data_8VIP
# 
_entry.id   8VIP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8VIP         pdb_00008vip 10.2210/pdb8vip/pdb 
WWPDB D_1000280328 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
3 'Structure model' 1 2 2024-12-04 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 3 'Structure model' citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
5 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VIP 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu Scott   Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 jbose@kumc.edu  Jeffrey Bose   ? 'principal investigator/group leader' 0000-0003-3394-9557 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lovell, S.'       1 0000-0002-3215-4472 
'Kashipathy, M.M.' 2 0000-0003-0435-989X 
'Battaile, K.P.'   3 0000-0003-0833-3259 
'Bose, J.L.'       4 0000-0003-0514-281X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            300 
_citation.language                  ? 
_citation.page_first                107920 
_citation.page_last                 107920 
_citation.title                     
'Molecular insights into the structure and function of the Staphylococcus aureus fatty acid kinase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.107920 
_citation.pdbx_database_id_PubMed   39454961 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Myers, M.J.'       1  ? 
primary 'Xu, Z.'            2  ? 
primary 'Ryan, B.J.'        3  ? 
primary 'DeMars, Z.R.'      4  ? 
primary 'Ridder, M.J.'      5  ? 
primary 'Johnson, D.K.'     6  ? 
primary 'Krute, C.N.'       7  ? 
primary 'Flynn, T.S.'       8  ? 
primary 'Kashipathy, M.M.'  9  ? 
primary 'Battaile, K.P.'    10 ? 
primary 'Schnicker, N.'     11 ? 
primary 'Lovell, S.'        12 ? 
primary 'Freudenthal, B.D.' 13 ? 
primary 'Bose, J.L.'        14 ? 
# 
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 'FATTY ACID KINASE A'                         24816.246 1   ? ? ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   1   ? ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION'                          54.938    2   ? ? ? ? 
4 water       nat water                                         18.015    143 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNL
SKNIGELGKTFSKGLLMGARGNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAA
QAAIEKANNTEDCIELMEYIIVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNL
SKNIGELGKTFSKGLLMGARGNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAA
QAAIEKANNTEDCIELMEYIIVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_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 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
3 'MANGANESE (II) ION'                          MN  
4 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  ILE n 
1 23  SER n 
1 24  LYS n 
1 25  ILE n 
1 26  ASN n 
1 27  GLY n 
1 28  LYS n 
1 29  LEU n 
1 30  PHE n 
1 31  ALA n 
1 32  ASP n 
1 33  MET n 
1 34  ILE n 
1 35  ILE n 
1 36  GLN n 
1 37  GLY n 
1 38  ALA n 
1 39  GLN n 
1 40  ASN n 
1 41  LEU n 
1 42  SER n 
1 43  ASN n 
1 44  ASN n 
1 45  ALA n 
1 46  ASP n 
1 47  LEU n 
1 48  VAL n 
1 49  ASP n 
1 50  SER n 
1 51  LEU n 
1 52  ASN n 
1 53  VAL n 
1 54  TYR n 
1 55  PRO n 
1 56  VAL n 
1 57  PRO n 
1 58  ASP n 
1 59  GLY n 
1 60  ASP n 
1 61  THR n 
1 62  GLY n 
1 63  THR n 
1 64  ASN n 
1 65  MET n 
1 66  ASN n 
1 67  LEU n 
1 68  THR n 
1 69  MET n 
1 70  THR n 
1 71  SER n 
1 72  GLY n 
1 73  ARG n 
1 74  GLU n 
1 75  GLU n 
1 76  VAL n 
1 77  GLU n 
1 78  ASN n 
1 79  ASN n 
1 80  LEU n 
1 81  SER n 
1 82  LYS n 
1 83  ASN n 
1 84  ILE n 
1 85  GLY n 
1 86  GLU n 
1 87  LEU n 
1 88  GLY n 
1 89  LYS n 
1 90  THR n 
1 91  PHE n 
1 92  SER n 
1 93  LYS n 
1 94  GLY n 
1 95  LEU n 
1 96  LEU n 
1 97  MET n 
1 98  GLY n 
1 99  ALA n 
1 100 ARG n 
1 101 GLY n 
1 102 ASN n 
1 103 SER n 
1 104 GLY n 
1 105 VAL n 
1 106 ILE n 
1 107 LEU n 
1 108 SER n 
1 109 GLN n 
1 110 LEU n 
1 111 PHE n 
1 112 ARG n 
1 113 GLY n 
1 114 PHE n 
1 115 CYS n 
1 116 LYS n 
1 117 ASN n 
1 118 ILE n 
1 119 GLU n 
1 120 SER n 
1 121 GLU n 
1 122 SER n 
1 123 GLU n 
1 124 ILE n 
1 125 ASN n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 LEU n 
1 130 ALA n 
1 131 GLU n 
1 132 SER n 
1 133 PHE n 
1 134 GLN n 
1 135 ALA n 
1 136 GLY n 
1 137 VAL n 
1 138 GLU n 
1 139 THR n 
1 140 ALA n 
1 141 TYR n 
1 142 LYS n 
1 143 ALA n 
1 144 VAL n 
1 145 MET n 
1 146 LYS n 
1 147 PRO n 
1 148 VAL n 
1 149 GLU n 
1 150 GLY n 
1 151 THR n 
1 152 ILE n 
1 153 LEU n 
1 154 THR n 
1 155 VAL n 
1 156 ALA n 
1 157 LYS n 
1 158 ASP n 
1 159 ALA n 
1 160 ALA n 
1 161 GLN n 
1 162 ALA n 
1 163 ALA n 
1 164 ILE n 
1 165 GLU n 
1 166 LYS n 
1 167 ALA n 
1 168 ASN n 
1 169 ASN n 
1 170 THR n 
1 171 GLU n 
1 172 ASP n 
1 173 CYS n 
1 174 ILE n 
1 175 GLU n 
1 176 LEU n 
1 177 MET n 
1 178 GLU n 
1 179 TYR n 
1 180 ILE n 
1 181 ILE n 
1 182 VAL n 
1 183 LYS n 
1 184 ALA n 
1 185 ASN n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 GLU n 
1 190 ASN n 
1 191 THR n 
1 192 PRO n 
1 193 ASN n 
1 194 LEU n 
1 195 LEU n 
1 196 ALA n 
1 197 VAL n 
1 198 LEU n 
1 199 LYS n 
1 200 GLU n 
1 201 VAL n 
1 202 GLY n 
1 203 VAL n 
1 204 VAL n 
1 205 ASP n 
1 206 SER n 
1 207 GLY n 
1 208 GLY n 
1 209 LYS n 
1 210 GLY n 
1 211 LEU n 
1 212 LEU n 
1 213 CYS n 
1 214 VAL n 
1 215 TYR n 
1 216 GLU n 
1 217 GLY n 
1 218 PHE n 
1 219 LEU n 
1 220 LYS n 
1 221 ALA n 
1 222 LEU n 
1 223 LYS n 
1 224 GLY n 
1 225 GLU n 
1 226 LYS n 
1 227 VAL n 
1 228 GLU n 
1 229 ALA n 
1 230 LYS n 
1 231 VAL n 
1 232 ALA 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                   232 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAOUHSC_01193 
_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      'Staphylococcus aureus subsp. aureus NCTC 8325' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     93061 
_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               'BL21(DE3)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
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 
MN  non-polymer         . 'MANGANESE (II) ION'                          ? 'Mn 2'              54.938  
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 
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   1   MET MET A . n 
A 1 22  ILE 22  2   2   ILE ILE A . n 
A 1 23  SER 23  3   3   SER SER A . n 
A 1 24  LYS 24  4   4   LYS LYS A . n 
A 1 25  ILE 25  5   5   ILE ILE A . n 
A 1 26  ASN 26  6   6   ASN ASN A . n 
A 1 27  GLY 27  7   7   GLY GLY A . n 
A 1 28  LYS 28  8   8   LYS LYS A . n 
A 1 29  LEU 29  9   9   LEU LEU A . n 
A 1 30  PHE 30  10  10  PHE PHE A . n 
A 1 31  ALA 31  11  11  ALA ALA A . n 
A 1 32  ASP 32  12  12  ASP ASP A . n 
A 1 33  MET 33  13  13  MET MET A . n 
A 1 34  ILE 34  14  14  ILE ILE A . n 
A 1 35  ILE 35  15  15  ILE ILE A . n 
A 1 36  GLN 36  16  16  GLN GLN A . n 
A 1 37  GLY 37  17  17  GLY GLY A . n 
A 1 38  ALA 38  18  18  ALA ALA A . n 
A 1 39  GLN 39  19  19  GLN GLN A . n 
A 1 40  ASN 40  20  20  ASN ASN A . n 
A 1 41  LEU 41  21  21  LEU LEU A . n 
A 1 42  SER 42  22  22  SER SER A . n 
A 1 43  ASN 43  23  23  ASN ASN A . n 
A 1 44  ASN 44  24  24  ASN ASN A . n 
A 1 45  ALA 45  25  25  ALA ALA A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  LEU 47  27  27  LEU LEU A . n 
A 1 48  VAL 48  28  28  VAL VAL A . n 
A 1 49  ASP 49  29  29  ASP ASP A . n 
A 1 50  SER 50  30  30  SER SER A . n 
A 1 51  LEU 51  31  31  LEU LEU A . n 
A 1 52  ASN 52  32  32  ASN ASN A . n 
A 1 53  VAL 53  33  33  VAL VAL A . n 
A 1 54  TYR 54  34  34  TYR TYR A . n 
A 1 55  PRO 55  35  35  PRO PRO A . n 
A 1 56  VAL 56  36  36  VAL VAL A . n 
A 1 57  PRO 57  37  37  PRO PRO A . n 
A 1 58  ASP 58  38  38  ASP ASP A . n 
A 1 59  GLY 59  39  39  GLY GLY A . n 
A 1 60  ASP 60  40  40  ASP ASP A . n 
A 1 61  THR 61  41  41  THR THR A . n 
A 1 62  GLY 62  42  42  GLY GLY A . n 
A 1 63  THR 63  43  43  THR THR A . n 
A 1 64  ASN 64  44  44  ASN ASN A . n 
A 1 65  MET 65  45  45  MET MET A . n 
A 1 66  ASN 66  46  46  ASN ASN A . n 
A 1 67  LEU 67  47  47  LEU LEU A . n 
A 1 68  THR 68  48  48  THR THR A . n 
A 1 69  MET 69  49  49  MET MET A . n 
A 1 70  THR 70  50  50  THR THR A . n 
A 1 71  SER 71  51  51  SER SER A . n 
A 1 72  GLY 72  52  52  GLY GLY A . n 
A 1 73  ARG 73  53  53  ARG ARG A . n 
A 1 74  GLU 74  54  54  GLU GLU A . n 
A 1 75  GLU 75  55  55  GLU GLU A . n 
A 1 76  VAL 76  56  56  VAL VAL A . n 
A 1 77  GLU 77  57  57  GLU GLU A . n 
A 1 78  ASN 78  58  58  ASN ASN A . n 
A 1 79  ASN 79  59  59  ASN ASN A . n 
A 1 80  LEU 80  60  60  LEU LEU A . n 
A 1 81  SER 81  61  61  SER SER A . n 
A 1 82  LYS 82  62  62  LYS LYS A . n 
A 1 83  ASN 83  63  63  ASN ASN A . n 
A 1 84  ILE 84  64  64  ILE ILE A . n 
A 1 85  GLY 85  65  65  GLY GLY A . n 
A 1 86  GLU 86  66  66  GLU GLU A . n 
A 1 87  LEU 87  67  67  LEU LEU A . n 
A 1 88  GLY 88  68  68  GLY GLY A . n 
A 1 89  LYS 89  69  69  LYS LYS A . n 
A 1 90  THR 90  70  70  THR THR A . n 
A 1 91  PHE 91  71  71  PHE PHE A . n 
A 1 92  SER 92  72  72  SER SER A . n 
A 1 93  LYS 93  73  73  LYS LYS A . n 
A 1 94  GLY 94  74  74  GLY GLY A . n 
A 1 95  LEU 95  75  75  LEU LEU A . n 
A 1 96  LEU 96  76  76  LEU LEU A . n 
A 1 97  MET 97  77  77  MET MET A . n 
A 1 98  GLY 98  78  78  GLY GLY A . n 
A 1 99  ALA 99  79  79  ALA ALA A . n 
A 1 100 ARG 100 80  80  ARG ARG A . n 
A 1 101 GLY 101 81  81  GLY GLY A . n 
A 1 102 ASN 102 82  82  ASN ASN A . n 
A 1 103 SER 103 83  83  SER SER A . n 
A 1 104 GLY 104 84  84  GLY GLY A . n 
A 1 105 VAL 105 85  85  VAL VAL A . n 
A 1 106 ILE 106 86  86  ILE ILE A . n 
A 1 107 LEU 107 87  87  LEU LEU A . n 
A 1 108 SER 108 88  88  SER SER A . n 
A 1 109 GLN 109 89  89  GLN GLN A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 PHE 111 91  91  PHE PHE A . n 
A 1 112 ARG 112 92  92  ARG ARG A . n 
A 1 113 GLY 113 93  93  GLY GLY A . n 
A 1 114 PHE 114 94  94  PHE PHE A . n 
A 1 115 CYS 115 95  95  CYS CYS A . n 
A 1 116 LYS 116 96  96  LYS LYS A . n 
A 1 117 ASN 117 97  97  ASN ASN A . n 
A 1 118 ILE 118 98  98  ILE ILE A . n 
A 1 119 GLU 119 99  99  GLU GLU A . n 
A 1 120 SER 120 100 100 SER SER A . n 
A 1 121 GLU 121 101 101 GLU GLU A . n 
A 1 122 SER 122 102 102 SER SER A . n 
A 1 123 GLU 123 103 103 GLU GLU A . n 
A 1 124 ILE 124 104 104 ILE ILE A . n 
A 1 125 ASN 125 105 105 ASN ASN A . n 
A 1 126 SER 126 106 106 SER SER A . n 
A 1 127 LYS 127 107 107 LYS LYS A . n 
A 1 128 LEU 128 108 108 LEU LEU A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 ALA 130 110 110 ALA ALA A . n 
A 1 131 GLU 131 111 111 GLU GLU A . n 
A 1 132 SER 132 112 112 SER SER A . n 
A 1 133 PHE 133 113 113 PHE PHE A . n 
A 1 134 GLN 134 114 114 GLN GLN A . n 
A 1 135 ALA 135 115 115 ALA ALA A . n 
A 1 136 GLY 136 116 116 GLY GLY A . n 
A 1 137 VAL 137 117 117 VAL VAL A . n 
A 1 138 GLU 138 118 118 GLU GLU A . n 
A 1 139 THR 139 119 119 THR THR A . n 
A 1 140 ALA 140 120 120 ALA ALA A . n 
A 1 141 TYR 141 121 121 TYR TYR A . n 
A 1 142 LYS 142 122 122 LYS LYS A . n 
A 1 143 ALA 143 123 123 ALA ALA A . n 
A 1 144 VAL 144 124 124 VAL VAL A . n 
A 1 145 MET 145 125 125 MET MET A . n 
A 1 146 LYS 146 126 126 LYS LYS A . n 
A 1 147 PRO 147 127 127 PRO PRO A . n 
A 1 148 VAL 148 128 128 VAL VAL A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 GLY 150 130 130 GLY GLY A . n 
A 1 151 THR 151 131 131 THR THR A . n 
A 1 152 ILE 152 132 132 ILE ILE A . n 
A 1 153 LEU 153 133 133 LEU LEU A . n 
A 1 154 THR 154 134 134 THR THR A . n 
A 1 155 VAL 155 135 135 VAL VAL A . n 
A 1 156 ALA 156 136 136 ALA ALA A . n 
A 1 157 LYS 157 137 137 LYS LYS A . n 
A 1 158 ASP 158 138 138 ASP ASP A . n 
A 1 159 ALA 159 139 139 ALA ALA A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 GLN 161 141 141 GLN GLN A . n 
A 1 162 ALA 162 142 142 ALA ALA A . n 
A 1 163 ALA 163 143 143 ALA ALA A . n 
A 1 164 ILE 164 144 144 ILE ILE A . n 
A 1 165 GLU 165 145 145 GLU GLU A . n 
A 1 166 LYS 166 146 146 LYS LYS A . n 
A 1 167 ALA 167 147 147 ALA ALA A . n 
A 1 168 ASN 168 148 148 ASN ASN A . n 
A 1 169 ASN 169 149 149 ASN ASN A . n 
A 1 170 THR 170 150 150 THR THR A . n 
A 1 171 GLU 171 151 151 GLU GLU A . n 
A 1 172 ASP 172 152 152 ASP ASP A . n 
A 1 173 CYS 173 153 153 CYS CYS A . n 
A 1 174 ILE 174 154 154 ILE ILE A . n 
A 1 175 GLU 175 155 155 GLU GLU A . n 
A 1 176 LEU 176 156 156 LEU LEU A . n 
A 1 177 MET 177 157 157 MET MET A . n 
A 1 178 GLU 178 158 158 GLU GLU A . n 
A 1 179 TYR 179 159 159 TYR TYR A . n 
A 1 180 ILE 180 160 160 ILE ILE A . n 
A 1 181 ILE 181 161 161 ILE ILE A . n 
A 1 182 VAL 182 162 162 VAL VAL A . n 
A 1 183 LYS 183 163 163 LYS LYS A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 ASN 185 165 165 ASN ASN A . n 
A 1 186 GLU 186 166 166 GLU GLU A . n 
A 1 187 SER 187 167 167 SER SER A . n 
A 1 188 LEU 188 168 168 LEU LEU A . n 
A 1 189 GLU 189 169 169 GLU GLU A . n 
A 1 190 ASN 190 170 170 ASN ASN A . n 
A 1 191 THR 191 171 171 THR THR A . n 
A 1 192 PRO 192 172 172 PRO PRO A . n 
A 1 193 ASN 193 173 173 ASN ASN A . n 
A 1 194 LEU 194 174 174 LEU LEU A . n 
A 1 195 LEU 195 175 175 LEU LEU A . n 
A 1 196 ALA 196 176 176 ALA ALA A . n 
A 1 197 VAL 197 177 177 VAL VAL A . n 
A 1 198 LEU 198 178 178 LEU LEU A . n 
A 1 199 LYS 199 179 179 LYS LYS A . n 
A 1 200 GLU 200 180 180 GLU GLU A . n 
A 1 201 VAL 201 181 181 VAL VAL A . n 
A 1 202 GLY 202 182 182 GLY GLY A . n 
A 1 203 VAL 203 183 183 VAL VAL A . n 
A 1 204 VAL 204 184 184 VAL VAL A . n 
A 1 205 ASP 205 185 185 ASP ASP A . n 
A 1 206 SER 206 186 186 SER SER A . n 
A 1 207 GLY 207 187 187 GLY GLY A . n 
A 1 208 GLY 208 188 188 GLY GLY A . n 
A 1 209 LYS 209 189 189 LYS LYS A . n 
A 1 210 GLY 210 190 190 GLY GLY A . n 
A 1 211 LEU 211 191 191 LEU LEU A . n 
A 1 212 LEU 212 192 192 LEU LEU A . n 
A 1 213 CYS 213 193 193 CYS CYS A . n 
A 1 214 VAL 214 194 194 VAL VAL A . n 
A 1 215 TYR 215 195 195 TYR TYR A . n 
A 1 216 GLU 216 196 196 GLU GLU A . n 
A 1 217 GLY 217 197 197 GLY GLY A . n 
A 1 218 PHE 218 198 198 PHE PHE A . n 
A 1 219 LEU 219 199 199 LEU LEU A . n 
A 1 220 LYS 220 200 200 LYS LYS A . n 
A 1 221 ALA 221 201 201 ALA ALA A . n 
A 1 222 LEU 222 202 202 LEU LEU A . n 
A 1 223 LYS 223 203 203 LYS LYS A . n 
A 1 224 GLY 224 204 204 GLY GLY A . n 
A 1 225 GLU 225 205 205 GLU GLU A . n 
A 1 226 LYS 226 206 206 LYS LYS A . n 
A 1 227 VAL 227 207 207 VAL VAL A . n 
A 1 228 GLU 228 208 208 GLU GLU A . n 
A 1 229 ALA 229 209 209 ALA ALA A . n 
A 1 230 LYS 230 210 ?   ?   ?   A . n 
A 1 231 VAL 231 211 ?   ?   ?   A . n 
A 1 232 ALA 232 212 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 ANP 1   301 1   ANP ANP A . 
C 3 MN  1   302 1   MN  MN  A . 
D 3 MN  1   303 2   MN  MN  A . 
E 4 HOH 1   401 137 HOH HOH A . 
E 4 HOH 2   402 97  HOH HOH A . 
E 4 HOH 3   403 116 HOH HOH A . 
E 4 HOH 4   404 123 HOH HOH A . 
E 4 HOH 5   405 59  HOH HOH A . 
E 4 HOH 6   406 1   HOH HOH A . 
E 4 HOH 7   407 15  HOH HOH A . 
E 4 HOH 8   408 89  HOH HOH A . 
E 4 HOH 9   409 127 HOH HOH A . 
E 4 HOH 10  410 85  HOH HOH A . 
E 4 HOH 11  411 33  HOH HOH A . 
E 4 HOH 12  412 139 HOH HOH A . 
E 4 HOH 13  413 96  HOH HOH A . 
E 4 HOH 14  414 140 HOH HOH A . 
E 4 HOH 15  415 11  HOH HOH A . 
E 4 HOH 16  416 7   HOH HOH A . 
E 4 HOH 17  417 52  HOH HOH A . 
E 4 HOH 18  418 9   HOH HOH A . 
E 4 HOH 19  419 110 HOH HOH A . 
E 4 HOH 20  420 31  HOH HOH A . 
E 4 HOH 21  421 143 HOH HOH A . 
E 4 HOH 22  422 133 HOH HOH A . 
E 4 HOH 23  423 35  HOH HOH A . 
E 4 HOH 24  424 36  HOH HOH A . 
E 4 HOH 25  425 102 HOH HOH A . 
E 4 HOH 26  426 79  HOH HOH A . 
E 4 HOH 27  427 129 HOH HOH A . 
E 4 HOH 28  428 3   HOH HOH A . 
E 4 HOH 29  429 30  HOH HOH A . 
E 4 HOH 30  430 73  HOH HOH A . 
E 4 HOH 31  431 64  HOH HOH A . 
E 4 HOH 32  432 98  HOH HOH A . 
E 4 HOH 33  433 41  HOH HOH A . 
E 4 HOH 34  434 74  HOH HOH A . 
E 4 HOH 35  435 114 HOH HOH A . 
E 4 HOH 36  436 39  HOH HOH A . 
E 4 HOH 37  437 119 HOH HOH A . 
E 4 HOH 38  438 144 HOH HOH A . 
E 4 HOH 39  439 58  HOH HOH A . 
E 4 HOH 40  440 83  HOH HOH A . 
E 4 HOH 41  441 38  HOH HOH A . 
E 4 HOH 42  442 40  HOH HOH A . 
E 4 HOH 43  443 10  HOH HOH A . 
E 4 HOH 44  444 34  HOH HOH A . 
E 4 HOH 45  445 5   HOH HOH A . 
E 4 HOH 46  446 124 HOH HOH A . 
E 4 HOH 47  447 92  HOH HOH A . 
E 4 HOH 48  448 121 HOH HOH A . 
E 4 HOH 49  449 134 HOH HOH A . 
E 4 HOH 50  450 69  HOH HOH A . 
E 4 HOH 51  451 105 HOH HOH A . 
E 4 HOH 52  452 12  HOH HOH A . 
E 4 HOH 53  453 16  HOH HOH A . 
E 4 HOH 54  454 43  HOH HOH A . 
E 4 HOH 55  455 50  HOH HOH A . 
E 4 HOH 56  456 6   HOH HOH A . 
E 4 HOH 57  457 13  HOH HOH A . 
E 4 HOH 58  458 115 HOH HOH A . 
E 4 HOH 59  459 26  HOH HOH A . 
E 4 HOH 60  460 44  HOH HOH A . 
E 4 HOH 61  461 22  HOH HOH A . 
E 4 HOH 62  462 90  HOH HOH A . 
E 4 HOH 63  463 101 HOH HOH A . 
E 4 HOH 64  464 70  HOH HOH A . 
E 4 HOH 65  465 68  HOH HOH A . 
E 4 HOH 66  466 8   HOH HOH A . 
E 4 HOH 67  467 95  HOH HOH A . 
E 4 HOH 68  468 60  HOH HOH A . 
E 4 HOH 69  469 48  HOH HOH A . 
E 4 HOH 70  470 37  HOH HOH A . 
E 4 HOH 71  471 77  HOH HOH A . 
E 4 HOH 72  472 62  HOH HOH A . 
E 4 HOH 73  473 51  HOH HOH A . 
E 4 HOH 74  474 100 HOH HOH A . 
E 4 HOH 75  475 84  HOH HOH A . 
E 4 HOH 76  476 17  HOH HOH A . 
E 4 HOH 77  477 42  HOH HOH A . 
E 4 HOH 78  478 19  HOH HOH A . 
E 4 HOH 79  479 25  HOH HOH A . 
E 4 HOH 80  480 49  HOH HOH A . 
E 4 HOH 81  481 75  HOH HOH A . 
E 4 HOH 82  482 24  HOH HOH A . 
E 4 HOH 83  483 113 HOH HOH A . 
E 4 HOH 84  484 46  HOH HOH A . 
E 4 HOH 85  485 27  HOH HOH A . 
E 4 HOH 86  486 20  HOH HOH A . 
E 4 HOH 87  487 28  HOH HOH A . 
E 4 HOH 88  488 118 HOH HOH A . 
E 4 HOH 89  489 2   HOH HOH A . 
E 4 HOH 90  490 67  HOH HOH A . 
E 4 HOH 91  491 63  HOH HOH A . 
E 4 HOH 92  492 91  HOH HOH A . 
E 4 HOH 93  493 61  HOH HOH A . 
E 4 HOH 94  494 108 HOH HOH A . 
E 4 HOH 95  495 82  HOH HOH A . 
E 4 HOH 96  496 122 HOH HOH A . 
E 4 HOH 97  497 29  HOH HOH A . 
E 4 HOH 98  498 131 HOH HOH A . 
E 4 HOH 99  499 45  HOH HOH A . 
E 4 HOH 100 500 78  HOH HOH A . 
E 4 HOH 101 501 47  HOH HOH A . 
E 4 HOH 102 502 18  HOH HOH A . 
E 4 HOH 103 503 54  HOH HOH A . 
E 4 HOH 104 504 23  HOH HOH A . 
E 4 HOH 105 505 56  HOH HOH A . 
E 4 HOH 106 506 106 HOH HOH A . 
E 4 HOH 107 507 21  HOH HOH A . 
E 4 HOH 108 508 14  HOH HOH A . 
E 4 HOH 109 509 86  HOH HOH A . 
E 4 HOH 110 510 66  HOH HOH A . 
E 4 HOH 111 511 145 HOH HOH A . 
E 4 HOH 112 512 80  HOH HOH A . 
E 4 HOH 113 513 111 HOH HOH A . 
E 4 HOH 114 514 94  HOH HOH A . 
E 4 HOH 115 515 72  HOH HOH A . 
E 4 HOH 116 516 141 HOH HOH A . 
E 4 HOH 117 517 128 HOH HOH A . 
E 4 HOH 118 518 142 HOH HOH A . 
E 4 HOH 119 519 87  HOH HOH A . 
E 4 HOH 120 520 65  HOH HOH A . 
E 4 HOH 121 521 146 HOH HOH A . 
E 4 HOH 122 522 130 HOH HOH A . 
E 4 HOH 123 523 125 HOH HOH A . 
E 4 HOH 124 524 120 HOH HOH A . 
E 4 HOH 125 525 55  HOH HOH A . 
E 4 HOH 126 526 117 HOH HOH A . 
E 4 HOH 127 527 32  HOH HOH A . 
E 4 HOH 128 528 76  HOH HOH A . 
E 4 HOH 129 529 132 HOH HOH A . 
E 4 HOH 130 530 57  HOH HOH A . 
E 4 HOH 131 531 93  HOH HOH A . 
E 4 HOH 132 532 99  HOH HOH A . 
E 4 HOH 133 533 71  HOH HOH A . 
E 4 HOH 134 534 138 HOH HOH A . 
E 4 HOH 135 535 107 HOH HOH A . 
E 4 HOH 136 536 126 HOH HOH A . 
E 4 HOH 137 537 135 HOH HOH A . 
E 4 HOH 138 538 103 HOH HOH A . 
E 4 HOH 139 539 109 HOH HOH A . 
E 4 HOH 140 540 136 HOH HOH A . 
E 4 HOH 141 541 81  HOH HOH A . 
E 4 HOH 142 542 104 HOH HOH A . 
E 4 HOH 143 543 112 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 MET 1   ? CG  ? A MET 21  CG  
2  1 Y 1 A MET 1   ? SD  ? A MET 21  SD  
3  1 Y 1 A MET 1   ? CE  ? A MET 21  CE  
4  1 Y 1 A LYS 4   ? CE  ? A LYS 24  CE  
5  1 Y 1 A LYS 4   ? NZ  ? A LYS 24  NZ  
6  1 Y 1 A LYS 73  ? CE  ? A LYS 93  CE  
7  1 Y 1 A LYS 73  ? NZ  ? A LYS 93  NZ  
8  1 Y 1 A ARG 80  ? CD  ? A ARG 100 CD  
9  1 Y 1 A ARG 80  ? NE  ? A ARG 100 NE  
10 1 Y 1 A ARG 80  ? CZ  ? A ARG 100 CZ  
11 1 Y 1 A ARG 80  ? NH1 ? A ARG 100 NH1 
12 1 Y 1 A ARG 80  ? NH2 ? A ARG 100 NH2 
13 1 Y 1 A LYS 107 ? CD  ? A LYS 127 CD  
14 1 Y 1 A LYS 107 ? CE  ? A LYS 127 CE  
15 1 Y 1 A LYS 107 ? NZ  ? A LYS 127 NZ  
16 1 Y 1 A LYS 179 ? CE  ? A LYS 199 CE  
17 1 Y 1 A LYS 179 ? NZ  ? A LYS 199 NZ  
18 1 Y 1 A LYS 206 ? CE  ? A LYS 226 CE  
19 1 Y 1 A LYS 206 ? NZ  ? A LYS 226 NZ  
20 1 Y 1 A GLU 208 ? CG  ? A GLU 228 CG  
21 1 Y 1 A GLU 208 ? CD  ? A GLU 228 CD  
22 1 Y 1 A GLU 208 ? OE1 ? A GLU 228 OE1 
23 1 Y 1 A GLU 208 ? OE2 ? A GLU 228 OE2 
# 
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  ? ? ? '(1.15_3460: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? CRANK2  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VIP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.812 
_cell.length_a_esd                 ? 
_cell.length_b                     57.025 
_cell.length_b_esd                 ? 
_cell.length_c                     81.696 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VIP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8VIP 
_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             2.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.78 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              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    
;Proplex D9: 15% (w/v) PEG 6000, 100 mM MES pH 6.5, 5% (v/v) 2-methyl-2,4-pentanediol, Cryo: 85% crystallization solution and 15% (v/v) MPD, 2.5 mM MnCl2 and 2.5 mM AMP-PNP added to the protein prior to crystallization.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-03-30 
_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                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.7712 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.7712 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VIP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               46.76 
_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                                     36210 
_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                           97.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.91 
_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                                0.068 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.065 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.77 
_reflns_shell.d_res_low                                     1.81 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           2095 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             798 
_reflns_shell.percent_possible_obs                          72.5 
_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                               2.6 
_reflns_shell.pdbx_chi_squared                              0.82 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.5 
_reflns_shell.pdbx_Rrim_I_all                               0.404 
_reflns_shell.pdbx_Rpim_I_all                               0.220 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.884 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.335 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8VIP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.770 
_refine.ls_d_res_low                             46.760 
_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                     36210 
_refine.ls_number_reflns_R_free                  1756 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.18 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1499 
_refine.ls_R_factor_R_free                       0.1861 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1481 
_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                          0.09 
_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          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.07 
_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                            0.16 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.770 
_refine_hist.d_res_low                        46.760 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               1712 
_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        1536 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.009  ? 1582 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.092  ? 2143 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.303 ? 957  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061  ? 257  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 275  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.7701 1.8180 . . 77  1817 66.00  . . . . 0.2122 . . . . . . . . . . . 0.2708 
'X-RAY DIFFRACTION' 1.8180 1.8715 . . 127 2553 92.00  . . . . 0.1869 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 1.8715 1.9319 . . 137 2664 97.00  . . . . 0.1669 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 1.9319 2.0009 . . 113 2711 98.00  . . . . 0.1531 . . . . . . . . . . . 0.2436 
'X-RAY DIFFRACTION' 2.0009 2.0811 . . 148 2714 99.00  . . . . 0.1429 . . . . . . . . . . . 0.1888 
'X-RAY DIFFRACTION' 2.0811 2.1758 . . 156 2706 99.00  . . . . 0.1356 . . . . . . . . . . . 0.1749 
'X-RAY DIFFRACTION' 2.1758 2.2905 . . 149 2767 100.00 . . . . 0.1358 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.2905 2.4340 . . 139 2737 100.00 . . . . 0.1342 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 2.4340 2.6219 . . 121 2789 100.00 . . . . 0.1292 . . . . . . . . . . . 0.1816 
'X-RAY DIFFRACTION' 2.6219 2.8857 . . 161 2732 100.00 . . . . 0.1452 . . . . . . . . . . . 0.1913 
'X-RAY DIFFRACTION' 2.8857 3.3032 . . 130 2770 100.00 . . . . 0.1537 . . . . . . . . . . . 0.1640 
'X-RAY DIFFRACTION' 3.3032 4.1613 . . 166 2727 100.00 . . . . 0.1373 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 4.1613 46.760 . . 132 2767 100.00 . . . . 0.1648 . . . . . . . . . . . 0.1677 
# 
_struct.entry_id                     8VIP 
_struct.title                        
'Crystal structure of the N-terminal domain of fatty acid kinase A (FakA) from Staphylococcus aureus (Mn and AMP-PNP)' 
_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        8VIP 
_struct_keywords.text            'Fatty Acid Kinase A, MRSA, proline isomerization, fatty acid metabolism, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Y1193_STAA8 
_struct_ref.pdbx_db_accession          Q2FZ58 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNLSKNIGELGKTFSKGLLMGAR
GNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAAQAAIEKANNTEDCIELMEYI
IVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_struct_ref.pdbx_align_begin           0 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VIP 
_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                 232 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q2FZ58 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  212 
_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       212 
# 
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 8VIP MET A 1  ? UNP Q2FZ58 ? ? 'expression tag' -19 1  
1 8VIP GLY A 2  ? UNP Q2FZ58 ? ? 'expression tag' -18 2  
1 8VIP SER A 3  ? UNP Q2FZ58 ? ? 'expression tag' -17 3  
1 8VIP SER A 4  ? UNP Q2FZ58 ? ? 'expression tag' -16 4  
1 8VIP HIS A 5  ? UNP Q2FZ58 ? ? 'expression tag' -15 5  
1 8VIP HIS A 6  ? UNP Q2FZ58 ? ? 'expression tag' -14 6  
1 8VIP HIS A 7  ? UNP Q2FZ58 ? ? 'expression tag' -13 7  
1 8VIP HIS A 8  ? UNP Q2FZ58 ? ? 'expression tag' -12 8  
1 8VIP HIS A 9  ? UNP Q2FZ58 ? ? 'expression tag' -11 9  
1 8VIP HIS A 10 ? UNP Q2FZ58 ? ? 'expression tag' -10 10 
1 8VIP SER A 11 ? UNP Q2FZ58 ? ? 'expression tag' -9  11 
1 8VIP SER A 12 ? UNP Q2FZ58 ? ? 'expression tag' -8  12 
1 8VIP GLY A 13 ? UNP Q2FZ58 ? ? 'expression tag' -7  13 
1 8VIP LEU A 14 ? UNP Q2FZ58 ? ? 'expression tag' -6  14 
1 8VIP VAL A 15 ? UNP Q2FZ58 ? ? 'expression tag' -5  15 
1 8VIP PRO A 16 ? UNP Q2FZ58 ? ? 'expression tag' -4  16 
1 8VIP ARG A 17 ? UNP Q2FZ58 ? ? 'expression tag' -3  17 
1 8VIP GLY A 18 ? UNP Q2FZ58 ? ? 'expression tag' -2  18 
1 8VIP SER A 19 ? UNP Q2FZ58 ? ? 'expression tag' -1  19 
1 8VIP HIS A 20 ? UNP Q2FZ58 ? ? 'expression tag' 0   20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 27  ? ASN A 44  ? GLY A 7   ASN A 24  1 ? 18 
HELX_P HELX_P2  AA2 ASN A 44  ? ASN A 52  ? ASN A 24  ASN A 32  1 ? 9  
HELX_P HELX_P3  AA3 ASP A 60  ? ASN A 79  ? ASP A 40  ASN A 59  1 ? 20 
HELX_P HELX_P4  AA4 ASN A 83  ? MET A 97  ? ASN A 63  MET A 77  1 ? 15 
HELX_P HELX_P5  AA5 ARG A 100 ? ASN A 117 ? ARG A 80  ASN A 97  1 ? 18 
HELX_P HELX_P6  AA6 ASN A 125 ? VAL A 144 ? ASN A 105 VAL A 124 1 ? 20 
HELX_P HELX_P7  AA7 THR A 151 ? ASN A 168 ? THR A 131 ASN A 148 1 ? 18 
HELX_P HELX_P8  AA8 ASP A 172 ? THR A 191 ? ASP A 152 THR A 171 1 ? 20 
HELX_P HELX_P9  AA9 PRO A 192 ? LEU A 194 ? PRO A 172 LEU A 174 5 ? 3  
HELX_P HELX_P10 AB1 LEU A 195 ? GLY A 202 ? LEU A 175 GLY A 182 1 ? 8  
HELX_P HELX_P11 AB2 ASP A 205 ? LYS A 223 ? ASP A 185 LYS A 203 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASN 52 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASN 32  A MN  302 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc2  metalc ? ? A ASP 58 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 38  A MN  302 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc3  metalc ? ? A ASP 58 OD2 ? ? ? 1_555 D MN  . MN ? ? A ASP 38  A MN  303 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc4  metalc ? ? A ASP 60 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 40  A MN  302 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc5  metalc ? ? A ASP 60 OD2 ? ? ? 1_555 D MN  . MN ? ? A ASP 40  A MN  303 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc6  metalc ? ? B ANP .  O2B ? ? ? 1_555 C MN  . MN ? ? A ANP 301 A MN  302 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc7  metalc ? ? B ANP .  O1A ? ? ? 1_555 C MN  . MN ? ? A ANP 301 A MN  302 1_555 ? ? ? ? ? ? ? 2.160 ? ? 
metalc8  metalc ? ? B ANP .  O2B ? ? ? 1_555 D MN  . MN ? ? A ANP 301 A MN  303 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc9  metalc ? ? C MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  302 A HOH 406 1_555 ? ? ? ? ? ? ? 2.171 ? ? 
metalc10 metalc ? ? D MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  303 A HOH 407 1_555 ? ? ? ? ? ? ? 1.736 ? ? 
metalc11 metalc ? ? D MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  303 A HOH 441 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc12 metalc ? ? D MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  303 A HOH 507 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 OD1 ? A ASP 58 ? A ASP 38  ? 1_555 82.7  ? 
2  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 86.7  ? 
3  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 90.1  ? 
4  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 176.6 ? 
5  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 100.7 ? 
6  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 93.3  ? 
7  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 91.0  ? 
8  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 173.7 ? 
9  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 90.0  ? 
10 O2B ? B ANP .  ? A ANP 301 ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 85.6  ? 
11 OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .  ? A HOH 406 ? 1_555 94.6  ? 
12 OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .  ? A HOH 406 ? 1_555 88.0  ? 
13 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .  ? A HOH 406 ? 1_555 177.6 ? 
14 O2B ? B ANP .  ? A ANP 301 ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .  ? A HOH 406 ? 1_555 85.5  ? 
15 O1A ? B ANP .  ? A ANP 301 ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .  ? A HOH 406 ? 1_555 92.1  ? 
16 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 90.6  ? 
17 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 89.4  ? 
18 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 99.7  ? 
19 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 407 ? 1_555 96.6  ? 
20 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 407 ? 1_555 172.7 ? 
21 O2B ? B ANP .  ? A ANP 301 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 407 ? 1_555 81.8  ? 
22 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 441 ? 1_555 178.1 ? 
23 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 441 ? 1_555 87.6  ? 
24 O2B ? B ANP .  ? A ANP 301 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 441 ? 1_555 90.8  ? 
25 O   ? E HOH .  ? A HOH 407 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 441 ? 1_555 85.2  ? 
26 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 507 ? 1_555 89.5  ? 
27 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 507 ? 1_555 87.5  ? 
28 O2B ? B ANP .  ? A ANP 301 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 507 ? 1_555 172.7 ? 
29 O   ? E HOH .  ? A HOH 407 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 507 ? 1_555 91.2  ? 
30 O   ? E HOH .  ? A HOH 441 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .  ? A HOH 507 ? 1_555 90.5  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           54 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            34 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    55 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     35 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -4.45 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 ILE A 25  ? ASN A 26  ? ILE A 5   ASN A 6   
AA1 2 GLU A 123 ? ILE A 124 ? GLU A 103 ILE A 104 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    25 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     5 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    124 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     104 
# 
_pdbx_entry_details.entry_id                   8VIP 
_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_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 LYS 210 ? A LYS 230 
22 1 Y 1 A VAL 211 ? A VAL 231 
23 1 Y 1 A ALA 212 ? A ALA 232 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MN  MN     MN N N 298 
PHE N      N  N N 299 
PHE CA     C  N S 300 
PHE C      C  N N 301 
PHE O      O  N N 302 
PHE CB     C  N N 303 
PHE CG     C  Y N 304 
PHE CD1    C  Y N 305 
PHE CD2    C  Y N 306 
PHE CE1    C  Y N 307 
PHE CE2    C  Y N 308 
PHE CZ     C  Y N 309 
PHE OXT    O  N N 310 
PHE H      H  N N 311 
PHE H2     H  N N 312 
PHE HA     H  N N 313 
PHE HB2    H  N N 314 
PHE HB3    H  N N 315 
PHE HD1    H  N N 316 
PHE HD2    H  N N 317 
PHE HE1    H  N N 318 
PHE HE2    H  N N 319 
PHE HZ     H  N N 320 
PHE HXT    H  N N 321 
PRO N      N  N N 322 
PRO CA     C  N S 323 
PRO C      C  N N 324 
PRO O      O  N N 325 
PRO CB     C  N N 326 
PRO CG     C  N N 327 
PRO CD     C  N N 328 
PRO OXT    O  N N 329 
PRO H      H  N N 330 
PRO HA     H  N N 331 
PRO HB2    H  N N 332 
PRO HB3    H  N N 333 
PRO HG2    H  N N 334 
PRO HG3    H  N N 335 
PRO HD2    H  N N 336 
PRO HD3    H  N N 337 
PRO HXT    H  N N 338 
SER N      N  N N 339 
SER CA     C  N S 340 
SER C      C  N N 341 
SER O      O  N N 342 
SER CB     C  N N 343 
SER OG     O  N N 344 
SER OXT    O  N N 345 
SER H      H  N N 346 
SER H2     H  N N 347 
SER HA     H  N N 348 
SER HB2    H  N N 349 
SER HB3    H  N N 350 
SER HG     H  N N 351 
SER HXT    H  N N 352 
THR N      N  N N 353 
THR CA     C  N S 354 
THR C      C  N N 355 
THR O      O  N N 356 
THR CB     C  N R 357 
THR OG1    O  N N 358 
THR CG2    C  N N 359 
THR OXT    O  N N 360 
THR H      H  N N 361 
THR H2     H  N N 362 
THR HA     H  N N 363 
THR HB     H  N N 364 
THR HG1    H  N N 365 
THR HG21   H  N N 366 
THR HG22   H  N N 367 
THR HG23   H  N N 368 
THR HXT    H  N N 369 
TYR N      N  N N 370 
TYR CA     C  N S 371 
TYR C      C  N N 372 
TYR O      O  N N 373 
TYR CB     C  N N 374 
TYR CG     C  Y N 375 
TYR CD1    C  Y N 376 
TYR CD2    C  Y N 377 
TYR CE1    C  Y N 378 
TYR CE2    C  Y N 379 
TYR CZ     C  Y N 380 
TYR OH     O  N N 381 
TYR OXT    O  N N 382 
TYR H      H  N N 383 
TYR H2     H  N N 384 
TYR HA     H  N N 385 
TYR HB2    H  N N 386 
TYR HB3    H  N N 387 
TYR HD1    H  N N 388 
TYR HD2    H  N N 389 
TYR HE1    H  N N 390 
TYR HE2    H  N N 391 
TYR HH     H  N N 392 
TYR HXT    H  N N 393 
VAL N      N  N N 394 
VAL CA     C  N S 395 
VAL C      C  N N 396 
VAL O      O  N N 397 
VAL CB     C  N N 398 
VAL CG1    C  N N 399 
VAL CG2    C  N N 400 
VAL OXT    O  N N 401 
VAL H      H  N N 402 
VAL H2     H  N N 403 
VAL HA     H  N N 404 
VAL HB     H  N N 405 
VAL HG11   H  N N 406 
VAL HG12   H  N N 407 
VAL HG13   H  N N 408 
VAL HG21   H  N N 409 
VAL HG22   H  N N 410 
VAL HG23   H  N N 411 
VAL HXT    H  N N 412 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TYR N     CA     sing N N 356 
TYR N     H      sing N N 357 
TYR N     H2     sing N N 358 
TYR CA    C      sing N N 359 
TYR CA    CB     sing N N 360 
TYR CA    HA     sing N N 361 
TYR C     O      doub N N 362 
TYR C     OXT    sing N N 363 
TYR CB    CG     sing N N 364 
TYR CB    HB2    sing N N 365 
TYR CB    HB3    sing N N 366 
TYR CG    CD1    doub Y N 367 
TYR CG    CD2    sing Y N 368 
TYR CD1   CE1    sing Y N 369 
TYR CD1   HD1    sing N N 370 
TYR CD2   CE2    doub Y N 371 
TYR CD2   HD2    sing N N 372 
TYR CE1   CZ     doub Y N 373 
TYR CE1   HE1    sing N N 374 
TYR CE2   CZ     sing Y N 375 
TYR CE2   HE2    sing N N 376 
TYR CZ    OH     sing N N 377 
TYR OH    HH     sing N N 378 
TYR OXT   HXT    sing N N 379 
VAL N     CA     sing N N 380 
VAL N     H      sing N N 381 
VAL N     H2     sing N N 382 
VAL CA    C      sing N N 383 
VAL CA    CB     sing N N 384 
VAL CA    HA     sing N N 385 
VAL C     O      doub N N 386 
VAL C     OXT    sing N N 387 
VAL CB    CG1    sing N N 388 
VAL CB    CG2    sing N N 389 
VAL CB    HB     sing N N 390 
VAL CG1   HG11   sing N N 391 
VAL CG1   HG12   sing N N 392 
VAL CG1   HG13   sing N N 393 
VAL CG2   HG21   sing N N 394 
VAL CG2   HG22   sing N N 395 
VAL CG2   HG23   sing N N 396 
VAL OXT   HXT    sing N N 397 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'P30 GM110761' 
_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   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VIP 
_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]   0.023358 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017536 
_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]   0.012241 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 21  ? 43.029 -2.849  11.491 1.00 38.13 ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 21  ? 43.107 -1.346  11.528 1.00 33.49 ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 21  ? 41.712 -0.727  11.541 1.00 33.75 ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 21  ? 40.789 -1.211  10.882 1.00 32.87 ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 21  ? 43.885 -0.804  10.333 1.00 37.52 ? 1   MET A CB    1 
ATOM   6    N  N     . ILE A 1 22  ? 41.555 0.339   12.315 1.00 26.88 ? 2   ILE A N     1 
ATOM   7    C  CA    . ILE A 1 22  ? 40.325 1.113   12.376 1.00 20.64 ? 2   ILE A CA    1 
ATOM   8    C  C     . ILE A 1 22  ? 40.735 2.559   12.154 1.00 22.84 ? 2   ILE A C     1 
ATOM   9    O  O     . ILE A 1 22  ? 41.322 3.176   13.047 1.00 25.12 ? 2   ILE A O     1 
ATOM   10   C  CB    . ILE A 1 22  ? 39.604 0.962   13.730 1.00 20.97 ? 2   ILE A CB    1 
ATOM   11   C  CG1   . ILE A 1 22  ? 39.093 -0.463  13.918 1.00 24.13 ? 2   ILE A CG1   1 
ATOM   12   C  CG2   . ILE A 1 22  ? 38.485 1.962   13.851 1.00 19.63 ? 2   ILE A CG2   1 
ATOM   13   C  CD1   . ILE A 1 22  ? 38.022 -0.905  12.875 1.00 27.17 ? 2   ILE A CD1   1 
ATOM   14   N  N     . SER A 1 23  ? 40.441 3.106   10.982 1.00 19.79 ? 3   SER A N     1 
ATOM   15   C  CA    . SER A 1 23  ? 40.805 4.496   10.743 1.00 23.63 ? 3   SER A CA    1 
ATOM   16   C  C     . SER A 1 23  ? 39.731 5.462   11.218 1.00 22.23 ? 3   SER A C     1 
ATOM   17   O  O     . SER A 1 23  ? 40.043 6.597   11.592 1.00 23.72 ? 3   SER A O     1 
ATOM   18   C  CB    . SER A 1 23  ? 41.066 4.750   9.248  1.00 28.69 ? 3   SER A CB    1 
ATOM   19   O  OG    . SER A 1 23  ? 42.050 3.866   8.743  1.00 40.55 ? 3   SER A OG    1 
ATOM   20   N  N     . LYS A 1 24  ? 38.477 5.044   11.175 1.00 21.85 ? 4   LYS A N     1 
ATOM   21   C  CA    . LYS A 1 24  ? 37.345 5.905   11.486 1.00 23.47 ? 4   LYS A CA    1 
ATOM   22   C  C     . LYS A 1 24  ? 36.326 5.113   12.287 1.00 25.73 ? 4   LYS A C     1 
ATOM   23   O  O     . LYS A 1 24  ? 36.116 3.928   12.022 1.00 21.45 ? 4   LYS A O     1 
ATOM   24   C  CB    . LYS A 1 24  ? 36.660 6.436   10.226 1.00 25.37 ? 4   LYS A CB    1 
ATOM   25   C  CG    . LYS A 1 24  ? 37.563 7.124   9.195  1.00 29.91 ? 4   LYS A CG    1 
ATOM   26   C  CD    . LYS A 1 24  ? 38.042 8.462   9.688  1.00 33.08 ? 4   LYS A CD    1 
ATOM   27   N  N     . ILE A 1 25  ? 35.685 5.783   13.251 1.00 19.01 ? 5   ILE A N     1 
ATOM   28   C  CA    . ILE A 1 25  ? 34.651 5.198   14.107 1.00 19.37 ? 5   ILE A CA    1 
ATOM   29   C  C     . ILE A 1 25  ? 33.321 5.847   13.761 1.00 17.15 ? 5   ILE A C     1 
ATOM   30   O  O     . ILE A 1 25  ? 33.114 7.037   14.036 1.00 17.97 ? 5   ILE A O     1 
ATOM   31   C  CB    . ILE A 1 25  ? 34.968 5.397   15.595 1.00 17.99 ? 5   ILE A CB    1 
ATOM   32   C  CG1   . ILE A 1 25  ? 36.358 4.835   15.900 1.00 20.10 ? 5   ILE A CG1   1 
ATOM   33   C  CG2   . ILE A 1 25  ? 33.878 4.765   16.466 1.00 21.12 ? 5   ILE A CG2   1 
ATOM   34   C  CD1   . ILE A 1 25  ? 36.864 5.178   17.287 1.00 20.21 ? 5   ILE A CD1   1 
ATOM   35   N  N     . ASN A 1 26  ? 32.405 5.074   13.179 1.00 18.63 ? 6   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 26  ? 31.076 5.588   12.876 1.00 16.99 ? 6   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 26  ? 30.117 5.270   14.023 1.00 20.36 ? 6   ASN A C     1 
ATOM   38   O  O     . ASN A 1 26  ? 30.510 4.773   15.088 1.00 17.04 ? 6   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 26  ? 30.541 5.057   11.532 1.00 22.14 ? 6   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 26  ? 30.215 3.544   11.526 1.00 18.83 ? 6   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 26  ? 30.014 2.891   12.548 1.00 16.91 ? 6   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 26  ? 30.170 2.986   10.309 1.00 29.22 ? 6   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 27  ? 28.835 5.571   13.811 1.00 17.90 ? 7   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 27  ? 27.872 5.471   14.892 1.00 15.58 ? 7   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 27  ? 27.631 4.053   15.360 1.00 19.54 ? 7   GLY A C     1 
ATOM   46   O  O     . GLY A 1 27  ? 27.407 3.819   16.554 1.00 16.39 ? 7   GLY A O     1 
ATOM   47   N  N     . LYS A 1 28  ? 27.689 3.078   14.449 1.00 17.82 ? 8   LYS A N     1 
ATOM   48   C  CA    . LYS A 1 28  ? 27.508 1.697   14.876 1.00 16.62 ? 8   LYS A CA    1 
ATOM   49   C  C     . LYS A 1 28  ? 28.749 1.160   15.578 1.00 18.27 ? 8   LYS A C     1 
ATOM   50   O  O     . LYS A 1 28  ? 28.625 0.374   16.524 1.00 17.13 ? 8   LYS A O     1 
ATOM   51   C  CB    . LYS A 1 28  ? 27.137 0.788   13.688 1.00 18.58 ? 8   LYS A CB    1 
ATOM   52   C  CG    . LYS A 1 28  ? 26.876 -0.659  14.103 1.00 15.92 ? 8   LYS A CG    1 
ATOM   53   C  CD    . LYS A 1 28  ? 25.836 -0.750  15.256 1.00 18.46 ? 8   LYS A CD    1 
ATOM   54   C  CE    . LYS A 1 28  ? 25.204 -2.140  15.384 1.00 19.36 ? 8   LYS A CE    1 
ATOM   55   N  NZ    . LYS A 1 28  ? 26.183 -3.250  15.588 1.00 20.42 ? 8   LYS A NZ    1 
ATOM   56   N  N     . LEU A 1 29  ? 29.945 1.563   15.157 1.00 16.91 ? 9   LEU A N     1 
ATOM   57   C  CA    . LEU A 1 29  ? 31.119 1.131   15.897 1.00 18.88 ? 9   LEU A CA    1 
ATOM   58   C  C     . LEU A 1 29  ? 31.098 1.714   17.306 1.00 15.78 ? 9   LEU A C     1 
ATOM   59   O  O     . LEU A 1 29  ? 31.373 1.010   18.283 1.00 18.32 ? 9   LEU A O     1 
ATOM   60   C  CB    . LEU A 1 29  ? 32.394 1.520   15.157 1.00 16.38 ? 9   LEU A CB    1 
ATOM   61   C  CG    . LEU A 1 29  ? 33.689 0.954   15.764 1.00 18.37 ? 9   LEU A CG    1 
ATOM   62   C  CD1   . LEU A 1 29  ? 33.552 -0.515  16.137 1.00 18.66 ? 9   LEU A CD1   1 
ATOM   63   C  CD2   . LEU A 1 29  ? 34.872 1.162   14.790 1.00 20.14 ? 9   LEU A CD2   1 
ATOM   64   N  N     . PHE A 1 30  ? 30.741 2.994   17.434 1.00 15.95 ? 10  PHE A N     1 
ATOM   65   C  CA    . PHE A 1 30  ? 30.601 3.576   18.764 1.00 16.14 ? 10  PHE A CA    1 
ATOM   66   C  C     . PHE A 1 30  ? 29.546 2.844   19.592 1.00 20.68 ? 10  PHE A C     1 
ATOM   67   O  O     . PHE A 1 30  ? 29.751 2.577   20.792 1.00 16.03 ? 10  PHE A O     1 
ATOM   68   C  CB    . PHE A 1 30  ? 30.273 5.065   18.642 1.00 18.18 ? 10  PHE A CB    1 
ATOM   69   C  CG    . PHE A 1 30  ? 30.358 5.829   19.972 1.00 16.42 ? 10  PHE A CG    1 
ATOM   70   C  CD1   . PHE A 1 30  ? 31.277 5.471   20.946 1.00 19.36 ? 10  PHE A CD1   1 
ATOM   71   C  CD2   . PHE A 1 30  ? 29.516 6.913   20.223 1.00 18.56 ? 10  PHE A CD2   1 
ATOM   72   C  CE1   . PHE A 1 30  ? 31.362 6.177   22.176 1.00 20.96 ? 10  PHE A CE1   1 
ATOM   73   C  CE2   . PHE A 1 30  ? 29.606 7.632   21.451 1.00 18.90 ? 10  PHE A CE2   1 
ATOM   74   C  CZ    . PHE A 1 30  ? 30.531 7.260   22.413 1.00 18.96 ? 10  PHE A CZ    1 
ATOM   75   N  N     . ALA A 1 31  ? 28.417 2.485   18.974 1.00 16.45 ? 11  ALA A N     1 
ATOM   76   C  CA    . ALA A 1 31  ? 27.395 1.752   19.708 1.00 18.77 ? 11  ALA A CA    1 
ATOM   77   C  C     . ALA A 1 31  ? 27.935 0.414   20.188 1.00 18.56 ? 11  ALA A C     1 
ATOM   78   O  O     . ALA A 1 31  ? 27.658 -0.003  21.318 1.00 16.55 ? 11  ALA A O     1 
ATOM   79   C  CB    . ALA A 1 31  ? 26.149 1.546   18.853 1.00 18.60 ? 11  ALA A CB    1 
ATOM   80   N  N     . ASP A 1 32  ? 28.719 -0.263  19.345 1.00 17.40 ? 12  ASP A N     1 
ATOM   81   C  CA    . ASP A 1 32  ? 29.340 -1.517  19.743 1.00 15.75 ? 12  ASP A CA    1 
ATOM   82   C  C     . ASP A 1 32  ? 30.289 -1.300  20.923 1.00 15.62 ? 12  ASP A C     1 
ATOM   83   O  O     . ASP A 1 32  ? 30.328 -2.117  21.845 1.00 17.32 ? 12  ASP A O     1 
ATOM   84   C  CB    . ASP A 1 32  ? 30.137 -2.132  18.582 1.00 15.19 ? 12  ASP A CB    1 
ATOM   85   C  CG    . ASP A 1 32  ? 29.266 -2.739  17.508 1.00 20.61 ? 12  ASP A CG    1 
ATOM   86   O  OD1   . ASP A 1 32  ? 28.052 -2.849  17.711 1.00 20.68 ? 12  ASP A OD1   1 
ATOM   87   O  OD2   . ASP A 1 32  ? 29.839 -3.137  16.467 1.00 20.92 ? 12  ASP A OD2   1 
ATOM   88   N  N     . MET A 1 33  ? 31.095 -0.231  20.875 1.00 14.72 ? 13  MET A N     1 
ATOM   89   C  CA    . MET A 1 33  ? 31.989 0.087   21.992 1.00 18.28 ? 13  MET A CA    1 
ATOM   90   C  C     . MET A 1 33  ? 31.197 0.274   23.289 1.00 17.95 ? 13  MET A C     1 
ATOM   91   O  O     . MET A 1 33  ? 31.560 -0.277  24.339 1.00 16.98 ? 13  MET A O     1 
ATOM   92   C  CB    . MET A 1 33  ? 32.803 1.331   21.649 1.00 16.25 ? 13  MET A CB    1 
ATOM   93   C  CG    . MET A 1 33  ? 33.803 1.130   20.515 1.00 16.97 ? 13  MET A CG    1 
ATOM   94   S  SD    . MET A 1 33  ? 34.363 2.702   19.814 1.00 18.84 ? 13  MET A SD    1 
ATOM   95   C  CE    . MET A 1 33  ? 35.348 3.332   21.169 1.00 22.07 ? 13  MET A CE    1 
ATOM   96   N  N     . ILE A 1 34  ? 30.080 1.008   23.216 1.00 15.78 ? 14  ILE A N     1 
ATOM   97   C  CA    . ILE A 1 34  ? 29.201 1.196   24.373 1.00 16.18 ? 14  ILE A CA    1 
ATOM   98   C  C     . ILE A 1 34  ? 28.667 -0.141  24.882 1.00 18.73 ? 14  ILE A C     1 
ATOM   99   O  O     . ILE A 1 34  ? 28.695 -0.429  26.088 1.00 17.35 ? 14  ILE A O     1 
ATOM   100  C  CB    . ILE A 1 34  ? 28.054 2.156   23.995 1.00 16.98 ? 14  ILE A CB    1 
ATOM   101  C  CG1   . ILE A 1 34  ? 28.609 3.576   23.882 1.00 17.66 ? 14  ILE A CG1   1 
ATOM   102  C  CG2   . ILE A 1 34  ? 26.914 2.107   25.000 1.00 17.07 ? 14  ILE A CG2   1 
ATOM   103  C  CD1   . ILE A 1 34  ? 27.775 4.480   23.007 1.00 19.43 ? 14  ILE A CD1   1 
ATOM   104  N  N     . ILE A 1 35  ? 28.148 -0.966  23.975 1.00 16.82 ? 15  ILE A N     1 
ATOM   105  C  CA    . ILE A 1 35  ? 27.517 -2.221  24.369 1.00 19.26 ? 15  ILE A CA    1 
ATOM   106  C  C     . ILE A 1 35  ? 28.533 -3.163  25.003 1.00 20.52 ? 15  ILE A C     1 
ATOM   107  O  O     . ILE A 1 35  ? 28.267 -3.763  26.050 1.00 18.81 ? 15  ILE A O     1 
ATOM   108  C  CB    . ILE A 1 35  ? 26.809 -2.864  23.154 1.00 16.97 ? 15  ILE A CB    1 
ATOM   109  C  CG1   . ILE A 1 35  ? 25.622 -1.996  22.754 1.00 19.77 ? 15  ILE A CG1   1 
ATOM   110  C  CG2   . ILE A 1 35  ? 26.327 -4.276  23.493 1.00 20.31 ? 15  ILE A CG2   1 
ATOM   111  C  CD1   . ILE A 1 35  ? 25.080 -2.297  21.354 1.00 25.91 ? 15  ILE A CD1   1 
ATOM   112  N  N     . GLN A 1 36  ? 29.718 -3.304  24.386 1.00 16.47 ? 16  GLN A N     1 
ATOM   113  C  CA    . GLN A 1 36  ? 30.727 -4.215  24.934 1.00 21.60 ? 16  GLN A CA    1 
ATOM   114  C  C     . GLN A 1 36  ? 31.368 -3.651  26.202 1.00 20.70 ? 16  GLN A C     1 
ATOM   115  O  O     . GLN A 1 36  ? 31.685 -4.407  27.130 1.00 18.11 ? 16  GLN A O     1 
ATOM   116  C  CB    . GLN A 1 36  ? 31.813 -4.517  23.886 1.00 17.25 ? 16  GLN A CB    1 
ATOM   117  C  CG    . GLN A 1 36  ? 31.310 -5.188  22.603 1.00 20.22 ? 16  GLN A CG    1 
ATOM   118  C  CD    . GLN A 1 36  ? 30.264 -6.278  22.822 1.00 21.03 ? 16  GLN A CD    1 
ATOM   119  O  OE1   . GLN A 1 36  ? 30.474 -7.198  23.592 1.00 21.95 ? 16  GLN A OE1   1 
ATOM   120  N  NE2   . GLN A 1 36  ? 29.134 -6.170  22.116 1.00 26.47 ? 16  GLN A NE2   1 
ATOM   121  N  N     . GLY A 1 37  ? 31.563 -2.331  26.258 1.00 19.54 ? 17  GLY A N     1 
ATOM   122  C  CA    . GLY A 1 37  ? 31.983 -1.708  27.507 1.00 16.71 ? 17  GLY A CA    1 
ATOM   123  C  C     . GLY A 1 37  ? 30.994 -1.967  28.630 1.00 16.98 ? 17  GLY A C     1 
ATOM   124  O  O     . GLY A 1 37  ? 31.373 -2.320  29.759 1.00 18.21 ? 17  GLY A O     1 
ATOM   125  N  N     . ALA A 1 38  ? 29.712 -1.775  28.347 1.00 18.08 ? 18  ALA A N     1 
ATOM   126  C  CA    . ALA A 1 38  ? 28.698 -2.024  29.373 1.00 19.77 ? 18  ALA A CA    1 
ATOM   127  C  C     . ALA A 1 38  ? 28.696 -3.490  29.802 1.00 18.42 ? 18  ALA A C     1 
ATOM   128  O  O     . ALA A 1 38  ? 28.542 -3.797  30.990 1.00 17.21 ? 18  ALA A O     1 
ATOM   129  C  CB    . ALA A 1 38  ? 27.324 -1.614  28.851 1.00 17.70 ? 18  ALA A CB    1 
ATOM   130  N  N     . GLN A 1 39  ? 28.827 -4.420  28.847 1.00 20.42 ? 19  GLN A N     1 
ATOM   131  C  CA    . GLN A 1 39  ? 28.816 -5.834  29.213 1.00 17.32 ? 19  GLN A CA    1 
ATOM   132  C  C     . GLN A 1 39  ? 30.025 -6.190  30.059 1.00 19.65 ? 19  GLN A C     1 
ATOM   133  O  O     . GLN A 1 39  ? 29.918 -6.976  31.013 1.00 19.70 ? 19  GLN A O     1 
ATOM   134  C  CB    . GLN A 1 39  ? 28.783 -6.718  27.963 1.00 25.48 ? 19  GLN A CB    1 
ATOM   135  C  CG    . GLN A 1 39  ? 28.574 -8.198  28.278 1.00 26.61 ? 19  GLN A CG    1 
ATOM   136  C  CD    . GLN A 1 39  ? 27.241 -8.444  28.967 1.00 26.65 ? 19  GLN A CD    1 
ATOM   137  O  OE1   . GLN A 1 39  ? 26.197 -8.097  28.431 1.00 27.05 ? 19  GLN A OE1   1 
ATOM   138  N  NE2   . GLN A 1 39  ? 27.278 -8.997  30.177 1.00 29.42 ? 19  GLN A NE2   1 
ATOM   139  N  N     . ASN A 1 40  ? 31.190 -5.662  29.702 1.00 16.75 ? 20  ASN A N     1 
ATOM   140  C  CA    . ASN A 1 40  ? 32.375 -5.968  30.490 1.00 19.40 ? 20  ASN A CA    1 
ATOM   141  C  C     . ASN A 1 40  ? 32.278 -5.398  31.902 1.00 20.32 ? 20  ASN A C     1 
ATOM   142  O  O     . ASN A 1 40  ? 32.697 -6.041  32.883 1.00 21.05 ? 20  ASN A O     1 
ATOM   143  C  CB    . ASN A 1 40  ? 33.617 -5.436  29.805 1.00 22.17 ? 20  ASN A CB    1 
ATOM   144  C  CG    . ASN A 1 40  ? 34.856 -6.015  30.412 1.00 29.31 ? 20  ASN A CG    1 
ATOM   145  O  OD1   . ASN A 1 40  ? 34.941 -7.237  30.590 1.00 27.27 ? 20  ASN A OD1   1 
ATOM   146  N  ND2   . ASN A 1 40  ? 35.793 -5.159  30.803 1.00 20.49 ? 20  ASN A ND2   1 
ATOM   147  N  N     . LEU A 1 41  ? 31.739 -4.190  32.029 1.00 19.71 ? 21  LEU A N     1 
ATOM   148  C  CA    . LEU A 1 41  ? 31.518 -3.629  33.354 1.00 18.44 ? 21  LEU A CA    1 
ATOM   149  C  C     . LEU A 1 41  ? 30.499 -4.459  34.136 1.00 20.25 ? 21  LEU A C     1 
ATOM   150  O  O     . LEU A 1 41  ? 30.680 -4.718  35.333 1.00 20.16 ? 21  LEU A O     1 
ATOM   151  C  CB    . LEU A 1 41  ? 31.070 -2.169  33.219 1.00 17.69 ? 21  LEU A CB    1 
ATOM   152  C  CG    . LEU A 1 41  ? 30.606 -1.460  34.492 1.00 17.76 ? 21  LEU A CG    1 
ATOM   153  C  CD1   . LEU A 1 41  ? 31.738 -1.419  35.501 1.00 18.09 ? 21  LEU A CD1   1 
ATOM   154  C  CD2   . LEU A 1 41  ? 30.073 -0.054  34.173 1.00 18.07 ? 21  LEU A CD2   1 
ATOM   155  N  N     . SER A 1 42  ? 29.427 -4.904  33.472 1.00 21.17 ? 22  SER A N     1 
ATOM   156  C  CA    . SER A 1 42  ? 28.448 -5.748  34.151 1.00 20.99 ? 22  SER A CA    1 
ATOM   157  C  C     . SER A 1 42  ? 29.100 -7.029  34.672 1.00 21.43 ? 22  SER A C     1 
ATOM   158  O  O     . SER A 1 42  ? 28.874 -7.441  35.825 1.00 25.00 ? 22  SER A O     1 
ATOM   159  C  CB    . SER A 1 42  ? 27.294 -6.060  33.196 1.00 21.92 ? 22  SER A CB    1 
ATOM   160  O  OG    . SER A 1 42  ? 26.349 -6.887  33.843 1.00 28.89 ? 22  SER A OG    1 
ATOM   161  N  N     . ASN A 1 43  ? 29.930 -7.659  33.841 1.00 19.21 ? 23  ASN A N     1 
ATOM   162  C  CA    . ASN A 1 43  ? 30.627 -8.871  34.253 1.00 26.97 ? 23  ASN A CA    1 
ATOM   163  C  C     . ASN A 1 43  ? 31.474 -8.626  35.499 1.00 27.45 ? 23  ASN A C     1 
ATOM   164  O  O     . ASN A 1 43  ? 31.611 -9.519  36.349 1.00 28.60 ? 23  ASN A O     1 
ATOM   165  C  CB    . ASN A 1 43  ? 31.499 -9.390  33.103 1.00 23.93 ? 23  ASN A CB    1 
ATOM   166  C  CG    . ASN A 1 43  ? 30.685 -9.983  31.960 1.00 23.09 ? 23  ASN A CG    1 
ATOM   167  O  OD1   . ASN A 1 43  ? 29.460 -10.124 32.049 1.00 24.95 ? 23  ASN A OD1   1 
ATOM   168  N  ND2   . ASN A 1 43  ? 31.362 -10.326 30.886 1.00 28.20 ? 23  ASN A ND2   1 
ATOM   169  N  N     . ASN A 1 44  ? 32.019 -7.416  35.643 1.00 22.42 ? 24  ASN A N     1 
ATOM   170  C  CA    . ASN A 1 44  ? 32.953 -7.084  36.717 1.00 23.05 ? 24  ASN A CA    1 
ATOM   171  C  C     . ASN A 1 44  ? 32.330 -6.264  37.845 1.00 24.17 ? 24  ASN A C     1 
ATOM   172  O  O     . ASN A 1 44  ? 33.052 -5.814  38.744 1.00 26.45 ? 24  ASN A O     1 
ATOM   173  C  CB    . ASN A 1 44  ? 34.152 -6.342  36.116 1.00 21.89 ? 24  ASN A CB    1 
ATOM   174  C  CG    . ASN A 1 44  ? 35.109 -7.262  35.422 1.00 30.99 ? 24  ASN A CG    1 
ATOM   175  O  OD1   . ASN A 1 44  ? 35.891 -7.970  36.069 1.00 30.36 ? 24  ASN A OD1   1 
ATOM   176  N  ND2   . ASN A 1 44  ? 35.067 -7.262  34.092 1.00 25.54 ? 24  ASN A ND2   1 
ATOM   177  N  N     . ALA A 1 45  ? 31.004 -6.125  37.865 1.00 19.23 ? 25  ALA A N     1 
ATOM   178  C  CA    . ALA A 1 45  ? 30.365 -5.235  38.829 1.00 21.68 ? 25  ALA A CA    1 
ATOM   179  C  C     . ALA A 1 45  ? 30.575 -5.707  40.269 1.00 23.98 ? 25  ALA A C     1 
ATOM   180  O  O     . ALA A 1 45  ? 30.823 -4.894  41.172 1.00 20.86 ? 25  ALA A O     1 
ATOM   181  C  CB    . ALA A 1 45  ? 28.869 -5.126  38.516 1.00 24.36 ? 25  ALA A CB    1 
ATOM   182  N  N     . ASP A 1 46  ? 30.481 -7.015  40.505 1.00 26.34 ? 26  ASP A N     1 
ATOM   183  C  CA    . ASP A 1 46  ? 30.752 -7.534  41.843 1.00 26.07 ? 26  ASP A CA    1 
ATOM   184  C  C     . ASP A 1 46  ? 32.199 -7.285  42.249 1.00 23.96 ? 26  ASP A C     1 
ATOM   185  O  O     . ASP A 1 46  ? 32.470 -6.900  43.397 1.00 27.00 ? 26  ASP A O     1 
ATOM   186  C  CB    . ASP A 1 46  ? 30.435 -9.023  41.901 1.00 31.63 ? 26  ASP A CB    1 
ATOM   187  C  CG    . ASP A 1 46  ? 28.967 -9.311  41.762 1.00 37.77 ? 26  ASP A CG    1 
ATOM   188  O  OD1   . ASP A 1 46  ? 28.138 -8.441  42.137 1.00 36.35 ? 26  ASP A OD1   1 
ATOM   189  O  OD2   . ASP A 1 46  ? 28.653 -10.432 41.301 1.00 38.98 ? 26  ASP A OD2   1 
ATOM   190  N  N     . LEU A 1 47  ? 33.141 -7.501  41.334 1.00 26.13 ? 27  LEU A N     1 
ATOM   191  C  CA    . LEU A 1 47  ? 34.544 -7.202  41.633 1.00 25.06 ? 27  LEU A CA    1 
ATOM   192  C  C     . LEU A 1 47  ? 34.732 -5.731  42.005 1.00 29.56 ? 27  LEU A C     1 
ATOM   193  O  O     . LEU A 1 47  ? 35.414 -5.405  42.990 1.00 23.93 ? 27  LEU A O     1 
ATOM   194  C  CB    . LEU A 1 47  ? 35.425 -7.590  40.444 1.00 25.97 ? 27  LEU A CB    1 
ATOM   195  C  CG    . LEU A 1 47  ? 36.914 -7.236  40.520 1.00 27.81 ? 27  LEU A CG    1 
ATOM   196  C  CD1   . LEU A 1 47  ? 37.512 -7.718  41.840 1.00 33.28 ? 27  LEU A CD1   1 
ATOM   197  C  CD2   . LEU A 1 47  ? 37.654 -7.838  39.352 1.00 37.91 ? 27  LEU A CD2   1 
ATOM   198  N  N     . VAL A 1 48  ? 34.143 -4.823  41.221 1.00 23.17 ? 28  VAL A N     1 
ATOM   199  C  CA    . VAL A 1 48  ? 34.266 -3.395  41.511 1.00 24.35 ? 28  VAL A CA    1 
ATOM   200  C  C     . VAL A 1 48  ? 33.593 -3.056  42.837 1.00 21.45 ? 28  VAL A C     1 
ATOM   201  O  O     . VAL A 1 48  ? 34.134 -2.281  43.638 1.00 26.43 ? 28  VAL A O     1 
ATOM   202  C  CB    . VAL A 1 48  ? 33.707 -2.568  40.334 1.00 19.38 ? 28  VAL A CB    1 
ATOM   203  C  CG1   . VAL A 1 48  ? 33.701 -1.054  40.643 1.00 18.24 ? 28  VAL A CG1   1 
ATOM   204  C  CG2   . VAL A 1 48  ? 34.514 -2.867  39.075 1.00 21.79 ? 28  VAL A CG2   1 
ATOM   205  N  N     . ASP A 1 49  ? 32.415 -3.637  43.108 1.00 21.45 ? 29  ASP A N     1 
ATOM   206  C  CA    . ASP A 1 49  ? 31.776 -3.432  44.408 1.00 21.78 ? 29  ASP A CA    1 
ATOM   207  C  C     . ASP A 1 49  ? 32.708 -3.825  45.538 1.00 20.14 ? 29  ASP A C     1 
ATOM   208  O  O     . ASP A 1 49  ? 32.724 -3.176  46.593 1.00 23.42 ? 29  ASP A O     1 
ATOM   209  C  CB    . ASP A 1 49  ? 30.499 -4.263  44.549 1.00 24.51 ? 29  ASP A CB    1 
ATOM   210  C  CG    . ASP A 1 49  ? 29.320 -3.671  43.860 1.00 22.36 ? 29  ASP A CG    1 
ATOM   211  O  OD1   . ASP A 1 49  ? 29.382 -2.498  43.428 1.00 23.99 ? 29  ASP A OD1   1 
ATOM   212  O  OD2   . ASP A 1 49  ? 28.306 -4.398  43.735 1.00 24.94 ? 29  ASP A OD2   1 
ATOM   213  N  N     . SER A 1 50  ? 33.449 -4.919  45.350 1.00 24.17 ? 30  SER A N     1 
ATOM   214  C  CA    . SER A 1 50  ? 34.258 -5.494  46.424 1.00 27.47 ? 30  SER A CA    1 
ATOM   215  C  C     . SER A 1 50  ? 35.405 -4.583  46.829 1.00 28.22 ? 30  SER A C     1 
ATOM   216  O  O     . SER A 1 50  ? 35.906 -4.700  47.954 1.00 26.62 ? 30  SER A O     1 
ATOM   217  C  CB    . SER A 1 50  ? 34.793 -6.866  45.998 1.00 24.66 ? 30  SER A CB    1 
ATOM   218  O  OG    . SER A 1 50  ? 35.974 -6.821  45.187 1.00 26.82 ? 30  SER A OG    1 
ATOM   219  N  N     . LEU A 1 51  ? 35.812 -3.670  45.952 1.00 23.21 ? 31  LEU A N     1 
ATOM   220  C  CA    . LEU A 1 51  ? 36.920 -2.762  46.200 1.00 21.24 ? 31  LEU A CA    1 
ATOM   221  C  C     . LEU A 1 51  ? 36.475 -1.448  46.805 1.00 18.02 ? 31  LEU A C     1 
ATOM   222  O  O     . LEU A 1 51  ? 37.320 -0.649  47.209 1.00 21.10 ? 31  LEU A O     1 
ATOM   223  C  CB    . LEU A 1 51  ? 37.663 -2.456  44.881 1.00 19.91 ? 31  LEU A CB    1 
ATOM   224  C  CG    . LEU A 1 51  ? 38.172 -3.673  44.119 1.00 23.87 ? 31  LEU A CG    1 
ATOM   225  C  CD1   . LEU A 1 51  ? 38.807 -3.210  42.836 1.00 28.78 ? 31  LEU A CD1   1 
ATOM   226  C  CD2   . LEU A 1 51  ? 39.158 -4.418  44.966 1.00 26.18 ? 31  LEU A CD2   1 
ATOM   227  N  N     . ASN A 1 52  ? 35.177 -1.197  46.877 1.00 17.72 ? 32  ASN A N     1 
ATOM   228  C  CA    . ASN A 1 52  ? 34.689 0.148   47.163 1.00 15.79 ? 32  ASN A CA    1 
ATOM   229  C  C     . ASN A 1 52  ? 34.890 0.437   48.651 1.00 19.79 ? 32  ASN A C     1 
ATOM   230  O  O     . ASN A 1 52  ? 34.121 -0.023  49.489 1.00 22.69 ? 32  ASN A O     1 
ATOM   231  C  CB    . ASN A 1 52  ? 33.225 0.254   46.738 1.00 17.45 ? 32  ASN A CB    1 
ATOM   232  C  CG    . ASN A 1 52  ? 32.587 1.603   47.059 1.00 17.25 ? 32  ASN A CG    1 
ATOM   233  O  OD1   . ASN A 1 52  ? 31.368 1.684   47.254 1.00 20.18 ? 32  ASN A OD1   1 
ATOM   234  N  ND2   . ASN A 1 52  ? 33.395 2.663   47.116 1.00 18.35 ? 32  ASN A ND2   1 
ATOM   235  N  N     . VAL A 1 53  ? 35.920 1.217   48.970 1.00 21.39 ? 33  VAL A N     1 
ATOM   236  C  CA    . VAL A 1 53  ? 36.185 1.658   50.338 1.00 24.13 ? 33  VAL A CA    1 
ATOM   237  C  C     . VAL A 1 53  ? 36.074 3.165   50.506 1.00 23.07 ? 33  VAL A C     1 
ATOM   238  O  O     . VAL A 1 53  ? 36.071 3.647   51.651 1.00 24.74 ? 33  VAL A O     1 
ATOM   239  C  CB    . VAL A 1 53  ? 37.576 1.195   50.829 1.00 24.58 ? 33  VAL A CB    1 
ATOM   240  C  CG1   . VAL A 1 53  ? 37.656 -0.298  50.855 1.00 24.27 ? 33  VAL A CG1   1 
ATOM   241  C  CG2   . VAL A 1 53  ? 38.691 1.818   49.987 1.00 22.76 ? 33  VAL A CG2   1 
ATOM   242  N  N     . TYR A 1 54  ? 36.006 3.931   49.425 1.00 23.88 ? 34  TYR A N     1 
ATOM   243  C  CA    . TYR A 1 54  ? 36.092 5.376   49.501 1.00 21.53 ? 34  TYR A CA    1 
ATOM   244  C  C     . TYR A 1 54  ? 34.997 6.019   48.663 1.00 23.54 ? 34  TYR A C     1 
ATOM   245  O  O     . TYR A 1 54  ? 34.730 5.569   47.536 1.00 22.71 ? 34  TYR A O     1 
ATOM   246  C  CB    . TYR A 1 54  ? 37.476 5.863   49.003 1.00 24.24 ? 34  TYR A CB    1 
ATOM   247  C  CG    . TYR A 1 54  ? 37.495 7.346   48.782 1.00 21.77 ? 34  TYR A CG    1 
ATOM   248  C  CD1   . TYR A 1 54  ? 37.746 8.205   49.826 1.00 29.16 ? 34  TYR A CD1   1 
ATOM   249  C  CD2   . TYR A 1 54  ? 37.221 7.890   47.540 1.00 30.44 ? 34  TYR A CD2   1 
ATOM   250  C  CE1   . TYR A 1 54  ? 37.716 9.566   49.659 1.00 31.17 ? 34  TYR A CE1   1 
ATOM   251  C  CE2   . TYR A 1 54  ? 37.200 9.267   47.361 1.00 31.60 ? 34  TYR A CE2   1 
ATOM   252  C  CZ    . TYR A 1 54  ? 37.445 10.088  48.437 1.00 33.33 ? 34  TYR A CZ    1 
ATOM   253  O  OH    . TYR A 1 54  ? 37.438 11.450  48.301 1.00 45.66 ? 34  TYR A OH    1 
ATOM   254  N  N     . PRO A 1 55  ? 34.365 7.101   49.147 1.00 23.16 ? 35  PRO A N     1 
ATOM   255  C  CA    . PRO A 1 55  ? 34.442 7.815   50.432 1.00 23.29 ? 35  PRO A CA    1 
ATOM   256  C  C     . PRO A 1 55  ? 33.954 6.983   51.615 1.00 23.55 ? 35  PRO A C     1 
ATOM   257  O  O     . PRO A 1 55  ? 34.503 7.086   52.710 1.00 24.67 ? 35  PRO A O     1 
ATOM   258  C  CB    . PRO A 1 55  ? 33.517 9.024   50.229 1.00 25.97 ? 35  PRO A CB    1 
ATOM   259  C  CG    . PRO A 1 55  ? 33.371 9.177   48.757 1.00 33.40 ? 35  PRO A CG    1 
ATOM   260  C  CD    . PRO A 1 55  ? 33.554 7.827   48.155 1.00 23.09 ? 35  PRO A CD    1 
ATOM   261  N  N     . VAL A 1 56  ? 32.907 6.201   51.392 1.00 19.36 ? 36  VAL A N     1 
ATOM   262  C  CA    . VAL A 1 56  ? 32.346 5.301   52.406 1.00 21.64 ? 36  VAL A CA    1 
ATOM   263  C  C     . VAL A 1 56  ? 32.501 3.884   51.869 1.00 19.17 ? 36  VAL A C     1 
ATOM   264  O  O     . VAL A 1 56  ? 32.298 3.666   50.666 1.00 18.90 ? 36  VAL A O     1 
ATOM   265  C  CB    . VAL A 1 56  ? 30.878 5.636   52.694 1.00 25.84 ? 36  VAL A CB    1 
ATOM   266  C  CG1   . VAL A 1 56  ? 30.250 4.606   53.636 1.00 30.31 ? 36  VAL A CG1   1 
ATOM   267  C  CG2   . VAL A 1 56  ? 30.778 7.024   53.305 1.00 28.09 ? 36  VAL A CG2   1 
ATOM   268  N  N     . PRO A 1 57  ? 32.832 2.898   52.705 1.00 16.35 ? 37  PRO A N     1 
ATOM   269  C  CA    . PRO A 1 57  ? 32.989 1.500   52.243 1.00 19.13 ? 37  PRO A CA    1 
ATOM   270  C  C     . PRO A 1 57  ? 31.653 0.755   52.158 1.00 22.33 ? 37  PRO A C     1 
ATOM   271  O  O     . PRO A 1 57  ? 31.418 -0.262  52.814 1.00 18.76 ? 37  PRO A O     1 
ATOM   272  C  CB    . PRO A 1 57  ? 33.937 0.915   53.308 1.00 17.88 ? 37  PRO A CB    1 
ATOM   273  C  CG    . PRO A 1 57  ? 33.530 1.652   54.590 1.00 18.44 ? 37  PRO A CG    1 
ATOM   274  C  CD    . PRO A 1 57  ? 33.240 3.075   54.117 1.00 18.48 ? 37  PRO A CD    1 
ATOM   275  N  N     . ASP A 1 58  ? 30.745 1.254   51.319 1.00 17.42 ? 38  ASP A N     1 
ATOM   276  C  CA    . ASP A 1 58  ? 29.410 0.685   51.237 1.00 17.50 ? 38  ASP A CA    1 
ATOM   277  C  C     . ASP A 1 58  ? 29.238 -0.300  50.081 1.00 19.00 ? 38  ASP A C     1 
ATOM   278  O  O     . ASP A 1 58  ? 28.126 -0.788  49.870 1.00 26.07 ? 38  ASP A O     1 
ATOM   279  C  CB    . ASP A 1 58  ? 28.363 1.796   51.183 1.00 20.67 ? 38  ASP A CB    1 
ATOM   280  C  CG    . ASP A 1 58  ? 28.508 2.715   49.997 1.00 20.72 ? 38  ASP A CG    1 
ATOM   281  O  OD1   . ASP A 1 58  ? 29.464 2.565   49.240 1.00 15.09 ? 38  ASP A OD1   1 
ATOM   282  O  OD2   . ASP A 1 58  ? 27.630 3.591   49.874 1.00 22.48 ? 38  ASP A OD2   1 
ATOM   283  N  N     . GLY A 1 59  ? 30.315 -0.648  49.385 1.00 20.44 ? 39  GLY A N     1 
ATOM   284  C  CA    . GLY A 1 59  ? 30.343 -1.817  48.515 1.00 22.13 ? 39  GLY A CA    1 
ATOM   285  C  C     . GLY A 1 59  ? 29.442 -1.746  47.296 1.00 22.20 ? 39  GLY A C     1 
ATOM   286  O  O     . GLY A 1 59  ? 28.868 -2.773  46.897 1.00 23.98 ? 39  GLY A O     1 
ATOM   287  N  N     . ASP A 1 60  ? 29.307 -0.565  46.673 1.00 21.23 ? 40  ASP A N     1 
ATOM   288  C  CA    . ASP A 1 60  ? 28.291 -0.397  45.633 1.00 22.25 ? 40  ASP A CA    1 
ATOM   289  C  C     . ASP A 1 60  ? 28.771 0.304   44.367 1.00 20.95 ? 40  ASP A C     1 
ATOM   290  O  O     . ASP A 1 60  ? 27.942 0.595   43.492 1.00 17.18 ? 40  ASP A O     1 
ATOM   291  C  CB    . ASP A 1 60  ? 27.090 0.373   46.172 1.00 21.01 ? 40  ASP A CB    1 
ATOM   292  C  CG    . ASP A 1 60  ? 27.434 1.774   46.586 1.00 21.41 ? 40  ASP A CG    1 
ATOM   293  O  OD1   . ASP A 1 60  ? 28.586 2.191   46.376 1.00 20.22 ? 40  ASP A OD1   1 
ATOM   294  O  OD2   . ASP A 1 60  ? 26.567 2.457   47.161 1.00 21.00 ? 40  ASP A OD2   1 
ATOM   295  N  N     . THR A 1 61  ? 30.066 0.587   44.237 1.00 17.93 ? 41  THR A N     1 
ATOM   296  C  CA    . THR A 1 61  ? 30.543 1.301   43.050 1.00 16.98 ? 41  THR A CA    1 
ATOM   297  C  C     . THR A 1 61  ? 30.207 0.548   41.775 1.00 16.22 ? 41  THR A C     1 
ATOM   298  O  O     . THR A 1 61  ? 29.810 1.156   40.772 1.00 17.44 ? 41  THR A O     1 
ATOM   299  C  CB    . THR A 1 61  ? 32.051 1.507   43.116 1.00 16.42 ? 41  THR A CB    1 
ATOM   300  O  OG1   . THR A 1 61  ? 32.405 2.122   44.354 1.00 16.17 ? 41  THR A OG1   1 
ATOM   301  C  CG2   . THR A 1 61  ? 32.530 2.391   41.942 1.00 16.49 ? 41  THR A CG2   1 
ATOM   302  N  N     . GLY A 1 62  ? 30.435 -0.767  41.773 1.00 16.61 ? 42  GLY A N     1 
ATOM   303  C  CA    . GLY A 1 62  ? 30.186 -1.554  40.582 1.00 19.58 ? 42  GLY A CA    1 
ATOM   304  C  C     . GLY A 1 62  ? 28.726 -1.537  40.197 1.00 22.02 ? 42  GLY A C     1 
ATOM   305  O  O     . GLY A 1 62  ? 28.378 -1.332  39.030 1.00 21.92 ? 42  GLY A O     1 
ATOM   306  N  N     . THR A 1 63  ? 27.854 -1.698  41.185 1.00 20.10 ? 43  THR A N     1 
ATOM   307  C  CA    . THR A 1 63  ? 26.420 -1.656  40.936 1.00 22.45 ? 43  THR A CA    1 
ATOM   308  C  C     . THR A 1 63  ? 25.995 -0.291  40.430 1.00 20.67 ? 43  THR A C     1 
ATOM   309  O  O     . THR A 1 63  ? 25.257 -0.193  39.439 1.00 19.71 ? 43  THR A O     1 
ATOM   310  C  CB    . THR A 1 63  ? 25.670 -2.021  42.215 1.00 22.82 ? 43  THR A CB    1 
ATOM   311  O  OG1   . THR A 1 63  ? 25.962 -3.384  42.533 1.00 25.55 ? 43  THR A OG1   1 
ATOM   312  C  CG2   . THR A 1 63  ? 24.172 -1.859  42.023 1.00 26.89 ? 43  THR A CG2   1 
ATOM   313  N  N     . ASN A 1 64  ? 26.501 0.774   41.058 1.00 17.76 ? 44  ASN A N     1 
ATOM   314  C  CA    . ASN A 1 64  ? 26.155 2.121   40.619 1.00 19.21 ? 44  ASN A CA    1 
ATOM   315  C  C     . ASN A 1 64  ? 26.595 2.368   39.182 1.00 21.30 ? 44  ASN A C     1 
ATOM   316  O  O     . ASN A 1 64  ? 25.817 2.869   38.353 1.00 19.31 ? 44  ASN A O     1 
ATOM   317  C  CB    . ASN A 1 64  ? 26.797 3.144   41.543 1.00 17.04 ? 44  ASN A CB    1 
ATOM   318  C  CG    . ASN A 1 64  ? 26.119 3.207   42.883 1.00 20.86 ? 44  ASN A CG    1 
ATOM   319  O  OD1   . ASN A 1 64  ? 24.987 2.742   43.032 1.00 20.84 ? 44  ASN A OD1   1 
ATOM   320  N  ND2   . ASN A 1 64  ? 26.802 3.780   43.870 1.00 17.84 ? 44  ASN A ND2   1 
ATOM   321  N  N     . MET A 1 65  ? 27.849 2.034   38.869 1.00 17.48 ? 45  MET A N     1 
ATOM   322  C  CA    . MET A 1 65  ? 28.339 2.273   37.513 1.00 18.81 ? 45  MET A CA    1 
ATOM   323  C  C     . MET A 1 65  ? 27.628 1.376   36.508 1.00 16.59 ? 45  MET A C     1 
ATOM   324  O  O     . MET A 1 65  ? 27.289 1.822   35.400 1.00 18.06 ? 45  MET A O     1 
ATOM   325  C  CB    . MET A 1 65  ? 29.860 2.082   37.467 1.00 16.39 ? 45  MET A CB    1 
ATOM   326  C  CG    . MET A 1 65  ? 30.627 3.132   38.302 1.00 18.50 ? 45  MET A CG    1 
ATOM   327  S  SD    . MET A 1 65  ? 32.431 2.943   38.153 1.00 16.97 ? 45  MET A SD    1 
ATOM   328  C  CE    . MET A 1 65  ? 32.730 3.471   36.461 1.00 18.82 ? 45  MET A CE    1 
ATOM   329  N  N     . ASN A 1 66  ? 27.384 0.117   36.874 1.00 17.05 ? 46  ASN A N     1 
ATOM   330  C  CA    . ASN A 1 66  ? 26.662 -0.808  35.995 1.00 19.61 ? 46  ASN A CA    1 
ATOM   331  C  C     . ASN A 1 66  ? 25.270 -0.289  35.657 1.00 18.29 ? 46  ASN A C     1 
ATOM   332  O  O     . ASN A 1 66  ? 24.848 -0.333  34.497 1.00 19.13 ? 46  ASN A O     1 
ATOM   333  C  CB    . ASN A 1 66  ? 26.576 -2.180  36.662 1.00 19.20 ? 46  ASN A CB    1 
ATOM   334  C  CG    . ASN A 1 66  ? 26.040 -3.270  35.734 1.00 23.32 ? 46  ASN A CG    1 
ATOM   335  O  OD1   . ASN A 1 66  ? 26.118 -3.178  34.506 1.00 22.79 ? 46  ASN A OD1   1 
ATOM   336  N  ND2   . ASN A 1 66  ? 25.496 -4.318  36.335 1.00 25.68 ? 46  ASN A ND2   1 
ATOM   337  N  N     . LEU A 1 67  ? 24.543 0.212   36.654 1.00 18.43 ? 47  LEU A N     1 
ATOM   338  C  CA    . LEU A 1 67  ? 23.187 0.712   36.424 1.00 19.85 ? 47  LEU A CA    1 
ATOM   339  C  C     . LEU A 1 67  ? 23.202 1.948   35.545 1.00 21.17 ? 47  LEU A C     1 
ATOM   340  O  O     . LEU A 1 67  ? 22.317 2.130   34.695 1.00 20.09 ? 47  LEU A O     1 
ATOM   341  C  CB    . LEU A 1 67  ? 22.509 1.025   37.760 1.00 21.29 ? 47  LEU A CB    1 
ATOM   342  C  CG    . LEU A 1 67  ? 22.102 -0.213  38.564 1.00 22.84 ? 47  LEU A CG    1 
ATOM   343  C  CD1   . LEU A 1 67  ? 21.644 0.202   39.960 1.00 29.25 ? 47  LEU A CD1   1 
ATOM   344  C  CD2   . LEU A 1 67  ? 21.022 -0.997  37.844 1.00 29.38 ? 47  LEU A CD2   1 
ATOM   345  N  N     . THR A 1 68  ? 24.214 2.798   35.727 1.00 17.16 ? 48  THR A N     1 
ATOM   346  C  CA    . THR A 1 68  ? 24.348 3.998   34.913 1.00 17.62 ? 48  THR A CA    1 
ATOM   347  C  C     . THR A 1 68  ? 24.643 3.640   33.461 1.00 18.39 ? 48  THR A C     1 
ATOM   348  O  O     . THR A 1 68  ? 23.962 4.107   32.535 1.00 18.68 ? 48  THR A O     1 
ATOM   349  C  CB    . THR A 1 68  ? 25.463 4.872   35.490 1.00 16.83 ? 48  THR A CB    1 
ATOM   350  O  OG1   . THR A 1 68  ? 25.129 5.221   36.835 1.00 19.87 ? 48  THR A OG1   1 
ATOM   351  C  CG2   . THR A 1 68  ? 25.647 6.135   34.701 1.00 18.07 ? 48  THR A CG2   1 
ATOM   352  N  N     . MET A 1 69  ? 25.676 2.823   33.255 1.00 16.29 ? 49  MET A N     1 
ATOM   353  C  CA    . MET A 1 69  ? 26.075 2.407   31.923 1.00 19.31 ? 49  MET A CA    1 
ATOM   354  C  C     . MET A 1 69  ? 24.956 1.631   31.229 1.00 18.15 ? 49  MET A C     1 
ATOM   355  O  O     . MET A 1 69  ? 24.740 1.781   30.015 1.00 18.50 ? 49  MET A O     1 
ATOM   356  C  CB    . MET A 1 69  ? 27.359 1.587   32.059 1.00 20.34 ? 49  MET A CB    1 
ATOM   357  C  CG    . MET A 1 69  ? 28.092 1.365   30.784 1.00 24.90 ? 49  MET A CG    1 
ATOM   358  S  SD    . MET A 1 69  ? 28.809 2.878   30.134 1.00 20.23 ? 49  MET A SD    1 
ATOM   359  C  CE    . MET A 1 69  ? 29.626 2.085   28.742 1.00 25.00 ? 49  MET A CE    1 
ATOM   360  N  N     . THR A 1 70  ? 24.211 0.817   31.988 1.00 21.08 ? 50  THR A N     1 
ATOM   361  C  CA    . THR A 1 70  ? 23.079 0.081   31.420 1.00 24.08 ? 50  THR A CA    1 
ATOM   362  C  C     . THR A 1 70  ? 22.003 1.022   30.874 1.00 23.61 ? 50  THR A C     1 
ATOM   363  O  O     . THR A 1 70  ? 21.383 0.745   29.833 1.00 19.03 ? 50  THR A O     1 
ATOM   364  C  CB    . THR A 1 70  ? 22.487 -0.848  32.488 1.00 25.78 ? 50  THR A CB    1 
ATOM   365  O  OG1   . THR A 1 70  ? 23.400 -1.919  32.737 1.00 22.89 ? 50  THR A OG1   1 
ATOM   366  C  CG2   . THR A 1 70  ? 21.164 -1.425  32.027 1.00 25.95 ? 50  THR A CG2   1 
ATOM   367  N  N     . SER A 1 71  ? 21.753 2.131   31.572 1.00 19.19 ? 51  SER A N     1 
ATOM   368  C  CA    . SER A 1 71  ? 20.770 3.102   31.097 1.00 21.37 ? 51  SER A CA    1 
ATOM   369  C  C     . SER A 1 71  ? 21.201 3.719   29.774 1.00 23.62 ? 51  SER A C     1 
ATOM   370  O  O     . SER A 1 71  ? 20.382 3.903   28.860 1.00 21.68 ? 51  SER A O     1 
ATOM   371  C  CB    . SER A 1 71  ? 20.575 4.172   32.168 1.00 24.19 ? 51  SER A CB    1 
ATOM   372  O  OG    . SER A 1 71  ? 19.601 5.131   31.786 1.00 30.46 ? 51  SER A OG    1 
ATOM   373  N  N     . GLY A 1 72  ? 22.496 4.020   29.635 1.00 19.48 ? 52  GLY A N     1 
ATOM   374  C  CA    . GLY A 1 72  ? 22.988 4.493   28.360 1.00 18.47 ? 52  GLY A CA    1 
ATOM   375  C  C     . GLY A 1 72  ? 22.929 3.419   27.296 1.00 19.48 ? 52  GLY A C     1 
ATOM   376  O  O     . GLY A 1 72  ? 22.541 3.685   26.159 1.00 18.30 ? 52  GLY A O     1 
ATOM   377  N  N     . ARG A 1 73  ? 23.276 2.186   27.662 1.00 17.36 ? 53  ARG A N     1 
ATOM   378  C  CA    . ARG A 1 73  ? 23.301 1.091   26.696 1.00 19.37 ? 53  ARG A CA    1 
ATOM   379  C  C     . ARG A 1 73  ? 21.909 0.795   26.150 1.00 19.40 ? 53  ARG A C     1 
ATOM   380  O  O     . ARG A 1 73  ? 21.740 0.509   24.955 1.00 18.68 ? 53  ARG A O     1 
ATOM   381  C  CB    . ARG A 1 73  ? 23.897 -0.157  27.353 1.00 21.52 ? 53  ARG A CB    1 
ATOM   382  C  CG    . ARG A 1 73  ? 23.684 -1.447  26.558 1.00 25.28 ? 53  ARG A CG    1 
ATOM   383  C  CD    . ARG A 1 73  ? 23.978 -2.712  27.368 1.00 28.79 ? 53  ARG A CD    1 
ATOM   384  N  NE    . ARG A 1 73  ? 23.734 -3.906  26.555 1.00 38.70 ? 53  ARG A NE    1 
ATOM   385  C  CZ    . ARG A 1 73  ? 24.397 -5.059  26.650 1.00 39.41 ? 53  ARG A CZ    1 
ATOM   386  N  NH1   . ARG A 1 73  ? 25.381 -5.209  27.527 1.00 34.57 ? 53  ARG A NH1   1 
ATOM   387  N  NH2   . ARG A 1 73  ? 24.078 -6.068  25.843 1.00 36.34 ? 53  ARG A NH2   1 
ATOM   388  N  N     . GLU A 1 74  ? 20.908 0.804   27.018 1.00 22.12 ? 54  GLU A N     1 
ATOM   389  C  CA    . GLU A 1 74  ? 19.547 0.538   26.570 1.00 22.76 ? 54  GLU A CA    1 
ATOM   390  C  C     . GLU A 1 74  ? 19.032 1.627   25.629 1.00 20.74 ? 54  GLU A C     1 
ATOM   391  O  O     . GLU A 1 74  ? 18.351 1.327   24.645 1.00 22.84 ? 54  GLU A O     1 
ATOM   392  C  CB    . GLU A 1 74  ? 18.653 0.374   27.792 1.00 23.31 ? 54  GLU A CB    1 
ATOM   393  C  CG    . GLU A 1 74  ? 18.959 -0.944  28.499 1.00 28.43 ? 54  GLU A CG    1 
ATOM   394  C  CD    . GLU A 1 74  ? 18.208 -1.139  29.793 1.00 34.57 ? 54  GLU A CD    1 
ATOM   395  O  OE1   . GLU A 1 74  ? 17.614 -0.158  30.297 1.00 40.63 ? 54  GLU A OE1   1 
ATOM   396  O  OE2   . GLU A 1 74  ? 18.222 -2.284  30.301 1.00 40.60 ? 54  GLU A OE2   1 
ATOM   397  N  N     . GLU A 1 75  ? 19.340 2.895   25.892 1.00 20.45 ? 55  GLU A N     1 
ATOM   398  C  CA    . GLU A 1 75  ? 18.914 3.934   24.953 1.00 21.10 ? 55  GLU A CA    1 
ATOM   399  C  C     . GLU A 1 75  ? 19.553 3.729   23.589 1.00 24.16 ? 55  GLU A C     1 
ATOM   400  O  O     . GLU A 1 75  ? 18.894 3.881   22.552 1.00 21.40 ? 55  GLU A O     1 
ATOM   401  C  CB    . GLU A 1 75  ? 19.269 5.321   25.474 1.00 24.92 ? 55  GLU A CB    1 
ATOM   402  C  CG    . GLU A 1 75  ? 18.475 5.749   26.668 1.00 34.08 ? 55  GLU A CG    1 
ATOM   403  C  CD    . GLU A 1 75  ? 17.005 5.893   26.351 1.00 32.95 ? 55  GLU A CD    1 
ATOM   404  O  OE1   . GLU A 1 75  ? 16.671 6.470   25.288 1.00 37.90 ? 55  GLU A OE1   1 
ATOM   405  O  OE2   . GLU A 1 75  ? 16.198 5.403   27.143 1.00 39.17 ? 55  GLU A OE2   1 
ATOM   406  N  N     . VAL A 1 76  ? 20.844 3.412   23.583 1.00 21.32 ? 56  VAL A N     1 
ATOM   407  C  CA    . VAL A 1 76  ? 21.586 3.180   22.345 1.00 20.02 ? 56  VAL A CA    1 
ATOM   408  C  C     . VAL A 1 76  ? 21.013 1.986   21.586 1.00 18.87 ? 56  VAL A C     1 
ATOM   409  O  O     . VAL A 1 76  ? 20.768 2.049   20.368 1.00 21.44 ? 56  VAL A O     1 
ATOM   410  C  CB    . VAL A 1 76  ? 23.070 2.984   22.697 1.00 20.25 ? 56  VAL A CB    1 
ATOM   411  C  CG1   . VAL A 1 76  ? 23.828 2.302   21.569 1.00 20.57 ? 56  VAL A CG1   1 
ATOM   412  C  CG2   . VAL A 1 76  ? 23.670 4.330   23.081 1.00 17.81 ? 56  VAL A CG2   1 
ATOM   413  N  N     . GLU A 1 77  ? 20.784 0.883   22.292 1.00 16.47 ? 57  GLU A N     1 
ATOM   414  C  CA    . GLU A 1 77  ? 20.291 -0.322  21.633 1.00 25.57 ? 57  GLU A CA    1 
ATOM   415  C  C     . GLU A 1 77  ? 18.926 -0.096  21.003 1.00 28.44 ? 57  GLU A C     1 
ATOM   416  O  O     . GLU A 1 77  ? 18.596 -0.738  19.998 1.00 27.81 ? 57  GLU A O     1 
ATOM   417  C  CB    . GLU A 1 77  ? 20.228 -1.484  22.628 1.00 25.58 ? 57  GLU A CB    1 
ATOM   418  C  CG    . GLU A 1 77  ? 21.580 -2.127  22.864 1.00 27.79 ? 57  GLU A CG    1 
ATOM   419  C  CD    . GLU A 1 77  ? 21.554 -3.205  23.921 1.00 31.21 ? 57  GLU A CD    1 
ATOM   420  O  OE1   . GLU A 1 77  ? 20.616 -3.212  24.752 1.00 38.88 ? 57  GLU A OE1   1 
ATOM   421  O  OE2   . GLU A 1 77  ? 22.479 -4.037  23.913 1.00 34.46 ? 57  GLU A OE2   1 
ATOM   422  N  N     . ASN A 1 78  ? 18.134 0.812   21.552 1.00 23.06 ? 58  ASN A N     1 
ATOM   423  C  CA    . ASN A 1 78  ? 16.825 1.102   20.984 1.00 28.95 ? 58  ASN A CA    1 
ATOM   424  C  C     . ASN A 1 78  ? 16.815 2.250   19.977 1.00 28.29 ? 58  ASN A C     1 
ATOM   425  O  O     . ASN A 1 78  ? 15.772 2.499   19.360 1.00 26.72 ? 58  ASN A O     1 
ATOM   426  C  CB    . ASN A 1 78  ? 15.849 1.380   22.111 1.00 29.97 ? 58  ASN A CB    1 
ATOM   427  C  CG    . ASN A 1 78  ? 15.396 0.109   22.772 1.00 35.73 ? 58  ASN A CG    1 
ATOM   428  O  OD1   . ASN A 1 78  ? 14.766 -0.733  22.135 1.00 41.97 ? 58  ASN A OD1   1 
ATOM   429  N  ND2   . ASN A 1 78  ? 15.735 -0.060  24.037 1.00 38.98 ? 58  ASN A ND2   1 
ATOM   430  N  N     . ASN A 1 79  ? 17.935 2.935   19.769 1.00 21.25 ? 59  ASN A N     1 
ATOM   431  C  CA    . ASN A 1 79  ? 18.003 4.068   18.840 1.00 25.01 ? 59  ASN A CA    1 
ATOM   432  C  C     . ASN A 1 79  ? 19.383 4.102   18.170 1.00 27.38 ? 59  ASN A C     1 
ATOM   433  O  O     . ASN A 1 79  ? 20.180 5.020   18.355 1.00 25.52 ? 59  ASN A O     1 
ATOM   434  C  CB    . ASN A 1 79  ? 17.742 5.391   19.567 1.00 30.70 ? 59  ASN A CB    1 
ATOM   435  C  CG    . ASN A 1 79  ? 16.449 5.402   20.312 1.00 33.77 ? 59  ASN A CG    1 
ATOM   436  O  OD1   . ASN A 1 79  ? 15.403 5.628   19.717 1.00 37.62 ? 59  ASN A OD1   1 
ATOM   437  N  ND2   . ASN A 1 79  ? 16.500 5.172   21.634 1.00 38.24 ? 59  ASN A ND2   1 
ATOM   438  N  N     . LEU A 1 80  ? 19.688 3.087   17.366 1.00 21.11 ? 60  LEU A N     1 
ATOM   439  C  CA    . LEU A 1 80  ? 20.972 3.061   16.684 1.00 24.43 ? 60  LEU A CA    1 
ATOM   440  C  C     . LEU A 1 80  ? 21.005 4.077   15.541 1.00 27.23 ? 60  LEU A C     1 
ATOM   441  O  O     . LEU A 1 80  ? 19.967 4.512   15.023 1.00 20.66 ? 60  LEU A O     1 
ATOM   442  C  CB    . LEU A 1 80  ? 21.259 1.662   16.151 1.00 19.89 ? 60  LEU A CB    1 
ATOM   443  C  CG    . LEU A 1 80  ? 21.388 0.522   17.162 1.00 22.45 ? 60  LEU A CG    1 
ATOM   444  C  CD1   . LEU A 1 80  ? 21.537 -0.815  16.461 1.00 24.63 ? 60  LEU A CD1   1 
ATOM   445  C  CD2   . LEU A 1 80  ? 22.595 0.751   18.034 1.00 24.65 ? 60  LEU A CD2   1 
ATOM   446  N  N     . SER A 1 81  ? 22.224 4.453   15.148 1.00 21.97 ? 61  SER A N     1 
ATOM   447  C  CA    . SER A 1 81  ? 22.441 5.407   14.062 1.00 24.96 ? 61  SER A CA    1 
ATOM   448  C  C     . SER A 1 81  ? 23.816 5.194   13.433 1.00 21.62 ? 61  SER A C     1 
ATOM   449  O  O     . SER A 1 81  ? 24.767 4.793   14.102 1.00 19.39 ? 61  SER A O     1 
ATOM   450  C  CB    . SER A 1 81  ? 22.317 6.853   14.566 1.00 24.05 ? 61  SER A CB    1 
ATOM   451  O  OG    . SER A 1 81  ? 22.546 7.770   13.498 1.00 27.32 ? 61  SER A OG    1 
ATOM   452  N  N     . LYS A 1 82  ? 23.922 5.482   12.129 1.00 21.93 ? 62  LYS A N     1 
ATOM   453  C  CA    . LYS A 1 82  ? 25.235 5.473   11.488 1.00 20.59 ? 62  LYS A CA    1 
ATOM   454  C  C     . LYS A 1 82  ? 26.067 6.699   11.851 1.00 18.92 ? 62  LYS A C     1 
ATOM   455  O  O     . LYS A 1 82  ? 27.283 6.728   11.581 1.00 21.95 ? 62  LYS A O     1 
ATOM   456  C  CB    . LYS A 1 82  ? 25.102 5.427   9.960  1.00 19.77 ? 62  LYS A CB    1 
ATOM   457  C  CG    . LYS A 1 82  ? 24.509 6.703   9.369  1.00 24.84 ? 62  LYS A CG    1 
ATOM   458  C  CD    . LYS A 1 82  ? 24.350 6.622   7.836  1.00 30.14 ? 62  LYS A CD    1 
ATOM   459  C  CE    . LYS A 1 82  ? 23.436 7.740   7.350  1.00 39.21 ? 62  LYS A CE    1 
ATOM   460  N  NZ    . LYS A 1 82  ? 23.276 7.763   5.844  1.00 39.93 ? 62  LYS A NZ    1 
ATOM   461  N  N     . ASN A 1 83  ? 25.422 7.720   12.392 1.00 18.36 ? 63  ASN A N     1 
ATOM   462  C  CA    . ASN A 1 83  ? 26.029 9.012   12.671 1.00 20.71 ? 63  ASN A CA    1 
ATOM   463  C  C     . ASN A 1 83  ? 26.488 9.016   14.126 1.00 18.21 ? 63  ASN A C     1 
ATOM   464  O  O     . ASN A 1 83  ? 25.658 8.919   15.030 1.00 17.90 ? 63  ASN A O     1 
ATOM   465  C  CB    . ASN A 1 83  ? 24.998 10.112  12.419 1.00 20.94 ? 63  ASN A CB    1 
ATOM   466  C  CG    . ASN A 1 83  ? 25.564 11.522  12.587 1.00 27.49 ? 63  ASN A CG    1 
ATOM   467  O  OD1   . ASN A 1 83  ? 25.763 12.018  13.718 1.00 25.40 ? 63  ASN A OD1   1 
ATOM   468  N  ND2   . ASN A 1 83  ? 25.803 12.194  11.450 1.00 28.84 ? 63  ASN A ND2   1 
ATOM   469  N  N     . ILE A 1 84  ? 27.794 9.123   14.343 1.00 17.07 ? 64  ILE A N     1 
ATOM   470  C  CA    . ILE A 1 84  ? 28.311 8.975   15.702 1.00 15.54 ? 64  ILE A CA    1 
ATOM   471  C  C     . ILE A 1 84  ? 27.835 10.119  16.590 1.00 17.29 ? 64  ILE A C     1 
ATOM   472  O  O     . ILE A 1 84  ? 27.629 9.926   17.789 1.00 17.28 ? 64  ILE A O     1 
ATOM   473  C  CB    . ILE A 1 84  ? 29.845 8.862   15.707 1.00 16.68 ? 64  ILE A CB    1 
ATOM   474  C  CG1   . ILE A 1 84  ? 30.336 8.340   17.068 1.00 19.80 ? 64  ILE A CG1   1 
ATOM   475  C  CG2   . ILE A 1 84  ? 30.510 10.194  15.316 1.00 19.04 ? 64  ILE A CG2   1 
ATOM   476  C  CD1   . ILE A 1 84  ? 31.848 8.190   17.136 1.00 20.21 ? 64  ILE A CD1   1 
ATOM   477  N  N     . GLY A 1 85  ? 27.670 11.322  16.034 1.00 17.69 ? 65  GLY A N     1 
ATOM   478  C  CA    . GLY A 1 85  ? 27.239 12.449  16.844 1.00 17.94 ? 65  GLY A CA    1 
ATOM   479  C  C     . GLY A 1 85  ? 25.831 12.258  17.364 1.00 18.20 ? 65  GLY A C     1 
ATOM   480  O  O     . GLY A 1 85  ? 25.546 12.534  18.532 1.00 18.05 ? 65  GLY A O     1 
ATOM   481  N  N     . GLU A 1 86  ? 24.926 11.782  16.502 1.00 21.04 ? 66  GLU A N     1 
ATOM   482  C  CA    . GLU A 1 86  ? 23.571 11.473  16.943 1.00 19.97 ? 66  GLU A CA    1 
ATOM   483  C  C     . GLU A 1 86  ? 23.555 10.320  17.933 1.00 16.40 ? 66  GLU A C     1 
ATOM   484  O  O     . GLU A 1 86  ? 22.830 10.367  18.933 1.00 18.76 ? 66  GLU A O     1 
ATOM   485  C  CB    . GLU A 1 86  ? 22.692 11.134  15.742 1.00 23.67 ? 66  GLU A CB    1 
ATOM   486  C  CG    . GLU A 1 86  ? 22.408 12.319  14.869 1.00 34.14 ? 66  GLU A CG    1 
ATOM   487  C  CD    . GLU A 1 86  ? 21.749 13.445  15.637 1.00 36.45 ? 66  GLU A CD    1 
ATOM   488  O  OE1   . GLU A 1 86  ? 20.789 13.169  16.395 1.00 41.79 ? 66  GLU A OE1   1 
ATOM   489  O  OE2   . GLU A 1 86  ? 22.211 14.598  15.492 1.00 39.08 ? 66  GLU A OE2   1 
ATOM   490  N  N     . LEU A 1 87  ? 24.358 9.280   17.690 1.00 17.62 ? 67  LEU A N     1 
ATOM   491  C  CA    . LEU A 1 87  ? 24.358 8.174   18.638 1.00 17.25 ? 67  LEU A CA    1 
ATOM   492  C  C     . LEU A 1 87  ? 24.917 8.613   19.992 1.00 19.49 ? 67  LEU A C     1 
ATOM   493  O  O     . LEU A 1 87  ? 24.419 8.184   21.049 1.00 18.65 ? 67  LEU A O     1 
ATOM   494  C  CB    . LEU A 1 87  ? 25.131 6.986   18.077 1.00 17.00 ? 67  LEU A CB    1 
ATOM   495  C  CG    . LEU A 1 87  ? 24.818 5.830   19.032 1.00 25.95 ? 67  LEU A CG    1 
ATOM   496  C  CD1   . LEU A 1 87  ? 24.000 4.807   18.379 1.00 25.83 ? 67  LEU A CD1   1 
ATOM   497  C  CD2   . LEU A 1 87  ? 26.052 5.238   19.756 1.00 21.41 ? 67  LEU A CD2   1 
ATOM   498  N  N     . GLY A 1 88  ? 25.892 9.517   19.974 1.00 17.65 ? 68  GLY A N     1 
ATOM   499  C  CA    . GLY A 1 88  ? 26.411 10.063  21.211 1.00 17.75 ? 68  GLY A CA    1 
ATOM   500  C  C     . GLY A 1 88  ? 25.386 10.851  22.008 1.00 20.23 ? 68  GLY A C     1 
ATOM   501  O  O     . GLY A 1 88  ? 25.418 10.856  23.243 1.00 18.42 ? 68  GLY A O     1 
ATOM   502  N  N     . LYS A 1 89  ? 24.501 11.579  21.323 1.00 18.18 ? 69  LYS A N     1 
ATOM   503  C  CA    . LYS A 1 89  ? 23.440 12.282  22.051 1.00 19.47 ? 69  LYS A CA    1 
ATOM   504  C  C     . LYS A 1 89  ? 22.524 11.296  22.756 1.00 19.60 ? 69  LYS A C     1 
ATOM   505  O  O     . LYS A 1 89  ? 22.106 11.519  23.905 1.00 18.78 ? 69  LYS A O     1 
ATOM   506  C  CB    . LYS A 1 89  ? 22.616 13.153  21.106 1.00 23.38 ? 69  LYS A CB    1 
ATOM   507  C  CG    . LYS A 1 89  ? 23.392 14.267  20.426 1.00 23.71 ? 69  LYS A CG    1 
ATOM   508  C  CD    . LYS A 1 89  ? 22.456 15.007  19.476 1.00 29.62 ? 69  LYS A CD    1 
ATOM   509  C  CE    . LYS A 1 89  ? 23.184 16.009  18.627 1.00 33.47 ? 69  LYS A CE    1 
ATOM   510  N  NZ    . LYS A 1 89  ? 22.332 16.545  17.548 1.00 41.33 ? 69  LYS A NZ    1 
ATOM   511  N  N     . THR A 1 90  ? 22.185 10.209  22.070 1.00 16.49 ? 70  THR A N     1 
ATOM   512  C  CA    . THR A 1 90  ? 21.377 9.144   22.653 1.00 18.40 ? 70  THR A CA    1 
ATOM   513  C  C     . THR A 1 90  ? 22.053 8.518   23.873 1.00 17.41 ? 70  THR A C     1 
ATOM   514  O  O     . THR A 1 90  ? 21.416 8.315   24.911 1.00 18.65 ? 70  THR A O     1 
ATOM   515  C  CB    . THR A 1 90  ? 21.108 8.086   21.588 1.00 21.55 ? 70  THR A CB    1 
ATOM   516  O  OG1   . THR A 1 90  ? 20.355 8.684   20.523 1.00 20.17 ? 70  THR A OG1   1 
ATOM   517  C  CG2   . THR A 1 90  ? 20.371 6.894   22.159 1.00 19.84 ? 70  THR A CG2   1 
ATOM   518  N  N     . PHE A 1 91  ? 23.338 8.172   23.747 1.00 19.27 ? 71  PHE A N     1 
ATOM   519  C  CA    . PHE A 1 91  ? 24.070 7.568   24.857 1.00 14.41 ? 71  PHE A CA    1 
ATOM   520  C  C     . PHE A 1 91  ? 24.137 8.528   26.023 1.00 16.25 ? 71  PHE A C     1 
ATOM   521  O  O     . PHE A 1 91  ? 23.859 8.161   27.175 1.00 16.00 ? 71  PHE A O     1 
ATOM   522  C  CB    . PHE A 1 91  ? 25.472 7.206   24.382 1.00 14.18 ? 71  PHE A CB    1 
ATOM   523  C  CG    . PHE A 1 91  ? 26.359 6.589   25.438 1.00 17.97 ? 71  PHE A CG    1 
ATOM   524  C  CD1   . PHE A 1 91  ? 25.915 5.543   26.224 1.00 18.16 ? 71  PHE A CD1   1 
ATOM   525  C  CD2   . PHE A 1 91  ? 27.686 7.003   25.558 1.00 21.41 ? 71  PHE A CD2   1 
ATOM   526  C  CE1   . PHE A 1 91  ? 26.752 4.967   27.184 1.00 20.12 ? 71  PHE A CE1   1 
ATOM   527  C  CE2   . PHE A 1 91  ? 28.527 6.430   26.492 1.00 18.66 ? 71  PHE A CE2   1 
ATOM   528  C  CZ    . PHE A 1 91  ? 28.051 5.400   27.311 1.00 17.23 ? 71  PHE A CZ    1 
ATOM   529  N  N     . SER A 1 92  ? 24.533 9.767   25.731 1.00 17.50 ? 72  SER A N     1 
ATOM   530  C  CA    . SER A 1 92  ? 24.693 10.781  26.776 1.00 19.93 ? 72  SER A CA    1 
ATOM   531  C  C     . SER A 1 92  ? 23.395 10.976  27.553 1.00 19.85 ? 72  SER A C     1 
ATOM   532  O  O     . SER A 1 92  ? 23.393 11.005  28.793 1.00 19.94 ? 72  SER A O     1 
ATOM   533  C  CB    . SER A 1 92  ? 25.154 12.093  26.126 1.00 21.89 ? 72  SER A CB    1 
ATOM   534  O  OG    . SER A 1 92  ? 25.304 13.144  27.082 1.00 27.92 ? 72  SER A OG    1 
ATOM   535  N  N     . LYS A 1 93  ? 22.278 11.135  26.836 1.00 17.87 ? 73  LYS A N     1 
ATOM   536  C  CA    . LYS A 1 93  ? 20.979 11.278  27.487 1.00 20.53 ? 73  LYS A CA    1 
ATOM   537  C  C     . LYS A 1 93  ? 20.671 10.087  28.389 1.00 21.14 ? 73  LYS A C     1 
ATOM   538  O  O     . LYS A 1 93  ? 20.202 10.263  29.518 1.00 18.95 ? 73  LYS A O     1 
ATOM   539  C  CB    . LYS A 1 93  ? 19.880 11.454  26.431 1.00 23.54 ? 73  LYS A CB    1 
ATOM   540  C  CG    . LYS A 1 93  ? 18.443 11.444  26.967 1.00 27.51 ? 73  LYS A CG    1 
ATOM   541  C  CD    . LYS A 1 93  ? 17.432 11.597  25.841 1.00 30.33 ? 73  LYS A CD    1 
ATOM   542  N  N     . GLY A 1 94  ? 20.964 8.873   27.928 1.00 17.34 ? 74  GLY A N     1 
ATOM   543  C  CA    . GLY A 1 94  ? 20.685 7.694   28.729 1.00 17.66 ? 74  GLY A CA    1 
ATOM   544  C  C     . GLY A 1 94  ? 21.481 7.650   30.020 1.00 17.78 ? 74  GLY A C     1 
ATOM   545  O  O     . GLY A 1 94  ? 20.953 7.293   31.089 1.00 17.57 ? 74  GLY A O     1 
ATOM   546  N  N     . LEU A 1 95  ? 22.763 7.986   29.940 1.00 17.49 ? 75  LEU A N     1 
ATOM   547  C  CA    . LEU A 1 95  ? 23.582 8.063   31.147 1.00 16.95 ? 75  LEU A CA    1 
ATOM   548  C  C     . LEU A 1 95  ? 23.055 9.122   32.105 1.00 15.97 ? 75  LEU A C     1 
ATOM   549  O  O     . LEU A 1 95  ? 22.994 8.906   33.324 1.00 18.10 ? 75  LEU A O     1 
ATOM   550  C  CB    . LEU A 1 95  ? 25.039 8.387   30.794 1.00 17.60 ? 75  LEU A CB    1 
ATOM   551  C  CG    . LEU A 1 95  ? 25.804 7.383   29.939 1.00 18.51 ? 75  LEU A CG    1 
ATOM   552  C  CD1   . LEU A 1 95  ? 27.134 7.987   29.480 1.00 22.73 ? 75  LEU A CD1   1 
ATOM   553  C  CD2   . LEU A 1 95  ? 26.021 6.106   30.670 1.00 18.55 ? 75  LEU A CD2   1 
ATOM   554  N  N     . LEU A 1 96  ? 22.779 10.313  31.583 1.00 15.70 ? 76  LEU A N     1 
ATOM   555  C  CA    . LEU A 1 96  ? 22.462 11.442  32.445 1.00 16.53 ? 76  LEU A CA    1 
ATOM   556  C  C     . LEU A 1 96  ? 21.112 11.278  33.122 1.00 21.51 ? 76  LEU A C     1 
ATOM   557  O  O     . LEU A 1 96  ? 20.906 11.808  34.218 1.00 20.97 ? 76  LEU A O     1 
ATOM   558  C  CB    . LEU A 1 96  ? 22.499 12.736  31.634 1.00 16.68 ? 76  LEU A CB    1 
ATOM   559  C  CG    . LEU A 1 96  ? 23.915 13.148  31.207 1.00 19.82 ? 76  LEU A CG    1 
ATOM   560  C  CD1   . LEU A 1 96  ? 23.877 14.128  30.046 1.00 21.66 ? 76  LEU A CD1   1 
ATOM   561  C  CD2   . LEU A 1 96  ? 24.648 13.759  32.394 1.00 18.28 ? 76  LEU A CD2   1 
ATOM   562  N  N     . MET A 1 97  ? 20.180 10.571  32.489 1.00 16.21 ? 77  MET A N     1 
ATOM   563  C  CA    . MET A 1 97  ? 18.906 10.248  33.128 1.00 19.94 ? 77  MET A CA    1 
ATOM   564  C  C     . MET A 1 97  ? 18.972 8.980   33.964 1.00 24.17 ? 77  MET A C     1 
ATOM   565  O  O     . MET A 1 97  ? 17.976 8.633   34.597 1.00 28.85 ? 77  MET A O     1 
ATOM   566  C  CB    . MET A 1 97  ? 17.797 10.113  32.066 1.00 23.29 ? 77  MET A CB    1 
ATOM   567  C  CG    . MET A 1 97  ? 17.401 11.453  31.478 1.00 32.22 ? 77  MET A CG    1 
ATOM   568  S  SD    . MET A 1 97  ? 16.287 11.326  30.070 1.00 44.58 ? 77  MET A SD    1 
ATOM   569  C  CE    . MET A 1 97  ? 16.026 9.539   29.957 1.00 38.53 ? 77  MET A CE    1 
ATOM   570  N  N     . GLY A 1 98  ? 20.118 8.295   34.016 1.00 25.66 ? 78  GLY A N     1 
ATOM   571  C  CA    . GLY A 1 98  ? 20.219 7.099   34.826 1.00 25.09 ? 78  GLY A CA    1 
ATOM   572  C  C     . GLY A 1 98  ? 21.402 7.052   35.777 1.00 23.49 ? 78  GLY A C     1 
ATOM   573  O  O     . GLY A 1 98  ? 21.792 5.968   36.208 1.00 22.19 ? 78  GLY A O     1 
ATOM   574  N  N     . ALA A 1 99  ? 21.986 8.204   36.113 1.00 21.66 ? 79  ALA A N     1 
ATOM   575  C  CA    . ALA A 1 99  ? 23.220 8.217   36.891 1.00 22.66 ? 79  ALA A CA    1 
ATOM   576  C  C     . ALA A 1 99  ? 22.949 7.855   38.348 1.00 24.29 ? 79  ALA A C     1 
ATOM   577  O  O     . ALA A 1 99  ? 22.039 8.413   38.968 1.00 26.11 ? 79  ALA A O     1 
ATOM   578  C  CB    . ALA A 1 99  ? 23.867 9.590   36.818 1.00 18.29 ? 79  ALA A CB    1 
ATOM   579  N  N     . ARG A 1 100 ? 23.734 6.914   38.880 1.00 21.10 ? 80  ARG A N     1 
ATOM   580  C  CA    . ARG A 1 100 ? 23.632 6.435   40.260 1.00 22.62 ? 80  ARG A CA    1 
ATOM   581  C  C     . ARG A 1 100 ? 24.980 6.558   40.962 1.00 23.24 ? 80  ARG A C     1 
ATOM   582  O  O     . ARG A 1 100 ? 25.988 6.044   40.454 1.00 21.37 ? 80  ARG A O     1 
ATOM   583  C  CB    . ARG A 1 100 ? 23.194 4.956   40.316 1.00 22.77 ? 80  ARG A CB    1 
ATOM   584  C  CG    . ARG A 1 100 ? 21.794 4.674   39.762 1.00 29.01 ? 80  ARG A CG    1 
ATOM   585  N  N     . GLY A 1 101 ? 24.986 7.191   42.144 1.00 20.67 ? 81  GLY A N     1 
ATOM   586  C  CA    . GLY A 1 101 ? 26.169 7.274   42.978 1.00 21.44 ? 81  GLY A CA    1 
ATOM   587  C  C     . GLY A 1 101 ? 27.165 8.296   42.469 1.00 18.76 ? 81  GLY A C     1 
ATOM   588  O  O     . GLY A 1 101 ? 27.049 8.815   41.350 1.00 20.91 ? 81  GLY A O     1 
ATOM   589  N  N     . ASN A 1 102 ? 28.179 8.582   43.305 1.00 20.35 ? 82  ASN A N     1 
ATOM   590  C  CA    . ASN A 1 102 ? 29.262 9.470   42.872 1.00 24.32 ? 82  ASN A CA    1 
ATOM   591  C  C     . ASN A 1 102 ? 29.870 8.965   41.566 1.00 20.01 ? 82  ASN A C     1 
ATOM   592  O  O     . ASN A 1 102 ? 30.172 9.751   40.662 1.00 18.50 ? 82  ASN A O     1 
ATOM   593  C  CB    . ASN A 1 102 ? 30.411 9.580   43.897 1.00 20.62 ? 82  ASN A CB    1 
ATOM   594  C  CG    . ASN A 1 102 ? 29.971 9.968   45.334 1.00 32.06 ? 82  ASN A CG    1 
ATOM   595  O  OD1   . ASN A 1 102 ? 30.705 9.706   46.293 1.00 40.42 ? 82  ASN A OD1   1 
ATOM   596  N  ND2   . ASN A 1 102 ? 28.830 10.583  45.476 1.00 29.57 ? 82  ASN A ND2   1 
ATOM   597  N  N     . SER A 1 103 ? 30.088 7.646   41.481 1.00 16.62 ? 83  SER A N     1 
ATOM   598  C  CA    . SER A 1 103 ? 30.810 7.070   40.363 1.00 17.61 ? 83  SER A CA    1 
ATOM   599  C  C     . SER A 1 103 ? 29.962 7.139   39.098 1.00 17.08 ? 83  SER A C     1 
ATOM   600  O  O     . SER A 1 103 ? 30.475 7.490   38.036 1.00 17.03 ? 83  SER A O     1 
ATOM   601  C  CB    . SER A 1 103 ? 31.226 5.626   40.674 1.00 17.80 ? 83  SER A CB    1 
ATOM   602  O  OG    . SER A 1 103 ? 30.107 4.792   40.931 1.00 19.67 ? 83  SER A OG    1 
ATOM   603  N  N     . GLY A 1 104 ? 28.656 6.870   39.220 1.00 15.43 ? 84  GLY A N     1 
ATOM   604  C  CA    . GLY A 1 104 ? 27.770 6.927   38.068 1.00 14.88 ? 84  GLY A CA    1 
ATOM   605  C  C     . GLY A 1 104 ? 27.586 8.341   37.561 1.00 15.67 ? 84  GLY A C     1 
ATOM   606  O  O     . GLY A 1 104 ? 27.551 8.573   36.351 1.00 15.25 ? 84  GLY A O     1 
ATOM   607  N  N     . VAL A 1 105 ? 27.456 9.305   38.475 1.00 14.96 ? 85  VAL A N     1 
ATOM   608  C  CA    . VAL A 1 105 ? 27.385 10.693  38.054 1.00 15.60 ? 85  VAL A CA    1 
ATOM   609  C  C     . VAL A 1 105 ? 28.666 11.086  37.330 1.00 17.80 ? 85  VAL A C     1 
ATOM   610  O  O     . VAL A 1 105 ? 28.620 11.691  36.260 1.00 16.20 ? 85  VAL A O     1 
ATOM   611  C  CB    . VAL A 1 105 ? 27.098 11.612  39.244 1.00 15.83 ? 85  VAL A CB    1 
ATOM   612  C  CG1   . VAL A 1 105 ? 27.226 13.057  38.835 1.00 19.99 ? 85  VAL A CG1   1 
ATOM   613  C  CG2   . VAL A 1 105 ? 25.699 11.322  39.824 1.00 17.52 ? 85  VAL A CG2   1 
ATOM   614  N  N     . ILE A 1 106 ? 29.827 10.733  37.886 1.00 16.66 ? 86  ILE A N     1 
ATOM   615  C  CA    . ILE A 1 106 ? 31.074 11.104  37.208 1.00 16.07 ? 86  ILE A CA    1 
ATOM   616  C  C     . ILE A 1 106 ? 31.177 10.418  35.842 1.00 15.33 ? 86  ILE A C     1 
ATOM   617  O  O     . ILE A 1 106 ? 31.519 11.055  34.840 1.00 13.33 ? 86  ILE A O     1 
ATOM   618  C  CB    . ILE A 1 106 ? 32.292 10.815  38.102 1.00 15.06 ? 86  ILE A CB    1 
ATOM   619  C  CG1   . ILE A 1 106 ? 32.312 11.794  39.266 1.00 16.33 ? 86  ILE A CG1   1 
ATOM   620  C  CG2   . ILE A 1 106 ? 33.588 10.978  37.302 1.00 16.83 ? 86  ILE A CG2   1 
ATOM   621  C  CD1   . ILE A 1 106 ? 33.298 11.392  40.342 1.00 18.88 ? 86  ILE A CD1   1 
ATOM   622  N  N     . LEU A 1 107 ? 30.865 9.122   35.769 1.00 16.81 ? 87  LEU A N     1 
ATOM   623  C  CA    . LEU A 1 107 ? 30.828 8.450   34.465 1.00 15.72 ? 87  LEU A CA    1 
ATOM   624  C  C     . LEU A 1 107 ? 29.917 9.173   33.460 1.00 15.80 ? 87  LEU A C     1 
ATOM   625  O  O     . LEU A 1 107 ? 30.272 9.339   32.281 1.00 13.49 ? 87  LEU A O     1 
ATOM   626  C  CB    . LEU A 1 107 ? 30.358 7.011   34.653 1.00 16.97 ? 87  LEU A CB    1 
ATOM   627  C  CG    . LEU A 1 107 ? 30.382 6.147   33.399 1.00 16.25 ? 87  LEU A CG    1 
ATOM   628  C  CD1   . LEU A 1 107 ? 31.800 5.851   32.972 1.00 18.51 ? 87  LEU A CD1   1 
ATOM   629  C  CD2   . LEU A 1 107 ? 29.634 4.859   33.673 1.00 20.33 ? 87  LEU A CD2   1 
ATOM   630  N  N     . SER A 1 108 ? 28.744 9.609   33.901 1.00 13.82 ? 88  SER A N     1 
ATOM   631  C  CA    . SER A 1 108 ? 27.836 10.297  32.990 1.00 14.65 ? 88  SER A CA    1 
ATOM   632  C  C     . SER A 1 108 ? 28.413 11.635  32.522 1.00 15.69 ? 88  SER A C     1 
ATOM   633  O  O     . SER A 1 108 ? 28.183 12.037  31.371 1.00 15.42 ? 88  SER A O     1 
ATOM   634  C  CB    . SER A 1 108 ? 26.474 10.489  33.655 1.00 15.20 ? 88  SER A CB    1 
ATOM   635  O  OG    . SER A 1 108 ? 26.477 11.496  34.669 1.00 16.87 ? 88  SER A OG    1 
ATOM   636  N  N     . GLN A 1 109 ? 29.158 12.322  33.392 1.00 14.95 ? 89  GLN A N     1 
ATOM   637  C  CA    . GLN A 1 109 ? 29.738 13.611  33.040 1.00 13.84 ? 89  GLN A CA    1 
ATOM   638  C  C     . GLN A 1 109 ? 30.935 13.429  32.122 1.00 13.12 ? 89  GLN A C     1 
ATOM   639  O  O     . GLN A 1 109 ? 31.090 14.174  31.145 1.00 16.94 ? 89  GLN A O     1 
ATOM   640  C  CB    . GLN A 1 109 ? 30.113 14.392  34.312 1.00 14.09 ? 89  GLN A CB    1 
ATOM   641  C  CG    . GLN A 1 109 ? 28.875 14.761  35.172 1.00 14.59 ? 89  GLN A CG    1 
ATOM   642  C  CD    . GLN A 1 109 ? 27.949 15.743  34.474 1.00 16.62 ? 89  GLN A CD    1 
ATOM   643  O  OE1   . GLN A 1 109 ? 28.387 16.554  33.647 1.00 17.97 ? 89  GLN A OE1   1 
ATOM   644  N  NE2   . GLN A 1 109 ? 26.663 15.645  34.766 1.00 17.78 ? 89  GLN A NE2   1 
ATOM   645  N  N     . LEU A 1 110 ? 31.781 12.432  32.409 1.00 15.84 ? 90  LEU A N     1 
ATOM   646  C  CA    . LEU A 1 110 ? 32.853 12.068  31.487 1.00 14.97 ? 90  LEU A CA    1 
ATOM   647  C  C     . LEU A 1 110 ? 32.311 11.868  30.078 1.00 16.56 ? 90  LEU A C     1 
ATOM   648  O  O     . LEU A 1 110 ? 32.847 12.412  29.107 1.00 16.24 ? 90  LEU A O     1 
ATOM   649  C  CB    . LEU A 1 110 ? 33.578 10.792  31.953 1.00 11.34 ? 90  LEU A CB    1 
ATOM   650  C  CG    . LEU A 1 110 ? 34.568 10.923  33.129 1.00 15.24 ? 90  LEU A CG    1 
ATOM   651  C  CD1   . LEU A 1 110 ? 34.962 9.533   33.600 1.00 17.78 ? 90  LEU A CD1   1 
ATOM   652  C  CD2   . LEU A 1 110 ? 35.787 11.727  32.727 1.00 15.14 ? 90  LEU A CD2   1 
ATOM   653  N  N     . PHE A 1 111 ? 31.233 11.112  29.939 1.00 16.35 ? 91  PHE A N     1 
ATOM   654  C  CA    . PHE A 1 111 ? 30.774 10.850  28.579 1.00 17.97 ? 91  PHE A CA    1 
ATOM   655  C  C     . PHE A 1 111 ? 29.888 11.945  28.030 1.00 15.39 ? 91  PHE A C     1 
ATOM   656  O  O     . PHE A 1 111 ? 29.799 12.092  26.802 1.00 16.06 ? 91  PHE A O     1 
ATOM   657  C  CB    . PHE A 1 111 ? 30.111 9.482   28.508 1.00 16.15 ? 91  PHE A CB    1 
ATOM   658  C  CG    . PHE A 1 111 ? 31.127 8.380   28.385 1.00 20.41 ? 91  PHE A CG    1 
ATOM   659  C  CD1   . PHE A 1 111 ? 31.944 8.311   27.266 1.00 22.40 ? 91  PHE A CD1   1 
ATOM   660  C  CD2   . PHE A 1 111 ? 31.322 7.464   29.394 1.00 23.32 ? 91  PHE A CD2   1 
ATOM   661  C  CE1   . PHE A 1 111 ? 32.936 7.336   27.163 1.00 21.65 ? 91  PHE A CE1   1 
ATOM   662  C  CE2   . PHE A 1 111 ? 32.319 6.477   29.287 1.00 26.36 ? 91  PHE A CE2   1 
ATOM   663  C  CZ    . PHE A 1 111 ? 33.119 6.423   28.178 1.00 23.35 ? 91  PHE A CZ    1 
ATOM   664  N  N     . ARG A 1 112 ? 29.253 12.751  28.888 1.00 17.15 ? 92  ARG A N     1 
ATOM   665  C  CA    . ARG A 1 112 ? 28.602 13.951  28.372 1.00 17.82 ? 92  ARG A CA    1 
ATOM   666  C  C     . ARG A 1 112 ? 29.606 14.829  27.633 1.00 17.75 ? 92  ARG A C     1 
ATOM   667  O  O     . ARG A 1 112 ? 29.322 15.329  26.539 1.00 16.88 ? 92  ARG A O     1 
ATOM   668  C  CB    . ARG A 1 112 ? 27.930 14.745  29.489 1.00 17.42 ? 92  ARG A CB    1 
ATOM   669  C  CG    . ARG A 1 112 ? 27.366 16.096  28.973 1.00 17.34 ? 92  ARG A CG    1 
ATOM   670  C  CD    . ARG A 1 112 ? 26.573 16.802  30.044 1.00 17.49 ? 92  ARG A CD    1 
ATOM   671  N  NE    . ARG A 1 112 ? 27.311 17.394  31.173 1.00 17.23 ? 92  ARG A NE    1 
ATOM   672  C  CZ    . ARG A 1 112 ? 27.646 18.683  31.277 1.00 19.04 ? 92  ARG A CZ    1 
ATOM   673  N  NH1   . ARG A 1 112 ? 27.454 19.532  30.277 1.00 19.19 ? 92  ARG A NH1   1 
ATOM   674  N  NH2   . ARG A 1 112 ? 28.206 19.126  32.381 1.00 18.62 ? 92  ARG A NH2   1 
ATOM   675  N  N     . GLY A 1 113 ? 30.783 15.050  28.223 1.00 16.66 ? 93  GLY A N     1 
ATOM   676  C  CA    . GLY A 1 113 ? 31.761 15.898  27.562 1.00 16.79 ? 93  GLY A CA    1 
ATOM   677  C  C     . GLY A 1 113 ? 32.336 15.249  26.317 1.00 16.98 ? 93  GLY A C     1 
ATOM   678  O  O     . GLY A 1 113 ? 32.574 15.924  25.301 1.00 16.45 ? 93  GLY A O     1 
ATOM   679  N  N     . PHE A 1 114 ? 32.573 13.933  26.379 1.00 16.39 ? 94  PHE A N     1 
ATOM   680  C  CA    . PHE A 1 114 ? 33.060 13.184  25.223 1.00 13.67 ? 94  PHE A CA    1 
ATOM   681  C  C     . PHE A 1 114 ? 32.094 13.327  24.058 1.00 18.58 ? 94  PHE A C     1 
ATOM   682  O  O     . PHE A 1 114 ? 32.486 13.637  22.917 1.00 15.94 ? 94  PHE A O     1 
ATOM   683  C  CB    . PHE A 1 114 ? 33.207 11.714  25.637 1.00 13.37 ? 94  PHE A CB    1 
ATOM   684  C  CG    . PHE A 1 114 ? 33.734 10.794  24.561 1.00 17.19 ? 94  PHE A CG    1 
ATOM   685  C  CD1   . PHE A 1 114 ? 35.030 10.320  24.622 1.00 16.74 ? 94  PHE A CD1   1 
ATOM   686  C  CD2   . PHE A 1 114 ? 32.911 10.355  23.538 1.00 17.08 ? 94  PHE A CD2   1 
ATOM   687  C  CE1   . PHE A 1 114 ? 35.520 9.446   23.669 1.00 20.29 ? 94  PHE A CE1   1 
ATOM   688  C  CE2   . PHE A 1 114 ? 33.389 9.491   22.558 1.00 18.03 ? 94  PHE A CE2   1 
ATOM   689  C  CZ    . PHE A 1 114 ? 34.701 9.030   22.626 1.00 20.27 ? 94  PHE A CZ    1 
ATOM   690  N  N     . CYS A 1 115 ? 30.817 13.082  24.335 1.00 15.08 ? 95  CYS A N     1 
ATOM   691  C  CA    . CYS A 1 115 ? 29.802 13.079  23.292 1.00 15.12 ? 95  CYS A CA    1 
ATOM   692  C  C     . CYS A 1 115 ? 29.534 14.479  22.766 1.00 18.03 ? 95  CYS A C     1 
ATOM   693  O  O     . CYS A 1 115 ? 29.359 14.665  21.555 1.00 17.25 ? 95  CYS A O     1 
ATOM   694  C  CB    . CYS A 1 115 ? 28.527 12.419  23.815 1.00 18.27 ? 95  CYS A CB    1 
ATOM   695  S  SG    . CYS A 1 115 ? 28.708 10.629  24.076 1.00 17.86 ? 95  CYS A SG    1 
ATOM   696  N  N     . LYS A 1 116 ? 29.539 15.483  23.638 1.00 16.05 ? 96  LYS A N     1 
ATOM   697  C  CA    . LYS A 1 116 ? 29.348 16.841  23.153 1.00 18.97 ? 96  LYS A CA    1 
ATOM   698  C  C     . LYS A 1 116 ? 30.427 17.204  22.145 1.00 17.08 ? 96  LYS A C     1 
ATOM   699  O  O     . LYS A 1 116 ? 30.165 17.938  21.185 1.00 19.87 ? 96  LYS A O     1 
ATOM   700  C  CB    . LYS A 1 116 ? 29.351 17.825  24.324 1.00 17.81 ? 96  LYS A CB    1 
ATOM   701  C  CG    . LYS A 1 116 ? 29.268 19.281  23.911 1.00 23.38 ? 96  LYS A CG    1 
ATOM   702  C  CD    . LYS A 1 116 ? 27.910 19.606  23.295 1.00 28.27 ? 96  LYS A CD    1 
ATOM   703  C  CE    . LYS A 1 116 ? 27.792 21.112  23.049 1.00 35.57 ? 96  LYS A CE    1 
ATOM   704  N  NZ    . LYS A 1 116 ? 26.472 21.482  22.467 1.00 43.26 ? 96  LYS A NZ    1 
ATOM   705  N  N     . ASN A 1 117 ? 31.634 16.682  22.342 1.00 17.40 ? 97  ASN A N     1 
ATOM   706  C  CA    . ASN A 1 117 ? 32.765 17.044  21.497 1.00 17.00 ? 97  ASN A CA    1 
ATOM   707  C  C     . ASN A 1 117 ? 32.609 16.558  20.056 1.00 19.66 ? 97  ASN A C     1 
ATOM   708  O  O     . ASN A 1 117 ? 33.275 17.097  19.170 1.00 22.14 ? 97  ASN A O     1 
ATOM   709  C  CB    . ASN A 1 117 ? 34.046 16.472  22.077 1.00 17.71 ? 97  ASN A CB    1 
ATOM   710  C  CG    . ASN A 1 117 ? 35.276 17.148  21.524 1.00 24.25 ? 97  ASN A CG    1 
ATOM   711  O  OD1   . ASN A 1 117 ? 35.408 18.367  21.636 1.00 23.38 ? 97  ASN A OD1   1 
ATOM   712  N  ND2   . ASN A 1 117 ? 36.186 16.369  20.922 1.00 23.17 ? 97  ASN A ND2   1 
ATOM   713  N  N     . ILE A 1 118 ? 31.766 15.550  19.812 1.00 19.96 ? 98  ILE A N     1 
ATOM   714  C  CA    . ILE A 1 118 ? 31.628 14.915  18.506 1.00 21.21 ? 98  ILE A CA    1 
ATOM   715  C  C     . ILE A 1 118 ? 30.205 15.073  17.962 1.00 21.17 ? 98  ILE A C     1 
ATOM   716  O  O     . ILE A 1 118 ? 29.819 14.402  17.001 1.00 20.06 ? 98  ILE A O     1 
ATOM   717  C  CB    . ILE A 1 118 ? 32.046 13.430  18.572 1.00 19.28 ? 98  ILE A CB    1 
ATOM   718  C  CG1   . ILE A 1 118 ? 31.160 12.659  19.546 1.00 17.90 ? 98  ILE A CG1   1 
ATOM   719  C  CG2   . ILE A 1 118 ? 33.500 13.303  18.994 1.00 21.83 ? 98  ILE A CG2   1 
ATOM   720  C  CD1   . ILE A 1 118 ? 31.312 11.173  19.495 1.00 21.03 ? 98  ILE A CD1   1 
ATOM   721  N  N     . GLU A 1 119 ? 29.429 15.973  18.574 1.00 17.61 ? 99  GLU A N     1 
ATOM   722  C  CA    . GLU A 1 119 ? 27.995 16.099  18.313 1.00 23.04 ? 99  GLU A CA    1 
ATOM   723  C  C     . GLU A 1 119 ? 27.655 16.272  16.835 1.00 23.62 ? 99  GLU A C     1 
ATOM   724  O  O     . GLU A 1 119 ? 26.604 15.812  16.368 1.00 22.23 ? 99  GLU A O     1 
ATOM   725  C  CB    . GLU A 1 119 ? 27.461 17.295  19.089 1.00 27.81 ? 99  GLU A CB    1 
ATOM   726  C  CG    . GLU A 1 119 ? 26.248 16.953  19.859 1.00 37.52 ? 99  GLU A CG    1 
ATOM   727  C  CD    . GLU A 1 119 ? 25.814 18.072  20.778 1.00 39.94 ? 99  GLU A CD    1 
ATOM   728  O  OE1   . GLU A 1 119 ? 26.017 19.250  20.393 1.00 33.61 ? 99  GLU A OE1   1 
ATOM   729  O  OE2   . GLU A 1 119 ? 25.292 17.746  21.878 1.00 35.66 ? 99  GLU A OE2   1 
ATOM   730  N  N     . SER A 1 120 ? 28.499 16.962  16.096 1.00 21.76 ? 100 SER A N     1 
ATOM   731  C  CA    . SER A 1 120 ? 28.212 17.261  14.699 1.00 29.82 ? 100 SER A CA    1 
ATOM   732  C  C     . SER A 1 120 ? 28.881 16.306  13.720 1.00 30.60 ? 100 SER A C     1 
ATOM   733  O  O     . SER A 1 120 ? 28.706 16.466  12.506 1.00 26.63 ? 100 SER A O     1 
ATOM   734  C  CB    . SER A 1 120 ? 28.631 18.694  14.399 1.00 33.84 ? 100 SER A CB    1 
ATOM   735  O  OG    . SER A 1 120 ? 27.820 19.566  15.174 1.00 36.92 ? 100 SER A OG    1 
ATOM   736  N  N     . GLU A 1 121 ? 29.612 15.308  14.209 1.00 22.58 ? 101 GLU A N     1 
ATOM   737  C  CA    . GLU A 1 121 ? 30.366 14.397  13.357 1.00 22.11 ? 101 GLU A CA    1 
ATOM   738  C  C     . GLU A 1 121 ? 29.541 13.169  12.987 1.00 24.92 ? 101 GLU A C     1 
ATOM   739  O  O     . GLU A 1 121 ? 28.689 12.714  13.752 1.00 22.64 ? 101 GLU A O     1 
ATOM   740  C  CB    . GLU A 1 121 ? 31.641 13.933  14.061 1.00 23.38 ? 101 GLU A CB    1 
ATOM   741  C  CG    . GLU A 1 121 ? 32.476 15.046  14.637 1.00 28.63 ? 101 GLU A CG    1 
ATOM   742  C  CD    . GLU A 1 121 ? 32.934 16.025  13.590 1.00 40.82 ? 101 GLU A CD    1 
ATOM   743  O  OE1   . GLU A 1 121 ? 33.317 15.585  12.476 1.00 33.58 ? 101 GLU A OE1   1 
ATOM   744  O  OE2   . GLU A 1 121 ? 32.873 17.236  13.884 1.00 49.78 ? 101 GLU A OE2   1 
ATOM   745  N  N     . SER A 1 122 ? 29.835 12.606  11.814 1.00 23.90 ? 102 SER A N     1 
ATOM   746  C  CA    . SER A 1 122 ? 29.272 11.320  11.441 1.00 22.03 ? 102 SER A CA    1 
ATOM   747  C  C     . SER A 1 122 ? 30.217 10.175  11.769 1.00 17.79 ? 102 SER A C     1 
ATOM   748  O  O     . SER A 1 122 ? 29.756 9.071   12.058 1.00 18.82 ? 102 SER A O     1 
ATOM   749  C  CB    . SER A 1 122 ? 28.918 11.304  9.938  1.00 25.67 ? 102 SER A CB    1 
ATOM   750  O  OG    . SER A 1 122 ? 30.034 11.665  9.151  1.00 27.31 ? 102 SER A OG    1 
ATOM   751  N  N     . GLU A 1 123 ? 31.522 10.414  11.703 1.00 21.11 ? 103 GLU A N     1 
ATOM   752  C  CA    . GLU A 1 123 ? 32.523 9.461   12.162 1.00 22.58 ? 103 GLU A CA    1 
ATOM   753  C  C     . GLU A 1 123 ? 33.737 10.254  12.639 1.00 21.01 ? 103 GLU A C     1 
ATOM   754  O  O     . GLU A 1 123 ? 33.919 11.419  12.268 1.00 24.63 ? 103 GLU A O     1 
ATOM   755  C  CB    . GLU A 1 123 ? 32.911 8.445   11.069 1.00 24.43 ? 103 GLU A CB    1 
ATOM   756  C  CG    . GLU A 1 123 ? 33.695 8.999   9.907  1.00 29.38 ? 103 GLU A CG    1 
ATOM   757  C  CD    . GLU A 1 123 ? 32.883 9.941   9.036  1.00 40.96 ? 103 GLU A CD    1 
ATOM   758  O  OE1   . GLU A 1 123 ? 31.741 9.573   8.668  1.00 38.77 ? 103 GLU A OE1   1 
ATOM   759  O  OE2   . GLU A 1 123 ? 33.389 11.054  8.729  1.00 38.80 ? 103 GLU A OE2   1 
ATOM   760  N  N     . ILE A 1 124 ? 34.570 9.620   13.467 1.00 19.44 ? 104 ILE A N     1 
ATOM   761  C  CA    . ILE A 1 124 ? 35.748 10.283  14.018 1.00 21.60 ? 104 ILE A CA    1 
ATOM   762  C  C     . ILE A 1 124 ? 37.003 9.446   13.791 1.00 20.82 ? 104 ILE A C     1 
ATOM   763  O  O     . ILE A 1 124 ? 36.958 8.214   13.697 1.00 22.84 ? 104 ILE A O     1 
ATOM   764  C  CB    . ILE A 1 124 ? 35.591 10.608  15.528 1.00 18.62 ? 104 ILE A CB    1 
ATOM   765  C  CG1   . ILE A 1 124 ? 35.572 9.347   16.378 1.00 18.02 ? 104 ILE A CG1   1 
ATOM   766  C  CG2   . ILE A 1 124 ? 34.345 11.452  15.774 1.00 19.49 ? 104 ILE A CG2   1 
ATOM   767  C  CD1   . ILE A 1 124 ? 35.446 9.668   17.895 1.00 19.63 ? 104 ILE A CD1   1 
ATOM   768  N  N     . ASN A 1 125 ? 38.137 10.136  13.703 1.00 19.90 ? 105 ASN A N     1 
ATOM   769  C  CA    . ASN A 1 125 ? 39.432 9.501   13.560 1.00 21.37 ? 105 ASN A CA    1 
ATOM   770  C  C     . ASN A 1 125 ? 40.096 9.417   14.929 1.00 19.52 ? 105 ASN A C     1 
ATOM   771  O  O     . ASN A 1 125 ? 39.513 9.792   15.955 1.00 21.30 ? 105 ASN A O     1 
ATOM   772  C  CB    . ASN A 1 125 ? 40.290 10.263  12.542 1.00 21.92 ? 105 ASN A CB    1 
ATOM   773  C  CG    . ASN A 1 125 ? 40.645 11.678  12.981 1.00 27.35 ? 105 ASN A CG    1 
ATOM   774  O  OD1   . ASN A 1 125 ? 40.464 12.077  14.137 1.00 24.44 ? 105 ASN A OD1   1 
ATOM   775  N  ND2   . ASN A 1 125 ? 41.162 12.449  12.041 1.00 29.01 ? 105 ASN A ND2   1 
ATOM   776  N  N     . SER A 1 126 ? 41.326 8.898   14.954 1.00 18.43 ? 106 SER A N     1 
ATOM   777  C  CA    . SER A 1 126 ? 41.972 8.648   16.240 1.00 18.92 ? 106 SER A CA    1 
ATOM   778  C  C     . SER A 1 126 ? 42.266 9.944   16.983 1.00 20.57 ? 106 SER A C     1 
ATOM   779  O  O     . SER A 1 126 ? 42.175 9.978   18.222 1.00 18.31 ? 106 SER A O     1 
ATOM   780  C  CB    . SER A 1 126 ? 43.269 7.852   16.057 1.00 22.10 ? 106 SER A CB    1 
ATOM   781  O  OG    . SER A 1 126 ? 44.181 8.581   15.245 1.00 23.14 ? 106 SER A OG    1 
ATOM   782  N  N     . LYS A 1 127 ? 42.597 11.023  16.258 1.00 19.00 ? 107 LYS A N     1 
ATOM   783  C  CA    . LYS A 1 127 ? 42.877 12.286  16.934 1.00 22.64 ? 107 LYS A CA    1 
ATOM   784  C  C     . LYS A 1 127 ? 41.624 12.849  17.596 1.00 20.20 ? 107 LYS A C     1 
ATOM   785  O  O     . LYS A 1 127 ? 41.683 13.364  18.717 1.00 19.54 ? 107 LYS A O     1 
ATOM   786  C  CB    . LYS A 1 127 ? 43.459 13.299  15.960 1.00 21.95 ? 107 LYS A CB    1 
ATOM   787  C  CG    . LYS A 1 127 ? 44.889 12.979  15.548 1.00 30.18 ? 107 LYS A CG    1 
ATOM   788  N  N     . LEU A 1 128 ? 40.483 12.764  16.927 1.00 17.31 ? 108 LEU A N     1 
ATOM   789  C  CA    . LEU A 1 128 ? 39.267 13.294  17.529 1.00 20.78 ? 108 LEU A CA    1 
ATOM   790  C  C     . LEU A 1 128 ? 38.781 12.398  18.664 1.00 19.25 ? 108 LEU A C     1 
ATOM   791  O  O     . LEU A 1 128 ? 38.206 12.891  19.645 1.00 19.00 ? 108 LEU A O     1 
ATOM   792  C  CB    . LEU A 1 128 ? 38.196 13.453  16.457 1.00 18.37 ? 108 LEU A CB    1 
ATOM   793  C  CG    . LEU A 1 128 ? 36.879 14.125  16.819 1.00 22.60 ? 108 LEU A CG    1 
ATOM   794  C  CD1   . LEU A 1 128 ? 37.084 15.372  17.667 1.00 31.16 ? 108 LEU A CD1   1 
ATOM   795  C  CD2   . LEU A 1 128 ? 36.195 14.484  15.516 1.00 33.02 ? 108 LEU A CD2   1 
ATOM   796  N  N     . LEU A 1 129 ? 39.031 11.090  18.576 1.00 19.00 ? 109 LEU A N     1 
ATOM   797  C  CA    . LEU A 1 129 ? 38.743 10.210  19.712 1.00 18.66 ? 109 LEU A CA    1 
ATOM   798  C  C     . LEU A 1 129 ? 39.498 10.664  20.965 1.00 17.86 ? 109 LEU A C     1 
ATOM   799  O  O     . LEU A 1 129 ? 38.906 10.843  22.047 1.00 17.61 ? 109 LEU A O     1 
ATOM   800  C  CB    . LEU A 1 129 ? 39.116 8.768   19.336 1.00 20.16 ? 109 LEU A CB    1 
ATOM   801  C  CG    . LEU A 1 129 ? 38.995 7.721   20.442 1.00 18.36 ? 109 LEU A CG    1 
ATOM   802  C  CD1   . LEU A 1 129 ? 37.590 7.630   20.955 1.00 18.48 ? 109 LEU A CD1   1 
ATOM   803  C  CD2   . LEU A 1 129 ? 39.449 6.371   19.962 1.00 15.76 ? 109 LEU A CD2   1 
ATOM   804  N  N     . ALA A 1 130 ? 40.809 10.884  20.821 1.00 16.33 ? 110 ALA A N     1 
ATOM   805  C  CA    . ALA A 1 130 ? 41.649 11.353  21.918 1.00 20.21 ? 110 ALA A CA    1 
ATOM   806  C  C     . ALA A 1 130 ? 41.174 12.704  22.447 1.00 18.89 ? 110 ALA A C     1 
ATOM   807  O  O     . ALA A 1 130 ? 41.083 12.914  23.668 1.00 17.03 ? 110 ALA A O     1 
ATOM   808  C  CB    . ALA A 1 130 ? 43.099 11.442  21.438 1.00 18.34 ? 110 ALA A CB    1 
ATOM   809  N  N     . GLU A 1 131 ? 40.877 13.641  21.539 1.00 16.83 ? 111 GLU A N     1 
ATOM   810  C  CA    . GLU A 1 131 ? 40.389 14.943  21.976 1.00 18.39 ? 111 GLU A CA    1 
ATOM   811  C  C     . GLU A 1 131 ? 39.071 14.818  22.743 1.00 17.22 ? 111 GLU A C     1 
ATOM   812  O  O     . GLU A 1 131 ? 38.809 15.604  23.663 1.00 18.27 ? 111 GLU A O     1 
ATOM   813  C  CB    . GLU A 1 131 ? 40.238 15.856  20.759 1.00 20.67 ? 111 GLU A CB    1 
ATOM   814  C  CG    . GLU A 1 131 ? 39.632 17.229  21.036 1.00 30.25 ? 111 GLU A CG    1 
ATOM   815  C  CD    . GLU A 1 131 ? 39.257 17.969  19.736 1.00 44.22 ? 111 GLU A CD    1 
ATOM   816  O  OE1   . GLU A 1 131 ? 40.168 18.274  18.916 1.00 42.70 ? 111 GLU A OE1   1 
ATOM   817  O  OE2   . GLU A 1 131 ? 38.050 18.207  19.521 1.00 30.44 ? 111 GLU A OE2   1 
ATOM   818  N  N     . SER A 1 132 ? 38.254 13.812  22.412 1.00 16.21 ? 112 SER A N     1 
ATOM   819  C  CA    . SER A 1 132 ? 36.972 13.605  23.085 1.00 18.39 ? 112 SER A CA    1 
ATOM   820  C  C     . SER A 1 132 ? 37.146 13.005  24.477 1.00 16.98 ? 112 SER A C     1 
ATOM   821  O  O     . SER A 1 132 ? 36.408 13.382  25.408 1.00 16.79 ? 112 SER A O     1 
ATOM   822  C  CB    . SER A 1 132 ? 36.072 12.724  22.223 1.00 19.70 ? 112 SER A CB    1 
ATOM   823  O  OG    . SER A 1 132 ? 35.823 13.384  20.988 1.00 20.00 ? 112 SER A OG    1 
ATOM   824  N  N     . PHE A 1 133 ? 38.121 12.107  24.661 1.00 17.84 ? 113 PHE A N     1 
ATOM   825  C  CA    . PHE A 1 133 ? 38.443 11.678  26.023 1.00 15.65 ? 113 PHE A CA    1 
ATOM   826  C  C     . PHE A 1 133 ? 38.859 12.883  26.862 1.00 19.59 ? 113 PHE A C     1 
ATOM   827  O  O     . PHE A 1 133 ? 38.391 13.064  27.999 1.00 16.36 ? 113 PHE A O     1 
ATOM   828  C  CB    . PHE A 1 133 ? 39.549 10.625  26.025 1.00 15.13 ? 113 PHE A CB    1 
ATOM   829  C  CG    . PHE A 1 133 ? 39.087 9.232   25.628 1.00 17.12 ? 113 PHE A CG    1 
ATOM   830  C  CD1   . PHE A 1 133 ? 38.148 8.561   26.395 1.00 21.11 ? 113 PHE A CD1   1 
ATOM   831  C  CD2   . PHE A 1 133 ? 39.595 8.607   24.499 1.00 20.49 ? 113 PHE A CD2   1 
ATOM   832  C  CE1   . PHE A 1 133 ? 37.728 7.289   26.046 1.00 25.93 ? 113 PHE A CE1   1 
ATOM   833  C  CE2   . PHE A 1 133 ? 39.181 7.333   24.142 1.00 15.49 ? 113 PHE A CE2   1 
ATOM   834  C  CZ    . PHE A 1 133 ? 38.248 6.675   24.910 1.00 20.13 ? 113 PHE A CZ    1 
ATOM   835  N  N     . GLN A 1 134 ? 39.712 13.745  26.300 1.00 16.62 ? 114 GLN A N     1 
ATOM   836  C  CA    . GLN A 1 134 ? 40.148 14.938  27.029 1.00 18.94 ? 114 GLN A CA    1 
ATOM   837  C  C     . GLN A 1 134 ? 38.970 15.854  27.356 1.00 18.17 ? 114 GLN A C     1 
ATOM   838  O  O     . GLN A 1 134 ? 38.863 16.363  28.481 1.00 17.98 ? 114 GLN A O     1 
ATOM   839  C  CB    . GLN A 1 134 ? 41.218 15.698  26.231 1.00 19.77 ? 114 GLN A CB    1 
ATOM   840  C  CG    . GLN A 1 134 ? 41.678 17.012  26.893 1.00 24.26 ? 114 GLN A CG    1 
ATOM   841  C  CD    . GLN A 1 134 ? 42.191 16.809  28.319 1.00 36.29 ? 114 GLN A CD    1 
ATOM   842  O  OE1   . GLN A 1 134 ? 41.936 17.624  29.220 1.00 49.03 ? 114 GLN A OE1   1 
ATOM   843  N  NE2   . GLN A 1 134 ? 42.897 15.703  28.538 1.00 43.97 ? 114 GLN A NE2   1 
ATOM   844  N  N     . ALA A 1 135 ? 38.058 16.069  26.397 1.00 16.02 ? 115 ALA A N     1 
ATOM   845  C  CA    . ALA A 1 135 ? 36.903 16.934  26.667 1.00 18.13 ? 115 ALA A CA    1 
ATOM   846  C  C     . ALA A 1 135 ? 36.032 16.369  27.791 1.00 17.57 ? 115 ALA A C     1 
ATOM   847  O  O     . ALA A 1 135 ? 35.500 17.128  28.623 1.00 17.69 ? 115 ALA A O     1 
ATOM   848  C  CB    . ALA A 1 135 ? 36.089 17.132  25.391 1.00 17.94 ? 115 ALA A CB    1 
ATOM   849  N  N     . GLY A 1 136 ? 35.933 15.042  27.878 1.00 16.87 ? 116 GLY A N     1 
ATOM   850  C  CA    . GLY A 1 136 ? 35.172 14.433  28.954 1.00 16.59 ? 116 GLY A CA    1 
ATOM   851  C  C     . GLY A 1 136 ? 35.818 14.639  30.305 1.00 16.90 ? 116 GLY A C     1 
ATOM   852  O  O     . GLY A 1 136 ? 35.130 14.897  31.295 1.00 16.22 ? 116 GLY A O     1 
ATOM   853  N  N     . VAL A 1 137 ? 37.147 14.545  30.358 1.00 15.28 ? 117 VAL A N     1 
ATOM   854  C  CA    . VAL A 1 137 ? 37.879 14.802  31.587 1.00 15.14 ? 117 VAL A CA    1 
ATOM   855  C  C     . VAL A 1 137 ? 37.619 16.221  32.066 1.00 14.41 ? 117 VAL A C     1 
ATOM   856  O  O     . VAL A 1 137 ? 37.372 16.450  33.254 1.00 15.63 ? 117 VAL A O     1 
ATOM   857  C  CB    . VAL A 1 137 ? 39.386 14.556  31.370 1.00 20.58 ? 117 VAL A CB    1 
ATOM   858  C  CG1   . VAL A 1 137 ? 40.188 15.064  32.561 1.00 22.16 ? 117 VAL A CG1   1 
ATOM   859  C  CG2   . VAL A 1 137 ? 39.651 13.081  31.127 1.00 17.76 ? 117 VAL A CG2   1 
ATOM   860  N  N     . GLU A 1 138 ? 37.670 17.195  31.156 1.00 14.05 ? 118 GLU A N     1 
ATOM   861  C  CA    . GLU A 1 138 ? 37.417 18.583  31.546 1.00 18.24 ? 118 GLU A CA    1 
ATOM   862  C  C     . GLU A 1 138 ? 36.001 18.755  32.089 1.00 17.15 ? 118 GLU A C     1 
ATOM   863  O  O     . GLU A 1 138 ? 35.793 19.423  33.111 1.00 18.41 ? 118 GLU A O     1 
ATOM   864  C  CB    . GLU A 1 138 ? 37.634 19.527  30.364 1.00 19.63 ? 118 GLU A CB    1 
ATOM   865  C  CG    . GLU A 1 138 ? 39.047 19.529  29.825 1.00 25.82 ? 118 GLU A CG    1 
ATOM   866  C  CD    . GLU A 1 138 ? 40.013 20.201  30.780 1.00 48.70 ? 118 GLU A CD    1 
ATOM   867  O  OE1   . GLU A 1 138 ? 39.627 21.230  31.385 1.00 46.69 ? 118 GLU A OE1   1 
ATOM   868  O  OE2   . GLU A 1 138 ? 41.148 19.694  30.935 1.00 58.47 ? 118 GLU A OE2   1 
ATOM   869  N  N     . THR A 1 139 ? 35.018 18.152  31.427 1.00 16.38 ? 119 THR A N     1 
ATOM   870  C  CA    . THR A 1 139 ? 33.645 18.253  31.911 1.00 17.68 ? 119 THR A CA    1 
ATOM   871  C  C     . THR A 1 139 ? 33.504 17.637  33.297 1.00 19.24 ? 119 THR A C     1 
ATOM   872  O  O     . THR A 1 139 ? 32.901 18.237  34.208 1.00 17.21 ? 119 THR A O     1 
ATOM   873  C  CB    . THR A 1 139 ? 32.690 17.576  30.915 1.00 18.15 ? 119 THR A CB    1 
ATOM   874  O  OG1   . THR A 1 139 ? 32.762 18.235  29.640 1.00 18.75 ? 119 THR A OG1   1 
ATOM   875  C  CG2   . THR A 1 139 ? 31.267 17.621  31.427 1.00 15.83 ? 119 THR A CG2   1 
ATOM   876  N  N     . ALA A 1 140 ? 34.064 16.440  33.494 1.00 16.18 ? 120 ALA A N     1 
ATOM   877  C  CA    . ALA A 1 140 ? 33.888 15.773  34.783 1.00 14.40 ? 120 ALA A CA    1 
ATOM   878  C  C     . ALA A 1 140 ? 34.579 16.520  35.922 1.00 15.65 ? 120 ALA A C     1 
ATOM   879  O  O     . ALA A 1 140 ? 34.018 16.604  37.026 1.00 15.11 ? 120 ALA A O     1 
ATOM   880  C  CB    . ALA A 1 140 ? 34.363 14.331  34.722 1.00 16.62 ? 120 ALA A CB    1 
ATOM   881  N  N     . TYR A 1 141 ? 35.787 17.050  35.695 1.00 17.20 ? 121 TYR A N     1 
ATOM   882  C  CA    . TYR A 1 141 ? 36.453 17.815  36.745 1.00 18.05 ? 121 TYR A CA    1 
ATOM   883  C  C     . TYR A 1 141 ? 35.659 19.070  37.098 1.00 18.25 ? 121 TYR A C     1 
ATOM   884  O  O     . TYR A 1 141 ? 35.606 19.461  38.262 1.00 19.16 ? 121 TYR A O     1 
ATOM   885  C  CB    . TYR A 1 141 ? 37.867 18.213  36.328 1.00 17.23 ? 121 TYR A CB    1 
ATOM   886  C  CG    . TYR A 1 141 ? 38.961 17.256  36.782 1.00 17.68 ? 121 TYR A CG    1 
ATOM   887  C  CD1   . TYR A 1 141 ? 39.673 17.476  37.953 1.00 21.86 ? 121 TYR A CD1   1 
ATOM   888  C  CD2   . TYR A 1 141 ? 39.263 16.126  36.047 1.00 16.74 ? 121 TYR A CD2   1 
ATOM   889  C  CE1   . TYR A 1 141 ? 40.674 16.586  38.376 1.00 22.83 ? 121 TYR A CE1   1 
ATOM   890  C  CE2   . TYR A 1 141 ? 40.246 15.234  36.467 1.00 19.25 ? 121 TYR A CE2   1 
ATOM   891  C  CZ    . TYR A 1 141 ? 40.949 15.478  37.611 1.00 20.29 ? 121 TYR A CZ    1 
ATOM   892  O  OH    . TYR A 1 141 ? 41.925 14.585  37.971 1.00 19.75 ? 121 TYR A OH    1 
ATOM   893  N  N     . LYS A 1 142 ? 35.075 19.736  36.105 1.00 16.68 ? 122 LYS A N     1 
ATOM   894  C  CA    . LYS A 1 142 ? 34.277 20.932  36.396 1.00 18.73 ? 122 LYS A CA    1 
ATOM   895  C  C     . LYS A 1 142 ? 33.002 20.590  37.150 1.00 18.48 ? 122 LYS A C     1 
ATOM   896  O  O     . LYS A 1 142 ? 32.494 21.423  37.907 1.00 21.08 ? 122 LYS A O     1 
ATOM   897  C  CB    . LYS A 1 142 ? 33.913 21.666  35.109 1.00 18.87 ? 122 LYS A CB    1 
ATOM   898  C  CG    . LYS A 1 142 ? 35.088 22.385  34.442 1.00 24.70 ? 122 LYS A CG    1 
ATOM   899  C  CD    . LYS A 1 142 ? 34.629 23.019  33.120 1.00 30.27 ? 122 LYS A CD    1 
ATOM   900  C  CE    . LYS A 1 142 ? 35.779 23.529  32.290 1.00 39.45 ? 122 LYS A CE    1 
ATOM   901  N  NZ    . LYS A 1 142 ? 35.470 23.318  30.845 1.00 42.24 ? 122 LYS A NZ    1 
ATOM   902  N  N     . ALA A 1 143 ? 32.465 19.385  36.947 1.00 17.45 ? 123 ALA A N     1 
ATOM   903  C  CA    . ALA A 1 143 ? 31.208 18.996  37.575 1.00 17.34 ? 123 ALA A CA    1 
ATOM   904  C  C     . ALA A 1 143 ? 31.381 18.615  39.042 1.00 19.87 ? 123 ALA A C     1 
ATOM   905  O  O     . ALA A 1 143 ? 30.418 18.683  39.813 1.00 16.41 ? 123 ALA A O     1 
ATOM   906  C  CB    . ALA A 1 143 ? 30.585 17.824  36.812 1.00 21.27 ? 123 ALA A CB    1 
ATOM   907  N  N     . VAL A 1 144 ? 32.567 18.180  39.429 1.00 17.80 ? 124 VAL A N     1 
ATOM   908  C  CA    . VAL A 1 144 ? 32.854 17.789  40.814 1.00 18.04 ? 124 VAL A CA    1 
ATOM   909  C  C     . VAL A 1 144 ? 33.336 19.012  41.583 1.00 17.64 ? 124 VAL A C     1 
ATOM   910  O  O     . VAL A 1 144 ? 34.329 19.641  41.220 1.00 19.77 ? 124 VAL A O     1 
ATOM   911  C  CB    . VAL A 1 144 ? 33.892 16.663  40.873 1.00 16.46 ? 124 VAL A CB    1 
ATOM   912  C  CG1   . VAL A 1 144 ? 34.252 16.353  42.320 1.00 16.53 ? 124 VAL A CG1   1 
ATOM   913  C  CG2   . VAL A 1 144 ? 33.344 15.437  40.156 1.00 17.05 ? 124 VAL A CG2   1 
ATOM   914  N  N     . MET A 1 145 ? 32.640 19.342  42.672 1.00 15.94 ? 125 MET A N     1 
ATOM   915  C  CA    . MET A 1 145 ? 32.956 20.590  43.348 1.00 20.94 ? 125 MET A CA    1 
ATOM   916  C  C     . MET A 1 145 ? 34.341 20.558  43.967 1.00 20.85 ? 125 MET A C     1 
ATOM   917  O  O     . MET A 1 145 ? 35.059 21.563  43.926 1.00 21.24 ? 125 MET A O     1 
ATOM   918  C  CB    . MET A 1 145 ? 31.898 20.893  44.411 1.00 22.40 ? 125 MET A CB    1 
ATOM   919  C  CG    . MET A 1 145 ? 30.657 21.497  43.793 1.00 20.54 ? 125 MET A CG    1 
ATOM   920  S  SD    . MET A 1 145 ? 29.390 21.960  44.990 1.00 23.21 ? 125 MET A SD    1 
ATOM   921  C  CE    . MET A 1 145 ? 28.928 20.385  45.659 1.00 26.38 ? 125 MET A CE    1 
ATOM   922  N  N     . LYS A 1 146 ? 34.724 19.431  44.571 1.00 20.38 ? 126 LYS A N     1 
ATOM   923  C  CA    . LYS A 1 146 ? 36.043 19.257  45.192 1.00 21.43 ? 126 LYS A CA    1 
ATOM   924  C  C     . LYS A 1 146 ? 36.651 17.944  44.713 1.00 17.51 ? 126 LYS A C     1 
ATOM   925  O  O     . LYS A 1 146 ? 36.574 16.909  45.385 1.00 21.44 ? 126 LYS A O     1 
ATOM   926  C  CB    . LYS A 1 146 ? 35.944 19.325  46.711 1.00 25.01 ? 126 LYS A CB    1 
ATOM   927  C  CG    . LYS A 1 146 ? 35.565 20.741  47.227 1.00 25.22 ? 126 LYS A CG    1 
ATOM   928  C  CD    . LYS A 1 146 ? 35.667 20.838  48.751 1.00 32.65 ? 126 LYS A CD    1 
ATOM   929  C  CE    . LYS A 1 146 ? 34.721 21.884  49.340 1.00 48.97 ? 126 LYS A CE    1 
ATOM   930  N  NZ    . LYS A 1 146 ? 35.149 23.277  49.055 1.00 55.29 ? 126 LYS A NZ    1 
ATOM   931  N  N     . PRO A 1 147 ? 37.252 17.960  43.536 1.00 22.65 ? 127 PRO A N     1 
ATOM   932  C  CA    . PRO A 1 147 ? 37.914 16.756  43.018 1.00 21.99 ? 127 PRO A CA    1 
ATOM   933  C  C     . PRO A 1 147 ? 39.044 16.286  43.926 1.00 25.57 ? 127 PRO A C     1 
ATOM   934  O  O     . PRO A 1 147 ? 39.834 17.084  44.436 1.00 22.28 ? 127 PRO A O     1 
ATOM   935  C  CB    . PRO A 1 147 ? 38.451 17.214  41.661 1.00 22.48 ? 127 PRO A CB    1 
ATOM   936  C  CG    . PRO A 1 147 ? 37.698 18.426  41.307 1.00 21.86 ? 127 PRO A CG    1 
ATOM   937  C  CD    . PRO A 1 147 ? 37.314 19.089  42.595 1.00 23.75 ? 127 PRO A CD    1 
ATOM   938  N  N     . VAL A 1 148 ? 39.127 14.972  44.096 1.00 17.42 ? 128 VAL A N     1 
ATOM   939  C  CA    . VAL A 1 148 ? 40.160 14.306  44.871 1.00 18.07 ? 128 VAL A CA    1 
ATOM   940  C  C     . VAL A 1 148 ? 40.959 13.402  43.940 1.00 19.45 ? 128 VAL A C     1 
ATOM   941  O  O     . VAL A 1 148 ? 40.386 12.722  43.085 1.00 19.07 ? 128 VAL A O     1 
ATOM   942  C  CB    . VAL A 1 148 ? 39.498 13.521  46.017 1.00 20.90 ? 128 VAL A CB    1 
ATOM   943  C  CG1   . VAL A 1 148 ? 40.475 12.587  46.701 1.00 24.64 ? 128 VAL A CG1   1 
ATOM   944  C  CG2   . VAL A 1 148 ? 38.905 14.517  47.011 1.00 24.12 ? 128 VAL A CG2   1 
ATOM   945  N  N     . GLU A 1 149 ? 42.279 13.400  44.085 1.00 18.75 ? 129 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 149 ? 43.113 12.553  43.238 1.00 17.91 ? 129 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 149 ? 43.224 11.131  43.807 1.00 16.26 ? 129 GLU A C     1 
ATOM   948  O  O     . GLU A 1 149 ? 43.037 10.888  45.006 1.00 18.94 ? 129 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 149 ? 44.499 13.184  43.077 1.00 20.94 ? 129 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 149 ? 44.493 14.502  42.323 1.00 20.42 ? 129 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 149 ? 44.039 14.355  40.853 1.00 23.48 ? 129 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 149 ? 44.469 13.405  40.159 1.00 23.96 ? 129 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 149 ? 43.230 15.192  40.396 1.00 24.99 ? 129 GLU A OE2   1 
ATOM   954  N  N     . GLY A 1 150 ? 43.585 10.189  42.929 1.00 15.69 ? 130 GLY A N     1 
ATOM   955  C  CA    . GLY A 1 150 ? 43.569 8.782   43.274 1.00 15.87 ? 130 GLY A CA    1 
ATOM   956  C  C     . GLY A 1 150 ? 42.259 8.111   42.956 1.00 16.74 ? 130 GLY A C     1 
ATOM   957  O  O     . GLY A 1 150 ? 41.960 7.054   43.522 1.00 16.63 ? 130 GLY A O     1 
ATOM   958  N  N     . THR A 1 151 ? 41.482 8.690   42.047 1.00 15.79 ? 131 THR A N     1 
ATOM   959  C  CA    . THR A 1 151 ? 40.095 8.336   41.794 1.00 17.54 ? 131 THR A CA    1 
ATOM   960  C  C     . THR A 1 151 ? 39.842 8.060   40.317 1.00 13.53 ? 131 THR A C     1 
ATOM   961  O  O     . THR A 1 151 ? 40.770 8.088   39.504 1.00 16.86 ? 131 THR A O     1 
ATOM   962  C  CB    . THR A 1 151 ? 39.190 9.480   42.239 1.00 17.00 ? 131 THR A CB    1 
ATOM   963  O  OG1   . THR A 1 151 ? 39.513 10.667  41.476 1.00 17.25 ? 131 THR A OG1   1 
ATOM   964  C  CG2   . THR A 1 151 ? 39.353 9.738   43.724 1.00 17.49 ? 131 THR A CG2   1 
ATOM   965  N  N     . ILE A 1 152 ? 38.560 7.889   39.977 1.00 15.35 ? 132 ILE A N     1 
ATOM   966  C  CA    . ILE A 1 152 ? 38.127 7.758   38.588 1.00 13.42 ? 132 ILE A CA    1 
ATOM   967  C  C     . ILE A 1 152 ? 38.552 8.982   37.784 1.00 14.20 ? 132 ILE A C     1 
ATOM   968  O  O     . ILE A 1 152 ? 38.885 8.865   36.594 1.00 15.05 ? 132 ILE A O     1 
ATOM   969  C  CB    . ILE A 1 152 ? 36.599 7.513   38.540 1.00 14.13 ? 132 ILE A CB    1 
ATOM   970  C  CG1   . ILE A 1 152 ? 36.120 7.192   37.115 1.00 16.26 ? 132 ILE A CG1   1 
ATOM   971  C  CG2   . ILE A 1 152 ? 35.850 8.718   39.122 1.00 14.94 ? 132 ILE A CG2   1 
ATOM   972  C  CD1   . ILE A 1 152 ? 34.644 6.831   37.005 1.00 16.06 ? 132 ILE A CD1   1 
ATOM   973  N  N     . LEU A 1 153 ? 38.558 10.173  38.399 1.00 14.06 ? 133 LEU A N     1 
ATOM   974  C  CA    . LEU A 1 153 ? 39.012 11.367  37.673 1.00 14.88 ? 133 LEU A CA    1 
ATOM   975  C  C     . LEU A 1 153 ? 40.488 11.270  37.277 1.00 15.74 ? 133 LEU A C     1 
ATOM   976  O  O     . LEU A 1 153 ? 40.865 11.633  36.157 1.00 14.78 ? 133 LEU A O     1 
ATOM   977  C  CB    . LEU A 1 153 ? 38.791 12.623  38.520 1.00 15.26 ? 133 LEU A CB    1 
ATOM   978  C  CG    . LEU A 1 153 ? 37.344 13.052  38.769 1.00 14.10 ? 133 LEU A CG    1 
ATOM   979  C  CD1   . LEU A 1 153 ? 37.318 14.327  39.573 1.00 17.74 ? 133 LEU A CD1   1 
ATOM   980  C  CD2   . LEU A 1 153 ? 36.624 13.254  37.462 1.00 18.63 ? 133 LEU A CD2   1 
ATOM   981  N  N     . THR A 1 154 ? 41.333 10.822  38.196 1.00 13.69 ? 134 THR A N     1 
ATOM   982  C  CA    . THR A 1 154 ? 42.762 10.643  37.925 1.00 14.15 ? 134 THR A CA    1 
ATOM   983  C  C     . THR A 1 154 ? 42.992 9.648   36.792 1.00 15.39 ? 134 THR A C     1 
ATOM   984  O  O     . THR A 1 154 ? 43.793 9.892   35.876 1.00 16.67 ? 134 THR A O     1 
ATOM   985  C  CB    . THR A 1 154 ? 43.470 10.143  39.191 1.00 17.85 ? 134 THR A CB    1 
ATOM   986  O  OG1   . THR A 1 154 ? 43.213 11.035  40.293 1.00 18.06 ? 134 THR A OG1   1 
ATOM   987  C  CG2   . THR A 1 154 ? 45.007 9.983   38.973 1.00 20.10 ? 134 THR A CG2   1 
ATOM   988  N  N     . VAL A 1 155 ? 42.319 8.500   36.858 1.00 15.87 ? 135 VAL A N     1 
ATOM   989  C  CA    . VAL A 1 155 ? 42.478 7.487   35.823 1.00 18.57 ? 135 VAL A CA    1 
ATOM   990  C  C     . VAL A 1 155 ? 42.020 8.052   34.481 1.00 16.52 ? 135 VAL A C     1 
ATOM   991  O  O     . VAL A 1 155 ? 42.720 7.944   33.469 1.00 16.13 ? 135 VAL A O     1 
ATOM   992  C  CB    . VAL A 1 155 ? 41.718 6.210   36.223 1.00 15.26 ? 135 VAL A CB    1 
ATOM   993  C  CG1   . VAL A 1 155 ? 41.727 5.185   35.097 1.00 18.03 ? 135 VAL A CG1   1 
ATOM   994  C  CG2   . VAL A 1 155 ? 42.315 5.628   37.534 1.00 17.59 ? 135 VAL A CG2   1 
ATOM   995  N  N     . ALA A 1 156 ? 40.856 8.702   34.460 1.00 13.86 ? 136 ALA A N     1 
ATOM   996  C  CA    . ALA A 1 156 ? 40.368 9.287   33.206 1.00 16.30 ? 136 ALA A CA    1 
ATOM   997  C  C     . ALA A 1 156 ? 41.338 10.336  32.661 1.00 17.46 ? 136 ALA A C     1 
ATOM   998  O  O     . ALA A 1 156 ? 41.570 10.413  31.446 1.00 15.93 ? 136 ALA A O     1 
ATOM   999  C  CB    . ALA A 1 156 ? 38.990 9.897   33.427 1.00 17.01 ? 136 ALA A CB    1 
ATOM   1000 N  N     . LYS A 1 157 ? 41.906 11.156  33.549 1.00 16.06 ? 137 LYS A N     1 
ATOM   1001 C  CA    . LYS A 1 157 ? 42.842 12.201  33.139 1.00 17.74 ? 137 LYS A CA    1 
ATOM   1002 C  C     . LYS A 1 157 ? 44.108 11.601  32.518 1.00 18.33 ? 137 LYS A C     1 
ATOM   1003 O  O     . LYS A 1 157 ? 44.554 12.029  31.440 1.00 15.69 ? 137 LYS A O     1 
ATOM   1004 C  CB    . LYS A 1 157 ? 43.199 13.079  34.352 1.00 17.67 ? 137 LYS A CB    1 
ATOM   1005 C  CG    . LYS A 1 157 ? 44.268 14.138  34.083 1.00 22.94 ? 137 LYS A CG    1 
ATOM   1006 C  CD    . LYS A 1 157 ? 44.647 14.869  35.412 1.00 25.42 ? 137 LYS A CD    1 
ATOM   1007 C  CE    . LYS A 1 157 ? 45.360 13.943  36.434 1.00 28.88 ? 137 LYS A CE    1 
ATOM   1008 N  NZ    . LYS A 1 157 ? 45.185 14.476  37.820 1.00 37.54 ? 137 LYS A NZ    1 
ATOM   1009 N  N     . ASP A 1 158 ? 44.710 10.617  33.199 1.00 15.88 ? 138 ASP A N     1 
ATOM   1010 C  CA    . ASP A 1 158 ? 45.919 9.971   32.688 1.00 18.40 ? 138 ASP A CA    1 
ATOM   1011 C  C     . ASP A 1 158 ? 45.642 9.209   31.384 1.00 19.10 ? 138 ASP A C     1 
ATOM   1012 O  O     . ASP A 1 158 ? 46.479 9.208   30.469 1.00 18.12 ? 138 ASP A O     1 
ATOM   1013 C  CB    . ASP A 1 158 ? 46.511 9.059   33.773 1.00 17.00 ? 138 ASP A CB    1 
ATOM   1014 C  CG    . ASP A 1 158 ? 47.042 9.854   34.973 1.00 23.11 ? 138 ASP A CG    1 
ATOM   1015 O  OD1   . ASP A 1 158 ? 47.396 11.035  34.774 1.00 25.54 ? 138 ASP A OD1   1 
ATOM   1016 O  OD2   . ASP A 1 158 ? 47.111 9.314   36.105 1.00 19.94 ? 138 ASP A OD2   1 
ATOM   1017 N  N     . ALA A 1 159 ? 44.471 8.579   31.266 1.00 15.90 ? 139 ALA A N     1 
ATOM   1018 C  CA    . ALA A 1 159 ? 44.111 7.914   30.015 1.00 16.24 ? 139 ALA A CA    1 
ATOM   1019 C  C     . ALA A 1 159 ? 44.013 8.919   28.871 1.00 18.28 ? 139 ALA A C     1 
ATOM   1020 O  O     . ALA A 1 159 ? 44.437 8.649   27.730 1.00 15.54 ? 139 ALA A O     1 
ATOM   1021 C  CB    . ALA A 1 159 ? 42.786 7.173   30.195 1.00 19.28 ? 139 ALA A CB    1 
ATOM   1022 N  N     . ALA A 1 160 ? 43.436 10.083  29.148 1.00 16.77 ? 140 ALA A N     1 
ATOM   1023 C  CA    . ALA A 1 160 ? 43.237 11.064  28.098 1.00 18.18 ? 140 ALA A CA    1 
ATOM   1024 C  C     . ALA A 1 160 ? 44.565 11.675  27.677 1.00 18.60 ? 140 ALA A C     1 
ATOM   1025 O  O     . ALA A 1 160 ? 44.791 11.938  26.491 1.00 19.20 ? 140 ALA A O     1 
ATOM   1026 C  CB    . ALA A 1 160 ? 42.249 12.137  28.557 1.00 19.09 ? 140 ALA A CB    1 
ATOM   1027 N  N     . GLN A 1 161 ? 45.459 11.913  28.637 1.00 17.00 ? 141 GLN A N     1 
ATOM   1028 C  CA    . GLN A 1 161 ? 46.776 12.429  28.300 1.00 18.18 ? 141 GLN A CA    1 
ATOM   1029 C  C     . GLN A 1 161 ? 47.538 11.422  27.444 1.00 18.54 ? 141 GLN A C     1 
ATOM   1030 O  O     . GLN A 1 161 ? 48.168 11.788  26.436 1.00 19.45 ? 141 GLN A O     1 
ATOM   1031 C  CB    . GLN A 1 161 ? 47.526 12.774  29.589 1.00 19.65 ? 141 GLN A CB    1 
ATOM   1032 C  CG    . GLN A 1 161 ? 48.916 13.385  29.355 1.00 25.54 ? 141 GLN A CG    1 
ATOM   1033 C  CD    . GLN A 1 161 ? 48.826 14.716  28.639 1.00 38.96 ? 141 GLN A CD    1 
ATOM   1034 O  OE1   . GLN A 1 161 ? 48.047 15.594  29.029 1.00 43.81 ? 141 GLN A OE1   1 
ATOM   1035 N  NE2   . GLN A 1 161 ? 49.590 14.858  27.558 1.00 40.75 ? 141 GLN A NE2   1 
ATOM   1036 N  N     . ALA A 1 162 ? 47.444 10.142  27.789 1.00 16.41 ? 142 ALA A N     1 
ATOM   1037 C  CA    . ALA A 1 162 ? 48.019 9.101   26.950 1.00 17.73 ? 142 ALA A CA    1 
ATOM   1038 C  C     . ALA A 1 162 ? 47.391 9.111   25.562 1.00 17.21 ? 142 ALA A C     1 
ATOM   1039 O  O     . ALA A 1 162 ? 48.090 8.947   24.550 1.00 19.36 ? 142 ALA A O     1 
ATOM   1040 C  CB    . ALA A 1 162 ? 47.830 7.744   27.616 1.00 17.39 ? 142 ALA A CB    1 
ATOM   1041 N  N     . ALA A 1 163 ? 46.071 9.318   25.484 1.00 16.50 ? 143 ALA A N     1 
ATOM   1042 C  CA    . ALA A 1 163 ? 45.399 9.279   24.193 1.00 17.27 ? 143 ALA A CA    1 
ATOM   1043 C  C     . ALA A 1 163 ? 45.918 10.385  23.282 1.00 18.58 ? 143 ALA A C     1 
ATOM   1044 O  O     . ALA A 1 163 ? 46.203 10.158  22.098 1.00 18.91 ? 143 ALA A O     1 
ATOM   1045 C  CB    . ALA A 1 163 ? 43.879 9.417   24.360 1.00 17.94 ? 143 ALA A CB    1 
ATOM   1046 N  N     . ILE A 1 164 ? 46.019 11.596  23.824 1.00 16.67 ? 144 ILE A N     1 
ATOM   1047 C  CA    . ILE A 1 164 ? 46.479 12.731  23.046 1.00 17.71 ? 144 ILE A CA    1 
ATOM   1048 C  C     . ILE A 1 164 ? 47.886 12.478  22.524 1.00 21.42 ? 144 ILE A C     1 
ATOM   1049 O  O     . ILE A 1 164 ? 48.168 12.704  21.344 1.00 21.05 ? 144 ILE A O     1 
ATOM   1050 C  CB    . ILE A 1 164 ? 46.382 14.014  23.885 1.00 21.43 ? 144 ILE A CB    1 
ATOM   1051 C  CG1   . ILE A 1 164 ? 44.911 14.365  24.128 1.00 22.42 ? 144 ILE A CG1   1 
ATOM   1052 C  CG2   . ILE A 1 164 ? 47.149 15.176  23.219 1.00 27.67 ? 144 ILE A CG2   1 
ATOM   1053 C  CD1   . ILE A 1 164 ? 44.121 14.846  22.888 1.00 29.04 ? 144 ILE A CD1   1 
ATOM   1054 N  N     . GLU A 1 165 ? 48.774 11.964  23.373 1.00 18.93 ? 145 GLU A N     1 
ATOM   1055 C  CA    . GLU A 1 165 ? 50.162 11.775  22.956 1.00 18.58 ? 145 GLU A CA    1 
ATOM   1056 C  C     . GLU A 1 165 ? 50.272 10.702  21.875 1.00 23.87 ? 145 GLU A C     1 
ATOM   1057 O  O     . GLU A 1 165 ? 50.987 10.881  20.889 1.00 20.86 ? 145 GLU A O     1 
ATOM   1058 C  CB    . GLU A 1 165 ? 51.015 11.407  24.165 1.00 21.93 ? 145 GLU A CB    1 
ATOM   1059 C  CG    . GLU A 1 165 ? 51.286 12.582  25.100 1.00 32.43 ? 145 GLU A CG    1 
ATOM   1060 C  CD    . GLU A 1 165 ? 52.034 12.166  26.350 1.00 38.50 ? 145 GLU A CD    1 
ATOM   1061 O  OE1   . GLU A 1 165 ? 52.776 11.154  26.291 1.00 40.63 ? 145 GLU A OE1   1 
ATOM   1062 O  OE2   . GLU A 1 165 ? 51.873 12.840  27.392 1.00 38.29 ? 145 GLU A OE2   1 
ATOM   1063 N  N     . LYS A 1 166 ? 49.573 9.583   22.054 1.00 19.13 ? 146 LYS A N     1 
ATOM   1064 C  CA    . LYS A 1 166 ? 49.669 8.469   21.125 1.00 22.24 ? 146 LYS A CA    1 
ATOM   1065 C  C     . LYS A 1 166 ? 49.012 8.802   19.791 1.00 22.14 ? 146 LYS A C     1 
ATOM   1066 O  O     . LYS A 1 166 ? 49.549 8.466   18.734 1.00 24.82 ? 146 LYS A O     1 
ATOM   1067 C  CB    . LYS A 1 166 ? 49.023 7.239   21.757 1.00 18.36 ? 146 LYS A CB    1 
ATOM   1068 C  CG    . LYS A 1 166 ? 49.129 5.947   20.962 1.00 21.77 ? 146 LYS A CG    1 
ATOM   1069 C  CD    . LYS A 1 166 ? 50.564 5.436   20.856 1.00 27.75 ? 146 LYS A CD    1 
ATOM   1070 C  CE    . LYS A 1 166 ? 50.623 4.159   20.040 1.00 34.21 ? 146 LYS A CE    1 
ATOM   1071 N  NZ    . LYS A 1 166 ? 52.008 3.656   19.978 1.00 38.56 ? 146 LYS A NZ    1 
ATOM   1072 N  N     . ALA A 1 167 ? 47.842 9.455   19.817 1.00 20.20 ? 147 ALA A N     1 
ATOM   1073 C  CA    . ALA A 1 167 ? 47.088 9.721   18.595 1.00 23.87 ? 147 ALA A CA    1 
ATOM   1074 C  C     . ALA A 1 167 ? 47.841 10.641  17.643 1.00 26.51 ? 147 ALA A C     1 
ATOM   1075 O  O     . ALA A 1 167 ? 47.555 10.644  16.441 1.00 23.05 ? 147 ALA A O     1 
ATOM   1076 C  CB    . ALA A 1 167 ? 45.736 10.338  18.939 1.00 20.07 ? 147 ALA A CB    1 
ATOM   1077 N  N     . ASN A 1 168 ? 48.798 11.410  18.159 1.00 25.09 ? 148 ASN A N     1 
ATOM   1078 C  CA    . ASN A 1 168 ? 49.561 12.324  17.315 1.00 29.67 ? 148 ASN A CA    1 
ATOM   1079 C  C     . ASN A 1 168 ? 50.332 11.580  16.234 1.00 28.98 ? 148 ASN A C     1 
ATOM   1080 O  O     . ASN A 1 168 ? 50.610 12.153  15.175 1.00 34.18 ? 148 ASN A O     1 
ATOM   1081 C  CB    . ASN A 1 168 ? 50.518 13.141  18.183 1.00 30.25 ? 148 ASN A CB    1 
ATOM   1082 C  CG    . ASN A 1 168 ? 50.966 14.419  17.512 1.00 39.02 ? 148 ASN A CG    1 
ATOM   1083 O  OD1   . ASN A 1 168 ? 50.175 15.124  16.867 1.00 37.87 ? 148 ASN A OD1   1 
ATOM   1084 N  ND2   . ASN A 1 168 ? 52.244 14.719  17.643 1.00 33.42 ? 148 ASN A ND2   1 
ATOM   1085 N  N     . ASN A 1 169 ? 50.683 10.312  16.475 1.00 27.13 ? 149 ASN A N     1 
ATOM   1086 C  CA    . ASN A 1 169 ? 51.457 9.514   15.525 1.00 29.76 ? 149 ASN A CA    1 
ATOM   1087 C  C     . ASN A 1 169 ? 50.808 8.176   15.190 1.00 30.03 ? 149 ASN A C     1 
ATOM   1088 O  O     . ASN A 1 169 ? 51.468 7.318   14.594 1.00 28.89 ? 149 ASN A O     1 
ATOM   1089 C  CB    . ASN A 1 169 ? 52.856 9.248   16.086 1.00 32.11 ? 149 ASN A CB    1 
ATOM   1090 C  CG    . ASN A 1 169 ? 52.805 8.555   17.431 1.00 35.56 ? 149 ASN A CG    1 
ATOM   1091 O  OD1   . ASN A 1 169 ? 52.542 7.356   17.512 1.00 40.65 ? 149 ASN A OD1   1 
ATOM   1092 N  ND2   . ASN A 1 169 ? 53.048 9.313   18.507 1.00 44.48 ? 149 ASN A ND2   1 
ATOM   1093 N  N     . THR A 1 170 ? 49.543 7.970   15.554 1.00 26.38 ? 150 THR A N     1 
ATOM   1094 C  CA    . THR A 1 170 ? 48.895 6.661   15.471 1.00 26.93 ? 150 THR A CA    1 
ATOM   1095 C  C     . THR A 1 170 ? 47.519 6.852   14.843 1.00 25.36 ? 150 THR A C     1 
ATOM   1096 O  O     . THR A 1 170 ? 46.626 7.420   15.473 1.00 26.21 ? 150 THR A O     1 
ATOM   1097 C  CB    . THR A 1 170 ? 48.790 6.026   16.872 1.00 27.33 ? 150 THR A CB    1 
ATOM   1098 O  OG1   . THR A 1 170 ? 50.106 5.856   17.418 1.00 29.97 ? 150 THR A OG1   1 
ATOM   1099 C  CG2   . THR A 1 170 ? 48.116 4.674   16.851 1.00 22.82 ? 150 THR A CG2   1 
ATOM   1100 N  N     . GLU A 1 171 ? 47.351 6.402   13.595 1.00 25.27 ? 151 GLU A N     1 
ATOM   1101 C  CA    . GLU A 1 171 ? 46.053 6.475   12.937 1.00 20.29 ? 151 GLU A CA    1 
ATOM   1102 C  C     . GLU A 1 171 ? 45.113 5.353   13.380 1.00 20.42 ? 151 GLU A C     1 
ATOM   1103 O  O     . GLU A 1 171 ? 43.891 5.535   13.373 1.00 22.87 ? 151 GLU A O     1 
ATOM   1104 C  CB    . GLU A 1 171 ? 46.264 6.433   11.416 1.00 30.52 ? 151 GLU A CB    1 
ATOM   1105 C  CG    . GLU A 1 171 ? 45.017 6.468   10.581 1.00 29.89 ? 151 GLU A CG    1 
ATOM   1106 C  CD    . GLU A 1 171 ? 45.268 6.131   9.102  1.00 45.49 ? 151 GLU A CD    1 
ATOM   1107 O  OE1   . GLU A 1 171 ? 46.445 6.123   8.664  1.00 39.08 ? 151 GLU A OE1   1 
ATOM   1108 O  OE2   . GLU A 1 171 ? 44.277 5.863   8.384  1.00 43.46 ? 151 GLU A OE2   1 
ATOM   1109 N  N     . ASP A 1 172 ? 45.651 4.184   13.711 1.00 22.37 ? 152 ASP A N     1 
ATOM   1110 C  CA    . ASP A 1 172 ? 44.838 3.017   14.038 1.00 17.75 ? 152 ASP A CA    1 
ATOM   1111 C  C     . ASP A 1 172 ? 44.220 3.187   15.419 1.00 20.43 ? 152 ASP A C     1 
ATOM   1112 O  O     . ASP A 1 172 ? 44.943 3.246   16.412 1.00 18.98 ? 152 ASP A O     1 
ATOM   1113 C  CB    . ASP A 1 172 ? 45.695 1.764   14.013 1.00 18.79 ? 152 ASP A CB    1 
ATOM   1114 C  CG    . ASP A 1 172 ? 44.932 0.516   14.422 1.00 23.70 ? 152 ASP A CG    1 
ATOM   1115 O  OD1   . ASP A 1 172 ? 43.681 0.498   14.314 1.00 23.64 ? 152 ASP A OD1   1 
ATOM   1116 O  OD2   . ASP A 1 172 ? 45.591 -0.451  14.859 1.00 24.26 ? 152 ASP A OD2   1 
ATOM   1117 N  N     . CYS A 1 173 ? 42.896 3.225   15.483 1.00 19.02 ? 153 CYS A N     1 
ATOM   1118 C  CA    . CYS A 1 173 ? 42.225 3.346   16.775 1.00 19.92 ? 153 CYS A CA    1 
ATOM   1119 C  C     . CYS A 1 173 ? 42.368 2.105   17.650 1.00 19.85 ? 153 CYS A C     1 
ATOM   1120 O  O     . CYS A 1 173 ? 42.189 2.213   18.867 1.00 18.14 ? 153 CYS A O     1 
ATOM   1121 C  CB    . CYS A 1 173 ? 40.735 3.671   16.572 1.00 17.23 ? 153 CYS A CB    1 
ATOM   1122 S  SG    . CYS A 1 173 ? 40.407 5.262   15.795 1.00 22.47 ? 153 CYS A SG    1 
ATOM   1123 N  N     . ILE A 1 174 ? 42.655 0.929   17.090 1.00 16.59 ? 154 ILE A N     1 
ATOM   1124 C  CA    . ILE A 1 174 ? 42.896 -0.239  17.940 1.00 17.50 ? 154 ILE A CA    1 
ATOM   1125 C  C     . ILE A 1 174 ? 44.202 -0.067  18.716 1.00 19.77 ? 154 ILE A C     1 
ATOM   1126 O  O     . ILE A 1 174 ? 44.245 -0.245  19.939 1.00 21.04 ? 154 ILE A O     1 
ATOM   1127 C  CB    . ILE A 1 174 ? 42.903 -1.538  17.112 1.00 19.40 ? 154 ILE A CB    1 
ATOM   1128 C  CG1   . ILE A 1 174 ? 41.518 -1.801  16.514 1.00 22.33 ? 154 ILE A CG1   1 
ATOM   1129 C  CG2   . ILE A 1 174 ? 43.308 -2.739  17.972 1.00 22.88 ? 154 ILE A CG2   1 
ATOM   1130 C  CD1   . ILE A 1 174 ? 41.517 -2.860  15.416 1.00 25.39 ? 154 ILE A CD1   1 
ATOM   1131 N  N     . GLU A 1 175 ? 45.277 0.302   18.017 1.00 20.11 ? 155 GLU A N     1 
ATOM   1132 C  CA    . GLU A 1 175 ? 46.558 0.536   18.683 1.00 23.06 ? 155 GLU A CA    1 
ATOM   1133 C  C     . GLU A 1 175 ? 46.440 1.665   19.698 1.00 20.57 ? 155 GLU A C     1 
ATOM   1134 O  O     . GLU A 1 175 ? 47.001 1.587   20.790 1.00 19.96 ? 155 GLU A O     1 
ATOM   1135 C  CB    . GLU A 1 175 ? 47.648 0.856   17.644 1.00 23.65 ? 155 GLU A CB    1 
ATOM   1136 C  CG    . GLU A 1 175 ? 49.033 1.144   18.237 1.00 22.63 ? 155 GLU A CG    1 
ATOM   1137 C  CD    . GLU A 1 175 ? 50.096 1.405   17.192 1.00 30.66 ? 155 GLU A CD    1 
ATOM   1138 O  OE1   . GLU A 1 175 ? 49.783 1.288   15.988 1.00 29.19 ? 155 GLU A OE1   1 
ATOM   1139 O  OE2   . GLU A 1 175 ? 51.239 1.742   17.578 1.00 36.12 ? 155 GLU A OE2   1 
ATOM   1140 N  N     . LEU A 1 176 ? 45.716 2.727   19.344 1.00 17.75 ? 156 LEU A N     1 
ATOM   1141 C  CA    . LEU A 1 176 ? 45.474 3.818   20.284 1.00 17.21 ? 156 LEU A CA    1 
ATOM   1142 C  C     . LEU A 1 176 ? 44.794 3.310   21.543 1.00 21.27 ? 156 LEU A C     1 
ATOM   1143 O  O     . LEU A 1 176 ? 45.235 3.593   22.664 1.00 19.60 ? 156 LEU A O     1 
ATOM   1144 C  CB    . LEU A 1 176 ? 44.631 4.900   19.616 1.00 20.42 ? 156 LEU A CB    1 
ATOM   1145 C  CG    . LEU A 1 176 ? 44.263 6.109   20.479 1.00 17.15 ? 156 LEU A CG    1 
ATOM   1146 C  CD1   . LEU A 1 176 ? 45.528 6.764   21.009 1.00 21.88 ? 156 LEU A CD1   1 
ATOM   1147 C  CD2   . LEU A 1 176 ? 43.400 7.094   19.732 1.00 22.28 ? 156 LEU A CD2   1 
ATOM   1148 N  N     . MET A 1 177 ? 43.706 2.562   21.381 1.00 18.60 ? 157 MET A N     1 
ATOM   1149 C  CA    . MET A 1 177 ? 42.946 2.143   22.549 1.00 17.63 ? 157 MET A CA    1 
ATOM   1150 C  C     . MET A 1 177 ? 43.748 1.179   23.409 1.00 22.14 ? 157 MET A C     1 
ATOM   1151 O  O     . MET A 1 177 ? 43.632 1.193   24.639 1.00 19.57 ? 157 MET A O     1 
ATOM   1152 C  CB    . MET A 1 177 ? 41.615 1.525   22.108 1.00 19.34 ? 157 MET A CB    1 
ATOM   1153 C  CG    . MET A 1 177 ? 40.586 1.423   23.209 1.00 20.51 ? 157 MET A CG    1 
ATOM   1154 S  SD    . MET A 1 177 ? 39.958 3.056   23.703 1.00 20.31 ? 157 MET A SD    1 
ATOM   1155 C  CE    . MET A 1 177 ? 39.901 2.853   25.482 1.00 18.65 ? 157 MET A CE    1 
ATOM   1156 N  N     . GLU A 1 178 ? 44.559 0.324   22.782 1.00 19.41 ? 158 GLU A N     1 
ATOM   1157 C  CA    . GLU A 1 178 ? 45.431 -0.550  23.551 1.00 16.65 ? 158 GLU A CA    1 
ATOM   1158 C  C     . GLU A 1 178 ? 46.363 0.275   24.428 1.00 17.54 ? 158 GLU A C     1 
ATOM   1159 O  O     . GLU A 1 178 ? 46.522 -0.007  25.617 1.00 20.56 ? 158 GLU A O     1 
ATOM   1160 C  CB    . GLU A 1 178 ? 46.251 -1.467  22.632 1.00 24.74 ? 158 GLU A CB    1 
ATOM   1161 C  CG    . GLU A 1 178 ? 45.406 -2.584  21.987 1.00 31.53 ? 158 GLU A CG    1 
ATOM   1162 C  CD    . GLU A 1 178 ? 46.127 -3.346  20.869 1.00 41.87 ? 158 GLU A CD    1 
ATOM   1163 O  OE1   . GLU A 1 178 ? 47.155 -2.851  20.358 1.00 36.29 ? 158 GLU A OE1   1 
ATOM   1164 O  OE2   . GLU A 1 178 ? 45.646 -4.443  20.500 1.00 44.78 ? 158 GLU A OE2   1 
ATOM   1165 N  N     . TYR A 1 179 ? 46.963 1.321   23.857 1.00 17.88 ? 159 TYR A N     1 
ATOM   1166 C  CA    . TYR A 1 179 ? 47.875 2.171   24.622 1.00 21.26 ? 159 TYR A CA    1 
ATOM   1167 C  C     . TYR A 1 179 ? 47.131 2.904   25.733 1.00 19.35 ? 159 TYR A C     1 
ATOM   1168 O  O     . TYR A 1 179 ? 47.610 2.993   26.872 1.00 17.01 ? 159 TYR A O     1 
ATOM   1169 C  CB    . TYR A 1 179 ? 48.546 3.171   23.682 1.00 18.20 ? 159 TYR A CB    1 
ATOM   1170 C  CG    . TYR A 1 179 ? 49.583 4.055   24.342 1.00 21.40 ? 159 TYR A CG    1 
ATOM   1171 C  CD1   . TYR A 1 179 ? 50.833 3.548   24.675 1.00 24.00 ? 159 TYR A CD1   1 
ATOM   1172 C  CD2   . TYR A 1 179 ? 49.310 5.392   24.629 1.00 20.77 ? 159 TYR A CD2   1 
ATOM   1173 C  CE1   . TYR A 1 179 ? 51.783 4.335   25.254 1.00 27.43 ? 159 TYR A CE1   1 
ATOM   1174 C  CE2   . TYR A 1 179 ? 50.261 6.190   25.201 1.00 22.74 ? 159 TYR A CE2   1 
ATOM   1175 C  CZ    . TYR A 1 179 ? 51.502 5.653   25.514 1.00 24.10 ? 159 TYR A CZ    1 
ATOM   1176 O  OH    . TYR A 1 179 ? 52.461 6.423   26.097 1.00 22.81 ? 159 TYR A OH    1 
ATOM   1177 N  N     . ILE A 1 180 ? 45.953 3.437   25.420 1.00 19.14 ? 160 ILE A N     1 
ATOM   1178 C  CA    . ILE A 1 180 ? 45.147 4.086   26.452 1.00 17.49 ? 160 ILE A CA    1 
ATOM   1179 C  C     . ILE A 1 180 ? 44.900 3.142   27.627 1.00 19.53 ? 160 ILE A C     1 
ATOM   1180 O  O     . ILE A 1 180 ? 45.017 3.536   28.795 1.00 17.99 ? 160 ILE A O     1 
ATOM   1181 C  CB    . ILE A 1 180 ? 43.833 4.598   25.838 1.00 16.39 ? 160 ILE A CB    1 
ATOM   1182 C  CG1   . ILE A 1 180 ? 44.134 5.737   24.845 1.00 17.29 ? 160 ILE A CG1   1 
ATOM   1183 C  CG2   . ILE A 1 180 ? 42.852 5.069   26.927 1.00 16.32 ? 160 ILE A CG2   1 
ATOM   1184 C  CD1   . ILE A 1 180 ? 42.915 6.146   24.015 1.00 16.92 ? 160 ILE A CD1   1 
ATOM   1185 N  N     . ILE A 1 181 ? 44.602 1.875   27.344 1.00 16.11 ? 161 ILE A N     1 
ATOM   1186 C  CA    . ILE A 1 181 ? 44.332 0.916   28.415 1.00 15.75 ? 161 ILE A CA    1 
ATOM   1187 C  C     . ILE A 1 181 ? 45.598 0.612   29.223 1.00 16.37 ? 161 ILE A C     1 
ATOM   1188 O  O     . ILE A 1 181 ? 45.546 0.472   30.458 1.00 18.99 ? 161 ILE A O     1 
ATOM   1189 C  CB    . ILE A 1 181 ? 43.708 -0.357  27.824 1.00 16.23 ? 161 ILE A CB    1 
ATOM   1190 C  CG1   . ILE A 1 181 ? 42.267 -0.055  27.376 1.00 20.22 ? 161 ILE A CG1   1 
ATOM   1191 C  CG2   . ILE A 1 181 ? 43.725 -1.485  28.845 1.00 19.59 ? 161 ILE A CG2   1 
ATOM   1192 C  CD1   . ILE A 1 181 ? 41.683 -1.040  26.402 1.00 22.20 ? 161 ILE A CD1   1 
ATOM   1193 N  N     . VAL A 1 182 ? 46.748 0.489   28.555 1.00 18.57 ? 162 VAL A N     1 
ATOM   1194 C  CA    . VAL A 1 182 ? 47.990 0.272   29.295 1.00 18.58 ? 162 VAL A CA    1 
ATOM   1195 C  C     . VAL A 1 182 ? 48.215 1.423   30.263 1.00 16.88 ? 162 VAL A C     1 
ATOM   1196 O  O     . VAL A 1 182 ? 48.507 1.222   31.449 1.00 18.67 ? 162 VAL A O     1 
ATOM   1197 C  CB    . VAL A 1 182 ? 49.191 0.126   28.345 1.00 19.05 ? 162 VAL A CB    1 
ATOM   1198 C  CG1   . VAL A 1 182 ? 50.499 0.238   29.134 1.00 25.35 ? 162 VAL A CG1   1 
ATOM   1199 C  CG2   . VAL A 1 182 ? 49.137 -1.184  27.624 1.00 23.50 ? 162 VAL A CG2   1 
ATOM   1200 N  N     . LYS A 1 183 ? 48.067 2.646   29.772 1.00 15.92 ? 163 LYS A N     1 
ATOM   1201 C  CA    . LYS A 1 183 ? 48.372 3.805   30.608 1.00 16.04 ? 163 LYS A CA    1 
ATOM   1202 C  C     . LYS A 1 183 ? 47.295 4.044   31.655 1.00 17.39 ? 163 LYS A C     1 
ATOM   1203 O  O     . LYS A 1 183 ? 47.594 4.521   32.768 1.00 16.50 ? 163 LYS A O     1 
ATOM   1204 C  CB    . LYS A 1 183 ? 48.549 5.026   29.731 1.00 16.96 ? 163 LYS A CB    1 
ATOM   1205 C  CG    . LYS A 1 183 ? 49.834 4.977   28.833 1.00 18.18 ? 163 LYS A CG    1 
ATOM   1206 C  CD    . LYS A 1 183 ? 51.075 4.791   29.697 1.00 28.12 ? 163 LYS A CD    1 
ATOM   1207 C  CE    . LYS A 1 183 ? 52.368 4.848   28.958 1.00 33.44 ? 163 LYS A CE    1 
ATOM   1208 N  NZ    . LYS A 1 183 ? 53.471 4.791   29.969 1.00 38.37 ? 163 LYS A NZ    1 
ATOM   1209 N  N     . ALA A 1 184 ? 46.046 3.748   31.324 1.00 14.70 ? 164 ALA A N     1 
ATOM   1210 C  CA    . ALA A 1 184 ? 44.989 3.849   32.316 1.00 18.43 ? 164 ALA A CA    1 
ATOM   1211 C  C     . ALA A 1 184 ? 45.215 2.852   33.435 1.00 17.43 ? 164 ALA A C     1 
ATOM   1212 O  O     . ALA A 1 184 ? 44.998 3.159   34.611 1.00 15.97 ? 164 ALA A O     1 
ATOM   1213 C  CB    . ALA A 1 184 ? 43.620 3.620   31.675 1.00 17.55 ? 164 ALA A CB    1 
ATOM   1214 N  N     . ASN A 1 185 ? 45.655 1.649   33.092 1.00 16.11 ? 165 ASN A N     1 
ATOM   1215 C  CA    . ASN A 1 185 ? 45.919 0.669   34.127 1.00 18.84 ? 165 ASN A CA    1 
ATOM   1216 C  C     . ASN A 1 185 ? 47.105 1.085   35.008 1.00 18.66 ? 165 ASN A C     1 
ATOM   1217 O  O     . ASN A 1 185 ? 47.072 0.871   36.223 1.00 19.84 ? 165 ASN A O     1 
ATOM   1218 C  CB    . ASN A 1 185 ? 46.139 -0.692  33.490 1.00 22.18 ? 165 ASN A CB    1 
ATOM   1219 C  CG    . ASN A 1 185 ? 46.201 -1.791  34.512 1.00 36.47 ? 165 ASN A CG    1 
ATOM   1220 O  OD1   . ASN A 1 185 ? 45.169 -2.233  35.026 1.00 42.78 ? 165 ASN A OD1   1 
ATOM   1221 N  ND2   . ASN A 1 185 ? 47.414 -2.234  34.830 1.00 41.84 ? 165 ASN A ND2   1 
ATOM   1222 N  N     . GLU A 1 186 ? 48.152 1.690   34.425 1.00 18.72 ? 166 GLU A N     1 
ATOM   1223 C  CA    . GLU A 1 186 ? 49.258 2.199   35.251 1.00 17.85 ? 166 GLU A CA    1 
ATOM   1224 C  C     . GLU A 1 186 ? 48.756 3.257   36.235 1.00 19.85 ? 166 GLU A C     1 
ATOM   1225 O  O     . GLU A 1 186 ? 49.139 3.260   37.418 1.00 17.06 ? 166 GLU A O     1 
ATOM   1226 C  CB    . GLU A 1 186 ? 50.383 2.776   34.377 1.00 19.99 ? 166 GLU A CB    1 
ATOM   1227 C  CG    . GLU A 1 186 ? 51.133 1.700   33.591 1.00 24.40 ? 166 GLU A CG    1 
ATOM   1228 C  CD    . GLU A 1 186 ? 52.233 2.260   32.689 1.00 31.25 ? 166 GLU A CD    1 
ATOM   1229 O  OE1   . GLU A 1 186 ? 52.424 3.498   32.653 1.00 28.66 ? 166 GLU A OE1   1 
ATOM   1230 O  OE2   . GLU A 1 186 ? 52.927 1.445   32.040 1.00 31.59 ? 166 GLU A OE2   1 
ATOM   1231 N  N     . SER A 1 187 ? 47.890 4.158   35.765 1.00 19.19 ? 167 SER A N     1 
ATOM   1232 C  CA    . SER A 1 187 ? 47.309 5.166   36.651 1.00 17.43 ? 167 SER A CA    1 
ATOM   1233 C  C     . SER A 1 187 ? 46.463 4.513   37.746 1.00 15.98 ? 167 SER A C     1 
ATOM   1234 O  O     . SER A 1 187 ? 46.555 4.875   38.938 1.00 17.12 ? 167 SER A O     1 
ATOM   1235 C  CB    . SER A 1 187 ? 46.495 6.138   35.804 1.00 15.47 ? 167 SER A CB    1 
ATOM   1236 O  OG    . SER A 1 187 ? 45.861 7.109   36.589 1.00 17.13 ? 167 SER A OG    1 
ATOM   1237 N  N     . LEU A 1 188 ? 45.674 3.509   37.373 1.00 16.36 ? 168 LEU A N     1 
ATOM   1238 C  CA    . LEU A 1 188 ? 44.843 2.822   38.353 1.00 14.70 ? 168 LEU A CA    1 
ATOM   1239 C  C     . LEU A 1 188 ? 45.703 2.154   39.419 1.00 16.83 ? 168 LEU A C     1 
ATOM   1240 O  O     . LEU A 1 188 ? 45.393 2.239   40.614 1.00 16.21 ? 168 LEU A O     1 
ATOM   1241 C  CB    . LEU A 1 188 ? 43.968 1.783   37.653 1.00 16.59 ? 168 LEU A CB    1 
ATOM   1242 C  CG    . LEU A 1 188 ? 43.063 0.941   38.563 1.00 18.67 ? 168 LEU A CG    1 
ATOM   1243 C  CD1   . LEU A 1 188 ? 42.067 1.817   39.330 1.00 16.98 ? 168 LEU A CD1   1 
ATOM   1244 C  CD2   . LEU A 1 188 ? 42.319 -0.102  37.775 1.00 21.96 ? 168 LEU A CD2   1 
ATOM   1245 N  N     . GLU A 1 189 ? 46.789 1.490   38.999 1.00 17.21 ? 169 GLU A N     1 
ATOM   1246 C  CA    . GLU A 1 189 ? 47.685 0.828   39.943 1.00 18.91 ? 169 GLU A CA    1 
ATOM   1247 C  C     . GLU A 1 189 ? 48.380 1.829   40.845 1.00 16.94 ? 169 GLU A C     1 
ATOM   1248 O  O     . GLU A 1 189 ? 48.807 1.466   41.943 1.00 16.34 ? 169 GLU A O     1 
ATOM   1249 C  CB    . GLU A 1 189 ? 48.711 -0.022  39.189 1.00 19.76 ? 169 GLU A CB    1 
ATOM   1250 C  CG    . GLU A 1 189 ? 48.107 -1.263  38.508 1.00 23.41 ? 169 GLU A CG    1 
ATOM   1251 C  CD    . GLU A 1 189 ? 47.208 -2.114  39.418 1.00 35.63 ? 169 GLU A CD    1 
ATOM   1252 O  OE1   . GLU A 1 189 ? 47.646 -2.516  40.523 1.00 42.76 ? 169 GLU A OE1   1 
ATOM   1253 O  OE2   . GLU A 1 189 ? 46.034 -2.367  39.030 1.00 51.21 ? 169 GLU A OE2   1 
ATOM   1254 N  N     . ASN A 1 190 ? 48.457 3.081   40.426 1.00 16.54 ? 170 ASN A N     1 
ATOM   1255 C  CA    . ASN A 1 190 ? 49.078 4.134   41.214 1.00 20.18 ? 170 ASN A CA    1 
ATOM   1256 C  C     . ASN A 1 190 ? 48.097 4.842   42.142 1.00 16.69 ? 170 ASN A C     1 
ATOM   1257 O  O     . ASN A 1 190 ? 48.528 5.645   42.981 1.00 17.25 ? 170 ASN A O     1 
ATOM   1258 C  CB    . ASN A 1 190 ? 49.715 5.168   40.270 1.00 18.24 ? 170 ASN A CB    1 
ATOM   1259 C  CG    . ASN A 1 190 ? 50.550 6.201   41.006 1.00 19.74 ? 170 ASN A CG    1 
ATOM   1260 O  OD1   . ASN A 1 190 ? 51.527 5.847   41.648 1.00 17.66 ? 170 ASN A OD1   1 
ATOM   1261 N  ND2   . ASN A 1 190 ? 50.179 7.487   40.897 1.00 19.48 ? 170 ASN A ND2   1 
ATOM   1262 N  N     . THR A 1 191 ? 46.799 4.582   42.023 1.00 15.92 ? 171 THR A N     1 
ATOM   1263 C  CA    . THR A 1 191 ? 45.844 5.328   42.845 1.00 16.57 ? 171 THR A CA    1 
ATOM   1264 C  C     . THR A 1 191 ? 46.114 5.167   44.341 1.00 17.00 ? 171 THR A C     1 
ATOM   1265 O  O     . THR A 1 191 ? 45.937 6.158   45.066 1.00 14.81 ? 171 THR A O     1 
ATOM   1266 C  CB    . THR A 1 191 ? 44.373 4.975   42.529 1.00 13.48 ? 171 THR A CB    1 
ATOM   1267 O  OG1   . THR A 1 191 ? 44.122 3.568   42.602 1.00 16.06 ? 171 THR A OG1   1 
ATOM   1268 C  CG2   . THR A 1 191 ? 43.979 5.482   41.135 1.00 18.43 ? 171 THR A CG2   1 
ATOM   1269 N  N     . PRO A 1 192 ? 46.525 4.007   44.864 1.00 16.35 ? 172 PRO A N     1 
ATOM   1270 C  CA    . PRO A 1 192 ? 46.850 3.941   46.313 1.00 16.23 ? 172 PRO A CA    1 
ATOM   1271 C  C     . PRO A 1 192 ? 47.972 4.885   46.738 1.00 18.58 ? 172 PRO A C     1 
ATOM   1272 O  O     . PRO A 1 192 ? 48.063 5.219   47.928 1.00 17.52 ? 172 PRO A O     1 
ATOM   1273 C  CB    . PRO A 1 192 ? 47.243 2.470   46.536 1.00 18.40 ? 172 PRO A CB    1 
ATOM   1274 C  CG    . PRO A 1 192 ? 46.664 1.718   45.383 1.00 21.18 ? 172 PRO A CG    1 
ATOM   1275 C  CD    . PRO A 1 192 ? 46.719 2.698   44.201 1.00 18.04 ? 172 PRO A CD    1 
ATOM   1276 N  N     . ASN A 1 193 ? 48.848 5.317   45.829 1.00 14.75 ? 173 ASN A N     1 
ATOM   1277 C  CA    . ASN A 1 193 ? 49.888 6.270   46.209 1.00 17.34 ? 173 ASN A CA    1 
ATOM   1278 C  C     . ASN A 1 193 ? 49.391 7.704   46.270 1.00 16.70 ? 173 ASN A C     1 
ATOM   1279 O  O     . ASN A 1 193 ? 50.149 8.591   46.676 1.00 16.96 ? 173 ASN A O     1 
ATOM   1280 C  CB    . ASN A 1 193 ? 51.068 6.185   45.246 1.00 18.33 ? 173 ASN A CB    1 
ATOM   1281 C  CG    . ASN A 1 193 ? 51.671 4.818   45.230 1.00 19.30 ? 173 ASN A CG    1 
ATOM   1282 O  OD1   . ASN A 1 193 ? 51.856 4.211   46.271 1.00 20.52 ? 173 ASN A OD1   1 
ATOM   1283 N  ND2   . ASN A 1 193 ? 51.940 4.306   44.045 1.00 21.36 ? 173 ASN A ND2   1 
ATOM   1284 N  N     . LEU A 1 194 ? 48.148 7.956   45.890 1.00 13.51 ? 174 LEU A N     1 
ATOM   1285 C  CA    . LEU A 1 194 ? 47.568 9.290   45.988 1.00 16.17 ? 174 LEU A CA    1 
ATOM   1286 C  C     . LEU A 1 194 ? 46.516 9.405   47.072 1.00 15.98 ? 174 LEU A C     1 
ATOM   1287 O  O     . LEU A 1 194 ? 46.283 10.499  47.575 1.00 15.51 ? 174 LEU A O     1 
ATOM   1288 C  CB    . LEU A 1 194 ? 46.938 9.691   44.650 1.00 12.16 ? 174 LEU A CB    1 
ATOM   1289 C  CG    . LEU A 1 194 ? 47.937 10.023  43.545 1.00 14.27 ? 174 LEU A CG    1 
ATOM   1290 C  CD1   . LEU A 1 194 ? 47.280 9.875   42.172 1.00 19.63 ? 174 LEU A CD1   1 
ATOM   1291 C  CD2   . LEU A 1 194 ? 48.459 11.414  43.734 1.00 17.86 ? 174 LEU A CD2   1 
ATOM   1292 N  N     . LEU A 1 195 ? 45.871 8.298   47.428 1.00 16.85 ? 175 LEU A N     1 
ATOM   1293 C  CA    . LEU A 1 195 ? 44.722 8.311   48.311 1.00 19.87 ? 175 LEU A CA    1 
ATOM   1294 C  C     . LEU A 1 195 ? 45.006 7.313   49.426 1.00 20.77 ? 175 LEU A C     1 
ATOM   1295 O  O     . LEU A 1 195 ? 45.100 6.107   49.182 1.00 22.04 ? 175 LEU A O     1 
ATOM   1296 C  CB    . LEU A 1 195 ? 43.456 7.988   47.521 1.00 20.98 ? 175 LEU A CB    1 
ATOM   1297 C  CG    . LEU A 1 195 ? 42.107 7.948   48.220 1.00 24.80 ? 175 LEU A CG    1 
ATOM   1298 C  CD1   . LEU A 1 195 ? 41.815 9.264   48.950 1.00 21.65 ? 175 LEU A CD1   1 
ATOM   1299 C  CD2   . LEU A 1 195 ? 40.996 7.644   47.193 1.00 18.66 ? 175 LEU A CD2   1 
ATOM   1300 N  N     . ALA A 1 196 ? 45.181 7.837   50.642 1.00 20.22 ? 176 ALA A N     1 
ATOM   1301 C  CA    . ALA A 1 196 ? 45.701 7.049   51.756 1.00 21.21 ? 176 ALA A CA    1 
ATOM   1302 C  C     . ALA A 1 196 ? 44.848 5.814   52.052 1.00 21.21 ? 176 ALA A C     1 
ATOM   1303 O  O     . ALA A 1 196 ? 45.390 4.728   52.307 1.00 21.21 ? 176 ALA A O     1 
ATOM   1304 C  CB    . ALA A 1 196 ? 45.804 7.929   52.999 1.00 23.16 ? 176 ALA A CB    1 
ATOM   1305 N  N     . VAL A 1 197 ? 43.514 5.952   52.052 1.00 19.15 ? 177 VAL A N     1 
ATOM   1306 C  CA    . VAL A 1 197 ? 42.701 4.813   52.467 1.00 17.74 ? 177 VAL A CA    1 
ATOM   1307 C  C     . VAL A 1 197 ? 42.896 3.644   51.514 1.00 18.06 ? 177 VAL A C     1 
ATOM   1308 O  O     . VAL A 1 197 ? 42.820 2.484   51.921 1.00 16.50 ? 177 VAL A O     1 
ATOM   1309 C  CB    . VAL A 1 197 ? 41.207 5.200   52.608 1.00 22.01 ? 177 VAL A CB    1 
ATOM   1310 C  CG1   . VAL A 1 197 ? 40.607 5.576   51.272 1.00 21.07 ? 177 VAL A CG1   1 
ATOM   1311 C  CG2   . VAL A 1 197 ? 40.411 4.033   53.221 1.00 21.25 ? 177 VAL A CG2   1 
ATOM   1312 N  N     . LEU A 1 198 ? 43.177 3.915   50.237 1.00 16.60 ? 178 LEU A N     1 
ATOM   1313 C  CA    . LEU A 1 198 ? 43.413 2.823   49.297 1.00 18.25 ? 178 LEU A CA    1 
ATOM   1314 C  C     . LEU A 1 198 ? 44.660 2.024   49.653 1.00 17.65 ? 178 LEU A C     1 
ATOM   1315 O  O     . LEU A 1 198 ? 44.657 0.797   49.570 1.00 20.51 ? 178 LEU A O     1 
ATOM   1316 C  CB    . LEU A 1 198 ? 43.546 3.363   47.880 1.00 17.42 ? 178 LEU A CB    1 
ATOM   1317 C  CG    . LEU A 1 198 ? 42.331 4.094   47.316 1.00 17.78 ? 178 LEU A CG    1 
ATOM   1318 C  CD1   . LEU A 1 198 ? 42.643 4.584   45.877 1.00 16.20 ? 178 LEU A CD1   1 
ATOM   1319 C  CD2   . LEU A 1 198 ? 41.077 3.228   47.313 1.00 19.18 ? 178 LEU A CD2   1 
ATOM   1320 N  N     . LYS A 1 199 ? 45.749 2.706   50.000 1.00 16.70 ? 179 LYS A N     1 
ATOM   1321 C  CA    . LYS A 1 199 ? 46.976 2.009   50.380 1.00 19.16 ? 179 LYS A CA    1 
ATOM   1322 C  C     . LYS A 1 199 ? 46.802 1.282   51.708 1.00 19.50 ? 179 LYS A C     1 
ATOM   1323 O  O     . LYS A 1 199 ? 47.280 0.151   51.877 1.00 22.65 ? 179 LYS A O     1 
ATOM   1324 C  CB    . LYS A 1 199 ? 48.123 3.023   50.470 1.00 22.79 ? 179 LYS A CB    1 
ATOM   1325 C  CG    . LYS A 1 199 ? 49.517 2.406   50.713 1.00 27.51 ? 179 LYS A CG    1 
ATOM   1326 C  CD    . LYS A 1 199 ? 50.496 2.719   49.563 1.00 33.33 ? 179 LYS A CD    1 
ATOM   1327 N  N     . GLU A 1 200 ? 46.113 1.921   52.656 1.00 17.36 ? 180 GLU A N     1 
ATOM   1328 C  CA    . GLU A 1 200 ? 45.924 1.323   53.986 1.00 19.55 ? 180 GLU A CA    1 
ATOM   1329 C  C     . GLU A 1 200 ? 45.108 0.040   53.910 1.00 24.33 ? 180 GLU A C     1 
ATOM   1330 O  O     . GLU A 1 200 ? 45.436 -0.951  54.579 1.00 19.94 ? 180 GLU A O     1 
ATOM   1331 C  CB    . GLU A 1 200 ? 45.261 2.333   54.922 1.00 21.83 ? 180 GLU A CB    1 
ATOM   1332 C  CG    . GLU A 1 200 ? 46.188 3.481   55.311 1.00 27.49 ? 180 GLU A CG    1 
ATOM   1333 C  CD    . GLU A 1 200 ? 45.476 4.756   55.807 1.00 36.96 ? 180 GLU A CD    1 
ATOM   1334 O  OE1   . GLU A 1 200 ? 44.219 4.824   55.850 1.00 35.62 ? 180 GLU A OE1   1 
ATOM   1335 O  OE2   . GLU A 1 200 ? 46.209 5.714   56.148 1.00 32.14 ? 180 GLU A OE2   1 
ATOM   1336 N  N     . VAL A 1 201 ? 44.055 0.030   53.085 1.00 17.91 ? 181 VAL A N     1 
ATOM   1337 C  CA    . VAL A 1 201 ? 43.226 -1.161  52.951 1.00 19.89 ? 181 VAL A CA    1 
ATOM   1338 C  C     . VAL A 1 201 ? 43.863 -2.135  51.977 1.00 22.02 ? 181 VAL A C     1 
ATOM   1339 O  O     . VAL A 1 201 ? 43.696 -3.347  52.117 1.00 24.85 ? 181 VAL A O     1 
ATOM   1340 C  CB    . VAL A 1 201 ? 41.792 -0.794  52.507 1.00 23.30 ? 181 VAL A CB    1 
ATOM   1341 C  CG1   . VAL A 1 201 ? 40.962 -2.070  52.266 1.00 24.12 ? 181 VAL A CG1   1 
ATOM   1342 C  CG2   . VAL A 1 201 ? 41.078 0.140   53.534 1.00 18.56 ? 181 VAL A CG2   1 
ATOM   1343 N  N     . GLY A 1 202 ? 44.581 -1.631  50.970 1.00 20.84 ? 182 GLY A N     1 
ATOM   1344 C  CA    . GLY A 1 202 ? 45.253 -2.484  50.001 1.00 19.56 ? 182 GLY A CA    1 
ATOM   1345 C  C     . GLY A 1 202 ? 44.449 -2.738  48.736 1.00 20.95 ? 182 GLY A C     1 
ATOM   1346 O  O     . GLY A 1 202 ? 44.442 -3.864  48.231 1.00 22.57 ? 182 GLY A O     1 
ATOM   1347 N  N     . VAL A 1 203 ? 43.779 -1.710  48.202 1.00 20.30 ? 183 VAL A N     1 
ATOM   1348 C  CA    . VAL A 1 203 ? 42.954 -1.835  46.998 1.00 17.16 ? 183 VAL A CA    1 
ATOM   1349 C  C     . VAL A 1 203 ? 43.234 -0.656  46.077 1.00 19.14 ? 183 VAL A C     1 
ATOM   1350 O  O     . VAL A 1 203 ? 43.648 0.418   46.520 1.00 20.09 ? 183 VAL A O     1 
ATOM   1351 C  CB    . VAL A 1 203 ? 41.438 -1.869  47.314 1.00 19.88 ? 183 VAL A CB    1 
ATOM   1352 C  CG1   . VAL A 1 203 ? 41.072 -3.154  48.032 1.00 24.59 ? 183 VAL A CG1   1 
ATOM   1353 C  CG2   . VAL A 1 203 ? 41.036 -0.660  48.167 1.00 20.55 ? 183 VAL A CG2   1 
ATOM   1354 N  N     . VAL A 1 204 ? 42.962 -0.847  44.786 1.00 18.08 ? 184 VAL A N     1 
ATOM   1355 C  CA    . VAL A 1 204 ? 42.942 0.286   43.862 1.00 17.40 ? 184 VAL A CA    1 
ATOM   1356 C  C     . VAL A 1 204 ? 41.560 0.940   43.914 1.00 16.23 ? 184 VAL A C     1 
ATOM   1357 O  O     . VAL A 1 204 ? 40.627 0.409   44.525 1.00 19.17 ? 184 VAL A O     1 
ATOM   1358 C  CB    . VAL A 1 204 ? 43.303 -0.139  42.427 1.00 16.53 ? 184 VAL A CB    1 
ATOM   1359 C  CG1   . VAL A 1 204 ? 44.742 -0.734  42.349 1.00 20.51 ? 184 VAL A CG1   1 
ATOM   1360 C  CG2   . VAL A 1 204 ? 42.283 -1.112  41.868 1.00 19.07 ? 184 VAL A CG2   1 
ATOM   1361 N  N     . ASP A 1 205 ? 41.423 2.106   43.289 1.00 17.61 ? 185 ASP A N     1 
ATOM   1362 C  CA    . ASP A 1 205 ? 40.162 2.827   43.343 1.00 16.44 ? 185 ASP A CA    1 
ATOM   1363 C  C     . ASP A 1 205 ? 39.069 2.096   42.566 1.00 15.60 ? 185 ASP A C     1 
ATOM   1364 O  O     . ASP A 1 205 ? 39.239 1.752   41.400 1.00 16.27 ? 185 ASP A O     1 
ATOM   1365 C  CB    . ASP A 1 205 ? 40.332 4.242   42.815 1.00 15.65 ? 185 ASP A CB    1 
ATOM   1366 C  CG    . ASP A 1 205 ? 39.052 5.041   42.940 1.00 17.72 ? 185 ASP A CG    1 
ATOM   1367 O  OD1   . ASP A 1 205 ? 38.642 5.361   44.085 1.00 19.99 ? 185 ASP A OD1   1 
ATOM   1368 O  OD2   . ASP A 1 205 ? 38.408 5.279   41.903 1.00 17.20 ? 185 ASP A OD2   1 
ATOM   1369 N  N     . SER A 1 206 ? 37.916 1.913   43.209 1.00 16.04 ? 186 SER A N     1 
ATOM   1370 C  CA    . SER A 1 206 ? 36.812 1.196   42.574 1.00 16.92 ? 186 SER A CA    1 
ATOM   1371 C  C     . SER A 1 206 ? 36.264 1.946   41.357 1.00 16.12 ? 186 SER A C     1 
ATOM   1372 O  O     . SER A 1 206 ? 35.967 1.330   40.338 1.00 17.42 ? 186 SER A O     1 
ATOM   1373 C  CB    . SER A 1 206 ? 35.702 0.936   43.597 1.00 20.20 ? 186 SER A CB    1 
ATOM   1374 O  OG    . SER A 1 206 ? 35.245 2.162   44.122 1.00 26.12 ? 186 SER A OG    1 
ATOM   1375 N  N     . GLY A 1 207 ? 36.094 3.264   41.449 1.00 14.71 ? 187 GLY A N     1 
ATOM   1376 C  CA    . GLY A 1 207 ? 35.603 4.016   40.298 1.00 14.84 ? 187 GLY A CA    1 
ATOM   1377 C  C     . GLY A 1 207 ? 36.520 3.910   39.096 1.00 16.46 ? 187 GLY A C     1 
ATOM   1378 O  O     . GLY A 1 207 ? 36.063 3.696   37.970 1.00 15.70 ? 187 GLY A O     1 
ATOM   1379 N  N     . GLY A 1 208 ? 37.827 4.051   39.322 1.00 15.32 ? 188 GLY A N     1 
ATOM   1380 C  CA    . GLY A 1 208 ? 38.772 3.880   38.233 1.00 16.65 ? 188 GLY A CA    1 
ATOM   1381 C  C     . GLY A 1 208 ? 38.761 2.474   37.664 1.00 16.57 ? 188 GLY A C     1 
ATOM   1382 O  O     . GLY A 1 208 ? 38.927 2.282   36.457 1.00 16.24 ? 188 GLY A O     1 
ATOM   1383 N  N     . LYS A 1 209 ? 38.561 1.470   38.521 1.00 14.83 ? 189 LYS A N     1 
ATOM   1384 C  CA    . LYS A 1 209 ? 38.507 0.111   38.011 1.00 15.29 ? 189 LYS A CA    1 
ATOM   1385 C  C     . LYS A 1 209 ? 37.299 -0.078  37.108 1.00 13.95 ? 189 LYS A C     1 
ATOM   1386 O  O     . LYS A 1 209 ? 37.407 -0.698  36.040 1.00 16.61 ? 189 LYS A O     1 
ATOM   1387 C  CB    . LYS A 1 209 ? 38.500 -0.876  39.175 1.00 15.36 ? 189 LYS A CB    1 
ATOM   1388 C  CG    . LYS A 1 209 ? 38.524 -2.348  38.754 1.00 21.25 ? 189 LYS A CG    1 
ATOM   1389 C  CD    . LYS A 1 209 ? 39.784 -2.714  38.071 1.00 27.45 ? 189 LYS A CD    1 
ATOM   1390 C  CE    . LYS A 1 209 ? 39.869 -4.214  37.850 1.00 39.70 ? 189 LYS A CE    1 
ATOM   1391 N  NZ    . LYS A 1 209 ? 40.573 -4.504  36.577 1.00 46.62 ? 189 LYS A NZ    1 
ATOM   1392 N  N     . GLY A 1 210 ? 36.148 0.476   37.497 1.00 16.24 ? 190 GLY A N     1 
ATOM   1393 C  CA    . GLY A 1 210 ? 34.966 0.393   36.645 1.00 19.09 ? 190 GLY A CA    1 
ATOM   1394 C  C     . GLY A 1 210 ? 35.178 1.054   35.295 1.00 16.34 ? 190 GLY A C     1 
ATOM   1395 O  O     . GLY A 1 210 ? 34.763 0.528   34.264 1.00 15.69 ? 190 GLY A O     1 
ATOM   1396 N  N     . LEU A 1 211 ? 35.833 2.219   35.287 1.00 15.14 ? 191 LEU A N     1 
ATOM   1397 C  CA    . LEU A 1 211 ? 36.159 2.885   34.028 1.00 16.37 ? 191 LEU A CA    1 
ATOM   1398 C  C     . LEU A 1 211 ? 37.080 2.038   33.163 1.00 14.84 ? 191 LEU A C     1 
ATOM   1399 O  O     . LEU A 1 211 ? 36.857 1.909   31.952 1.00 16.31 ? 191 LEU A O     1 
ATOM   1400 C  CB    . LEU A 1 211 ? 36.786 4.240   34.325 1.00 15.41 ? 191 LEU A CB    1 
ATOM   1401 C  CG    . LEU A 1 211 ? 37.043 5.124   33.119 1.00 17.18 ? 191 LEU A CG    1 
ATOM   1402 C  CD1   . LEU A 1 211 ? 35.722 5.514   32.461 1.00 19.34 ? 191 LEU A CD1   1 
ATOM   1403 C  CD2   . LEU A 1 211 ? 37.851 6.364   33.570 1.00 20.27 ? 191 LEU A CD2   1 
ATOM   1404 N  N     . LEU A 1 212 ? 38.096 1.416   33.763 1.00 16.75 ? 192 LEU A N     1 
ATOM   1405 C  CA    . LEU A 1 212 ? 38.951 0.524   32.981 1.00 17.46 ? 192 LEU A CA    1 
ATOM   1406 C  C     . LEU A 1 212 ? 38.146 -0.620  32.360 1.00 17.00 ? 192 LEU A C     1 
ATOM   1407 O  O     . LEU A 1 212 ? 38.402 -1.020  31.220 1.00 17.21 ? 192 LEU A O     1 
ATOM   1408 C  CB    . LEU A 1 212 ? 40.078 -0.021  33.852 1.00 19.85 ? 192 LEU A CB    1 
ATOM   1409 C  CG    . LEU A 1 212 ? 41.290 -0.663  33.187 1.00 29.74 ? 192 LEU A CG    1 
ATOM   1410 C  CD1   . LEU A 1 212 ? 41.888 0.225   32.120 1.00 26.83 ? 192 LEU A CD1   1 
ATOM   1411 C  CD2   . LEU A 1 212 ? 42.322 -1.008  34.258 1.00 38.77 ? 192 LEU A CD2   1 
ATOM   1412 N  N     . CYS A 1 213 ? 37.176 -1.161  33.095 1.00 17.49 ? 193 CYS A N     1 
ATOM   1413 C  CA    . CYS A 1 213 ? 36.287 -2.188  32.538 1.00 17.93 ? 193 CYS A CA    1 
ATOM   1414 C  C     . CYS A 1 213 ? 35.558 -1.711  31.289 1.00 18.86 ? 193 CYS A C     1 
ATOM   1415 O  O     . CYS A 1 213 ? 35.435 -2.454  30.316 1.00 18.32 ? 193 CYS A O     1 
ATOM   1416 C  CB    . CYS A 1 213 ? 35.273 -2.625  33.601 1.00 20.02 ? 193 CYS A CB    1 
ATOM   1417 S  SG    . CYS A 1 213 ? 35.991 -3.627  34.919 1.00 25.39 ? 193 CYS A SG    1 
ATOM   1418 N  N     . VAL A 1 214 ? 35.065 -0.478  31.296 1.00 17.36 ? 194 VAL A N     1 
ATOM   1419 C  CA    . VAL A 1 214 ? 34.425 0.077   30.109 1.00 17.41 ? 194 VAL A CA    1 
ATOM   1420 C  C     . VAL A 1 214 ? 35.434 0.209   28.968 1.00 15.61 ? 194 VAL A C     1 
ATOM   1421 O  O     . VAL A 1 214 ? 35.154 -0.169  27.820 1.00 17.23 ? 194 VAL A O     1 
ATOM   1422 C  CB    . VAL A 1 214 ? 33.776 1.429   30.458 1.00 13.60 ? 194 VAL A CB    1 
ATOM   1423 C  CG1   . VAL A 1 214 ? 33.222 2.125   29.225 1.00 18.95 ? 194 VAL A CG1   1 
ATOM   1424 C  CG2   . VAL A 1 214 ? 32.696 1.234   31.543 1.00 16.76 ? 194 VAL A CG2   1 
ATOM   1425 N  N     . TYR A 1 215 ? 36.634 0.722   29.266 1.00 16.98 ? 195 TYR A N     1 
ATOM   1426 C  CA    . TYR A 1 215 ? 37.626 0.903   28.211 1.00 17.07 ? 195 TYR A CA    1 
ATOM   1427 C  C     . TYR A 1 215 ? 38.043 -0.435  27.606 1.00 19.09 ? 195 TYR A C     1 
ATOM   1428 O  O     . TYR A 1 215 ? 38.328 -0.521  26.401 1.00 16.63 ? 195 TYR A O     1 
ATOM   1429 C  CB    . TYR A 1 215 ? 38.860 1.634   28.742 1.00 18.40 ? 195 TYR A CB    1 
ATOM   1430 C  CG    . TYR A 1 215 ? 38.667 3.118   29.062 1.00 16.63 ? 195 TYR A CG    1 
ATOM   1431 C  CD1   . TYR A 1 215 ? 37.486 3.780   28.750 1.00 15.50 ? 195 TYR A CD1   1 
ATOM   1432 C  CD2   . TYR A 1 215 ? 39.689 3.855   29.659 1.00 21.71 ? 195 TYR A CD2   1 
ATOM   1433 C  CE1   . TYR A 1 215 ? 37.317 5.128   29.038 1.00 18.76 ? 195 TYR A CE1   1 
ATOM   1434 C  CE2   . TYR A 1 215 ? 39.529 5.213   29.941 1.00 19.83 ? 195 TYR A CE2   1 
ATOM   1435 C  CZ    . TYR A 1 215 ? 38.345 5.838   29.618 1.00 19.50 ? 195 TYR A CZ    1 
ATOM   1436 O  OH    . TYR A 1 215 ? 38.184 7.169   29.896 1.00 22.07 ? 195 TYR A OH    1 
ATOM   1437 N  N     . GLU A 1 216 ? 38.128 -1.485  28.426 1.00 15.29 ? 196 GLU A N     1 
ATOM   1438 C  CA    . GLU A 1 216 ? 38.470 -2.797  27.882 1.00 17.45 ? 196 GLU A CA    1 
ATOM   1439 C  C     . GLU A 1 216 ? 37.390 -3.290  26.921 1.00 16.46 ? 196 GLU A C     1 
ATOM   1440 O  O     . GLU A 1 216 ? 37.701 -3.920  25.900 1.00 18.67 ? 196 GLU A O     1 
ATOM   1441 C  CB    . GLU A 1 216 ? 38.692 -3.793  29.007 1.00 21.98 ? 196 GLU A CB    1 
ATOM   1442 C  CG    . GLU A 1 216 ? 40.022 -3.563  29.787 1.00 23.13 ? 196 GLU A CG    1 
ATOM   1443 C  CD    . GLU A 1 216 ? 40.053 -4.347  31.091 1.00 42.62 ? 196 GLU A CD    1 
ATOM   1444 O  OE1   . GLU A 1 216 ? 39.010 -4.967  31.428 1.00 44.47 ? 196 GLU A OE1   1 
ATOM   1445 O  OE2   . GLU A 1 216 ? 41.109 -4.343  31.771 1.00 40.43 ? 196 GLU A OE2   1 
ATOM   1446 N  N     . GLY A 1 217 ? 36.121 -3.009  27.227 1.00 19.29 ? 197 GLY A N     1 
ATOM   1447 C  CA    . GLY A 1 217 ? 35.056 -3.305  26.280 1.00 18.30 ? 197 GLY A CA    1 
ATOM   1448 C  C     . GLY A 1 217 ? 35.151 -2.496  24.999 1.00 20.94 ? 197 GLY A C     1 
ATOM   1449 O  O     . GLY A 1 217 ? 34.894 -3.015  23.908 1.00 18.75 ? 197 GLY A O     1 
ATOM   1450 N  N     . PHE A 1 218 ? 35.496 -1.209  25.110 1.00 18.12 ? 198 PHE A N     1 
ATOM   1451 C  CA    . PHE A 1 218 ? 35.748 -0.401  23.917 1.00 19.33 ? 198 PHE A CA    1 
ATOM   1452 C  C     . PHE A 1 218 ? 36.712 -1.109  22.956 1.00 17.94 ? 198 PHE A C     1 
ATOM   1453 O  O     . PHE A 1 218 ? 36.472 -1.171  21.744 1.00 16.31 ? 198 PHE A O     1 
ATOM   1454 C  CB    . PHE A 1 218 ? 36.325 0.970   24.309 1.00 18.20 ? 198 PHE A CB    1 
ATOM   1455 C  CG    . PHE A 1 218 ? 35.294 1.988   24.794 1.00 15.87 ? 198 PHE A CG    1 
ATOM   1456 C  CD1   . PHE A 1 218 ? 34.008 1.611   25.178 1.00 17.40 ? 198 PHE A CD1   1 
ATOM   1457 C  CD2   . PHE A 1 218 ? 35.630 3.344   24.831 1.00 21.97 ? 198 PHE A CD2   1 
ATOM   1458 C  CE1   . PHE A 1 218 ? 33.089 2.553   25.603 1.00 19.75 ? 198 PHE A CE1   1 
ATOM   1459 C  CE2   . PHE A 1 218 ? 34.714 4.295   25.252 1.00 19.75 ? 198 PHE A CE2   1 
ATOM   1460 C  CZ    . PHE A 1 218 ? 33.435 3.900   25.635 1.00 22.42 ? 198 PHE A CZ    1 
ATOM   1461 N  N     . LEU A 1 219 ? 37.828 -1.626  23.491 1.00 16.82 ? 199 LEU A N     1 
ATOM   1462 C  CA    . LEU A 1 219 ? 38.839 -2.270  22.663 1.00 16.72 ? 199 LEU A CA    1 
ATOM   1463 C  C     . LEU A 1 219 ? 38.288 -3.521  21.998 1.00 17.86 ? 199 LEU A C     1 
ATOM   1464 O  O     . LEU A 1 219 ? 38.517 -3.746  20.806 1.00 17.47 ? 199 LEU A O     1 
ATOM   1465 C  CB    . LEU A 1 219 ? 40.058 -2.603  23.525 1.00 19.26 ? 199 LEU A CB    1 
ATOM   1466 C  CG    . LEU A 1 219 ? 41.187 -3.397  22.879 1.00 21.02 ? 199 LEU A CG    1 
ATOM   1467 C  CD1   . LEU A 1 219 ? 41.804 -2.586  21.750 1.00 23.59 ? 199 LEU A CD1   1 
ATOM   1468 C  CD2   . LEU A 1 219 ? 42.268 -3.795  23.928 1.00 23.42 ? 199 LEU A CD2   1 
ATOM   1469 N  N     . LYS A 1 220 ? 37.555 -4.347  22.746 1.00 19.31 ? 200 LYS A N     1 
ATOM   1470 C  CA    . LYS A 1 220 ? 36.958 -5.536  22.144 1.00 21.39 ? 200 LYS A CA    1 
ATOM   1471 C  C     . LYS A 1 220 ? 36.110 -5.159  20.945 1.00 21.32 ? 200 LYS A C     1 
ATOM   1472 O  O     . LYS A 1 220 ? 36.207 -5.776  19.881 1.00 19.23 ? 200 LYS A O     1 
ATOM   1473 C  CB    . LYS A 1 220 ? 36.125 -6.283  23.178 1.00 23.67 ? 200 LYS A CB    1 
ATOM   1474 C  CG    . LYS A 1 220 ? 36.983 -6.956  24.196 1.00 28.00 ? 200 LYS A CG    1 
ATOM   1475 C  CD    . LYS A 1 220 ? 37.416 -8.318  23.685 1.00 32.78 ? 200 LYS A CD    1 
ATOM   1476 C  CE    . LYS A 1 220 ? 36.398 -9.357  24.076 1.00 39.69 ? 200 LYS A CE    1 
ATOM   1477 N  NZ    . LYS A 1 220 ? 36.792 -10.718 23.613 1.00 42.65 ? 200 LYS A NZ    1 
ATOM   1478 N  N     . ALA A 1 221 ? 35.280 -4.134  21.092 1.00 18.44 ? 201 ALA A N     1 
ATOM   1479 C  CA    . ALA A 1 221 ? 34.436 -3.715  19.971 1.00 19.63 ? 201 ALA A CA    1 
ATOM   1480 C  C     . ALA A 1 221 ? 35.249 -3.203  18.786 1.00 19.69 ? 201 ALA A C     1 
ATOM   1481 O  O     . ALA A 1 221 ? 34.869 -3.426  17.628 1.00 19.04 ? 201 ALA A O     1 
ATOM   1482 C  CB    . ALA A 1 221 ? 33.446 -2.636  20.423 1.00 19.06 ? 201 ALA A CB    1 
ATOM   1483 N  N     . LEU A 1 222 ? 36.352 -2.491  19.042 1.00 16.61 ? 202 LEU A N     1 
ATOM   1484 C  CA    . LEU A 1 222 ? 37.151 -1.972  17.936 1.00 18.45 ? 202 LEU A CA    1 
ATOM   1485 C  C     . LEU A 1 222 ? 37.757 -3.113  17.131 1.00 16.81 ? 202 LEU A C     1 
ATOM   1486 O  O     . LEU A 1 222 ? 37.990 -2.977  15.920 1.00 21.85 ? 202 LEU A O     1 
ATOM   1487 C  CB    . LEU A 1 222 ? 38.248 -1.042  18.478 1.00 21.69 ? 202 LEU A CB    1 
ATOM   1488 C  CG    . LEU A 1 222 ? 37.764 0.331   18.962 1.00 19.84 ? 202 LEU A CG    1 
ATOM   1489 C  CD1   . LEU A 1 222 ? 38.889 1.048   19.750 1.00 20.52 ? 202 LEU A CD1   1 
ATOM   1490 C  CD2   . LEU A 1 222 ? 37.274 1.197   17.799 1.00 23.47 ? 202 LEU A CD2   1 
ATOM   1491 N  N     . LYS A 1 223 ? 38.020 -4.235  17.793 1.00 19.65 ? 203 LYS A N     1 
ATOM   1492 C  CA    . LYS A 1 223 ? 38.555 -5.423  17.143 1.00 21.27 ? 203 LYS A CA    1 
ATOM   1493 C  C     . LYS A 1 223 ? 37.477 -6.253  16.465 1.00 25.44 ? 203 LYS A C     1 
ATOM   1494 O  O     . LYS A 1 223 ? 37.798 -7.309  15.905 1.00 24.92 ? 203 LYS A O     1 
ATOM   1495 C  CB    . LYS A 1 223 ? 39.292 -6.283  18.177 1.00 21.85 ? 203 LYS A CB    1 
ATOM   1496 C  CG    . LYS A 1 223 ? 40.568 -5.647  18.742 1.00 27.03 ? 203 LYS A CG    1 
ATOM   1497 C  CD    . LYS A 1 223 ? 41.169 -6.552  19.801 1.00 30.25 ? 203 LYS A CD    1 
ATOM   1498 C  CE    . LYS A 1 223 ? 42.481 -6.020  20.344 1.00 40.86 ? 203 LYS A CE    1 
ATOM   1499 N  NZ    . LYS A 1 223 ? 43.531 -5.963  19.278 1.00 56.53 ? 203 LYS A NZ    1 
ATOM   1500 N  N     . GLY A 1 224 ? 36.220 -5.792  16.492 1.00 21.96 ? 204 GLY A N     1 
ATOM   1501 C  CA    . GLY A 1 224 ? 35.086 -6.556  16.003 1.00 24.52 ? 204 GLY A CA    1 
ATOM   1502 C  C     . GLY A 1 224 ? 34.696 -7.741  16.856 1.00 24.97 ? 204 GLY A C     1 
ATOM   1503 O  O     . GLY A 1 224 ? 34.064 -8.675  16.352 1.00 30.02 ? 204 GLY A O     1 
ATOM   1504 N  N     . GLU A 1 225 ? 35.062 -7.745  18.132 1.00 19.09 ? 205 GLU A N     1 
ATOM   1505 C  CA    . GLU A 1 225 ? 34.793 -8.855  19.032 1.00 19.84 ? 205 GLU A CA    1 
ATOM   1506 C  C     . GLU A 1 225 ? 33.706 -8.498  20.040 1.00 24.73 ? 205 GLU A C     1 
ATOM   1507 O  O     . GLU A 1 225 ? 33.283 -7.344  20.177 1.00 21.10 ? 205 GLU A O     1 
ATOM   1508 C  CB    . GLU A 1 225 ? 36.085 -9.276  19.749 1.00 24.85 ? 205 GLU A CB    1 
ATOM   1509 C  CG    . GLU A 1 225 ? 37.237 -9.647  18.763 1.00 25.21 ? 205 GLU A CG    1 
ATOM   1510 C  CD    . GLU A 1 225 ? 38.571 -10.002 19.462 1.00 33.90 ? 205 GLU A CD    1 
ATOM   1511 O  OE1   . GLU A 1 225 ? 38.581 -10.203 20.694 1.00 35.37 ? 205 GLU A OE1   1 
ATOM   1512 O  OE2   . GLU A 1 225 ? 39.610 -10.071 18.761 1.00 32.79 ? 205 GLU A OE2   1 
ATOM   1513 N  N     . LYS A 1 226 ? 33.235 -9.531  20.739 1.00 25.89 ? 206 LYS A N     1 
ATOM   1514 C  CA    . LYS A 1 226 ? 32.145 -9.407  21.695 1.00 26.52 ? 206 LYS A CA    1 
ATOM   1515 C  C     . LYS A 1 226 ? 32.655 -9.864  23.053 1.00 29.11 ? 206 LYS A C     1 
ATOM   1516 O  O     . LYS A 1 226 ? 33.483 -10.769 23.140 1.00 29.43 ? 206 LYS A O     1 
ATOM   1517 C  CB    . LYS A 1 226 ? 30.915 -10.240 21.299 1.00 27.06 ? 206 LYS A CB    1 
ATOM   1518 C  CG    . LYS A 1 226 ? 30.295 -9.879  19.946 1.00 31.60 ? 206 LYS A CG    1 
ATOM   1519 C  CD    . LYS A 1 226 ? 29.313 -8.732  20.079 1.00 38.49 ? 206 LYS A CD    1 
ATOM   1520 N  N     . VAL A 1 227 ? 32.184 -9.211  24.104 1.00 26.68 ? 207 VAL A N     1 
ATOM   1521 C  CA    . VAL A 1 227 ? 32.447 -9.655  25.465 1.00 26.73 ? 207 VAL A CA    1 
ATOM   1522 C  C     . VAL A 1 227 ? 31.470 -10.767 25.805 1.00 28.00 ? 207 VAL A C     1 
ATOM   1523 O  O     . VAL A 1 227 ? 30.259 -10.613 25.617 1.00 28.88 ? 207 VAL A O     1 
ATOM   1524 C  CB    . VAL A 1 227 ? 32.306 -8.485  26.451 1.00 24.89 ? 207 VAL A CB    1 
ATOM   1525 C  CG1   . VAL A 1 227 ? 32.346 -8.990  27.872 1.00 28.93 ? 207 VAL A CG1   1 
ATOM   1526 C  CG2   . VAL A 1 227 ? 33.393 -7.459  26.208 1.00 28.93 ? 207 VAL A CG2   1 
ATOM   1527 N  N     . GLU A 1 228 ? 31.987 -11.883 26.309 1.00 32.20 ? 208 GLU A N     1 
ATOM   1528 C  CA    . GLU A 1 228 ? 31.118 -12.962 26.770 1.00 40.51 ? 208 GLU A CA    1 
ATOM   1529 C  C     . GLU A 1 228 ? 30.198 -12.457 27.879 1.00 37.97 ? 208 GLU A C     1 
ATOM   1530 O  O     . GLU A 1 228 ? 30.648 -11.821 28.831 1.00 37.24 ? 208 GLU A O     1 
ATOM   1531 C  CB    . GLU A 1 228 ? 31.959 -14.139 27.278 1.00 39.40 ? 208 GLU A CB    1 
ATOM   1532 N  N     . ALA A 1 229 ? 28.914 -12.762 27.763 1.00 35.87 ? 209 ALA A N     1 
ATOM   1533 C  CA    . ALA A 1 229 ? 27.919 -12.298 28.724 1.00 39.12 ? 209 ALA A CA    1 
ATOM   1534 C  C     . ALA A 1 229 ? 27.930 -13.115 30.030 1.00 42.64 ? 209 ALA A C     1 
ATOM   1535 O  O     . ALA A 1 229 ? 28.987 -13.492 30.551 1.00 53.33 ? 209 ALA A O     1 
ATOM   1536 C  CB    . ALA A 1 229 ? 26.555 -12.353 28.099 1.00 45.12 ? 209 ALA A CB    1 
HETATM 1537 P  PG    . ANP B 2 .   ? 29.512 7.614   49.278 1.00 39.39 ? 301 ANP A PG    1 
HETATM 1538 O  O1G   . ANP B 2 .   ? 30.859 6.960   49.320 1.00 32.04 ? 301 ANP A O1G   1 
HETATM 1539 O  O2G   . ANP B 2 .   ? 28.477 6.744   50.078 1.00 35.10 ? 301 ANP A O2G   1 
HETATM 1540 O  O3G   . ANP B 2 .   ? 29.517 9.073   49.863 1.00 42.03 ? 301 ANP A O3G   1 
HETATM 1541 P  PB    . ANP B 2 .   ? 28.849 6.573   46.679 1.00 22.67 ? 301 ANP A PB    1 
HETATM 1542 O  O1B   . ANP B 2 .   ? 27.672 6.968   45.825 1.00 30.12 ? 301 ANP A O1B   1 
HETATM 1543 O  O2B   . ANP B 2 .   ? 28.700 5.169   47.287 1.00 20.35 ? 301 ANP A O2B   1 
HETATM 1544 N  N3B   . ANP B 2 .   ? 29.080 7.868   47.651 1.00 26.00 ? 301 ANP A N3B   1 
HETATM 1545 P  PA    . ANP B 2 .   ? 30.367 5.322   44.653 1.00 18.75 ? 301 ANP A PA    1 
HETATM 1546 O  O1A   . ANP B 2 .   ? 30.704 4.102   45.403 1.00 15.38 ? 301 ANP A O1A   1 
HETATM 1547 O  O2A   . ANP B 2 .   ? 29.400 5.205   43.476 1.00 15.72 ? 301 ANP A O2A   1 
HETATM 1548 O  O3A   . ANP B 2 .   ? 30.034 6.534   45.615 1.00 17.35 ? 301 ANP A O3A   1 
HETATM 1549 O  "O5'" . ANP B 2 .   ? 31.712 5.824   43.961 1.00 18.34 ? 301 ANP A "O5'" 1 
HETATM 1550 C  "C5'" . ANP B 2 .   ? 32.982 5.924   44.640 1.00 14.97 ? 301 ANP A "C5'" 1 
HETATM 1551 C  "C4'" . ANP B 2 .   ? 34.009 6.390   43.647 1.00 18.29 ? 301 ANP A "C4'" 1 
HETATM 1552 O  "O4'" . ANP B 2 .   ? 33.668 7.722   43.205 1.00 17.84 ? 301 ANP A "O4'" 1 
HETATM 1553 C  "C3'" . ANP B 2 .   ? 35.431 6.506   44.189 1.00 17.52 ? 301 ANP A "C3'" 1 
HETATM 1554 O  "O3'" . ANP B 2 .   ? 36.069 5.236   44.133 1.00 19.40 ? 301 ANP A "O3'" 1 
HETATM 1555 C  "C2'" . ANP B 2 .   ? 36.043 7.547   43.252 1.00 16.76 ? 301 ANP A "C2'" 1 
HETATM 1556 O  "O2'" . ANP B 2 .   ? 36.397 6.974   42.015 1.00 15.25 ? 301 ANP A "O2'" 1 
HETATM 1557 C  "C1'" . ANP B 2 .   ? 34.848 8.455   42.940 1.00 18.61 ? 301 ANP A "C1'" 1 
HETATM 1558 N  N9    . ANP B 2 .   ? 34.812 9.678   43.722 1.00 16.74 ? 301 ANP A N9    1 
HETATM 1559 C  C8    . ANP B 2 .   ? 34.096 9.950   44.862 1.00 20.63 ? 301 ANP A C8    1 
HETATM 1560 N  N7    . ANP B 2 .   ? 34.267 11.169  45.318 1.00 18.86 ? 301 ANP A N7    1 
HETATM 1561 C  C5    . ANP B 2 .   ? 35.175 11.727  44.427 1.00 17.55 ? 301 ANP A C5    1 
HETATM 1562 C  C6    . ANP B 2 .   ? 35.790 12.993  44.361 1.00 18.36 ? 301 ANP A C6    1 
HETATM 1563 N  N6    . ANP B 2 .   ? 35.561 13.981  45.231 1.00 20.81 ? 301 ANP A N6    1 
HETATM 1564 N  N1    . ANP B 2 .   ? 36.633 13.227  43.333 1.00 18.74 ? 301 ANP A N1    1 
HETATM 1565 C  C2    . ANP B 2 .   ? 36.857 12.252  42.449 1.00 17.66 ? 301 ANP A C2    1 
HETATM 1566 N  N3    . ANP B 2 .   ? 36.349 11.021  42.415 1.00 17.07 ? 301 ANP A N3    1 
HETATM 1567 C  C4    . ANP B 2 .   ? 35.508 10.820  43.436 1.00 16.88 ? 301 ANP A C4    1 
HETATM 1568 MN MN    . MN  C 3 .   ? 30.003 3.419   47.329 1.00 16.89 ? 302 MN  A MN    1 
HETATM 1569 MN MN    . MN  D 3 .   ? 26.622 4.428   48.074 1.00 23.41 ? 303 MN  A MN    1 
HETATM 1570 O  O     . HOH E 4 .   ? 26.459 8.096   47.468 1.00 35.50 ? 401 HOH A O     1 
HETATM 1571 O  O     . HOH E 4 .   ? 44.084 14.877  30.463 1.00 31.02 ? 402 HOH A O     1 
HETATM 1572 O  O     . HOH E 4 .   ? 30.739 7.361   8.418  1.00 37.99 ? 403 HOH A O     1 
HETATM 1573 O  O     . HOH E 4 .   ? 26.792 11.115  29.589 1.00 32.33 ? 404 HOH A O     1 
HETATM 1574 O  O     . HOH E 4 .   ? 42.209 17.719  44.421 1.00 36.49 ? 405 HOH A O     1 
HETATM 1575 O  O     . HOH E 4 .   ? 31.406 4.699   48.381 1.00 19.69 ? 406 HOH A O     1 
HETATM 1576 O  O     . HOH E 4 .   ? 26.531 6.067   48.639 1.00 27.35 ? 407 HOH A O     1 
HETATM 1577 O  O     . HOH E 4 .   ? 39.344 -4.297  34.339 1.00 44.49 ? 408 HOH A O     1 
HETATM 1578 O  O     . HOH E 4 .   ? 26.078 -2.225  50.421 1.00 34.34 ? 409 HOH A O     1 
HETATM 1579 O  O     . HOH E 4 .   ? 18.118 8.691   37.167 1.00 36.46 ? 410 HOH A O     1 
HETATM 1580 O  O     . HOH E 4 .   ? 27.080 -1.914  32.479 1.00 27.78 ? 411 HOH A O     1 
HETATM 1581 O  O     . HOH E 4 .   ? 51.649 8.877   26.920 1.00 28.19 ? 412 HOH A O     1 
HETATM 1582 O  O     . HOH E 4 .   ? 48.380 -0.904  42.986 1.00 34.89 ? 413 HOH A O     1 
HETATM 1583 O  O     . HOH E 4 .   ? 54.129 5.844   41.294 1.00 28.78 ? 414 HOH A O     1 
HETATM 1584 O  O     . HOH E 4 .   ? 30.715 -2.800  52.629 1.00 18.90 ? 415 HOH A O     1 
HETATM 1585 O  O     . HOH E 4 .   ? 42.375 7.555   12.603 1.00 20.56 ? 416 HOH A O     1 
HETATM 1586 O  O     . HOH E 4 .   ? 20.925 7.548   18.133 1.00 20.22 ? 417 HOH A O     1 
HETATM 1587 O  O     . HOH E 4 .   ? 38.448 1.458   46.033 1.00 18.76 ? 418 HOH A O     1 
HETATM 1588 O  O     . HOH E 4 .   ? 34.571 -12.130 26.908 1.00 45.08 ? 419 HOH A O     1 
HETATM 1589 O  O     . HOH E 4 .   ? 42.692 -5.693  51.296 1.00 26.91 ? 420 HOH A O     1 
HETATM 1590 O  O     . HOH E 4 .   ? 25.746 14.685  14.062 1.00 31.98 ? 421 HOH A O     1 
HETATM 1591 O  O     . HOH E 4 .   ? 48.191 10.007  38.473 1.00 27.09 ? 422 HOH A O     1 
HETATM 1592 O  O     . HOH E 4 .   ? 35.859 8.480   29.502 1.00 32.28 ? 423 HOH A O     1 
HETATM 1593 O  O     . HOH E 4 .   ? 48.728 -1.339  50.152 1.00 33.32 ? 424 HOH A O     1 
HETATM 1594 O  O     . HOH E 4 .   ? 38.129 -8.241  45.984 1.00 33.63 ? 425 HOH A O     1 
HETATM 1595 O  O     . HOH E 4 .   ? 52.236 11.858  29.893 1.00 35.24 ? 426 HOH A O     1 
HETATM 1596 O  O     . HOH E 4 .   ? 35.544 13.518  11.714 1.00 38.09 ? 427 HOH A O     1 
HETATM 1597 O  O     . HOH E 4 .   ? 35.416 21.897  40.178 1.00 29.23 ? 428 HOH A O     1 
HETATM 1598 O  O     . HOH E 4 .   ? 27.903 -6.966  44.511 1.00 35.02 ? 429 HOH A O     1 
HETATM 1599 O  O     . HOH E 4 .   ? 24.612 -5.350  16.296 1.00 29.69 ? 430 HOH A O     1 
HETATM 1600 O  O     . HOH E 4 .   ? 28.487 -8.862  24.531 1.00 29.31 ? 431 HOH A O     1 
HETATM 1601 O  O     . HOH E 4 .   ? 46.817 10.336  13.842 1.00 33.69 ? 432 HOH A O     1 
HETATM 1602 O  O     . HOH E 4 .   ? 36.774 4.452   54.161 1.00 21.44 ? 433 HOH A O     1 
HETATM 1603 O  O     . HOH E 4 .   ? 51.548 2.215   38.172 1.00 28.89 ? 434 HOH A O     1 
HETATM 1604 O  O     . HOH E 4 .   ? 19.967 0.738   34.592 1.00 32.64 ? 435 HOH A O     1 
HETATM 1605 O  O     . HOH E 4 .   ? 31.456 -5.811  18.840 1.00 25.23 ? 436 HOH A O     1 
HETATM 1606 O  O     . HOH E 4 .   ? 44.926 -5.871  22.720 1.00 44.96 ? 437 HOH A O     1 
HETATM 1607 O  O     . HOH E 4 .   ? 43.995 10.480  13.282 1.00 37.76 ? 438 HOH A O     1 
HETATM 1608 O  O     . HOH E 4 .   ? 22.312 13.765  35.525 1.00 26.07 ? 439 HOH A O     1 
HETATM 1609 O  O     . HOH E 4 .   ? 37.422 22.918  44.242 1.00 36.77 ? 440 HOH A O     1 
HETATM 1610 O  O     . HOH E 4 .   ? 25.602 5.211   46.217 1.00 24.95 ? 441 HOH A O     1 
HETATM 1611 O  O     . HOH E 4 .   ? 49.413 -1.220  32.315 1.00 27.02 ? 442 HOH A O     1 
HETATM 1612 O  O     . HOH E 4 .   ? 49.119 8.838   31.123 1.00 21.24 ? 443 HOH A O     1 
HETATM 1613 O  O     . HOH E 4 .   ? 39.819 9.344   29.532 1.00 21.40 ? 444 HOH A O     1 
HETATM 1614 O  O     . HOH E 4 .   ? 27.060 13.338  20.834 1.00 17.93 ? 445 HOH A O     1 
HETATM 1615 O  O     . HOH E 4 .   ? 33.556 12.677  47.506 1.00 40.01 ? 446 HOH A O     1 
HETATM 1616 O  O     . HOH E 4 .   ? 49.642 5.899   12.155 1.00 36.49 ? 447 HOH A O     1 
HETATM 1617 O  O     . HOH E 4 .   ? 27.263 -9.483  33.698 1.00 35.34 ? 448 HOH A O     1 
HETATM 1618 O  O     . HOH E 4 .   ? 43.946 12.069  47.325 1.00 21.76 ? 449 HOH A O     1 
HETATM 1619 O  O     . HOH E 4 .   ? 48.257 -0.694  14.201 1.00 30.39 ? 450 HOH A O     1 
HETATM 1620 O  O     . HOH E 4 .   ? 46.368 -2.690  26.235 1.00 33.38 ? 451 HOH A O     1 
HETATM 1621 O  O     . HOH E 4 .   ? 32.342 -4.285  16.648 1.00 19.73 ? 452 HOH A O     1 
HETATM 1622 O  O     . HOH E 4 .   ? 25.022 13.375  36.077 1.00 19.91 ? 453 HOH A O     1 
HETATM 1623 O  O     . HOH E 4 .   ? 28.292 7.175   9.047  1.00 26.34 ? 454 HOH A O     1 
HETATM 1624 O  O     . HOH E 4 .   ? 28.841 -5.343  15.127 1.00 29.99 ? 455 HOH A O     1 
HETATM 1625 O  O     . HOH E 4 .   ? 49.632 6.469   49.837 1.00 20.81 ? 456 HOH A O     1 
HETATM 1626 O  O     . HOH E 4 .   ? 31.176 20.359  33.743 1.00 18.21 ? 457 HOH A O     1 
HETATM 1627 O  O     . HOH E 4 .   ? 17.640 -2.588  32.997 1.00 46.27 ? 458 HOH A O     1 
HETATM 1628 O  O     . HOH E 4 .   ? 51.911 6.096   33.518 1.00 26.61 ? 459 HOH A O     1 
HETATM 1629 O  O     . HOH E 4 .   ? 45.379 -3.245  14.880 1.00 35.93 ? 460 HOH A O     1 
HETATM 1630 O  O     . HOH E 4 .   ? 34.195 -9.924  30.881 1.00 32.53 ? 461 HOH A O     1 
HETATM 1631 O  O     . HOH E 4 .   ? 33.766 20.003  23.221 1.00 32.19 ? 462 HOH A O     1 
HETATM 1632 O  O     . HOH E 4 .   ? 51.938 4.195   16.078 1.00 40.10 ? 463 HOH A O     1 
HETATM 1633 O  O     . HOH E 4 .   ? 46.416 -3.557  54.173 1.00 36.75 ? 464 HOH A O     1 
HETATM 1634 O  O     . HOH E 4 .   ? 39.539 -9.522  15.977 1.00 32.58 ? 465 HOH A O     1 
HETATM 1635 O  O     . HOH E 4 .   ? 49.368 6.714   33.013 1.00 19.00 ? 466 HOH A O     1 
HETATM 1636 O  O     . HOH E 4 .   ? 35.691 15.892  47.876 1.00 38.01 ? 467 HOH A O     1 
HETATM 1637 O  O     . HOH E 4 .   ? 46.667 -1.484  57.075 1.00 27.34 ? 468 HOH A O     1 
HETATM 1638 O  O     . HOH E 4 .   ? 37.357 10.780  29.322 1.00 24.22 ? 469 HOH A O     1 
HETATM 1639 O  O     . HOH E 4 .   ? 38.540 -4.457  13.563 1.00 29.62 ? 470 HOH A O     1 
HETATM 1640 O  O     . HOH E 4 .   ? 42.334 14.981  12.579 1.00 40.83 ? 471 HOH A O     1 
HETATM 1641 O  O     . HOH E 4 .   ? 46.727 13.872  19.191 1.00 35.99 ? 472 HOH A O     1 
HETATM 1642 O  O     . HOH E 4 .   ? 27.692 -4.854  19.697 1.00 27.12 ? 473 HOH A O     1 
HETATM 1643 O  O     . HOH E 4 .   ? 25.413 10.853  8.964  1.00 33.32 ? 474 HOH A O     1 
HETATM 1644 O  O     . HOH E 4 .   ? 34.575 19.645  27.646 1.00 24.67 ? 475 HOH A O     1 
HETATM 1645 O  O     . HOH E 4 .   ? 48.701 6.392   54.924 1.00 25.13 ? 476 HOH A O     1 
HETATM 1646 O  O     . HOH E 4 .   ? 39.743 18.297  24.042 1.00 29.46 ? 477 HOH A O     1 
HETATM 1647 O  O     . HOH E 4 .   ? 26.649 15.195  25.466 1.00 20.87 ? 478 HOH A O     1 
HETATM 1648 O  O     . HOH E 4 .   ? 42.377 8.584   52.395 1.00 20.64 ? 479 HOH A O     1 
HETATM 1649 O  O     . HOH E 4 .   ? 49.500 0.270   21.397 1.00 28.78 ? 480 HOH A O     1 
HETATM 1650 O  O     . HOH E 4 .   ? 20.147 11.436  18.836 1.00 32.30 ? 481 HOH A O     1 
HETATM 1651 O  O     . HOH E 4 .   ? 36.325 3.343   46.598 1.00 19.40 ? 482 HOH A O     1 
HETATM 1652 O  O     . HOH E 4 .   ? 18.550 8.693   25.151 1.00 33.17 ? 483 HOH A O     1 
HETATM 1653 O  O     . HOH E 4 .   ? 32.421 -4.528  49.150 1.00 26.89 ? 484 HOH A O     1 
HETATM 1654 O  O     . HOH E 4 .   ? 39.895 -5.831  26.033 1.00 24.60 ? 485 HOH A O     1 
HETATM 1655 O  O     . HOH E 4 .   ? 32.682 -9.395  39.169 1.00 24.98 ? 486 HOH A O     1 
HETATM 1656 O  O     . HOH E 4 .   ? 47.538 7.557   39.525 1.00 28.73 ? 487 HOH A O     1 
HETATM 1657 O  O     . HOH E 4 .   ? 31.408 20.816  29.527 1.00 32.45 ? 488 HOH A O     1 
HETATM 1658 O  O     . HOH E 4 .   ? 27.634 19.300  27.375 1.00 23.30 ? 489 HOH A O     1 
HETATM 1659 O  O     . HOH E 4 .   ? 26.993 14.783  10.824 1.00 31.94 ? 490 HOH A O     1 
HETATM 1660 O  O     . HOH E 4 .   ? 32.688 18.825  25.623 1.00 27.25 ? 491 HOH A O     1 
HETATM 1661 O  O     . HOH E 4 .   ? 26.036 4.484   52.167 1.00 37.81 ? 492 HOH A O     1 
HETATM 1662 O  O     . HOH E 4 .   ? 29.477 -8.893  38.488 1.00 31.28 ? 493 HOH A O     1 
HETATM 1663 O  O     . HOH E 4 .   ? 21.672 14.376  24.461 1.00 35.74 ? 494 HOH A O     1 
HETATM 1664 O  O     . HOH E 4 .   ? 32.198 13.701  10.432 1.00 29.72 ? 495 HOH A O     1 
HETATM 1665 O  O     . HOH E 4 .   ? 26.278 -7.847  37.169 1.00 36.40 ? 496 HOH A O     1 
HETATM 1666 O  O     . HOH E 4 .   ? 32.737 17.428  45.461 1.00 21.78 ? 497 HOH A O     1 
HETATM 1667 O  O     . HOH E 4 .   ? 41.306 11.379  9.280  1.00 39.99 ? 498 HOH A O     1 
HETATM 1668 O  O     . HOH E 4 .   ? 31.146 18.112  16.774 1.00 32.15 ? 499 HOH A O     1 
HETATM 1669 O  O     . HOH E 4 .   ? 29.670 18.222  42.649 1.00 25.76 ? 500 HOH A O     1 
HETATM 1670 O  O     . HOH E 4 .   ? 26.753 -7.972  22.035 1.00 37.60 ? 501 HOH A O     1 
HETATM 1671 O  O     . HOH E 4 .   ? 44.304 10.572  51.479 1.00 20.90 ? 502 HOH A O     1 
HETATM 1672 O  O     . HOH E 4 .   ? 19.784 3.739   36.146 1.00 38.11 ? 503 HOH A O     1 
HETATM 1673 O  O     . HOH E 4 .   ? 26.093 14.956  22.757 1.00 22.94 ? 504 HOH A O     1 
HETATM 1674 O  O     . HOH E 4 .   ? 34.992 -10.385 37.712 1.00 38.73 ? 505 HOH A O     1 
HETATM 1675 O  O     . HOH E 4 .   ? 36.779 -9.146  32.377 1.00 41.10 ? 506 HOH A O     1 
HETATM 1676 O  O     . HOH E 4 .   ? 24.612 3.947   49.000 1.00 25.89 ? 507 HOH A O     1 
HETATM 1677 O  O     . HOH E 4 .   ? 42.920 -3.877  44.274 1.00 20.62 ? 508 HOH A O     1 
HETATM 1678 O  O     . HOH E 4 .   ? 22.537 14.503  26.797 1.00 35.03 ? 509 HOH A O     1 
HETATM 1679 O  O     . HOH E 4 .   ? 37.652 13.044  12.720 1.00 27.02 ? 510 HOH A O     1 
HETATM 1680 O  O     . HOH E 4 .   ? 25.484 -4.983  39.374 1.00 36.41 ? 511 HOH A O     1 
HETATM 1681 O  O     . HOH E 4 .   ? 30.604 19.203  27.576 1.00 28.99 ? 512 HOH A O     1 
HETATM 1682 O  O     . HOH E 4 .   ? 54.744 2.914   46.179 1.00 38.94 ? 513 HOH A O     1 
HETATM 1683 O  O     . HOH E 4 .   ? 48.691 3.412   13.257 1.00 34.05 ? 514 HOH A O     1 
HETATM 1684 O  O     . HOH E 4 .   ? 34.761 18.088  16.517 1.00 47.97 ? 515 HOH A O     1 
HETATM 1685 O  O     . HOH E 4 .   ? 22.694 9.330   42.786 1.00 34.76 ? 516 HOH A O     1 
HETATM 1686 O  O     . HOH E 4 .   ? 44.370 14.905  19.564 1.00 40.91 ? 517 HOH A O     1 
HETATM 1687 O  O     . HOH E 4 .   ? 45.595 17.646  38.226 1.00 38.68 ? 518 HOH A O     1 
HETATM 1688 O  O     . HOH E 4 .   ? 24.811 -3.708  30.443 1.00 33.31 ? 519 HOH A O     1 
HETATM 1689 O  O     . HOH E 4 .   ? 34.058 24.246  37.435 1.00 31.70 ? 520 HOH A O     1 
HETATM 1690 O  O     . HOH E 4 .   ? 46.854 -0.964  47.402 1.00 36.31 ? 521 HOH A O     1 
HETATM 1691 O  O     . HOH E 4 .   ? 43.085 -3.821  39.250 1.00 39.13 ? 522 HOH A O     1 
HETATM 1692 O  O     . HOH E 4 .   ? 50.877 1.041   45.784 1.00 49.75 ? 523 HOH A O     1 
HETATM 1693 O  O     . HOH E 4 .   ? 52.872 2.969   40.466 1.00 36.90 ? 524 HOH A O     1 
HETATM 1694 O  O     . HOH E 4 .   ? 52.176 5.876   49.272 1.00 38.22 ? 525 HOH A O     1 
HETATM 1695 O  O     . HOH E 4 .   ? 50.473 10.646  33.065 1.00 37.74 ? 526 HOH A O     1 
HETATM 1696 O  O     . HOH E 4 .   ? 30.720 16.369  43.873 1.00 35.64 ? 527 HOH A O     1 
HETATM 1697 O  O     . HOH E 4 .   ? 34.446 23.927  41.051 1.00 34.08 ? 528 HOH A O     1 
HETATM 1698 O  O     . HOH E 4 .   ? 43.522 9.539   10.868 1.00 39.90 ? 529 HOH A O     1 
HETATM 1699 O  O     . HOH E 4 .   ? 29.003 -6.647  18.174 1.00 33.97 ? 530 HOH A O     1 
HETATM 1700 O  O     . HOH E 4 .   ? 37.180 -9.157  48.395 1.00 34.37 ? 531 HOH A O     1 
HETATM 1701 O  O     . HOH E 4 .   ? 36.827 20.680  26.742 1.00 37.56 ? 532 HOH A O     1 
HETATM 1702 O  O     . HOH E 4 .   ? 51.315 8.964   29.641 1.00 30.71 ? 533 HOH A O     1 
HETATM 1703 O  O     . HOH E 4 .   ? 25.893 17.861  26.263 1.00 22.28 ? 534 HOH A O     1 
HETATM 1704 O  O     . HOH E 4 .   ? 40.773 -7.122  23.650 1.00 28.46 ? 535 HOH A O     1 
HETATM 1705 O  O     . HOH E 4 .   ? 42.014 -4.968  27.555 1.00 35.52 ? 536 HOH A O     1 
HETATM 1706 O  O     . HOH E 4 .   ? 23.522 17.102  27.828 1.00 21.64 ? 537 HOH A O     1 
HETATM 1707 O  O     . HOH E 4 .   ? 25.216 -5.622  19.654 1.00 45.14 ? 538 HOH A O     1 
HETATM 1708 O  O     . HOH E 4 .   ? 51.847 -0.270  37.242 1.00 32.73 ? 539 HOH A O     1 
HETATM 1709 O  O     . HOH E 4 .   ? 42.849 12.423  49.926 1.00 23.79 ? 540 HOH A O     1 
HETATM 1710 O  O     . HOH E 4 .   ? 31.748 18.582  48.020 1.00 36.83 ? 541 HOH A O     1 
HETATM 1711 O  O     . HOH E 4 .   ? 42.925 16.678  15.005 1.00 43.22 ? 542 HOH A O     1 
HETATM 1712 O  O     . HOH E 4 .   ? 42.360 -4.885  41.513 1.00 45.01 ? 543 HOH A O     1 
# 
