA   A CA  1 
ATOM   1450 C C   . ALA   A 1 212 ? -22.34476 11.71395 16.37850  1.000 54.50437  ? 192 ALA   A C   1 
ATOM   1451 O O   . ALA   A 1 212 ? -21.11435 11.68626 16.29447  1.000 64.41822  ? 192 ALA   A O   1 
ATOM   1452 C CB  . ALA   A 1 212 ? -22.22562 10.88353 18.76052  1.000 64.32849  ? 192 ALA   A CB  1 
ATOM   1453 N N   . ILE   A 1 213 ? -23.10889 12.32118 15.47142  1.000 62.10164  ? 193 ILE   A N   1 
ATOM   1454 C CA  . ILE   A 1 213 ? -22.52564 12.99018 14.31454  1.000 59.80452  ? 193 ILE   A CA  1 
ATOM   1455 C C   . ILE   A 1 213 ? -21.84466 14.27747 14.75573  1.000 58.59853  ? 193 ILE   A C   1 
ATOM   1456 O O   . ILE   A 1 213 ? -22.43680 15.10054 15.46560  1.000 62.35787  ? 193 ILE   A O   1 
ATOM   1457 C CB  . ILE   A 1 213 ? -23.60507 13.27829 13.26127  1.000 70.53532  ? 193 ILE   A CB  1 
ATOM   1458 C CG1 . ILE   A 1 213 ? -24.23678 11.97724 12.76523  1.000 65.75838  ? 193 ILE   A CG1 1 
ATOM   1459 C CG2 . ILE   A 1 213 ? -23.02355 14.08308 12.10584  1.000 66.49385  ? 193 ILE   A CG2 1 
ATOM   1460 C CD1 . ILE   A 1 213 ? -25.59345 12.17909 12.12560  1.000 65.49127  ? 193 ILE   A CD1 1 
ATOM   1461 N N   . THR   A 1 214 ? -20.59495 14.46173 14.33053  1.000 62.02272  ? 194 THR   A N   1 
ATOM   1462 C CA  . THR   A 1 214 ? -19.90625 15.72766 14.54874  1.000 65.33046  ? 194 THR   A CA  1 
ATOM   1463 C C   . THR   A 1 214 ? -19.95492 16.56841 13.27719  1.000 60.78575  ? 194 THR   A C   1 
ATOM   1464 O O   . THR   A 1 214 ? -20.63291 17.60008 13.23319  1.000 65.04333  ? 194 THR   A O   1 
ATOM   1465 C CB  . THR   A 1 214 ? -18.45825 15.49609 14.99467  1.000 63.52831  ? 194 THR   A CB  1 
ATOM   1466 O OG1 . THR   A 1 214 ? -17.76774 14.70958 14.01583  1.000 67.95707  ? 194 THR   A OG1 1 
ATOM   1467 C CG2 . THR   A 1 214 ? -18.42417 14.76996 16.33509  1.000 63.16572  ? 194 THR   A CG2 1 
ATOM   1468 N N   . ASP   A 1 215 ? -19.25436 16.12926 12.23846  1.000 49.49570  ? 195 ASP   A N   1 
ATOM   1469 C CA  . ASP   A 1 215 ? -19.22919 16.78762 10.93788  1.000 58.72874  ? 195 ASP   A CA  1 
ATOM   1470 C C   . ASP   A 1 215 ? -19.82723 15.85401 9.88572   1.000 59.99578  ? 195 ASP   A C   1 
ATOM   1471 O O   . ASP   A 1 215 ? -20.25758 14.73647 10.18635  1.000 58.16995  ? 195 ASP   A O   1 
ATOM   1472 C CB  . ASP   A 1 215 ? -17.79988 17.20035 10.56690  1.000 51.59207  ? 195 ASP   A CB  1 
ATOM   1473 C CG  . ASP   A 1 215 ? -16.81402 16.04653 10.66792  1.000 63.69738  ? 195 ASP   A CG  1 
ATOM   1474 O OD1 . ASP   A 1 215 ? -17.19791 14.97646 11.18888  1.000 67.85944  ? 195 ASP   A OD1 1 
ATOM   1475 O OD2 . ASP   A 1 215 ? -15.65485 16.20779 10.22948  1.000 56.48967  ? 195 ASP   A OD2 1 
ATOM   1476 N N   . GLU   A 1 216 ? -19.84904 16.32701 8.63534   1.000 43.94884  ? 196 GLU   A N   1 
ATOM   1477 C CA  . GLU   A 1 216 ? -20.36016 15.50934 7.53889   1.000 47.48131  ? 196 GLU   A CA  1 
ATOM   1478 C C   . GLU   A 1 216 ? -19.48640 14.28667 7.29885   1.000 47.97700  ? 196 GLU   A C   1 
ATOM   1479 O O   . GLU   A 1 216 ? -19.99918 13.22454 6.92807   1.000 46.22249  ? 196 GLU   A O   1 
ATOM   1480 C CB  . GLU   A 1 216 ? -20.46375 16.33637 6.25328   1.000 47.02650  ? 196 GLU   A CB  1 
ATOM   1481 C CG  . GLU   A 1 216 ? -21.63936 17.30567 6.20137   1.000 53.87297  ? 196 GLU   A CG  1 
ATOM   1482 C CD  . GLU   A 1 216 ? -21.56800 18.36999 7.28327   1.000 59.65734  ? 196 GLU   A CD  1 
ATOM   1483 O OE1 . GLU   A 1 216 ? -22.63310 18.78482 7.78495   1.000 59.77636  ? 196 GLU   A OE1 1 
ATOM   1484 O OE2 . GLU   A 1 216 ? -20.44469 18.79106 7.63729   1.000 59.04883  ? 196 GLU   A OE2 1 
ATOM   1485 N N   . ALA   A 1 217 ? -18.17135 14.41819 7.49492   1.000 45.05402  ? 197 ALA   A N   1 
ATOM   1486 C CA  . ALA   A 1 217 ? -17.27642 13.28853 7.27860   1.000 51.76974  ? 197 ALA   A CA  1 
ATOM   1487 C C   . ALA   A 1 217 ? -17.58922 12.14208 8.22938   1.000 55.73836  ? 197 ALA   A C   1 
ATOM   1488 O O   . ALA   A 1 217 ? -17.48113 10.97172 7.84714   1.000 48.34593  ? 197 ALA   A O   1 
ATOM   1489 C CB  . ALA   A 1 217 ? -15.82278 13.73622 7.43450   1.000 43.12375  ? 197 ALA   A CB  1 
ATOM   1490 N N   . SER   A 1 218 ? -17.98947 12.45773 9.46373   1.000 49.74724  ? 198 SER   A N   1 
ATOM   1491 C CA  . SER   A 1 218 ? -18.32543 11.41542 10.42652  1.000 58.58398  ? 198 SER   A CA  1 
ATOM   1492 C C   . SER   A 1 218 ? -19.57108 10.64523 10.00911  1.000 51.30796  ? 198 SER   A C   1 
ATOM   1493 O O   . SER   A 1 218 ? -19.67655 9.44636  10.28865  1.000 54.94988  ? 198 SER   A O   1 
ATOM   1494 C CB  . SER   A 1 218 ? -18.51820 12.02793 11.81498  1.000 48.95052  ? 198 SER   A CB  1 
ATOM   1495 O OG  . SER   A 1 218 ? -19.59684 12.94961 11.81690  1.000 55.53346  ? 198 SER   A OG  1 
ATOM   1496 N N   . ALA   A 1 219 ? -20.52280 11.31039 9.34889   1.000 52.13735  ? 199 ALA   A N   1 
ATOM   1497 C CA  . ALA   A 1 219 ? -21.69670 10.60497 8.84614   1.000 51.80016  ? 199 ALA   A CA  1 
ATOM   1498 C C   . ALA   A 1 219 ? -21.33283 9.72143  7.66174   1.000 55.43790  ? 199 ALA   A C   1 
ATOM   1499 O O   . ALA   A 1 219 ? -21.83368 8.59714  7.53939   1.000 51.09460  ? 199 ALA   A O   1 
ATOM   1500 C CB  . ALA   A 1 219 ? -22.78819 11.60173 8.45992   1.000 42.13886  ? 199 ALA   A CB  1 
ATOM   1501 N N   . MET   A 1 220 ? -20.45943 10.21433 6.78107   1.000 48.30676  ? 200 MET   A N   1 
ATOM   1502 C CA  . MET   A 1 220 ? -19.98263 9.39602  5.67241   1.000 54.28897  ? 200 MET   A CA  1 
ATOM   1503 C C   . MET   A 1 220 ? -19.14524 8.22812  6.17556   1.000 56.90005  ? 200 MET   A C   1 
ATOM   1504 O O   . MET   A 1 220 ? -19.20941 7.12464  5.62014   1.000 56.20231  ? 200 MET   A O   1 
ATOM   1505 C CB  . MET   A 1 220 ? -19.17729 10.25495 4.69794   1.000 48.42569  ? 200 MET   A CB  1 
ATOM   1506 C CG  . MET   A 1 220 ? -19.96026 11.41761 4.11576   1.000 56.30404  ? 200 MET   A CG  1 
ATOM   1507 S SD  . MET   A 1 220 ? -21.30654 10.86473 3.05310   1.000 60.53916  ? 200 MET   A SD  1 
ATOM   1508 C CE  . MET   A 1 220 ? -20.39677 10.27436 1.62662   1.000 52.17468  ? 200 MET   A CE  1 
ATOM   1509 N N   . GLU   A 1 221 ? -18.35714 8.45179  7.23026   1.000 53.82552  ? 201 GLU   A N   1 
ATOM   1510 C CA  . GLU   A 1 221 ? -17.54271 7.37773  7.79024   1.000 49.99896  ? 201 GLU   A CA  1 
ATOM   1511 C C   . GLU   A 1 221 ? -18.41245 6.28781  8.40318   1.000 55.94766  ? 201 GLU   A C   1 
ATOM   1512 O O   . GLU   A 1 221 ? -18.15737 5.09450  8.20244   1.000 49.26612  ? 201 GLU   A O   1 
ATOM   1513 C CB  . GLU   A 1 221 ? -16.57408 7.94336  8.82832   1.000 52.56085  ? 201 GLU   A CB  1 
ATOM   1514 C CG  . GLU   A 1 221 ? -15.31786 8.55583  8.22820   1.000 56.71449  ? 201 GLU   A CG  1 
ATOM   1515 C CD  . GLU   A 1 221 ? -14.68894 9.60389  9.12673   1.000 64.69720  ? 201 GLU   A CD  1 
ATOM   1516 O OE1 . GLU   A 1 221 ? -14.47703 10.74216 8.65227   1.000 56.24376  ? 201 GLU   A OE1 1 
ATOM   1517 O OE2 . GLU   A 1 221 ? -14.41167 9.29308  10.30607  1.000 64.56097  ? 201 GLU   A OE2 1 
ATOM   1518 N N   . TRP   A 1 222 ? -19.44373 6.67794  9.15515   1.000 52.09638  ? 202 TRP   A N   1 
ATOM   1519 C CA  . TRP   A 1 222 ? -20.37094 5.69191  9.69844   1.000 57.99107  ? 202 TRP   A CA  1 
ATOM   1520 C C   . TRP   A 1 222 ? -21.07022 4.91120  8.59327   1.000 60.60907  ? 202 TRP   A C   1 
ATOM   1521 O O   . TRP   A 1 222 ? -21.36571 3.72132  8.76380   1.000 52.92305  ? 202 TRP   A O   1 
ATOM   1522 C CB  . TRP   A 1 222 ? -21.40137 6.37541  10.59673  1.000 45.88842  ? 202 TRP   A CB  1 
ATOM   1523 C CG  . TRP   A 1 222 ? -22.56154 5.49347  10.93228  1.000 58.22970  ? 202 TRP   A CG  1 
ATOM   1524 C CD1 . TRP   A 1 222 ? -22.62802 4.57307  11.93661  1.000 57.05291  ? 202 TRP   A CD1 1 
ATOM   1525 C CD2 . TRP   A 1 222 ? -23.82244 5.43742  10.25194  1.000 58.57854  ? 202 TRP   A CD2 1 
ATOM   1526 N NE1 . TRP   A 1 222 ? -23.85333 3.95071  11.92771  1.000 60.22977  ? 202 TRP   A NE1 1 
ATOM   1527 C CE2 . TRP   A 1 222 ? -24.60459 4.46268  10.90262  1.000 59.92546  ? 202 TRP   A CE2 1 
ATOM   1528 C CE3 . TRP   A 1 222 ? -24.36524 6.11690  9.15616   1.000 51.64088  ? 202 TRP   A CE3 1 
ATOM   1529 C CZ2 . TRP   A 1 222 ? -25.90166 4.15148  10.49540  1.000 58.63126  ? 202 TRP   A CZ2 1 
ATOM   1530 C CZ3 . TRP   A 1 222 ? -25.65334 5.80744  8.75387   1.000 57.36055  ? 202 TRP   A CZ3 1 
ATOM   1531 C CH2 . TRP   A 1 222 ? -26.40652 4.83305  9.42181   1.000 62.04030  ? 202 TRP   A CH2 1 
ATOM   1532 N N   . ALA   A 1 223 ? -21.33813 5.55682  7.45665   1.000 56.05069  ? 203 ALA   A N   1 
ATOM   1533 C CA  . ALA   A 1 223 ? -21.97520 4.88043  6.33388   1.000 52.14734  ? 203 ALA   A CA  1 
ATOM   1534 C C   . ALA   A 1 223 ? -21.02734 3.95613  5.58255   1.000 52.22866  ? 203 ALA   A C   1 
ATOM   1535 O O   . ALA   A 1 223 ? -21.46657 3.28636  4.64109   1.000 60.91490  ? 203 ALA   A O   1 
ATOM   1536 C CB  . ALA   A 1 223 ? -22.57361 5.90720  5.36946   1.000 48.06530  ? 203 ALA   A CB  1 
ATOM   1537 N N   . GLY   A 1 224 ? -19.75135 3.90445  5.96381   1.000 57.45366  ? 204 GLY   A N   1 
ATOM   1538 C CA  . GLY   A 1 224 ? -18.78873 2.99181  5.38555   1.000 54.54049  ? 204 GLY   A CA  1 
ATOM   1539 C C   . GLY   A 1 224 ? -17.75325 3.64171  4.49255   1.000 59.61638  ? 204 GLY   A C   1 
ATOM   1540 O O   . GLY   A 1 224 ? -16.70967 3.02742  4.23173   1.000 54.68977  ? 204 GLY   A O   1 
ATOM   1541 N N   . TYR   A 1 225 ? -17.99929 4.86229  4.02491   1.000 61.57775  ? 205 TYR   A N   1 
ATOM   1542 C CA  . TYR   A 1 225 ? -17.10035 5.49920  3.07418   1.000 55.86282  ? 205 TYR   A CA  1 
ATOM   1543 C C   . TYR   A 1 225 ? -15.89945 6.11357  3.78206   1.000 51.02139  ? 205 TYR   A C   1 
ATOM   1544 O O   . TYR   A 1 225 ? -15.98198 6.54772  4.93551   1.000 52.69560  ? 205 TYR   A O   1 
ATOM   1545 C CB  . TYR   A 1 225 ? -17.84194 6.56870  2.27435   1.000 45.99098  ? 205 TYR   A CB  1 
ATOM   1546 C CG  . TYR   A 1 225 ? -19.14382 6.07280  1.69890   1.000 51.88180  ? 205 TYR   A CG  1 
ATOM   1547 C CD1 . TYR   A 1 225 ? -19.15744 5.11133  0.69757   1.000 60.76240  ? 205 TYR   A CD1 1 
ATOM   1548 C CD2 . TYR   A 1 225 ? -20.36014 6.55499  2.16328   1.000 49.65731  ? 205 TYR   A CD2 1 
ATOM   1549 C CE1 . TYR   A 1 225 ? -20.34690 4.64487  0.17108   1.000 66.32754  ? 205 TYR   A CE1 1 
ATOM   1550 C CE2 . TYR   A 1 225 ? -21.55499 6.09662  1.64231   1.000 55.29334  ? 205 TYR   A CE2 1 
ATOM   1551 C CZ  . TYR   A 1 225 ? -21.54249 5.14197  0.64605   1.000 61.78999  ? 205 TYR   A CZ  1 
ATOM   1552 O OH  . TYR   A 1 225 ? -22.72798 4.68059  0.12278   1.000 66.51783  ? 205 TYR   A OH  1 
ATOM   1553 N N   . ALA   A 1 226 ? -14.77049 6.14114  3.07329   1.000 47.32371  ? 206 ALA   A N   1 
ATOM   1554 C CA  . ALA   A 1 226 ? -13.53325 6.71909  3.58856   1.000 45.33701  ? 206 ALA   A CA  1 
ATOM   1555 C C   . ALA   A 1 226 ? -13.26618 8.04695  2.89280   1.000 55.82205  ? 206 ALA   A C   1 
ATOM   1556 O O   . ALA   A 1 226 ? -12.81677 8.06129  1.73572   1.000 51.60070  ? 206 ALA   A O   1 
ATOM   1557 C CB  . ALA   A 1 226 ? -12.35900 5.75964  3.38044   1.000 46.34743  ? 206 ALA   A CB  1 
ATOM   1558 N N   . PRO   A 1 227 ? -13.52374 9.18182  3.54014   1.000 55.45978  ? 207 PRO   A N   1 
ATOM   1559 C CA  . PRO   A 1 227 ? -13.30641 10.47243 2.87811   1.000 47.50239  ? 207 PRO   A CA  1 
ATOM   1560 C C   . PRO   A 1 227 ? -11.82994 10.73695 2.63256   1.000 48.37673  ? 207 PRO   A C   1 
ATOM   1561 O O   . PRO   A 1 227 ? -10.96099 10.34097 3.41334   1.000 49.56616  ? 207 PRO   A O   1 
ATOM   1562 C CB  . PRO   A 1 227 ? -13.88915 11.48900 3.86986   1.000 42.24177  ? 207 PRO   A CB  1 
ATOM   1563 C CG  . PRO   A 1 227 ? -14.73240 10.69056 4.81290   1.000 42.10189  ? 207 PRO   A CG  1 
ATOM   1564 C CD  . PRO   A 1 227 ? -14.09304 9.34135  4.88693   1.000 52.83418  ? 207 PRO   A CD  1 
ATOM   1565 N N   . LYS   A 1 228 ? -11.55533 11.42242 1.52688   1.000 45.01662  ? 208 LYS   A N   1 
ATOM   1566 C CA  . LYS   A 1 228 ? -10.19453 11.81648 1.19562   1.000 47.87558  ? 208 LYS   A CA  1 
ATOM   1567 C C   . LYS   A 1 228 ? -9.77516  13.01257 2.03888   1.000 52.18613  ? 208 LYS   A C   1 
ATOM   1568 O O   . LYS   A 1 228 ? -10.58253 13.89615 2.33674   1.000 50.10986  ? 208 LYS   A O   1 
ATOM   1569 C CB  . LYS   A 1 228 ? -10.08592 12.16730 -0.28952  1.000 51.15757  ? 208 LYS   A CB  1 
ATOM   1570 C CG  . LYS   A 1 228 ? -8.67713  12.09601 -0.85987  1.000 53.63510  ? 208 LYS   A CG  1 
ATOM   1571 C CD  . LYS   A 1 228 ? -8.18627  10.65347 -0.90788  1.000 74.74892  ? 208 LYS   A CD  1 
ATOM   1572 C CE  . LYS   A 1 228 ? -6.92101  10.52880 -1.75134  1.000 81.41232  ? 208 LYS   A CE  1 
ATOM   1573 N NZ  . LYS   A 1 228 ? -6.56440  9.09332  -1.95456  1.000 86.10649  ? 208 LYS   A NZ  1 
ATOM   1574 N N   . LEU   A 1 229 ? -8.50542  13.04525 2.42026   1.000 50.19815  ? 209 LEU   A N   1 
ATOM   1575 C CA  . LEU   A 1 229 ? -7.95115  14.18693 3.13145   1.000 47.55390  ? 209 LEU   A CA  1 
ATOM   1576 C C   . LEU   A 1 229 ? -7.26558  15.10597 2.13132   1.000 51.46963  ? 209 LEU   A C   1 
ATOM   1577 O O   . LEU   A 1 229 ? -6.48825  14.64594 1.28838   1.000 49.48983  ? 209 LEU   A O   1 
ATOM   1578 C CB  . LEU   A 1 229 ? -6.97335  13.73839 4.21730   1.000 43.29272  ? 209 LEU   A CB  1 
ATOM   1579 C CG  . LEU   A 1 229 ? -7.62731  13.05390 5.42018   1.000 59.63571  ? 209 LEU   A CG  1 
ATOM   1580 C CD1 . LEU   A 1 229 ? -6.59571  12.29793 6.23740   1.000 53.19404  ? 209 LEU   A CD1 1 
ATOM   1581 C CD2 . LEU   A 1 229 ? -8.35524  14.07191 6.28789   1.000 45.87837  ? 209 LEU   A CD2 1 
ATOM   1582 N N   . VAL   A 1 230 ? -7.58159  16.39489 2.20782   1.000 57.28368  ? 210 VAL   A N   1 
ATOM   1583 C CA  . VAL   A 1 230 ? -6.97532  17.41758 1.36459   1.000 45.54480  ? 210 VAL   A CA  1 
ATOM   1584 C C   . VAL   A 1 230 ? -6.32814  18.43825 2.28550   1.000 52.42330  ? 210 VAL   A C   1 
ATOM   1585 O O   . VAL   A 1 230 ? -7.01798  19.08594 3.08327   1.000 51.57492  ? 210 VAL   A O   1 
ATOM   1586 C CB  . VAL   A 1 230 ? -8.00457  18.08504 0.44044   1.000 49.66562  ? 210 VAL   A CB  1 
ATOM   1587 C CG1 . VAL   A 1 230 ? -7.33076  19.13530 -0.42973  1.000 47.52237  ? 210 VAL   A CG1 1 
ATOM   1588 C CG2 . VAL   A 1 230 ? -8.70786  17.03803 -0.41403  1.000 53.15505  ? 210 VAL   A CG2 1 
ATOM   1589 N N   . GLU   A 1 231 ? -5.00902  18.57520 2.18697   1.000 41.99881  ? 211 GLU   A N   1 
ATOM   1590 C CA  . GLU   A 1 231 ? -4.29613  19.46223 3.09390   1.000 44.35125  ? 211 GLU   A CA  1 
ATOM   1591 C C   . GLU   A 1 231 ? -4.64585  20.91462 2.80410   1.000 50.30717  ? 211 GLU   A C   1 
ATOM   1592 O O   . GLU   A 1 231 ? -4.58237  21.36446 1.65613   1.000 48.75047  ? 211 GLU   A O   1 
ATOM   1593 C CB  . GLU   A 1 231 ? -2.78754  19.25839 2.98649   1.000 47.28631  ? 211 GLU   A CB  1 
ATOM   1594 C CG  . GLU   A 1 231 ? -2.00792  20.32474 3.74228   1.000 58.19261  ? 211 GLU   A CG  1 
ATOM   1595 C CD  . GLU   A 1 231 ? -0.57410  19.93185 4.02324   1.000 65.47604  ? 211 GLU   A CD  1 
ATOM   1596 O OE1 . GLU   A 1 231 ? 0.00951   20.47394 4.98648   1.000 60.81456  ? 211 GLU   A OE1 1 
ATOM   1597 O OE2 . GLU   A 1 231 ? -0.03187  19.08154 3.28667   1.000 72.90764  ? 211 GLU   A OE2 1 
ATOM   1598 N N   . GLY   A 1 232 ? -5.01912  21.64502 3.85135   1.000 47.50152  ? 212 GLY   A N   1 
ATOM   1599 C CA  . GLY   A 1 232 ? -5.30750  23.05837 3.72855   1.000 58.32591  ? 212 GLY   A CA  1 
ATOM   1600 C C   . GLY   A 1 232 ? -4.40342  23.90254 4.60075   1.000 54.29084  ? 212 GLY   A C   1 
ATOM   1601 O O   . GLY   A 1 232 ? -3.44428  23.39215 5.18765   1.000 61.59488  ? 212 GLY   A O   1 
ATOM   1602 N N   . ARG   A 1 233 ? -4.69657  25.19447 4.69420   1.000 54.43372  ? 213 ARG   A N   1 
ATOM   1603 C CA  . ARG   A 1 233 ? -3.90816  26.08812 5.52659   1.000 53.54967  ? 213 ARG   A CA  1 
ATOM   1604 C C   . ARG   A 1 233 ? -4.30148  25.94739 6.99158   1.000 52.11889  ? 213 ARG   A C   1 
ATOM   1605 O O   . ARG   A 1 233 ? -5.44322  25.61684 7.32453   1.000 53.11033  ? 213 ARG   A O   1 
ATOM   1606 C CB  . ARG   A 1 233 ? -4.08819  27.53908 5.08165   1.000 53.63554  ? 213 ARG   A CB  1 
ATOM   1607 C CG  . ARG   A 1 233 ? -3.47832  27.86695 3.73002   1.000 58.53481  ? 213 ARG   A CG  1 
ATOM   1608 C CD  . ARG   A 1 233 ? -3.70538  29.33263 3.37902   1.000 58.92420  ? 213 ARG   A CD  1 
ATOM   1609 N NE  . ARG   A 1 233 ? -3.25730  30.21956 4.44648   1.000 61.25390  ? 213 ARG   A NE  1 
ATOM   1610 C CZ  . ARG   A 1 233 ? -2.05831  30.78432 4.50026   1.000 74.09678  ? 213 ARG   A CZ  1 
ATOM   1611 N NH1 . ARG   A 1 233 ? -1.16031  30.59267 3.54772   1.000 63.31702  ? 213 ARG   A NH1 1 
ATOM   1612 N NH2 . ARG   A 1 233 ? -1.75154  31.55902 5.53752   1.000 67.38408  ? 213 ARG   A NH2 1 
ATOM   1613 N N   . ALA   A 1 234 ? -3.33803  26.21612 7.87272   1.000 58.96167  ? 214 ALA   A N   1 
ATOM   1614 C CA  . ALA   A 1 234 ? -3.57387  26.09692 9.30501   1.000 54.98443  ? 214 ALA   A CA  1 
ATOM   1615 C C   . ALA   A 1 234 ? -4.31381  27.29233 9.88970   1.000 57.53289  ? 214 ALA   A C   1 
ATOM   1616 O O   . ALA   A 1 234 ? -4.95249  27.14981 10.93894  1.000 55.36672  ? 214 ALA   A O   1 
ATOM   1617 C CB  . ALA   A 1 234 ? -2.24719  25.90508 10.04198  1.000 54.72466  ? 214 ALA   A CB  1 
ATOM   1618 N N   . ASP   A 1 235 ? -4.24589  28.45970 9.24861   1.000 50.03270  ? 215 ASP   A N   1 
ATOM   1619 C CA  . ASP   A 1 235 ? -4.92403  29.64207 9.76618   1.000 61.70694  ? 215 ASP   A CA  1 
ATOM   1620 C C   . ASP   A 1 235 ? -6.38997  29.71859 9.34765   1.000 55.19990  ? 215 ASP   A C   1 
ATOM   1621 O O   . ASP   A 1 235 ? -7.02583  30.75553 9.55873   1.000 56.05063  ? 215 ASP   A O   1 
ATOM   1622 C CB  . ASP   A 1 235 ? -4.18122  30.91523 9.34021   1.000 63.66186  ? 215 ASP   A CB  1 
ATOM   1623 C CG  . ASP   A 1 235 ? -3.99889  31.01933 7.83719   1.000 64.89985  ? 215 ASP   A CG  1 
ATOM   1624 O OD1 . ASP   A 1 235 ? -4.43765  30.10334 7.11099   1.000 66.64784  ? 215 ASP   A OD1 1 
ATOM   1625 O OD2 . ASP   A 1 235 ? -3.40892  32.02379 7.38181   1.000 72.16047  ? 215 ASP   A OD2 1 
ATOM   1626 N N   . ASN   A 1 236 ? -6.93903  28.65111 8.76630   1.000 55.82491  ? 216 ASN   A N   1 
ATOM   1627 C CA  . ASN   A 1 236 ? -8.37467  28.55486 8.50121   1.000 49.91214  ? 216 ASN   A CA  1 
ATOM   1628 C C   . ASN   A 1 236 ? -9.10533  28.14476 9.78463   1.000 53.36702  ? 216 ASN   A C   1 
ATOM   1629 O O   . ASN   A 1 236 ? -9.79359  27.12619 9.86411   1.000 59.76499  ? 216 ASN   A O   1 
ATOM   1630 C CB  . ASN   A 1 236 ? -8.62493  27.57611 7.36016   1.000 48.14896  ? 216 ASN   A CB  1 
ATOM   1631 C CG  . ASN   A 1 236 ? -10.09554 27.45139 6.99614   1.000 51.72885  ? 216 ASN   A CG  1 
ATOM   1632 O OD1 . ASN   A 1 236 ? -10.88554 28.37071 7.21349   1.000 58.27322  ? 216 ASN   A OD1 1 
ATOM   1633 N ND2 . ASN   A 1 236 ? -10.46957 26.30199 6.44329   1.000 53.90836  ? 216 ASN   A ND2 1 
ATOM   1634 N N   . LEU   A 1 237 ? -8.93952  28.98044 10.80697  1.000 51.53171  ? 217 LEU   A N   1 
ATOM   1635 C CA  . LEU   A 1 237 ? -9.35779  28.62986 12.15537  1.000 51.56348  ? 217 LEU   A CA  1 
ATOM   1636 C C   . LEU   A 1 237 ? -10.83691 28.92295 12.37586  1.000 52.36146  ? 217 LEU   A C   1 
ATOM   1637 O O   . LEU   A 1 237 ? -11.42773 29.79488 11.73253  1.000 49.01719  ? 217 LEU   A O   1 
ATOM   1638 C CB  . LEU   A 1 237 ? -8.51503  29.38198 13.19202  1.000 55.26093  ? 217 LEU   A CB  1 
ATOM   1639 C CG  . LEU   A 1 237 ? -8.50470  30.91524 13.19576  1.000 60.17220  ? 217 LEU   A CG  1 
ATOM   1640 C CD1 . LEU   A 1 237 ? -9.62569  31.49349 14.06170  1.000 62.67941  ? 217 LEU   A CD1 1 
ATOM   1641 C CD2 . LEU   A 1 237 ? -7.14401  31.43134 13.65468  1.000 65.31173  ? 217 LEU   A CD2 1 
ATOM   1642 N N   . LYS   A 1 238 ? -11.42840 28.17990 13.30630  1.000 49.08091  ? 218 LYS   A N   1 
ATOM   1643 C CA  . LYS   A 1 238 ? -12.79556 28.40933 13.73963  1.000 55.19876  ? 218 LYS   A CA  1 
ATOM   1644 C C   . LYS   A 1 238 ? -12.79176 29.33972 14.94341  1.000 55.17581  ? 218 LYS   A C   1 
ATOM   1645 O O   . LYS   A 1 238 ? -11.96411 29.19981 15.85023  1.000 66.95021  ? 218 LYS   A O   1 
ATOM   1646 C CB  . LYS   A 1 238 ? -13.47278 27.08379 14.09164  1.000 47.50079  ? 218 LYS   A CB  1 
ATOM   1647 C CG  . LYS   A 1 238 ? -14.96027 27.18833 14.40198  1.000 56.39611  ? 218 LYS   A CG  1 
ATOM   1648 C CD  . LYS   A 1 238 ? -15.57971 25.79540 14.46149  1.000 60.08626  ? 218 LYS   A CD  1 
ATOM   1649 C CE  . LYS   A 1 238 ? -17.09886 25.84207 14.57080  1.000 61.41970  ? 218 LYS   A CE  1 
ATOM   1650 N NZ  . LYS   A 1 238 ? -17.56344 25.71922 15.98074  1.000 66.81311  ? 218 LYS   A NZ  1 
ATOM   1651 N N   . ILE   A 1 239 ? -13.71477 30.29763 14.94146  1.000 52.09994  ? 219 ILE   A N   1 
ATOM   1652 C CA  . ILE   A 1 239 ? -13.82858 31.26615 16.02613  1.000 55.03240  ? 219 ILE   A CA  1 
ATOM   1653 C C   . ILE   A 1 239 ? -14.71467 30.64385 17.10034  1.000 47.92746  ? 219 ILE   A C   1 
ATOM   1654 O O   . ILE   A 1 239 ? -15.93929 30.61681 16.97775  1.000 48.56205  ? 219 ILE   A O   1 
ATOM   1655 C CB  . ILE   A 1 239 ? -14.37785 32.60742 15.53920  1.000 60.95145  ? 219 ILE   A CB  1 
ATOM   1656 C CG1 . ILE   A 1 239 ? -13.45427 33.20089 14.47991  1.000 48.87079  ? 219 ILE   A CG1 1 
ATOM   1657 C CG2 . ILE   A 1 239 ? -14.54211 33.56983 16.70200  1.000 53.27819  ? 219 ILE   A CG2 1 
ATOM   1658 C CD1 . ILE   A 1 239 ? -13.87073 34.56699 14.00523  1.000 55.14569  ? 219 ILE   A CD1 1 
ATOM   1659 N N   . THR   A 1 240 ? -14.08563 30.13250 18.15768  1.000 60.28047  ? 220 THR   A N   1 
ATOM   1660 C CA  . THR   A 1 240 ? -14.79823 29.52435 19.27475  1.000 69.45950  ? 220 THR   A CA  1 
ATOM   1661 C C   . THR   A 1 240 ? -14.84604 30.41539 20.50557  1.000 64.45250  ? 220 THR   A C   1 
ATOM   1662 O O   . THR   A 1 240 ? -15.83178 30.37404 21.24871  1.000 64.99024  ? 220 THR   A O   1 
ATOM   1663 C CB  . THR   A 1 240 ? -14.15580 28.18398 19.64873  1.000 56.85094  ? 220 THR   A CB  1 
ATOM   1664 O OG1 . THR   A 1 240 ? -12.75073 28.37525 19.85518  1.000 66.18190  ? 220 THR   A OG1 1 
ATOM   1665 C CG2 . THR   A 1 240 ? -14.36697 27.17362 18.53074  1.000 61.96181  ? 220 THR   A CG2 1 
ATOM   1666 N N   . THR   A 1 241 ? -13.79955 31.20029 20.74615  1.000 65.17244  ? 221 THR   A N   1 
ATOM   1667 C CA  . THR   A 1 241 ? -13.77583 32.19287 21.80168  1.000 69.84447  ? 221 THR   A CA  1 
ATOM   1668 C C   . THR   A 1 241 ? -13.55700 33.57390 21.19595  1.000 75.60188  ? 221 THR   A C   1 
ATOM   1669 O O   . THR   A 1 241 ? -12.90444 33.69901 20.15414  1.000 68.17189  ? 221 THR   A O   1 
ATOM   1670 C CB  . THR   A 1 241 ? -12.66532 31.90181 22.82072  1.000 77.69682  ? 221 THR   A CB  1 
ATOM   1671 O OG1 . THR   A 1 241 ? -11.38468 32.01223 22.18578  1.000 73.40134  ? 221 THR   A OG1 1 
ATOM   1672 C CG2 . THR   A 1 241 ? -12.81853 30.50080 23.39320  1.000 73.81416  ? 221 THR   A CG2 1 
ATOM   1673 N N   . PRO   A 1 242 ? -14.09849 34.62774 21.81340  1.000 83.50730  ? 222 PRO   A N   1 
ATOM   1674 C CA  . PRO   A 1 242 ? -13.79329 35.98874 21.33925  1.000 79.61159  ? 222 PRO   A CA  1 
ATOM   1675 C C   . PRO   A 1 242 ? -12.30592 36.30092 21.31704  1.000 77.86780  ? 222 PRO   A C   1 
ATOM   1676 O O   . PRO   A 1 242 ? -11.89454 37.24689 20.63299  1.000 70.52977  ? 222 PRO   A O   1 
ATOM   1677 C CB  . PRO   A 1 242 ? -14.54136 36.88399 22.33631  1.000 73.17388  ? 222 PRO   A CB  1 
ATOM   1678 C CG  . PRO   A 1 242 ? -15.65605 36.02843 22.84284  1.000 69.73564  ? 222 PRO   A CG  1 
ATOM   1679 C CD  . PRO   A 1 242 ? -15.11722 34.62395 22.87793  1.000 79.07999  ? 222 PRO   A CD  1 
ATOM   1680 N N   . GLU   A 1 243 ? -11.48651 35.53627 22.04274  1.000 72.59160  ? 223 GLU   A N   1 
ATOM   1681 C CA  . GLU   A 1 243 ? -10.04260 35.71601 21.96164  1.000 71.89991  ? 223 GLU   A CA  1 
ATOM   1682 C C   . GLU   A 1 243 ? -9.49057  35.22964 20.62626  1.000 81.51036  ? 223 GLU   A C   1 
ATOM   1683 O O   . GLU   A 1 243 ? -8.45681  35.72989 20.16885  1.000 85.76345  ? 223 GLU   A O   1 
ATOM   1684 C CB  . GLU   A 1 243 ? -9.36040  34.99226 23.12281  1.000 77.96270  ? 223 GLU   A CB  1 
ATOM   1685 C CG  . GLU   A 1 243 ? -9.79990  35.47500 24.49883  1.000 78.81343  ? 223 GLU   A CG  1 
ATOM   1686 N N   . ASP   A 1 244 ? -10.15813 34.26265 19.98610  1.000 78.59956  ? 224 ASP   A N   1 
ATOM   1687 C CA  . ASP   A 1 244 ? -9.73454  33.82584 18.65963  1.000 67.77830  ? 224 ASP   A CA  1 
ATOM   1688 C C   . ASP   A 1 244 ? -9.93851  34.90639 17.60725  1.000 67.03607  ? 224 ASP   A C   1 
ATOM   1689 O O   . ASP   A 1 244 ? -9.29855  34.85289 16.55096  1.000 66.58008  ? 224 ASP   A O   1 
ATOM   1690 C CB  . ASP   A 1 244 ? -10.48012 32.55654 18.23960  1.000 67.46243  ? 224 ASP   A CB  1 
ATOM   1691 C CG  . ASP   A 1 244 ? -9.90230  31.30329 18.86789  1.000 80.36095  ? 224 ASP   A CG  1 
ATOM   1692 O OD1 . ASP   A 1 244 ? -10.65659 30.32246 19.04833  1.000 74.62665  ? 224 ASP   A OD1 1 
ATOM   1693 O OD2 . ASP   A 1 244 ? -8.69681  31.30510 19.19581  1.000 83.73479  ? 224 ASP   A OD2 1 
ATOM   1694 N N   . LEU   A 1 245 ? -10.82113 35.87578 17.86560  1.000 64.65497  ? 225 LEU   A N   1 
ATOM   1695 C CA  . LEU   A 1 245 ? -10.96235 37.00598 16.95390  1.000 70.48769  ? 225 LEU   A CA  1 
ATOM   1696 C C   . LEU   A 1 245 ? -9.64652  37.75545 16.80589  1.000 62.02782  ? 225 LEU   A C   1 
ATOM   1697 O O   . LEU   A 1 245 ? -9.30666  38.21785 15.71092  1.000 61.54168  ? 225 LEU   A O   1 
ATOM   1698 C CB  . LEU   A 1 245 ? -12.05957 37.94962 17.44654  1.000 69.16733  ? 225 LEU   A CB  1 
ATOM   1699 C CG  . LEU   A 1 245 ? -13.44134 37.80802 16.80829  1.000 65.46270  ? 225 LEU   A CG  1 
ATOM   1700 C CD1 . LEU   A 1 245 ? -14.40898 38.80228 17.42797  1.000 60.54840  ? 225 LEU   A CD1 1 
ATOM   1701 C CD2 . LEU   A 1 245 ? -13.35364 38.00560 15.30363  1.000 60.30091  ? 225 LEU   A CD2 1 
ATOM   1702 N N   . LEU   A 1 246 ? -8.88396  37.86561 17.89729  1.000 58.03108  ? 226 LEU   A N   1 
ATOM   1703 C CA  . LEU   A 1 246 ? -7.63617  38.62053 17.87123  1.000 63.20041  ? 226 LEU   A CA  1 
ATOM   1704 C C   . LEU   A 1 246 ? -6.64281  38.04076 16.87313  1.000 62.16677  ? 226 LEU   A C   1 
ATOM   1705 O O   . LEU   A 1 246 ? -5.83280  38.78149 16.30352  1.000 55.57321  ? 226 LEU   A O   1 
ATOM   1706 C CB  . LEU   A 1 246 ? -7.03095  38.65633 19.27331  1.000 63.43188  ? 226 LEU   A CB  1 
ATOM   1707 C CG  . LEU   A 1 246 ? -7.93573  39.25743 20.35025  1.000 64.35307  ? 226 LEU   A CG  1 
ATOM   1708 C CD1 . LEU   A 1 246 ? -7.44325  38.88272 21.73868  1.000 66.54300  ? 226 LEU   A CD1 1 
ATOM   1709 C CD2 . LEU   A 1 246 ? -8.00839  40.76844 20.19322  1.000 66.78158  ? 226 LEU   A CD2 1 
ATOM   1710 N N   . ARG   A 1 247 ? -6.69246  36.72618 16.64242  1.000 68.58659  ? 227 ARG   A N   1 
ATOM   1711 C CA  . ARG   A 1 247 ? -5.79188  36.11219 15.67358  1.000 62.25869  ? 227 ARG   A CA  1 
ATOM   1712 C C   . ARG   A 1 247 ? -6.08534  36.58489 14.25638  1.000 55.74693  ? 227 ARG   A C   1 
ATOM   1713 O O   . ARG   A 1 247 ? -5.16981  36.66352 13.42921  1.000 58.51776  ? 227 ARG   A O   1 
ATOM   1714 C CB  . ARG   A 1 247 ? -5.89660  34.58708 15.74364  1.000 47.93295  ? 227 ARG   A CB  1 
ATOM   1715 C CG  . ARG   A 1 247 ? -6.14028  34.03189 17.13378  1.000 70.01813  ? 227 ARG   A CG  1 
ATOM   1716 C CD  . ARG   A 1 247 ? -6.18641  32.51113 17.11883  1.000 77.13186  ? 227 ARG   A CD  1 
ATOM   1717 N N   . LEU   A 1 248 ? -7.34338  36.90661 13.95858  1.000 55.81776  ? 228 LEU   A N   1 
ATOM   1718 C CA  . LEU   A 1 248 ? -7.76441  37.22297 12.60121  1.000 61.10645  ? 228 LEU   A CA  1 
ATOM   1719 C C   . LEU   A 1 248 ? -7.93797  38.71405 12.34678  1.000 68.90772  ? 228 LEU   A C   1 
ATOM   1720 O O   . LEU   A 1 248 ? -8.30285  39.09329 11.22946  1.000 72.80002  ? 228 LEU   A O   1 
ATOM   1721 C CB  . LEU   A 1 248 ? -9.07356  36.49662 12.27639  1.000 59.10841  ? 228 LEU   A CB  1 
ATOM   1722 C CG  . LEU   A 1 248 ? -8.98143  34.97835 12.13473  1.000 58.84312  ? 228 LEU   A CG  1 
ATOM   1723 C CD1 . LEU   A 1 248 ? -10.35050 34.38642 11.84727  1.000 61.11728  ? 228 LEU   A CD1 1 
ATOM   1724 C CD2 . LEU   A 1 248 ? -7.99351  34.61141 11.03872  1.000 56.88412  ? 228 LEU   A CD2 1 
ATOM   1725 N N   . GLN   A 1 249 ? -7.68187  39.56828 13.34214  1.000 72.56477  ? 229 GLN   A N   1 
ATOM   1726 C CA  . GLN   A 1 249 ? -7.95536  40.99283 13.17223  1.000 76.88284  ? 229 GLN   A CA  1 
ATOM   1727 C C   . GLN   A 1 249 ? -7.05594  41.62466 12.11638  1.000 73.70490  ? 229 GLN   A C   1 
ATOM   1728 O O   . GLN   A 1 249 ? -7.44997  42.60798 11.47830  1.000 77.74467  ? 229 GLN   A O   1 
ATOM   1729 C CB  . GLN   A 1 249 ? -7.80616  41.72426 14.50743  1.000 74.66154  ? 229 GLN   A CB  1 
ATOM   1730 C CG  . GLN   A 1 249 ? -8.84005  41.32780 15.55540  1.000 66.97426  ? 229 GLN   A CG  1 
ATOM   1731 C CD  . GLN   A 1 249 ? -10.26617 41.64789 15.13531  1.000 81.39701  ? 229 GLN   A CD  1 
ATOM   1732 O OE1 . GLN   A 1 249 ? -10.50047 42.50523 14.28212  1.000 78.16749  ? 229 GLN   A OE1 1 
ATOM   1733 N NE2 . GLN   A 1 249 ? -11.22831 40.95666 15.73769  1.000 84.80439  ? 229 GLN   A NE2 1 
ATOM   1734 N N   . ARG   A 1 250 ? -5.86124  41.07650 11.90788  1.000 67.28371  ? 230 ARG   A N   1 
ATOM   1735 C CA  . ARG   A 1 250 ? -4.93519  41.58572 10.90625  1.000 71.32295  ? 230 ARG   A CA  1 
ATOM   1736 C C   . ARG   A 1 250 ? -4.99103  40.80179 9.60195   1.000 76.35556  ? 230 ARG   A C   1 
ATOM   1737 O O   . ARG   A 1 250 ? -4.21902  41.09404 8.68316   1.000 77.33484  ? 230 ARG   A O   1 
ATOM   1738 C CB  . ARG   A 1 250 ? -3.50569  41.56930 11.45696  1.000 75.55250  ? 230 ARG   A CB  1 
ATOM   1739 C CG  . ARG   A 1 250 ? -3.39221  42.02608 12.90269  1.000 81.02517  ? 230 ARG   A CG  1 
ATOM   1740 C CD  . ARG   A 1 250 ? -3.88391  43.45518 13.08700  1.000 85.18864  ? 230 ARG   A CD  1 
ATOM   1741 N NE  . ARG   A 1 250 ? -3.88610  43.83938 14.49473  1.000 88.25176  ? 230 ARG   A NE  1 
ATOM   1742 N N   . SER   A 1 251 ? -5.88449  39.82073 9.49893   1.000 73.71099  ? 231 SER   A N   1 
ATOM   1743 C CA  . SER   A 1 251 ? -5.95527  38.93108 8.34773   1.000 78.30362  ? 231 SER   A CA  1 
ATOM   1744 C C   . SER   A 1 251 ? -6.77893  39.49867 7.19919   1.000 82.95904  ? 231 SER   A C   1 
ATOM   1745 O O   . SER   A 1 251 ? -6.84298  38.87316 6.13523   1.000 78.58106  ? 231 SER   A O   1 
ATOM   1746 C CB  . SER   A 1 251 ? -6.53273  37.57568 8.77072   1.000 76.02242  ? 231 SER   A CB  1 
ATOM   1747 O OG  . SER   A 1 251 ? -5.83236  37.05146 9.88548   1.000 70.06262  ? 231 SER   A OG  1 
ATOM   1748 N N   . PHE   A 1 252 ? -7.40709  40.65904 7.38354   1.000 78.81006  ? 232 PHE   A N   1 
ATOM   1749 C CA  . PHE   A 1 252 ? -8.22038  41.27870 6.34973   1.000 78.35137  ? 232 PHE   A CA  1 
ATOM   1750 C C   . PHE   A 1 252 ? -7.76380  42.72369 6.17049   1.000 86.53633  ? 232 PHE   A C   1 
ATOM   1751 O O   . PHE   A 1 252 ? -7.57823  43.43952 7.17028   1.000 90.18692  ? 232 PHE   A O   1 
ATOM   1752 C CB  . PHE   A 1 252 ? -9.70922  41.21875 6.71480   1.000 63.03688  ? 232 PHE   A CB  1 
ATOM   1753 C CG  . PHE   A 1 252 ? -10.20290 39.82851 6.99738   1.000 77.74863  ? 232 PHE   A CG  1 
ATOM   1754 C CD1 . PHE   A 1 252 ? -10.64985 39.01559 5.96805   1.000 66.30354  ? 232 PHE   A CD1 1 
ATOM   1755 C CD2 . PHE   A 1 252 ? -10.21089 39.33078 8.29071   1.000 62.61622  ? 232 PHE   A CD2 1 
ATOM   1756 C CE1 . PHE   A 1 252 ? -11.09938 37.73430 6.22296   1.000 67.40451  ? 232 PHE   A CE1 1 
ATOM   1757 C CE2 . PHE   A 1 252 ? -10.65791 38.05121 8.55155   1.000 72.59378  ? 232 PHE   A CE2 1 
ATOM   1758 C CZ  . PHE   A 1 252 ? -11.10382 37.25091 7.51645   1.000 66.20302  ? 232 PHE   A CZ  1 
ATOM   1759 N N   . PRO   A 1 253 ? -7.57621  43.19610 4.92572   1.000 98.01183  ? 233 PRO   A N   1 
ATOM   1760 C CA  . PRO   A 1 253 ? -7.83449  42.47597 3.67101   1.000 98.47290  ? 233 PRO   A CA  1 
ATOM   1761 C C   . PRO   A 1 253 ? -6.76673  41.44247 3.30663   1.000 91.56976  ? 233 PRO   A C   1 
ATOM   1762 O O   . PRO   A 1 253 ? -5.70048  41.41665 3.92219   1.000 96.82873  ? 233 PRO   A O   1 
ATOM   1763 C CB  . PRO   A 1 253 ? -7.85673  43.59926 2.63481   1.000 89.11899  ? 233 PRO   A CB  1 
ATOM   1764 C CG  . PRO   A 1 253 ? -6.89945  44.59914 3.17921   1.000 80.89857  ? 233 PRO   A CG  1 
ATOM   1765 C CD  . PRO   A 1 253 ? -7.09358  44.56724 4.67487   1.000 89.18087  ? 233 PRO   A CD  1 
HETATM 1766 C C10 . A1IJT B 2 .   ? -25.04509 24.57291 15.61997  1.000 44.96789  ? 301 A1IJT A C10 1 
HETATM 1767 C C01 . A1IJT B 2 .   ? -23.74893 25.35747 13.52136  1.000 45.16706  ? 301 A1IJT A C01 1 
HETATM 1768 C C03 . A1IJT B 2 .   ? -26.26460 24.69986 13.55898  1.000 52.14014  ? 301 A1IJT A C03 1 
HETATM 1769 C C04 . A1IJT B 2 .   ? -27.22347 24.22444 14.62449  1.000 47.43252  ? 301 A1IJT A C04 1 
HETATM 1770 C C06 . A1IJT B 2 .   ? -29.17903 23.51110 15.60454  1.000 56.47419  ? 301 A1IJT A C06 1 
HETATM 1771 C C07 . A1IJT B 2 .   ? -28.57121 23.40264 16.84429  1.000 54.66572  ? 301 A1IJT A C07 1 
HETATM 1772 C C08 . A1IJT B 2 .   ? -27.23198 23.72364 16.95658  1.000 55.05732  ? 301 A1IJT A C08 1 
HETATM 1773 C C09 . A1IJT B 2 .   ? -26.50962 24.14738 15.84414  1.000 51.84868  ? 301 A1IJT A C09 1 
HETATM 1774 N N02 . A1IJT B 2 .   ? -25.03512 24.89403 14.13565  1.000 54.39687  ? 301 A1IJT A N02 1 
HETATM 1775 N N05 . A1IJT B 2 .   ? -28.53487 23.91891 14.47414  1.000 57.47501  ? 301 A1IJT A N05 1 
HETATM 1776 O O11 . A1IJT B 2 .   ? -26.50089 24.89143 12.37930  1.000 52.80454  ? 301 A1IJT A O11 1 
HETATM 1777 O O   . HOH   C 3 .   ? -34.34962 30.51096 8.73074   1.000 60.18232  ? 401 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -6.17624  31.79667 -2.03323  1.000 65.59866  ? 402 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -0.43950  22.37336 6.42271   1.000 64.45164  ? 403 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -17.73741 28.96489 17.12040  1.000 55.97457  ? 404 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -34.42520 35.45990 11.30286  1.000 54.81051  ? 405 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -3.01433  5.74748  18.80960  1.000 65.63041  ? 406 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -7.31108  29.02530 3.58482   1.000 53.11736  ? 407 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 2.10766   13.24676 19.54251  1.000 59.80305  ? 408 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -2.155    23.809   21.526    1.000 59.59333  ? 409 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 1.44642   15.46644 11.69803  1.000 60.22817  ? 410 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -1.20977  21.85740 10.68209  1.000 65.19075  ? 411 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -11.31806 30.41560 8.80863   1.000 47.05225  ? 412 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -25.18022 17.65405 14.49684  1.000 59.76692  ? 413 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -29.67843 31.12663 13.17781  1.000 50.92203  ? 414 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -31.06160 38.63940 26.27275  1.000 63.08191  ? 415 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -21.50295 19.02920 -9.17999  1.000 60.83890  ? 416 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -22.10219 31.39801 15.93919  1.000 50.52641  ? 417 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -27.28607 31.44033 -4.28439  1.000 59.53789  ? 418 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -24.28172 28.51799 14.75939  1.000 51.11653  ? 419 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -19.15578 27.88694 12.84848  1.000 53.06936  ? 420 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -11.27656 41.96506 18.38362  1.000 68.81742  ? 421 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -18.45739 20.81253 7.62935   1.000 50.50778  ? 422 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -7.60251  24.94247 5.60476   1.000 60.71598  ? 423 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -25.96267 20.66578 17.28808  1.000 55.96059  ? 424 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -30.88787 42.84136 13.32768  1.000 58.58162  ? 425 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -23.28419 34.27962 -5.68829  1.000 64.14953  ? 426 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -13.83115 39.00960 4.18375   1.000 65.04344  ? 427 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -34.11475 42.12140 6.52491   1.000 59.48978  ? 428 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -24.60822 7.32134  1.73030   1.000 56.00297  ? 429 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -27.09479 39.07380 27.43676  1.000 54.78292  ? 430 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -21.81755 7.55868  18.03582  1.000 61.91951  ? 431 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -17.74719 20.91530 10.86630  1.000 55.41251  ? 432 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -32.83270 36.14057 4.28660   1.000 64.16984  ? 433 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -33.74761 37.88317 0.22912   1.000 58.08917  ? 434 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 0.07678   3.85162  31.74152  1.000 56.20093  ? 435 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -26.33652 5.55741  4.50603   1.000 69.95962  ? 436 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -2.91218  20.20981 17.36260  1.000 65.11188  ? 437 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -16.635   8.458    12.599    1.000 61.53449  ? 438 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -33.22918 35.06341 -1.48564  1.000 59.87796  ? 439 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -0.18824  26.32021 6.64332   1.000 64.93903  ? 440 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 0.249     25.315   21.923    1.000 63.80675  ? 441 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -31.33029 25.62074 -11.48606 1.000 68.76801  ? 442 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -23.25103 28.26322 -12.09348 1.000 69.62075  ? 443 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -8.94865  35.10056 3.35655   1.000 64.59785  ? 444 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -21.01533 43.42414 14.28852  1.000 63.81978  ? 445 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -34.951   32.108   30.142    1.000 64.45014  ? 446 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -33.87614 40.12433 -2.43488  1.000 54.97358  ? 447 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -23.05005 44.49085 10.44456  1.000 67.12167  ? 448 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -37.22506 38.60793 22.29563  1.000 75.19643  ? 449 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -4.24800  1.55105  29.27585  1.000 57.56080  ? 450 HOH   A O   1 
# 
