data_8RUO
# 
_entry.id   8RUO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8RUO         pdb_00008ruo 10.2210/pdb8ruo/pdb 
WWPDB D_1292136252 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RUO 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              a.guskov@rug.nl 
_pdbx_contact_author.name_first         Albert 
_pdbx_contact_author.name_last          Guskov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2340-2216 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wiedemann, C.'   1 0000-0003-4351-8857 
'Whittaker, J.J.' 2 0000-0001-8966-111X 
'Guskov, A.'      3 0000-0003-2340-2216 
'Hellmich, U.A.'  4 0000-0001-7162-285X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of the LpMIP mutant D44E' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wiedemann, C.'   1 0000-0003-4351-8857 
primary 'Whittaker, J.J.' 2 0000-0001-8966-111X 
primary 'Guskov, A.'      3 0000-0003-2340-2216 
primary 'Hellmich, U.A.'  4 0000-0001-7162-285X 
# 
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 'Outer membrane protein MIP'           22152.273 1  5.2.1.8 ? ? ? 
2 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1  ?       ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                106.120   3  ?       ? ? ? 
4 water       nat water                                  18.015    37 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Macrophage infectivity potentiator,Peptidyl-prolyl cis-trans isomerase,PPIase,Rotamase' 
# 
_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       
;TDKDKLSYSIGADLGKNFKNQGIDVNPEAMAKGMQEAMSGAQLALTEQQMKDVLNKFQKDLMAKRTAEFNKKADENKVKG
EAFLTENKNKPGVVVLPSGLQYKVINSGNGVKPGKSDTVTVEYTGRLIDGTVFDSTEKTGKPATFQVSQVIPGWTEALQL
MPAGSTWEIYVPSGLAYGPRSVGGPIGPNETLIFKIHLISVKKSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TDKDKLSYSIGADLGKNFKNQGIDVNPEAMAKGMQEAMSGAQLALTEQQMKDVLNKFQKDLMAKRTAEFNKKADENKVKG
EAFLTENKNKPGVVVLPSGLQYKVINSGNGVKPGKSDTVTVEYTGRLIDGTVFDSTEKTGKPATFQVSQVIPGWTEALQL
MPAGSTWEIYVPSGLAYGPRSVGGPIGPNETLIFKIHLISVKKSS
;
_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 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
3 'DI(HYDROXYETHYL)ETHER'                PEG 
4 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ASP n 
1 3   LYS n 
1 4   ASP n 
1 5   LYS n 
1 6   LEU n 
1 7   SER n 
1 8   TYR n 
1 9   SER n 
1 10  ILE n 
1 11  GLY n 
1 12  ALA n 
1 13  ASP n 
1 14  LEU n 
1 15  GLY n 
1 16  LYS n 
1 17  ASN n 
1 18  PHE n 
1 19  LYS n 
1 20  ASN n 
1 21  GLN n 
1 22  GLY n 
1 23  ILE n 
1 24  ASP n 
1 25  VAL n 
1 26  ASN n 
1 27  PRO n 
1 28  GLU n 
1 29  ALA n 
1 30  MET n 
1 31  ALA n 
1 32  LYS n 
1 33  GLY n 
1 34  MET n 
1 35  GLN n 
1 36  GLU n 
1 37  ALA n 
1 38  MET n 
1 39  SER n 
1 40  GLY n 
1 41  ALA n 
1 42  GLN n 
1 43  LEU n 
1 44  ALA n 
1 45  LEU n 
1 46  THR n 
1 47  GLU n 
1 48  GLN n 
1 49  GLN n 
1 50  MET n 
1 51  LYS n 
1 52  ASP n 
1 53  VAL n 
1 54  LEU n 
1 55  ASN n 
1 56  LYS n 
1 57  PHE n 
1 58  GLN n 
1 59  LYS n 
1 60  ASP n 
1 61  LEU n 
1 62  MET n 
1 63  ALA n 
1 64  LYS n 
1 65  ARG n 
1 66  THR n 
1 67  ALA n 
1 68  GLU n 
1 69  PHE n 
1 70  ASN n 
1 71  LYS n 
1 72  LYS n 
1 73  ALA n 
1 74  ASP n 
1 75  GLU n 
1 76  ASN n 
1 77  LYS n 
1 78  VAL n 
1 79  LYS n 
1 80  GLY n 
1 81  GLU n 
1 82  ALA n 
1 83  PHE n 
1 84  LEU n 
1 85  THR n 
1 86  GLU n 
1 87  ASN n 
1 88  LYS n 
1 89  ASN n 
1 90  LYS n 
1 91  PRO n 
1 92  GLY n 
1 93  VAL n 
1 94  VAL n 
1 95  VAL n 
1 96  LEU n 
1 97  PRO n 
1 98  SER n 
1 99  GLY n 
1 100 LEU n 
1 101 GLN n 
1 102 TYR n 
1 103 LYS n 
1 104 VAL n 
1 105 ILE n 
1 106 ASN n 
1 107 SER n 
1 108 GLY n 
1 109 ASN n 
1 110 GLY n 
1 111 VAL n 
1 112 LYS n 
1 113 PRO n 
1 114 GLY n 
1 115 LYS n 
1 116 SER n 
1 117 ASP n 
1 118 THR n 
1 119 VAL n 
1 120 THR n 
1 121 VAL n 
1 122 GLU n 
1 123 TYR n 
1 124 THR n 
1 125 GLY n 
1 126 ARG n 
1 127 LEU n 
1 128 ILE n 
1 129 ASP n 
1 130 GLY n 
1 131 THR n 
1 132 VAL n 
1 133 PHE n 
1 134 ASP n 
1 135 SER n 
1 136 THR n 
1 137 GLU n 
1 138 LYS n 
1 139 THR n 
1 140 GLY n 
1 141 LYS n 
1 142 PRO n 
1 143 ALA n 
1 144 THR n 
1 145 PHE n 
1 146 GLN n 
1 147 VAL n 
1 148 SER n 
1 149 GLN n 
1 150 VAL n 
1 151 ILE n 
1 152 PRO n 
1 153 GLY n 
1 154 TRP n 
1 155 THR n 
1 156 GLU n 
1 157 ALA n 
1 158 LEU n 
1 159 GLN n 
1 160 LEU n 
1 161 MET n 
1 162 PRO n 
1 163 ALA n 
1 164 GLY n 
1 165 SER n 
1 166 THR n 
1 167 TRP n 
1 168 GLU n 
1 169 ILE n 
1 170 TYR n 
1 171 VAL n 
1 172 PRO n 
1 173 SER n 
1 174 GLY n 
1 175 LEU n 
1 176 ALA n 
1 177 TYR n 
1 178 GLY n 
1 179 PRO n 
1 180 ARG n 
1 181 SER n 
1 182 VAL n 
1 183 GLY n 
1 184 GLY n 
1 185 PRO n 
1 186 ILE n 
1 187 GLY n 
1 188 PRO n 
1 189 ASN n 
1 190 GLU n 
1 191 THR n 
1 192 LEU n 
1 193 ILE n 
1 194 PHE n 
1 195 LYS n 
1 196 ILE n 
1 197 HIS n 
1 198 LEU n 
1 199 ILE n 
1 200 SER n 
1 201 VAL n 
1 202 LYS n 
1 203 LYS n 
1 204 SER n 
1 205 SER 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                   205 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mip 
_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      'Legionella pneumophila' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     446 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                        ? 'C4 H7 N O4'     133.103 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ? 'C6 H13 N O4 S'  195.237 
MET 'L-peptide linking' y METHIONINE                             ? 'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                ? 'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE                          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   9   9   THR THR A . n 
A 1 2   ASP 2   10  10  ASP ASP A . n 
A 1 3   LYS 3   11  11  LYS LYS A . n 
A 1 4   ASP 4   12  12  ASP ASP A . n 
A 1 5   LYS 5   13  13  LYS LYS A . n 
A 1 6   LEU 6   14  14  LEU LEU A . n 
A 1 7   SER 7   15  15  SER SER A . n 
A 1 8   TYR 8   16  16  TYR TYR A . n 
A 1 9   SER 9   17  17  SER SER A . n 
A 1 10  ILE 10  18  18  ILE ILE A . n 
A 1 11  GLY 11  19  19  GLY GLY A . n 
A 1 12  ALA 12  20  20  ALA ALA A . n 
A 1 13  ASP 13  21  21  ASP ASP A . n 
A 1 14  LEU 14  22  22  LEU LEU A . n 
A 1 15  GLY 15  23  23  GLY GLY A . n 
A 1 16  LYS 16  24  24  LYS LYS A . n 
A 1 17  ASN 17  25  25  ASN ASN A . n 
A 1 18  PHE 18  26  26  PHE PHE A . n 
A 1 19  LYS 19  27  27  LYS LYS A . n 
A 1 20  ASN 20  28  28  ASN ASN A . n 
A 1 21  GLN 21  29  29  GLN GLN A . n 
A 1 22  GLY 22  30  30  GLY GLY A . n 
A 1 23  ILE 23  31  31  ILE ILE A . n 
A 1 24  ASP 24  32  32  ASP ASP A . n 
A 1 25  VAL 25  33  33  VAL VAL A . n 
A 1 26  ASN 26  34  34  ASN ASN A . n 
A 1 27  PRO 27  35  35  PRO PRO A . n 
A 1 28  GLU 28  36  36  GLU GLU A . n 
A 1 29  ALA 29  37  37  ALA ALA A . n 
A 1 30  MET 30  38  38  MET MET A . n 
A 1 31  ALA 31  39  39  ALA ALA A . n 
A 1 32  LYS 32  40  40  LYS LYS A . n 
A 1 33  GLY 33  41  41  GLY GLY A . n 
A 1 34  MET 34  42  42  MET MET A . n 
A 1 35  GLN 35  43  43  GLN GLN A . n 
A 1 36  GLU 36  44  44  GLU GLU A . n 
A 1 37  ALA 37  45  45  ALA ALA A . n 
A 1 38  MET 38  46  46  MET MET A . n 
A 1 39  SER 39  47  47  SER SER A . n 
A 1 40  GLY 40  48  48  GLY GLY A . n 
A 1 41  ALA 41  49  49  ALA ALA A . n 
A 1 42  GLN 42  50  50  GLN GLN A . n 
A 1 43  LEU 43  51  51  LEU LEU A . n 
A 1 44  ALA 44  52  52  ALA ALA A . n 
A 1 45  LEU 45  53  53  LEU LEU A . n 
A 1 46  THR 46  54  54  THR THR A . n 
A 1 47  GLU 47  55  55  GLU GLU A . n 
A 1 48  GLN 48  56  56  GLN GLN A . n 
A 1 49  GLN 49  57  57  GLN GLN A . n 
A 1 50  MET 50  58  58  MET MET A . n 
A 1 51  LYS 51  59  59  LYS LYS A . n 
A 1 52  ASP 52  60  60  ASP ASP A . n 
A 1 53  VAL 53  61  61  VAL VAL A . n 
A 1 54  LEU 54  62  62  LEU LEU A . n 
A 1 55  ASN 55  63  63  ASN ASN A . n 
A 1 56  LYS 56  64  64  LYS LYS A . n 
A 1 57  PHE 57  65  65  PHE PHE A . n 
A 1 58  GLN 58  66  66  GLN GLN A . n 
A 1 59  LYS 59  67  67  LYS LYS A . n 
A 1 60  ASP 60  68  68  ASP ASP A . n 
A 1 61  LEU 61  69  69  LEU LEU A . n 
A 1 62  MET 62  70  70  MET MET A . n 
A 1 63  ALA 63  71  71  ALA ALA A . n 
A 1 64  LYS 64  72  72  LYS LYS A . n 
A 1 65  ARG 65  73  73  ARG ARG A . n 
A 1 66  THR 66  74  74  THR THR A . n 
A 1 67  ALA 67  75  75  ALA ALA A . n 
A 1 68  GLU 68  76  76  GLU GLU A . n 
A 1 69  PHE 69  77  77  PHE PHE A . n 
A 1 70  ASN 70  78  78  ASN ASN A . n 
A 1 71  LYS 71  79  79  LYS LYS A . n 
A 1 72  LYS 72  80  80  LYS LYS A . n 
A 1 73  ALA 73  81  81  ALA ALA A . n 
A 1 74  ASP 74  82  82  ASP ASP A . n 
A 1 75  GLU 75  83  83  GLU GLU A . n 
A 1 76  ASN 76  84  84  ASN ASN A . n 
A 1 77  LYS 77  85  85  LYS LYS A . n 
A 1 78  VAL 78  86  86  VAL VAL A . n 
A 1 79  LYS 79  87  87  LYS LYS A . n 
A 1 80  GLY 80  88  88  GLY GLY A . n 
A 1 81  GLU 81  89  89  GLU GLU A . n 
A 1 82  ALA 82  90  90  ALA ALA A . n 
A 1 83  PHE 83  91  91  PHE PHE A . n 
A 1 84  LEU 84  92  92  LEU LEU A . n 
A 1 85  THR 85  93  93  THR THR A . n 
A 1 86  GLU 86  94  94  GLU GLU A . n 
A 1 87  ASN 87  95  95  ASN ASN A . n 
A 1 88  LYS 88  96  96  LYS LYS A . n 
A 1 89  ASN 89  97  97  ASN ASN A . n 
A 1 90  LYS 90  98  98  LYS LYS A . n 
A 1 91  PRO 91  99  99  PRO PRO A . n 
A 1 92  GLY 92  100 100 GLY GLY A . n 
A 1 93  VAL 93  101 101 VAL VAL A . n 
A 1 94  VAL 94  102 102 VAL VAL A . n 
A 1 95  VAL 95  103 103 VAL VAL A . n 
A 1 96  LEU 96  104 104 LEU LEU A . n 
A 1 97  PRO 97  105 105 PRO PRO A . n 
A 1 98  SER 98  106 106 SER SER A . n 
A 1 99  GLY 99  107 107 GLY GLY A . n 
A 1 100 LEU 100 108 108 LEU LEU A . n 
A 1 101 GLN 101 109 109 GLN GLN A . n 
A 1 102 TYR 102 110 110 TYR TYR A . n 
A 1 103 LYS 103 111 111 LYS LYS A . n 
A 1 104 VAL 104 112 112 VAL VAL A . n 
A 1 105 ILE 105 113 113 ILE ILE A . n 
A 1 106 ASN 106 114 114 ASN ASN A . n 
A 1 107 SER 107 115 115 SER SER A . n 
A 1 108 GLY 108 116 116 GLY GLY A . n 
A 1 109 ASN 109 117 117 ASN ASN A . n 
A 1 110 GLY 110 118 118 GLY GLY A . n 
A 1 111 VAL 111 119 119 VAL VAL A . n 
A 1 112 LYS 112 120 120 LYS LYS A . n 
A 1 113 PRO 113 121 121 PRO PRO A . n 
A 1 114 GLY 114 122 122 GLY GLY A . n 
A 1 115 LYS 115 123 123 LYS LYS A . n 
A 1 116 SER 116 124 124 SER SER A . n 
A 1 117 ASP 117 125 125 ASP ASP A . n 
A 1 118 THR 118 126 126 THR THR A . n 
A 1 119 VAL 119 127 127 VAL VAL A . n 
A 1 120 THR 120 128 128 THR THR A . n 
A 1 121 VAL 121 129 129 VAL VAL A . n 
A 1 122 GLU 122 130 130 GLU GLU A . n 
A 1 123 TYR 123 131 131 TYR TYR A . n 
A 1 124 THR 124 132 132 THR THR A . n 
A 1 125 GLY 125 133 133 GLY GLY A . n 
A 1 126 ARG 126 134 134 ARG ARG A . n 
A 1 127 LEU 127 135 135 LEU LEU A . n 
A 1 128 ILE 128 136 136 ILE ILE A . n 
A 1 129 ASP 129 137 137 ASP ASP A . n 
A 1 130 GLY 130 138 138 GLY GLY A . n 
A 1 131 THR 131 139 139 THR THR A . n 
A 1 132 VAL 132 140 140 VAL VAL A . n 
A 1 133 PHE 133 141 141 PHE PHE A . n 
A 1 134 ASP 134 142 142 ASP ASP A . n 
A 1 135 SER 135 143 143 SER SER A . n 
A 1 136 THR 136 144 144 THR THR A . n 
A 1 137 GLU 137 145 145 GLU GLU A . n 
A 1 138 LYS 138 146 146 LYS LYS A . n 
A 1 139 THR 139 147 147 THR THR A . n 
A 1 140 GLY 140 148 148 GLY GLY A . n 
A 1 141 LYS 141 149 149 LYS LYS A . n 
A 1 142 PRO 142 150 150 PRO PRO A . n 
A 1 143 ALA 143 151 151 ALA ALA A . n 
A 1 144 THR 144 152 152 THR THR A . n 
A 1 145 PHE 145 153 153 PHE PHE A . n 
A 1 146 GLN 146 154 154 GLN GLN A . n 
A 1 147 VAL 147 155 155 VAL VAL A . n 
A 1 148 SER 148 156 156 SER SER A . n 
A 1 149 GLN 149 157 157 GLN GLN A . n 
A 1 150 VAL 150 158 158 VAL VAL A . n 
A 1 151 ILE 151 159 159 ILE ILE A . n 
A 1 152 PRO 152 160 160 PRO PRO A . n 
A 1 153 GLY 153 161 161 GLY GLY A . n 
A 1 154 TRP 154 162 162 TRP TRP A . n 
A 1 155 THR 155 163 163 THR THR A . n 
A 1 156 GLU 156 164 164 GLU GLU A . n 
A 1 157 ALA 157 165 165 ALA ALA A . n 
A 1 158 LEU 158 166 166 LEU LEU A . n 
A 1 159 GLN 159 167 167 GLN GLN A . n 
A 1 160 LEU 160 168 168 LEU LEU A . n 
A 1 161 MET 161 169 169 MET MET A . n 
A 1 162 PRO 162 170 170 PRO PRO A . n 
A 1 163 ALA 163 171 171 ALA ALA A . n 
A 1 164 GLY 164 172 172 GLY GLY A . n 
A 1 165 SER 165 173 173 SER SER A . n 
A 1 166 THR 166 174 174 THR THR A . n 
A 1 167 TRP 167 175 175 TRP TRP A . n 
A 1 168 GLU 168 176 176 GLU GLU A . n 
A 1 169 ILE 169 177 177 ILE ILE A . n 
A 1 170 TYR 170 178 178 TYR TYR A . n 
A 1 171 VAL 171 179 179 VAL VAL A . n 
A 1 172 PRO 172 180 180 PRO PRO A . n 
A 1 173 SER 173 181 181 SER SER A . n 
A 1 174 GLY 174 182 182 GLY GLY A . n 
A 1 175 LEU 175 183 183 LEU LEU A . n 
A 1 176 ALA 176 184 184 ALA ALA A . n 
A 1 177 TYR 177 185 185 TYR TYR A . n 
A 1 178 GLY 178 186 186 GLY GLY A . n 
A 1 179 PRO 179 187 187 PRO PRO A . n 
A 1 180 ARG 180 188 188 ARG ARG A . n 
A 1 181 SER 181 189 189 SER SER A . n 
A 1 182 VAL 182 190 190 VAL VAL A . n 
A 1 183 GLY 183 191 191 GLY GLY A . n 
A 1 184 GLY 184 192 192 GLY GLY A . n 
A 1 185 PRO 185 193 193 PRO PRO A . n 
A 1 186 ILE 186 194 194 ILE ILE A . n 
A 1 187 GLY 187 195 195 GLY GLY A . n 
A 1 188 PRO 188 196 196 PRO PRO A . n 
A 1 189 ASN 189 197 197 ASN ASN A . n 
A 1 190 GLU 190 198 198 GLU GLU A . n 
A 1 191 THR 191 199 199 THR THR A . n 
A 1 192 LEU 192 200 200 LEU LEU A . n 
A 1 193 ILE 193 201 201 ILE ILE A . n 
A 1 194 PHE 194 202 202 PHE PHE A . n 
A 1 195 LYS 195 203 203 LYS LYS A . n 
A 1 196 ILE 196 204 204 ILE ILE A . n 
A 1 197 HIS 197 205 205 HIS HIS A . n 
A 1 198 LEU 198 206 206 LEU LEU A . n 
A 1 199 ILE 199 207 207 ILE ILE A . n 
A 1 200 SER 200 208 208 SER SER A . n 
A 1 201 VAL 201 209 209 VAL VAL A . n 
A 1 202 LYS 202 210 210 LYS LYS A . n 
A 1 203 LYS 203 211 211 LYS LYS A . n 
A 1 204 SER 204 212 212 SER SER A . n 
A 1 205 SER 205 213 213 SER SER A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MES 1  301 301 MES MES A . 
C 3 PEG 1  302 301 PEG PEG A . 
D 3 PEG 1  303 302 PEG PEG A . 
E 3 PEG 1  304 303 PEG PEG A . 
F 4 HOH 1  401 52  HOH HOH A . 
F 4 HOH 2  402 1   HOH HOH A . 
F 4 HOH 3  403 34  HOH HOH A . 
F 4 HOH 4  404 2   HOH HOH A . 
F 4 HOH 5  405 55  HOH HOH A . 
F 4 HOH 6  406 46  HOH HOH A . 
F 4 HOH 7  407 5   HOH HOH A . 
F 4 HOH 8  408 59  HOH HOH A . 
F 4 HOH 9  409 8   HOH HOH A . 
F 4 HOH 10 410 31  HOH HOH A . 
F 4 HOH 11 411 10  HOH HOH A . 
F 4 HOH 12 412 57  HOH HOH A . 
F 4 HOH 13 413 53  HOH HOH A . 
F 4 HOH 14 414 44  HOH HOH A . 
F 4 HOH 15 415 26  HOH HOH A . 
F 4 HOH 16 416 22  HOH HOH A . 
F 4 HOH 17 417 60  HOH HOH A . 
F 4 HOH 18 418 14  HOH HOH A . 
F 4 HOH 19 419 63  HOH HOH A . 
F 4 HOH 20 420 47  HOH HOH A . 
F 4 HOH 21 421 9   HOH HOH A . 
F 4 HOH 22 422 18  HOH HOH A . 
F 4 HOH 23 423 51  HOH HOH A . 
F 4 HOH 24 424 38  HOH HOH A . 
F 4 HOH 25 425 45  HOH HOH A . 
F 4 HOH 26 426 62  HOH HOH A . 
F 4 HOH 27 427 43  HOH HOH A . 
F 4 HOH 28 428 54  HOH HOH A . 
F 4 HOH 29 429 39  HOH HOH A . 
F 4 HOH 30 430 50  HOH HOH A . 
F 4 HOH 31 431 61  HOH HOH A . 
F 4 HOH 32 432 19  HOH HOH A . 
F 4 HOH 33 433 40  HOH HOH A . 
F 4 HOH 34 434 4   HOH HOH A . 
F 4 HOH 35 435 37  HOH HOH A . 
F 4 HOH 36 436 29  HOH HOH A . 
F 4 HOH 37 437 49  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MoRDa  ? ? ? .        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                     8RUO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.185 
_cell.length_a_esd                 ? 
_cell.length_b                     77.185 
_cell.length_b_esd                 ? 
_cell.length_c                     103.517 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8RUO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   8RUO 
_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             3.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.37 
_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              6.2 
_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    
;MES 50mM
Magnesium chloride 500mM
Zinc chloride 50mM
PEG 8000 15%
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9677 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9677 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          71.76 
_reflns.entry_id                                       8RUO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.54 
_reflns.d_resolution_low                               43.02 
_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                                     10829 
_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                           99.92 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.95 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.54 
_reflns_shell.d_res_low                                     2.631 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1047 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.78 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.13 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.13 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               70.023 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.923 
_refine.correlation_coeff_Fo_to_Fc_free          0.877 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8RUO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.54 
_refine.ls_d_res_low                             43.02 
_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                     10322 
_refine.ls_number_reflns_R_free                  508 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.25355 
_refine.ls_R_factor_R_free                       0.31851 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.25047 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.423 
_refine.pdbx_overall_ESU_R_Free                  0.327 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             15.157 
_refine.overall_SU_ML                            0.309 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.54 
_refine_hist.d_res_low                        43.02 
_refine_hist.number_atoms_solvent             37 
_refine_hist.number_atoms_total               1625 
_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        1567 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_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' ? 0.007  0.012  1612 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1590 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.787  1.828  2165 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.586  1.765  3694 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.431  5.000  204  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.361  5.000  3    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.257 10.000 293  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  241  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1817 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  319  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.822  6.830  819  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.814  6.831  819  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 8.516  12.281 1022 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.514  12.288 1023 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.766  7.450  793  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.762  7.452  794  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 10.232 13.374 1144 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 15.594 86.26  1828 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 15.598 86.30  1826 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.540 
_refine_ls_shell.d_res_low                        2.606 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             33 
_refine_ls_shell.number_reflns_R_work             733 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.395 
_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   20 
_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                  0.460 
# 
_struct.entry_id                     8RUO 
_struct.title                        'D44E mutant crystal structure of LpMIP' 
_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        8RUO 
_struct_keywords.text            'Mutant, potentiator, stalk helix, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MIP_LEGPN 
_struct_ref.pdbx_db_accession          Q70YI1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TDKDKLSYSIGADLGKNFKNQGIDVNPEAMAKGMQDAMSGAQLALTEQQMKDVLNKFQKDLMAKRTAEFNKKADENKVKG
EAFLTENKNKPGVVVLPSGLQYKVINAGNGVKPGKSDTVTVEYTGRLIDGTVFDSTEKTGKPATFQVSQVIPGWTEALQL
MPAGSTWEIYVPSGLAYGPRSVGGPIGPNETLIFKIHLISVKKSS
;
_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              8RUO 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 205 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q70YI1 
_struct_ref_seq.db_align_beg                  29 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  233 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       213 
# 
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 8RUO GLU A 36  ? UNP Q70YI1 ASP 64  'engineered mutation' 44  1 
1 8RUO SER A 107 ? UNP Q70YI1 ALA 135 conflict              115 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 910   ? 
1 MORE         11    ? 
1 'SSA (A^2)'  13530 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'NMR relaxation study' 
_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 LYS A 3   ? GLN A 21  ? LYS A 11  GLN A 29  1 ? 19 
HELX_P HELX_P2 AA2 ASN A 26  ? SER A 39  ? ASN A 34  SER A 47  1 ? 14 
HELX_P HELX_P3 AA3 THR A 46  ? LYS A 88  ? THR A 54  LYS A 96  1 ? 43 
HELX_P HELX_P4 AA4 GLU A 137 ? THR A 139 ? GLU A 145 THR A 147 5 ? 3  
HELX_P HELX_P5 AA5 SER A 148 ? VAL A 150 ? SER A 156 VAL A 158 5 ? 3  
HELX_P HELX_P6 AA6 ILE A 151 ? GLN A 159 ? ILE A 159 GLN A 167 1 ? 9  
HELX_P HELX_P7 AA7 PRO A 172 ? ALA A 176 ? PRO A 180 ALA A 184 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 93  ? VAL A 95  ? VAL A 101 VAL A 103 
AA1 2 GLN A 101 ? ASN A 106 ? GLN A 109 ASN A 114 
AA1 3 THR A 166 ? VAL A 171 ? THR A 174 VAL A 179 
AA1 4 LEU A 192 ? VAL A 201 ? LEU A 200 VAL A 209 
AA1 5 THR A 118 ? LEU A 127 ? THR A 126 LEU A 135 
AA1 6 VAL A 132 ? SER A 135 ? VAL A 140 SER A 143 
AA2 1 VAL A 93  ? VAL A 95  ? VAL A 101 VAL A 103 
AA2 2 GLN A 101 ? ASN A 106 ? GLN A 109 ASN A 114 
AA2 3 THR A 166 ? VAL A 171 ? THR A 174 VAL A 179 
AA2 4 LEU A 192 ? VAL A 201 ? LEU A 200 VAL A 209 
AA2 5 THR A 118 ? LEU A 127 ? THR A 126 LEU A 135 
AA2 6 ALA A 143 ? GLN A 146 ? ALA A 151 GLN A 154 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 94  ? N VAL A 102 O TYR A 102 ? O TYR A 110 
AA1 2 3 N ASN A 106 ? N ASN A 114 O THR A 166 ? O THR A 174 
AA1 3 4 N TRP A 167 ? N TRP A 175 O ILE A 196 ? O ILE A 204 
AA1 4 5 O HIS A 197 ? O HIS A 205 N GLU A 122 ? N GLU A 130 
AA1 5 6 N GLY A 125 ? N GLY A 133 O ASP A 134 ? O ASP A 142 
AA2 1 2 N VAL A 94  ? N VAL A 102 O TYR A 102 ? O TYR A 110 
AA2 2 3 N ASN A 106 ? N ASN A 114 O THR A 166 ? O THR A 174 
AA2 3 4 N TRP A 167 ? N TRP A 175 O ILE A 196 ? O ILE A 204 
AA2 4 5 O HIS A 197 ? O HIS A 205 N GLU A 122 ? N GLU A 130 
AA2 5 6 N VAL A 119 ? N VAL A 127 O PHE A 145 ? O PHE A 153 
# 
_pdbx_entry_details.entry_id                   8RUO 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    55 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.64 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1  1 NE2 A HIS 205 ? ? 1_555 O3S A MES 301 ? ? 3_554 1.03 
2  1 OE1 A GLU 130 ? ? 1_555 O1  A MES 301 ? ? 3_554 1.34 
3  1 OE2 A GLU 130 ? ? 1_555 C2  A MES 301 ? ? 3_554 1.84 
4  1 NZ  A LYS 11  ? ? 1_555 CD  A GLU 89  ? ? 3_544 1.90 
5  1 CD2 A HIS 205 ? ? 1_555 O3S A MES 301 ? ? 3_554 1.92 
6  1 OE1 A GLU 130 ? ? 1_555 C2  A MES 301 ? ? 3_554 1.95 
7  1 NZ  A LYS 11  ? ? 1_555 OE1 A GLU 89  ? ? 3_544 2.07 
8  1 CE1 A HIS 205 ? ? 1_555 O3S A MES 301 ? ? 3_554 2.11 
9  1 NZ  A LYS 11  ? ? 1_555 CG  A GLU 89  ? ? 3_544 2.12 
10 1 CD  A GLU 130 ? ? 1_555 C2  A MES 301 ? ? 3_554 2.13 
11 1 OE2 A GLU 130 ? ? 1_555 C3  A MES 301 ? ? 3_554 2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 11  ? ? 90.86   -64.28  
2 1 ASP A 32  ? ? -65.20  94.55   
3 1 SER A 124 ? ? -108.28 41.12   
4 1 ALA A 184 ? ? -111.64 -121.97 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MES O1   O N N 216 
MES C2   C N N 217 
MES C3   C N N 218 
MES N4   N N N 219 
MES C5   C N N 220 
MES C6   C N N 221 
MES C7   C N N 222 
MES C8   C N N 223 
MES S    S N N 224 
MES O1S  O N N 225 
MES O2S  O N N 226 
MES O3S  O N N 227 
MES H21  H N N 228 
MES H22  H N N 229 
MES H31  H N N 230 
MES H32  H N N 231 
MES HN4  H N N 232 
MES H51  H N N 233 
MES H52  H N N 234 
MES H61  H N N 235 
MES H62  H N N 236 
MES H71  H N N 237 
MES H72  H N N 238 
MES H81  H N N 239 
MES H82  H N N 240 
MET N    N N N 241 
MET CA   C N S 242 
MET C    C N N 243 
MET O    O N N 244 
MET CB   C N N 245 
MET CG   C N N 246 
MET SD   S N N 247 
MET CE   C N N 248 
MET OXT  O N N 249 
MET H    H N N 250 
MET H2   H N N 251 
MET HA   H N N 252 
MET HB2  H N N 253 
MET HB3  H N N 254 
MET HG2  H N N 255 
MET HG3  H N N 256 
MET HE1  H N N 257 
MET HE2  H N N 258 
MET HE3  H N N 259 
MET HXT  H N N 260 
PEG C1   C N N 261 
PEG O1   O N N 262 
PEG C2   C N N 263 
PEG O2   O N N 264 
PEG C3   C N N 265 
PEG C4   C N N 266 
PEG O4   O N N 267 
PEG H11  H N N 268 
PEG H12  H N N 269 
PEG HO1  H N N 270 
PEG H21  H N N 271 
PEG H22  H N N 272 
PEG H31  H N N 273 
PEG H32  H N N 274 
PEG H41  H N N 275 
PEG H42  H N N 276 
PEG HO4  H N N 277 
PHE N    N N N 278 
PHE CA   C N S 279 
PHE C    C N N 280 
PHE O    O N N 281 
PHE CB   C N N 282 
PHE CG   C Y N 283 
PHE CD1  C Y N 284 
PHE CD2  C Y N 285 
PHE CE1  C Y N 286 
PHE CE2  C Y N 287 
PHE CZ   C Y N 288 
PHE OXT  O N N 289 
PHE H    H N N 290 
PHE H2   H N N 291 
PHE HA   H N N 292 
PHE HB2  H N N 293 
PHE HB3  H N N 294 
PHE HD1  H N N 295 
PHE HD2  H N N 296 
PHE HE1  H N N 297 
PHE HE2  H N N 298 
PHE HZ   H N N 299 
PHE HXT  H N N 300 
PRO N    N N N 301 
PRO CA   C N S 302 
PRO C    C N N 303 
PRO O    O N N 304 
PRO CB   C N N 305 
PRO CG   C N N 306 
PRO CD   C N N 307 
PRO OXT  O N N 308 
PRO H    H N N 309 
PRO HA   H N N 310 
PRO HB2  H N N 311 
PRO HB3  H N N 312 
PRO HG2  H N N 313 
PRO HG3  H N N 314 
PRO HD2  H N N 315 
PRO HD3  H N N 316 
PRO HXT  H N N 317 
SER N    N N N 318 
SER CA   C N S 319 
SER C    C N N 320 
SER O    O N N 321 
SER CB   C N N 322 
SER OG   O N N 323 
SER OXT  O N N 324 
SER H    H N N 325 
SER H2   H N N 326 
SER HA   H N N 327 
SER HB2  H N N 328 
SER HB3  H N N 329 
SER HG   H N N 330 
SER HXT  H N N 331 
THR N    N N N 332 
THR CA   C N S 333 
THR C    C N N 334 
THR O    O N N 335 
THR CB   C N R 336 
THR OG1  O N N 337 
THR CG2  C N N 338 
THR OXT  O N N 339 
THR H    H N N 340 
THR H2   H N N 341 
THR HA   H N N 342 
THR HB   H N N 343 
THR HG1  H N N 344 
THR HG21 H N N 345 
THR HG22 H N N 346 
THR HG23 H N N 347 
THR HXT  H N N 348 
TRP N    N N N 349 
TRP CA   C N S 350 
TRP C    C N N 351 
TRP O    O N N 352 
TRP CB   C N N 353 
TRP CG   C Y N 354 
TRP CD1  C Y N 355 
TRP CD2  C Y N 356 
TRP NE1  N Y N 357 
TRP CE2  C Y N 358 
TRP CE3  C Y N 359 
TRP CZ2  C Y N 360 
TRP CZ3  C Y N 361 
TRP CH2  C Y N 362 
TRP OXT  O N N 363 
TRP H    H N N 364 
TRP H2   H N N 365 
TRP HA   H N N 366 
TRP HB2  H N N 367 
TRP HB3  H N N 368 
TRP HD1  H N N 369 
TRP HE1  H N N 370 
TRP HE3  H N N 371 
TRP HZ2  H N N 372 
TRP HZ3  H N N 373 
TRP HH2  H N N 374 
TRP HXT  H N N 375 
TYR N    N N N 376 
TYR CA   C N S 377 
TYR C    C N N 378 
TYR O    O N N 379 
TYR CB   C N N 380 
TYR CG   C Y N 381 
TYR CD1  C Y N 382 
TYR CD2  C Y N 383 
TYR CE1  C Y N 384 
TYR CE2  C Y N 385 
TYR CZ   C Y N 386 
TYR OH   O N N 387 
TYR OXT  O N N 388 
TYR H    H N N 389 
TYR H2   H N N 390 
TYR HA   H N N 391 
TYR HB2  H N N 392 
TYR HB3  H N N 393 
TYR HD1  H N N 394 
TYR HD2  H N N 395 
TYR HE1  H N N 396 
TYR HE2  H N N 397 
TYR HH   H N N 398 
TYR HXT  H N N 399 
VAL N    N N N 400 
VAL CA   C N S 401 
VAL C    C N N 402 
VAL O    O N N 403 
VAL CB   C N N 404 
VAL CG1  C N N 405 
VAL CG2  C N N 406 
VAL OXT  O N N 407 
VAL H    H N N 408 
VAL H2   H N N 409 
VAL HA   H N N 410 
VAL HB   H N N 411 
VAL HG11 H N N 412 
VAL HG12 H N N 413 
VAL HG13 H N N 414 
VAL HG21 H N N 415 
VAL HG22 H N N 416 
VAL HG23 H N N 417 
VAL HXT  H N N 418 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MES O1  C2   sing N N 205 
MES O1  C6   sing N N 206 
MES C2  C3   sing N N 207 
MES C2  H21  sing N N 208 
MES C2  H22  sing N N 209 
MES C3  N4   sing N N 210 
MES C3  H31  sing N N 211 
MES C3  H32  sing N N 212 
MES N4  C5   sing N N 213 
MES N4  C7   sing N N 214 
MES N4  HN4  sing N N 215 
MES C5  C6   sing N N 216 
MES C5  H51  sing N N 217 
MES C5  H52  sing N N 218 
MES C6  H61  sing N N 219 
MES C6  H62  sing N N 220 
MES C7  C8   sing N N 221 
MES C7  H71  sing N N 222 
MES C7  H72  sing N N 223 
MES C8  S    sing N N 224 
MES C8  H81  sing N N 225 
MES C8  H82  sing N N 226 
MES S   O1S  doub N N 227 
MES S   O2S  doub N N 228 
MES S   O3S  sing N N 229 
MET N   CA   sing N N 230 
MET N   H    sing N N 231 
MET N   H2   sing N N 232 
MET CA  C    sing N N 233 
MET CA  CB   sing N N 234 
MET CA  HA   sing N N 235 
MET C   O    doub N N 236 
MET C   OXT  sing N N 237 
MET CB  CG   sing N N 238 
MET CB  HB2  sing N N 239 
MET CB  HB3  sing N N 240 
MET CG  SD   sing N N 241 
MET CG  HG2  sing N N 242 
MET CG  HG3  sing N N 243 
MET SD  CE   sing N N 244 
MET CE  HE1  sing N N 245 
MET CE  HE2  sing N N 246 
MET CE  HE3  sing N N 247 
MET OXT HXT  sing N N 248 
PEG C1  O1   sing N N 249 
PEG C1  C2   sing N N 250 
PEG C1  H11  sing N N 251 
PEG C1  H12  sing N N 252 
PEG O1  HO1  sing N N 253 
PEG C2  O2   sing N N 254 
PEG C2  H21  sing N N 255 
PEG C2  H22  sing N N 256 
PEG O2  C3   sing N N 257 
PEG C3  C4   sing N N 258 
PEG C3  H31  sing N N 259 
PEG C3  H32  sing N N 260 
PEG C4  O4   sing N N 261 
PEG C4  H41  sing N N 262 
PEG C4  H42  sing N N 263 
PEG O4  HO4  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           390713860 
_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   8BJC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RUO 
_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]   0.012956 
_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]   0.012956 
_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]   0.009660 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . THR A 1 1   ? 15.094  -16.148 7.736  1.00 102.61 ? 9   THR A N   1 
ATOM   2    C CA  . THR A 1 1   ? 14.709  -17.008 8.886  1.00 104.38 ? 9   THR A CA  1 
ATOM   3    C C   . THR A 1 1   ? 13.452  -16.455 9.579  1.00 96.30  ? 9   THR A C   1 
ATOM   4    O O   . THR A 1 1   ? 13.417  -16.333 10.800 1.00 101.95 ? 9   THR A O   1 
ATOM   5    C CB  . THR A 1 1   ? 15.909  -17.155 9.837  1.00 102.11 ? 9   THR A CB  1 
ATOM   6    O OG1 . THR A 1 1   ? 16.856  -16.140 9.519  1.00 100.02 ? 9   THR A OG1 1 
ATOM   7    C CG2 . THR A 1 1   ? 16.662  -18.462 9.672  1.00 95.32  ? 9   THR A CG2 1 
ATOM   8    N N   . ASP A 1 2   ? 12.420  -16.129 8.804  1.00 92.46  ? 10  ASP A N   1 
ATOM   9    C CA  . ASP A 1 2   ? 11.206  -15.495 9.393  1.00 79.07  ? 10  ASP A CA  1 
ATOM   10   C C   . ASP A 1 2   ? 10.774  -16.273 10.639 1.00 77.50  ? 10  ASP A C   1 
ATOM   11   O O   . ASP A 1 2   ? 10.835  -17.514 10.558 1.00 96.46  ? 10  ASP A O   1 
ATOM   12   C CB  . ASP A 1 2   ? 10.141  -15.299 8.329  1.00 72.22  ? 10  ASP A CB  1 
ATOM   13   C CG  . ASP A 1 2   ? 10.138  -13.933 7.663  1.00 78.67  ? 10  ASP A CG  1 
ATOM   14   O OD1 . ASP A 1 2   ? 10.347  -13.883 6.435  1.00 82.12  ? 10  ASP A OD1 1 
ATOM   15   O OD2 . ASP A 1 2   ? 9.927   -12.934 8.379  1.00 83.05  ? 10  ASP A OD2 1 
ATOM   16   N N   . LYS A 1 3   ? 10.225  -15.576 11.647 1.00 66.49  ? 11  LYS A N   1 
ATOM   17   C CA  . LYS A 1 3   ? 9.804   -16.176 12.950 1.00 67.81  ? 11  LYS A CA  1 
ATOM   18   C C   . LYS A 1 3   ? 11.019  -16.070 13.883 1.00 69.42  ? 11  LYS A C   1 
ATOM   19   O O   . LYS A 1 3   ? 10.926  -15.333 14.886 1.00 65.47  ? 11  LYS A O   1 
ATOM   20   C CB  . LYS A 1 3   ? 9.227   -17.600 12.917 1.00 63.06  ? 11  LYS A CB  1 
ATOM   21   C CG  . LYS A 1 3   ? 9.224   -18.340 14.248 1.00 66.33  ? 11  LYS A CG  1 
ATOM   22   C CD  . LYS A 1 3   ? 10.102  -19.586 14.246 1.00 68.69  ? 11  LYS A CD  1 
ATOM   23   C CE  . LYS A 1 3   ? 10.397  -20.075 12.864 1.00 70.07  ? 11  LYS A CE  1 
ATOM   24   N NZ  . LYS A 1 3   ? 9.513   -21.177 12.478 1.00 70.61  ? 11  LYS A NZ  1 
ATOM   25   N N   . ASP A 1 4   ? 12.115  -16.747 13.569 1.00 72.64  ? 12  ASP A N   1 
ATOM   26   C CA  . ASP A 1 4   ? 13.324  -16.570 14.416 1.00 68.70  ? 12  ASP A CA  1 
ATOM   27   C C   . ASP A 1 4   ? 13.812  -15.133 14.215 1.00 66.33  ? 12  ASP A C   1 
ATOM   28   O O   . ASP A 1 4   ? 14.377  -14.547 15.155 1.00 66.71  ? 12  ASP A O   1 
ATOM   29   C CB  . ASP A 1 4   ? 14.365  -17.648 14.152 1.00 60.54  ? 12  ASP A CB  1 
ATOM   30   C CG  . ASP A 1 4   ? 14.490  -18.716 15.228 1.00 73.55  ? 12  ASP A CG  1 
ATOM   31   O OD1 . ASP A 1 4   ? 13.736  -18.638 16.217 1.00 77.54  ? 12  ASP A OD1 1 
ATOM   32   O OD2 . ASP A 1 4   ? 15.342  -19.616 15.069 1.00 61.26  ? 12  ASP A OD2 1 
ATOM   33   N N   . LYS A 1 5   ? 13.573  -14.587 13.026 1.00 65.32  ? 13  LYS A N   1 
ATOM   34   C CA  . LYS A 1 5   ? 13.979  -13.182 12.768 1.00 70.52  ? 13  LYS A CA  1 
ATOM   35   C C   . LYS A 1 5   ? 12.951  -12.243 13.412 1.00 68.18  ? 13  LYS A C   1 
ATOM   36   O O   . LYS A 1 5   ? 13.372  -11.242 14.030 1.00 65.27  ? 13  LYS A O   1 
ATOM   37   C CB  . LYS A 1 5   ? 14.130  -12.952 11.261 1.00 88.41  ? 13  LYS A CB  1 
ATOM   38   C CG  . LYS A 1 5   ? 15.529  -13.258 10.750 1.00 108.60 ? 13  LYS A CG  1 
ATOM   39   C CD  . LYS A 1 5   ? 16.603  -12.990 11.799 1.00 119.87 ? 13  LYS A CD  1 
ATOM   40   C CE  . LYS A 1 5   ? 17.335  -14.220 12.243 1.00 110.53 ? 13  LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 5   ? 17.105  -14.501 13.662 1.00 101.70 ? 13  LYS A NZ  1 
ATOM   42   N N   . LEU A 1 6   ? 11.659  -12.551 13.275 1.00 71.20  ? 14  LEU A N   1 
ATOM   43   C CA  . LEU A 1 6   ? 10.669  -11.727 13.947 1.00 65.38  ? 14  LEU A CA  1 
ATOM   44   C C   . LEU A 1 6   ? 10.982  -11.677 15.451 1.00 64.37  ? 14  LEU A C   1 
ATOM   45   O O   . LEU A 1 6   ? 10.968  -10.610 16.061 1.00 60.26  ? 14  LEU A O   1 
ATOM   46   C CB  . LEU A 1 6   ? 9.262   -12.240 13.650 1.00 59.46  ? 14  LEU A CB  1 
ATOM   47   C CG  . LEU A 1 6   ? 8.126   -11.599 14.462 1.00 57.96  ? 14  LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 6   ? 7.852   -10.140 14.141 1.00 52.72  ? 14  LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 6   ? 6.863   -12.408 14.283 1.00 62.42  ? 14  LEU A CD2 1 
ATOM   50   N N   . SER A 1 7   ? 11.283  -12.831 16.050 1.00 57.94  ? 15  SER A N   1 
ATOM   51   C CA  . SER A 1 7   ? 11.634  -12.888 17.455 1.00 64.14  ? 15  SER A CA  1 
ATOM   52   C C   . SER A 1 7   ? 12.760  -11.902 17.757 1.00 69.22  ? 15  SER A C   1 
ATOM   53   O O   . SER A 1 7   ? 12.678  -11.147 18.725 1.00 69.49  ? 15  SER A O   1 
ATOM   54   C CB  . SER A 1 7   ? 12.024  -14.283 17.858 1.00 69.82  ? 15  SER A CB  1 
ATOM   55   O OG  . SER A 1 7   ? 11.033  -15.234 17.493 1.00 69.32  ? 15  SER A OG  1 
ATOM   56   N N   . TYR A 1 8   ? 13.807  -11.925 16.925 1.00 65.61  ? 16  TYR A N   1 
ATOM   57   C CA  . TYR A 1 8   ? 14.974  -11.073 17.114 1.00 67.62  ? 16  TYR A CA  1 
ATOM   58   C C   . TYR A 1 8   ? 14.536  -9.603  17.126 1.00 63.26  ? 16  TYR A C   1 
ATOM   59   O O   . TYR A 1 8   ? 14.858  -8.843  18.038 1.00 59.19  ? 16  TYR A O   1 
ATOM   60   C CB  . TYR A 1 8   ? 16.026  -11.376 16.029 1.00 68.82  ? 16  TYR A CB  1 
ATOM   61   C CG  . TYR A 1 8   ? 17.407  -10.754 16.231 1.00 65.25  ? 16  TYR A CG  1 
ATOM   62   C CD1 . TYR A 1 8   ? 17.705  -9.473  15.774 1.00 66.08  ? 16  TYR A CD1 1 
ATOM   63   C CD2 . TYR A 1 8   ? 18.409  -11.439 16.910 1.00 69.22  ? 16  TYR A CD2 1 
ATOM   64   C CE1 . TYR A 1 8   ? 18.953  -8.899  15.990 1.00 72.08  ? 16  TYR A CE1 1 
ATOM   65   C CE2 . TYR A 1 8   ? 19.659  -10.879 17.126 1.00 73.33  ? 16  TYR A CE2 1 
ATOM   66   C CZ  . TYR A 1 8   ? 19.930  -9.602  16.669 1.00 74.37  ? 16  TYR A CZ  1 
ATOM   67   O OH  . TYR A 1 8   ? 21.161  -9.037  16.852 1.00 73.24  ? 16  TYR A OH  1 
ATOM   68   N N   . SER A 1 9   ? 13.784  -9.199  16.103 1.00 63.09  ? 17  SER A N   1 
ATOM   69   C CA  . SER A 1 9   ? 13.366  -7.813  15.957 1.00 66.19  ? 17  SER A CA  1 
ATOM   70   C C   . SER A 1 9   ? 12.594  -7.332  17.186 1.00 66.26  ? 17  SER A C   1 
ATOM   71   O O   . SER A 1 9   ? 12.737  -6.183  17.595 1.00 64.08  ? 17  SER A O   1 
ATOM   72   C CB  . SER A 1 9   ? 12.549  -7.637  14.693 1.00 67.60  ? 17  SER A CB  1 
ATOM   73   O OG  . SER A 1 9   ? 13.271  -8.074  13.545 1.00 59.31  ? 17  SER A OG  1 
ATOM   74   N N   . ILE A 1 10  ? 11.766  -8.226  17.744 1.00 71.01  ? 18  ILE A N   1 
ATOM   75   C CA  . ILE A 1 10  ? 10.942  -7.945  18.910 1.00 72.42  ? 18  ILE A CA  1 
ATOM   76   C C   . ILE A 1 10  ? 11.838  -7.746  20.135 1.00 62.81  ? 18  ILE A C   1 
ATOM   77   O O   . ILE A 1 10  ? 11.713  -6.737  20.822 1.00 58.91  ? 18  ILE A O   1 
ATOM   78   C CB  . ILE A 1 10  ? 9.889   -9.057  19.130 1.00 75.09  ? 18  ILE A CB  1 
ATOM   79   C CG1 . ILE A 1 10  ? 8.739   -8.972  18.119 1.00 71.39  ? 18  ILE A CG1 1 
ATOM   80   C CG2 . ILE A 1 10  ? 9.351   -9.030  20.560 1.00 74.02  ? 18  ILE A CG2 1 
ATOM   81   C CD1 . ILE A 1 10  ? 7.800   -10.168 18.122 1.00 65.33  ? 18  ILE A CD1 1 
ATOM   82   N N   . GLY A 1 11  ? 12.714  -8.724  20.407 1.00 65.85  ? 19  GLY A N   1 
ATOM   83   C CA  . GLY A 1 11  ? 13.698  -8.647  21.484 1.00 66.19  ? 19  GLY A CA  1 
ATOM   84   C C   . GLY A 1 11  ? 14.481  -7.329  21.476 1.00 67.82  ? 19  GLY A C   1 
ATOM   85   O O   . GLY A 1 11  ? 14.554  -6.644  22.488 1.00 65.98  ? 19  GLY A O   1 
ATOM   86   N N   . ALA A 1 12  ? 15.050  -6.968  20.321 1.00 71.18  ? 20  ALA A N   1 
ATOM   87   C CA  . ALA A 1 12  ? 15.789  -5.725  20.163 1.00 71.27  ? 20  ALA A CA  1 
ATOM   88   C C   . ALA A 1 12  ? 14.939  -4.506  20.533 1.00 65.03  ? 20  ALA A C   1 
ATOM   89   O O   . ALA A 1 12  ? 15.443  -3.579  21.162 1.00 68.49  ? 20  ALA A O   1 
ATOM   90   C CB  . ALA A 1 12  ? 16.313  -5.623  18.739 1.00 73.77  ? 20  ALA A CB  1 
ATOM   91   N N   . ASP A 1 13  ? 13.663  -4.476  20.122 1.00 60.71  ? 21  ASP A N   1 
ATOM   92   C CA  . ASP A 1 13  ? 12.829  -3.321  20.416 1.00 66.09  ? 21  ASP A CA  1 
ATOM   93   C C   . ASP A 1 13  ? 12.572  -3.264  21.923 1.00 66.22  ? 21  ASP A C   1 
ATOM   94   O O   . ASP A 1 13  ? 12.452  -2.184  22.499 1.00 69.52  ? 21  ASP A O   1 
ATOM   95   C CB  . ASP A 1 13  ? 11.540  -3.292  19.608 1.00 62.52  ? 21  ASP A CB  1 
ATOM   96   C CG  . ASP A 1 13  ? 10.781  -1.973  19.683 1.00 66.23  ? 21  ASP A CG  1 
ATOM   97   O OD1 . ASP A 1 13  ? 11.405  -0.914  19.445 1.00 78.30  ? 21  ASP A OD1 1 
ATOM   98   O OD2 . ASP A 1 13  ? 9.569   -2.002  19.967 1.00 67.08  ? 21  ASP A OD2 1 
ATOM   99   N N   . LEU A 1 14  ? 12.508  -4.445  22.546 1.00 55.27  ? 22  LEU A N   1 
ATOM   100  C CA  . LEU A 1 14  ? 12.325  -4.564  23.978 1.00 61.84  ? 22  LEU A CA  1 
ATOM   101  C C   . LEU A 1 14  ? 13.572  -4.138  24.758 1.00 64.11  ? 22  LEU A C   1 
ATOM   102  O O   . LEU A 1 14  ? 13.459  -3.493  25.793 1.00 57.55  ? 22  LEU A O   1 
ATOM   103  C CB  . LEU A 1 14  ? 11.974  -6.016  24.282 1.00 59.88  ? 22  LEU A CB  1 
ATOM   104  C CG  . LEU A 1 14  ? 10.496  -6.340  24.485 1.00 64.41  ? 22  LEU A CG  1 
ATOM   105  C CD1 . LEU A 1 14  ? 10.416  -7.805  24.825 1.00 67.48  ? 22  LEU A CD1 1 
ATOM   106  C CD2 . LEU A 1 14  ? 9.841   -5.511  25.578 1.00 67.38  ? 22  LEU A CD2 1 
ATOM   107  N N   . GLY A 1 15  ? 14.748  -4.574  24.293 1.00 66.12  ? 23  GLY A N   1 
ATOM   108  C CA  . GLY A 1 15  ? 16.006  -4.290  24.959 1.00 65.87  ? 23  GLY A CA  1 
ATOM   109  C C   . GLY A 1 15  ? 16.368  -2.815  24.853 1.00 65.45  ? 23  GLY A C   1 
ATOM   110  O O   . GLY A 1 15  ? 16.792  -2.222  25.838 1.00 73.08  ? 23  GLY A O   1 
ATOM   111  N N   . LYS A 1 16  ? 16.222  -2.252  23.646 1.00 68.42  ? 24  LYS A N   1 
ATOM   112  C CA  . LYS A 1 16  ? 16.298  -0.814  23.440 1.00 73.90  ? 24  LYS A CA  1 
ATOM   113  C C   . LYS A 1 16  ? 15.594  -0.110  24.606 1.00 78.61  ? 24  LYS A C   1 
ATOM   114  O O   . LYS A 1 16  ? 16.182  0.755   25.246 1.00 80.66  ? 24  LYS A O   1 
ATOM   115  C CB  . LYS A 1 16  ? 15.735  -0.411  22.064 1.00 78.77  ? 24  LYS A CB  1 
ATOM   116  C CG  . LYS A 1 16  ? 16.734  -0.482  20.891 1.00 98.76  ? 24  LYS A CG  1 
ATOM   117  C CD  . LYS A 1 16  ? 16.209  -0.460  19.447 1.00 103.77 ? 24  LYS A CD  1 
ATOM   118  C CE  . LYS A 1 16  ? 17.310  -0.590  18.407 1.00 88.56  ? 24  LYS A CE  1 
ATOM   119  N NZ  . LYS A 1 16  ? 16.782  -0.860  17.070 1.00 77.18  ? 24  LYS A NZ  1 
ATOM   120  N N   . ASN A 1 17  ? 14.357  -0.523  24.916 1.00 78.13  ? 25  ASN A N   1 
ATOM   121  C CA  . ASN A 1 17  ? 13.467  0.258   25.760 1.00 78.01  ? 25  ASN A CA  1 
ATOM   122  C C   . ASN A 1 17  ? 13.820  0.097   27.244 1.00 74.02  ? 25  ASN A C   1 
ATOM   123  O O   . ASN A 1 17  ? 13.679  1.042   28.019 1.00 68.89  ? 25  ASN A O   1 
ATOM   124  C CB  . ASN A 1 17  ? 12.018  -0.082  25.435 1.00 84.50  ? 25  ASN A CB  1 
ATOM   125  C CG  . ASN A 1 17  ? 11.063  0.976   25.938 1.00 95.55  ? 25  ASN A CG  1 
ATOM   126  O OD1 . ASN A 1 17  ? 11.149  2.140   25.519 1.00 100.78 ? 25  ASN A OD1 1 
ATOM   127  N ND2 . ASN A 1 17  ? 10.154  0.596   26.826 1.00 85.94  ? 25  ASN A ND2 1 
ATOM   128  N N   . PHE A 1 18  ? 14.292  -1.097  27.632 1.00 78.30  ? 26  PHE A N   1 
ATOM   129  C CA  . PHE A 1 18  ? 14.648  -1.399  29.012 1.00 74.12  ? 26  PHE A CA  1 
ATOM   130  C C   . PHE A 1 18  ? 15.927  -0.674  29.415 1.00 76.50  ? 26  PHE A C   1 
ATOM   131  O O   . PHE A 1 18  ? 16.033  -0.220  30.550 1.00 68.22  ? 26  PHE A O   1 
ATOM   132  C CB  . PHE A 1 18  ? 14.930  -2.884  29.252 1.00 73.57  ? 26  PHE A CB  1 
ATOM   133  C CG  . PHE A 1 18  ? 13.727  -3.810  29.360 1.00 77.67  ? 26  PHE A CG  1 
ATOM   134  C CD1 . PHE A 1 18  ? 12.584  -3.438  30.056 1.00 82.92  ? 26  PHE A CD1 1 
ATOM   135  C CD2 . PHE A 1 18  ? 13.760  -5.080  28.792 1.00 85.80  ? 26  PHE A CD2 1 
ATOM   136  C CE1 . PHE A 1 18  ? 11.500  -4.299  30.154 1.00 86.34  ? 26  PHE A CE1 1 
ATOM   137  C CE2 . PHE A 1 18  ? 12.677  -5.941  28.901 1.00 82.55  ? 26  PHE A CE2 1 
ATOM   138  C CZ  . PHE A 1 18  ? 11.547  -5.547  29.576 1.00 80.72  ? 26  PHE A CZ  1 
ATOM   139  N N   . LYS A 1 19  ? 16.897  -0.628  28.489 1.00 81.76  ? 27  LYS A N   1 
ATOM   140  C CA  . LYS A 1 19  ? 18.170  0.055   28.683 1.00 86.71  ? 27  LYS A CA  1 
ATOM   141  C C   . LYS A 1 19  ? 17.982  1.577   28.665 1.00 84.91  ? 27  LYS A C   1 
ATOM   142  O O   . LYS A 1 19  ? 18.785  2.315   29.231 1.00 89.98  ? 27  LYS A O   1 
ATOM   143  C CB  . LYS A 1 19  ? 19.135  -0.426  27.593 1.00 87.11  ? 27  LYS A CB  1 
ATOM   144  C CG  . LYS A 1 19  ? 20.557  0.110   27.671 1.00 96.28  ? 27  LYS A CG  1 
ATOM   145  C CD  . LYS A 1 19  ? 21.299  -0.240  28.957 1.00 99.56  ? 27  LYS A CD  1 
ATOM   146  C CE  . LYS A 1 19  ? 22.734  0.183   28.886 1.00 96.18  ? 27  LYS A CE  1 
ATOM   147  N NZ  . LYS A 1 19  ? 23.474  -0.158  30.102 1.00 99.24  ? 27  LYS A NZ  1 
ATOM   148  N N   . ASN A 1 20  ? 16.920  2.048   28.005 1.00 87.06  ? 28  ASN A N   1 
ATOM   149  C CA  . ASN A 1 20  ? 16.566  3.458   28.017 1.00 91.40  ? 28  ASN A CA  1 
ATOM   150  C C   . ASN A 1 20  ? 15.996  3.854   29.362 1.00 83.99  ? 28  ASN A C   1 
ATOM   151  O O   . ASN A 1 20  ? 16.306  4.922   29.876 1.00 97.24  ? 28  ASN A O   1 
ATOM   152  C CB  . ASN A 1 20  ? 15.477  3.800   27.011 1.00 98.25  ? 28  ASN A CB  1 
ATOM   153  C CG  . ASN A 1 20  ? 16.000  3.733   25.602 1.00 100.03 ? 28  ASN A CG  1 
ATOM   154  O OD1 . ASN A 1 20  ? 17.221  3.754   25.391 1.00 93.02  ? 28  ASN A OD1 1 
ATOM   155  N ND2 . ASN A 1 20  ? 15.092  3.658   24.639 1.00 99.37  ? 28  ASN A ND2 1 
ATOM   156  N N   . GLN A 1 21  ? 15.171  2.969   29.915 1.00 76.28  ? 29  GLN A N   1 
ATOM   157  C CA  . GLN A 1 21  ? 14.507  3.266   31.206 1.00 73.15  ? 29  GLN A CA  1 
ATOM   158  C C   . GLN A 1 21  ? 15.351  2.727   32.363 1.00 70.32  ? 29  GLN A C   1 
ATOM   159  O O   . GLN A 1 21  ? 14.946  2.917   33.516 1.00 77.87  ? 29  GLN A O   1 
ATOM   160  C CB  . GLN A 1 21  ? 13.117  2.641   31.165 1.00 71.31  ? 29  GLN A CB  1 
ATOM   161  C CG  . GLN A 1 21  ? 12.237  3.184   30.047 1.00 68.66  ? 29  GLN A CG  1 
ATOM   162  C CD  . GLN A 1 21  ? 10.846  2.593   30.052 1.00 77.92  ? 29  GLN A CD  1 
ATOM   163  O OE1 . GLN A 1 21  ? 10.420  1.956   31.020 1.00 92.23  ? 29  GLN A OE1 1 
ATOM   164  N NE2 . GLN A 1 21  ? 10.121  2.805   28.965 1.00 85.91  ? 29  GLN A NE2 1 
ATOM   165  N N   . GLY A 1 22  ? 16.467  2.071   32.059 1.00 72.17  ? 30  GLY A N   1 
ATOM   166  C CA  . GLY A 1 22  ? 17.371  1.572   33.109 1.00 72.75  ? 30  GLY A CA  1 
ATOM   167  C C   . GLY A 1 22  ? 16.779  0.398   33.856 1.00 79.51  ? 30  GLY A C   1 
ATOM   168  O O   . GLY A 1 22  ? 16.317  0.597   34.993 1.00 89.91  ? 30  GLY A O   1 
ATOM   169  N N   . ILE A 1 23  ? 16.817  -0.793  33.251 1.00 90.50  ? 31  ILE A N   1 
ATOM   170  C CA  . ILE A 1 23  ? 16.279  -2.015  33.921 1.00 87.66  ? 31  ILE A CA  1 
ATOM   171  C C   . ILE A 1 23  ? 17.243  -3.210  33.800 1.00 92.10  ? 31  ILE A C   1 
ATOM   172  O O   . ILE A 1 23  ? 17.259  -3.808  32.713 1.00 98.25  ? 31  ILE A O   1 
ATOM   173  C CB  . ILE A 1 23  ? 14.881  -2.362  33.368 1.00 88.62  ? 31  ILE A CB  1 
ATOM   174  C CG1 . ILE A 1 23  ? 14.125  -1.133  32.863 1.00 77.28  ? 31  ILE A CG1 1 
ATOM   175  C CG2 . ILE A 1 23  ? 14.061  -3.118  34.412 1.00 89.17  ? 31  ILE A CG2 1 
ATOM   176  C CD1 . ILE A 1 23  ? 12.626  -1.188  33.084 1.00 73.79  ? 31  ILE A CD1 1 
ATOM   177  N N   . ASP A 1 24  ? 17.969  -3.546  34.871 1.00 89.33  ? 32  ASP A N   1 
ATOM   178  C CA  . ASP A 1 24  ? 18.830  -4.758  34.843 1.00 76.88  ? 32  ASP A CA  1 
ATOM   179  C C   . ASP A 1 24  ? 17.889  -5.948  34.716 1.00 75.53  ? 32  ASP A C   1 
ATOM   180  O O   . ASP A 1 24  ? 17.352  -6.394  35.742 1.00 74.94  ? 32  ASP A O   1 
ATOM   181  C CB  . ASP A 1 24  ? 19.761  -4.867  36.041 1.00 63.21  ? 32  ASP A CB  1 
ATOM   182  C CG  . ASP A 1 24  ? 20.896  -5.873  35.899 1.00 69.64  ? 32  ASP A CG  1 
ATOM   183  O OD1 . ASP A 1 24  ? 21.141  -6.318  34.760 1.00 83.70  ? 32  ASP A OD1 1 
ATOM   184  O OD2 . ASP A 1 24  ? 21.529  -6.203  36.924 1.00 39.11  ? 32  ASP A OD2 1 
ATOM   185  N N   . VAL A 1 25  ? 17.662  -6.396  33.489 1.00 75.38  ? 33  VAL A N   1 
ATOM   186  C CA  . VAL A 1 25  ? 16.809  -7.556  33.254 1.00 72.79  ? 33  VAL A CA  1 
ATOM   187  C C   . VAL A 1 25  ? 17.736  -8.604  32.632 1.00 67.92  ? 33  VAL A C   1 
ATOM   188  O O   . VAL A 1 25  ? 18.699  -8.261  31.952 1.00 68.92  ? 33  VAL A O   1 
ATOM   189  C CB  . VAL A 1 25  ? 15.559  -7.360  32.372 1.00 81.69  ? 33  VAL A CB  1 
ATOM   190  C CG1 . VAL A 1 25  ? 14.484  -8.387  32.688 1.00 89.99  ? 33  VAL A CG1 1 
ATOM   191  C CG2 . VAL A 1 25  ? 14.937  -5.986  32.506 1.00 89.34  ? 33  VAL A CG2 1 
ATOM   192  N N   . ASN A 1 26  ? 17.458  -9.883  32.896 1.00 65.78  ? 34  ASN A N   1 
ATOM   193  C CA  . ASN A 1 26  ? 18.251  -10.969 32.345 1.00 71.26  ? 34  ASN A CA  1 
ATOM   194  C C   . ASN A 1 26  ? 17.436  -11.651 31.246 1.00 64.82  ? 34  ASN A C   1 
ATOM   195  O O   . ASN A 1 26  ? 16.488  -12.380 31.536 1.00 57.01  ? 34  ASN A O   1 
ATOM   196  C CB  . ASN A 1 26  ? 18.725  -11.919 33.440 1.00 76.52  ? 34  ASN A CB  1 
ATOM   197  C CG  . ASN A 1 26  ? 19.596  -13.029 32.897 1.00 75.58  ? 34  ASN A CG  1 
ATOM   198  O OD1 . ASN A 1 26  ? 20.420  -12.791 32.011 1.00 76.80  ? 34  ASN A OD1 1 
ATOM   199  N ND2 . ASN A 1 26  ? 19.414  -14.248 33.387 1.00 80.01  ? 34  ASN A ND2 1 
ATOM   200  N N   . PRO A 1 27  ? 17.771  -11.398 29.958 1.00 67.42  ? 35  PRO A N   1 
ATOM   201  C CA  . PRO A 1 27  ? 17.065  -11.995 28.815 1.00 74.98  ? 35  PRO A CA  1 
ATOM   202  C C   . PRO A 1 27  ? 16.836  -13.507 28.790 1.00 73.38  ? 35  PRO A C   1 
ATOM   203  O O   . PRO A 1 27  ? 15.805  -13.946 28.289 1.00 69.17  ? 35  PRO A O   1 
ATOM   204  C CB  . PRO A 1 27  ? 17.931  -11.572 27.606 1.00 75.47  ? 35  PRO A CB  1 
ATOM   205  C CG  . PRO A 1 27  ? 18.605  -10.283 28.046 1.00 73.19  ? 35  PRO A CG  1 
ATOM   206  C CD  . PRO A 1 27  ? 18.819  -10.454 29.536 1.00 70.43  ? 35  PRO A CD  1 
ATOM   207  N N   . GLU A 1 28  ? 17.800  -14.292 29.295 1.00 76.66  ? 36  GLU A N   1 
ATOM   208  C CA  . GLU A 1 28  ? 17.731  -15.743 29.178 1.00 87.52  ? 36  GLU A CA  1 
ATOM   209  C C   . GLU A 1 28  ? 16.767  -16.289 30.227 1.00 78.80  ? 36  GLU A C   1 
ATOM   210  O O   . GLU A 1 28  ? 16.068  -17.269 29.981 1.00 85.96  ? 36  GLU A O   1 
ATOM   211  C CB  . GLU A 1 28  ? 19.095  -16.438 29.254 1.00 94.66  ? 36  GLU A CB  1 
ATOM   212  C CG  . GLU A 1 28  ? 19.875  -16.462 27.936 1.00 101.00 ? 36  GLU A CG  1 
ATOM   213  C CD  . GLU A 1 28  ? 19.451  -17.466 26.859 1.00 109.20 ? 36  GLU A CD  1 
ATOM   214  O OE1 . GLU A 1 28  ? 19.218  -18.658 27.185 1.00 105.27 ? 36  GLU A OE1 1 
ATOM   215  O OE2 . GLU A 1 28  ? 19.404  -17.071 25.666 1.00 100.80 ? 36  GLU A OE2 1 
ATOM   216  N N   . ALA A 1 29  ? 16.733  -15.645 31.392 1.00 73.27  ? 37  ALA A N   1 
ATOM   217  C CA  . ALA A 1 29  ? 15.782  -16.016 32.424 1.00 79.76  ? 37  ALA A CA  1 
ATOM   218  C C   . ALA A 1 29  ? 14.381  -15.693 31.931 1.00 75.07  ? 37  ALA A C   1 
ATOM   219  O O   . ALA A 1 29  ? 13.423  -16.373 32.266 1.00 81.33  ? 37  ALA A O   1 
ATOM   220  C CB  . ALA A 1 29  ? 16.093  -15.288 33.719 1.00 84.51  ? 37  ALA A CB  1 
ATOM   221  N N   . MET A 1 30  ? 14.288  -14.624 31.143 1.00 83.42  ? 38  MET A N   1 
ATOM   222  C CA  . MET A 1 30  ? 13.041  -14.242 30.509 1.00 89.20  ? 38  MET A CA  1 
ATOM   223  C C   . MET A 1 30  ? 12.659  -15.253 29.428 1.00 80.30  ? 38  MET A C   1 
ATOM   224  O O   . MET A 1 30  ? 11.517  -15.696 29.361 1.00 68.57  ? 38  MET A O   1 
ATOM   225  C CB  . MET A 1 30  ? 13.180  -12.860 29.872 1.00 85.52  ? 38  MET A CB  1 
ATOM   226  C CG  . MET A 1 30  ? 11.876  -12.310 29.361 1.00 88.00  ? 38  MET A CG  1 
ATOM   227  S SD  . MET A 1 30  ? 12.072  -10.583 28.898 1.00 84.53  ? 38  MET A SD  1 
ATOM   228  C CE  . MET A 1 30  ? 12.363  -9.816  30.496 1.00 81.48  ? 38  MET A CE  1 
ATOM   229  N N   . ALA A 1 31  ? 13.620  -15.578 28.562 1.00 78.33  ? 39  ALA A N   1 
ATOM   230  C CA  . ALA A 1 31  ? 13.430  -16.620 27.574 1.00 79.73  ? 39  ALA A CA  1 
ATOM   231  C C   . ALA A 1 31  ? 12.825  -17.847 28.241 1.00 80.95  ? 39  ALA A C   1 
ATOM   232  O O   . ALA A 1 31  ? 11.753  -18.292 27.826 1.00 77.33  ? 39  ALA A O   1 
ATOM   233  C CB  . ALA A 1 31  ? 14.738  -16.957 26.906 1.00 82.09  ? 39  ALA A CB  1 
ATOM   234  N N   . LYS A 1 32  ? 13.496  -18.349 29.291 1.00 83.11  ? 40  LYS A N   1 
ATOM   235  C CA  . LYS A 1 32  ? 13.151  -19.645 29.861 1.00 90.23  ? 40  LYS A CA  1 
ATOM   236  C C   . LYS A 1 32  ? 11.671  -19.664 30.246 1.00 89.44  ? 40  LYS A C   1 
ATOM   237  O O   . LYS A 1 32  ? 10.961  -20.608 29.910 1.00 96.47  ? 40  LYS A O   1 
ATOM   238  C CB  . LYS A 1 32  ? 13.973  -20.099 31.077 1.00 96.51  ? 40  LYS A CB  1 
ATOM   239  C CG  . LYS A 1 32  ? 13.926  -21.628 31.278 1.00 113.17 ? 40  LYS A CG  1 
ATOM   240  C CD  . LYS A 1 32  ? 14.135  -22.171 32.691 1.00 120.63 ? 40  LYS A CD  1 
ATOM   241  C CE  . LYS A 1 32  ? 14.036  -23.677 32.789 1.00 114.00 ? 40  LYS A CE  1 
ATOM   242  N NZ  . LYS A 1 32  ? 13.478  -24.114 34.079 1.00 102.87 ? 40  LYS A NZ  1 
ATOM   243  N N   . GLY A 1 33  ? 11.217  -18.614 30.943 1.00 88.18  ? 41  GLY A N   1 
ATOM   244  C CA  . GLY A 1 33  ? 9.875   -18.569 31.506 1.00 80.03  ? 41  GLY A CA  1 
ATOM   245  C C   . GLY A 1 33  ? 8.807   -18.231 30.467 1.00 78.29  ? 41  GLY A C   1 
ATOM   246  O O   . GLY A 1 33  ? 7.622   -18.457 30.705 1.00 67.94  ? 41  GLY A O   1 
ATOM   247  N N   . MET A 1 34  ? 9.232   -17.655 29.335 1.00 75.95  ? 42  MET A N   1 
ATOM   248  C CA  . MET A 1 34  ? 8.338   -17.415 28.218 1.00 76.36  ? 42  MET A CA  1 
ATOM   249  C C   . MET A 1 34  ? 8.013   -18.757 27.571 1.00 75.41  ? 42  MET A C   1 
ATOM   250  O O   . MET A 1 34  ? 6.856   -19.040 27.302 1.00 75.42  ? 42  MET A O   1 
ATOM   251  C CB  . MET A 1 34  ? 8.977   -16.475 27.189 1.00 78.81  ? 42  MET A CB  1 
ATOM   252  C CG  . MET A 1 34  ? 7.970   -15.777 26.271 1.00 77.61  ? 42  MET A CG  1 
ATOM   253  S SD  . MET A 1 34  ? 8.689   -14.921 24.848 1.00 76.51  ? 42  MET A SD  1 
ATOM   254  C CE  . MET A 1 34  ? 10.292  -14.410 25.488 1.00 96.67  ? 42  MET A CE  1 
ATOM   255  N N   . GLN A 1 35  ? 9.061   -19.561 27.349 1.00 82.60  ? 43  GLN A N   1 
ATOM   256  C CA  . GLN A 1 35  ? 8.963   -20.915 26.816 1.00 83.74  ? 43  GLN A CA  1 
ATOM   257  C C   . GLN A 1 35  ? 8.082   -21.780 27.719 1.00 77.31  ? 43  GLN A C   1 
ATOM   258  O O   . GLN A 1 35  ? 7.114   -22.372 27.254 1.00 75.92  ? 43  GLN A O   1 
ATOM   259  C CB  . GLN A 1 35  ? 10.389  -21.444 26.616 1.00 92.22  ? 43  GLN A CB  1 
ATOM   260  C CG  . GLN A 1 35  ? 10.561  -22.951 26.780 1.00 107.66 ? 43  GLN A CG  1 
ATOM   261  C CD  . GLN A 1 35  ? 9.798   -23.761 25.755 1.00 126.08 ? 43  GLN A CD  1 
ATOM   262  O OE1 . GLN A 1 35  ? 10.048  -23.662 24.549 1.00 140.10 ? 43  GLN A OE1 1 
ATOM   263  N NE2 . GLN A 1 35  ? 8.870   -24.587 26.220 1.00 132.94 ? 43  GLN A NE2 1 
ATOM   264  N N   . GLU A 1 36  ? 8.418   -21.849 29.010 1.00 76.63  ? 44  GLU A N   1 
ATOM   265  C CA  . GLU A 1 36  ? 7.709   -22.721 29.930 1.00 80.29  ? 44  GLU A CA  1 
ATOM   266  C C   . GLU A 1 36  ? 6.229   -22.343 29.913 1.00 80.06  ? 44  GLU A C   1 
ATOM   267  O O   . GLU A 1 36  ? 5.370   -23.195 30.127 1.00 98.07  ? 44  GLU A O   1 
ATOM   268  C CB  . GLU A 1 36  ? 8.308   -22.716 31.345 1.00 88.58  ? 44  GLU A CB  1 
ATOM   269  C CG  . GLU A 1 36  ? 9.754   -23.219 31.432 1.00 89.47  ? 44  GLU A CG  1 
ATOM   270  C CD  . GLU A 1 36  ? 10.353  -23.437 32.823 1.00 87.81  ? 44  GLU A CD  1 
ATOM   271  O OE1 . GLU A 1 36  ? 9.756   -23.119 33.872 1.00 84.78  ? 44  GLU A OE1 1 
ATOM   272  O OE2 . GLU A 1 36  ? 11.463  -23.991 32.857 1.00 88.09  ? 44  GLU A OE2 1 
ATOM   273  N N   . ALA A 1 37  ? 5.937   -21.067 29.635 1.00 76.67  ? 45  ALA A N   1 
ATOM   274  C CA  . ALA A 1 37  ? 4.573   -20.552 29.697 1.00 79.94  ? 45  ALA A CA  1 
ATOM   275  C C   . ALA A 1 37  ? 3.822   -20.860 28.407 1.00 76.43  ? 45  ALA A C   1 
ATOM   276  O O   . ALA A 1 37  ? 2.608   -21.054 28.403 1.00 70.52  ? 45  ALA A O   1 
ATOM   277  C CB  . ALA A 1 37  ? 4.591   -19.059 29.954 1.00 79.85  ? 45  ALA A CB  1 
ATOM   278  N N   . MET A 1 38  ? 4.561   -20.877 27.303 1.00 77.48  ? 46  MET A N   1 
ATOM   279  C CA  . MET A 1 38  ? 3.967   -21.090 26.001 1.00 80.72  ? 46  MET A CA  1 
ATOM   280  C C   . MET A 1 38  ? 3.804   -22.579 25.712 1.00 84.78  ? 46  MET A C   1 
ATOM   281  O O   . MET A 1 38  ? 3.026   -22.938 24.834 1.00 100.90 ? 46  MET A O   1 
ATOM   282  C CB  . MET A 1 38  ? 4.835   -20.440 24.925 1.00 79.26  ? 46  MET A CB  1 
ATOM   283  C CG  . MET A 1 38  ? 4.765   -18.942 24.967 1.00 78.45  ? 46  MET A CG  1 
ATOM   284  S SD  . MET A 1 38  ? 5.743   -18.285 23.609 1.00 84.78  ? 46  MET A SD  1 
ATOM   285  C CE  . MET A 1 38  ? 4.576   -18.471 22.249 1.00 84.00  ? 46  MET A CE  1 
ATOM   286  N N   . SER A 1 39  ? 4.556   -23.432 26.421 1.00 85.06  ? 47  SER A N   1 
ATOM   287  C CA  . SER A 1 39  ? 4.436   -24.875 26.274 1.00 79.90  ? 47  SER A CA  1 
ATOM   288  C C   . SER A 1 39  ? 3.612   -25.456 27.424 1.00 80.05  ? 47  SER A C   1 
ATOM   289  O O   . SER A 1 39  ? 3.724   -26.638 27.733 1.00 83.43  ? 47  SER A O   1 
ATOM   290  C CB  . SER A 1 39  ? 5.799   -25.512 26.191 1.00 80.19  ? 47  SER A CB  1 
ATOM   291  O OG  . SER A 1 39  ? 6.503   -25.356 27.416 1.00 84.85  ? 47  SER A OG  1 
ATOM   292  N N   . GLY A 1 40  ? 2.787   -24.611 28.057 1.00 78.29  ? 48  GLY A N   1 
ATOM   293  C CA  . GLY A 1 40  ? 2.003   -24.997 29.217 1.00 79.54  ? 48  GLY A CA  1 
ATOM   294  C C   . GLY A 1 40  ? 2.808   -25.852 30.196 1.00 85.55  ? 48  GLY A C   1 
ATOM   295  O O   . GLY A 1 40  ? 2.247   -26.756 30.811 1.00 69.93  ? 48  GLY A O   1 
ATOM   296  N N   . ALA A 1 41  ? 4.107   -25.540 30.346 1.00 83.13  ? 49  ALA A N   1 
ATOM   297  C CA  . ALA A 1 41  ? 5.034   -26.359 31.114 1.00 81.33  ? 49  ALA A CA  1 
ATOM   298  C C   . ALA A 1 41  ? 4.948   -26.017 32.601 1.00 85.73  ? 49  ALA A C   1 
ATOM   299  O O   . ALA A 1 41  ? 4.119   -25.199 32.988 1.00 93.77  ? 49  ALA A O   1 
ATOM   300  C CB  . ALA A 1 41  ? 6.431   -26.167 30.578 1.00 81.02  ? 49  ALA A CB  1 
ATOM   301  N N   . GLN A 1 42  ? 5.805   -26.660 33.414 1.00 100.35 ? 50  GLN A N   1 
ATOM   302  C CA  . GLN A 1 42  ? 5.839   -26.493 34.865 1.00 113.47 ? 50  GLN A CA  1 
ATOM   303  C C   . GLN A 1 42  ? 6.542   -25.183 35.236 1.00 119.96 ? 50  GLN A C   1 
ATOM   304  O O   . GLN A 1 42  ? 7.764   -25.061 35.072 1.00 118.92 ? 50  GLN A O   1 
ATOM   305  C CB  . GLN A 1 42  ? 6.595   -27.654 35.519 1.00 115.50 ? 50  GLN A CB  1 
ATOM   306  C CG  . GLN A 1 42  ? 6.486   -27.707 37.040 1.00 114.17 ? 50  GLN A CG  1 
ATOM   307  C CD  . GLN A 1 42  ? 5.226   -28.395 37.524 1.00 115.78 ? 50  GLN A CD  1 
ATOM   308  O OE1 . GLN A 1 42  ? 5.138   -29.630 37.562 1.00 111.10 ? 50  GLN A OE1 1 
ATOM   309  N NE2 . GLN A 1 42  ? 4.246   -27.599 37.931 1.00 104.68 ? 50  GLN A NE2 1 
ATOM   310  N N   . LEU A 1 43  ? 5.757   -24.229 35.770 1.00 103.39 ? 51  LEU A N   1 
ATOM   311  C CA  . LEU A 1 43  ? 6.242   -22.887 36.057 1.00 98.99  ? 51  LEU A CA  1 
ATOM   312  C C   . LEU A 1 43  ? 7.064   -22.904 37.340 1.00 102.80 ? 51  LEU A C   1 
ATOM   313  O O   . LEU A 1 43  ? 6.568   -23.306 38.389 1.00 112.32 ? 51  LEU A O   1 
ATOM   314  C CB  . LEU A 1 43  ? 5.122   -21.848 36.154 1.00 96.71  ? 51  LEU A CB  1 
ATOM   315  C CG  . LEU A 1 43  ? 4.627   -21.260 34.826 1.00 101.66 ? 51  LEU A CG  1 
ATOM   316  C CD1 . LEU A 1 43  ? 3.714   -20.056 35.052 1.00 98.72  ? 51  LEU A CD1 1 
ATOM   317  C CD2 . LEU A 1 43  ? 5.777   -20.887 33.898 1.00 98.63  ? 51  LEU A CD2 1 
ATOM   318  N N   . ALA A 1 44  ? 8.302   -22.402 37.233 1.00 107.50 ? 52  ALA A N   1 
ATOM   319  C CA  . ALA A 1 44  ? 9.233   -22.313 38.349 1.00 102.66 ? 52  ALA A CA  1 
ATOM   320  C C   . ALA A 1 44  ? 8.660   -21.520 39.530 1.00 92.26  ? 52  ALA A C   1 
ATOM   321  O O   . ALA A 1 44  ? 9.225   -21.606 40.617 1.00 79.60  ? 52  ALA A O   1 
ATOM   322  C CB  . ALA A 1 44  ? 10.546  -21.725 37.871 1.00 95.35  ? 52  ALA A CB  1 
ATOM   323  N N   . LEU A 1 45  ? 7.560   -20.765 39.327 1.00 85.33  ? 53  LEU A N   1 
ATOM   324  C CA  . LEU A 1 45  ? 6.952   -19.966 40.387 1.00 91.59  ? 53  LEU A CA  1 
ATOM   325  C C   . LEU A 1 45  ? 5.429   -19.905 40.215 1.00 86.56  ? 53  LEU A C   1 
ATOM   326  O O   . LEU A 1 45  ? 4.935   -19.920 39.091 1.00 79.40  ? 53  LEU A O   1 
ATOM   327  C CB  . LEU A 1 45  ? 7.549   -18.554 40.387 1.00 101.16 ? 53  LEU A CB  1 
ATOM   328  C CG  . LEU A 1 45  ? 9.078   -18.411 40.483 1.00 98.78  ? 53  LEU A CG  1 
ATOM   329  C CD1 . LEU A 1 45  ? 9.434   -17.006 40.041 1.00 87.10  ? 53  LEU A CD1 1 
ATOM   330  C CD2 . LEU A 1 45  ? 9.678   -18.691 41.865 1.00 94.74  ? 53  LEU A CD2 1 
ATOM   331  N N   . THR A 1 46  ? 4.703   -19.744 41.339 1.00 97.50  ? 54  THR A N   1 
ATOM   332  C CA  . THR A 1 46  ? 3.244   -19.838 41.395 1.00 103.69 ? 54  THR A CA  1 
ATOM   333  C C   . THR A 1 46  ? 2.641   -18.506 40.937 1.00 97.43  ? 54  THR A C   1 
ATOM   334  O O   . THR A 1 46  ? 3.356   -17.534 40.720 1.00 80.47  ? 54  THR A O   1 
ATOM   335  C CB  . THR A 1 46  ? 2.756   -19.996 42.845 1.00 104.22 ? 54  THR A CB  1 
ATOM   336  O OG1 . THR A 1 46  ? 2.942   -18.751 43.511 1.00 91.39  ? 54  THR A OG1 1 
ATOM   337  C CG2 . THR A 1 46  ? 3.472   -21.081 43.630 1.00 101.83 ? 54  THR A CG2 1 
ATOM   338  N N   . GLU A 1 47  ? 1.317   -18.468 40.864 1.00 112.24 ? 55  GLU A N   1 
ATOM   339  C CA  . GLU A 1 47  ? 0.621   -17.235 40.434 1.00 123.22 ? 55  GLU A CA  1 
ATOM   340  C C   . GLU A 1 47  ? 1.016   -16.078 41.359 1.00 123.72 ? 55  GLU A C   1 
ATOM   341  O O   . GLU A 1 47  ? 1.573   -15.085 40.852 1.00 123.71 ? 55  GLU A O   1 
ATOM   342  C CB  . GLU A 1 47  ? -0.888  -17.475 40.475 1.00 125.53 ? 55  GLU A CB  1 
ATOM   343  C CG  . GLU A 1 47  ? -1.271  -18.816 41.094 1.00 128.18 ? 55  GLU A CG  1 
ATOM   344  C CD  . GLU A 1 47  ? -1.306  -19.962 40.099 1.00 146.22 ? 55  GLU A CD  1 
ATOM   345  O OE1 . GLU A 1 47  ? -2.224  -19.983 39.254 1.00 153.13 ? 55  GLU A OE1 1 
ATOM   346  O OE2 . GLU A 1 47  ? -0.409  -20.829 40.165 1.00 149.19 ? 55  GLU A OE2 1 
ATOM   347  N N   . GLN A 1 48  ? 0.738   -16.199 42.657 1.00 122.45 ? 56  GLN A N   1 
ATOM   348  C CA  . GLN A 1 48  ? 0.997   -15.066 43.584 1.00 124.69 ? 56  GLN A CA  1 
ATOM   349  C C   . GLN A 1 48  ? 2.476   -14.671 43.525 1.00 113.95 ? 56  GLN A C   1 
ATOM   350  O O   . GLN A 1 48  ? 2.753   -13.469 43.445 1.00 121.11 ? 56  GLN A O   1 
ATOM   351  C CB  . GLN A 1 48  ? 0.602   -15.419 45.015 1.00 133.65 ? 56  GLN A CB  1 
ATOM   352  C CG  . GLN A 1 48  ? -0.554  -14.586 45.558 1.00 136.49 ? 56  GLN A CG  1 
ATOM   353  C CD  . GLN A 1 48  ? -0.200  -13.129 45.766 1.00 133.48 ? 56  GLN A CD  1 
ATOM   354  O OE1 . GLN A 1 48  ? -0.237  -12.317 44.836 1.00 140.56 ? 56  GLN A OE1 1 
ATOM   355  N NE2 . GLN A 1 48  ? 0.136   -12.781 46.998 1.00 113.10 ? 56  GLN A NE2 1 
ATOM   356  N N   . GLN A 1 49  ? 3.376   -15.651 43.576 1.00 104.72 ? 57  GLN A N   1 
ATOM   357  C CA  . GLN A 1 49  ? 4.833   -15.367 43.533 1.00 100.03 ? 57  GLN A CA  1 
ATOM   358  C C   . GLN A 1 49  ? 5.124   -14.407 42.376 1.00 97.96  ? 57  GLN A C   1 
ATOM   359  O O   . GLN A 1 49  ? 5.627   -13.295 42.625 1.00 83.22  ? 57  GLN A O   1 
ATOM   360  C CB  . GLN A 1 49  ? 5.612   -16.664 43.344 1.00 93.88  ? 57  GLN A CB  1 
ATOM   361  C CG  . GLN A 1 49  ? 6.273   -17.185 44.615 1.00 88.13  ? 57  GLN A CG  1 
ATOM   362  C CD  . GLN A 1 49  ? 6.286   -18.694 44.694 1.00 88.60  ? 57  GLN A CD  1 
ATOM   363  O OE1 . GLN A 1 49  ? 6.737   -19.385 43.774 1.00 78.97  ? 57  GLN A OE1 1 
ATOM   364  N NE2 . GLN A 1 49  ? 5.783   -19.223 45.799 1.00 94.13  ? 57  GLN A NE2 1 
ATOM   365  N N   . MET A 1 50  ? 4.821   -14.834 41.156 1.00 92.75  ? 58  MET A N   1 
ATOM   366  C CA  . MET A 1 50  ? 5.015   -13.962 40.008 1.00 86.06  ? 58  MET A CA  1 
ATOM   367  C C   . MET A 1 50  ? 4.212   -12.669 40.153 1.00 85.91  ? 58  MET A C   1 
ATOM   368  O O   . MET A 1 50  ? 4.661   -11.617 39.718 1.00 82.49  ? 58  MET A O   1 
ATOM   369  C CB  . MET A 1 50  ? 4.577   -14.651 38.719 1.00 85.65  ? 58  MET A CB  1 
ATOM   370  C CG  . MET A 1 50  ? 5.543   -15.702 38.250 1.00 93.33  ? 58  MET A CG  1 
ATOM   371  S SD  . MET A 1 50  ? 4.777   -16.818 37.059 1.00 112.09 ? 58  MET A SD  1 
ATOM   372  C CE  . MET A 1 50  ? 6.306   -17.327 36.273 1.00 91.74  ? 58  MET A CE  1 
ATOM   373  N N   . LYS A 1 51  ? 3.025   -12.740 40.741 1.00 89.91  ? 59  LYS A N   1 
ATOM   374  C CA  . LYS A 1 51  ? 2.225   -11.497 40.814 1.00 100.99 ? 59  LYS A CA  1 
ATOM   375  C C   . LYS A 1 51  ? 2.935   -10.548 41.782 1.00 92.55  ? 59  LYS A C   1 
ATOM   376  O O   . LYS A 1 51  ? 3.195   -9.388  41.416 1.00 82.00  ? 59  LYS A O   1 
ATOM   377  C CB  . LYS A 1 51  ? 0.802   -11.779 41.300 1.00 109.86 ? 59  LYS A CB  1 
ATOM   378  C CG  . LYS A 1 51  ? 0.013   -10.562 41.760 1.00 109.61 ? 59  LYS A CG  1 
ATOM   379  C CD  . LYS A 1 51  ? -0.276  -9.571  40.638 1.00 116.02 ? 59  LYS A CD  1 
ATOM   380  C CE  . LYS A 1 51  ? -1.467  -8.713  40.919 1.00 117.25 ? 59  LYS A CE  1 
ATOM   381  N NZ  . LYS A 1 51  ? -1.265  -7.339  40.453 1.00 113.82 ? 59  LYS A NZ  1 
ATOM   382  N N   . ASP A 1 52  ? 3.236   -11.046 42.974 1.00 94.26  ? 60  ASP A N   1 
ATOM   383  C CA  . ASP A 1 52  ? 3.895   -10.192 43.990 1.00 93.29  ? 60  ASP A CA  1 
ATOM   384  C C   . ASP A 1 52  ? 5.205   -9.677  43.395 1.00 87.40  ? 60  ASP A C   1 
ATOM   385  O O   . ASP A 1 52  ? 5.582   -8.537  43.711 1.00 87.10  ? 60  ASP A O   1 
ATOM   386  C CB  . ASP A 1 52  ? 4.069   -10.935 45.302 1.00 96.29  ? 60  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 52  ? 2.806   -11.089 46.134 1.00 103.98 ? 60  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 52  ? 1.781   -10.485 45.759 1.00 114.54 ? 60  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 52  ? 2.860   -11.812 47.150 1.00 106.75 ? 60  ASP A OD2 1 
ATOM   390  N N   . VAL A 1 53  ? 5.861   -10.480 42.555 1.00 83.10  ? 61  VAL A N   1 
ATOM   391  C CA  . VAL A 1 53  ? 7.073   -9.970  41.911 1.00 83.36  ? 61  VAL A CA  1 
ATOM   392  C C   . VAL A 1 53  ? 6.751   -8.764  41.012 1.00 85.15  ? 61  VAL A C   1 
ATOM   393  O O   . VAL A 1 53  ? 7.558   -7.838  40.954 1.00 85.63  ? 61  VAL A O   1 
ATOM   394  C CB  . VAL A 1 53  ? 7.893   -11.022 41.120 1.00 79.94  ? 61  VAL A CB  1 
ATOM   395  C CG1 . VAL A 1 53  ? 8.668   -10.428 39.944 1.00 76.93  ? 61  VAL A CG1 1 
ATOM   396  C CG2 . VAL A 1 53  ? 8.866   -11.804 41.996 1.00 72.24  ? 61  VAL A CG2 1 
ATOM   397  N N   . LEU A 1 54  ? 5.607   -8.762  40.302 1.00 82.30  ? 62  LEU A N   1 
ATOM   398  C CA  . LEU A 1 54  ? 5.339   -7.741  39.293 1.00 75.77  ? 62  LEU A CA  1 
ATOM   399  C C   . LEU A 1 54  ? 4.732   -6.484  39.909 1.00 77.15  ? 62  LEU A C   1 
ATOM   400  O O   . LEU A 1 54  ? 4.575   -5.486  39.209 1.00 83.62  ? 62  LEU A O   1 
ATOM   401  C CB  . LEU A 1 54  ? 4.452   -8.277  38.173 1.00 72.33  ? 62  LEU A CB  1 
ATOM   402  C CG  . LEU A 1 54  ? 5.108   -9.322  37.263 1.00 73.40  ? 62  LEU A CG  1 
ATOM   403  C CD1 . LEU A 1 54  ? 4.065   -9.942  36.377 1.00 75.38  ? 62  LEU A CD1 1 
ATOM   404  C CD2 . LEU A 1 54  ? 6.230   -8.767  36.409 1.00 75.38  ? 62  LEU A CD2 1 
ATOM   405  N N   . ASN A 1 55  ? 4.399   -6.535  41.203 1.00 77.51  ? 63  ASN A N   1 
ATOM   406  C CA  . ASN A 1 55  ? 3.885   -5.377  41.914 1.00 89.86  ? 63  ASN A CA  1 
ATOM   407  C C   . ASN A 1 55  ? 5.047   -4.610  42.538 1.00 86.42  ? 63  ASN A C   1 
ATOM   408  O O   . ASN A 1 55  ? 5.097   -3.383  42.431 1.00 85.07  ? 63  ASN A O   1 
ATOM   409  C CB  . ASN A 1 55  ? 2.828   -5.785  42.934 1.00 97.49  ? 63  ASN A CB  1 
ATOM   410  C CG  . ASN A 1 55  ? 1.577   -6.316  42.273 1.00 104.72 ? 63  ASN A CG  1 
ATOM   411  O OD1 . ASN A 1 55  ? 1.384   -6.170  41.058 1.00 91.42  ? 63  ASN A OD1 1 
ATOM   412  N ND2 . ASN A 1 55  ? 0.707   -6.928  43.062 1.00 113.40 ? 63  ASN A ND2 1 
ATOM   413  N N   . LYS A 1 56  ? 5.971   -5.354  43.174 1.00 82.91  ? 64  LYS A N   1 
ATOM   414  C CA  . LYS A 1 56  ? 7.237   -4.817  43.656 1.00 77.56  ? 64  LYS A CA  1 
ATOM   415  C C   . LYS A 1 56  ? 7.999   -4.187  42.490 1.00 77.72  ? 64  LYS A C   1 
ATOM   416  O O   . LYS A 1 56  ? 8.826   -3.311  42.702 1.00 84.38  ? 64  LYS A O   1 
ATOM   417  C CB  . LYS A 1 56  ? 8.069   -5.885  44.379 1.00 71.35  ? 64  LYS A CB  1 
ATOM   418  C CG  . LYS A 1 56  ? 9.476   -5.505  44.870 1.00 78.70  ? 64  LYS A CG  1 
ATOM   419  C CD  . LYS A 1 56  ? 9.605   -4.413  45.933 1.00 88.63  ? 64  LYS A CD  1 
ATOM   420  C CE  . LYS A 1 56  ? 11.053  -4.098  46.249 1.00 94.78  ? 64  LYS A CE  1 
ATOM   421  N NZ  . LYS A 1 56  ? 11.244  -2.764  46.824 1.00 94.12  ? 64  LYS A NZ  1 
ATOM   422  N N   . PHE A 1 57  ? 7.700   -4.617  41.259 1.00 75.36  ? 65  PHE A N   1 
ATOM   423  C CA  . PHE A 1 57  ? 8.294   -4.022  40.076 1.00 71.90  ? 65  PHE A CA  1 
ATOM   424  C C   . PHE A 1 57  ? 7.653   -2.666  39.756 1.00 79.81  ? 65  PHE A C   1 
ATOM   425  O O   . PHE A 1 57  ? 8.370   -1.676  39.619 1.00 84.12  ? 65  PHE A O   1 
ATOM   426  C CB  . PHE A 1 57  ? 8.160   -4.991  38.903 1.00 68.82  ? 65  PHE A CB  1 
ATOM   427  C CG  . PHE A 1 57  ? 8.810   -4.422  37.657 1.00 73.79  ? 65  PHE A CG  1 
ATOM   428  C CD1 . PHE A 1 57  ? 10.072  -3.837  37.726 1.00 76.54  ? 65  PHE A CD1 1 
ATOM   429  C CD2 . PHE A 1 57  ? 8.122   -4.395  36.447 1.00 81.28  ? 65  PHE A CD2 1 
ATOM   430  C CE1 . PHE A 1 57  ? 10.650  -3.284  36.597 1.00 86.88  ? 65  PHE A CE1 1 
ATOM   431  C CE2 . PHE A 1 57  ? 8.701   -3.834  35.319 1.00 84.19  ? 65  PHE A CE2 1 
ATOM   432  C CZ  . PHE A 1 57  ? 9.964   -3.286  35.393 1.00 89.06  ? 65  PHE A CZ  1 
ATOM   433  N N   . GLN A 1 58  ? 6.318   -2.641  39.606 1.00 76.20  ? 66  GLN A N   1 
ATOM   434  C CA  . GLN A 1 58  ? 5.552   -1.424  39.365 1.00 80.02  ? 66  GLN A CA  1 
ATOM   435  C C   . GLN A 1 58  ? 5.788   -0.394  40.473 1.00 88.64  ? 66  GLN A C   1 
ATOM   436  O O   . GLN A 1 58  ? 5.918   0.787   40.182 1.00 90.04  ? 66  GLN A O   1 
ATOM   437  C CB  . GLN A 1 58  ? 4.056   -1.745  39.324 1.00 84.78  ? 66  GLN A CB  1 
ATOM   438  C CG  . GLN A 1 58  ? 3.595   -2.517  38.092 1.00 88.55  ? 66  GLN A CG  1 
ATOM   439  C CD  . GLN A 1 58  ? 2.715   -1.702  37.165 1.00 101.87 ? 66  GLN A CD  1 
ATOM   440  O OE1 . GLN A 1 58  ? 1.704   -1.124  37.582 1.00 99.01  ? 66  GLN A OE1 1 
ATOM   441  N NE2 . GLN A 1 58  ? 3.071   -1.654  35.888 1.00 110.89 ? 66  GLN A NE2 1 
ATOM   442  N N   . LYS A 1 59  ? 5.777   -0.843  41.737 1.00 89.89  ? 67  LYS A N   1 
ATOM   443  C CA  . LYS A 1 59  ? 6.157   -0.022  42.879 1.00 92.30  ? 67  LYS A CA  1 
ATOM   444  C C   . LYS A 1 59  ? 7.577   0.526   42.711 1.00 91.24  ? 67  LYS A C   1 
ATOM   445  O O   . LYS A 1 59  ? 7.809   1.697   42.988 1.00 85.21  ? 67  LYS A O   1 
ATOM   446  C CB  . LYS A 1 59  ? 6.160   -0.808  44.198 1.00 101.18 ? 67  LYS A CB  1 
ATOM   447  C CG  . LYS A 1 59  ? 4.955   -0.664  45.121 1.00 108.27 ? 67  LYS A CG  1 
ATOM   448  C CD  . LYS A 1 59  ? 3.760   -1.566  44.845 1.00 108.56 ? 67  LYS A CD  1 
ATOM   449  C CE  . LYS A 1 59  ? 2.927   -1.735  46.075 1.00 107.57 ? 67  LYS A CE  1 
ATOM   450  N NZ  . LYS A 1 59  ? 1.965   -2.819  45.881 1.00 109.97 ? 67  LYS A NZ  1 
ATOM   451  N N   . ASP A 1 60  ? 8.532   -0.347  42.342 1.00 89.83  ? 68  ASP A N   1 
ATOM   452  C CA  . ASP A 1 60  ? 9.903   0.052   42.056 1.00 81.57  ? 68  ASP A CA  1 
ATOM   453  C C   . ASP A 1 60  ? 9.868   1.152   40.995 1.00 80.48  ? 68  ASP A C   1 
ATOM   454  O O   . ASP A 1 60  ? 10.524  2.182   41.124 1.00 82.48  ? 68  ASP A O   1 
ATOM   455  C CB  . ASP A 1 60  ? 10.774  -1.102  41.552 1.00 86.90  ? 68  ASP A CB  1 
ATOM   456  C CG  . ASP A 1 60  ? 11.377  -2.085  42.560 1.00 94.69  ? 68  ASP A CG  1 
ATOM   457  O OD1 . ASP A 1 60  ? 11.862  -3.175  42.120 1.00 85.29  ? 68  ASP A OD1 1 
ATOM   458  O OD2 . ASP A 1 60  ? 11.375  -1.770  43.774 1.00 98.84  ? 68  ASP A OD2 1 
ATOM   459  N N   . LEU A 1 61  ? 9.068   0.926   39.952 1.00 80.88  ? 69  LEU A N   1 
ATOM   460  C CA  . LEU A 1 61  ? 9.138   1.693   38.719 1.00 80.56  ? 69  LEU A CA  1 
ATOM   461  C C   . LEU A 1 61  ? 8.385   3.022   38.836 1.00 80.62  ? 69  LEU A C   1 
ATOM   462  O O   . LEU A 1 61  ? 8.715   3.979   38.136 1.00 70.13  ? 69  LEU A O   1 
ATOM   463  C CB  . LEU A 1 61  ? 8.555   0.772   37.648 1.00 79.51  ? 69  LEU A CB  1 
ATOM   464  C CG  . LEU A 1 61  ? 8.850   1.108   36.183 1.00 88.97  ? 69  LEU A CG  1 
ATOM   465  C CD1 . LEU A 1 61  ? 10.334  1.255   35.830 1.00 92.04  ? 69  LEU A CD1 1 
ATOM   466  C CD2 . LEU A 1 61  ? 8.213   0.005   35.350 1.00 87.16  ? 69  LEU A CD2 1 
ATOM   467  N N   . MET A 1 62  ? 7.356   3.060   39.696 1.00 87.23  ? 70  MET A N   1 
ATOM   468  C CA  . MET A 1 62  ? 6.645   4.285   40.037 1.00 86.49  ? 70  MET A CA  1 
ATOM   469  C C   . MET A 1 62  ? 7.558   5.209   40.840 1.00 84.80  ? 70  MET A C   1 
ATOM   470  O O   . MET A 1 62  ? 7.491   6.422   40.689 1.00 87.59  ? 70  MET A O   1 
ATOM   471  C CB  . MET A 1 62  ? 5.393   4.007   40.880 1.00 96.44  ? 70  MET A CB  1 
ATOM   472  C CG  . MET A 1 62  ? 4.089   3.910   40.100 1.00 103.88 ? 70  MET A CG  1 
ATOM   473  S SD  . MET A 1 62  ? 2.669   3.501   41.144 1.00 121.01 ? 70  MET A SD  1 
ATOM   474  C CE  . MET A 1 62  ? 2.760   4.522   42.625 1.00 102.51 ? 70  MET A CE  1 
ATOM   475  N N   . ALA A 1 63  ? 8.396   4.628   41.706 1.00 85.42  ? 71  ALA A N   1 
ATOM   476  C CA  . ALA A 1 63  ? 9.365   5.385   42.487 1.00 82.63  ? 71  ALA A CA  1 
ATOM   477  C C   . ALA A 1 63  ? 10.469  5.952   41.586 1.00 75.50  ? 71  ALA A C   1 
ATOM   478  O O   . ALA A 1 63  ? 10.767  7.142   41.655 1.00 71.17  ? 71  ALA A O   1 
ATOM   479  C CB  . ALA A 1 63  ? 9.928   4.509   43.597 1.00 80.63  ? 71  ALA A CB  1 
ATOM   480  N N   . LYS A 1 64  ? 11.090  5.098   40.760 1.00 68.92  ? 72  LYS A N   1 
ATOM   481  C CA  . LYS A 1 64  ? 12.061  5.559   39.782 1.00 70.20  ? 72  LYS A CA  1 
ATOM   482  C C   . LYS A 1 64  ? 11.493  6.766   39.025 1.00 66.84  ? 72  LYS A C   1 
ATOM   483  O O   . LYS A 1 64  ? 12.121  7.817   38.976 1.00 64.45  ? 72  LYS A O   1 
ATOM   484  C CB  . LYS A 1 64  ? 12.471  4.462   38.787 1.00 74.71  ? 72  LYS A CB  1 
ATOM   485  C CG  . LYS A 1 64  ? 13.481  4.913   37.706 1.00 86.11  ? 72  LYS A CG  1 
ATOM   486  C CD  . LYS A 1 64  ? 13.182  4.496   36.261 1.00 92.57  ? 72  LYS A CD  1 
ATOM   487  C CE  . LYS A 1 64  ? 13.868  5.359   35.220 1.00 93.06  ? 72  LYS A CE  1 
ATOM   488  N NZ  . LYS A 1 64  ? 13.222  5.291   33.902 1.00 94.29  ? 72  LYS A NZ  1 
ATOM   489  N N   . ARG A 1 65  ? 10.302  6.636   38.431 1.00 62.64  ? 73  ARG A N   1 
ATOM   490  C CA  . ARG A 1 65  ? 9.852   7.643   37.485 1.00 66.61  ? 73  ARG A CA  1 
ATOM   491  C C   . ARG A 1 65  ? 9.368   8.902   38.204 1.00 68.21  ? 73  ARG A C   1 
ATOM   492  O O   . ARG A 1 65  ? 9.351   9.990   37.634 1.00 76.19  ? 73  ARG A O   1 
ATOM   493  C CB  . ARG A 1 65  ? 8.917   7.034   36.437 1.00 68.85  ? 73  ARG A CB  1 
ATOM   494  C CG  . ARG A 1 65  ? 9.760   6.140   35.533 1.00 93.60  ? 73  ARG A CG  1 
ATOM   495  C CD  . ARG A 1 65  ? 9.652   6.413   34.034 1.00 110.51 ? 73  ARG A CD  1 
ATOM   496  N NE  . ARG A 1 65  ? 8.264   6.291   33.578 1.00 121.78 ? 73  ARG A NE  1 
ATOM   497  C CZ  . ARG A 1 65  ? 7.535   5.184   33.673 1.00 113.85 ? 73  ARG A CZ  1 
ATOM   498  N NH1 . ARG A 1 65  ? 8.099   4.040   34.038 1.00 100.17 ? 73  ARG A NH1 1 
ATOM   499  N NH2 . ARG A 1 65  ? 6.246   5.226   33.379 1.00 114.03 ? 73  ARG A NH2 1 
ATOM   500  N N   . THR A 1 66  ? 9.025   8.786   39.482 1.00 72.35  ? 74  THR A N   1 
ATOM   501  C CA  . THR A 1 66  ? 8.764   9.972   40.273 1.00 69.31  ? 74  THR A CA  1 
ATOM   502  C C   . THR A 1 66  ? 10.051  10.777  40.407 1.00 66.71  ? 74  THR A C   1 
ATOM   503  O O   . THR A 1 66  ? 10.040  11.998  40.275 1.00 63.85  ? 74  THR A O   1 
ATOM   504  C CB  . THR A 1 66  ? 8.189   9.548   41.618 1.00 76.75  ? 74  THR A CB  1 
ATOM   505  O OG1 . THR A 1 66  ? 6.852   9.279   41.210 1.00 70.51  ? 74  THR A OG1 1 
ATOM   506  C CG2 . THR A 1 66  ? 8.270   10.628  42.686 1.00 80.24  ? 74  THR A CG2 1 
ATOM   507  N N   . ALA A 1 67  ? 11.155  10.071  40.652 1.00 69.00  ? 75  ALA A N   1 
ATOM   508  C CA  . ALA A 1 67  ? 12.450  10.706  40.827 1.00 80.60  ? 75  ALA A CA  1 
ATOM   509  C C   . ALA A 1 67  ? 12.947  11.291  39.504 1.00 74.59  ? 75  ALA A C   1 
ATOM   510  O O   . ALA A 1 67  ? 13.489  12.386  39.499 1.00 76.10  ? 75  ALA A O   1 
ATOM   511  C CB  . ALA A 1 67  ? 13.437  9.719   41.424 1.00 85.56  ? 75  ALA A CB  1 
ATOM   512  N N   . GLU A 1 68  ? 12.779  10.550  38.399 1.00 78.95  ? 76  GLU A N   1 
ATOM   513  C CA  . GLU A 1 68  ? 13.053  11.060  37.063 1.00 76.51  ? 76  GLU A CA  1 
ATOM   514  C C   . GLU A 1 68  ? 12.287  12.373  36.873 1.00 65.39  ? 76  GLU A C   1 
ATOM   515  O O   . GLU A 1 68  ? 12.883  13.397  36.557 1.00 62.43  ? 76  GLU A O   1 
ATOM   516  C CB  . GLU A 1 68  ? 12.735  9.966   36.035 1.00 87.92  ? 76  GLU A CB  1 
ATOM   517  C CG  . GLU A 1 68  ? 12.698  10.424  34.576 1.00 98.39  ? 76  GLU A CG  1 
ATOM   518  C CD  . GLU A 1 68  ? 12.086  9.414   33.614 1.00 104.34 ? 76  GLU A CD  1 
ATOM   519  O OE1 . GLU A 1 68  ? 12.667  8.317   33.463 1.00 117.51 ? 76  GLU A OE1 1 
ATOM   520  O OE2 . GLU A 1 68  ? 11.022  9.710   33.024 1.00 95.14  ? 76  GLU A OE2 1 
ATOM   521  N N   . PHE A 1 69  ? 10.976  12.357  37.133 1.00 58.95  ? 77  PHE A N   1 
ATOM   522  C CA  . PHE A 1 69  ? 10.130  13.517  36.901 1.00 63.45  ? 77  PHE A CA  1 
ATOM   523  C C   . PHE A 1 69  ? 10.568  14.732  37.718 1.00 63.05  ? 77  PHE A C   1 
ATOM   524  O O   . PHE A 1 69  ? 10.452  15.857  37.251 1.00 68.41  ? 77  PHE A O   1 
ATOM   525  C CB  . PHE A 1 69  ? 8.701   13.112  37.248 1.00 66.11  ? 77  PHE A CB  1 
ATOM   526  C CG  . PHE A 1 69  ? 7.641   14.193  37.075 1.00 73.58  ? 77  PHE A CG  1 
ATOM   527  C CD1 . PHE A 1 69  ? 6.849   14.238  35.928 1.00 76.84  ? 77  PHE A CD1 1 
ATOM   528  C CD2 . PHE A 1 69  ? 7.403   15.128  38.077 1.00 73.64  ? 77  PHE A CD2 1 
ATOM   529  C CE1 . PHE A 1 69  ? 5.852   15.193  35.787 1.00 76.52  ? 77  PHE A CE1 1 
ATOM   530  C CE2 . PHE A 1 69  ? 6.405   16.084  37.930 1.00 76.44  ? 77  PHE A CE2 1 
ATOM   531  C CZ  . PHE A 1 69  ? 5.637   16.113  36.787 1.00 74.48  ? 77  PHE A CZ  1 
ATOM   532  N N   . ASN A 1 70  ? 11.055  14.499  38.942 1.00 64.10  ? 78  ASN A N   1 
ATOM   533  C CA  . ASN A 1 70  ? 11.431  15.565  39.859 1.00 60.49  ? 78  ASN A CA  1 
ATOM   534  C C   . ASN A 1 70  ? 12.783  16.174  39.499 1.00 61.59  ? 78  ASN A C   1 
ATOM   535  O O   . ASN A 1 70  ? 12.952  17.378  39.625 1.00 75.67  ? 78  ASN A O   1 
ATOM   536  C CB  . ASN A 1 70  ? 11.421  15.081  41.304 1.00 61.21  ? 78  ASN A CB  1 
ATOM   537  C CG  . ASN A 1 70  ? 10.021  14.802  41.797 1.00 62.94  ? 78  ASN A CG  1 
ATOM   538  O OD1 . ASN A 1 70  ? 9.031   15.233  41.193 1.00 68.72  ? 78  ASN A OD1 1 
ATOM   539  N ND2 . ASN A 1 70  ? 9.913   14.080  42.898 1.00 65.32  ? 78  ASN A ND2 1 
ATOM   540  N N   . LYS A 1 71  ? 13.752  15.355  39.080 1.00 65.22  ? 79  LYS A N   1 
ATOM   541  C CA  . LYS A 1 71  ? 15.006  15.871  38.551 1.00 66.90  ? 79  LYS A CA  1 
ATOM   542  C C   . LYS A 1 71  ? 14.694  16.787  37.368 1.00 69.54  ? 79  LYS A C   1 
ATOM   543  O O   . LYS A 1 71  ? 15.149  17.926  37.336 1.00 72.80  ? 79  LYS A O   1 
ATOM   544  C CB  . LYS A 1 71  ? 15.941  14.724  38.150 1.00 69.38  ? 79  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 71  ? 16.392  13.846  39.315 1.00 84.13  ? 79  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 71  ? 16.910  12.454  38.951 1.00 91.84  ? 79  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 71  ? 17.189  11.584  40.146 1.00 84.10  ? 79  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 71  ? 17.941  10.395  39.743 1.00 82.75  ? 79  LYS A NZ  1 
ATOM   549  N N   . LYS A 1 72  ? 13.865  16.282  36.442 1.00 65.24  ? 80  LYS A N   1 
ATOM   550  C CA  . LYS A 1 72  ? 13.476  16.989  35.233 1.00 66.64  ? 80  LYS A CA  1 
ATOM   551  C C   . LYS A 1 72  ? 12.850  18.341  35.571 1.00 63.72  ? 80  LYS A C   1 
ATOM   552  O O   . LYS A 1 72  ? 13.132  19.352  34.922 1.00 53.31  ? 80  LYS A O   1 
ATOM   553  C CB  . LYS A 1 72  ? 12.490  16.131  34.435 1.00 70.29  ? 80  LYS A CB  1 
ATOM   554  C CG  . LYS A 1 72  ? 13.135  14.981  33.682 1.00 75.78  ? 80  LYS A CG  1 
ATOM   555  C CD  . LYS A 1 72  ? 12.138  14.069  32.974 1.00 91.65  ? 80  LYS A CD  1 
ATOM   556  C CE  . LYS A 1 72  ? 12.774  13.161  31.952 1.00 94.71  ? 80  LYS A CE  1 
ATOM   557  N NZ  . LYS A 1 72  ? 11.789  12.647  30.996 1.00 91.55  ? 80  LYS A NZ  1 
ATOM   558  N N   . ALA A 1 73  ? 12.006  18.355  36.602 1.00 56.88  ? 81  ALA A N   1 
ATOM   559  C CA  . ALA A 1 73  ? 11.391  19.599  37.026 1.00 60.68  ? 81  ALA A CA  1 
ATOM   560  C C   . ALA A 1 73  ? 12.424  20.587  37.598 1.00 63.01  ? 81  ALA A C   1 
ATOM   561  O O   . ALA A 1 73  ? 12.367  21.740  37.175 1.00 67.38  ? 81  ALA A O   1 
ATOM   562  C CB  . ALA A 1 73  ? 10.247  19.309  37.966 1.00 55.93  ? 81  ALA A CB  1 
ATOM   563  N N   . ASP A 1 74  ? 13.346  20.191  38.522 1.00 57.22  ? 82  ASP A N   1 
ATOM   564  C CA  . ASP A 1 74  ? 14.332  21.147  39.049 1.00 60.11  ? 82  ASP A CA  1 
ATOM   565  C C   . ASP A 1 74  ? 15.174  21.580  37.853 1.00 54.56  ? 82  ASP A C   1 
ATOM   566  O O   . ASP A 1 74  ? 15.401  22.771  37.673 1.00 58.14  ? 82  ASP A O   1 
ATOM   567  C CB  . ASP A 1 74  ? 15.052  20.792  40.371 1.00 54.45  ? 82  ASP A CB  1 
ATOM   568  C CG  . ASP A 1 74  ? 16.345  21.549  40.762 1.00 67.93  ? 82  ASP A CG  1 
ATOM   569  O OD1 . ASP A 1 74  ? 16.367  22.483  41.625 1.00 69.85  ? 82  ASP A OD1 1 
ATOM   570  O OD2 . ASP A 1 74  ? 17.415  21.162  40.280 1.00 74.10  ? 82  ASP A OD2 1 
ATOM   571  N N   . GLU A 1 75  ? 15.566  20.648  36.983 1.00 56.73  ? 83  GLU A N   1 
ATOM   572  C CA  . GLU A 1 75  ? 16.545  21.000  35.964 1.00 68.50  ? 83  GLU A CA  1 
ATOM   573  C C   . GLU A 1 75  ? 15.894  21.883  34.891 1.00 66.72  ? 83  GLU A C   1 
ATOM   574  O O   . GLU A 1 75  ? 16.504  22.859  34.452 1.00 58.71  ? 83  GLU A O   1 
ATOM   575  C CB  . GLU A 1 75  ? 17.318  19.795  35.422 1.00 81.46  ? 83  GLU A CB  1 
ATOM   576  C CG  . GLU A 1 75  ? 16.616  19.041  34.297 1.00 101.84 ? 83  GLU A CG  1 
ATOM   577  C CD  . GLU A 1 75  ? 17.391  17.841  33.774 1.00 121.07 ? 83  GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 75  ? 18.476  17.542  34.328 1.00 131.02 ? 83  GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 75  ? 16.903  17.201  32.811 1.00 122.18 ? 83  GLU A OE2 1 
ATOM   580  N N   . ASN A 1 76  ? 14.654  21.564  34.489 1.00 63.49  ? 84  ASN A N   1 
ATOM   581  C CA  . ASN A 1 76  ? 13.992  22.319  33.436 1.00 59.52  ? 84  ASN A CA  1 
ATOM   582  C C   . ASN A 1 76  ? 13.749  23.752  33.919 1.00 57.43  ? 84  ASN A C   1 
ATOM   583  O O   . ASN A 1 76  ? 13.841  24.699  33.138 1.00 51.21  ? 84  ASN A O   1 
ATOM   584  C CB  . ASN A 1 76  ? 12.688  21.666  32.963 1.00 68.50  ? 84  ASN A CB  1 
ATOM   585  C CG  . ASN A 1 76  ? 12.825  20.472  32.031 1.00 65.27  ? 84  ASN A CG  1 
ATOM   586  O OD1 . ASN A 1 76  ? 13.903  20.187  31.490 1.00 61.45  ? 84  ASN A OD1 1 
ATOM   587  N ND2 . ASN A 1 76  ? 11.720  19.767  31.805 1.00 60.04  ? 84  ASN A ND2 1 
ATOM   588  N N   . LYS A 1 77  ? 13.430  23.916  35.211 1.00 58.16  ? 85  LYS A N   1 
ATOM   589  C CA  . LYS A 1 77  ? 13.081  25.229  35.748 1.00 57.80  ? 85  LYS A CA  1 
ATOM   590  C C   . LYS A 1 77  ? 14.338  26.098  35.853 1.00 59.99  ? 85  LYS A C   1 
ATOM   591  O O   . LYS A 1 77  ? 14.307  27.296  35.598 1.00 61.22  ? 85  LYS A O   1 
ATOM   592  C CB  . LYS A 1 77  ? 12.298  25.106  37.062 1.00 57.14  ? 85  LYS A CB  1 
ATOM   593  C CG  . LYS A 1 77  ? 11.816  26.423  37.643 1.00 63.86  ? 85  LYS A CG  1 
ATOM   594  C CD  . LYS A 1 77  ? 10.490  26.352  38.398 1.00 76.30  ? 85  LYS A CD  1 
ATOM   595  C CE  . LYS A 1 77  ? 10.564  25.723  39.768 1.00 82.54  ? 85  LYS A CE  1 
ATOM   596  N NZ  . LYS A 1 77  ? 9.253   25.588  40.417 1.00 79.62  ? 85  LYS A NZ  1 
ATOM   597  N N   . VAL A 1 78  ? 15.468  25.482  36.188 1.00 60.53  ? 86  VAL A N   1 
ATOM   598  C CA  . VAL A 1 78  ? 16.725  26.202  36.291 1.00 62.40  ? 86  VAL A CA  1 
ATOM   599  C C   . VAL A 1 78  ? 17.217  26.607  34.899 1.00 60.41  ? 86  VAL A C   1 
ATOM   600  O O   . VAL A 1 78  ? 17.714  27.711  34.727 1.00 67.08  ? 86  VAL A O   1 
ATOM   601  C CB  . VAL A 1 78  ? 17.740  25.336  37.075 1.00 64.31  ? 86  VAL A CB  1 
ATOM   602  C CG1 . VAL A 1 78  ? 19.148  25.366  36.500 1.00 64.87  ? 86  VAL A CG1 1 
ATOM   603  C CG2 . VAL A 1 78  ? 17.760  25.711  38.546 1.00 60.53  ? 86  VAL A CG2 1 
ATOM   604  N N   . LYS A 1 79  ? 17.094  25.715  33.909 1.00 65.94  ? 87  LYS A N   1 
ATOM   605  C CA  . LYS A 1 79  ? 17.518  26.012  32.548 1.00 62.90  ? 87  LYS A CA  1 
ATOM   606  C C   . LYS A 1 79  ? 16.670  27.131  31.937 1.00 61.12  ? 87  LYS A C   1 
ATOM   607  O O   . LYS A 1 79  ? 17.167  27.886  31.104 1.00 60.20  ? 87  LYS A O   1 
ATOM   608  C CB  . LYS A 1 79  ? 17.483  24.741  31.698 1.00 69.01  ? 87  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 79  ? 18.608  23.766  31.997 1.00 82.96  ? 87  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 79  ? 18.449  22.439  31.268 1.00 98.53  ? 87  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 79  ? 19.463  21.410  31.674 1.00 108.67 ? 87  LYS A CE  1 
ATOM   612  N NZ  . LYS A 1 79  ? 19.146  20.095  31.104 1.00 111.30 ? 87  LYS A NZ  1 
ATOM   613  N N   . GLY A 1 80  ? 15.402  27.250  32.365 1.00 60.36  ? 88  GLY A N   1 
ATOM   614  C CA  . GLY A 1 80  ? 14.520  28.309  31.899 1.00 53.14  ? 88  GLY A CA  1 
ATOM   615  C C   . GLY A 1 80  ? 14.857  29.653  32.540 1.00 57.97  ? 88  GLY A C   1 
ATOM   616  O O   . GLY A 1 80  ? 14.807  30.670  31.852 1.00 58.05  ? 88  GLY A O   1 
ATOM   617  N N   . GLU A 1 81  ? 15.166  29.652  33.843 1.00 57.57  ? 89  GLU A N   1 
ATOM   618  C CA  . GLU A 1 81  ? 15.430  30.934  34.554 1.00 56.15  ? 89  GLU A CA  1 
ATOM   619  C C   . GLU A 1 81  ? 16.774  31.503  34.075 1.00 55.70  ? 89  GLU A C   1 
ATOM   620  O O   . GLU A 1 81  ? 17.041  32.661  34.398 1.00 52.04  ? 89  GLU A O   1 
ATOM   621  C CB  . GLU A 1 81  ? 15.368  30.784  36.077 1.00 64.05  ? 89  GLU A CB  1 
ATOM   622  C CG  . GLU A 1 81  ? 16.370  29.788  36.651 1.00 67.38  ? 89  GLU A CG  1 
ATOM   623  C CD  . GLU A 1 81  ? 17.740  30.353  36.981 1.00 73.37  ? 89  GLU A CD  1 
ATOM   624  O OE1 . GLU A 1 81  ? 18.732  29.606  36.851 1.00 58.29  ? 89  GLU A OE1 1 
ATOM   625  O OE2 . GLU A 1 81  ? 17.814  31.539  37.362 1.00 86.37  ? 89  GLU A OE2 1 
ATOM   626  N N   . ALA A 1 82  ? 17.598  30.707  33.393 1.00 51.73  ? 90  ALA A N   1 
ATOM   627  C CA  . ALA A 1 82  ? 18.865  31.174  32.800 1.00 56.37  ? 90  ALA A CA  1 
ATOM   628  C C   . ALA A 1 82  ? 18.637  31.533  31.340 1.00 61.61  ? 90  ALA A C   1 
ATOM   629  O O   . ALA A 1 82  ? 19.197  32.530  30.866 1.00 57.21  ? 90  ALA A O   1 
ATOM   630  C CB  . ALA A 1 82  ? 19.888  30.086  32.916 1.00 55.24  ? 90  ALA A CB  1 
ATOM   631  N N   . PHE A 1 83  ? 17.846  30.719  30.649 1.00 64.91  ? 91  PHE A N   1 
ATOM   632  C CA  . PHE A 1 83  ? 17.540  31.036  29.267 1.00 60.17  ? 91  PHE A CA  1 
ATOM   633  C C   . PHE A 1 83  ? 16.896  32.418  29.248 1.00 61.23  ? 91  PHE A C   1 
ATOM   634  O O   . PHE A 1 83  ? 17.281  33.261  28.444 1.00 67.06  ? 91  PHE A O   1 
ATOM   635  C CB  . PHE A 1 83  ? 16.641  30.029  28.547 1.00 56.19  ? 91  PHE A CB  1 
ATOM   636  C CG  . PHE A 1 83  ? 16.228  30.489  27.150 1.00 64.60  ? 91  PHE A CG  1 
ATOM   637  C CD1 . PHE A 1 83  ? 17.020  30.215  26.034 1.00 60.54  ? 91  PHE A CD1 1 
ATOM   638  C CD2 . PHE A 1 83  ? 15.043  31.207  26.949 1.00 69.29  ? 91  PHE A CD2 1 
ATOM   639  C CE1 . PHE A 1 83  ? 16.634  30.638  24.770 1.00 56.44  ? 91  PHE A CE1 1 
ATOM   640  C CE2 . PHE A 1 83  ? 14.662  31.623  25.681 1.00 60.81  ? 91  PHE A CE2 1 
ATOM   641  C CZ  . PHE A 1 83  ? 15.467  31.343  24.599 1.00 57.95  ? 91  PHE A CZ  1 
ATOM   642  N N   . LEU A 1 84  ? 15.931  32.634  30.150 1.00 52.79  ? 92  LEU A N   1 
ATOM   643  C CA  . LEU A 1 84  ? 15.134  33.847  30.153 1.00 50.13  ? 92  LEU A CA  1 
ATOM   644  C C   . LEU A 1 84  ? 15.990  35.015  30.619 1.00 47.21  ? 92  LEU A C   1 
ATOM   645  O O   . LEU A 1 84  ? 15.838  36.135  30.163 1.00 52.81  ? 92  LEU A O   1 
ATOM   646  C CB  . LEU A 1 84  ? 13.903  33.657  31.039 1.00 51.94  ? 92  LEU A CB  1 
ATOM   647  C CG  . LEU A 1 84  ? 12.799  32.754  30.482 1.00 53.46  ? 92  LEU A CG  1 
ATOM   648  C CD1 . LEU A 1 84  ? 11.803  32.387  31.572 1.00 52.73  ? 92  LEU A CD1 1 
ATOM   649  C CD2 . LEU A 1 84  ? 12.070  33.416  29.309 1.00 53.23  ? 92  LEU A CD2 1 
ATOM   650  N N   . THR A 1 85  ? 16.901  34.731  31.533 1.00 56.09  ? 93  THR A N   1 
ATOM   651  C CA  . THR A 1 85  ? 17.805  35.738  32.053 1.00 61.20  ? 93  THR A CA  1 
ATOM   652  C C   . THR A 1 85  ? 18.702  36.242  30.918 1.00 63.75  ? 93  THR A C   1 
ATOM   653  O O   . THR A 1 85  ? 18.834  37.450  30.723 1.00 59.47  ? 93  THR A O   1 
ATOM   654  C CB  . THR A 1 85  ? 18.567  35.135  33.239 1.00 59.03  ? 93  THR A CB  1 
ATOM   655  O OG1 . THR A 1 85  ? 17.578  34.874  34.234 1.00 48.68  ? 93  THR A OG1 1 
ATOM   656  C CG2 . THR A 1 85  ? 19.590  36.080  33.838 1.00 57.17  ? 93  THR A CG2 1 
ATOM   657  N N   . GLU A 1 86  ? 19.295  35.330  30.138 1.00 64.63  ? 94  GLU A N   1 
ATOM   658  C CA  . GLU A 1 86  ? 20.198  35.749  29.074 1.00 66.50  ? 94  GLU A CA  1 
ATOM   659  C C   . GLU A 1 86  ? 19.386  36.360  27.922 1.00 62.05  ? 94  GLU A C   1 
ATOM   660  O O   . GLU A 1 86  ? 19.866  37.243  27.219 1.00 63.99  ? 94  GLU A O   1 
ATOM   661  C CB  . GLU A 1 86  ? 21.173  34.628  28.673 1.00 77.87  ? 94  GLU A CB  1 
ATOM   662  C CG  . GLU A 1 86  ? 22.325  34.359  29.654 1.00 86.14  ? 94  GLU A CG  1 
ATOM   663  C CD  . GLU A 1 86  ? 23.766  34.780  29.322 1.00 99.37  ? 94  GLU A CD  1 
ATOM   664  O OE1 . GLU A 1 86  ? 24.018  35.396  28.258 1.00 98.26  ? 94  GLU A OE1 1 
ATOM   665  O OE2 . GLU A 1 86  ? 24.675  34.477  30.142 1.00 99.07  ? 94  GLU A OE2 1 
ATOM   666  N N   . ASN A 1 87  ? 18.139  35.923  27.724 1.00 65.58  ? 95  ASN A N   1 
ATOM   667  C CA  . ASN A 1 87  ? 17.362  36.374  26.578 1.00 59.85  ? 95  ASN A CA  1 
ATOM   668  C C   . ASN A 1 87  ? 17.012  37.847  26.749 1.00 61.39  ? 95  ASN A C   1 
ATOM   669  O O   . ASN A 1 87  ? 16.923  38.595  25.786 1.00 61.94  ? 95  ASN A O   1 
ATOM   670  C CB  . ASN A 1 87  ? 16.068  35.588  26.394 1.00 55.45  ? 95  ASN A CB  1 
ATOM   671  C CG  . ASN A 1 87  ? 15.557  35.719  24.976 1.00 54.20  ? 95  ASN A CG  1 
ATOM   672  O OD1 . ASN A 1 87  ? 16.350  35.566  24.051 1.00 57.89  ? 95  ASN A OD1 1 
ATOM   673  N ND2 . ASN A 1 87  ? 14.284  36.023  24.765 1.00 48.96  ? 95  ASN A ND2 1 
ATOM   674  N N   . LYS A 1 88  ? 16.770  38.216  28.003 1.00 57.97  ? 96  LYS A N   1 
ATOM   675  C CA  . LYS A 1 88  ? 16.451  39.567  28.435 1.00 63.09  ? 96  LYS A CA  1 
ATOM   676  C C   . LYS A 1 88  ? 17.375  40.624  27.817 1.00 58.20  ? 96  LYS A C   1 
ATOM   677  O O   . LYS A 1 88  ? 16.920  41.734  27.591 1.00 61.37  ? 96  LYS A O   1 
ATOM   678  C CB  . LYS A 1 88  ? 16.582  39.506  29.967 1.00 68.17  ? 96  LYS A CB  1 
ATOM   679  C CG  . LYS A 1 88  ? 15.718  40.413  30.783 1.00 65.92  ? 96  LYS A CG  1 
ATOM   680  C CD  . LYS A 1 88  ? 15.740  40.074  32.269 1.00 72.30  ? 96  LYS A CD  1 
ATOM   681  C CE  . LYS A 1 88  ? 17.006  40.462  32.964 1.00 74.37  ? 96  LYS A CE  1 
ATOM   682  N NZ  . LYS A 1 88  ? 16.768  40.847  34.358 1.00 73.14  ? 96  LYS A NZ  1 
ATOM   683  N N   . ASN A 1 89  ? 18.667  40.305  27.610 1.00 59.84  ? 97  ASN A N   1 
ATOM   684  C CA  . ASN A 1 89  ? 19.681  41.253  27.159 1.00 65.38  ? 97  ASN A CA  1 
ATOM   685  C C   . ASN A 1 89  ? 19.851  41.266  25.643 1.00 62.82  ? 97  ASN A C   1 
ATOM   686  O O   . ASN A 1 89  ? 20.632  42.048  25.120 1.00 62.41  ? 97  ASN A O   1 
ATOM   687  C CB  . ASN A 1 89  ? 21.080  40.900  27.647 1.00 72.42  ? 97  ASN A CB  1 
ATOM   688  C CG  . ASN A 1 89  ? 21.166  40.889  29.150 1.00 76.95  ? 97  ASN A CG  1 
ATOM   689  O OD1 . ASN A 1 89  ? 21.222  41.952  29.774 1.00 90.51  ? 97  ASN A OD1 1 
ATOM   690  N ND2 . ASN A 1 89  ? 21.198  39.706  29.739 1.00 74.86  ? 97  ASN A ND2 1 
ATOM   691  N N   . LYS A 1 90  ? 19.173  40.355  24.950 1.00 68.54  ? 98  LYS A N   1 
ATOM   692  C CA  . LYS A 1 90  ? 19.281  40.264  23.507 1.00 70.33  ? 98  LYS A CA  1 
ATOM   693  C C   . LYS A 1 90  ? 18.419  41.377  22.915 1.00 66.51  ? 98  LYS A C   1 
ATOM   694  O O   . LYS A 1 90  ? 17.330  41.642  23.408 1.00 62.12  ? 98  LYS A O   1 
ATOM   695  C CB  . LYS A 1 90  ? 18.877  38.866  23.024 1.00 70.79  ? 98  LYS A CB  1 
ATOM   696  C CG  . LYS A 1 90  ? 19.528  37.705  23.754 1.00 78.05  ? 98  LYS A CG  1 
ATOM   697  C CD  . LYS A 1 90  ? 21.050  37.644  23.707 1.00 91.88  ? 98  LYS A CD  1 
ATOM   698  C CE  . LYS A 1 90  ? 21.578  36.354  24.288 1.00 105.86 ? 98  LYS A CE  1 
ATOM   699  N NZ  . LYS A 1 90  ? 23.037  36.222  24.193 1.00 113.85 ? 98  LYS A NZ  1 
ATOM   700  N N   . PRO A 1 91  ? 18.884  42.081  21.860 1.00 67.67  ? 99  PRO A N   1 
ATOM   701  C CA  . PRO A 1 91  ? 18.152  43.229  21.325 1.00 65.39  ? 99  PRO A CA  1 
ATOM   702  C C   . PRO A 1 91  ? 16.786  42.848  20.770 1.00 59.92  ? 99  PRO A C   1 
ATOM   703  O O   . PRO A 1 91  ? 16.620  41.766  20.218 1.00 63.91  ? 99  PRO A O   1 
ATOM   704  C CB  . PRO A 1 91  ? 19.094  43.736  20.229 1.00 68.58  ? 99  PRO A CB  1 
ATOM   705  C CG  . PRO A 1 91  ? 19.834  42.492  19.798 1.00 68.14  ? 99  PRO A CG  1 
ATOM   706  C CD  . PRO A 1 91  ? 20.118  41.797  21.113 1.00 67.77  ? 99  PRO A CD  1 
ATOM   707  N N   . GLY A 1 92  ? 15.820  43.759  20.925 1.00 57.23  ? 100 GLY A N   1 
ATOM   708  C CA  . GLY A 1 92  ? 14.479  43.538  20.426 1.00 56.71  ? 100 GLY A CA  1 
ATOM   709  C C   . GLY A 1 92  ? 13.557  42.941  21.487 1.00 62.11  ? 100 GLY A C   1 
ATOM   710  O O   . GLY A 1 92  ? 12.333  43.019  21.344 1.00 63.58  ? 100 GLY A O   1 
ATOM   711  N N   . VAL A 1 93  ? 14.138  42.379  22.559 1.00 58.57  ? 101 VAL A N   1 
ATOM   712  C CA  . VAL A 1 93  ? 13.372  41.575  23.499 1.00 59.75  ? 101 VAL A CA  1 
ATOM   713  C C   . VAL A 1 93  ? 12.806  42.480  24.591 1.00 54.67  ? 101 VAL A C   1 
ATOM   714  O O   . VAL A 1 93  ? 13.514  43.326  25.111 1.00 61.69  ? 101 VAL A O   1 
ATOM   715  C CB  . VAL A 1 93  ? 14.247  40.430  24.044 1.00 61.47  ? 101 VAL A CB  1 
ATOM   716  C CG1 . VAL A 1 93  ? 13.632  39.706  25.239 1.00 62.50  ? 101 VAL A CG1 1 
ATOM   717  C CG2 . VAL A 1 93  ? 14.577  39.443  22.931 1.00 59.95  ? 101 VAL A CG2 1 
ATOM   718  N N   . VAL A 1 94  ? 11.509  42.312  24.884 1.00 51.95  ? 102 VAL A N   1 
ATOM   719  C CA  . VAL A 1 94  ? 10.803  43.009  25.947 1.00 50.98  ? 102 VAL A CA  1 
ATOM   720  C C   . VAL A 1 94  ? 10.255  41.983  26.942 1.00 51.41  ? 102 VAL A C   1 
ATOM   721  O O   . VAL A 1 94  ? 9.670   40.979  26.527 1.00 42.65  ? 102 VAL A O   1 
ATOM   722  C CB  . VAL A 1 94  ? 9.672   43.836  25.315 1.00 56.22  ? 102 VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 94  ? 8.518   44.122  26.278 1.00 55.53  ? 102 VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 94  ? 10.224  45.112  24.717 1.00 59.37  ? 102 VAL A CG2 1 
ATOM   725  N N   . VAL A 1 95  ? 10.454  42.256  28.249 1.00 57.55  ? 103 VAL A N   1 
ATOM   726  C CA  . VAL A 1 95  ? 9.907   41.443  29.335 1.00 52.83  ? 103 VAL A CA  1 
ATOM   727  C C   . VAL A 1 95  ? 8.621   42.098  29.838 1.00 44.88  ? 103 VAL A C   1 
ATOM   728  O O   . VAL A 1 95  ? 8.598   43.282  30.127 1.00 45.03  ? 103 VAL A O   1 
ATOM   729  C CB  . VAL A 1 95  ? 10.882  41.212  30.505 1.00 52.49  ? 103 VAL A CB  1 
ATOM   730  C CG1 . VAL A 1 95  ? 10.303  40.236  31.529 1.00 54.05  ? 103 VAL A CG1 1 
ATOM   731  C CG2 . VAL A 1 95  ? 12.254  40.740  30.029 1.00 49.67  ? 103 VAL A CG2 1 
ATOM   732  N N   . LEU A 1 96  ? 7.533   41.332  29.869 1.00 43.43  ? 104 LEU A N   1 
ATOM   733  C CA  . LEU A 1 96  ? 6.270   41.796  30.409 1.00 46.89  ? 104 LEU A CA  1 
ATOM   734  C C   . LEU A 1 96  ? 6.205   41.470  31.898 1.00 52.32  ? 104 LEU A C   1 
ATOM   735  O O   . LEU A 1 96  ? 6.953   40.601  32.383 1.00 42.23  ? 104 LEU A O   1 
ATOM   736  C CB  . LEU A 1 96  ? 5.165   41.090  29.637 1.00 44.69  ? 104 LEU A CB  1 
ATOM   737  C CG  . LEU A 1 96  ? 4.921   41.636  28.230 1.00 47.81  ? 104 LEU A CG  1 
ATOM   738  C CD1 . LEU A 1 96  ? 4.086   40.672  27.433 1.00 45.84  ? 104 LEU A CD1 1 
ATOM   739  C CD2 . LEU A 1 96  ? 4.271   43.007  28.256 1.00 44.86  ? 104 LEU A CD2 1 
ATOM   740  N N   . PRO A 1 97  ? 5.266   42.110  32.638 1.00 52.44  ? 105 PRO A N   1 
ATOM   741  C CA  . PRO A 1 97  ? 5.223   41.985  34.101 1.00 54.13  ? 105 PRO A CA  1 
ATOM   742  C C   . PRO A 1 97  ? 5.120   40.517  34.514 1.00 56.96  ? 105 PRO A C   1 
ATOM   743  O O   . PRO A 1 97  ? 5.698   40.114  35.521 1.00 57.83  ? 105 PRO A O   1 
ATOM   744  C CB  . PRO A 1 97  ? 3.981   42.784  34.513 1.00 51.86  ? 105 PRO A CB  1 
ATOM   745  C CG  . PRO A 1 97  ? 3.700   43.677  33.327 1.00 50.41  ? 105 PRO A CG  1 
ATOM   746  C CD  . PRO A 1 97  ? 4.161   42.916  32.098 1.00 47.68  ? 105 PRO A CD  1 
ATOM   747  N N   . SER A 1 98  ? 4.413   39.714  33.705 1.00 51.57  ? 106 SER A N   1 
ATOM   748  C CA  . SER A 1 98  ? 4.153   38.329  34.055 1.00 46.17  ? 106 SER A CA  1 
ATOM   749  C C   . SER A 1 98  ? 5.343   37.424  33.756 1.00 44.84  ? 106 SER A C   1 
ATOM   750  O O   . SER A 1 98  ? 5.236   36.218  33.963 1.00 48.17  ? 106 SER A O   1 
ATOM   751  C CB  . SER A 1 98  ? 2.912   37.811  33.370 1.00 48.63  ? 106 SER A CB  1 
ATOM   752  O OG  . SER A 1 98  ? 3.153   37.564  31.987 1.00 53.36  ? 106 SER A OG  1 
ATOM   753  N N   . GLY A 1 99  ? 6.457   37.970  33.247 1.00 53.54  ? 107 GLY A N   1 
ATOM   754  C CA  . GLY A 1 99  ? 7.639   37.164  32.932 1.00 51.16  ? 107 GLY A CA  1 
ATOM   755  C C   . GLY A 1 99  ? 7.657   36.684  31.475 1.00 51.21  ? 107 GLY A C   1 
ATOM   756  O O   . GLY A 1 99  ? 8.669   36.207  31.001 1.00 52.93  ? 107 GLY A O   1 
ATOM   757  N N   . LEU A 1 100 ? 6.531   36.792  30.766 1.00 54.81  ? 108 LEU A N   1 
ATOM   758  C CA  . LEU A 1 100 ? 6.481   36.559  29.331 1.00 58.25  ? 108 LEU A CA  1 
ATOM   759  C C   . LEU A 1 100 ? 7.349   37.584  28.603 1.00 50.58  ? 108 LEU A C   1 
ATOM   760  O O   . LEU A 1 100 ? 7.275   38.769  28.892 1.00 54.27  ? 108 LEU A O   1 
ATOM   761  C CB  . LEU A 1 100 ? 5.015   36.658  28.907 1.00 61.86  ? 108 LEU A CB  1 
ATOM   762  C CG  . LEU A 1 100 ? 4.695   36.407  27.432 1.00 61.18  ? 108 LEU A CG  1 
ATOM   763  C CD1 . LEU A 1 100 ? 5.103   35.025  26.990 1.00 64.11  ? 108 LEU A CD1 1 
ATOM   764  C CD2 . LEU A 1 100 ? 3.216   36.603  27.228 1.00 66.17  ? 108 LEU A CD2 1 
ATOM   765  N N   . GLN A 1 101 ? 8.169   37.114  27.661 1.00 47.95  ? 109 GLN A N   1 
ATOM   766  C CA  . GLN A 1 101 ? 8.935   37.989  26.786 1.00 50.72  ? 109 GLN A CA  1 
ATOM   767  C C   . GLN A 1 101 ? 8.489   37.825  25.331 1.00 49.46  ? 109 GLN A C   1 
ATOM   768  O O   . GLN A 1 101 ? 7.982   36.780  24.935 1.00 46.29  ? 109 GLN A O   1 
ATOM   769  C CB  . GLN A 1 101 ? 10.413  37.623  26.836 1.00 48.76  ? 109 GLN A CB  1 
ATOM   770  C CG  . GLN A 1 101 ? 10.934  37.308  28.235 1.00 48.49  ? 109 GLN A CG  1 
ATOM   771  C CD  . GLN A 1 101 ? 12.406  36.949  28.215 1.00 51.30  ? 109 GLN A CD  1 
ATOM   772  O OE1 . GLN A 1 101 ? 12.985  36.693  27.150 1.00 51.16  ? 109 GLN A OE1 1 
ATOM   773  N NE2 . GLN A 1 101 ? 13.026  36.921  29.387 1.00 50.15  ? 109 GLN A NE2 1 
ATOM   774  N N   . TYR A 1 102 ? 8.734   38.857  24.521 1.00 55.49  ? 110 TYR A N   1 
ATOM   775  C CA  . TYR A 1 102 ? 8.467   38.805  23.091 1.00 54.81  ? 110 TYR A CA  1 
ATOM   776  C C   . TYR A 1 102 ? 9.504   39.654  22.351 1.00 48.79  ? 110 TYR A C   1 
ATOM   777  O O   . TYR A 1 102 ? 10.032  40.611  22.904 1.00 41.43  ? 110 TYR A O   1 
ATOM   778  C CB  . TYR A 1 102 ? 7.024   39.249  22.788 1.00 55.19  ? 110 TYR A CB  1 
ATOM   779  C CG  . TYR A 1 102 ? 6.760   40.723  23.068 1.00 56.71  ? 110 TYR A CG  1 
ATOM   780  C CD1 . TYR A 1 102 ? 6.457   41.160  24.351 1.00 58.99  ? 110 TYR A CD1 1 
ATOM   781  C CD2 . TYR A 1 102 ? 6.855   41.686  22.067 1.00 56.95  ? 110 TYR A CD2 1 
ATOM   782  C CE1 . TYR A 1 102 ? 6.237   42.498  24.633 1.00 55.81  ? 110 TYR A CE1 1 
ATOM   783  C CE2 . TYR A 1 102 ? 6.631   43.026  22.336 1.00 55.95  ? 110 TYR A CE2 1 
ATOM   784  C CZ  . TYR A 1 102 ? 6.324   43.436  23.626 1.00 54.45  ? 110 TYR A CZ  1 
ATOM   785  O OH  . TYR A 1 102 ? 6.110   44.749  23.946 1.00 51.02  ? 110 TYR A OH  1 
ATOM   786  N N   . LYS A 1 103 ? 9.784   39.262  21.097 1.00 56.11  ? 111 LYS A N   1 
ATOM   787  C CA  . LYS A 1 103 ? 10.476  40.066  20.096 1.00 53.90  ? 111 LYS A CA  1 
ATOM   788  C C   . LYS A 1 103 ? 9.483   40.303  18.947 1.00 52.61  ? 111 LYS A C   1 
ATOM   789  O O   . LYS A 1 103 ? 8.851   39.354  18.464 1.00 50.14  ? 111 LYS A O   1 
ATOM   790  C CB  . LYS A 1 103 ? 11.743  39.268  19.751 1.00 55.17  ? 111 LYS A CB  1 
ATOM   791  C CG  . LYS A 1 103 ? 12.824  39.944  18.917 1.00 61.43  ? 111 LYS A CG  1 
ATOM   792  C CD  . LYS A 1 103 ? 13.976  39.030  18.499 1.00 64.11  ? 111 LYS A CD  1 
ATOM   793  C CE  . LYS A 1 103 ? 13.590  38.012  17.469 1.00 72.05  ? 111 LYS A CE  1 
ATOM   794  N NZ  . LYS A 1 103 ? 14.641  37.029  17.164 1.00 76.10  ? 111 LYS A NZ  1 
ATOM   795  N N   . VAL A 1 104 ? 9.273   41.571  18.557 1.00 51.09  ? 112 VAL A N   1 
ATOM   796  C CA  . VAL A 1 104 ? 8.400   41.863  17.423 1.00 57.64  ? 112 VAL A CA  1 
ATOM   797  C C   . VAL A 1 104 ? 9.191   41.685  16.127 1.00 54.01  ? 112 VAL A C   1 
ATOM   798  O O   . VAL A 1 104 ? 10.260  42.255  15.957 1.00 54.31  ? 112 VAL A O   1 
ATOM   799  C CB  . VAL A 1 104 ? 7.713   43.240  17.403 1.00 56.93  ? 112 VAL A CB  1 
ATOM   800  C CG1 . VAL A 1 104 ? 6.820   43.388  16.169 1.00 55.97  ? 112 VAL A CG1 1 
ATOM   801  C CG2 . VAL A 1 104 ? 6.910   43.481  18.674 1.00 56.14  ? 112 VAL A CG2 1 
ATOM   802  N N   . ILE A 1 105 ? 8.632   40.905  15.204 1.00 52.04  ? 113 ILE A N   1 
ATOM   803  C CA  . ILE A 1 105 ? 9.243   40.686  13.902 1.00 53.33  ? 113 ILE A CA  1 
ATOM   804  C C   . ILE A 1 105 ? 8.536   41.537  12.847 1.00 49.11  ? 113 ILE A C   1 
ATOM   805  O O   . ILE A 1 105 ? 9.205   42.066  11.962 1.00 46.09  ? 113 ILE A O   1 
ATOM   806  C CB  . ILE A 1 105 ? 9.215   39.189  13.560 1.00 53.48  ? 113 ILE A CB  1 
ATOM   807  C CG1 . ILE A 1 105 ? 10.132  38.397  14.501 1.00 56.87  ? 113 ILE A CG1 1 
ATOM   808  C CG2 . ILE A 1 105 ? 9.568   38.962  12.093 1.00 54.38  ? 113 ILE A CG2 1 
ATOM   809  C CD1 . ILE A 1 105 ? 9.904   36.897  14.482 1.00 56.97  ? 113 ILE A CD1 1 
ATOM   810  N N   . ASN A 1 106 ? 7.202   41.654  12.968 1.00 44.51  ? 114 ASN A N   1 
ATOM   811  C CA  . ASN A 1 106 ? 6.396   42.519  12.131 1.00 46.81  ? 114 ASN A CA  1 
ATOM   812  C C   . ASN A 1 106 ? 5.097   42.909  12.842 1.00 45.21  ? 114 ASN A C   1 
ATOM   813  O O   . ASN A 1 106 ? 4.343   42.035  13.271 1.00 48.89  ? 114 ASN A O   1 
ATOM   814  C CB  . ASN A 1 106 ? 6.072   41.840  10.802 1.00 50.62  ? 114 ASN A CB  1 
ATOM   815  C CG  . ASN A 1 106 ? 5.353   42.772  9.860  1.00 50.58  ? 114 ASN A CG  1 
ATOM   816  O OD1 . ASN A 1 106 ? 5.896   43.832  9.505  1.00 50.06  ? 114 ASN A OD1 1 
ATOM   817  N ND2 . ASN A 1 106 ? 4.150   42.390  9.448  1.00 49.28  ? 114 ASN A ND2 1 
ATOM   818  N N   . SER A 1 107 ? 4.822   44.225  12.874 1.00 46.87  ? 115 SER A N   1 
ATOM   819  C CA  . SER A 1 107 ? 3.654   44.822  13.508 1.00 52.20  ? 115 SER A CA  1 
ATOM   820  C C   . SER A 1 107 ? 2.449   44.853  12.571 1.00 49.13  ? 115 SER A C   1 
ATOM   821  O O   . SER A 1 107 ? 2.460   45.513  11.537 1.00 55.65  ? 115 SER A O   1 
ATOM   822  C CB  . SER A 1 107 ? 3.961   46.225  13.964 1.00 55.99  ? 115 SER A CB  1 
ATOM   823  O OG  . SER A 1 107 ? 5.173   46.268  14.706 1.00 60.65  ? 115 SER A OG  1 
ATOM   824  N N   . GLY A 1 108 ? 1.378   44.179  12.963 1.00 46.62  ? 116 GLY A N   1 
ATOM   825  C CA  . GLY A 1 108 ? 0.120   44.325  12.253 1.00 50.95  ? 116 GLY A CA  1 
ATOM   826  C C   . GLY A 1 108 ? -0.606  45.594  12.693 1.00 45.53  ? 116 GLY A C   1 
ATOM   827  O O   . GLY A 1 108 ? -0.111  46.357  13.496 1.00 46.31  ? 116 GLY A O   1 
ATOM   828  N N   . ASN A 1 109 ? -1.792  45.801  12.143 1.00 45.56  ? 117 ASN A N   1 
ATOM   829  C CA  . ASN A 1 109 ? -2.597  46.975  12.401 1.00 43.49  ? 117 ASN A CA  1 
ATOM   830  C C   . ASN A 1 109 ? -4.061  46.565  12.513 1.00 44.67  ? 117 ASN A C   1 
ATOM   831  O O   . ASN A 1 109 ? -4.906  47.435  12.619 1.00 49.11  ? 117 ASN A O   1 
ATOM   832  C CB  . ASN A 1 109 ? -2.432  48.011  11.295 1.00 53.32  ? 117 ASN A CB  1 
ATOM   833  C CG  . ASN A 1 109 ? -2.699  47.453  9.906  1.00 55.84  ? 117 ASN A CG  1 
ATOM   834  O OD1 . ASN A 1 109 ? -3.819  46.997  9.616  1.00 52.88  ? 117 ASN A OD1 1 
ATOM   835  N ND2 . ASN A 1 109 ? -1.681  47.465  9.049  1.00 49.70  ? 117 ASN A ND2 1 
ATOM   836  N N   . GLY A 1 110 ? -4.350  45.254  12.501 1.00 44.47  ? 118 GLY A N   1 
ATOM   837  C CA  . GLY A 1 110 ? -5.712  44.759  12.606 1.00 48.71  ? 118 GLY A CA  1 
ATOM   838  C C   . GLY A 1 110 ? -6.196  44.739  14.055 1.00 50.93  ? 118 GLY A C   1 
ATOM   839  O O   . GLY A 1 110 ? -5.489  45.186  14.954 1.00 47.22  ? 118 GLY A O   1 
ATOM   840  N N   . VAL A 1 111 ? -7.397  44.180  14.270 1.00 57.68  ? 119 VAL A N   1 
ATOM   841  C CA  . VAL A 1 111 ? -7.988  44.125  15.601 1.00 62.76  ? 119 VAL A CA  1 
ATOM   842  C C   . VAL A 1 111 ? -7.116  43.234  16.469 1.00 58.22  ? 119 VAL A C   1 
ATOM   843  O O   . VAL A 1 111 ? -6.423  42.360  15.948 1.00 56.17  ? 119 VAL A O   1 
ATOM   844  C CB  . VAL A 1 111 ? -9.450  43.646  15.708 1.00 58.82  ? 119 VAL A CB  1 
ATOM   845  C CG1 . VAL A 1 111 ? -10.390 44.572  14.959 1.00 69.40  ? 119 VAL A CG1 1 
ATOM   846  C CG2 . VAL A 1 111 ? -9.623  42.205  15.259 1.00 58.28  ? 119 VAL A CG2 1 
ATOM   847  N N   . LYS A 1 112 ? -7.179  43.496  17.786 1.00 64.00  ? 120 LYS A N   1 
ATOM   848  C CA  . LYS A 1 112 ? -6.576  42.649  18.811 1.00 56.31  ? 120 LYS A CA  1 
ATOM   849  C C   . LYS A 1 112 ? -7.655  41.723  19.347 1.00 50.53  ? 120 LYS A C   1 
ATOM   850  O O   . LYS A 1 112 ? -8.795  42.134  19.527 1.00 59.72  ? 120 LYS A O   1 
ATOM   851  C CB  . LYS A 1 112 ? -6.037  43.418  20.021 1.00 53.53  ? 120 LYS A CB  1 
ATOM   852  C CG  . LYS A 1 112 ? -4.964  44.449  19.759 1.00 55.71  ? 120 LYS A CG  1 
ATOM   853  C CD  . LYS A 1 112 ? -5.005  45.612  20.741 1.00 61.77  ? 120 LYS A CD  1 
ATOM   854  C CE  . LYS A 1 112 ? -4.008  46.663  20.388 1.00 72.73  ? 120 LYS A CE  1 
ATOM   855  N NZ  . LYS A 1 112 ? -4.283  47.958  21.016 1.00 80.18  ? 120 LYS A NZ  1 
ATOM   856  N N   . PRO A 1 113 ? -7.359  40.437  19.588 1.00 50.67  ? 121 PRO A N   1 
ATOM   857  C CA  . PRO A 1 113 ? -8.351  39.550  20.184 1.00 56.27  ? 121 PRO A CA  1 
ATOM   858  C C   . PRO A 1 113 ? -8.460  39.708  21.702 1.00 62.63  ? 121 PRO A C   1 
ATOM   859  O O   . PRO A 1 113 ? -7.579  40.270  22.359 1.00 57.73  ? 121 PRO A O   1 
ATOM   860  C CB  . PRO A 1 113 ? -7.865  38.159  19.754 1.00 55.18  ? 121 PRO A CB  1 
ATOM   861  C CG  . PRO A 1 113 ? -6.378  38.295  19.489 1.00 50.47  ? 121 PRO A CG  1 
ATOM   862  C CD  . PRO A 1 113 ? -6.101  39.764  19.259 1.00 52.62  ? 121 PRO A CD  1 
ATOM   863  N N   . GLY A 1 114 ? -9.591  39.225  22.225 1.00 66.60  ? 122 GLY A N   1 
ATOM   864  C CA  . GLY A 1 114 ? -9.872  39.160  23.645 1.00 54.52  ? 122 GLY A CA  1 
ATOM   865  C C   . GLY A 1 114 ? -10.197 37.724  24.024 1.00 59.12  ? 122 GLY A C   1 
ATOM   866  O O   . GLY A 1 114 ? -10.097 36.827  23.187 1.00 56.29  ? 122 GLY A O   1 
ATOM   867  N N   . LYS A 1 115 ? -10.589 37.542  25.295 1.00 72.46  ? 123 LYS A N   1 
ATOM   868  C CA  . LYS A 1 115 ? -10.758 36.237  25.917 1.00 69.13  ? 123 LYS A CA  1 
ATOM   869  C C   . LYS A 1 115 ? -11.729 35.363  25.129 1.00 70.66  ? 123 LYS A C   1 
ATOM   870  O O   . LYS A 1 115 ? -11.518 34.166  24.976 1.00 66.14  ? 123 LYS A O   1 
ATOM   871  C CB  . LYS A 1 115 ? -11.286 36.423  27.342 1.00 84.46  ? 123 LYS A CB  1 
ATOM   872  C CG  . LYS A 1 115 ? -10.309 36.079  28.444 1.00 94.17  ? 123 LYS A CG  1 
ATOM   873  C CD  . LYS A 1 115 ? -9.089  36.975  28.503 1.00 99.19  ? 123 LYS A CD  1 
ATOM   874  C CE  . LYS A 1 115 ? -7.894  36.098  28.536 1.00 115.18 ? 123 LYS A CE  1 
ATOM   875  N NZ  . LYS A 1 115 ? -6.650  36.865  28.635 1.00 126.66 ? 123 LYS A NZ  1 
ATOM   876  N N   . SER A 1 116 ? -12.802 35.977  24.635 1.00 76.39  ? 124 SER A N   1 
ATOM   877  C CA  . SER A 1 116 ? -13.919 35.234  24.096 1.00 81.07  ? 124 SER A CA  1 
ATOM   878  C C   . SER A 1 116 ? -13.951 35.376  22.578 1.00 89.78  ? 124 SER A C   1 
ATOM   879  O O   . SER A 1 116 ? -15.018 35.537  21.993 1.00 113.55 ? 124 SER A O   1 
ATOM   880  C CB  . SER A 1 116 ? -15.183 35.720  24.744 1.00 89.18  ? 124 SER A CB  1 
ATOM   881  O OG  . SER A 1 116 ? -14.993 35.867  26.147 1.00 94.04  ? 124 SER A OG  1 
ATOM   882  N N   . ASP A 1 117 ? -12.769 35.317  21.950 1.00 89.95  ? 125 ASP A N   1 
ATOM   883  C CA  . ASP A 1 117 ? -12.641 35.404  20.503 1.00 77.76  ? 125 ASP A CA  1 
ATOM   884  C C   . ASP A 1 117 ? -11.966 34.140  19.988 1.00 69.61  ? 125 ASP A C   1 
ATOM   885  O O   . ASP A 1 117 ? -11.371 33.399  20.760 1.00 69.69  ? 125 ASP A O   1 
ATOM   886  C CB  . ASP A 1 117 ? -11.824 36.613  20.084 1.00 74.41  ? 125 ASP A CB  1 
ATOM   887  C CG  . ASP A 1 117 ? -12.389 37.977  20.453 1.00 76.34  ? 125 ASP A CG  1 
ATOM   888  O OD1 . ASP A 1 117 ? -13.532 38.035  20.967 1.00 73.85  ? 125 ASP A OD1 1 
ATOM   889  O OD2 . ASP A 1 117 ? -11.667 38.976  20.219 1.00 71.38  ? 125 ASP A OD2 1 
ATOM   890  N N   . THR A 1 118 ? -12.068 33.909  18.681 1.00 65.75  ? 126 THR A N   1 
ATOM   891  C CA  . THR A 1 118 ? -11.354 32.823  18.039 1.00 70.08  ? 126 THR A CA  1 
ATOM   892  C C   . THR A 1 118 ? -10.303 33.440  17.123 1.00 64.85  ? 126 THR A C   1 
ATOM   893  O O   . THR A 1 118 ? -10.542 34.473  16.522 1.00 70.18  ? 126 THR A O   1 
ATOM   894  C CB  . THR A 1 118 ? -12.328 31.929  17.274 1.00 72.18  ? 126 THR A CB  1 
ATOM   895  O OG1 . THR A 1 118 ? -13.401 31.763  18.190 1.00 80.11  ? 126 THR A OG1 1 
ATOM   896  C CG2 . THR A 1 118 ? -11.742 30.576  16.912 1.00 72.76  ? 126 THR A CG2 1 
ATOM   897  N N   . VAL A 1 119 ? -9.133  32.809  17.037 1.00 60.28  ? 127 VAL A N   1 
ATOM   898  C CA  . VAL A 1 119 ? -8.054  33.328  16.223 1.00 55.53  ? 127 VAL A CA  1 
ATOM   899  C C   . VAL A 1 119 ? -7.572  32.220  15.293 1.00 55.68  ? 127 VAL A C   1 
ATOM   900  O O   . VAL A 1 119 ? -7.616  31.039  15.648 1.00 51.11  ? 127 VAL A O   1 
ATOM   901  C CB  . VAL A 1 119 ? -6.893  33.882  17.076 1.00 54.56  ? 127 VAL A CB  1 
ATOM   902  C CG1 . VAL A 1 119 ? -7.299  35.126  17.849 1.00 54.54  ? 127 VAL A CG1 1 
ATOM   903  C CG2 . VAL A 1 119 ? -6.317  32.837  18.024 1.00 51.94  ? 127 VAL A CG2 1 
ATOM   904  N N   . THR A 1 120 ? -7.111  32.638  14.105 1.00 55.15  ? 128 THR A N   1 
ATOM   905  C CA  . THR A 1 120 ? -6.401  31.770  13.183 1.00 52.28  ? 128 THR A CA  1 
ATOM   906  C C   . THR A 1 120 ? -4.947  32.217  13.167 1.00 49.11  ? 128 THR A C   1 
ATOM   907  O O   . THR A 1 120 ? -4.686  33.414  13.072 1.00 51.18  ? 128 THR A O   1 
ATOM   908  C CB  . THR A 1 120 ? -7.022  31.887  11.794 1.00 58.15  ? 128 THR A CB  1 
ATOM   909  O OG1 . THR A 1 120 ? -8.413  32.029  12.029 1.00 62.23  ? 128 THR A OG1 1 
ATOM   910  C CG2 . THR A 1 120 ? -6.749  30.670  10.928 1.00 62.52  ? 128 THR A CG2 1 
ATOM   911  N N   . VAL A 1 121 ? -4.011  31.260  13.237 1.00 47.95  ? 129 VAL A N   1 
ATOM   912  C CA  . VAL A 1 121 ? -2.603  31.586  13.430 1.00 47.77  ? 129 VAL A CA  1 
ATOM   913  C C   . VAL A 1 121 ? -1.774  30.538  12.715 1.00 45.22  ? 129 VAL A C   1 
ATOM   914  O O   . VAL A 1 121 ? -2.174  29.384  12.656 1.00 47.91  ? 129 VAL A O   1 
ATOM   915  C CB  . VAL A 1 121 ? -2.147  31.624  14.910 1.00 46.68  ? 129 VAL A CB  1 
ATOM   916  C CG1 . VAL A 1 121 ? -2.982  32.553  15.774 1.00 48.10  ? 129 VAL A CG1 1 
ATOM   917  C CG2 . VAL A 1 121 ? -2.180  30.247  15.547 1.00 45.86  ? 129 VAL A CG2 1 
ATOM   918  N N   . GLU A 1 122 ? -0.541  30.974  12.412 1.00 51.53  ? 130 GLU A N   1 
ATOM   919  C CA  . GLU A 1 122 ? 0.501   30.049  11.933 1.00 57.28  ? 130 GLU A CA  1 
ATOM   920  C C   . GLU A 1 122 ? 1.564   30.183  13.038 1.00 54.70  ? 130 GLU A C   1 
ATOM   921  O O   . GLU A 1 122 ? 1.719   31.304  13.548 1.00 51.17  ? 130 GLU A O   1 
ATOM   922  C CB  . GLU A 1 122 ? 1.009   30.459  10.553 1.00 61.45  ? 130 GLU A CB  1 
ATOM   923  C CG  . GLU A 1 122 ? 0.096   30.048  9.404  1.00 69.45  ? 130 GLU A CG  1 
ATOM   924  C CD  . GLU A 1 122 ? 0.536   30.588  8.056  1.00 81.63  ? 130 GLU A CD  1 
ATOM   925  O OE1 . GLU A 1 122 ? 1.598   31.237  7.983  1.00 95.82  ? 130 GLU A OE1 1 
ATOM   926  O OE2 . GLU A 1 122 ? -0.190  30.358  7.070  1.00 92.17  ? 130 GLU A OE2 1 
ATOM   927  N N   . TYR A 1 123 ? 2.227   29.092  13.444 1.00 51.97  ? 131 TYR A N   1 
ATOM   928  C CA  . TYR A 1 123 ? 3.194   29.138  14.531 1.00 53.69  ? 131 TYR A CA  1 
ATOM   929  C C   . TYR A 1 123 ? 4.203   28.013  14.410 1.00 51.40  ? 131 TYR A C   1 
ATOM   930  O O   . TYR A 1 123 ? 3.931   26.997  13.779 1.00 58.57  ? 131 TYR A O   1 
ATOM   931  C CB  . TYR A 1 123 ? 2.600   28.945  15.927 1.00 59.17  ? 131 TYR A CB  1 
ATOM   932  C CG  . TYR A 1 123 ? 1.991   27.574  16.226 1.00 61.36  ? 131 TYR A CG  1 
ATOM   933  C CD1 . TYR A 1 123 ? 0.644   27.317  15.993 1.00 55.98  ? 131 TYR A CD1 1 
ATOM   934  C CD2 . TYR A 1 123 ? 2.746   26.554  16.807 1.00 64.09  ? 131 TYR A CD2 1 
ATOM   935  C CE1 . TYR A 1 123 ? 0.077   26.092  16.307 1.00 56.30  ? 131 TYR A CE1 1 
ATOM   936  C CE2 . TYR A 1 123 ? 2.190   25.322  17.118 1.00 56.88  ? 131 TYR A CE2 1 
ATOM   937  C CZ  . TYR A 1 123 ? 0.849   25.100  16.876 1.00 53.12  ? 131 TYR A CZ  1 
ATOM   938  O OH  . TYR A 1 123 ? 0.289   23.894  17.138 1.00 57.55  ? 131 TYR A OH  1 
ATOM   939  N N   . THR A 1 124 ? 5.362   28.234  15.036 1.00 52.54  ? 132 THR A N   1 
ATOM   940  C CA  . THR A 1 124 ? 6.301   27.166  15.328 1.00 54.68  ? 132 THR A CA  1 
ATOM   941  C C   . THR A 1 124 ? 6.679   27.242  16.804 1.00 61.44  ? 132 THR A C   1 
ATOM   942  O O   . THR A 1 124 ? 7.032   28.318  17.280 1.00 65.61  ? 132 THR A O   1 
ATOM   943  C CB  . THR A 1 124 ? 7.524   27.283  14.430 1.00 56.62  ? 132 THR A CB  1 
ATOM   944  O OG1 . THR A 1 124 ? 6.951   27.094  13.136 1.00 58.70  ? 132 THR A OG1 1 
ATOM   945  C CG2 . THR A 1 124 ? 8.590   26.252  14.778 1.00 60.03  ? 132 THR A CG2 1 
ATOM   946  N N   . GLY A 1 125 ? 6.565   26.102  17.507 1.00 60.86  ? 133 GLY A N   1 
ATOM   947  C CA  . GLY A 1 125 ? 7.003   25.970  18.890 1.00 62.81  ? 133 GLY A CA  1 
ATOM   948  C C   . GLY A 1 125 ? 8.294   25.152  19.011 1.00 61.76  ? 133 GLY A C   1 
ATOM   949  O O   . GLY A 1 125 ? 8.436   24.114  18.375 1.00 60.32  ? 133 GLY A O   1 
ATOM   950  N N   . ARG A 1 126 ? 9.237   25.612  19.839 1.00 58.94  ? 134 ARG A N   1 
ATOM   951  C CA  . ARG A 1 126 ? 10.441  24.838  20.085 1.00 59.23  ? 134 ARG A CA  1 
ATOM   952  C C   . ARG A 1 126 ? 10.870  24.986  21.540 1.00 57.17  ? 134 ARG A C   1 
ATOM   953  O O   . ARG A 1 126 ? 10.485  25.932  22.222 1.00 64.04  ? 134 ARG A O   1 
ATOM   954  C CB  . ARG A 1 126 ? 11.569  25.179  19.102 1.00 59.71  ? 134 ARG A CB  1 
ATOM   955  C CG  . ARG A 1 126 ? 11.872  26.644  18.843 1.00 62.71  ? 134 ARG A CG  1 
ATOM   956  C CD  . ARG A 1 126 ? 12.941  26.836  17.773 1.00 74.56  ? 134 ARG A CD  1 
ATOM   957  N NE  . ARG A 1 126 ? 12.583  26.433  16.401 1.00 88.47  ? 134 ARG A NE  1 
ATOM   958  C CZ  . ARG A 1 126 ? 13.400  26.520  15.329 1.00 90.58  ? 134 ARG A CZ  1 
ATOM   959  N NH1 . ARG A 1 126 ? 14.601  27.078  15.430 1.00 91.44  ? 134 ARG A NH1 1 
ATOM   960  N NH2 . ARG A 1 126 ? 13.016  26.053  14.152 1.00 84.49  ? 134 ARG A NH2 1 
ATOM   961  N N   . LEU A 1 127 ? 11.654  24.009  21.997 1.00 58.16  ? 135 LEU A N   1 
ATOM   962  C CA  . LEU A 1 127 ? 12.228  24.014  23.330 1.00 61.58  ? 135 LEU A CA  1 
ATOM   963  C C   . LEU A 1 127 ? 13.523  24.823  23.298 1.00 63.66  ? 135 LEU A C   1 
ATOM   964  O O   . LEU A 1 127 ? 14.028  25.165  22.228 1.00 58.71  ? 135 LEU A O   1 
ATOM   965  C CB  . LEU A 1 127 ? 12.449  22.565  23.765 1.00 66.58  ? 135 LEU A CB  1 
ATOM   966  C CG  . LEU A 1 127 ? 11.202  21.669  23.751 1.00 68.50  ? 135 LEU A CG  1 
ATOM   967  C CD1 . LEU A 1 127 ? 11.579  20.208  23.855 1.00 71.07  ? 135 LEU A CD1 1 
ATOM   968  C CD2 . LEU A 1 127 ? 10.216  22.038  24.859 1.00 68.71  ? 135 LEU A CD2 1 
ATOM   969  N N   . ILE A 1 128 ? 14.037  25.120  24.495 1.00 69.22  ? 136 ILE A N   1 
ATOM   970  C CA  . ILE A 1 128 ? 15.202  25.966  24.702 1.00 65.32  ? 136 ILE A CA  1 
ATOM   971  C C   . ILE A 1 128 ? 16.374  25.504  23.838 1.00 64.68  ? 136 ILE A C   1 
ATOM   972  O O   . ILE A 1 128 ? 17.213  26.310  23.470 1.00 60.97  ? 136 ILE A O   1 
ATOM   973  C CB  . ILE A 1 128 ? 15.552  25.970  26.206 1.00 73.05  ? 136 ILE A CB  1 
ATOM   974  C CG1 . ILE A 1 128 ? 14.551  26.779  26.988 1.00 68.69  ? 136 ILE A CG1 1 
ATOM   975  C CG2 . ILE A 1 128 ? 16.978  26.443  26.491 1.00 84.31  ? 136 ILE A CG2 1 
ATOM   976  C CD1 . ILE A 1 128 ? 14.256  28.124  26.370 1.00 70.20  ? 136 ILE A CD1 1 
ATOM   977  N N   . ASP A 1 129 ? 16.456  24.206  23.543 1.00 74.05  ? 137 ASP A N   1 
ATOM   978  C CA  . ASP A 1 129 ? 17.575  23.679  22.781 1.00 79.01  ? 137 ASP A CA  1 
ATOM   979  C C   . ASP A 1 129 ? 17.213  23.564  21.305 1.00 76.84  ? 137 ASP A C   1 
ATOM   980  O O   . ASP A 1 129 ? 17.965  22.959  20.553 1.00 91.36  ? 137 ASP A O   1 
ATOM   981  C CB  . ASP A 1 129 ? 18.068  22.349  23.330 1.00 81.89  ? 137 ASP A CB  1 
ATOM   982  C CG  . ASP A 1 129 ? 17.184  21.144  23.053 1.00 87.14  ? 137 ASP A CG  1 
ATOM   983  O OD1 . ASP A 1 129 ? 16.219  21.287  22.270 1.00 89.04  ? 137 ASP A OD1 1 
ATOM   984  O OD2 . ASP A 1 129 ? 17.462  20.075  23.641 1.00 96.16  ? 137 ASP A OD2 1 
ATOM   985  N N   . GLY A 1 130 ? 16.063  24.115  20.897 1.00 69.10  ? 138 GLY A N   1 
ATOM   986  C CA  . GLY A 1 130 ? 15.763  24.289  19.483 1.00 69.40  ? 138 GLY A CA  1 
ATOM   987  C C   . GLY A 1 130 ? 15.059  23.085  18.867 1.00 64.92  ? 138 GLY A C   1 
ATOM   988  O O   . GLY A 1 130 ? 14.715  23.106  17.690 1.00 77.83  ? 138 GLY A O   1 
ATOM   989  N N   . THR A 1 131 ? 14.859  22.030  19.656 1.00 63.97  ? 139 THR A N   1 
ATOM   990  C CA  . THR A 1 131 ? 13.961  20.956  19.274 1.00 67.14  ? 139 THR A CA  1 
ATOM   991  C C   . THR A 1 131 ? 12.594  21.547  18.925 1.00 66.41  ? 139 THR A C   1 
ATOM   992  O O   . THR A 1 131 ? 11.929  22.109  19.785 1.00 62.90  ? 139 THR A O   1 
ATOM   993  C CB  . THR A 1 131 ? 13.877  19.973  20.439 1.00 70.66  ? 139 THR A CB  1 
ATOM   994  O OG1 . THR A 1 131 ? 15.201  19.453  20.497 1.00 80.20  ? 139 THR A OG1 1 
ATOM   995  C CG2 . THR A 1 131 ? 12.850  18.873  20.236 1.00 69.15  ? 139 THR A CG2 1 
ATOM   996  N N   . VAL A 1 132 ? 12.192  21.429  17.656 1.00 63.02  ? 140 VAL A N   1 
ATOM   997  C CA  . VAL A 1 132 ? 10.851  21.793  17.233 1.00 58.67  ? 140 VAL A CA  1 
ATOM   998  C C   . VAL A 1 132 ? 9.883   20.730  17.735 1.00 59.22  ? 140 VAL A C   1 
ATOM   999  O O   . VAL A 1 132 ? 10.121  19.554  17.528 1.00 61.07  ? 140 VAL A O   1 
ATOM   1000 C CB  . VAL A 1 132 ? 10.735  21.925  15.703 1.00 59.06  ? 140 VAL A CB  1 
ATOM   1001 C CG1 . VAL A 1 132 ? 9.293   22.158  15.279 1.00 64.78  ? 140 VAL A CG1 1 
ATOM   1002 C CG2 . VAL A 1 132 ? 11.642  23.013  15.139 1.00 59.82  ? 140 VAL A CG2 1 
ATOM   1003 N N   . PHE A 1 133 ? 8.781   21.149  18.366 1.00 63.94  ? 141 PHE A N   1 
ATOM   1004 C CA  . PHE A 1 133 ? 7.823   20.217  18.939 1.00 59.33  ? 141 PHE A CA  1 
ATOM   1005 C C   . PHE A 1 133 ? 6.448   20.355  18.279 1.00 61.24  ? 141 PHE A C   1 
ATOM   1006 O O   . PHE A 1 133 ? 5.604   19.497  18.482 1.00 63.20  ? 141 PHE A O   1 
ATOM   1007 C CB  . PHE A 1 133 ? 7.778   20.352  20.469 1.00 58.25  ? 141 PHE A CB  1 
ATOM   1008 C CG  . PHE A 1 133 ? 7.346   21.694  21.058 1.00 59.05  ? 141 PHE A CG  1 
ATOM   1009 C CD1 . PHE A 1 133 ? 6.002   22.039  21.152 1.00 58.96  ? 141 PHE A CD1 1 
ATOM   1010 C CD2 . PHE A 1 133 ? 8.279   22.600  21.554 1.00 55.27  ? 141 PHE A CD2 1 
ATOM   1011 C CE1 . PHE A 1 133 ? 5.610   23.258  21.698 1.00 55.98  ? 141 PHE A CE1 1 
ATOM   1012 C CE2 . PHE A 1 133 ? 7.880   23.821  22.085 1.00 51.66  ? 141 PHE A CE2 1 
ATOM   1013 C CZ  . PHE A 1 133 ? 6.553   24.142  22.169 1.00 51.34  ? 141 PHE A CZ  1 
ATOM   1014 N N   . ASP A 1 134 ? 6.195   21.418  17.505 1.00 68.61  ? 142 ASP A N   1 
ATOM   1015 C CA  . ASP A 1 134 ? 4.952   21.539  16.754 1.00 67.77  ? 142 ASP A CA  1 
ATOM   1016 C C   . ASP A 1 134 ? 5.065   22.709  15.781 1.00 64.41  ? 142 ASP A C   1 
ATOM   1017 O O   . ASP A 1 134 ? 5.717   23.697  16.103 1.00 61.60  ? 142 ASP A O   1 
ATOM   1018 C CB  . ASP A 1 134 ? 3.746   21.722  17.662 1.00 75.65  ? 142 ASP A CB  1 
ATOM   1019 C CG  . ASP A 1 134 ? 2.375   21.584  17.004 1.00 89.67  ? 142 ASP A CG  1 
ATOM   1020 O OD1 . ASP A 1 134 ? 2.308   21.308  15.777 1.00 98.56  ? 142 ASP A OD1 1 
ATOM   1021 O OD2 . ASP A 1 134 ? 1.369   21.745  17.730 1.00 81.38  ? 142 ASP A OD2 1 
ATOM   1022 N N   . SER A 1 135 ? 4.444   22.576  14.595 1.00 65.07  ? 143 SER A N   1 
ATOM   1023 C CA  . SER A 1 135 ? 4.447   23.639  13.599 1.00 60.44  ? 143 SER A CA  1 
ATOM   1024 C C   . SER A 1 135 ? 3.324   23.490  12.579 1.00 66.41  ? 143 SER A C   1 
ATOM   1025 O O   . SER A 1 135 ? 3.082   22.410  12.039 1.00 76.46  ? 143 SER A O   1 
ATOM   1026 C CB  . SER A 1 135 ? 5.747   23.728  12.883 1.00 52.65  ? 143 SER A CB  1 
ATOM   1027 O OG  . SER A 1 135 ? 5.749   24.943  12.158 1.00 58.51  ? 143 SER A OG  1 
ATOM   1028 N N   . THR A 1 136 ? 2.689   24.622  12.269 1.00 66.63  ? 144 THR A N   1 
ATOM   1029 C CA  . THR A 1 136 ? 1.688   24.666  11.216 1.00 65.70  ? 144 THR A CA  1 
ATOM   1030 C C   . THR A 1 136 ? 2.337   24.419  9.858  1.00 62.60  ? 144 THR A C   1 
ATOM   1031 O O   . THR A 1 136 ? 1.658   23.985  8.942  1.00 61.75  ? 144 THR A O   1 
ATOM   1032 C CB  . THR A 1 136 ? 0.964   26.008  11.228 1.00 66.79  ? 144 THR A CB  1 
ATOM   1033 O OG1 . THR A 1 136 ? 1.953   27.022  11.039 1.00 65.77  ? 144 THR A OG1 1 
ATOM   1034 C CG2 . THR A 1 136 ? 0.169   26.191  12.508 1.00 70.22  ? 144 THR A CG2 1 
ATOM   1035 N N   . GLU A 1 137 ? 3.635   24.709  9.722  1.00 64.64  ? 145 GLU A N   1 
ATOM   1036 C CA  . GLU A 1 137 ? 4.265   24.645  8.419  1.00 76.12  ? 145 GLU A CA  1 
ATOM   1037 C C   . GLU A 1 137 ? 4.583   23.165  8.137  1.00 81.87  ? 145 GLU A C   1 
ATOM   1038 O O   . GLU A 1 137 ? 4.951   22.809  7.022  1.00 84.38  ? 145 GLU A O   1 
ATOM   1039 C CB  . GLU A 1 137 ? 5.408   25.667  8.247  1.00 76.98  ? 145 GLU A CB  1 
ATOM   1040 C CG  . GLU A 1 137 ? 5.186   27.116  8.728  1.00 74.12  ? 145 GLU A CG  1 
ATOM   1041 C CD  . GLU A 1 137 ? 4.244   28.149  8.084  1.00 76.74  ? 145 GLU A CD  1 
ATOM   1042 O OE1 . GLU A 1 137 ? 4.670   29.293  7.723  1.00 67.34  ? 145 GLU A OE1 1 
ATOM   1043 O OE2 . GLU A 1 137 ? 3.028   27.842  8.030  1.00 72.87  ? 145 GLU A OE2 1 
ATOM   1044 N N   . LYS A 1 138 ? 4.384   22.281  9.125  1.00 85.92  ? 146 LYS A N   1 
ATOM   1045 C CA  . LYS A 1 138 ? 4.482   20.843  8.894  1.00 93.91  ? 146 LYS A CA  1 
ATOM   1046 C C   . LYS A 1 138 ? 3.130   20.243  8.499  1.00 92.85  ? 146 LYS A C   1 
ATOM   1047 O O   . LYS A 1 138 ? 3.095   19.147  7.947  1.00 93.11  ? 146 LYS A O   1 
ATOM   1048 C CB  . LYS A 1 138 ? 5.061   20.089  10.101 1.00 105.25 ? 146 LYS A CB  1 
ATOM   1049 C CG  . LYS A 1 138 ? 6.584   19.959  10.079 1.00 107.75 ? 146 LYS A CG  1 
ATOM   1050 C CD  . LYS A 1 138 ? 7.262   19.942  11.444 1.00 111.91 ? 146 LYS A CD  1 
ATOM   1051 C CE  . LYS A 1 138 ? 8.725   20.274  11.373 1.00 109.24 ? 146 LYS A CE  1 
ATOM   1052 N NZ  . LYS A 1 138 ? 8.924   21.662  10.949 1.00 104.31 ? 146 LYS A NZ  1 
ATOM   1053 N N   . THR A 1 139 ? 2.021   20.934  8.790  1.00 86.99  ? 147 THR A N   1 
ATOM   1054 C CA  . THR A 1 139 ? 0.709   20.483  8.343  1.00 85.02  ? 147 THR A CA  1 
ATOM   1055 C C   . THR A 1 139 ? 0.286   21.294  7.115  1.00 81.59  ? 147 THR A C   1 
ATOM   1056 O O   . THR A 1 139 ? -0.833  21.165  6.619  1.00 70.59  ? 147 THR A O   1 
ATOM   1057 C CB  . THR A 1 139 ? -0.318  20.577  9.479  1.00 89.75  ? 147 THR A CB  1 
ATOM   1058 O OG1 . THR A 1 139 ? -0.899  21.880  9.487  1.00 80.11  ? 147 THR A OG1 1 
ATOM   1059 C CG2 . THR A 1 139 ? 0.272   20.234  10.841 1.00 94.56  ? 147 THR A CG2 1 
ATOM   1060 N N   . GLY A 1 140 ? 1.183   22.163  6.643  1.00 85.05  ? 148 GLY A N   1 
ATOM   1061 C CA  . GLY A 1 140 ? 0.899   23.024  5.511  1.00 81.89  ? 148 GLY A CA  1 
ATOM   1062 C C   . GLY A 1 140 ? -0.276  23.962  5.763  1.00 84.98  ? 148 GLY A C   1 
ATOM   1063 O O   . GLY A 1 140 ? -0.556  24.801  4.915  1.00 106.74 ? 148 GLY A O   1 
ATOM   1064 N N   . LYS A 1 141 ? -0.936  23.852  6.925  1.00 80.42  ? 149 LYS A N   1 
ATOM   1065 C CA  . LYS A 1 141 ? -2.220  24.504  7.133  1.00 89.25  ? 149 LYS A CA  1 
ATOM   1066 C C   . LYS A 1 141 ? -2.271  25.242  8.475  1.00 88.09  ? 149 LYS A C   1 
ATOM   1067 O O   . LYS A 1 141 ? -1.710  24.787  9.470  1.00 80.83  ? 149 LYS A O   1 
ATOM   1068 C CB  . LYS A 1 141 ? -3.361  23.483  7.006  1.00 90.01  ? 149 LYS A CB  1 
ATOM   1069 C CG  . LYS A 1 141 ? -3.838  23.245  5.582  1.00 96.79  ? 149 LYS A CG  1 
ATOM   1070 C CD  . LYS A 1 141 ? -4.438  24.482  4.911  1.00 108.02 ? 149 LYS A CD  1 
ATOM   1071 C CE  . LYS A 1 141 ? -4.870  24.283  3.484  1.00 105.33 ? 149 LYS A CE  1 
ATOM   1072 N NZ  . LYS A 1 141 ? -3.763  23.914  2.598  1.00 99.49  ? 149 LYS A NZ  1 
ATOM   1073 N N   . PRO A 1 142 ? -2.992  26.390  8.536  1.00 82.32  ? 150 PRO A N   1 
ATOM   1074 C CA  . PRO A 1 142 ? -3.134  27.182  9.766  1.00 78.56  ? 150 PRO A CA  1 
ATOM   1075 C C   . PRO A 1 142 ? -4.064  26.608  10.835 1.00 67.12  ? 150 PRO A C   1 
ATOM   1076 O O   . PRO A 1 142 ? -4.820  25.691  10.548 1.00 71.82  ? 150 PRO A O   1 
ATOM   1077 C CB  . PRO A 1 142 ? -3.675  28.516  9.210  1.00 78.38  ? 150 PRO A CB  1 
ATOM   1078 C CG  . PRO A 1 142 ? -4.510  28.092  8.036  1.00 76.31  ? 150 PRO A CG  1 
ATOM   1079 C CD  . PRO A 1 142 ? -3.697  26.993  7.393  1.00 76.75  ? 150 PRO A CD  1 
ATOM   1080 N N   . ALA A 1 143 ? -4.023  27.196  12.044 1.00 64.66  ? 151 ALA A N   1 
ATOM   1081 C CA  . ALA A 1 143 ? -4.662  26.643  13.240 1.00 67.96  ? 151 ALA A CA  1 
ATOM   1082 C C   . ALA A 1 143 ? -5.709  27.601  13.805 1.00 64.90  ? 151 ALA A C   1 
ATOM   1083 O O   . ALA A 1 143 ? -5.521  28.817  13.781 1.00 71.30  ? 151 ALA A O   1 
ATOM   1084 C CB  . ALA A 1 143 ? -3.632  26.321  14.317 1.00 59.45  ? 151 ALA A CB  1 
ATOM   1085 N N   . THR A 1 144 ? -6.778  27.026  14.369 1.00 63.18  ? 152 THR A N   1 
ATOM   1086 C CA  . THR A 1 144 ? -7.874  27.807  14.913 1.00 71.09  ? 152 THR A CA  1 
ATOM   1087 C C   . THR A 1 144 ? -8.096  27.474  16.387 1.00 73.88  ? 152 THR A C   1 
ATOM   1088 O O   . THR A 1 144 ? -8.158  26.307  16.774 1.00 64.81  ? 152 THR A O   1 
ATOM   1089 C CB  . THR A 1 144 ? -9.116  27.569  14.065 1.00 70.74  ? 152 THR A CB  1 
ATOM   1090 O OG1 . THR A 1 144 ? -8.761  28.327  12.911 1.00 72.53  ? 152 THR A OG1 1 
ATOM   1091 C CG2 . THR A 1 144 ? -10.377 28.128  14.698 1.00 74.46  ? 152 THR A CG2 1 
ATOM   1092 N N   . PHE A 1 145 ? -8.125  28.524  17.213 1.00 73.28  ? 153 PHE A N   1 
ATOM   1093 C CA  . PHE A 1 145 ? -8.234  28.309  18.675 1.00 65.62  ? 153 PHE A CA  1 
ATOM   1094 C C   . PHE A 1 145 ? -9.006  29.424  19.314 1.00 59.01  ? 153 PHE A C   1 
ATOM   1095 O O   . PHE A 1 145 ? -9.043  30.532  18.764 1.00 53.08  ? 153 PHE A O   1 
ATOM   1096 C CB  . PHE A 1 145 ? -6.869  28.428  19.352 1.00 64.26  ? 153 PHE A CB  1 
ATOM   1097 C CG  . PHE A 1 145 ? -5.728  27.560  18.846 1.00 60.68  ? 153 PHE A CG  1 
ATOM   1098 C CD1 . PHE A 1 145 ? -5.622  26.229  19.225 1.00 66.82  ? 153 PHE A CD1 1 
ATOM   1099 C CD2 . PHE A 1 145 ? -4.744  28.091  18.024 1.00 58.94  ? 153 PHE A CD2 1 
ATOM   1100 C CE1 . PHE A 1 145 ? -4.573  25.447  18.775 1.00 65.55  ? 153 PHE A CE1 1 
ATOM   1101 C CE2 . PHE A 1 145 ? -3.696  27.304  17.582 1.00 63.44  ? 153 PHE A CE2 1 
ATOM   1102 C CZ  . PHE A 1 145 ? -3.614  25.985  17.956 1.00 60.36  ? 153 PHE A CZ  1 
ATOM   1103 N N   . GLN A 1 146 ? -9.614  29.136  20.470 1.00 71.94  ? 154 GLN A N   1 
ATOM   1104 C CA  . GLN A 1 146 ? -10.280 30.212  21.244 1.00 75.32  ? 154 GLN A CA  1 
ATOM   1105 C C   . GLN A 1 146 ? -9.193  30.817  22.142 1.00 66.96  ? 154 GLN A C   1 
ATOM   1106 O O   . GLN A 1 146 ? -8.442  30.036  22.770 1.00 61.46  ? 154 GLN A O   1 
ATOM   1107 C CB  . GLN A 1 146 ? -11.472 29.696  22.051 1.00 80.21  ? 154 GLN A CB  1 
ATOM   1108 C CG  . GLN A 1 146 ? -11.692 30.428  23.371 1.00 83.98  ? 154 GLN A CG  1 
ATOM   1109 C CD  . GLN A 1 146 ? -12.810 31.445  23.328 1.00 90.51  ? 154 GLN A CD  1 
ATOM   1110 O OE1 . GLN A 1 146 ? -13.362 31.837  24.361 1.00 82.40  ? 154 GLN A OE1 1 
ATOM   1111 N NE2 . GLN A 1 146 ? -13.161 31.883  22.127 1.00 102.62 ? 154 GLN A NE2 1 
ATOM   1112 N N   . VAL A 1 147 ? -9.093  32.144  22.184 1.00 66.24  ? 155 VAL A N   1 
ATOM   1113 C CA  . VAL A 1 147 ? -7.989  32.800  22.939 1.00 69.24  ? 155 VAL A CA  1 
ATOM   1114 C C   . VAL A 1 147 ? -7.880  32.257  24.367 1.00 75.94  ? 155 VAL A C   1 
ATOM   1115 O O   . VAL A 1 147 ? -6.748  32.160  24.864 1.00 86.70  ? 155 VAL A O   1 
ATOM   1116 C CB  . VAL A 1 147 ? -8.225  34.321  22.916 1.00 64.37  ? 155 VAL A CB  1 
ATOM   1117 C CG1 . VAL A 1 147 ? -7.236  35.083  23.789 1.00 59.84  ? 155 VAL A CG1 1 
ATOM   1118 C CG2 . VAL A 1 147 ? -8.204  34.854  21.491 1.00 55.77  ? 155 VAL A CG2 1 
ATOM   1119 N N   . SER A 1 148 ? -8.987  31.856  24.986 1.00 78.88  ? 156 SER A N   1 
ATOM   1120 C CA  . SER A 1 148 ? -8.876  31.496  26.391 1.00 85.11  ? 156 SER A CA  1 
ATOM   1121 C C   . SER A 1 148 ? -8.825  29.977  26.571 1.00 76.14  ? 156 SER A C   1 
ATOM   1122 O O   . SER A 1 148 ? -8.875  29.490  27.689 1.00 67.31  ? 156 SER A O   1 
ATOM   1123 C CB  . SER A 1 148 ? -10.013 32.097  27.167 1.00 92.54  ? 156 SER A CB  1 
ATOM   1124 O OG  . SER A 1 148 ? -11.252 31.712  26.584 1.00 102.10 ? 156 SER A OG  1 
ATOM   1125 N N   . GLN A 1 149 ? -8.708  29.229  25.471 1.00 76.40  ? 157 GLN A N   1 
ATOM   1126 C CA  . GLN A 1 149 ? -8.559  27.787  25.538 1.00 71.57  ? 157 GLN A CA  1 
ATOM   1127 C C   . GLN A 1 149 ? -7.133  27.391  25.161 1.00 64.17  ? 157 GLN A C   1 
ATOM   1128 O O   . GLN A 1 149 ? -6.945  26.300  24.651 1.00 66.80  ? 157 GLN A O   1 
ATOM   1129 C CB  . GLN A 1 149 ? -9.559  27.115  24.596 1.00 80.14  ? 157 GLN A CB  1 
ATOM   1130 C CG  . GLN A 1 149 ? -11.022 27.279  25.003 1.00 92.34  ? 157 GLN A CG  1 
ATOM   1131 C CD  . GLN A 1 149 ? -11.445 26.338  26.111 1.00 99.25  ? 157 GLN A CD  1 
ATOM   1132 O OE1 . GLN A 1 149 ? -11.039 26.488  27.270 1.00 98.79  ? 157 GLN A OE1 1 
ATOM   1133 N NE2 . GLN A 1 149 ? -12.275 25.362  25.766 1.00 99.32  ? 157 GLN A NE2 1 
ATOM   1134 N N   . VAL A 1 150 ? -6.138  28.263  25.407 1.00 59.39  ? 158 VAL A N   1 
ATOM   1135 C CA  . VAL A 1 150 ? -4.733  27.952  25.154 1.00 54.49  ? 158 VAL A CA  1 
ATOM   1136 C C   . VAL A 1 150 ? -3.899  28.383  26.357 1.00 52.84  ? 158 VAL A C   1 
ATOM   1137 O O   . VAL A 1 150 ? -4.357  29.102  27.236 1.00 53.90  ? 158 VAL A O   1 
ATOM   1138 C CB  . VAL A 1 150 ? -4.142  28.624  23.901 1.00 60.50  ? 158 VAL A CB  1 
ATOM   1139 C CG1 . VAL A 1 150 ? -4.718  28.053  22.608 1.00 62.41  ? 158 VAL A CG1 1 
ATOM   1140 C CG2 . VAL A 1 150 ? -4.305  30.143  23.966 1.00 61.09  ? 158 VAL A CG2 1 
ATOM   1141 N N   . ILE A 1 151 ? -2.635  27.968  26.350 1.00 52.33  ? 159 ILE A N   1 
ATOM   1142 C CA  . ILE A 1 151 ? -1.761  28.190  27.481 1.00 52.23  ? 159 ILE A CA  1 
ATOM   1143 C C   . ILE A 1 151 ? -1.774  29.674  27.844 1.00 52.25  ? 159 ILE A C   1 
ATOM   1144 O O   . ILE A 1 151 ? -1.970  30.540  26.994 1.00 43.92  ? 159 ILE A O   1 
ATOM   1145 C CB  . ILE A 1 151 ? -0.332  27.674  27.223 1.00 50.57  ? 159 ILE A CB  1 
ATOM   1146 C CG1 . ILE A 1 151 ? 0.301   28.355  25.990 1.00 46.59  ? 159 ILE A CG1 1 
ATOM   1147 C CG2 . ILE A 1 151 ? -0.313  26.139  27.163 1.00 49.22  ? 159 ILE A CG2 1 
ATOM   1148 C CD1 . ILE A 1 151 ? 1.724   27.915  25.694 1.00 47.65  ? 159 ILE A CD1 1 
ATOM   1149 N N   . PRO A 1 152 ? -1.627  29.976  29.151 1.00 47.60  ? 160 PRO A N   1 
ATOM   1150 C CA  . PRO A 1 152 ? -1.637  31.350  29.632 1.00 47.81  ? 160 PRO A CA  1 
ATOM   1151 C C   . PRO A 1 152 ? -0.832  32.354  28.818 1.00 48.20  ? 160 PRO A C   1 
ATOM   1152 O O   . PRO A 1 152 ? -1.288  33.461  28.607 1.00 48.79  ? 160 PRO A O   1 
ATOM   1153 C CB  . PRO A 1 152 ? -1.035  31.136  31.023 1.00 53.41  ? 160 PRO A CB  1 
ATOM   1154 C CG  . PRO A 1 152 ? -1.608  29.817  31.478 1.00 52.71  ? 160 PRO A CG  1 
ATOM   1155 C CD  . PRO A 1 152 ? -1.562  28.973  30.228 1.00 48.00  ? 160 PRO A CD  1 
ATOM   1156 N N   . GLY A 1 153 ? 0.378   31.965  28.407 1.00 52.20  ? 161 GLY A N   1 
ATOM   1157 C CA  . GLY A 1 153 ? 1.305   32.860  27.735 1.00 47.45  ? 161 GLY A CA  1 
ATOM   1158 C C   . GLY A 1 153 ? 0.825   33.254  26.337 1.00 47.67  ? 161 GLY A C   1 
ATOM   1159 O O   . GLY A 1 153 ? 1.047   34.383  25.873 1.00 45.62  ? 161 GLY A O   1 
ATOM   1160 N N   . TRP A 1 154 ? 0.158   32.325  25.657 1.00 47.09  ? 162 TRP A N   1 
ATOM   1161 C CA  . TRP A 1 154 ? -0.494  32.660  24.396 1.00 52.60  ? 162 TRP A CA  1 
ATOM   1162 C C   . TRP A 1 154 ? -1.608  33.679  24.628 1.00 55.32  ? 162 TRP A C   1 
ATOM   1163 O O   . TRP A 1 154 ? -1.692  34.675  23.904 1.00 56.08  ? 162 TRP A O   1 
ATOM   1164 C CB  . TRP A 1 154 ? -1.038  31.401  23.717 1.00 53.25  ? 162 TRP A CB  1 
ATOM   1165 C CG  . TRP A 1 154 ? -0.002  30.681  22.903 1.00 51.74  ? 162 TRP A CG  1 
ATOM   1166 C CD1 . TRP A 1 154 ? 1.302   30.429  23.205 1.00 54.04  ? 162 TRP A CD1 1 
ATOM   1167 C CD2 . TRP A 1 154 ? -0.207  30.169  21.584 1.00 50.85  ? 162 TRP A CD2 1 
ATOM   1168 N NE1 . TRP A 1 154 ? 1.913   29.761  22.183 1.00 49.78  ? 162 TRP A NE1 1 
ATOM   1169 C CE2 . TRP A 1 154 ? 1.012   29.601  21.171 1.00 52.56  ? 162 TRP A CE2 1 
ATOM   1170 C CE3 . TRP A 1 154 ? -1.306  30.133  20.730 1.00 54.14  ? 162 TRP A CE3 1 
ATOM   1171 C CZ2 . TRP A 1 154 ? 1.157   29.003  19.927 1.00 57.16  ? 162 TRP A CZ2 1 
ATOM   1172 C CZ3 . TRP A 1 154 ? -1.159  29.534  19.499 1.00 59.27  ? 162 TRP A CZ3 1 
ATOM   1173 C CH2 . TRP A 1 154 ? 0.056   28.984  19.104 1.00 55.55  ? 162 TRP A CH2 1 
ATOM   1174 N N   . THR A 1 155 ? -2.418  33.440  25.674 1.00 53.24  ? 163 THR A N   1 
ATOM   1175 C CA  . THR A 1 155 ? -3.533  34.312  26.014 1.00 55.49  ? 163 THR A CA  1 
ATOM   1176 C C   . THR A 1 155 ? -3.038  35.739  26.290 1.00 54.96  ? 163 THR A C   1 
ATOM   1177 O O   . THR A 1 155 ? -3.658  36.712  25.860 1.00 63.41  ? 163 THR A O   1 
ATOM   1178 C CB  . THR A 1 155 ? -4.288  33.709  27.199 1.00 58.83  ? 163 THR A CB  1 
ATOM   1179 O OG1 . THR A 1 155 ? -4.591  32.339  26.958 1.00 61.85  ? 163 THR A OG1 1 
ATOM   1180 C CG2 . THR A 1 155 ? -5.644  34.349  27.397 1.00 63.07  ? 163 THR A CG2 1 
ATOM   1181 N N   . GLU A 1 156 ? -1.948  35.854  27.044 1.00 51.07  ? 164 GLU A N   1 
ATOM   1182 C CA  . GLU A 1 156 ? -1.466  37.210  27.404 1.00 54.36  ? 164 GLU A CA  1 
ATOM   1183 C C   . GLU A 1 156 ? -0.936  37.891  26.137 1.00 51.02  ? 164 GLU A C   1 
ATOM   1184 O O   . GLU A 1 156 ? -1.326  39.051  25.880 1.00 54.28  ? 164 GLU A O   1 
ATOM   1185 C CB  . GLU A 1 156 ? -0.416  37.097  28.504 1.00 64.07  ? 164 GLU A CB  1 
ATOM   1186 C CG  . GLU A 1 156 ? -0.961  36.339  29.706 1.00 75.44  ? 164 GLU A CG  1 
ATOM   1187 C CD  . GLU A 1 156 ? 0.118   35.750  30.587 1.00 102.89 ? 164 GLU A CD  1 
ATOM   1188 O OE1 . GLU A 1 156 ? 1.227   36.319  30.614 1.00 131.33 ? 164 GLU A OE1 1 
ATOM   1189 O OE2 . GLU A 1 156 ? -0.167  34.733  31.247 1.00 112.52 ? 164 GLU A OE2 1 
ATOM   1190 N N   . ALA A 1 157 ? -0.100  37.187  25.372 1.00 52.26  ? 165 ALA A N   1 
ATOM   1191 C CA  . ALA A 1 157 ? 0.477   37.820  24.195 1.00 61.34  ? 165 ALA A CA  1 
ATOM   1192 C C   . ALA A 1 157 ? -0.618  38.210  23.186 1.00 61.80  ? 165 ALA A C   1 
ATOM   1193 O O   . ALA A 1 157 ? -0.703  39.351  22.719 1.00 58.81  ? 165 ALA A O   1 
ATOM   1194 C CB  . ALA A 1 157 ? 1.520   36.907  23.570 1.00 60.31  ? 165 ALA A CB  1 
ATOM   1195 N N   . LEU A 1 158 ? -1.485  37.259  22.855 1.00 56.98  ? 166 LEU A N   1 
ATOM   1196 C CA  . LEU A 1 158 ? -2.473  37.488  21.822 1.00 57.27  ? 166 LEU A CA  1 
ATOM   1197 C C   . LEU A 1 158 ? -3.274  38.762  22.080 1.00 59.90  ? 166 LEU A C   1 
ATOM   1198 O O   . LEU A 1 158 ? -3.557  39.507  21.128 1.00 57.03  ? 166 LEU A O   1 
ATOM   1199 C CB  . LEU A 1 158 ? -3.343  36.245  21.746 1.00 55.99  ? 166 LEU A CB  1 
ATOM   1200 C CG  . LEU A 1 158 ? -2.677  35.079  21.018 1.00 58.84  ? 166 LEU A CG  1 
ATOM   1201 C CD1 . LEU A 1 158 ? -3.473  33.826  21.287 1.00 57.59  ? 166 LEU A CD1 1 
ATOM   1202 C CD2 . LEU A 1 158 ? -2.544  35.350  19.499 1.00 66.04  ? 166 LEU A CD2 1 
ATOM   1203 N N   . GLN A 1 159 ? -3.574  39.036  23.359 1.00 48.21  ? 167 GLN A N   1 
ATOM   1204 C CA  . GLN A 1 159 ? -4.357  40.211  23.710 1.00 55.51  ? 167 GLN A CA  1 
ATOM   1205 C C   . GLN A 1 159 ? -3.597  41.518  23.484 1.00 54.62  ? 167 GLN A C   1 
ATOM   1206 O O   . GLN A 1 159 ? -4.165  42.597  23.642 1.00 51.01  ? 167 GLN A O   1 
ATOM   1207 C CB  . GLN A 1 159 ? -4.723  40.176  25.187 1.00 61.36  ? 167 GLN A CB  1 
ATOM   1208 C CG  . GLN A 1 159 ? -5.800  39.164  25.547 1.00 61.95  ? 167 GLN A CG  1 
ATOM   1209 C CD  . GLN A 1 159 ? -6.133  39.277  27.018 1.00 69.35  ? 167 GLN A CD  1 
ATOM   1210 O OE1 . GLN A 1 159 ? -5.358  38.838  27.874 1.00 67.05  ? 167 GLN A OE1 1 
ATOM   1211 N NE2 . GLN A 1 159 ? -7.266  39.897  27.336 1.00 65.50  ? 167 GLN A NE2 1 
ATOM   1212 N N   . LEU A 1 160 ? -2.302  41.409  23.163 1.00 59.82  ? 168 LEU A N   1 
ATOM   1213 C CA  . LEU A 1 160 ? -1.488  42.554  22.792 1.00 60.65  ? 168 LEU A CA  1 
ATOM   1214 C C   . LEU A 1 160 ? -1.183  42.621  21.288 1.00 56.32  ? 168 LEU A C   1 
ATOM   1215 O O   . LEU A 1 160 ? -0.585  43.617  20.858 1.00 50.81  ? 168 LEU A O   1 
ATOM   1216 C CB  . LEU A 1 160 ? -0.206  42.416  23.602 1.00 58.62  ? 168 LEU A CB  1 
ATOM   1217 C CG  . LEU A 1 160 ? -0.394  42.377  25.121 1.00 56.83  ? 168 LEU A CG  1 
ATOM   1218 C CD1 . LEU A 1 160 ? 0.890   41.857  25.707 1.00 55.51  ? 168 LEU A CD1 1 
ATOM   1219 C CD2 . LEU A 1 160 ? -0.746  43.736  25.684 1.00 52.39  ? 168 LEU A CD2 1 
ATOM   1220 N N   . MET A 1 161 ? -1.561  41.577  20.515 1.00 49.66  ? 169 MET A N   1 
ATOM   1221 C CA  . MET A 1 161 ? -1.125  41.433  19.123 1.00 54.15  ? 169 MET A CA  1 
ATOM   1222 C C   . MET A 1 161 ? -2.222  41.855  18.155 1.00 50.54  ? 169 MET A C   1 
ATOM   1223 O O   . MET A 1 161 ? -3.244  41.166  18.050 1.00 48.33  ? 169 MET A O   1 
ATOM   1224 C CB  . MET A 1 161 ? -0.802  39.986  18.737 1.00 52.83  ? 169 MET A CB  1 
ATOM   1225 C CG  . MET A 1 161 ? 0.565   39.556  19.188 1.00 57.15  ? 169 MET A CG  1 
ATOM   1226 S SD  . MET A 1 161 ? 0.807   37.807  18.864 1.00 64.52  ? 169 MET A SD  1 
ATOM   1227 C CE  . MET A 1 161 ? 1.083   37.879  17.090 1.00 66.85  ? 169 MET A CE  1 
ATOM   1228 N N   . PRO A 1 162 ? -2.038  42.975  17.412 1.00 46.50  ? 170 PRO A N   1 
ATOM   1229 C CA  . PRO A 1 162 ? -2.906  43.292  16.271 1.00 48.34  ? 170 PRO A CA  1 
ATOM   1230 C C   . PRO A 1 162 ? -2.776  42.164  15.258 1.00 45.32  ? 170 PRO A C   1 
ATOM   1231 O O   . PRO A 1 162 ? -1.676  41.629  15.053 1.00 38.55  ? 170 PRO A O   1 
ATOM   1232 C CB  . PRO A 1 162 ? -2.406  44.626  15.723 1.00 48.58  ? 170 PRO A CB  1 
ATOM   1233 C CG  . PRO A 1 162 ? -1.616  45.192  16.891 1.00 52.68  ? 170 PRO A CG  1 
ATOM   1234 C CD  . PRO A 1 162 ? -1.005  43.996  17.626 1.00 44.83  ? 170 PRO A CD  1 
ATOM   1235 N N   . ALA A 1 163 ? -3.927  41.773  14.697 1.00 48.99  ? 171 ALA A N   1 
ATOM   1236 C CA  . ALA A 1 163 ? -3.974  40.846  13.574 1.00 52.13  ? 171 ALA A CA  1 
ATOM   1237 C C   . ALA A 1 163 ? -3.060  41.353  12.461 1.00 51.58  ? 171 ALA A C   1 
ATOM   1238 O O   . ALA A 1 163 ? -3.003  42.562  12.209 1.00 54.03  ? 171 ALA A O   1 
ATOM   1239 C CB  . ALA A 1 163 ? -5.400  40.687  13.112 1.00 51.00  ? 171 ALA A CB  1 
ATOM   1240 N N   . GLY A 1 164 ? -2.301  40.415  11.868 1.00 54.11  ? 172 GLY A N   1 
ATOM   1241 C CA  . GLY A 1 164 ? -1.298  40.701  10.851 1.00 48.49  ? 172 GLY A CA  1 
ATOM   1242 C C   . GLY A 1 164 ? 0.116   40.634  11.416 1.00 47.80  ? 172 GLY A C   1 
ATOM   1243 O O   . GLY A 1 164 ? 1.086   40.598  10.651 1.00 45.70  ? 172 GLY A O   1 
ATOM   1244 N N   . SER A 1 165 ? 0.198   40.582  12.755 1.00 48.83  ? 173 SER A N   1 
ATOM   1245 C CA  . SER A 1 165 ? 1.442   40.662  13.512 1.00 48.28  ? 173 SER A CA  1 
ATOM   1246 C C   . SER A 1 165 ? 2.207   39.348  13.443 1.00 41.64  ? 173 SER A C   1 
ATOM   1247 O O   . SER A 1 165 ? 1.595   38.292  13.390 1.00 38.85  ? 173 SER A O   1 
ATOM   1248 C CB  . SER A 1 165 ? 1.164   41.008  14.973 1.00 52.43  ? 173 SER A CB  1 
ATOM   1249 O OG  . SER A 1 165 ? 0.628   42.319  15.111 1.00 50.85  ? 173 SER A OG  1 
ATOM   1250 N N   . THR A 1 166 ? 3.543   39.426  13.485 1.00 44.65  ? 174 THR A N   1 
ATOM   1251 C CA  . THR A 1 166 ? 4.377   38.245  13.670 1.00 48.71  ? 174 THR A CA  1 
ATOM   1252 C C   . THR A 1 166 ? 5.343   38.574  14.804 1.00 50.31  ? 174 THR A C   1 
ATOM   1253 O O   . THR A 1 166 ? 6.031   39.586  14.724 1.00 49.77  ? 174 THR A O   1 
ATOM   1254 C CB  . THR A 1 166 ? 5.093   37.817  12.376 1.00 44.95  ? 174 THR A CB  1 
ATOM   1255 O OG1 . THR A 1 166 ? 4.053   37.397  11.508 1.00 41.28  ? 174 THR A OG1 1 
ATOM   1256 C CG2 . THR A 1 166 ? 5.983   36.588  12.513 1.00 40.81  ? 174 THR A CG2 1 
ATOM   1257 N N   . TRP A 1 167 ? 5.322   37.730  15.856 1.00 56.60  ? 175 TRP A N   1 
ATOM   1258 C CA  . TRP A 1 167 ? 6.090   37.890  17.094 1.00 51.31  ? 175 TRP A CA  1 
ATOM   1259 C C   . TRP A 1 167 ? 6.805   36.575  17.421 1.00 46.61  ? 175 TRP A C   1 
ATOM   1260 O O   . TRP A 1 167 ? 6.274   35.506  17.133 1.00 51.56  ? 175 TRP A O   1 
ATOM   1261 C CB  . TRP A 1 167 ? 5.161   38.251  18.262 1.00 45.43  ? 175 TRP A CB  1 
ATOM   1262 C CG  . TRP A 1 167 ? 4.598   39.643  18.300 1.00 50.02  ? 175 TRP A CG  1 
ATOM   1263 C CD1 . TRP A 1 167 ? 4.537   40.588  17.319 1.00 56.03  ? 175 TRP A CD1 1 
ATOM   1264 C CD2 . TRP A 1 167 ? 3.946   40.228  19.448 1.00 59.30  ? 175 TRP A CD2 1 
ATOM   1265 N NE1 . TRP A 1 167 ? 3.925   41.723  17.782 1.00 57.46  ? 175 TRP A NE1 1 
ATOM   1266 C CE2 . TRP A 1 167 ? 3.544   41.529  19.081 1.00 55.99  ? 175 TRP A CE2 1 
ATOM   1267 C CE3 . TRP A 1 167 ? 3.666   39.775  20.746 1.00 60.90  ? 175 TRP A CE3 1 
ATOM   1268 C CZ2 . TRP A 1 167 ? 2.881   42.377  19.966 1.00 63.49  ? 175 TRP A CZ2 1 
ATOM   1269 C CZ3 . TRP A 1 167 ? 2.998   40.610  21.616 1.00 59.62  ? 175 TRP A CZ3 1 
ATOM   1270 C CH2 . TRP A 1 167 ? 2.618   41.897  21.230 1.00 62.29  ? 175 TRP A CH2 1 
ATOM   1271 N N   . GLU A 1 168 ? 7.982   36.652  18.047 1.00 44.35  ? 176 GLU A N   1 
ATOM   1272 C CA  . GLU A 1 168 ? 8.587   35.510  18.736 1.00 51.94  ? 176 GLU A CA  1 
ATOM   1273 C C   . GLU A 1 168 ? 8.354   35.701  20.241 1.00 53.07  ? 176 GLU A C   1 
ATOM   1274 O O   . GLU A 1 168 ? 8.644   36.759  20.788 1.00 51.06  ? 176 GLU A O   1 
ATOM   1275 C CB  . GLU A 1 168 ? 10.072  35.472  18.353 1.00 61.26  ? 176 GLU A CB  1 
ATOM   1276 C CG  . GLU A 1 168 ? 10.791  34.135  18.534 1.00 68.22  ? 176 GLU A CG  1 
ATOM   1277 C CD  . GLU A 1 168 ? 12.185  34.054  17.908 1.00 77.04  ? 176 GLU A CD  1 
ATOM   1278 O OE1 . GLU A 1 168 ? 12.986  35.007  18.047 1.00 71.97  ? 176 GLU A OE1 1 
ATOM   1279 O OE2 . GLU A 1 168 ? 12.497  33.010  17.287 1.00 93.10  ? 176 GLU A OE2 1 
ATOM   1280 N N   . ILE A 1 169 ? 7.766   34.716  20.918 1.00 52.26  ? 177 ILE A N   1 
ATOM   1281 C CA  . ILE A 1 169 ? 7.525   34.837  22.352 1.00 53.14  ? 177 ILE A CA  1 
ATOM   1282 C C   . ILE A 1 169 ? 8.258   33.733  23.111 1.00 55.55  ? 177 ILE A C   1 
ATOM   1283 O O   . ILE A 1 169 ? 8.425   32.605  22.621 1.00 48.11  ? 177 ILE A O   1 
ATOM   1284 C CB  . ILE A 1 169 ? 6.027   34.801  22.706 1.00 57.67  ? 177 ILE A CB  1 
ATOM   1285 C CG1 . ILE A 1 169 ? 5.424   33.400  22.432 1.00 52.92  ? 177 ILE A CG1 1 
ATOM   1286 C CG2 . ILE A 1 169 ? 5.277   35.937  22.001 1.00 63.41  ? 177 ILE A CG2 1 
ATOM   1287 C CD1 . ILE A 1 169 ? 3.994   33.207  22.901 1.00 52.74  ? 177 ILE A CD1 1 
ATOM   1288 N N   . TYR A 1 170 ? 8.653   34.088  24.343 1.00 53.21  ? 178 TYR A N   1 
ATOM   1289 C CA  . TYR A 1 170 ? 9.415   33.206  25.212 1.00 51.84  ? 178 TYR A CA  1 
ATOM   1290 C C   . TYR A 1 170 ? 8.637   33.093  26.517 1.00 51.55  ? 178 TYR A C   1 
ATOM   1291 O O   . TYR A 1 170 ? 8.301   34.104  27.130 1.00 46.25  ? 178 TYR A O   1 
ATOM   1292 C CB  . TYR A 1 170 ? 10.829  33.769  25.373 1.00 52.53  ? 178 TYR A CB  1 
ATOM   1293 C CG  . TYR A 1 170 ? 11.454  34.298  24.090 1.00 52.74  ? 178 TYR A CG  1 
ATOM   1294 C CD1 . TYR A 1 170 ? 11.208  35.598  23.671 1.00 58.00  ? 178 TYR A CD1 1 
ATOM   1295 C CD2 . TYR A 1 170 ? 12.277  33.511  23.296 1.00 53.68  ? 178 TYR A CD2 1 
ATOM   1296 C CE1 . TYR A 1 170 ? 11.749  36.106  22.503 1.00 54.35  ? 178 TYR A CE1 1 
ATOM   1297 C CE2 . TYR A 1 170 ? 12.843  34.014  22.136 1.00 58.90  ? 178 TYR A CE2 1 
ATOM   1298 C CZ  . TYR A 1 170 ? 12.586  35.318  21.745 1.00 56.81  ? 178 TYR A CZ  1 
ATOM   1299 O OH  . TYR A 1 170 ? 13.126  35.863  20.623 1.00 62.35  ? 178 TYR A OH  1 
ATOM   1300 N N   . VAL A 1 171 ? 8.330   31.849  26.894 1.00 54.41  ? 179 VAL A N   1 
ATOM   1301 C CA  . VAL A 1 171 ? 7.199   31.553  27.757 1.00 55.41  ? 179 VAL A CA  1 
ATOM   1302 C C   . VAL A 1 171 ? 7.673   30.747  28.956 1.00 55.10  ? 179 VAL A C   1 
ATOM   1303 O O   . VAL A 1 171 ? 7.875   29.533  28.824 1.00 51.33  ? 179 VAL A O   1 
ATOM   1304 C CB  . VAL A 1 171 ? 6.115   30.757  27.012 1.00 54.67  ? 179 VAL A CB  1 
ATOM   1305 C CG1 . VAL A 1 171 ? 4.861   30.614  27.872 1.00 56.73  ? 179 VAL A CG1 1 
ATOM   1306 C CG2 . VAL A 1 171 ? 5.795   31.372  25.651 1.00 54.62  ? 179 VAL A CG2 1 
ATOM   1307 N N   . PRO A 1 172 ? 7.800   31.388  30.145 1.00 56.13  ? 180 PRO A N   1 
ATOM   1308 C CA  . PRO A 1 172 ? 8.104   30.664  31.388 1.00 61.12  ? 180 PRO A CA  1 
ATOM   1309 C C   . PRO A 1 172 ? 7.097   29.544  31.658 1.00 55.99  ? 180 PRO A C   1 
ATOM   1310 O O   . PRO A 1 172 ? 5.906   29.710  31.374 1.00 59.44  ? 180 PRO A O   1 
ATOM   1311 C CB  . PRO A 1 172 ? 8.090   31.751  32.487 1.00 57.96  ? 180 PRO A CB  1 
ATOM   1312 C CG  . PRO A 1 172 ? 7.401   32.938  31.849 1.00 58.96  ? 180 PRO A CG  1 
ATOM   1313 C CD  . PRO A 1 172 ? 7.640   32.837  30.353 1.00 53.45  ? 180 PRO A CD  1 
ATOM   1314 N N   . SER A 1 173 ? 7.583   28.409  32.196 1.00 48.96  ? 181 SER A N   1 
ATOM   1315 C CA  . SER A 1 173 ? 6.766   27.205  32.364 1.00 51.18  ? 181 SER A CA  1 
ATOM   1316 C C   . SER A 1 173 ? 5.467   27.467  33.136 1.00 51.96  ? 181 SER A C   1 
ATOM   1317 O O   . SER A 1 173 ? 4.458   26.817  32.890 1.00 48.14  ? 181 SER A O   1 
ATOM   1318 C CB  . SER A 1 173 ? 7.544   26.115  33.027 1.00 52.74  ? 181 SER A CB  1 
ATOM   1319 O OG  . SER A 1 173 ? 8.075   26.563  34.265 1.00 59.81  ? 181 SER A OG  1 
ATOM   1320 N N   . GLY A 1 174 ? 5.482   28.432  34.062 1.00 51.16  ? 182 GLY A N   1 
ATOM   1321 C CA  . GLY A 1 174 ? 4.284   28.836  34.771 1.00 51.61  ? 182 GLY A CA  1 
ATOM   1322 C C   . GLY A 1 174 ? 3.155   29.280  33.846 1.00 52.70  ? 182 GLY A C   1 
ATOM   1323 O O   . GLY A 1 174 ? 2.001   29.227  34.241 1.00 53.20  ? 182 GLY A O   1 
ATOM   1324 N N   . LEU A 1 175 ? 3.492   29.773  32.649 1.00 59.66  ? 183 LEU A N   1 
ATOM   1325 C CA  . LEU A 1 175 ? 2.500   30.295  31.723 1.00 59.94  ? 183 LEU A CA  1 
ATOM   1326 C C   . LEU A 1 175 ? 2.251   29.277  30.620 1.00 56.62  ? 183 LEU A C   1 
ATOM   1327 O O   . LEU A 1 175 ? 1.473   29.549  29.714 1.00 56.34  ? 183 LEU A O   1 
ATOM   1328 C CB  . LEU A 1 175 ? 2.947   31.633  31.124 1.00 58.87  ? 183 LEU A CB  1 
ATOM   1329 C CG  . LEU A 1 175 ? 3.056   32.816  32.092 1.00 56.10  ? 183 LEU A CG  1 
ATOM   1330 C CD1 . LEU A 1 175 ? 3.363   34.115  31.381 1.00 55.14  ? 183 LEU A CD1 1 
ATOM   1331 C CD2 . LEU A 1 175 ? 1.789   32.970  32.906 1.00 55.59  ? 183 LEU A CD2 1 
ATOM   1332 N N   . ALA A 1 176 ? 2.908   28.128  30.708 1.00 52.66  ? 184 ALA A N   1 
ATOM   1333 C CA  . ALA A 1 176 ? 2.743   27.077  29.685 1.00 55.58  ? 184 ALA A CA  1 
ATOM   1334 C C   . ALA A 1 176 ? 2.018   25.884  30.299 1.00 58.04  ? 184 ALA A C   1 
ATOM   1335 O O   . ALA A 1 176 ? 0.899   26.068  30.810 1.00 61.33  ? 184 ALA A O   1 
ATOM   1336 C CB  . ALA A 1 176 ? 4.090   26.681  29.158 1.00 59.33  ? 184 ALA A CB  1 
ATOM   1337 N N   . TYR A 1 177 ? 2.642   24.703  30.263 1.00 64.77  ? 185 TYR A N   1 
ATOM   1338 C CA  . TYR A 1 177 ? 1.998   23.469  30.793 1.00 64.01  ? 185 TYR A CA  1 
ATOM   1339 C C   . TYR A 1 177 ? 2.395   23.266  32.252 1.00 64.24  ? 185 TYR A C   1 
ATOM   1340 O O   . TYR A 1 177 ? 1.856   22.348  32.904 1.00 67.02  ? 185 TYR A O   1 
ATOM   1341 C CB  . TYR A 1 177 ? 2.405   22.280  29.919 1.00 62.92  ? 185 TYR A CB  1 
ATOM   1342 C CG  . TYR A 1 177 ? 2.078   22.482  28.447 1.00 60.49  ? 185 TYR A CG  1 
ATOM   1343 C CD1 . TYR A 1 177 ? 3.075   22.765  27.521 1.00 60.63  ? 185 TYR A CD1 1 
ATOM   1344 C CD2 . TYR A 1 177 ? 0.769   22.405  27.989 1.00 59.74  ? 185 TYR A CD2 1 
ATOM   1345 C CE1 . TYR A 1 177 ? 2.778   22.956  26.183 1.00 59.97  ? 185 TYR A CE1 1 
ATOM   1346 C CE2 . TYR A 1 177 ? 0.461   22.592  26.652 1.00 58.01  ? 185 TYR A CE2 1 
ATOM   1347 C CZ  . TYR A 1 177 ? 1.469   22.870  25.747 1.00 61.51  ? 185 TYR A CZ  1 
ATOM   1348 O OH  . TYR A 1 177 ? 1.173   23.057  24.428 1.00 78.36  ? 185 TYR A OH  1 
ATOM   1349 N N   . GLY A 1 178 ? 3.324   24.086  32.749 1.00 71.43  ? 186 GLY A N   1 
ATOM   1350 C CA  . GLY A 1 178 ? 3.737   23.998  34.160 1.00 66.89  ? 186 GLY A CA  1 
ATOM   1351 C C   . GLY A 1 178 ? 4.407   22.683  34.464 1.00 62.42  ? 186 GLY A C   1 
ATOM   1352 O O   . GLY A 1 178 ? 5.071   22.136  33.566 1.00 65.31  ? 186 GLY A O   1 
ATOM   1353 N N   . PRO A 1 179 ? 4.283   22.141  35.691 1.00 62.01  ? 187 PRO A N   1 
ATOM   1354 C CA  . PRO A 1 179 ? 4.836   20.818  35.989 1.00 70.66  ? 187 PRO A CA  1 
ATOM   1355 C C   . PRO A 1 179 ? 3.904   19.654  35.667 1.00 77.54  ? 187 PRO A C   1 
ATOM   1356 O O   . PRO A 1 179 ? 4.109   18.570  36.198 1.00 84.91  ? 187 PRO A O   1 
ATOM   1357 C CB  . PRO A 1 179 ? 5.090   20.965  37.503 1.00 65.33  ? 187 PRO A CB  1 
ATOM   1358 C CG  . PRO A 1 179 ? 3.916   21.787  37.992 1.00 59.77  ? 187 PRO A CG  1 
ATOM   1359 C CD  . PRO A 1 179 ? 3.560   22.715  36.837 1.00 61.04  ? 187 PRO A CD  1 
ATOM   1360 N N   . ARG A 1 180 ? 2.893   19.898  34.809 1.00 89.45  ? 188 ARG A N   1 
ATOM   1361 C CA  . ARG A 1 180 ? 1.821   18.953  34.523 1.00 83.88  ? 188 ARG A CA  1 
ATOM   1362 C C   . ARG A 1 180 ? 2.200   18.163  33.282 1.00 92.83  ? 188 ARG A C   1 
ATOM   1363 O O   . ARG A 1 180 ? 1.328   17.683  32.559 1.00 116.24 ? 188 ARG A O   1 
ATOM   1364 C CB  . ARG A 1 180 ? 0.461   19.616  34.254 1.00 86.80  ? 188 ARG A CB  1 
ATOM   1365 C CG  . ARG A 1 180 ? -0.231  20.256  35.453 1.00 96.39  ? 188 ARG A CG  1 
ATOM   1366 C CD  . ARG A 1 180 ? -0.072  21.779  35.571 1.00 96.68  ? 188 ARG A CD  1 
ATOM   1367 N NE  . ARG A 1 180 ? -0.987  22.540  34.710 1.00 111.41 ? 188 ARG A NE  1 
ATOM   1368 C CZ  . ARG A 1 180 ? -2.323  22.563  34.800 1.00 135.08 ? 188 ARG A CZ  1 
ATOM   1369 N NH1 . ARG A 1 180 ? -2.952  21.886  35.750 1.00 137.62 ? 188 ARG A NH1 1 
ATOM   1370 N NH2 . ARG A 1 180 ? -3.037  23.270  33.936 1.00 136.43 ? 188 ARG A NH2 1 
ATOM   1371 N N   . SER A 1 181 ? 3.490   18.128  32.963 1.00 97.06  ? 189 SER A N   1 
ATOM   1372 C CA  . SER A 1 181 ? 3.884   17.515  31.665 1.00 116.52 ? 189 SER A CA  1 
ATOM   1373 C C   . SER A 1 181 ? 4.235   16.031  31.806 1.00 111.98 ? 189 SER A C   1 
ATOM   1374 O O   . SER A 1 181 ? 5.291   15.724  32.388 1.00 96.20  ? 189 SER A O   1 
ATOM   1375 C CB  . SER A 1 181 ? 5.012   18.284  31.054 1.00 125.49 ? 189 SER A CB  1 
ATOM   1376 O OG  . SER A 1 181 ? 5.070   19.605  31.576 1.00 127.93 ? 189 SER A OG  1 
ATOM   1377 N N   . VAL A 1 182 ? 3.406   15.152  31.245 1.00 107.91 ? 190 VAL A N   1 
ATOM   1378 C CA  . VAL A 1 182 ? 3.646   13.694  31.457 1.00 119.79 ? 190 VAL A CA  1 
ATOM   1379 C C   . VAL A 1 182 ? 3.711   12.963  30.110 1.00 123.82 ? 190 VAL A C   1 
ATOM   1380 O O   . VAL A 1 182 ? 2.872   12.069  29.882 1.00 103.62 ? 190 VAL A O   1 
ATOM   1381 C CB  . VAL A 1 182 ? 2.566   13.080  32.367 1.00 125.21 ? 190 VAL A CB  1 
ATOM   1382 C CG1 . VAL A 1 182 ? 3.164   12.515  33.649 1.00 116.23 ? 190 VAL A CG1 1 
ATOM   1383 C CG2 . VAL A 1 182 ? 1.453   14.073  32.682 1.00 121.06 ? 190 VAL A CG2 1 
ATOM   1384 N N   . GLY A 1 183 ? 4.673   13.317  29.260 1.00 124.40 ? 191 GLY A N   1 
ATOM   1385 C CA  . GLY A 1 183 ? 4.824   12.546  28.018 1.00 115.73 ? 191 GLY A CA  1 
ATOM   1386 C C   . GLY A 1 183 ? 5.418   13.328  26.871 1.00 108.59 ? 191 GLY A C   1 
ATOM   1387 O O   . GLY A 1 183 ? 4.904   14.422  26.559 1.00 100.15 ? 191 GLY A O   1 
ATOM   1388 N N   . GLY A 1 184 ? 6.484   12.802  26.277 1.00 93.64  ? 192 GLY A N   1 
ATOM   1389 C CA  . GLY A 1 184 ? 7.001   13.421  25.051 1.00 82.80  ? 192 GLY A CA  1 
ATOM   1390 C C   . GLY A 1 184 ? 8.193   14.320  25.225 1.00 83.47  ? 192 GLY A C   1 
ATOM   1391 O O   . GLY A 1 184 ? 8.846   14.280  26.282 1.00 80.15  ? 192 GLY A O   1 
ATOM   1392 N N   . PRO A 1 185 ? 8.487   15.139  24.206 1.00 80.26  ? 193 PRO A N   1 
ATOM   1393 C CA  . PRO A 1 185 ? 9.622   16.063  24.228 1.00 82.67  ? 193 PRO A CA  1 
ATOM   1394 C C   . PRO A 1 185 ? 9.434   17.185  25.254 1.00 75.91  ? 193 PRO A C   1 
ATOM   1395 O O   . PRO A 1 185 ? 10.433  17.745  25.714 1.00 72.63  ? 193 PRO A O   1 
ATOM   1396 C CB  . PRO A 1 185 ? 9.691   16.590  22.778 1.00 77.88  ? 193 PRO A CB  1 
ATOM   1397 C CG  . PRO A 1 185 ? 8.249   16.515  22.308 1.00 77.95  ? 193 PRO A CG  1 
ATOM   1398 C CD  . PRO A 1 185 ? 7.652   15.289  23.001 1.00 75.85  ? 193 PRO A CD  1 
ATOM   1399 N N   . ILE A 1 186 ? 8.168   17.499  25.614 1.00 65.19  ? 194 ILE A N   1 
ATOM   1400 C CA  . ILE A 1 186 ? 7.886   18.528  26.611 1.00 73.43  ? 194 ILE A CA  1 
ATOM   1401 C C   . ILE A 1 186 ? 7.817   17.920  28.012 1.00 74.55  ? 194 ILE A C   1 
ATOM   1402 O O   . ILE A 1 186 ? 6.810   17.311  28.385 1.00 75.75  ? 194 ILE A O   1 
ATOM   1403 C CB  . ILE A 1 186 ? 6.603   19.325  26.310 1.00 72.88  ? 194 ILE A CB  1 
ATOM   1404 C CG1 . ILE A 1 186 ? 6.749   20.196  25.063 1.00 66.69  ? 194 ILE A CG1 1 
ATOM   1405 C CG2 . ILE A 1 186 ? 6.221   20.177  27.524 1.00 76.58  ? 194 ILE A CG2 1 
ATOM   1406 C CD1 . ILE A 1 186 ? 5.506   20.989  24.703 1.00 60.00  ? 194 ILE A CD1 1 
ATOM   1407 N N   . GLY A 1 187 ? 8.874   18.160  28.801 1.00 76.02  ? 195 GLY A N   1 
ATOM   1408 C CA  . GLY A 1 187 ? 8.941   17.695  30.180 1.00 84.58  ? 195 GLY A CA  1 
ATOM   1409 C C   . GLY A 1 187 ? 8.448   18.735  31.193 1.00 73.90  ? 195 GLY A C   1 
ATOM   1410 O O   . GLY A 1 187 ? 8.142   19.879  30.850 1.00 82.63  ? 195 GLY A O   1 
ATOM   1411 N N   . PRO A 1 188 ? 8.397   18.364  32.491 1.00 61.58  ? 196 PRO A N   1 
ATOM   1412 C CA  . PRO A 1 188 ? 7.853   19.235  33.537 1.00 59.49  ? 196 PRO A CA  1 
ATOM   1413 C C   . PRO A 1 188 ? 8.647   20.533  33.650 1.00 54.75  ? 196 PRO A C   1 
ATOM   1414 O O   . PRO A 1 188 ? 9.873   20.519  33.542 1.00 55.67  ? 196 PRO A O   1 
ATOM   1415 C CB  . PRO A 1 188 ? 7.938   18.376  34.806 1.00 63.14  ? 196 PRO A CB  1 
ATOM   1416 C CG  . PRO A 1 188 ? 9.034   17.373  34.509 1.00 64.13  ? 196 PRO A CG  1 
ATOM   1417 C CD  . PRO A 1 188 ? 8.948   17.109  33.020 1.00 64.01  ? 196 PRO A CD  1 
ATOM   1418 N N   . ASN A 1 189 ? 7.923   21.649  33.799 1.00 52.57  ? 197 ASN A N   1 
ATOM   1419 C CA  . ASN A 1 189 ? 8.511   22.977  33.924 1.00 56.79  ? 197 ASN A CA  1 
ATOM   1420 C C   . ASN A 1 189 ? 9.413   23.362  32.743 1.00 58.14  ? 197 ASN A C   1 
ATOM   1421 O O   . ASN A 1 189 ? 10.465  23.954  32.973 1.00 56.02  ? 197 ASN A O   1 
ATOM   1422 C CB  . ASN A 1 189 ? 9.347   23.104  35.193 1.00 54.73  ? 197 ASN A CB  1 
ATOM   1423 C CG  . ASN A 1 189 ? 8.524   22.909  36.439 1.00 60.82  ? 197 ASN A CG  1 
ATOM   1424 O OD1 . ASN A 1 189 ? 7.308   23.115  36.412 1.00 61.48  ? 197 ASN A OD1 1 
ATOM   1425 N ND2 . ASN A 1 189 ? 9.172   22.557  37.540 1.00 63.61  ? 197 ASN A ND2 1 
ATOM   1426 N N   . GLU A 1 190 ? 9.016   23.082  31.488 1.00 64.12  ? 198 GLU A N   1 
ATOM   1427 C CA  . GLU A 1 190 ? 9.856   23.468  30.354 1.00 60.13  ? 198 GLU A CA  1 
ATOM   1428 C C   . GLU A 1 190 ? 9.450   24.875  29.894 1.00 54.53  ? 198 GLU A C   1 
ATOM   1429 O O   . GLU A 1 190 ? 8.259   25.213  29.805 1.00 51.83  ? 198 GLU A O   1 
ATOM   1430 C CB  . GLU A 1 190 ? 9.916   22.377  29.272 1.00 60.52  ? 198 GLU A CB  1 
ATOM   1431 C CG  . GLU A 1 190 ? 11.321  22.233  28.671 1.00 63.04  ? 198 GLU A CG  1 
ATOM   1432 C CD  . GLU A 1 190 ? 11.900  20.844  28.408 1.00 64.60  ? 198 GLU A CD  1 
ATOM   1433 O OE1 . GLU A 1 190 ? 11.163  19.815  28.377 1.00 64.52  ? 198 GLU A OE1 1 
ATOM   1434 O OE2 . GLU A 1 190 ? 13.158  20.798  28.258 1.00 59.87  ? 198 GLU A OE2 1 
ATOM   1435 N N   . THR A 1 191 ? 10.468  25.723  29.691 1.00 54.43  ? 199 THR A N   1 
ATOM   1436 C CA  . THR A 1 191 ? 10.291  27.019  29.044 1.00 57.33  ? 199 THR A CA  1 
ATOM   1437 C C   . THR A 1 191 ? 10.220  26.813  27.525 1.00 59.24  ? 199 THR A C   1 
ATOM   1438 O O   . THR A 1 191 ? 11.049  26.096  26.955 1.00 63.68  ? 199 THR A O   1 
ATOM   1439 C CB  . THR A 1 191 ? 11.408  27.996  29.432 1.00 52.15  ? 199 THR A CB  1 
ATOM   1440 O OG1 . THR A 1 191 ? 11.091  28.522  30.714 1.00 52.72  ? 199 THR A OG1 1 
ATOM   1441 C CG2 . THR A 1 191 ? 11.459  29.218  28.535 1.00 52.11  ? 199 THR A CG2 1 
ATOM   1442 N N   . LEU A 1 192 ? 9.244   27.493  26.897 1.00 55.73  ? 200 LEU A N   1 
ATOM   1443 C CA  . LEU A 1 192 ? 8.829   27.259  25.523 1.00 55.63  ? 200 LEU A CA  1 
ATOM   1444 C C   . LEU A 1 192 ? 9.026   28.520  24.675 1.00 56.36  ? 200 LEU A C   1 
ATOM   1445 O O   . LEU A 1 192 ? 8.771   29.638  25.118 1.00 53.65  ? 200 LEU A O   1 
ATOM   1446 C CB  . LEU A 1 192 ? 7.349   26.870  25.524 1.00 56.22  ? 200 LEU A CB  1 
ATOM   1447 C CG  . LEU A 1 192 ? 6.947   25.610  26.292 1.00 55.07  ? 200 LEU A CG  1 
ATOM   1448 C CD1 . LEU A 1 192 ? 5.482   25.307  26.047 1.00 51.73  ? 200 LEU A CD1 1 
ATOM   1449 C CD2 . LEU A 1 192 ? 7.810   24.408  25.920 1.00 59.61  ? 200 LEU A CD2 1 
ATOM   1450 N N   . ILE A 1 193 ? 9.407   28.327  23.411 1.00 54.50  ? 201 ILE A N   1 
ATOM   1451 C CA  . ILE A 1 193 ? 9.579   29.434  22.490 1.00 52.90  ? 201 ILE A CA  1 
ATOM   1452 C C   . ILE A 1 193 ? 8.618   29.254  21.318 1.00 50.53  ? 201 ILE A C   1 
ATOM   1453 O O   . ILE A 1 193 ? 8.552   28.172  20.747 1.00 52.03  ? 201 ILE A O   1 
ATOM   1454 C CB  . ILE A 1 193 ? 11.034  29.505  22.003 1.00 56.18  ? 201 ILE A CB  1 
ATOM   1455 C CG1 . ILE A 1 193 ? 12.033  29.484  23.154 1.00 59.34  ? 201 ILE A CG1 1 
ATOM   1456 C CG2 . ILE A 1 193 ? 11.222  30.737  21.127 1.00 59.32  ? 201 ILE A CG2 1 
ATOM   1457 C CD1 . ILE A 1 193 ? 13.430  29.065  22.751 1.00 64.93  ? 201 ILE A CD1 1 
ATOM   1458 N N   . PHE A 1 194 ? 7.916   30.326  20.937 1.00 46.29  ? 202 PHE A N   1 
ATOM   1459 C CA  . PHE A 1 194 ? 7.067   30.289  19.758 1.00 47.92  ? 202 PHE A CA  1 
ATOM   1460 C C   . PHE A 1 194 ? 7.307   31.495  18.849 1.00 48.43  ? 202 PHE A C   1 
ATOM   1461 O O   . PHE A 1 194 ? 7.443   32.627  19.313 1.00 52.59  ? 202 PHE A O   1 
ATOM   1462 C CB  . PHE A 1 194 ? 5.580   30.279  20.107 1.00 51.85  ? 202 PHE A CB  1 
ATOM   1463 C CG  . PHE A 1 194 ? 5.109   29.161  21.025 1.00 54.94  ? 202 PHE A CG  1 
ATOM   1464 C CD1 . PHE A 1 194 ? 5.172   29.303  22.409 1.00 66.26  ? 202 PHE A CD1 1 
ATOM   1465 C CD2 . PHE A 1 194 ? 4.530   28.014  20.512 1.00 53.55  ? 202 PHE A CD2 1 
ATOM   1466 C CE1 . PHE A 1 194 ? 4.703   28.310  23.250 1.00 60.66  ? 202 PHE A CE1 1 
ATOM   1467 C CE2 . PHE A 1 194 ? 4.060   27.022  21.360 1.00 62.35  ? 202 PHE A CE2 1 
ATOM   1468 C CZ  . PHE A 1 194 ? 4.148   27.171  22.727 1.00 60.06  ? 202 PHE A CZ  1 
ATOM   1469 N N   . LYS A 1 195 ? 7.342   31.232  17.534 1.00 48.84  ? 203 LYS A N   1 
ATOM   1470 C CA  . LYS A 1 195 ? 7.057   32.247  16.534 1.00 50.05  ? 203 LYS A CA  1 
ATOM   1471 C C   . LYS A 1 195 ? 5.554   32.197  16.275 1.00 46.81  ? 203 LYS A C   1 
ATOM   1472 O O   . LYS A 1 195 ? 5.025   31.123  16.017 1.00 55.43  ? 203 LYS A O   1 
ATOM   1473 C CB  . LYS A 1 195 ? 7.892   32.003  15.272 1.00 58.03  ? 203 LYS A CB  1 
ATOM   1474 C CG  . LYS A 1 195 ? 7.828   33.118  14.232 1.00 65.66  ? 203 LYS A CG  1 
ATOM   1475 C CD  . LYS A 1 195 ? 8.972   33.112  13.222 1.00 75.25  ? 203 LYS A CD  1 
ATOM   1476 C CE  . LYS A 1 195 ? 8.712   33.980  12.008 1.00 89.39  ? 203 LYS A CE  1 
ATOM   1477 N NZ  . LYS A 1 195 ? 9.659   33.754  10.905 1.00 91.54  ? 203 LYS A NZ  1 
ATOM   1478 N N   . ILE A 1 196 ? 4.863   33.333  16.393 1.00 43.37  ? 204 ILE A N   1 
ATOM   1479 C CA  . ILE A 1 196 ? 3.429   33.344  16.191 1.00 49.37  ? 204 ILE A CA  1 
ATOM   1480 C C   . ILE A 1 196 ? 3.035   34.415  15.185 1.00 50.40  ? 204 ILE A C   1 
ATOM   1481 O O   . ILE A 1 196 ? 3.292   35.600  15.410 1.00 45.21  ? 204 ILE A O   1 
ATOM   1482 C CB  . ILE A 1 196 ? 2.666   33.537  17.504 1.00 55.86  ? 204 ILE A CB  1 
ATOM   1483 C CG1 . ILE A 1 196 ? 2.741   32.293  18.365 1.00 63.25  ? 204 ILE A CG1 1 
ATOM   1484 C CG2 . ILE A 1 196 ? 1.212   33.910  17.220 1.00 59.25  ? 204 ILE A CG2 1 
ATOM   1485 C CD1 . ILE A 1 196 ? 2.358   32.532  19.816 1.00 63.85  ? 204 ILE A CD1 1 
ATOM   1486 N N   . HIS A 1 197 ? 2.349   33.953  14.125 1.00 57.30  ? 205 HIS A N   1 
ATOM   1487 C CA  . HIS A 1 197 ? 1.776   34.877  13.113 1.00 59.24  ? 205 HIS A CA  1 
ATOM   1488 C C   . HIS A 1 197 ? 0.252   34.798  13.227 1.00 51.74  ? 205 HIS A C   1 
ATOM   1489 O O   . HIS A 1 197 ? -0.299  33.712  12.966 1.00 51.79  ? 205 HIS A O   1 
ATOM   1490 C CB  . HIS A 1 197 ? 2.225   34.537  11.691 1.00 57.95  ? 205 HIS A CB  1 
ATOM   1491 C CG  . HIS A 1 197 ? 1.492   35.367  10.692 1.00 61.34  ? 205 HIS A CG  1 
ATOM   1492 N ND1 . HIS A 1 197 ? 1.369   36.732  10.835 1.00 67.29  ? 205 HIS A ND1 1 
ATOM   1493 C CD2 . HIS A 1 197 ? 0.825   35.048  9.577  1.00 68.11  ? 205 HIS A CD2 1 
ATOM   1494 C CE1 . HIS A 1 197 ? 0.660   37.215  9.826  1.00 59.78  ? 205 HIS A CE1 1 
ATOM   1495 N NE2 . HIS A 1 197 ? 0.320   36.209  9.049  1.00 69.50  ? 205 HIS A NE2 1 
ATOM   1496 N N   . LEU A 1 198 ? -0.405  35.899  13.572 1.00 46.48  ? 206 LEU A N   1 
ATOM   1497 C CA  . LEU A 1 198 ? -1.834  36.008  13.784 1.00 47.88  ? 206 LEU A CA  1 
ATOM   1498 C C   . LEU A 1 198 ? -2.480  36.547  12.517 1.00 52.70  ? 206 LEU A C   1 
ATOM   1499 O O   . LEU A 1 198 ? -2.213  37.687  12.123 1.00 51.28  ? 206 LEU A O   1 
ATOM   1500 C CB  . LEU A 1 198 ? -2.110  36.952  14.949 1.00 47.56  ? 206 LEU A CB  1 
ATOM   1501 C CG  . LEU A 1 198 ? -3.591  37.269  15.153 1.00 47.79  ? 206 LEU A CG  1 
ATOM   1502 C CD1 . LEU A 1 198 ? -4.313  35.994  15.577 1.00 44.08  ? 206 LEU A CD1 1 
ATOM   1503 C CD2 . LEU A 1 198 ? -3.812  38.403  16.131 1.00 48.87  ? 206 LEU A CD2 1 
ATOM   1504 N N   . ILE A 1 199 ? -3.343  35.713  11.917 1.00 57.90  ? 207 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 199 ? -3.934  35.977  10.608 1.00 56.92  ? 207 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 199 ? -5.273  36.689  10.810 1.00 60.83  ? 207 ILE A C   1 
ATOM   1507 O O   . ILE A 1 199 ? -5.493  37.733  10.210 1.00 59.44  ? 207 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 199 ? -4.058  34.672  9.794  1.00 54.41  ? 207 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 199 ? -2.688  34.138  9.371  1.00 56.79  ? 207 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 199 ? -4.963  34.841  8.580  1.00 53.34  ? 207 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 199 ? -2.658  32.649  9.098  1.00 52.60  ? 207 ILE A CD1 1 
ATOM   1512 N N   . SER A 1 200 ? -6.150  36.168  11.685 1.00 62.72  ? 208 SER A N   1 
ATOM   1513 C CA  . SER A 1 200 ? -7.466  36.770  11.868 1.00 59.59  ? 208 SER A CA  1 
ATOM   1514 C C   . SER A 1 200 ? -8.085  36.428  13.221 1.00 54.30  ? 208 SER A C   1 
ATOM   1515 O O   . SER A 1 200 ? -7.723  35.445  13.858 1.00 56.95  ? 208 SER A O   1 
ATOM   1516 C CB  . SER A 1 200 ? -8.399  36.351  10.763 1.00 57.18  ? 208 SER A CB  1 
ATOM   1517 O OG  . SER A 1 200 ? -8.651  34.955  10.836 1.00 63.32  ? 208 SER A OG  1 
ATOM   1518 N N   . VAL A 1 201 ? -9.105  37.217  13.559 1.00 53.21  ? 209 VAL A N   1 
ATOM   1519 C CA  . VAL A 1 201 ? -9.796  37.204  14.828 1.00 54.43  ? 209 VAL A CA  1 
ATOM   1520 C C   . VAL A 1 201 ? -11.300 37.185  14.558 1.00 66.39  ? 209 VAL A C   1 
ATOM   1521 O O   . VAL A 1 201 ? -11.777 37.958  13.741 1.00 73.09  ? 209 VAL A O   1 
ATOM   1522 C CB  . VAL A 1 201 ? -9.347  38.495  15.548 1.00 56.42  ? 209 VAL A CB  1 
ATOM   1523 C CG1 . VAL A 1 201 ? -10.082 38.717  16.872 1.00 57.74  ? 209 VAL A CG1 1 
ATOM   1524 C CG2 . VAL A 1 201 ? -7.839  38.532  15.777 1.00 55.12  ? 209 VAL A CG2 1 
ATOM   1525 N N   . LYS A 1 202 ? -12.070 36.368  15.286 1.00 83.00  ? 210 LYS A N   1 
ATOM   1526 C CA  . LYS A 1 202 ? -13.486 36.226  14.998 1.00 83.95  ? 210 LYS A CA  1 
ATOM   1527 C C   . LYS A 1 202 ? -14.293 37.397  15.564 1.00 92.18  ? 210 LYS A C   1 
ATOM   1528 O O   . LYS A 1 202 ? -15.239 37.818  14.905 1.00 118.86 ? 210 LYS A O   1 
ATOM   1529 C CB  . LYS A 1 202 ? -14.028 34.865  15.445 1.00 96.60  ? 210 LYS A CB  1 
ATOM   1530 C CG  . LYS A 1 202 ? -15.301 34.405  14.717 1.00 105.07 ? 210 LYS A CG  1 
ATOM   1531 C CD  . LYS A 1 202 ? -15.310 34.611  13.203 1.00 106.89 ? 210 LYS A CD  1 
ATOM   1532 C CE  . LYS A 1 202 ? -16.271 33.723  12.457 1.00 116.29 ? 210 LYS A CE  1 
ATOM   1533 N NZ  . LYS A 1 202 ? -17.685 33.943  12.782 1.00 122.29 ? 210 LYS A NZ  1 
ATOM   1534 N N   . LYS A 1 203 ? -13.958 37.932  16.752 1.00 79.76  ? 211 LYS A N   1 
ATOM   1535 C CA  . LYS A 1 203 ? -14.694 39.084  17.278 1.00 87.04  ? 211 LYS A CA  1 
ATOM   1536 C C   . LYS A 1 203 ? -13.745 40.186  17.759 1.00 92.35  ? 211 LYS A C   1 
ATOM   1537 O O   . LYS A 1 203 ? -12.560 40.163  17.462 1.00 97.72  ? 211 LYS A O   1 
ATOM   1538 C CB  . LYS A 1 203 ? -15.685 38.622  18.354 1.00 91.70  ? 211 LYS A CB  1 
ATOM   1539 C CG  . LYS A 1 203 ? -16.744 37.648  17.856 1.00 87.33  ? 211 LYS A CG  1 
ATOM   1540 C CD  . LYS A 1 203 ? -17.180 36.622  18.891 1.00 88.94  ? 211 LYS A CD  1 
ATOM   1541 C CE  . LYS A 1 203 ? -17.606 35.358  18.213 1.00 96.85  ? 211 LYS A CE  1 
ATOM   1542 N NZ  . LYS A 1 203 ? -17.830 34.263  19.162 1.00 100.56 ? 211 LYS A NZ  1 
ATOM   1543 N N   . SER A 1 204 ? -14.277 41.191  18.469 1.00 122.93 ? 212 SER A N   1 
ATOM   1544 C CA  . SER A 1 204 ? -13.463 42.261  19.039 1.00 135.49 ? 212 SER A CA  1 
ATOM   1545 C C   . SER A 1 204 ? -12.687 41.708  20.227 1.00 127.68 ? 212 SER A C   1 
ATOM   1546 O O   . SER A 1 204 ? -11.459 41.722  20.238 1.00 113.17 ? 212 SER A O   1 
ATOM   1547 C CB  . SER A 1 204 ? -14.294 43.469  19.473 1.00 145.24 ? 212 SER A CB  1 
ATOM   1548 O OG  . SER A 1 204 ? -14.395 44.461  18.457 1.00 144.66 ? 212 SER A OG  1 
ATOM   1549 N N   . SER A 1 205 ? -13.455 41.225  21.212 1.00 136.90 ? 213 SER A N   1 
ATOM   1550 C CA  . SER A 1 205 ? -12.942 40.667  22.452 1.00 128.65 ? 213 SER A CA  1 
ATOM   1551 C C   . SER A 1 205 ? -14.064 39.870  23.136 1.00 117.78 ? 213 SER A C   1 
ATOM   1552 O O   . SER A 1 205 ? -13.722 39.013  23.974 1.00 107.87 ? 213 SER A O   1 
ATOM   1553 C CB  . SER A 1 205 ? -12.371 41.742  23.349 1.00 123.92 ? 213 SER A CB  1 
ATOM   1554 O OG  . SER A 1 205 ? -13.032 42.983  23.143 1.00 130.25 ? 213 SER A OG  1 
ATOM   1555 O OXT . SER A 1 205 ? -15.244 40.108  22.769 1.00 124.21 ? 213 SER A OXT 1 
HETATM 1556 O O1  . MES B 2 .   ? -6.901  36.419  32.739 1.00 66.60  ? 301 MES A O1  1 
HETATM 1557 C C2  . MES B 2 .   ? -7.621  37.358  31.961 1.00 54.89  ? 301 MES A C2  1 
HETATM 1558 C C3  . MES B 2 .   ? -6.715  38.457  31.475 1.00 44.33  ? 301 MES A C3  1 
HETATM 1559 N N4  . MES B 2 .   ? -5.305  38.166  31.872 1.00 41.85  ? 301 MES A N4  1 
HETATM 1560 C C5  . MES B 2 .   ? -4.928  36.795  31.413 1.00 40.26  ? 301 MES A C5  1 
HETATM 1561 C C6  . MES B 2 .   ? -5.918  35.790  31.936 1.00 42.59  ? 301 MES A C6  1 
HETATM 1562 C C7  . MES B 2 .   ? -4.364  39.201  31.335 1.00 45.94  ? 301 MES A C7  1 
HETATM 1563 C C8  . MES B 2 .   ? -3.590  39.915  32.423 1.00 55.10  ? 301 MES A C8  1 
HETATM 1564 S S   . MES B 2 .   ? -2.101  39.068  32.886 1.00 41.80  ? 301 MES A S   1 
HETATM 1565 O O1S . MES B 2 .   ? -1.198  40.081  33.337 1.00 38.43  ? 301 MES A O1S 1 
HETATM 1566 O O2S . MES B 2 .   ? -1.639  38.416  31.709 1.00 33.19  ? 301 MES A O2S 1 
HETATM 1567 O O3S . MES B 2 .   ? -2.464  38.144  33.913 1.00 53.47  ? 301 MES A O3S 1 
HETATM 1568 C C1  . PEG C 3 .   ? 12.871  42.577  34.061 1.00 75.71  ? 302 PEG A C1  1 
HETATM 1569 O O1  . PEG C 3 .   ? 14.246  42.752  33.764 1.00 72.15  ? 302 PEG A O1  1 
HETATM 1570 C C2  . PEG C 3 .   ? 12.626  41.346  34.874 1.00 79.91  ? 302 PEG A C2  1 
HETATM 1571 O O2  . PEG C 3 .   ? 12.825  40.189  34.066 1.00 81.64  ? 302 PEG A O2  1 
HETATM 1572 C C3  . PEG C 3 .   ? 13.520  39.128  34.719 1.00 70.35  ? 302 PEG A C3  1 
HETATM 1573 C C4  . PEG C 3 .   ? 13.016  37.809  34.203 1.00 69.12  ? 302 PEG A C4  1 
HETATM 1574 O O4  . PEG C 3 .   ? 14.015  36.790  34.182 1.00 66.81  ? 302 PEG A O4  1 
HETATM 1575 C C1  . PEG D 3 .   ? 6.181   46.585  21.126 1.00 93.93  ? 303 PEG A C1  1 
HETATM 1576 O O1  . PEG D 3 .   ? 5.919   47.959  21.282 1.00 111.97 ? 303 PEG A O1  1 
HETATM 1577 C C2  . PEG D 3 .   ? 4.934   45.741  21.188 1.00 97.02  ? 303 PEG A C2  1 
HETATM 1578 O O2  . PEG D 3 .   ? 3.823   46.360  20.539 1.00 85.53  ? 303 PEG A O2  1 
HETATM 1579 C C3  . PEG D 3 .   ? 2.800   46.790  21.433 1.00 84.16  ? 303 PEG A C3  1 
HETATM 1580 C C4  . PEG D 3 .   ? 2.341   45.670  22.329 1.00 78.08  ? 303 PEG A C4  1 
HETATM 1581 O O4  . PEG D 3 .   ? 2.585   45.933  23.709 1.00 74.13  ? 303 PEG A O4  1 
HETATM 1582 C C1  . PEG E 3 .   ? -1.654  47.057  22.672 1.00 86.77  ? 304 PEG A C1  1 
HETATM 1583 O O1  . PEG E 3 .   ? -0.403  47.493  22.176 1.00 87.64  ? 304 PEG A O1  1 
HETATM 1584 C C2  . PEG E 3 .   ? -1.686  46.889  24.158 1.00 79.55  ? 304 PEG A C2  1 
HETATM 1585 O O2  . PEG E 3 .   ? -2.936  47.351  24.667 1.00 83.47  ? 304 PEG A O2  1 
HETATM 1586 C C3  . PEG E 3 .   ? -4.020  46.437  24.514 1.00 84.02  ? 304 PEG A C3  1 
HETATM 1587 C C4  . PEG E 3 .   ? -5.207  47.159  23.933 1.00 89.58  ? 304 PEG A C4  1 
HETATM 1588 O O4  . PEG E 3 .   ? -6.378  47.039  24.705 1.00 86.90  ? 304 PEG A O4  1 
HETATM 1589 O O   . HOH F 4 .   ? 0.509   -21.973 39.431 1.00 68.56  ? 401 HOH A O   1 
HETATM 1590 O O   . HOH F 4 .   ? 8.791   -0.060  19.149 1.00 64.63  ? 402 HOH A O   1 
HETATM 1591 O O   . HOH F 4 .   ? 13.029  -1.668  47.773 1.00 88.54  ? 403 HOH A O   1 
HETATM 1592 O O   . HOH F 4 .   ? 14.756  34.799  16.475 1.00 59.50  ? 404 HOH A O   1 
HETATM 1593 O O   . HOH F 4 .   ? 12.579  6.964   31.533 1.00 76.48  ? 405 HOH A O   1 
HETATM 1594 O O   . HOH F 4 .   ? 9.841   35.776  9.682  1.00 52.35  ? 406 HOH A O   1 
HETATM 1595 O O   . HOH F 4 .   ? 3.284   39.790  10.258 1.00 45.01  ? 407 HOH A O   1 
HETATM 1596 O O   . HOH F 4 .   ? -13.120 45.831  16.968 1.00 66.80  ? 408 HOH A O   1 
HETATM 1597 O O   . HOH F 4 .   ? -5.726  49.662  20.151 1.00 60.59  ? 409 HOH A O   1 
HETATM 1598 O O   . HOH F 4 .   ? 15.317  18.887  23.534 1.00 65.13  ? 410 HOH A O   1 
HETATM 1599 O O   . HOH F 4 .   ? 10.369  43.611  19.905 1.00 45.73  ? 411 HOH A O   1 
HETATM 1600 O O   . HOH F 4 .   ? -1.139  47.790  19.787 1.00 68.48  ? 412 HOH A O   1 
HETATM 1601 O O   . HOH F 4 .   ? 9.529   11.639  32.367 1.00 69.54  ? 413 HOH A O   1 
HETATM 1602 O O   . HOH F 4 .   ? -2.119  22.046  2.138  1.00 76.60  ? 414 HOH A O   1 
HETATM 1603 O O   . HOH F 4 .   ? -6.804  42.297  23.689 1.00 52.57  ? 415 HOH A O   1 
HETATM 1604 O O   . HOH F 4 .   ? 25.527  0.687   28.811 1.00 61.17  ? 416 HOH A O   1 
HETATM 1605 O O   . HOH F 4 .   ? -4.704  47.219  16.368 1.00 64.51  ? 417 HOH A O   1 
HETATM 1606 O O   . HOH F 4 .   ? 11.179  -24.753 35.376 1.00 63.28  ? 418 HOH A O   1 
HETATM 1607 O O   . HOH F 4 .   ? 12.432  -26.537 34.126 1.00 77.31  ? 419 HOH A O   1 
HETATM 1608 O O   . HOH F 4 .   ? -17.217 39.623  20.979 1.00 75.82  ? 420 HOH A O   1 
HETATM 1609 O O   . HOH F 4 .   ? 23.398  33.804  22.902 1.00 90.54  ? 421 HOH A O   1 
HETATM 1610 O O   . HOH F 4 .   ? 18.439  33.728  24.532 1.00 51.53  ? 422 HOH A O   1 
HETATM 1611 O O   . HOH F 4 .   ? -10.613 43.946  22.041 1.00 74.39  ? 423 HOH A O   1 
HETATM 1612 O O   . HOH F 4 .   ? 11.878  13.911  28.467 1.00 59.96  ? 424 HOH A O   1 
HETATM 1613 O O   . HOH F 4 .   ? 13.957  -0.793  17.318 1.00 81.53  ? 425 HOH A O   1 
HETATM 1614 O O   . HOH F 4 .   ? 18.887  18.777  39.719 1.00 66.16  ? 426 HOH A O   1 
HETATM 1615 O O   . HOH F 4 .   ? 1.525   47.733  9.967  1.00 49.51  ? 427 HOH A O   1 
HETATM 1616 O O   . HOH F 4 .   ? 8.691   8.940   31.492 1.00 84.65  ? 428 HOH A O   1 
HETATM 1617 O O   . HOH F 4 .   ? 9.047   13.564  30.600 1.00 62.25  ? 429 HOH A O   1 
HETATM 1618 O O   . HOH F 4 .   ? 21.538  -8.693  32.988 1.00 73.96  ? 430 HOH A O   1 
HETATM 1619 O O   . HOH F 4 .   ? -20.399 33.283  14.218 1.00 76.27  ? 431 HOH A O   1 
HETATM 1620 O O   . HOH F 4 .   ? 14.594  38.962  14.455 1.00 76.20  ? 432 HOH A O   1 
HETATM 1621 O O   . HOH F 4 .   ? 10.116  29.376  34.397 1.00 51.52  ? 433 HOH A O   1 
HETATM 1622 O O   . HOH F 4 .   ? 7.398   36.073  9.173  1.00 58.10  ? 434 HOH A O   1 
HETATM 1623 O O   . HOH F 4 .   ? 8.822   30.358  9.357  1.00 59.71  ? 435 HOH A O   1 
HETATM 1624 O O   . HOH F 4 .   ? 21.085  32.948  24.947 1.00 59.42  ? 436 HOH A O   1 
HETATM 1625 O O   . HOH F 4 .   ? 11.109  -18.409 44.739 1.00 62.90  ? 437 HOH A O   1 
# 
