data_9JQ0
# 
_entry.id   9JQ0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9JQ0         pdb_00009jq0 10.2210/pdb9jq0/pdb 
WWPDB D_1300051954 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_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                        9JQ0 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              zhoujw1982@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Jingwen 
_pdbx_contact_author.name_last          Zhou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3949-3733 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, X.L.' 1 0009-0009-0407-8749 
'Linghu, K.' 2 0009-0004-4432-5154 
'Xu, K.J.'   3 0009-0004-5809-3606 
# 
_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 E104G mutant of Acid phosphatase KpAP at 1.93 A resolution' 
_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 'Wang, X.L.' 1 0009-0009-0407-8749 
primary 'Linghu, K.' 2 0009-0004-4432-5154 
primary 'Xu, K.J.'   3 0009-0004-5809-3606 
primary 'Zhou, J.W.' 4 0000-0002-3949-3733 
# 
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 'Acid phosphatase' 25309.475 1   3.1.3.2 E122G ? ? 
2 non-polymer syn 'PHOSPHATE ION'    94.971    7   ?       ?     ? ? 
3 non-polymer syn GLYCEROL           92.094    3   ?       ?     ? ? 
4 water       nat water              18.015    143 ?       ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MALVPPGNDVTTKPDLYYLTNAQAIDSLALLPPPPAVGSIAFLNDQAMYEQGRLLRNTERGKLAAEDANLSAGGVANAFS
SAFGSPITEKDAPQLHKLLTNMIGDAGDLATRGAKEKYMRIRPFAFYGVSTCNTTEQDKLSKNGSYPSGHTSIGWATALV
LAEINPQRQNEILKRGYELGESRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFAKTQKHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MALVPPGNDVTTKPDLYYLTNAQAIDSLALLPPPPAVGSIAFLNDQAMYEQGRLLRNTERGKLAAEDANLSAGGVANAFS
SAFGSPITEKDAPQLHKLLTNMIGDAGDLATRGAKEKYMRIRPFAFYGVSTCNTTEQDKLSKNGSYPSGHTSIGWATALV
LAEINPQRQNEILKRGYELGESRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFAKTQKHHH
;
_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 'PHOSPHATE ION' PO4 
3 GLYCEROL        GOL 
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   LEU n 
1 4   VAL n 
1 5   PRO n 
1 6   PRO n 
1 7   GLY n 
1 8   ASN n 
1 9   ASP n 
1 10  VAL n 
1 11  THR n 
1 12  THR n 
1 13  LYS n 
1 14  PRO n 
1 15  ASP n 
1 16  LEU n 
1 17  TYR n 
1 18  TYR n 
1 19  LEU n 
1 20  THR n 
1 21  ASN n 
1 22  ALA n 
1 23  GLN n 
1 24  ALA n 
1 25  ILE n 
1 26  ASP n 
1 27  SER n 
1 28  LEU n 
1 29  ALA n 
1 30  LEU n 
1 31  LEU n 
1 32  PRO n 
1 33  PRO n 
1 34  PRO n 
1 35  PRO n 
1 36  ALA n 
1 37  VAL n 
1 38  GLY n 
1 39  SER n 
1 40  ILE n 
1 41  ALA n 
1 42  PHE n 
1 43  LEU n 
1 44  ASN n 
1 45  ASP n 
1 46  GLN n 
1 47  ALA n 
1 48  MET n 
1 49  TYR n 
1 50  GLU n 
1 51  GLN n 
1 52  GLY n 
1 53  ARG n 
1 54  LEU n 
1 55  LEU n 
1 56  ARG n 
1 57  ASN n 
1 58  THR n 
1 59  GLU n 
1 60  ARG n 
1 61  GLY n 
1 62  LYS n 
1 63  LEU n 
1 64  ALA n 
1 65  ALA n 
1 66  GLU n 
1 67  ASP n 
1 68  ALA n 
1 69  ASN n 
1 70  LEU n 
1 71  SER n 
1 72  ALA n 
1 73  GLY n 
1 74  GLY n 
1 75  VAL n 
1 76  ALA n 
1 77  ASN n 
1 78  ALA n 
1 79  PHE n 
1 80  SER n 
1 81  SER n 
1 82  ALA n 
1 83  PHE n 
1 84  GLY n 
1 85  SER n 
1 86  PRO n 
1 87  ILE n 
1 88  THR n 
1 89  GLU n 
1 90  LYS n 
1 91  ASP n 
1 92  ALA n 
1 93  PRO n 
1 94  GLN n 
1 95  LEU n 
1 96  HIS n 
1 97  LYS n 
1 98  LEU n 
1 99  LEU n 
1 100 THR n 
1 101 ASN n 
1 102 MET n 
1 103 ILE n 
1 104 GLY n 
1 105 ASP n 
1 106 ALA n 
1 107 GLY n 
1 108 ASP n 
1 109 LEU n 
1 110 ALA n 
1 111 THR n 
1 112 ARG n 
1 113 GLY n 
1 114 ALA n 
1 115 LYS n 
1 116 GLU n 
1 117 LYS n 
1 118 TYR n 
1 119 MET n 
1 120 ARG n 
1 121 ILE n 
1 122 ARG n 
1 123 PRO n 
1 124 PHE n 
1 125 ALA n 
1 126 PHE n 
1 127 TYR n 
1 128 GLY n 
1 129 VAL n 
1 130 SER n 
1 131 THR n 
1 132 CYS n 
1 133 ASN n 
1 134 THR n 
1 135 THR n 
1 136 GLU n 
1 137 GLN n 
1 138 ASP n 
1 139 LYS n 
1 140 LEU n 
1 141 SER n 
1 142 LYS n 
1 143 ASN n 
1 144 GLY n 
1 145 SER n 
1 146 TYR n 
1 147 PRO n 
1 148 SER n 
1 149 GLY n 
1 150 HIS n 
1 151 THR n 
1 152 SER n 
1 153 ILE n 
1 154 GLY n 
1 155 TRP n 
1 156 ALA n 
1 157 THR n 
1 158 ALA n 
1 159 LEU n 
1 160 VAL n 
1 161 LEU n 
1 162 ALA n 
1 163 GLU n 
1 164 ILE n 
1 165 ASN n 
1 166 PRO n 
1 167 GLN n 
1 168 ARG n 
1 169 GLN n 
1 170 ASN n 
1 171 GLU n 
1 172 ILE n 
1 173 LEU n 
1 174 LYS n 
1 175 ARG n 
1 176 GLY n 
1 177 TYR n 
1 178 GLU n 
1 179 LEU n 
1 180 GLY n 
1 181 GLU n 
1 182 SER n 
1 183 ARG n 
1 184 VAL n 
1 185 ILE n 
1 186 CYS n 
1 187 GLY n 
1 188 TYR n 
1 189 HIS n 
1 190 TRP n 
1 191 GLN n 
1 192 SER n 
1 193 ASP n 
1 194 VAL n 
1 195 ASP n 
1 196 ALA n 
1 197 ALA n 
1 198 ARG n 
1 199 ILE n 
1 200 VAL n 
1 201 GLY n 
1 202 SER n 
1 203 ALA n 
1 204 VAL n 
1 205 VAL n 
1 206 ALA n 
1 207 THR n 
1 208 LEU n 
1 209 HIS n 
1 210 THR n 
1 211 ASN n 
1 212 PRO n 
1 213 ALA n 
1 214 PHE n 
1 215 GLN n 
1 216 GLN n 
1 217 GLN n 
1 218 LEU n 
1 219 GLN n 
1 220 LYS n 
1 221 ALA n 
1 222 LYS n 
1 223 ASP n 
1 224 GLU n 
1 225 PHE n 
1 226 ALA n 
1 227 LYS n 
1 228 THR n 
1 229 GLN n 
1 230 LYS n 
1 231 HIS n 
1 232 HIS n 
1 233 HIS 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                   233 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KPK_3238 
_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      'Klebsiella pneumoniae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     507522 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                               'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  THR 12  12  12  THR THR A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 ARG 120 120 120 ARG ARG A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 CYS 132 132 132 CYS CYS A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 HIS 150 150 150 HIS HIS A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 TRP 155 155 155 TRP TRP A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 CYS 186 186 186 CYS CYS A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 HIS 189 189 189 HIS HIS A . n 
A 1 190 TRP 190 190 190 TRP TRP A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 GLN 215 215 215 GLN GLN A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 HIS 233 233 233 HIS HIS 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 PO4 1   301 1   PO4 PO4 A . 
C 2 PO4 1   302 2   PO4 PO4 A . 
D 2 PO4 1   303 3   PO4 PO4 A . 
E 2 PO4 1   304 4   PO4 PO4 A . 
F 2 PO4 1   305 5   PO4 PO4 A . 
G 2 PO4 1   306 6   PO4 PO4 A . 
H 2 PO4 1   307 7   PO4 PO4 A . 
I 3 GOL 1   308 1   GOL GOL A . 
J 3 GOL 1   309 2   GOL GOL A . 
K 3 GOL 1   310 3   GOL GOL A . 
L 4 HOH 1   401 102 HOH HOH A . 
L 4 HOH 2   402 41  HOH HOH A . 
L 4 HOH 3   403 35  HOH HOH A . 
L 4 HOH 4   404 40  HOH HOH A . 
L 4 HOH 5   405 22  HOH HOH A . 
L 4 HOH 6   406 13  HOH HOH A . 
L 4 HOH 7   407 31  HOH HOH A . 
L 4 HOH 8   408 30  HOH HOH A . 
L 4 HOH 9   409 74  HOH HOH A . 
L 4 HOH 10  410 4   HOH HOH A . 
L 4 HOH 11  411 61  HOH HOH A . 
L 4 HOH 12  412 2   HOH HOH A . 
L 4 HOH 13  413 134 HOH HOH A . 
L 4 HOH 14  414 29  HOH HOH A . 
L 4 HOH 15  415 49  HOH HOH A . 
L 4 HOH 16  416 79  HOH HOH A . 
L 4 HOH 17  417 98  HOH HOH A . 
L 4 HOH 18  418 60  HOH HOH A . 
L 4 HOH 19  419 115 HOH HOH A . 
L 4 HOH 20  420 123 HOH HOH A . 
L 4 HOH 21  421 59  HOH HOH A . 
L 4 HOH 22  422 125 HOH HOH A . 
L 4 HOH 23  423 94  HOH HOH A . 
L 4 HOH 24  424 92  HOH HOH A . 
L 4 HOH 25  425 69  HOH HOH A . 
L 4 HOH 26  426 17  HOH HOH A . 
L 4 HOH 27  427 57  HOH HOH A . 
L 4 HOH 28  428 71  HOH HOH A . 
L 4 HOH 29  429 114 HOH HOH A . 
L 4 HOH 30  430 129 HOH HOH A . 
L 4 HOH 31  431 101 HOH HOH A . 
L 4 HOH 32  432 95  HOH HOH A . 
L 4 HOH 33  433 51  HOH HOH A . 
L 4 HOH 34  434 16  HOH HOH A . 
L 4 HOH 35  435 67  HOH HOH A . 
L 4 HOH 36  436 68  HOH HOH A . 
L 4 HOH 37  437 9   HOH HOH A . 
L 4 HOH 38  438 34  HOH HOH A . 
L 4 HOH 39  439 73  HOH HOH A . 
L 4 HOH 40  440 15  HOH HOH A . 
L 4 HOH 41  441 26  HOH HOH A . 
L 4 HOH 42  442 20  HOH HOH A . 
L 4 HOH 43  443 14  HOH HOH A . 
L 4 HOH 44  444 80  HOH HOH A . 
L 4 HOH 45  445 5   HOH HOH A . 
L 4 HOH 46  446 77  HOH HOH A . 
L 4 HOH 47  447 63  HOH HOH A . 
L 4 HOH 48  448 38  HOH HOH A . 
L 4 HOH 49  449 10  HOH HOH A . 
L 4 HOH 50  450 46  HOH HOH A . 
L 4 HOH 51  451 21  HOH HOH A . 
L 4 HOH 52  452 1   HOH HOH A . 
L 4 HOH 53  453 48  HOH HOH A . 
L 4 HOH 54  454 82  HOH HOH A . 
L 4 HOH 55  455 45  HOH HOH A . 
L 4 HOH 56  456 18  HOH HOH A . 
L 4 HOH 57  457 28  HOH HOH A . 
L 4 HOH 58  458 6   HOH HOH A . 
L 4 HOH 59  459 103 HOH HOH A . 
L 4 HOH 60  460 7   HOH HOH A . 
L 4 HOH 61  461 44  HOH HOH A . 
L 4 HOH 62  462 70  HOH HOH A . 
L 4 HOH 63  463 78  HOH HOH A . 
L 4 HOH 64  464 116 HOH HOH A . 
L 4 HOH 65  465 50  HOH HOH A . 
L 4 HOH 66  466 52  HOH HOH A . 
L 4 HOH 67  467 32  HOH HOH A . 
L 4 HOH 68  468 66  HOH HOH A . 
L 4 HOH 69  469 107 HOH HOH A . 
L 4 HOH 70  470 23  HOH HOH A . 
L 4 HOH 71  471 27  HOH HOH A . 
L 4 HOH 72  472 89  HOH HOH A . 
L 4 HOH 73  473 143 HOH HOH A . 
L 4 HOH 74  474 8   HOH HOH A . 
L 4 HOH 75  475 93  HOH HOH A . 
L 4 HOH 76  476 118 HOH HOH A . 
L 4 HOH 77  477 33  HOH HOH A . 
L 4 HOH 78  478 113 HOH HOH A . 
L 4 HOH 79  479 109 HOH HOH A . 
L 4 HOH 80  480 56  HOH HOH A . 
L 4 HOH 81  481 91  HOH HOH A . 
L 4 HOH 82  482 130 HOH HOH A . 
L 4 HOH 83  483 3   HOH HOH A . 
L 4 HOH 84  484 43  HOH HOH A . 
L 4 HOH 85  485 135 HOH HOH A . 
L 4 HOH 86  486 53  HOH HOH A . 
L 4 HOH 87  487 86  HOH HOH A . 
L 4 HOH 88  488 47  HOH HOH A . 
L 4 HOH 89  489 137 HOH HOH A . 
L 4 HOH 90  490 139 HOH HOH A . 
L 4 HOH 91  491 96  HOH HOH A . 
L 4 HOH 92  492 106 HOH HOH A . 
L 4 HOH 93  493 62  HOH HOH A . 
L 4 HOH 94  494 105 HOH HOH A . 
L 4 HOH 95  495 111 HOH HOH A . 
L 4 HOH 96  496 54  HOH HOH A . 
L 4 HOH 97  497 99  HOH HOH A . 
L 4 HOH 98  498 58  HOH HOH A . 
L 4 HOH 99  499 76  HOH HOH A . 
L 4 HOH 100 500 42  HOH HOH A . 
L 4 HOH 101 501 83  HOH HOH A . 
L 4 HOH 102 502 85  HOH HOH A . 
L 4 HOH 103 503 141 HOH HOH A . 
L 4 HOH 104 504 126 HOH HOH A . 
L 4 HOH 105 505 81  HOH HOH A . 
L 4 HOH 106 506 120 HOH HOH A . 
L 4 HOH 107 507 138 HOH HOH A . 
L 4 HOH 108 508 36  HOH HOH A . 
L 4 HOH 109 509 87  HOH HOH A . 
L 4 HOH 110 510 11  HOH HOH A . 
L 4 HOH 111 511 84  HOH HOH A . 
L 4 HOH 112 512 75  HOH HOH A . 
L 4 HOH 113 513 136 HOH HOH A . 
L 4 HOH 114 514 110 HOH HOH A . 
L 4 HOH 115 515 88  HOH HOH A . 
L 4 HOH 116 516 39  HOH HOH A . 
L 4 HOH 117 517 142 HOH HOH A . 
L 4 HOH 118 518 124 HOH HOH A . 
L 4 HOH 119 519 19  HOH HOH A . 
L 4 HOH 120 520 55  HOH HOH A . 
L 4 HOH 121 521 64  HOH HOH A . 
L 4 HOH 122 522 132 HOH HOH A . 
L 4 HOH 123 523 128 HOH HOH A . 
L 4 HOH 124 524 121 HOH HOH A . 
L 4 HOH 125 525 97  HOH HOH A . 
L 4 HOH 126 526 122 HOH HOH A . 
L 4 HOH 127 527 140 HOH HOH A . 
L 4 HOH 128 528 112 HOH HOH A . 
L 4 HOH 129 529 65  HOH HOH A . 
L 4 HOH 130 530 131 HOH HOH A . 
L 4 HOH 131 531 12  HOH HOH A . 
L 4 HOH 132 532 119 HOH HOH A . 
L 4 HOH 133 533 90  HOH HOH A . 
L 4 HOH 134 534 24  HOH HOH A . 
L 4 HOH 135 535 100 HOH HOH A . 
L 4 HOH 136 536 133 HOH HOH A . 
L 4 HOH 137 537 37  HOH HOH A . 
L 4 HOH 138 538 25  HOH HOH A . 
L 4 HOH 139 539 108 HOH HOH A . 
L 4 HOH 140 540 117 HOH HOH A . 
L 4 HOH 141 541 104 HOH HOH A . 
L 4 HOH 142 542 72  HOH HOH A . 
L 4 HOH 143 543 127 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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21     1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0123 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21     4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.7.0    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JQ0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     124.710 
_cell.length_a_esd                 ? 
_cell.length_b                     124.710 
_cell.length_b_esd                 ? 
_cell.length_c                     97.280 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9JQ0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                182 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63 2 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                   9JQ0 
_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             4.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.49 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Ammonium acetate, 0.1 M BIS-TRIS, 45% (v/v) (+/-)-2-Methyl-2,4-pentanediol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            300 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-17 
_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                    Si111 
_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   0.987 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JQ0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               47.21 
_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                                     34115 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                30.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.192 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.93 
_reflns_shell.d_res_low                                     1.97 
_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                             2242 
_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                               0.503 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.800 
_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]                            0.77 
_refine.aniso_B[1][2]                            0.39 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.77 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.51 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.159 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_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                                 9JQ0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.93 
_refine.ls_d_res_low                             47.21 
_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                     32342 
_refine.ls_number_reflns_R_free                  1765 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17917 
_refine.ls_R_factor_R_free                       0.19772 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17817 
_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                       0.100 
_refine.pdbx_overall_ESU_R_Free                  0.097 
_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                             4.630 
_refine.overall_SU_ML                            0.066 
_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                       1.93 
_refine_hist.d_res_low                        47.21 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               1968 
_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        1772 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_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' ? 0.004  0.019  1898 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1770 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.589  1.975  2587 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.684  3.000  4084 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 4.778  5.000  244  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.916 24.651 86   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.744 15.000 305  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.639 15.000 11   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.050  0.200  284  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.021  2163 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  416  ? 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' ? 0.430  2.215  941  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.431  2.213  940  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 0.791  3.317  1178 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.790  3.319  1179 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.493  2.473  957  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.492  2.473  957  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.705  3.669  1403 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.456  29.686 2341 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.001  28.398 2274 ? 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                       1.93 
_refine_ls_shell.d_res_low                        1.978 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             117 
_refine_ls_shell.number_reflns_R_work             2357 
_refine_ls_shell.percent_reflns_obs               99.84 
_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                  0.273 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.257 
# 
_struct.entry_id                     9JQ0 
_struct.title                        'Acid phosphatase KpAP mutant - E104G' 
_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        9JQ0 
_struct_keywords.text            'Acid phosphatase, E104G mutant, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    B5XS64_KLEP3 
_struct_ref.pdbx_db_accession          B5XS64 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ALVPPGNDVTTKPDLYYLTNAQAIDSLALLPPPPAVGSIAFLNDQAMYEQGRLLRNTERGKLAAEDANLSAGGVANAFSS
AFGSPITEKDAPQLHKLLTNMIEDAGDLATRGAKEKYMRIRPFAFYGVSTCNTTEQDKLSKNGSYPSGHTSIGWATALVL
AEINPQRQNEILKRGYELGESRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFAKTQK
;
_struct_ref.pdbx_align_begin           20 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JQ0 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 230 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             B5XS64 
_struct_ref_seq.db_align_beg                  20 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  248 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       230 
# 
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 9JQ0 MET A 1   ? UNP B5XS64 ?   ?   'initiating methionine' 1   1 
1 9JQ0 GLY A 104 ? UNP B5XS64 GLU 122 'engineered mutation'   104 2 
1 9JQ0 HIS A 231 ? UNP B5XS64 ?   ?   'expression tag'        231 3 
1 9JQ0 HIS A 232 ? UNP B5XS64 ?   ?   'expression tag'        232 4 
1 9JQ0 HIS A 233 ? UNP B5XS64 ?   ?   'expression tag'        233 5 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA hexameric 6 
2 author_and_software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 27120 ? 
1 MORE         -442  ? 
1 'SSA (A^2)'  49300 ? 
2 'ABSA (A^2)' 7200  ? 
2 MORE         -115  ? 
2 'SSA (A^2)'  18270 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3,4,5,6 A,B,C,D,E,F,G,H,I,J,K,L 
2 1,6         A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z           1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 2_545  -y,x-y-1,z      -0.5000000000 -0.8660254038 0.0000000000 62.3550000000  0.8660254038  
-0.5000000000 0.0000000000 -108.0020281060 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
3 'crystal symmetry operation' 3_655  -x+y+1,-x,z     -0.5000000000 0.8660254038  0.0000000000 124.7100000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000   
4 'crystal symmetry operation' 10_554 -y,-x,-z-1/2    0.5000000000  -0.8660254038 0.0000000000 0.0000000000   -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 -48.6400000000 
5 'crystal symmetry operation' 11_654 -x+y+1,y,-z-1/2 -1.0000000000 0.0000000000  0.0000000000 124.7100000000 0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 -1.0000000000 -48.6400000000 
6 'crystal symmetry operation' 12_544 x,x-y-1,-z-1/2  0.5000000000  0.8660254038  0.0000000000 62.3550000000  0.8660254038  
-0.5000000000 0.0000000000 -108.0020281060 0.0000000000 0.0000000000 -1.0000000000 -48.6400000000 
# 
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 THR A 20  ? ALA A 24  ? THR A 20  ALA A 24  5 ? 5  
HELX_P HELX_P2  AA2 ASP A 26  ? LEU A 31  ? ASP A 26  LEU A 31  1 ? 6  
HELX_P HELX_P3  AA3 SER A 39  ? ARG A 56  ? SER A 39  ARG A 56  1 ? 18 
HELX_P HELX_P4  AA4 THR A 58  ? ASN A 69  ? THR A 58  ASN A 69  1 ? 12 
HELX_P HELX_P5  AA5 SER A 71  ? GLY A 73  ? SER A 71  GLY A 73  5 ? 3  
HELX_P HELX_P6  AA6 GLY A 74  ? PHE A 79  ? GLY A 74  PHE A 79  1 ? 6  
HELX_P HELX_P7  AA7 PHE A 79  ? GLY A 84  ? PHE A 79  GLY A 84  1 ? 6  
HELX_P HELX_P8  AA8 ALA A 92  ? ASN A 101 ? ALA A 92  ASN A 101 1 ? 10 
HELX_P HELX_P9  AA9 MET A 102 ? ASP A 108 ? MET A 102 ASP A 108 1 ? 7  
HELX_P HELX_P10 AB1 THR A 111 ? MET A 119 ? THR A 111 MET A 119 1 ? 9  
HELX_P HELX_P11 AB2 ARG A 122 ? GLY A 128 ? ARG A 122 GLY A 128 1 ? 7  
HELX_P HELX_P12 AB3 SER A 148 ? ASN A 165 ? SER A 148 ASN A 165 1 ? 18 
HELX_P HELX_P13 AB4 ARG A 168 ? CYS A 186 ? ARG A 168 CYS A 186 1 ? 19 
HELX_P HELX_P14 AB5 TRP A 190 ? HIS A 209 ? TRP A 190 HIS A 209 1 ? 20 
HELX_P HELX_P15 AB6 ASN A 211 ? HIS A 233 ? ASN A 211 HIS A 233 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            132 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            186 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             132 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             186 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.048 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       132 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      186 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        132 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       186 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           146 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            146 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    147 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     147 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -8.82 
# 
_pdbx_entry_details.entry_id                   9JQ0 
_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   Y 
# 
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 ASN A 57  ? ? -96.88 38.95 
2 1 MET A 119 ? ? 38.95  49.28 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     517 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   L 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 41.8973 -68.5088 -12.3537 0.2126 ? -0.0125 ? -0.0367 ? 0.0781 ? 0.0396 ? 0.2148 ? 12.3029 ? 1.5242 
? -2.9641 ? 3.3092  ? -0.9565 ? 6.0157 ? -0.1209 ? 0.2630  ? -0.6881 ? -0.1706 ? 0.0061  ? -0.4886 ? 0.5778  ? 0.3682  ? 0.1148  ? 
2 'X-RAY DIFFRACTION' ? refined 46.7532 -51.4764 -15.8027 0.0282 ? -0.0162 ? -0.0092 ? 0.0135 ? 0.0139 ? 0.0311 ? 1.8200  ? 1.2789 
? -0.1196 ? 1.3369  ? -0.0648 ? 0.5958 ? 0.0748  ? -0.0128 ? -0.0780 ? 0.1051  ? -0.0090 ? 0.0254  ? 0.0957  ? -0.0770 ? -0.0658 ? 
3 'X-RAY DIFFRACTION' ? refined 33.2892 -48.9365 -8.5488  0.0561 ? -0.0427 ? 0.0071  ? 0.0816 ? 0.0163 ? 0.0167 ? 2.1850  ? 0.1369 
? -0.2942 ? 1.0089  ? -0.0308 ? 1.1181 ? 0.1162  ? -0.1877 ? 0.0531  ? 0.1865  ? -0.0384 ? 0.0875  ? 0.0289  ? -0.1891 ? -0.0778 ? 
4 'X-RAY DIFFRACTION' ? refined 52.6751 -44.7848 -4.2306  0.2014 ? -0.0711 ? 0.0216  ? 0.1475 ? 0.0155 ? 0.0314 ? 6.8486  ? 
-2.8471 ? -1.0678 ? 4.1805  ? 3.2440  ? 2.7844 ? -0.1092 ? -0.8228 ? -0.0898 ? 0.7493  ? 0.0009  ? 0.1413  ? 0.6678  ? -0.1891 ? 
0.1083  ? 
5 'X-RAY DIFFRACTION' ? refined 37.1620 -48.2325 -15.2290 0.0398 ? -0.0074 ? 0.0085  ? 0.0531 ? 0.0154 ? 0.0203 ? 3.4783  ? 1.0936 
? 0.4157  ? 1.2961  ? 0.7366  ? 1.0816 ? 0.1320  ? -0.1615 ? 0.1201  ? 0.1609  ? -0.0285 ? 0.0076  ? 0.0391  ? -0.1445 ? -0.1036 ? 
6 'X-RAY DIFFRACTION' ? refined 15.9054 -54.0808 -14.5577 0.0759 ? -0.0485 ? -0.0063 ? 0.2202 ? 0.0272 ? 0.1324 ? 10.3464 ? 
-6.1979 ? -1.8960 ? 12.0835 ? 1.3694  ? 5.0732 ? -0.0142 ? -0.1957 ? 0.0747  ? 0.1697  ? -0.0530 ? 0.7581  ? -0.3322 ? -0.4978 ? 
0.0672  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 2   ? ? ? A 11  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 12  ? ? ? A 55  ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 56  ? ? ? A 118 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? A 119 ? ? ? A 137 ? ? ? 
5 'X-RAY DIFFRACTION' 5 ? ? A 138 ? ? ? A 211 ? ? ? 
6 'X-RAY DIFFRACTION' 6 ? ? A 212 ? ? ? A 233 ? ? ? 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PO4 P    P N N 287 
PO4 O1   O N N 288 
PO4 O2   O N N 289 
PO4 O3   O N N 290 
PO4 O4   O N N 291 
PRO N    N N N 292 
PRO CA   C N S 293 
PRO C    C N N 294 
PRO O    O N N 295 
PRO CB   C N N 296 
PRO CG   C N N 297 
PRO CD   C N N 298 
PRO OXT  O N N 299 
PRO H    H N N 300 
PRO HA   H N N 301 
PRO HB2  H N N 302 
PRO HB3  H N N 303 
PRO HG2  H N N 304 
PRO HG3  H N N 305 
PRO HD2  H N N 306 
PRO HD3  H N N 307 
PRO HXT  H N N 308 
SER N    N N N 309 
SER CA   C N S 310 
SER C    C N N 311 
SER O    O N N 312 
SER CB   C N N 313 
SER OG   O N N 314 
SER OXT  O N N 315 
SER H    H N N 316 
SER H2   H N N 317 
SER HA   H N N 318 
SER HB2  H N N 319 
SER HB3  H N N 320 
SER HG   H N N 321 
SER HXT  H N N 322 
THR N    N N N 323 
THR CA   C N S 324 
THR C    C N N 325 
THR O    O N N 326 
THR CB   C N R 327 
THR OG1  O N N 328 
THR CG2  C N N 329 
THR OXT  O N N 330 
THR H    H N N 331 
THR H2   H N N 332 
THR HA   H N N 333 
THR HB   H N N 334 
THR HG1  H N N 335 
THR HG21 H N N 336 
THR HG22 H N N 337 
THR HG23 H N N 338 
THR HXT  H N N 339 
TRP N    N N N 340 
TRP CA   C N S 341 
TRP C    C N N 342 
TRP O    O N N 343 
TRP CB   C N N 344 
TRP CG   C Y N 345 
TRP CD1  C Y N 346 
TRP CD2  C Y N 347 
TRP NE1  N Y N 348 
TRP CE2  C Y N 349 
TRP CE3  C Y N 350 
TRP CZ2  C Y N 351 
TRP CZ3  C Y N 352 
TRP CH2  C Y N 353 
TRP OXT  O N N 354 
TRP H    H N N 355 
TRP H2   H N N 356 
TRP HA   H N N 357 
TRP HB2  H N N 358 
TRP HB3  H N N 359 
TRP HD1  H N N 360 
TRP HE1  H N N 361 
TRP HE3  H N N 362 
TRP HZ2  H N N 363 
TRP HZ3  H N N 364 
TRP HH2  H N N 365 
TRP HXT  H N N 366 
TYR N    N N N 367 
TYR CA   C N S 368 
TYR C    C N N 369 
TYR O    O N N 370 
TYR CB   C N N 371 
TYR CG   C Y N 372 
TYR CD1  C Y N 373 
TYR CD2  C Y N 374 
TYR CE1  C Y N 375 
TYR CE2  C Y N 376 
TYR CZ   C Y N 377 
TYR OH   O N N 378 
TYR OXT  O N N 379 
TYR H    H N N 380 
TYR H2   H N N 381 
TYR HA   H N N 382 
TYR HB2  H N N 383 
TYR HB3  H N N 384 
TYR HD1  H N N 385 
TYR HD2  H N N 386 
TYR HE1  H N N 387 
TYR HE2  H N N 388 
TYR HH   H N N 389 
TYR HXT  H N N 390 
VAL N    N N N 391 
VAL CA   C N S 392 
VAL C    C N N 393 
VAL O    O N N 394 
VAL CB   C N N 395 
VAL CG1  C N N 396 
VAL CG2  C N N 397 
VAL OXT  O N N 398 
VAL H    H N N 399 
VAL H2   H N N 400 
VAL HA   H N N 401 
VAL HB   H N N 402 
VAL HG11 H N N 403 
VAL HG12 H N N 404 
VAL HG13 H N N 405 
VAL HG21 H N N 406 
VAL HG22 H N N 407 
VAL HG23 H N N 408 
VAL HXT  H N N 409 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PO4 P   O1   doub N N 273 
PO4 P   O2   sing N N 274 
PO4 P   O3   sing N N 275 
PO4 P   O4   sing N N 276 
PRO N   CA   sing N N 277 
PRO N   CD   sing N N 278 
PRO N   H    sing N N 279 
PRO CA  C    sing N N 280 
PRO CA  CB   sing N N 281 
PRO CA  HA   sing N N 282 
PRO C   O    doub N N 283 
PRO C   OXT  sing N N 284 
PRO CB  CG   sing N N 285 
PRO CB  HB2  sing N N 286 
PRO CB  HB3  sing N N 287 
PRO CG  CD   sing N N 288 
PRO CG  HG2  sing N N 289 
PRO CG  HG3  sing N N 290 
PRO CD  HD2  sing N N 291 
PRO CD  HD3  sing N N 292 
PRO OXT HXT  sing N N 293 
SER N   CA   sing N N 294 
SER N   H    sing N N 295 
SER N   H2   sing N N 296 
SER CA  C    sing N N 297 
SER CA  CB   sing N N 298 
SER CA  HA   sing N N 299 
SER C   O    doub N N 300 
SER C   OXT  sing N N 301 
SER CB  OG   sing N N 302 
SER CB  HB2  sing N N 303 
SER CB  HB3  sing N N 304 
SER OG  HG   sing N N 305 
SER OXT HXT  sing N N 306 
THR N   CA   sing N N 307 
THR N   H    sing N N 308 
THR N   H2   sing N N 309 
THR CA  C    sing N N 310 
THR CA  CB   sing N N 311 
THR CA  HA   sing N N 312 
THR C   O    doub N N 313 
THR C   OXT  sing N N 314 
THR CB  OG1  sing N N 315 
THR CB  CG2  sing N N 316 
THR CB  HB   sing N N 317 
THR OG1 HG1  sing N N 318 
THR CG2 HG21 sing N N 319 
THR CG2 HG22 sing N N 320 
THR CG2 HG23 sing N N 321 
THR OXT HXT  sing N N 322 
TRP N   CA   sing N N 323 
TRP N   H    sing N N 324 
TRP N   H2   sing N N 325 
TRP CA  C    sing N N 326 
TRP CA  CB   sing N N 327 
TRP CA  HA   sing N N 328 
TRP C   O    doub N N 329 
TRP C   OXT  sing N N 330 
TRP CB  CG   sing N N 331 
TRP CB  HB2  sing N N 332 
TRP CB  HB3  sing N N 333 
TRP CG  CD1  doub Y N 334 
TRP CG  CD2  sing Y N 335 
TRP CD1 NE1  sing Y N 336 
TRP CD1 HD1  sing N N 337 
TRP CD2 CE2  doub Y N 338 
TRP CD2 CE3  sing Y N 339 
TRP NE1 CE2  sing Y N 340 
TRP NE1 HE1  sing N N 341 
TRP CE2 CZ2  sing Y N 342 
TRP CE3 CZ3  doub Y N 343 
TRP CE3 HE3  sing N N 344 
TRP CZ2 CH2  doub Y N 345 
TRP CZ2 HZ2  sing N N 346 
TRP CZ3 CH2  sing Y N 347 
TRP CZ3 HZ3  sing N N 348 
TRP CH2 HH2  sing N N 349 
TRP OXT HXT  sing N N 350 
TYR N   CA   sing N N 351 
TYR N   H    sing N N 352 
TYR N   H2   sing N N 353 
TYR CA  C    sing N N 354 
TYR CA  CB   sing N N 355 
TYR CA  HA   sing N N 356 
TYR C   O    doub N N 357 
TYR C   OXT  sing N N 358 
TYR CB  CG   sing N N 359 
TYR CB  HB2  sing N N 360 
TYR CB  HB3  sing N N 361 
TYR CG  CD1  doub Y N 362 
TYR CG  CD2  sing Y N 363 
TYR CD1 CE1  sing Y N 364 
TYR CD1 HD1  sing N N 365 
TYR CD2 CE2  doub Y N 366 
TYR CD2 HD2  sing N N 367 
TYR CE1 CZ   doub Y N 368 
TYR CE1 HE1  sing N N 369 
TYR CE2 CZ   sing Y N 370 
TYR CE2 HE2  sing N N 371 
TYR CZ  OH   sing N N 372 
TYR OH  HH   sing N N 373 
TYR OXT HXT  sing N N 374 
VAL N   CA   sing N N 375 
VAL N   H    sing N N 376 
VAL N   H2   sing N N 377 
VAL CA  C    sing N N 378 
VAL CA  CB   sing N N 379 
VAL CA  HA   sing N N 380 
VAL C   O    doub N N 381 
VAL C   OXT  sing N N 382 
VAL CB  CG1  sing N N 383 
VAL CB  CG2  sing N N 384 
VAL CB  HB   sing N N 385 
VAL CG1 HG11 sing N N 386 
VAL CG1 HG12 sing N N 387 
VAL CG1 HG13 sing N N 388 
VAL CG2 HG21 sing N N 389 
VAL CG2 HG22 sing N N 390 
VAL CG2 HG23 sing N N 391 
VAL OXT HXT  sing N N 392 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government' China 2019YFA0904900 1 
'Other government' China BK20202002     2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JQ0 
_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]   0.008019 
_atom_sites.fract_transf_matrix[1][2]   0.004630 
_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]   0.009259 
_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]   0.010280 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 2   ? 48.253 -67.508 -22.748 1.00 64.81 ? 2   ALA A N   1 
ATOM   2    C CA  . ALA A 1 2   ? 48.669 -67.758 -21.336 1.00 62.09 ? 2   ALA A CA  1 
ATOM   3    C C   . ALA A 1 2   ? 47.468 -68.119 -20.466 1.00 59.10 ? 2   ALA A C   1 
ATOM   4    O O   . ALA A 1 2   ? 46.385 -67.562 -20.636 1.00 58.14 ? 2   ALA A O   1 
ATOM   5    C CB  . ALA A 1 2   ? 49.376 -66.535 -20.771 1.00 60.54 ? 2   ALA A CB  1 
ATOM   6    N N   . LEU A 1 3   ? 47.665 -69.055 -19.541 1.00 58.54 ? 3   LEU A N   1 
ATOM   7    C CA  . LEU A 1 3   ? 46.630 -69.420 -18.574 1.00 55.67 ? 3   LEU A CA  1 
ATOM   8    C C   . LEU A 1 3   ? 46.596 -68.374 -17.468 1.00 51.85 ? 3   LEU A C   1 
ATOM   9    O O   . LEU A 1 3   ? 47.638 -67.832 -17.101 1.00 52.22 ? 3   LEU A O   1 
ATOM   10   C CB  . LEU A 1 3   ? 46.919 -70.795 -17.969 1.00 57.79 ? 3   LEU A CB  1 
ATOM   11   C CG  . LEU A 1 3   ? 46.858 -71.976 -18.943 1.00 62.17 ? 3   LEU A CG  1 
ATOM   12   C CD1 . LEU A 1 3   ? 47.744 -73.119 -18.470 1.00 65.58 ? 3   LEU A CD1 1 
ATOM   13   C CD2 . LEU A 1 3   ? 45.420 -72.438 -19.133 1.00 62.02 ? 3   LEU A CD2 1 
ATOM   14   N N   . VAL A 1 4   ? 45.407 -68.095 -16.936 1.00 48.62 ? 4   VAL A N   1 
ATOM   15   C CA  . VAL A 1 4   ? 45.277 -67.157 -15.824 1.00 45.56 ? 4   VAL A CA  1 
ATOM   16   C C   . VAL A 1 4   ? 45.969 -67.764 -14.602 1.00 45.07 ? 4   VAL A C   1 
ATOM   17   O O   . VAL A 1 4   ? 45.872 -68.973 -14.379 1.00 45.89 ? 4   VAL A O   1 
ATOM   18   C CB  . VAL A 1 4   ? 43.796 -66.827 -15.502 1.00 43.69 ? 4   VAL A CB  1 
ATOM   19   C CG1 . VAL A 1 4   ? 43.098 -67.994 -14.814 1.00 43.57 ? 4   VAL A CG1 1 
ATOM   20   C CG2 . VAL A 1 4   ? 43.697 -65.573 -14.646 1.00 42.20 ? 4   VAL A CG2 1 
ATOM   21   N N   . PRO A 1 5   ? 46.693 -66.940 -13.823 1.00 43.92 ? 5   PRO A N   1 
ATOM   22   C CA  . PRO A 1 5   ? 47.287 -67.482 -12.601 1.00 44.38 ? 5   PRO A CA  1 
ATOM   23   C C   . PRO A 1 5   ? 46.224 -67.959 -11.611 1.00 42.70 ? 5   PRO A C   1 
ATOM   24   O O   . PRO A 1 5   ? 45.063 -67.551 -11.718 1.00 40.50 ? 5   PRO A O   1 
ATOM   25   C CB  . PRO A 1 5   ? 48.062 -66.292 -12.023 1.00 44.66 ? 5   PRO A CB  1 
ATOM   26   C CG  . PRO A 1 5   ? 48.326 -65.402 -13.187 1.00 44.83 ? 5   PRO A CG  1 
ATOM   27   C CD  . PRO A 1 5   ? 47.127 -65.555 -14.076 1.00 43.62 ? 5   PRO A CD  1 
ATOM   28   N N   . PRO A 1 6   ? 46.613 -68.819 -10.650 1.00 44.10 ? 6   PRO A N   1 
ATOM   29   C CA  . PRO A 1 6   ? 45.656 -69.302 -9.654  1.00 43.26 ? 6   PRO A CA  1 
ATOM   30   C C   . PRO A 1 6   ? 44.947 -68.163 -8.924  1.00 40.70 ? 6   PRO A C   1 
ATOM   31   O O   . PRO A 1 6   ? 45.538 -67.106 -8.696  1.00 40.63 ? 6   PRO A O   1 
ATOM   32   C CB  . PRO A 1 6   ? 46.529 -70.093 -8.672  1.00 46.54 ? 6   PRO A CB  1 
ATOM   33   C CG  . PRO A 1 6   ? 47.729 -70.488 -9.455  1.00 49.01 ? 6   PRO A CG  1 
ATOM   34   C CD  . PRO A 1 6   ? 47.961 -69.378 -10.438 1.00 47.19 ? 6   PRO A CD  1 
ATOM   35   N N   . GLY A 1 7   ? 43.688 -68.377 -8.568  1.00 38.90 ? 7   GLY A N   1 
ATOM   36   C CA  . GLY A 1 7   ? 42.955 -67.387 -7.801  1.00 37.32 ? 7   GLY A CA  1 
ATOM   37   C C   . GLY A 1 7   ? 41.479 -67.680 -7.689  1.00 35.78 ? 7   GLY A C   1 
ATOM   38   O O   . GLY A 1 7   ? 40.995 -68.727 -8.127  1.00 35.98 ? 7   GLY A O   1 
ATOM   39   N N   . ASN A 1 8   ? 40.767 -66.735 -7.091  1.00 34.68 ? 8   ASN A N   1 
ATOM   40   C CA  . ASN A 1 8   ? 39.338 -66.862 -6.889  1.00 33.75 ? 8   ASN A CA  1 
ATOM   41   C C   . ASN A 1 8   ? 38.562 -66.714 -8.185  1.00 32.15 ? 8   ASN A C   1 
ATOM   42   O O   . ASN A 1 8   ? 39.021 -66.080 -9.136  1.00 31.34 ? 8   ASN A O   1 
ATOM   43   C CB  . ASN A 1 8   ? 38.852 -65.822 -5.879  1.00 34.21 ? 8   ASN A CB  1 
ATOM   44   C CG  . ASN A 1 8   ? 39.282 -66.148 -4.464  1.00 36.50 ? 8   ASN A CG  1 
ATOM   45   O OD1 . ASN A 1 8   ? 38.925 -67.194 -3.930  1.00 37.57 ? 8   ASN A OD1 1 
ATOM   46   N ND2 . ASN A 1 8   ? 40.051 -65.257 -3.850  1.00 38.05 ? 8   ASN A ND2 1 
ATOM   47   N N   . ASP A 1 9   ? 37.388 -67.328 -8.214  1.00 31.94 ? 9   ASP A N   1 
ATOM   48   C CA  . ASP A 1 9   ? 36.449 -67.152 -9.310  1.00 31.35 ? 9   ASP A CA  1 
ATOM   49   C C   . ASP A 1 9   ? 35.039 -67.464 -8.800  1.00 31.80 ? 9   ASP A C   1 
ATOM   50   O O   . ASP A 1 9   ? 34.811 -67.484 -7.586  1.00 32.05 ? 9   ASP A O   1 
ATOM   51   C CB  . ASP A 1 9   ? 36.864 -67.999 -10.525 1.00 31.87 ? 9   ASP A CB  1 
ATOM   52   C CG  . ASP A 1 9   ? 36.708 -69.494 -10.302 1.00 33.31 ? 9   ASP A CG  1 
ATOM   53   O OD1 . ASP A 1 9   ? 36.333 -69.926 -9.189  1.00 33.72 ? 9   ASP A OD1 1 
ATOM   54   O OD2 . ASP A 1 9   ? 36.974 -70.245 -11.265 1.00 34.35 ? 9   ASP A OD2 1 
ATOM   55   N N   . VAL A 1 10  ? 34.098 -67.682 -9.713  1.00 32.39 ? 10  VAL A N   1 
ATOM   56   C CA  . VAL A 1 10  ? 32.715 -67.991 -9.342  1.00 33.24 ? 10  VAL A CA  1 
ATOM   57   C C   . VAL A 1 10  ? 32.586 -69.215 -8.423  1.00 34.69 ? 10  VAL A C   1 
ATOM   58   O O   . VAL A 1 10  ? 31.678 -69.267 -7.594  1.00 35.37 ? 10  VAL A O   1 
ATOM   59   C CB  . VAL A 1 10  ? 31.825 -68.174 -10.596 1.00 34.12 ? 10  VAL A CB  1 
ATOM   60   C CG1 . VAL A 1 10  ? 32.212 -69.432 -11.368 1.00 35.62 ? 10  VAL A CG1 1 
ATOM   61   C CG2 . VAL A 1 10  ? 30.347 -68.193 -10.215 1.00 35.14 ? 10  VAL A CG2 1 
ATOM   62   N N   . THR A 1 11  ? 33.490 -70.186 -8.562  1.00 35.71 ? 11  THR A N   1 
ATOM   63   C CA  . THR A 1 11  ? 33.444 -71.404 -7.751  1.00 37.98 ? 11  THR A CA  1 
ATOM   64   C C   . THR A 1 11  ? 33.828 -71.171 -6.285  1.00 38.50 ? 11  THR A C   1 
ATOM   65   O O   . THR A 1 11  ? 33.443 -71.957 -5.422  1.00 40.66 ? 11  THR A O   1 
ATOM   66   C CB  . THR A 1 11  ? 34.346 -72.527 -8.319  1.00 39.90 ? 11  THR A CB  1 
ATOM   67   O OG1 . THR A 1 11  ? 35.726 -72.166 -8.184  1.00 39.20 ? 11  THR A OG1 1 
ATOM   68   C CG2 . THR A 1 11  ? 34.026 -72.802 -9.786  1.00 40.55 ? 11  THR A CG2 1 
ATOM   69   N N   . THR A 1 12  ? 34.592 -70.114 -6.008  1.00 37.14 ? 12  THR A N   1 
ATOM   70   C CA  . THR A 1 12  ? 34.979 -69.780 -4.631  1.00 37.92 ? 12  THR A CA  1 
ATOM   71   C C   . THR A 1 12  ? 34.217 -68.582 -4.059  1.00 37.77 ? 12  THR A C   1 
ATOM   72   O O   . THR A 1 12  ? 33.933 -68.546 -2.864  1.00 38.58 ? 12  THR A O   1 
ATOM   73   C CB  . THR A 1 12  ? 36.495 -69.518 -4.507  1.00 37.86 ? 12  THR A CB  1 
ATOM   74   O OG1 . THR A 1 12  ? 36.873 -68.388 -5.306  1.00 36.72 ? 12  THR A OG1 1 
ATOM   75   C CG2 . THR A 1 12  ? 37.287 -70.745 -4.943  1.00 38.44 ? 12  THR A CG2 1 
ATOM   76   N N   . LYS A 1 13  ? 33.899 -67.602 -4.902  1.00 36.77 ? 13  LYS A N   1 
ATOM   77   C CA  . LYS A 1 13  ? 33.210 -66.392 -4.460  1.00 36.64 ? 13  LYS A CA  1 
ATOM   78   C C   . LYS A 1 13  ? 32.082 -66.041 -5.431  1.00 36.02 ? 13  LYS A C   1 
ATOM   79   O O   . LYS A 1 13  ? 32.184 -65.067 -6.180  1.00 34.83 ? 13  LYS A O   1 
ATOM   80   C CB  . LYS A 1 13  ? 34.204 -65.234 -4.352  1.00 36.35 ? 13  LYS A CB  1 
ATOM   81   C CG  . LYS A 1 13  ? 35.275 -65.429 -3.293  1.00 37.23 ? 13  LYS A CG  1 
ATOM   82   C CD  . LYS A 1 13  ? 36.233 -64.248 -3.257  1.00 36.87 ? 13  LYS A CD  1 
ATOM   83   C CE  . LYS A 1 13  ? 37.200 -64.359 -2.090  1.00 37.83 ? 13  LYS A CE  1 
ATOM   84   N NZ  . LYS A 1 13  ? 38.137 -63.203 -2.054  1.00 37.52 ? 13  LYS A NZ  1 
ATOM   85   N N   . PRO A 1 14  ? 30.987 -66.825 -5.409  1.00 36.63 ? 14  PRO A N   1 
ATOM   86   C CA  . PRO A 1 14  ? 29.891 -66.643 -6.373  1.00 36.34 ? 14  PRO A CA  1 
ATOM   87   C C   . PRO A 1 14  ? 29.153 -65.301 -6.258  1.00 36.14 ? 14  PRO A C   1 
ATOM   88   O O   . PRO A 1 14  ? 28.409 -64.941 -7.171  1.00 36.02 ? 14  PRO A O   1 
ATOM   89   C CB  . PRO A 1 14  ? 28.949 -67.810 -6.057  1.00 37.20 ? 14  PRO A CB  1 
ATOM   90   C CG  . PRO A 1 14  ? 29.220 -68.136 -4.632  1.00 38.09 ? 14  PRO A CG  1 
ATOM   91   C CD  . PRO A 1 14  ? 30.685 -67.890 -4.434  1.00 37.81 ? 14  PRO A CD  1 
ATOM   92   N N   . ASP A 1 15  ? 29.357 -64.587 -5.150  1.00 36.28 ? 15  ASP A N   1 
ATOM   93   C CA  A ASP A 1 15  ? 28.768 -63.267 -4.924  0.50 36.29 ? 15  ASP A CA  1 
ATOM   94   C CA  B ASP A 1 15  ? 28.746 -63.271 -4.961  0.50 36.22 ? 15  ASP A CA  1 
ATOM   95   C C   . ASP A 1 15  ? 29.601 -62.142 -5.544  1.00 35.17 ? 15  ASP A C   1 
ATOM   96   O O   . ASP A 1 15  ? 29.126 -61.013 -5.678  1.00 34.88 ? 15  ASP A O   1 
ATOM   97   C CB  A ASP A 1 15  ? 28.588 -63.008 -3.417  0.50 37.50 ? 15  ASP A CB  1 
ATOM   98   C CB  B ASP A 1 15  ? 28.475 -63.007 -3.478  0.50 37.37 ? 15  ASP A CB  1 
ATOM   99   C CG  A ASP A 1 15  ? 29.876 -63.208 -2.614  0.50 37.84 ? 15  ASP A CG  1 
ATOM   100  C CG  B ASP A 1 15  ? 27.358 -63.876 -2.924  0.50 38.48 ? 15  ASP A CG  1 
ATOM   101  O OD1 A ASP A 1 15  ? 30.622 -64.170 -2.898  0.50 37.75 ? 15  ASP A OD1 1 
ATOM   102  O OD1 B ASP A 1 15  ? 26.450 -64.261 -3.691  0.50 38.49 ? 15  ASP A OD1 1 
ATOM   103  O OD2 A ASP A 1 15  ? 30.134 -62.412 -1.687  0.50 38.33 ? 15  ASP A OD2 1 
ATOM   104  O OD2 B ASP A 1 15  ? 27.386 -64.166 -1.712  0.50 39.64 ? 15  ASP A OD2 1 
ATOM   105  N N   . LEU A 1 16  ? 30.850 -62.445 -5.898  1.00 34.21 ? 16  LEU A N   1 
ATOM   106  C CA  . LEU A 1 16  ? 31.765 -61.447 -6.459  1.00 33.14 ? 16  LEU A CA  1 
ATOM   107  C C   . LEU A 1 16  ? 32.238 -61.741 -7.888  1.00 31.61 ? 16  LEU A C   1 
ATOM   108  O O   . LEU A 1 16  ? 32.844 -60.876 -8.517  1.00 30.43 ? 16  LEU A O   1 
ATOM   109  C CB  . LEU A 1 16  ? 32.976 -61.282 -5.533  1.00 33.68 ? 16  LEU A CB  1 
ATOM   110  C CG  . LEU A 1 16  ? 32.694 -60.505 -4.244  1.00 34.86 ? 16  LEU A CG  1 
ATOM   111  C CD1 . LEU A 1 16  ? 33.811 -60.708 -3.228  1.00 35.50 ? 16  LEU A CD1 1 
ATOM   112  C CD2 . LEU A 1 16  ? 32.504 -59.021 -4.542  1.00 34.65 ? 16  LEU A CD2 1 
ATOM   113  N N   . TYR A 1 17  ? 31.970 -62.946 -8.389  1.00 31.18 ? 17  TYR A N   1 
ATOM   114  C CA  . TYR A 1 17  ? 32.303 -63.322 -9.764  1.00 30.29 ? 17  TYR A CA  1 
ATOM   115  C C   . TYR A 1 17  ? 31.135 -64.062 -10.395 1.00 30.62 ? 17  TYR A C   1 
ATOM   116  O O   . TYR A 1 17  ? 30.488 -64.876 -9.738  1.00 31.05 ? 17  TYR A O   1 
ATOM   117  C CB  . TYR A 1 17  ? 33.490 -64.287 -9.815  1.00 30.16 ? 17  TYR A CB  1 
ATOM   118  C CG  . TYR A 1 17  ? 34.772 -63.837 -9.161  1.00 29.86 ? 17  TYR A CG  1 
ATOM   119  C CD1 . TYR A 1 17  ? 34.880 -63.755 -7.775  1.00 30.41 ? 17  TYR A CD1 1 
ATOM   120  C CD2 . TYR A 1 17  ? 35.901 -63.563 -9.922  1.00 29.04 ? 17  TYR A CD2 1 
ATOM   121  C CE1 . TYR A 1 17  ? 36.062 -63.366 -7.172  1.00 30.27 ? 17  TYR A CE1 1 
ATOM   122  C CE2 . TYR A 1 17  ? 37.091 -63.183 -9.325  1.00 29.05 ? 17  TYR A CE2 1 
ATOM   123  C CZ  . TYR A 1 17  ? 37.163 -63.086 -7.950  1.00 29.56 ? 17  TYR A CZ  1 
ATOM   124  O OH  . TYR A 1 17  ? 38.334 -62.707 -7.349  1.00 29.41 ? 17  TYR A OH  1 
ATOM   125  N N   . TYR A 1 18  ? 30.880 -63.779 -11.669 1.00 30.21 ? 18  TYR A N   1 
ATOM   126  C CA  . TYR A 1 18  ? 30.032 -64.620 -12.509 1.00 30.63 ? 18  TYR A CA  1 
ATOM   127  C C   . TYR A 1 18  ? 30.848 -65.688 -13.227 1.00 30.46 ? 18  TYR A C   1 
ATOM   128  O O   . TYR A 1 18  ? 30.324 -66.744 -13.563 1.00 30.92 ? 18  TYR A O   1 
ATOM   129  C CB  . TYR A 1 18  ? 29.319 -63.781 -13.571 1.00 30.55 ? 18  TYR A CB  1 
ATOM   130  C CG  . TYR A 1 18  ? 28.230 -62.889 -13.037 1.00 30.94 ? 18  TYR A CG  1 
ATOM   131  C CD1 . TYR A 1 18  ? 26.973 -63.401 -12.733 1.00 31.87 ? 18  TYR A CD1 1 
ATOM   132  C CD2 . TYR A 1 18  ? 28.448 -61.528 -12.851 1.00 30.73 ? 18  TYR A CD2 1 
ATOM   133  C CE1 . TYR A 1 18  ? 25.966 -62.584 -12.248 1.00 32.43 ? 18  TYR A CE1 1 
ATOM   134  C CE2 . TYR A 1 18  ? 27.448 -60.703 -12.368 1.00 31.33 ? 18  TYR A CE2 1 
ATOM   135  C CZ  . TYR A 1 18  ? 26.209 -61.234 -12.073 1.00 32.20 ? 18  TYR A CZ  1 
ATOM   136  O OH  . TYR A 1 18  ? 25.213 -60.416 -11.592 1.00 33.24 ? 18  TYR A OH  1 
ATOM   137  N N   . LEU A 1 19  ? 32.128 -65.411 -13.467 1.00 29.84 ? 19  LEU A N   1 
ATOM   138  C CA  . LEU A 1 19  ? 32.932 -66.213 -14.384 1.00 29.85 ? 19  LEU A CA  1 
ATOM   139  C C   . LEU A 1 19  ? 33.942 -67.110 -13.680 1.00 30.26 ? 19  LEU A C   1 
ATOM   140  O O   . LEU A 1 19  ? 34.332 -66.858 -12.537 1.00 30.13 ? 19  LEU A O   1 
ATOM   141  C CB  . LEU A 1 19  ? 33.671 -65.295 -15.360 1.00 29.28 ? 19  LEU A CB  1 
ATOM   142  C CG  . LEU A 1 19  ? 32.810 -64.298 -16.138 1.00 28.98 ? 19  LEU A CG  1 
ATOM   143  C CD1 . LEU A 1 19  ? 33.693 -63.412 -16.998 1.00 28.34 ? 19  LEU A CD1 1 
ATOM   144  C CD2 . LEU A 1 19  ? 31.775 -65.021 -16.990 1.00 29.50 ? 19  LEU A CD2 1 
ATOM   145  N N   . THR A 1 20  ? 34.362 -68.156 -14.386 1.00 30.72 ? 20  THR A N   1 
ATOM   146  C CA  . THR A 1 20  ? 35.406 -69.055 -13.910 1.00 31.38 ? 20  THR A CA  1 
ATOM   147  C C   . THR A 1 20  ? 36.775 -68.566 -14.360 1.00 31.09 ? 20  THR A C   1 
ATOM   148  O O   . THR A 1 20  ? 36.887 -67.714 -15.249 1.00 30.41 ? 20  THR A O   1 
ATOM   149  C CB  . THR A 1 20  ? 35.221 -70.483 -14.455 1.00 32.22 ? 20  THR A CB  1 
ATOM   150  O OG1 . THR A 1 20  ? 35.363 -70.476 -15.880 1.00 32.09 ? 20  THR A OG1 1 
ATOM   151  C CG2 . THR A 1 20  ? 33.854 -71.040 -14.075 1.00 32.81 ? 20  THR A CG2 1 
ATOM   152  N N   . ASN A 1 21  ? 37.816 -69.123 -13.753 1.00 31.72 ? 21  ASN A N   1 
ATOM   153  C CA  . ASN A 1 21  ? 39.188 -68.845 -14.168 1.00 31.52 ? 21  ASN A CA  1 
ATOM   154  C C   . ASN A 1 21  ? 39.416 -69.111 -15.656 1.00 31.57 ? 21  ASN A C   1 
ATOM   155  O O   . ASN A 1 21  ? 40.100 -68.339 -16.325 1.00 31.15 ? 21  ASN A O   1 
ATOM   156  C CB  . ASN A 1 21  ? 40.174 -69.663 -13.330 1.00 32.27 ? 21  ASN A CB  1 
ATOM   157  C CG  . ASN A 1 21  ? 40.379 -69.082 -11.945 1.00 32.28 ? 21  ASN A CG  1 
ATOM   158  O OD1 . ASN A 1 21  ? 40.442 -67.864 -11.777 1.00 31.37 ? 21  ASN A OD1 1 
ATOM   159  N ND2 . ASN A 1 21  ? 40.493 -69.951 -10.946 1.00 33.24 ? 21  ASN A ND2 1 
ATOM   160  N N   . ALA A 1 22  ? 38.825 -70.187 -16.169 1.00 32.17 ? 22  ALA A N   1 
ATOM   161  C CA  . ALA A 1 22  ? 38.941 -70.539 -17.590 1.00 32.59 ? 22  ALA A CA  1 
ATOM   162  C C   . ALA A 1 22  ? 38.316 -69.495 -18.530 1.00 31.82 ? 22  ALA A C   1 
ATOM   163  O O   . ALA A 1 22  ? 38.703 -69.399 -19.694 1.00 31.89 ? 22  ALA A O   1 
ATOM   164  C CB  . ALA A 1 22  ? 38.323 -71.907 -17.843 1.00 33.62 ? 22  ALA A CB  1 
ATOM   165  N N   . GLN A 1 23  ? 37.357 -68.722 -18.021 1.00 31.30 ? 23  GLN A N   1 
ATOM   166  C CA  . GLN A 1 23  ? 36.683 -67.683 -18.803 1.00 30.84 ? 23  GLN A CA  1 
ATOM   167  C C   . GLN A 1 23  ? 37.357 -66.309 -18.715 1.00 29.84 ? 23  GLN A C   1 
ATOM   168  O O   . GLN A 1 23  ? 36.890 -65.352 -19.333 1.00 29.32 ? 23  GLN A O   1 
ATOM   169  C CB  . GLN A 1 23  ? 35.229 -67.556 -18.349 1.00 31.00 ? 23  GLN A CB  1 
ATOM   170  C CG  . GLN A 1 23  ? 34.386 -68.787 -18.633 1.00 32.14 ? 23  GLN A CG  1 
ATOM   171  C CD  . GLN A 1 23  ? 33.000 -68.677 -18.034 1.00 32.47 ? 23  GLN A CD  1 
ATOM   172  O OE1 . GLN A 1 23  ? 32.846 -68.554 -16.822 1.00 32.46 ? 23  GLN A OE1 1 
ATOM   173  N NE2 . GLN A 1 23  ? 31.981 -68.725 -18.882 1.00 33.12 ? 23  GLN A NE2 1 
ATOM   174  N N   . ALA A 1 24  ? 38.437 -66.204 -17.948 1.00 29.52 ? 24  ALA A N   1 
ATOM   175  C CA  . ALA A 1 24  ? 39.123 -64.926 -17.773 1.00 28.80 ? 24  ALA A CA  1 
ATOM   176  C C   . ALA A 1 24  ? 39.705 -64.407 -19.084 1.00 28.50 ? 24  ALA A C   1 
ATOM   177  O O   . ALA A 1 24  ? 40.143 -65.180 -19.933 1.00 29.16 ? 24  ALA A O   1 
ATOM   178  C CB  . ALA A 1 24  ? 40.222 -65.052 -16.730 1.00 28.90 ? 24  ALA A CB  1 
ATOM   179  N N   . ILE A 1 25  ? 39.701 -63.088 -19.240 1.00 27.94 ? 25  ILE A N   1 
ATOM   180  C CA  . ILE A 1 25  ? 40.388 -62.451 -20.350 1.00 27.78 ? 25  ILE A CA  1 
ATOM   181  C C   . ILE A 1 25  ? 41.873 -62.729 -20.166 1.00 27.91 ? 25  ILE A C   1 
ATOM   182  O O   . ILE A 1 25  ? 42.403 -62.598 -19.058 1.00 27.70 ? 25  ILE A O   1 
ATOM   183  C CB  . ILE A 1 25  ? 40.145 -60.924 -20.379 1.00 27.24 ? 25  ILE A CB  1 
ATOM   184  C CG1 . ILE A 1 25  ? 38.652 -60.609 -20.551 1.00 27.46 ? 25  ILE A CG1 1 
ATOM   185  C CG2 . ILE A 1 25  ? 40.959 -60.264 -21.490 1.00 27.36 ? 25  ILE A CG2 1 
ATOM   186  C CD1 . ILE A 1 25  ? 37.989 -61.294 -21.730 1.00 28.01 ? 25  ILE A CD1 1 
ATOM   187  N N   . ASP A 1 26  ? 42.535 -63.137 -21.242 1.00 28.13 ? 26  ASP A N   1 
ATOM   188  C CA  . ASP A 1 26  ? 43.968 -63.385 -21.214 1.00 28.44 ? 26  ASP A CA  1 
ATOM   189  C C   . ASP A 1 26  ? 44.660 -62.028 -21.296 1.00 27.36 ? 26  ASP A C   1 
ATOM   190  O O   . ASP A 1 26  ? 45.096 -61.606 -22.363 1.00 27.17 ? 26  ASP A O   1 
ATOM   191  C CB  . ASP A 1 26  ? 44.379 -64.305 -22.371 1.00 29.59 ? 26  ASP A CB  1 
ATOM   192  C CG  . ASP A 1 26  ? 45.828 -64.767 -22.280 1.00 30.42 ? 26  ASP A CG  1 
ATOM   193  O OD1 . ASP A 1 26  ? 46.618 -64.187 -21.503 1.00 30.08 ? 26  ASP A OD1 1 
ATOM   194  O OD2 . ASP A 1 26  ? 46.185 -65.712 -23.010 1.00 31.52 ? 26  ASP A OD2 1 
ATOM   195  N N   . SER A 1 27  ? 44.739 -61.351 -20.153 1.00 26.59 ? 27  SER A N   1 
ATOM   196  C CA  . SER A 1 27  ? 45.269 -59.987 -20.088 1.00 26.01 ? 27  SER A CA  1 
ATOM   197  C C   . SER A 1 27  ? 46.745 -59.922 -20.462 1.00 26.11 ? 27  SER A C   1 
ATOM   198  O O   . SER A 1 27  ? 47.192 -58.950 -21.065 1.00 25.75 ? 27  SER A O   1 
ATOM   199  C CB  . SER A 1 27  ? 45.057 -59.389 -18.698 1.00 25.63 ? 27  SER A CB  1 
ATOM   200  O OG  . SER A 1 27  ? 45.648 -60.176 -17.679 1.00 25.84 ? 27  SER A OG  1 
ATOM   201  N N   . LEU A 1 28  ? 47.496 -60.960 -20.109 1.00 26.72 ? 28  LEU A N   1 
ATOM   202  C CA  . LEU A 1 28  ? 48.908 -61.027 -20.452 1.00 27.13 ? 28  LEU A CA  1 
ATOM   203  C C   . LEU A 1 28  ? 49.119 -61.074 -21.970 1.00 27.45 ? 28  LEU A C   1 
ATOM   204  O O   . LEU A 1 28  ? 49.999 -60.392 -22.499 1.00 27.34 ? 28  LEU A O   1 
ATOM   205  C CB  . LEU A 1 28  ? 49.557 -62.247 -19.796 1.00 28.16 ? 28  LEU A CB  1 
ATOM   206  C CG  . LEU A 1 28  ? 51.055 -62.438 -20.039 1.00 28.84 ? 28  LEU A CG  1 
ATOM   207  C CD1 . LEU A 1 28  ? 51.844 -61.191 -19.675 1.00 28.26 ? 28  LEU A CD1 1 
ATOM   208  C CD2 . LEU A 1 28  ? 51.557 -63.643 -19.258 1.00 29.83 ? 28  LEU A CD2 1 
ATOM   209  N N   . ALA A 1 29  ? 48.313 -61.872 -22.662 1.00 27.73 ? 29  ALA A N   1 
ATOM   210  C CA  . ALA A 1 29  ? 48.422 -61.988 -24.118 1.00 28.28 ? 29  ALA A CA  1 
ATOM   211  C C   . ALA A 1 29  ? 47.839 -60.780 -24.855 1.00 27.76 ? 29  ALA A C   1 
ATOM   212  O O   . ALA A 1 29  ? 48.356 -60.383 -25.900 1.00 27.75 ? 29  ALA A O   1 
ATOM   213  C CB  . ALA A 1 29  ? 47.754 -63.264 -24.596 1.00 29.08 ? 29  ALA A CB  1 
ATOM   214  N N   . LEU A 1 30  ? 46.764 -60.209 -24.319 1.00 27.23 ? 30  LEU A N   1 
ATOM   215  C CA  . LEU A 1 30  ? 46.045 -59.128 -24.995 1.00 26.98 ? 30  LEU A CA  1 
ATOM   216  C C   . LEU A 1 30  ? 46.756 -57.784 -24.876 1.00 26.60 ? 30  LEU A C   1 
ATOM   217  O O   . LEU A 1 30  ? 46.913 -57.069 -25.860 1.00 26.74 ? 30  LEU A O   1 
ATOM   218  C CB  . LEU A 1 30  ? 44.626 -59.010 -24.436 1.00 26.59 ? 30  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 30  ? 43.702 -57.965 -25.070 1.00 26.43 ? 30  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 30  ? 43.596 -58.155 -26.576 1.00 27.21 ? 30  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 30  ? 42.329 -58.027 -24.423 1.00 26.37 ? 30  LEU A CD2 1 
ATOM   222  N N   . LEU A 1 31  ? 47.172 -57.436 -23.665 1.00 26.24 ? 31  LEU A N   1 
ATOM   223  C CA  . LEU A 1 31  ? 47.766 -56.130 -23.412 1.00 25.87 ? 31  LEU A CA  1 
ATOM   224  C C   . LEU A 1 31  ? 49.219 -56.081 -23.857 1.00 26.53 ? 31  LEU A C   1 
ATOM   225  O O   . LEU A 1 31  ? 49.925 -57.086 -23.782 1.00 26.91 ? 31  LEU A O   1 
ATOM   226  C CB  . LEU A 1 31  ? 47.695 -55.797 -21.925 1.00 25.37 ? 31  LEU A CB  1 
ATOM   227  C CG  . LEU A 1 31  ? 46.295 -55.682 -21.326 1.00 25.10 ? 31  LEU A CG  1 
ATOM   228  C CD1 . LEU A 1 31  ? 46.377 -55.511 -19.820 1.00 24.89 ? 31  LEU A CD1 1 
ATOM   229  C CD2 . LEU A 1 31  ? 45.541 -54.528 -21.966 1.00 24.97 ? 31  LEU A CD2 1 
ATOM   230  N N   . PRO A 1 32  ? 49.680 -54.904 -24.309 1.00 26.62 ? 32  PRO A N   1 
ATOM   231  C CA  . PRO A 1 32  ? 51.122 -54.755 -24.454 1.00 27.04 ? 32  PRO A CA  1 
ATOM   232  C C   . PRO A 1 32  ? 51.767 -54.721 -23.075 1.00 26.65 ? 32  PRO A C   1 
ATOM   233  O O   . PRO A 1 32  ? 51.063 -54.574 -22.072 1.00 26.61 ? 32  PRO A O   1 
ATOM   234  C CB  . PRO A 1 32  ? 51.274 -53.406 -25.159 1.00 26.97 ? 32  PRO A CB  1 
ATOM   235  C CG  . PRO A 1 32  ? 50.050 -52.641 -24.797 1.00 26.67 ? 32  PRO A CG  1 
ATOM   236  C CD  . PRO A 1 32  ? 48.956 -53.643 -24.552 1.00 26.60 ? 32  PRO A CD  1 
ATOM   237  N N   . PRO A 1 33  ? 53.096 -54.868 -23.011 1.00 27.04 ? 33  PRO A N   1 
ATOM   238  C CA  . PRO A 1 33  ? 53.736 -54.651 -21.719 1.00 26.77 ? 33  PRO A CA  1 
ATOM   239  C C   . PRO A 1 33  ? 53.590 -53.188 -21.303 1.00 25.92 ? 33  PRO A C   1 
ATOM   240  O O   . PRO A 1 33  ? 53.354 -52.328 -22.159 1.00 25.73 ? 33  PRO A O   1 
ATOM   241  C CB  . PRO A 1 33  ? 55.212 -54.992 -21.975 1.00 27.21 ? 33  PRO A CB  1 
ATOM   242  C CG  . PRO A 1 33  ? 55.274 -55.600 -23.334 1.00 28.08 ? 33  PRO A CG  1 
ATOM   243  C CD  . PRO A 1 33  ? 54.067 -55.137 -24.083 1.00 27.69 ? 33  PRO A CD  1 
ATOM   244  N N   . PRO A 1 34  ? 53.718 -52.902 -20.001 1.00 25.26 ? 34  PRO A N   1 
ATOM   245  C CA  . PRO A 1 34  ? 53.676 -51.510 -19.592 1.00 24.69 ? 34  PRO A CA  1 
ATOM   246  C C   . PRO A 1 34  ? 54.915 -50.772 -20.100 1.00 24.48 ? 34  PRO A C   1 
ATOM   247  O O   . PRO A 1 34  ? 55.910 -51.412 -20.427 1.00 24.66 ? 34  PRO A O   1 
ATOM   248  C CB  . PRO A 1 34  ? 53.684 -51.591 -18.065 1.00 24.78 ? 34  PRO A CB  1 
ATOM   249  C CG  . PRO A 1 34  ? 54.343 -52.888 -17.753 1.00 25.30 ? 34  PRO A CG  1 
ATOM   250  C CD  . PRO A 1 34  ? 54.001 -53.811 -18.876 1.00 25.69 ? 34  PRO A CD  1 
ATOM   251  N N   . PRO A 1 35  ? 54.855 -49.435 -20.173 1.00 24.16 ? 35  PRO A N   1 
ATOM   252  C CA  . PRO A 1 35  ? 56.035 -48.668 -20.563 1.00 24.09 ? 35  PRO A CA  1 
ATOM   253  C C   . PRO A 1 35  ? 57.235 -48.994 -19.678 1.00 24.30 ? 35  PRO A C   1 
ATOM   254  O O   . PRO A 1 35  ? 57.088 -49.090 -18.462 1.00 24.34 ? 35  PRO A O   1 
ATOM   255  C CB  . PRO A 1 35  ? 55.590 -47.218 -20.346 1.00 23.79 ? 35  PRO A CB  1 
ATOM   256  C CG  . PRO A 1 35  ? 54.113 -47.255 -20.524 1.00 23.78 ? 35  PRO A CG  1 
ATOM   257  C CD  . PRO A 1 35  ? 53.689 -48.568 -19.935 1.00 23.83 ? 35  PRO A CD  1 
ATOM   258  N N   . ALA A 1 36  ? 58.398 -49.182 -20.289 1.00 24.38 ? 36  ALA A N   1 
ATOM   259  C CA  . ALA A 1 36  ? 59.634 -49.408 -19.546 1.00 24.62 ? 36  ALA A CA  1 
ATOM   260  C C   . ALA A 1 36  ? 60.258 -48.074 -19.156 1.00 24.16 ? 36  ALA A C   1 
ATOM   261  O O   . ALA A 1 36  ? 60.112 -47.075 -19.867 1.00 23.45 ? 36  ALA A O   1 
ATOM   262  C CB  . ALA A 1 36  ? 60.614 -50.207 -20.387 1.00 25.37 ? 36  ALA A CB  1 
ATOM   263  N N   . VAL A 1 37  ? 60.964 -48.063 -18.030 1.00 24.06 ? 37  VAL A N   1 
ATOM   264  C CA  . VAL A 1 37  ? 61.763 -46.905 -17.656 1.00 23.86 ? 37  VAL A CA  1 
ATOM   265  C C   . VAL A 1 37  ? 62.748 -46.657 -18.789 1.00 23.70 ? 37  VAL A C   1 
ATOM   266  O O   . VAL A 1 37  ? 63.395 -47.583 -19.263 1.00 24.24 ? 37  VAL A O   1 
ATOM   267  C CB  . VAL A 1 37  ? 62.527 -47.119 -16.335 1.00 24.37 ? 37  VAL A CB  1 
ATOM   268  C CG1 . VAL A 1 37  ? 63.513 -45.979 -16.087 1.00 24.50 ? 37  VAL A CG1 1 
ATOM   269  C CG2 . VAL A 1 37  ? 61.552 -47.242 -15.180 1.00 24.47 ? 37  VAL A CG2 1 
ATOM   270  N N   . GLY A 1 38  ? 62.835 -45.410 -19.236 1.00 22.93 ? 38  GLY A N   1 
ATOM   271  C CA  . GLY A 1 38  ? 63.669 -45.066 -20.374 1.00 23.11 ? 38  GLY A CA  1 
ATOM   272  C C   . GLY A 1 38  ? 62.905 -44.944 -21.677 1.00 22.81 ? 38  GLY A C   1 
ATOM   273  O O   . GLY A 1 38  ? 63.481 -44.544 -22.681 1.00 23.35 ? 38  GLY A O   1 
ATOM   274  N N   . SER A 1 39  ? 61.615 -45.281 -21.668 1.00 22.13 ? 39  SER A N   1 
ATOM   275  C CA  . SER A 1 39  ? 60.770 -45.110 -22.844 1.00 22.06 ? 39  SER A CA  1 
ATOM   276  C C   . SER A 1 39  ? 60.096 -43.741 -22.820 1.00 21.60 ? 39  SER A C   1 
ATOM   277  O O   . SER A 1 39  ? 59.856 -43.171 -21.754 1.00 20.97 ? 39  SER A O   1 
ATOM   278  C CB  . SER A 1 39  ? 59.694 -46.201 -22.916 1.00 22.03 ? 39  SER A CB  1 
ATOM   279  O OG  . SER A 1 39  ? 58.728 -46.045 -21.890 1.00 21.35 ? 39  SER A OG  1 
ATOM   280  N N   . ILE A 1 40  ? 59.765 -43.232 -23.998 1.00 21.66 ? 40  ILE A N   1 
ATOM   281  C CA  . ILE A 1 40  ? 58.995 -41.999 -24.092 1.00 21.68 ? 40  ILE A CA  1 
ATOM   282  C C   . ILE A 1 40  ? 57.623 -42.222 -23.453 1.00 21.34 ? 40  ILE A C   1 
ATOM   283  O O   . ILE A 1 40  ? 57.070 -41.319 -22.824 1.00 20.75 ? 40  ILE A O   1 
ATOM   284  C CB  . ILE A 1 40  ? 58.798 -41.530 -25.553 1.00 22.30 ? 40  ILE A CB  1 
ATOM   285  C CG1 . ILE A 1 40  ? 60.132 -41.395 -26.301 1.00 22.92 ? 40  ILE A CG1 1 
ATOM   286  C CG2 . ILE A 1 40  ? 58.045 -40.208 -25.590 1.00 22.28 ? 40  ILE A CG2 1 
ATOM   287  C CD1 . ILE A 1 40  ? 61.150 -40.511 -25.631 1.00 22.95 ? 40  ILE A CD1 1 
ATOM   288  N N   . ALA A 1 41  ? 57.080 -43.428 -23.617 1.00 21.43 ? 41  ALA A N   1 
ATOM   289  C CA  . ALA A 1 41  ? 55.784 -43.763 -23.040 1.00 21.30 ? 41  ALA A CA  1 
ATOM   290  C C   . ALA A 1 41  ? 55.791 -43.590 -21.519 1.00 21.00 ? 41  ALA A C   1 
ATOM   291  O O   . ALA A 1 41  ? 54.849 -43.032 -20.953 1.00 21.11 ? 41  ALA A O   1 
ATOM   292  C CB  . ALA A 1 41  ? 55.375 -45.174 -23.421 1.00 21.70 ? 41  ALA A CB  1 
ATOM   293  N N   . PHE A 1 42  ? 56.853 -44.041 -20.861 1.00 20.83 ? 42  PHE A N   1 
ATOM   294  C CA  . PHE A 1 42  ? 56.945 -43.866 -19.414 1.00 20.82 ? 42  PHE A CA  1 
ATOM   295  C C   . PHE A 1 42  ? 57.158 -42.406 -19.039 1.00 20.62 ? 42  PHE A C   1 
ATOM   296  O O   . PHE A 1 42  ? 56.617 -41.943 -18.045 1.00 20.68 ? 42  PHE A O   1 
ATOM   297  C CB  . PHE A 1 42  ? 58.043 -44.721 -18.786 1.00 20.93 ? 42  PHE A CB  1 
ATOM   298  C CG  . PHE A 1 42  ? 58.113 -44.572 -17.292 1.00 21.11 ? 42  PHE A CG  1 
ATOM   299  C CD1 . PHE A 1 42  ? 57.021 -44.922 -16.503 1.00 21.08 ? 42  PHE A CD1 1 
ATOM   300  C CD2 . PHE A 1 42  ? 59.233 -44.032 -16.677 1.00 21.25 ? 42  PHE A CD2 1 
ATOM   301  C CE1 . PHE A 1 42  ? 57.061 -44.763 -15.130 1.00 21.40 ? 42  PHE A CE1 1 
ATOM   302  C CE2 . PHE A 1 42  ? 59.282 -43.875 -15.301 1.00 21.38 ? 42  PHE A CE2 1 
ATOM   303  C CZ  . PHE A 1 42  ? 58.196 -44.241 -14.527 1.00 21.62 ? 42  PHE A CZ  1 
ATOM   304  N N   . LEU A 1 43  ? 57.948 -41.681 -19.825 1.00 20.78 ? 43  LEU A N   1 
ATOM   305  C CA  . LEU A 1 43  ? 58.114 -40.249 -19.597 1.00 20.94 ? 43  LEU A CA  1 
ATOM   306  C C   . LEU A 1 43  ? 56.747 -39.548 -19.625 1.00 21.21 ? 43  LEU A C   1 
ATOM   307  O O   . LEU A 1 43  ? 56.493 -38.643 -18.829 1.00 21.36 ? 43  LEU A O   1 
ATOM   308  C CB  . LEU A 1 43  ? 59.068 -39.641 -20.627 1.00 21.00 ? 43  LEU A CB  1 
ATOM   309  C CG  . LEU A 1 43  ? 59.403 -38.154 -20.487 1.00 21.10 ? 43  LEU A CG  1 
ATOM   310  C CD1 . LEU A 1 43  ? 60.087 -37.861 -19.161 1.00 21.08 ? 43  LEU A CD1 1 
ATOM   311  C CD2 . LEU A 1 43  ? 60.275 -37.725 -21.656 1.00 21.22 ? 43  LEU A CD2 1 
ATOM   312  N N   . ASN A 1 44  ? 55.867 -39.978 -20.528 1.00 21.63 ? 44  ASN A N   1 
ATOM   313  C CA  . ASN A 1 44  ? 54.502 -39.459 -20.562 1.00 22.01 ? 44  ASN A CA  1 
ATOM   314  C C   . ASN A 1 44  ? 53.685 -39.860 -19.338 1.00 21.58 ? 44  ASN A C   1 
ATOM   315  O O   . ASN A 1 44  ? 52.938 -39.042 -18.804 1.00 21.44 ? 44  ASN A O   1 
ATOM   316  C CB  . ASN A 1 44  ? 53.759 -39.890 -21.827 1.00 22.60 ? 44  ASN A CB  1 
ATOM   317  C CG  . ASN A 1 44  ? 52.426 -39.176 -21.981 1.00 23.34 ? 44  ASN A CG  1 
ATOM   318  O OD1 . ASN A 1 44  ? 51.369 -39.803 -22.024 1.00 25.09 ? 44  ASN A OD1 1 
ATOM   319  N ND2 . ASN A 1 44  ? 52.468 -37.870 -22.023 1.00 23.46 ? 44  ASN A ND2 1 
ATOM   320  N N   . ASP A 1 45  ? 53.810 -41.115 -18.904 1.00 21.39 ? 45  ASP A N   1 
ATOM   321  C CA  . ASP A 1 45  ? 53.213 -41.542 -17.634 1.00 21.44 ? 45  ASP A CA  1 
ATOM   322  C C   . ASP A 1 45  ? 53.635 -40.608 -16.503 1.00 21.50 ? 45  ASP A C   1 
ATOM   323  O O   . ASP A 1 45  ? 52.821 -40.236 -15.658 1.00 21.91 ? 45  ASP A O   1 
ATOM   324  C CB  . ASP A 1 45  ? 53.621 -42.976 -17.270 1.00 21.49 ? 45  ASP A CB  1 
ATOM   325  C CG  . ASP A 1 45  ? 52.726 -44.034 -17.896 1.00 21.67 ? 45  ASP A CG  1 
ATOM   326  O OD1 . ASP A 1 45  ? 51.596 -43.720 -18.330 1.00 21.99 ? 45  ASP A OD1 1 
ATOM   327  O OD2 . ASP A 1 45  ? 53.165 -45.201 -17.928 1.00 21.89 ? 45  ASP A OD2 1 
ATOM   328  N N   . GLN A 1 46  ? 54.911 -40.238 -16.481 1.00 21.10 ? 46  GLN A N   1 
ATOM   329  C CA  . GLN A 1 46  ? 55.409 -39.340 -15.450 1.00 21.25 ? 46  GLN A CA  1 
ATOM   330  C C   . GLN A 1 46  ? 54.819 -37.944 -15.608 1.00 21.52 ? 46  GLN A C   1 
ATOM   331  O O   . GLN A 1 46  ? 54.460 -37.318 -14.621 1.00 21.82 ? 46  GLN A O   1 
ATOM   332  C CB  . GLN A 1 46  ? 56.936 -39.302 -15.447 1.00 21.17 ? 46  GLN A CB  1 
ATOM   333  C CG  . GLN A 1 46  ? 57.542 -40.638 -15.043 1.00 21.16 ? 46  GLN A CG  1 
ATOM   334  C CD  . GLN A 1 46  ? 59.026 -40.546 -14.804 1.00 21.32 ? 46  GLN A CD  1 
ATOM   335  O OE1 . GLN A 1 46  ? 59.493 -40.585 -13.661 1.00 22.08 ? 46  GLN A OE1 1 
ATOM   336  N NE2 . GLN A 1 46  ? 59.773 -40.399 -15.874 1.00 20.94 ? 46  GLN A NE2 1 
ATOM   337  N N   . ALA A 1 47  ? 54.697 -37.473 -16.848 1.00 21.44 ? 47  ALA A N   1 
ATOM   338  C CA  . ALA A 1 47  ? 54.042 -36.196 -17.110 1.00 21.95 ? 47  ALA A CA  1 
ATOM   339  C C   . ALA A 1 47  ? 52.608 -36.190 -16.574 1.00 22.33 ? 47  ALA A C   1 
ATOM   340  O O   . ALA A 1 47  ? 52.184 -35.223 -15.954 1.00 22.19 ? 47  ALA A O   1 
ATOM   341  C CB  . ALA A 1 47  ? 54.050 -35.883 -18.597 1.00 22.07 ? 47  ALA A CB  1 
ATOM   342  N N   . MET A 1 48  ? 51.871 -37.274 -16.810 1.00 22.43 ? 48  MET A N   1 
ATOM   343  C CA  . MET A 1 48  ? 50.494 -37.375 -16.332 1.00 23.10 ? 48  MET A CA  1 
ATOM   344  C C   . MET A 1 48  ? 50.449 -37.469 -14.807 1.00 22.82 ? 48  MET A C   1 
ATOM   345  O O   . MET A 1 48  ? 49.533 -36.938 -14.178 1.00 23.12 ? 48  MET A O   1 
ATOM   346  C CB  . MET A 1 48  ? 49.777 -38.575 -16.958 1.00 23.62 ? 48  MET A CB  1 
ATOM   347  C CG  . MET A 1 48  ? 49.642 -38.536 -18.475 1.00 24.39 ? 48  MET A CG  1 
ATOM   348  S SD  . MET A 1 48  ? 48.836 -37.057 -19.122 1.00 26.71 ? 48  MET A SD  1 
ATOM   349  C CE  . MET A 1 48  ? 50.230 -35.964 -19.379 1.00 26.77 ? 48  MET A CE  1 
ATOM   350  N N   . TYR A 1 49  ? 51.439 -38.133 -14.218 1.00 22.15 ? 49  TYR A N   1 
ATOM   351  C CA  . TYR A 1 49  ? 51.570 -38.165 -12.766 1.00 22.55 ? 49  TYR A CA  1 
ATOM   352  C C   . TYR A 1 49  ? 51.756 -36.754 -12.209 1.00 23.34 ? 49  TYR A C   1 
ATOM   353  O O   . TYR A 1 49  ? 51.094 -36.370 -11.246 1.00 23.73 ? 49  TYR A O   1 
ATOM   354  C CB  . TYR A 1 49  ? 52.740 -39.057 -12.333 1.00 22.10 ? 49  TYR A CB  1 
ATOM   355  C CG  . TYR A 1 49  ? 53.068 -38.936 -10.860 1.00 22.70 ? 49  TYR A CG  1 
ATOM   356  C CD1 . TYR A 1 49  ? 52.397 -39.704 -9.913  1.00 22.94 ? 49  TYR A CD1 1 
ATOM   357  C CD2 . TYR A 1 49  ? 54.046 -38.047 -10.413 1.00 22.84 ? 49  TYR A CD2 1 
ATOM   358  C CE1 . TYR A 1 49  ? 52.689 -39.590 -8.565  1.00 23.75 ? 49  TYR A CE1 1 
ATOM   359  C CE2 . TYR A 1 49  ? 54.342 -37.927 -9.066  1.00 23.51 ? 49  TYR A CE2 1 
ATOM   360  C CZ  . TYR A 1 49  ? 53.659 -38.701 -8.148  1.00 23.84 ? 49  TYR A CZ  1 
ATOM   361  O OH  . TYR A 1 49  ? 53.952 -38.597 -6.816  1.00 24.85 ? 49  TYR A OH  1 
ATOM   362  N N   . GLU A 1 50  ? 52.660 -35.989 -12.817 1.00 23.44 ? 50  GLU A N   1 
ATOM   363  C CA  . GLU A 1 50  ? 52.938 -34.632 -12.350 1.00 24.29 ? 50  GLU A CA  1 
ATOM   364  C C   . GLU A 1 50  ? 51.743 -33.710 -12.563 1.00 25.10 ? 50  GLU A C   1 
ATOM   365  O O   . GLU A 1 50  ? 51.412 -32.911 -11.683 1.00 25.16 ? 50  GLU A O   1 
ATOM   366  C CB  . GLU A 1 50  ? 54.178 -34.054 -13.029 1.00 24.15 ? 50  GLU A CB  1 
ATOM   367  C CG  . GLU A 1 50  ? 55.468 -34.808 -12.739 1.00 24.00 ? 50  GLU A CG  1 
ATOM   368  C CD  . GLU A 1 50  ? 55.905 -34.753 -11.283 1.00 24.82 ? 50  GLU A CD  1 
ATOM   369  O OE1 . GLU A 1 50  ? 55.272 -34.057 -10.461 1.00 25.31 ? 50  GLU A OE1 1 
ATOM   370  O OE2 . GLU A 1 50  ? 56.904 -35.425 -10.965 1.00 25.44 ? 50  GLU A OE2 1 
ATOM   371  N N   . GLN A 1 51  ? 51.109 -33.819 -13.731 1.00 25.26 ? 51  GLN A N   1 
ATOM   372  C CA  A GLN A 1 51  ? 49.887 -33.080 -14.043 0.50 26.36 ? 51  GLN A CA  1 
ATOM   373  C CA  B GLN A 1 51  ? 49.906 -33.030 -13.994 0.50 26.08 ? 51  GLN A CA  1 
ATOM   374  C C   . GLN A 1 51  ? 48.834 -33.380 -12.971 1.00 26.69 ? 51  GLN A C   1 
ATOM   375  O O   . GLN A 1 51  ? 48.195 -32.483 -12.419 1.00 27.18 ? 51  GLN A O   1 
ATOM   376  C CB  A GLN A 1 51  ? 49.379 -33.515 -15.425 0.50 26.65 ? 51  GLN A CB  1 
ATOM   377  C CB  B GLN A 1 51  ? 49.363 -33.238 -15.408 0.50 26.06 ? 51  GLN A CB  1 
ATOM   378  C CG  A GLN A 1 51  ? 48.561 -32.493 -16.191 0.50 28.01 ? 51  GLN A CG  1 
ATOM   379  C CG  B GLN A 1 51  ? 48.133 -32.381 -15.705 0.50 27.11 ? 51  GLN A CG  1 
ATOM   380  C CD  A GLN A 1 51  ? 48.305 -32.941 -17.621 0.50 28.17 ? 51  GLN A CD  1 
ATOM   381  C CD  B GLN A 1 51  ? 48.390 -30.895 -15.502 0.50 27.95 ? 51  GLN A CD  1 
ATOM   382  O OE1 A GLN A 1 51  ? 47.476 -33.813 -17.868 0.50 28.54 ? 51  GLN A OE1 1 
ATOM   383  O OE1 B GLN A 1 51  ? 49.008 -30.245 -16.340 0.50 28.08 ? 51  GLN A OE1 1 
ATOM   384  N NE2 A GLN A 1 51  ? 49.028 -32.352 -18.568 0.50 28.53 ? 51  GLN A NE2 1 
ATOM   385  N NE2 B GLN A 1 51  ? 47.909 -30.350 -14.389 0.50 28.69 ? 51  GLN A NE2 1 
ATOM   386  N N   . GLY A 1 52  ? 48.658 -34.671 -12.706 1.00 26.10 ? 52  GLY A N   1 
ATOM   387  C CA  . GLY A 1 52  ? 47.715 -35.132 -11.693 1.00 26.81 ? 52  GLY A CA  1 
ATOM   388  C C   . GLY A 1 52  ? 48.020 -34.532 -10.335 1.00 27.41 ? 52  GLY A C   1 
ATOM   389  O O   . GLY A 1 52  ? 47.132 -34.031 -9.654  1.00 28.19 ? 52  GLY A O   1 
ATOM   390  N N   . ARG A 1 53  ? 49.294 -34.559 -9.963  1.00 27.32 ? 53  ARG A N   1 
ATOM   391  C CA  . ARG A 1 53  ? 49.748 -34.033 -8.681  1.00 28.30 ? 53  ARG A CA  1 
ATOM   392  C C   . ARG A 1 53  ? 49.371 -32.557 -8.511  1.00 29.24 ? 53  ARG A C   1 
ATOM   393  O O   . ARG A 1 53  ? 48.879 -32.150 -7.453  1.00 29.47 ? 53  ARG A O   1 
ATOM   394  C CB  . ARG A 1 53  ? 51.262 -34.226 -8.556  1.00 28.24 ? 53  ARG A CB  1 
ATOM   395  C CG  . ARG A 1 53  ? 51.803 -34.081 -7.150  1.00 29.36 ? 53  ARG A CG  1 
ATOM   396  C CD  . ARG A 1 53  ? 53.232 -34.591 -7.072  1.00 28.99 ? 53  ARG A CD  1 
ATOM   397  N NE  . ARG A 1 53  ? 54.127 -33.813 -7.921  1.00 28.75 ? 53  ARG A NE  1 
ATOM   398  C CZ  . ARG A 1 53  ? 54.675 -32.647 -7.584  1.00 29.26 ? 53  ARG A CZ  1 
ATOM   399  N NH1 . ARG A 1 53  ? 55.477 -32.027 -8.442  1.00 28.92 ? 53  ARG A NH1 1 
ATOM   400  N NH2 . ARG A 1 53  ? 54.441 -32.100 -6.394  1.00 30.23 ? 53  ARG A NH2 1 
ATOM   401  N N   . LEU A 1 54  ? 49.566 -31.764 -9.561  1.00 29.21 ? 54  LEU A N   1 
ATOM   402  C CA  . LEU A 1 54  ? 49.189 -30.347 -9.517  1.00 30.48 ? 54  LEU A CA  1 
ATOM   403  C C   . LEU A 1 54  ? 47.675 -30.129 -9.488  1.00 31.30 ? 54  LEU A C   1 
ATOM   404  O O   . LEU A 1 54  ? 47.224 -29.072 -9.072  1.00 32.66 ? 54  LEU A O   1 
ATOM   405  C CB  . LEU A 1 54  ? 49.801 -29.574 -10.693 1.00 30.36 ? 54  LEU A CB  1 
ATOM   406  C CG  . LEU A 1 54  ? 51.331 -29.528 -10.786 1.00 29.92 ? 54  LEU A CG  1 
ATOM   407  C CD1 . LEU A 1 54  ? 51.766 -28.463 -11.785 1.00 30.12 ? 54  LEU A CD1 1 
ATOM   408  C CD2 . LEU A 1 54  ? 51.978 -29.275 -9.433  1.00 30.47 ? 54  LEU A CD2 1 
ATOM   409  N N   . LEU A 1 55  ? 46.900 -31.117 -9.931  1.00 30.94 ? 55  LEU A N   1 
ATOM   410  C CA  . LEU A 1 55  ? 45.436 -31.043 -9.863  1.00 31.90 ? 55  LEU A CA  1 
ATOM   411  C C   . LEU A 1 55  ? 44.864 -31.412 -8.490  1.00 32.52 ? 55  LEU A C   1 
ATOM   412  O O   . LEU A 1 55  ? 43.678 -31.200 -8.246  1.00 33.23 ? 55  LEU A O   1 
ATOM   413  C CB  . LEU A 1 55  ? 44.800 -31.950 -10.923 1.00 31.54 ? 55  LEU A CB  1 
ATOM   414  C CG  . LEU A 1 55  ? 44.868 -31.478 -12.375 1.00 31.69 ? 55  LEU A CG  1 
ATOM   415  C CD1 . LEU A 1 55  ? 44.421 -32.597 -13.300 1.00 31.16 ? 55  LEU A CD1 1 
ATOM   416  C CD2 . LEU A 1 55  ? 44.026 -30.231 -12.594 1.00 33.12 ? 55  LEU A CD2 1 
ATOM   417  N N   . ARG A 1 56  ? 45.693 -31.952 -7.600  1.00 34.16 ? 56  ARG A N   1 
ATOM   418  C CA  . ARG A 1 56  ? 45.213 -32.452 -6.305  1.00 34.38 ? 56  ARG A CA  1 
ATOM   419  C C   . ARG A 1 56  ? 44.548 -31.387 -5.440  1.00 36.38 ? 56  ARG A C   1 
ATOM   420  O O   . ARG A 1 56  ? 43.619 -31.696 -4.695  1.00 36.17 ? 56  ARG A O   1 
ATOM   421  C CB  . ARG A 1 56  ? 46.342 -33.129 -5.532  1.00 33.81 ? 56  ARG A CB  1 
ATOM   422  C CG  . ARG A 1 56  ? 46.753 -34.453 -6.151  1.00 32.09 ? 56  ARG A CG  1 
ATOM   423  C CD  . ARG A 1 56  ? 47.959 -35.055 -5.461  1.00 31.96 ? 56  ARG A CD  1 
ATOM   424  N NE  . ARG A 1 56  ? 48.470 -36.206 -6.200  1.00 30.53 ? 56  ARG A NE  1 
ATOM   425  C CZ  . ARG A 1 56  ? 49.465 -36.987 -5.795  1.00 30.32 ? 56  ARG A CZ  1 
ATOM   426  N NH1 . ARG A 1 56  ? 50.065 -36.773 -4.627  1.00 31.34 ? 56  ARG A NH1 1 
ATOM   427  N NH2 . ARG A 1 56  ? 49.855 -37.998 -6.559  1.00 29.34 ? 56  ARG A NH2 1 
ATOM   428  N N   . ASN A 1 57  ? 45.014 -30.144 -5.557  1.00 38.43 ? 57  ASN A N   1 
ATOM   429  C CA  . ASN A 1 57  ? 44.436 -29.017 -4.823  1.00 40.94 ? 57  ASN A CA  1 
ATOM   430  C C   . ASN A 1 57  ? 43.422 -28.209 -5.639  1.00 41.09 ? 57  ASN A C   1 
ATOM   431  O O   . ASN A 1 57  ? 43.377 -26.984 -5.552  1.00 43.44 ? 57  ASN A O   1 
ATOM   432  C CB  . ASN A 1 57  ? 45.547 -28.099 -4.291  1.00 43.34 ? 57  ASN A CB  1 
ATOM   433  C CG  . ASN A 1 57  ? 45.766 -28.262 -2.803  1.00 45.18 ? 57  ASN A CG  1 
ATOM   434  O OD1 . ASN A 1 57  ? 45.992 -29.372 -2.316  1.00 45.87 ? 57  ASN A OD1 1 
ATOM   435  N ND2 . ASN A 1 57  ? 45.690 -27.161 -2.070  1.00 47.57 ? 57  ASN A ND2 1 
ATOM   436  N N   . THR A 1 58  ? 42.613 -28.903 -6.428  1.00 39.22 ? 58  THR A N   1 
ATOM   437  C CA  . THR A 1 58  ? 41.512 -28.289 -7.152  1.00 39.11 ? 58  THR A CA  1 
ATOM   438  C C   . THR A 1 58  ? 40.253 -29.063 -6.803  1.00 38.41 ? 58  THR A C   1 
ATOM   439  O O   . THR A 1 58  ? 40.316 -30.080 -6.108  1.00 37.20 ? 58  THR A O   1 
ATOM   440  C CB  . THR A 1 58  ? 41.723 -28.362 -8.675  1.00 38.15 ? 58  THR A CB  1 
ATOM   441  O OG1 . THR A 1 58  ? 41.702 -29.732 -9.096  1.00 36.25 ? 58  THR A OG1 1 
ATOM   442  C CG2 . THR A 1 58  ? 43.047 -27.729 -9.074  1.00 38.62 ? 58  THR A CG2 1 
ATOM   443  N N   . GLU A 1 59  ? 39.116 -28.596 -7.304  1.00 38.95 ? 59  GLU A N   1 
ATOM   444  C CA  . GLU A 1 59  ? 37.862 -29.319 -7.133  1.00 38.66 ? 59  GLU A CA  1 
ATOM   445  C C   . GLU A 1 59  ? 37.970 -30.718 -7.747  1.00 35.89 ? 59  GLU A C   1 
ATOM   446  O O   . GLU A 1 59  ? 37.495 -31.691 -7.166  1.00 34.88 ? 59  GLU A O   1 
ATOM   447  C CB  . GLU A 1 59  ? 36.702 -28.544 -7.764  1.00 40.69 ? 59  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 59  ? 35.325 -29.010 -7.318  1.00 41.99 ? 59  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 59  ? 35.087 -28.833 -5.827  1.00 44.05 ? 59  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 59  ? 35.706 -27.933 -5.213  1.00 46.51 ? 59  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 59  ? 34.269 -29.597 -5.268  1.00 45.02 ? 59  GLU A OE2 1 
ATOM   452  N N   . ARG A 1 60  ? 38.608 -30.816 -8.912  1.00 34.13 ? 60  ARG A N   1 
ATOM   453  C CA  . ARG A 1 60  ? 38.816 -32.110 -9.549  1.00 32.05 ? 60  ARG A CA  1 
ATOM   454  C C   . ARG A 1 60  ? 39.697 -33.017 -8.689  1.00 30.88 ? 60  ARG A C   1 
ATOM   455  O O   . ARG A 1 60  ? 39.492 -34.228 -8.652  1.00 29.72 ? 60  ARG A O   1 
ATOM   456  C CB  . ARG A 1 60  ? 39.426 -31.946 -10.947 1.00 31.53 ? 60  ARG A CB  1 
ATOM   457  C CG  . ARG A 1 60  ? 39.678 -33.258 -11.687 1.00 30.20 ? 60  ARG A CG  1 
ATOM   458  C CD  . ARG A 1 60  ? 38.386 -34.021 -11.927 1.00 29.58 ? 60  ARG A CD  1 
ATOM   459  N NE  . ARG A 1 60  ? 38.593 -35.343 -12.519 1.00 28.44 ? 60  ARG A NE  1 
ATOM   460  C CZ  . ARG A 1 60  ? 38.745 -36.483 -11.842 1.00 27.76 ? 60  ARG A CZ  1 
ATOM   461  N NH1 . ARG A 1 60  ? 38.755 -36.509 -10.509 1.00 27.98 ? 60  ARG A NH1 1 
ATOM   462  N NH2 . ARG A 1 60  ? 38.900 -37.618 -12.510 1.00 27.19 ? 60  ARG A NH2 1 
ATOM   463  N N   . GLY A 1 61  ? 40.679 -32.427 -8.018  1.00 31.30 ? 61  GLY A N   1 
ATOM   464  C CA  . GLY A 1 61  ? 41.522 -33.151 -7.073  1.00 31.11 ? 61  GLY A CA  1 
ATOM   465  C C   . GLY A 1 61  ? 40.758 -33.673 -5.870  1.00 31.19 ? 61  GLY A C   1 
ATOM   466  O O   . GLY A 1 61  ? 41.011 -34.782 -5.407  1.00 30.17 ? 61  GLY A O   1 
ATOM   467  N N   . LYS A 1 62  ? 39.830 -32.870 -5.358  1.00 32.43 ? 62  LYS A N   1 
ATOM   468  C CA  . LYS A 1 62  ? 38.966 -33.300 -4.256  1.00 33.03 ? 62  LYS A CA  1 
ATOM   469  C C   . LYS A 1 62  ? 38.158 -34.525 -4.679  1.00 31.61 ? 62  LYS A C   1 
ATOM   470  O O   . LYS A 1 62  ? 38.085 -35.509 -3.945  1.00 31.03 ? 62  LYS A O   1 
ATOM   471  C CB  . LYS A 1 62  ? 38.039 -32.164 -3.815  1.00 34.87 ? 62  LYS A CB  1 
ATOM   472  C CG  . LYS A 1 62  ? 37.143 -32.498 -2.628  1.00 35.98 ? 62  LYS A CG  1 
ATOM   473  C CD  . LYS A 1 62  ? 36.370 -31.269 -2.173  1.00 37.98 ? 62  LYS A CD  1 
ATOM   474  C CE  . LYS A 1 62  ? 35.449 -31.570 -1.001  1.00 39.14 ? 62  LYS A CE  1 
ATOM   475  N NZ  . LYS A 1 62  ? 34.360 -32.520 -1.365  1.00 38.56 ? 62  LYS A NZ  1 
ATOM   476  N N   . LEU A 1 63  ? 37.574 -34.466 -5.875  1.00 30.91 ? 63  LEU A N   1 
ATOM   477  C CA  . LEU A 1 63  ? 36.861 -35.609 -6.433  1.00 29.82 ? 63  LEU A CA  1 
ATOM   478  C C   . LEU A 1 63  ? 37.786 -36.815 -6.592  1.00 28.43 ? 63  LEU A C   1 
ATOM   479  O O   . LEU A 1 63  ? 37.385 -37.942 -6.312  1.00 27.74 ? 63  LEU A O   1 
ATOM   480  C CB  . LEU A 1 63  ? 36.218 -35.262 -7.784  1.00 29.79 ? 63  LEU A CB  1 
ATOM   481  C CG  . LEU A 1 63  ? 35.513 -36.423 -8.502  1.00 29.18 ? 63  LEU A CG  1 
ATOM   482  C CD1 . LEU A 1 63  ? 34.382 -36.995 -7.655  1.00 29.58 ? 63  LEU A CD1 1 
ATOM   483  C CD2 . LEU A 1 63  ? 34.999 -35.994 -9.870  1.00 29.46 ? 63  LEU A CD2 1 
ATOM   484  N N   . ALA A 1 64  ? 39.016 -36.578 -7.044  1.00 27.89 ? 64  ALA A N   1 
ATOM   485  C CA  . ALA A 1 64  ? 39.986 -37.658 -7.209  1.00 27.06 ? 64  ALA A CA  1 
ATOM   486  C C   . ALA A 1 64  ? 40.285 -38.369 -5.886  1.00 27.18 ? 64  ALA A C   1 
ATOM   487  O O   . ALA A 1 64  ? 40.310 -39.594 -5.837  1.00 26.48 ? 64  ALA A O   1 
ATOM   488  C CB  . ALA A 1 64  ? 41.272 -37.144 -7.843  1.00 27.00 ? 64  ALA A CB  1 
ATOM   489  N N   . ALA A 1 65  ? 40.503 -37.596 -4.827  1.00 28.48 ? 65  ALA A N   1 
ATOM   490  C CA  . ALA A 1 65  ? 40.747 -38.157 -3.490  1.00 29.41 ? 65  ALA A CA  1 
ATOM   491  C C   . ALA A 1 65  ? 39.557 -38.984 -3.000  1.00 29.58 ? 65  ALA A C   1 
ATOM   492  O O   . ALA A 1 65  ? 39.731 -40.064 -2.437  1.00 29.50 ? 65  ALA A O   1 
ATOM   493  C CB  . ALA A 1 65  ? 41.066 -37.047 -2.497  1.00 30.73 ? 65  ALA A CB  1 
ATOM   494  N N   . GLU A 1 66  ? 38.351 -38.474 -3.230  1.00 30.18 ? 66  GLU A N   1 
ATOM   495  C CA  . GLU A 1 66  ? 37.125 -39.190 -2.871  1.00 30.44 ? 66  GLU A CA  1 
ATOM   496  C C   . GLU A 1 66  ? 36.975 -40.473 -3.686  1.00 29.33 ? 66  GLU A C   1 
ATOM   497  O O   . GLU A 1 66  ? 36.658 -41.526 -3.136  1.00 29.17 ? 66  GLU A O   1 
ATOM   498  C CB  . GLU A 1 66  ? 35.909 -38.281 -3.057  1.00 31.26 ? 66  GLU A CB  1 
ATOM   499  C CG  . GLU A 1 66  ? 35.885 -37.131 -2.063  1.00 33.06 ? 66  GLU A CG  1 
ATOM   500  C CD  . GLU A 1 66  ? 34.911 -36.027 -2.424  1.00 34.05 ? 66  GLU A CD  1 
ATOM   501  O OE1 . GLU A 1 66  ? 34.771 -35.093 -1.610  1.00 35.67 ? 66  GLU A OE1 1 
ATOM   502  O OE2 . GLU A 1 66  ? 34.293 -36.078 -3.508  1.00 33.83 ? 66  GLU A OE2 1 
ATOM   503  N N   . ASP A 1 67  ? 37.224 -40.385 -4.990  1.00 28.62 ? 67  ASP A N   1 
ATOM   504  C CA  . ASP A 1 67  ? 37.229 -41.562 -5.856  1.00 27.85 ? 67  ASP A CA  1 
ATOM   505  C C   . ASP A 1 67  ? 38.276 -42.582 -5.410  1.00 27.71 ? 67  ASP A C   1 
ATOM   506  O O   . ASP A 1 67  ? 38.017 -43.784 -5.427  1.00 26.95 ? 67  ASP A O   1 
ATOM   507  C CB  . ASP A 1 67  ? 37.499 -41.174 -7.316  1.00 27.34 ? 67  ASP A CB  1 
ATOM   508  C CG  . ASP A 1 67  ? 36.282 -40.588 -8.013  1.00 27.78 ? 67  ASP A CG  1 
ATOM   509  O OD1 . ASP A 1 67  ? 35.175 -40.571 -7.422  1.00 28.53 ? 67  ASP A OD1 1 
ATOM   510  O OD2 . ASP A 1 67  ? 36.434 -40.143 -9.171  1.00 27.21 ? 67  ASP A OD2 1 
ATOM   511  N N   . ALA A 1 68  ? 39.455 -42.096 -5.024  1.00 28.00 ? 68  ALA A N   1 
ATOM   512  C CA  . ALA A 1 68  ? 40.543 -42.962 -4.568  1.00 28.08 ? 68  ALA A CA  1 
ATOM   513  C C   . ALA A 1 68  ? 40.218 -43.673 -3.248  1.00 28.79 ? 68  ALA A C   1 
ATOM   514  O O   . ALA A 1 68  ? 40.803 -44.715 -2.950  1.00 28.80 ? 68  ALA A O   1 
ATOM   515  C CB  . ALA A 1 68  ? 41.831 -42.160 -4.428  1.00 28.68 ? 68  ALA A CB  1 
ATOM   516  N N   . ASN A 1 69  ? 39.306 -43.104 -2.458  1.00 29.46 ? 69  ASN A N   1 
ATOM   517  C CA  . ASN A 1 69  ? 38.810 -43.761 -1.239  1.00 30.34 ? 69  ASN A CA  1 
ATOM   518  C C   . ASN A 1 69  ? 37.903 -44.967 -1.524  1.00 30.01 ? 69  ASN A C   1 
ATOM   519  O O   . ASN A 1 69  ? 37.671 -45.791 -0.639  1.00 30.51 ? 69  ASN A O   1 
ATOM   520  C CB  . ASN A 1 69  ? 38.026 -42.780 -0.359  1.00 31.43 ? 69  ASN A CB  1 
ATOM   521  C CG  . ASN A 1 69  ? 38.907 -41.771 0.355   1.00 32.52 ? 69  ASN A CG  1 
ATOM   522  O OD1 . ASN A 1 69  ? 40.114 -41.957 0.493   1.00 32.60 ? 69  ASN A OD1 1 
ATOM   523  N ND2 . ASN A 1 69  ? 38.290 -40.697 0.835   1.00 33.45 ? 69  ASN A ND2 1 
ATOM   524  N N   . LEU A 1 70  ? 37.371 -45.054 -2.741  1.00 29.15 ? 70  LEU A N   1 
ATOM   525  C CA  . LEU A 1 70  ? 36.448 -46.126 -3.096  1.00 29.04 ? 70  LEU A CA  1 
ATOM   526  C C   . LEU A 1 70  ? 37.130 -47.490 -3.102  1.00 28.85 ? 70  LEU A C   1 
ATOM   527  O O   . LEU A 1 70  ? 38.211 -47.650 -3.669  1.00 28.17 ? 70  LEU A O   1 
ATOM   528  C CB  . LEU A 1 70  ? 35.826 -45.877 -4.474  1.00 28.55 ? 70  LEU A CB  1 
ATOM   529  C CG  . LEU A 1 70  ? 34.937 -44.643 -4.650  1.00 29.00 ? 70  LEU A CG  1 
ATOM   530  C CD1 . LEU A 1 70  ? 34.576 -44.470 -6.116  1.00 28.55 ? 70  LEU A CD1 1 
ATOM   531  C CD2 . LEU A 1 70  ? 33.677 -44.751 -3.807  1.00 30.08 ? 70  LEU A CD2 1 
ATOM   532  N N   . SER A 1 71  ? 36.491 -48.465 -2.458  1.00 29.38 ? 71  SER A N   1 
ATOM   533  C CA  . SER A 1 71  ? 36.848 -49.868 -2.622  1.00 29.33 ? 71  SER A CA  1 
ATOM   534  C C   . SER A 1 71  ? 36.145 -50.367 -3.880  1.00 28.54 ? 71  SER A C   1 
ATOM   535  O O   . SER A 1 71  ? 35.329 -49.651 -4.461  1.00 27.99 ? 71  SER A O   1 
ATOM   536  C CB  . SER A 1 71  ? 36.405 -50.684 -1.407  1.00 30.39 ? 71  SER A CB  1 
ATOM   537  O OG  . SER A 1 71  ? 35.000 -50.598 -1.225  1.00 30.79 ? 71  SER A OG  1 
ATOM   538  N N   . ALA A 1 72  ? 36.447 -51.591 -4.294  1.00 28.40 ? 72  ALA A N   1 
ATOM   539  C CA  . ALA A 1 72  ? 35.799 -52.179 -5.467  1.00 28.10 ? 72  ALA A CA  1 
ATOM   540  C C   . ALA A 1 72  ? 34.270 -52.186 -5.321  1.00 28.54 ? 72  ALA A C   1 
ATOM   541  O O   . ALA A 1 72  ? 33.543 -51.934 -6.286  1.00 28.24 ? 72  ALA A O   1 
ATOM   542  C CB  . ALA A 1 72  ? 36.317 -53.589 -5.702  1.00 28.40 ? 72  ALA A CB  1 
ATOM   543  N N   . GLY A 1 73  ? 33.801 -52.458 -4.106  1.00 29.16 ? 73  GLY A N   1 
ATOM   544  C CA  . GLY A 1 73  ? 32.376 -52.501 -3.797  1.00 29.73 ? 73  GLY A CA  1 
ATOM   545  C C   . GLY A 1 73  ? 31.661 -51.164 -3.837  1.00 29.75 ? 73  GLY A C   1 
ATOM   546  O O   . GLY A 1 73  ? 30.440 -51.125 -3.975  1.00 30.07 ? 73  GLY A O   1 
ATOM   547  N N   . GLY A 1 74  ? 32.412 -50.071 -3.708  1.00 29.65 ? 74  GLY A N   1 
ATOM   548  C CA  . GLY A 1 74  ? 31.851 -48.722 -3.741  1.00 29.67 ? 74  GLY A CA  1 
ATOM   549  C C   . GLY A 1 74  ? 31.694 -48.149 -5.141  1.00 28.97 ? 74  GLY A C   1 
ATOM   550  O O   . GLY A 1 74  ? 31.078 -47.100 -5.317  1.00 29.08 ? 74  GLY A O   1 
ATOM   551  N N   . VAL A 1 75  ? 32.241 -48.832 -6.142  1.00 28.42 ? 75  VAL A N   1 
ATOM   552  C CA  . VAL A 1 75  ? 32.196 -48.336 -7.516  1.00 27.91 ? 75  VAL A CA  1 
ATOM   553  C C   . VAL A 1 75  ? 30.753 -48.178 -8.005  1.00 28.19 ? 75  VAL A C   1 
ATOM   554  O O   . VAL A 1 75  ? 30.399 -47.132 -8.547  1.00 27.98 ? 75  VAL A O   1 
ATOM   555  C CB  . VAL A 1 75  ? 33.011 -49.233 -8.472  1.00 27.43 ? 75  VAL A CB  1 
ATOM   556  C CG1 . VAL A 1 75  ? 32.770 -48.846 -9.928  1.00 27.14 ? 75  VAL A CG1 1 
ATOM   557  C CG2 . VAL A 1 75  ? 34.494 -49.127 -8.138  1.00 27.25 ? 75  VAL A CG2 1 
ATOM   558  N N   . ALA A 1 76  ? 29.922 -49.196 -7.787  1.00 28.45 ? 76  ALA A N   1 
ATOM   559  C CA  . ALA A 1 76  ? 28.529 -49.159 -8.245  1.00 28.94 ? 76  ALA A CA  1 
ATOM   560  C C   . ALA A 1 76  ? 27.823 -47.875 -7.812  1.00 29.51 ? 76  ALA A C   1 
ATOM   561  O O   . ALA A 1 76  ? 27.266 -47.148 -8.640  1.00 29.59 ? 76  ALA A O   1 
ATOM   562  C CB  . ALA A 1 76  ? 27.767 -50.374 -7.735  1.00 29.56 ? 76  ALA A CB  1 
ATOM   563  N N   . ASN A 1 77  ? 27.858 -47.597 -6.514  1.00 29.93 ? 77  ASN A N   1 
ATOM   564  C CA  . ASN A 1 77  ? 27.197 -46.417 -5.966  1.00 30.72 ? 77  ASN A CA  1 
ATOM   565  C C   . ASN A 1 77  ? 27.797 -45.105 -6.475  1.00 30.21 ? 77  ASN A C   1 
ATOM   566  O O   . ASN A 1 77  ? 27.100 -44.096 -6.575  1.00 30.37 ? 77  ASN A O   1 
ATOM   567  C CB  . ASN A 1 77  ? 27.236 -46.444 -4.441  1.00 31.75 ? 77  ASN A CB  1 
ATOM   568  C CG  . ASN A 1 77  ? 26.656 -45.191 -3.828  1.00 32.96 ? 77  ASN A CG  1 
ATOM   569  O OD1 . ASN A 1 77  ? 27.381 -44.378 -3.263  1.00 33.84 ? 77  ASN A OD1 1 
ATOM   570  N ND2 . ASN A 1 77  ? 25.349 -45.012 -3.966  1.00 33.68 ? 77  ASN A ND2 1 
ATOM   571  N N   . ALA A 1 78  ? 29.086 -45.134 -6.807  1.00 29.34 ? 78  ALA A N   1 
ATOM   572  C CA  . ALA A 1 78  ? 29.783 -43.952 -7.313  1.00 28.97 ? 78  ALA A CA  1 
ATOM   573  C C   . ALA A 1 78  ? 29.250 -43.464 -8.666  1.00 28.59 ? 78  ALA A C   1 
ATOM   574  O O   . ALA A 1 78  ? 29.581 -42.358 -9.093  1.00 28.92 ? 78  ALA A O   1 
ATOM   575  C CB  . ALA A 1 78  ? 31.280 -44.220 -7.399  1.00 28.35 ? 78  ALA A CB  1 
ATOM   576  N N   . PHE A 1 79  ? 28.438 -44.283 -9.334  1.00 27.93 ? 79  PHE A N   1 
ATOM   577  C CA  . PHE A 1 79  ? 27.804 -43.899 -10.598 1.00 27.73 ? 79  PHE A CA  1 
ATOM   578  C C   . PHE A 1 79  ? 26.435 -43.227 -10.430 1.00 28.37 ? 79  PHE A C   1 
ATOM   579  O O   . PHE A 1 79  ? 25.826 -42.834 -11.425 1.00 28.40 ? 79  PHE A O   1 
ATOM   580  C CB  . PHE A 1 79  ? 27.633 -45.130 -11.497 1.00 27.18 ? 79  PHE A CB  1 
ATOM   581  C CG  . PHE A 1 79  ? 28.863 -45.502 -12.262 1.00 26.23 ? 79  PHE A CG  1 
ATOM   582  C CD1 . PHE A 1 79  ? 29.797 -46.368 -11.720 1.00 25.76 ? 79  PHE A CD1 1 
ATOM   583  C CD2 . PHE A 1 79  ? 29.072 -45.007 -13.542 1.00 26.06 ? 79  PHE A CD2 1 
ATOM   584  C CE1 . PHE A 1 79  ? 30.927 -46.725 -12.434 1.00 25.12 ? 79  PHE A CE1 1 
ATOM   585  C CE2 . PHE A 1 79  ? 30.202 -45.356 -14.258 1.00 25.40 ? 79  PHE A CE2 1 
ATOM   586  C CZ  . PHE A 1 79  ? 31.128 -46.215 -13.705 1.00 25.08 ? 79  PHE A CZ  1 
ATOM   587  N N   . SER A 1 80  ? 25.961 -43.082 -9.191  1.00 28.65 ? 80  SER A N   1 
ATOM   588  C CA  . SER A 1 80  ? 24.583 -42.646 -8.932  1.00 29.54 ? 80  SER A CA  1 
ATOM   589  C C   . SER A 1 80  ? 24.190 -41.337 -9.623  1.00 30.08 ? 80  SER A C   1 
ATOM   590  O O   . SER A 1 80  ? 23.153 -41.276 -10.290 1.00 30.26 ? 80  SER A O   1 
ATOM   591  C CB  . SER A 1 80  ? 24.328 -42.531 -7.425  1.00 30.21 ? 80  SER A CB  1 
ATOM   592  O OG  . SER A 1 80  ? 24.356 -43.811 -6.812  1.00 30.08 ? 80  SER A OG  1 
ATOM   593  N N   . SER A 1 81  ? 25.012 -40.300 -9.464  1.00 30.10 ? 81  SER A N   1 
ATOM   594  C CA  A SER A 1 81  ? 24.719 -38.995 -10.057 0.50 30.84 ? 81  SER A CA  1 
ATOM   595  C CA  B SER A 1 81  ? 24.724 -38.994 -10.057 0.50 30.89 ? 81  SER A CA  1 
ATOM   596  C C   . SER A 1 81  ? 24.707 -39.067 -11.583 1.00 30.54 ? 81  SER A C   1 
ATOM   597  O O   . SER A 1 81  ? 23.829 -38.504 -12.229 1.00 31.28 ? 81  SER A O   1 
ATOM   598  C CB  A SER A 1 81  ? 25.728 -37.948 -9.586  0.50 30.99 ? 81  SER A CB  1 
ATOM   599  C CB  B SER A 1 81  ? 25.749 -37.956 -9.602  0.50 31.09 ? 81  SER A CB  1 
ATOM   600  O OG  A SER A 1 81  ? 25.561 -37.680 -8.206  0.50 31.54 ? 81  SER A OG  1 
ATOM   601  O OG  B SER A 1 81  ? 25.389 -36.664 -10.059 0.50 32.04 ? 81  SER A OG  1 
ATOM   602  N N   . ALA A 1 82  ? 25.685 -39.763 -12.152 1.00 29.64 ? 82  ALA A N   1 
ATOM   603  C CA  . ALA A 1 82  ? 25.752 -39.949 -13.601 1.00 29.55 ? 82  ALA A CA  1 
ATOM   604  C C   . ALA A 1 82  ? 24.562 -40.764 -14.111 1.00 29.99 ? 82  ALA A C   1 
ATOM   605  O O   . ALA A 1 82  ? 23.996 -40.465 -15.162 1.00 30.71 ? 82  ALA A O   1 
ATOM   606  C CB  . ALA A 1 82  ? 27.052 -40.635 -13.980 1.00 28.53 ? 82  ALA A CB  1 
ATOM   607  N N   . PHE A 1 83  ? 24.182 -41.783 -13.347 1.00 29.93 ? 83  PHE A N   1 
ATOM   608  C CA  . PHE A 1 83  ? 23.078 -42.672 -13.698 1.00 30.24 ? 83  PHE A CA  1 
ATOM   609  C C   . PHE A 1 83  ? 21.713 -41.980 -13.602 1.00 31.57 ? 83  PHE A C   1 
ATOM   610  O O   . PHE A 1 83  ? 20.774 -42.346 -14.312 1.00 31.87 ? 83  PHE A O   1 
ATOM   611  C CB  . PHE A 1 83  ? 23.123 -43.893 -12.780 1.00 29.95 ? 83  PHE A CB  1 
ATOM   612  C CG  . PHE A 1 83  ? 22.181 -44.990 -13.170 1.00 30.32 ? 83  PHE A CG  1 
ATOM   613  C CD1 . PHE A 1 83  ? 22.427 -45.764 -14.294 1.00 30.02 ? 83  PHE A CD1 1 
ATOM   614  C CD2 . PHE A 1 83  ? 21.061 -45.266 -12.400 1.00 31.23 ? 83  PHE A CD2 1 
ATOM   615  C CE1 . PHE A 1 83  ? 21.564 -46.784 -14.653 1.00 30.53 ? 83  PHE A CE1 1 
ATOM   616  C CE2 . PHE A 1 83  ? 20.192 -46.283 -12.751 1.00 31.64 ? 83  PHE A CE2 1 
ATOM   617  C CZ  . PHE A 1 83  ? 20.445 -47.047 -13.877 1.00 31.35 ? 83  PHE A CZ  1 
ATOM   618  N N   . GLY A 1 84  ? 21.611 -40.988 -12.721 1.00 32.24 ? 84  GLY A N   1 
ATOM   619  C CA  . GLY A 1 84  ? 20.388 -40.206 -12.556 1.00 33.70 ? 84  GLY A CA  1 
ATOM   620  C C   . GLY A 1 84  ? 19.509 -40.652 -11.398 1.00 34.48 ? 84  GLY A C   1 
ATOM   621  O O   . GLY A 1 84  ? 18.475 -40.043 -11.137 1.00 35.50 ? 84  GLY A O   1 
ATOM   622  N N   . SER A 1 85  ? 19.908 -41.720 -10.712 1.00 34.06 ? 85  SER A N   1 
ATOM   623  C CA  . SER A 1 85  ? 19.170 -42.215 -9.552  1.00 34.80 ? 85  SER A CA  1 
ATOM   624  C C   . SER A 1 85  ? 20.093 -43.044 -8.658  1.00 34.07 ? 85  SER A C   1 
ATOM   625  O O   . SER A 1 85  ? 21.141 -43.520 -9.119  1.00 32.81 ? 85  SER A O   1 
ATOM   626  C CB  . SER A 1 85  ? 17.964 -43.045 -9.995  1.00 35.49 ? 85  SER A CB  1 
ATOM   627  O OG  . SER A 1 85  ? 18.371 -44.142 -10.788 1.00 34.90 ? 85  SER A OG  1 
ATOM   628  N N   . PRO A 1 86  ? 19.716 -43.217 -7.376  1.00 34.52 ? 86  PRO A N   1 
ATOM   629  C CA  . PRO A 1 86  ? 20.622 -43.890 -6.448  1.00 33.85 ? 86  PRO A CA  1 
ATOM   630  C C   . PRO A 1 86  ? 20.895 -45.343 -6.819  1.00 32.94 ? 86  PRO A C   1 
ATOM   631  O O   . PRO A 1 86  ? 19.962 -46.128 -6.998  1.00 33.46 ? 86  PRO A O   1 
ATOM   632  C CB  . PRO A 1 86  ? 19.885 -43.812 -5.100  1.00 35.04 ? 86  PRO A CB  1 
ATOM   633  C CG  . PRO A 1 86  ? 18.857 -42.751 -5.262  1.00 36.17 ? 86  PRO A CG  1 
ATOM   634  C CD  . PRO A 1 86  ? 18.479 -42.770 -6.709  1.00 35.92 ? 86  PRO A CD  1 
ATOM   635  N N   . ILE A 1 87  ? 22.172 -45.685 -6.943  1.00 31.78 ? 87  ILE A N   1 
ATOM   636  C CA  . ILE A 1 87  ? 22.578 -47.069 -7.108  1.00 31.09 ? 87  ILE A CA  1 
ATOM   637  C C   . ILE A 1 87  ? 23.002 -47.569 -5.735  1.00 31.28 ? 87  ILE A C   1 
ATOM   638  O O   . ILE A 1 87  ? 24.174 -47.509 -5.357  1.00 30.73 ? 87  ILE A O   1 
ATOM   639  C CB  . ILE A 1 87  ? 23.707 -47.229 -8.135  1.00 29.99 ? 87  ILE A CB  1 
ATOM   640  C CG1 . ILE A 1 87  ? 23.271 -46.647 -9.484  1.00 29.96 ? 87  ILE A CG1 1 
ATOM   641  C CG2 . ILE A 1 87  ? 24.066 -48.702 -8.293  1.00 29.64 ? 87  ILE A CG2 1 
ATOM   642  C CD1 . ILE A 1 87  ? 24.407 -46.483 -10.470 1.00 29.19 ? 87  ILE A CD1 1 
ATOM   643  N N   . THR A 1 88  ? 22.017 -48.049 -4.991  1.00 31.95 ? 88  THR A N   1 
ATOM   644  C CA  . THR A 1 88  ? 22.217 -48.500 -3.627  1.00 32.65 ? 88  THR A CA  1 
ATOM   645  C C   . THR A 1 88  ? 21.486 -49.818 -3.409  1.00 33.34 ? 88  THR A C   1 
ATOM   646  O O   . THR A 1 88  ? 20.614 -50.198 -4.190  1.00 33.27 ? 88  THR A O   1 
ATOM   647  C CB  . THR A 1 88  ? 21.657 -47.480 -2.619  1.00 33.62 ? 88  THR A CB  1 
ATOM   648  O OG1 . THR A 1 88  ? 20.253 -47.316 -2.846  1.00 34.27 ? 88  THR A OG1 1 
ATOM   649  C CG2 . THR A 1 88  ? 22.353 -46.131 -2.751  1.00 33.30 ? 88  THR A CG2 1 
ATOM   650  N N   . GLU A 1 89  ? 21.835 -50.500 -2.328  1.00 34.00 ? 89  GLU A N   1 
ATOM   651  C CA  . GLU A 1 89  ? 21.133 -51.712 -1.939  1.00 35.16 ? 89  GLU A CA  1 
ATOM   652  C C   . GLU A 1 89  ? 19.705 -51.362 -1.512  1.00 36.49 ? 89  GLU A C   1 
ATOM   653  O O   . GLU A 1 89  ? 18.777 -52.135 -1.735  1.00 37.08 ? 89  GLU A O   1 
ATOM   654  C CB  . GLU A 1 89  ? 21.895 -52.426 -0.823  1.00 35.65 ? 89  GLU A CB  1 
ATOM   655  C CG  . GLU A 1 89  ? 23.277 -52.893 -1.259  1.00 34.78 ? 89  GLU A CG  1 
ATOM   656  C CD  . GLU A 1 89  ? 24.044 -53.602 -0.164  1.00 35.49 ? 89  GLU A CD  1 
ATOM   657  O OE1 . GLU A 1 89  ? 24.765 -54.568 -0.481  1.00 35.94 ? 89  GLU A OE1 1 
ATOM   658  O OE2 . GLU A 1 89  ? 23.935 -53.211 1.012   1.00 36.14 ? 89  GLU A OE2 1 
ATOM   659  N N   . LYS A 1 90  ? 19.545 -50.176 -0.927  1.00 37.28 ? 90  LYS A N   1 
ATOM   660  C CA  . LYS A 1 90  ? 18.239 -49.657 -0.513  1.00 38.82 ? 90  LYS A CA  1 
ATOM   661  C C   . LYS A 1 90  ? 17.286 -49.441 -1.691  1.00 38.50 ? 90  LYS A C   1 
ATOM   662  O O   . LYS A 1 90  ? 16.156 -49.928 -1.682  1.00 39.27 ? 90  LYS A O   1 
ATOM   663  C CB  . LYS A 1 90  ? 18.434 -48.323 0.223   1.00 39.73 ? 90  LYS A CB  1 
ATOM   664  C CG  . LYS A 1 90  ? 17.156 -47.623 0.657   1.00 41.53 ? 90  LYS A CG  1 
ATOM   665  C CD  . LYS A 1 90  ? 17.477 -46.378 1.471   1.00 42.60 ? 90  LYS A CD  1 
ATOM   666  C CE  . LYS A 1 90  ? 16.278 -45.448 1.584   1.00 44.27 ? 90  LYS A CE  1 
ATOM   667  N NZ  . LYS A 1 90  ? 15.999 -44.743 0.301   1.00 44.22 ? 90  LYS A NZ  1 
ATOM   668  N N   . ASP A 1 91  ? 17.757 -48.703 -2.693  1.00 37.08 ? 91  ASP A N   1 
ATOM   669  C CA  . ASP A 1 91  ? 16.904 -48.179 -3.764  1.00 37.07 ? 91  ASP A CA  1 
ATOM   670  C C   . ASP A 1 91  ? 16.898 -49.028 -5.033  1.00 36.09 ? 91  ASP A C   1 
ATOM   671  O O   . ASP A 1 91  ? 15.926 -49.006 -5.784  1.00 36.38 ? 91  ASP A O   1 
ATOM   672  C CB  . ASP A 1 91  ? 17.357 -46.762 -4.127  1.00 36.78 ? 91  ASP A CB  1 
ATOM   673  C CG  . ASP A 1 91  ? 17.418 -45.844 -2.922  1.00 37.66 ? 91  ASP A CG  1 
ATOM   674  O OD1 . ASP A 1 91  ? 16.350 -45.555 -2.344  1.00 39.09 ? 91  ASP A OD1 1 
ATOM   675  O OD2 . ASP A 1 91  ? 18.532 -45.419 -2.550  1.00 37.16 ? 91  ASP A OD2 1 
ATOM   676  N N   . ALA A 1 92  ? 17.984 -49.752 -5.284  1.00 34.76 ? 92  ALA A N   1 
ATOM   677  C CA  . ALA A 1 92  ? 18.118 -50.536 -6.511  1.00 33.92 ? 92  ALA A CA  1 
ATOM   678  C C   . ALA A 1 92  ? 18.879 -51.837 -6.236  1.00 33.29 ? 92  ALA A C   1 
ATOM   679  O O   . ALA A 1 92  ? 19.975 -52.043 -6.765  1.00 32.03 ? 92  ALA A O   1 
ATOM   680  C CB  . ALA A 1 92  ? 18.820 -49.706 -7.579  1.00 33.12 ? 92  ALA A CB  1 
ATOM   681  N N   . PRO A 1 93  ? 18.297 -52.720 -5.398  1.00 34.02 ? 93  PRO A N   1 
ATOM   682  C CA  . PRO A 1 93  ? 18.988 -53.945 -4.978  1.00 33.80 ? 93  PRO A CA  1 
ATOM   683  C C   . PRO A 1 93  ? 19.417 -54.861 -6.130  1.00 33.09 ? 93  PRO A C   1 
ATOM   684  O O   . PRO A 1 93  ? 20.514 -55.416 -6.091  1.00 32.23 ? 93  PRO A O   1 
ATOM   685  C CB  . PRO A 1 93  ? 17.959 -54.647 -4.076  1.00 35.16 ? 93  PRO A CB  1 
ATOM   686  C CG  . PRO A 1 93  ? 16.646 -54.015 -4.394  1.00 35.88 ? 93  PRO A CG  1 
ATOM   687  C CD  . PRO A 1 93  ? 16.967 -52.604 -4.773  1.00 35.21 ? 93  PRO A CD  1 
ATOM   688  N N   . GLN A 1 94  ? 18.568 -55.014 -7.142  1.00 33.43 ? 94  GLN A N   1 
ATOM   689  C CA  . GLN A 1 94  ? 18.894 -55.879 -8.278  1.00 33.32 ? 94  GLN A CA  1 
ATOM   690  C C   . GLN A 1 94  ? 20.061 -55.312 -9.080  1.00 31.94 ? 94  GLN A C   1 
ATOM   691  O O   . GLN A 1 94  ? 20.948 -56.054 -9.501  1.00 31.20 ? 94  GLN A O   1 
ATOM   692  C CB  . GLN A 1 94  ? 17.680 -56.091 -9.191  1.00 34.40 ? 94  GLN A CB  1 
ATOM   693  C CG  . GLN A 1 94  ? 16.478 -56.732 -8.507  1.00 36.07 ? 94  GLN A CG  1 
ATOM   694  C CD  . GLN A 1 94  ? 16.798 -58.075 -7.872  1.00 36.87 ? 94  GLN A CD  1 
ATOM   695  O OE1 . GLN A 1 94  ? 17.662 -58.816 -8.348  1.00 36.62 ? 94  GLN A OE1 1 
ATOM   696  N NE2 . GLN A 1 94  ? 16.101 -58.396 -6.788  1.00 38.21 ? 94  GLN A NE2 1 
ATOM   697  N N   . LEU A 1 95  ? 20.056 -53.997 -9.282  1.00 31.61 ? 95  LEU A N   1 
ATOM   698  C CA  . LEU A 1 95  ? 21.146 -53.327 -9.977  1.00 30.70 ? 95  LEU A CA  1 
ATOM   699  C C   . LEU A 1 95  ? 22.437 -53.418 -9.170  1.00 30.07 ? 95  LEU A C   1 
ATOM   700  O O   . LEU A 1 95  ? 23.494 -53.746 -9.711  1.00 29.31 ? 95  LEU A O   1 
ATOM   701  C CB  . LEU A 1 95  ? 20.797 -51.863 -10.237 1.00 30.76 ? 95  LEU A CB  1 
ATOM   702  C CG  . LEU A 1 95  ? 21.861 -51.019 -10.942 1.00 29.92 ? 95  LEU A CG  1 
ATOM   703  C CD1 . LEU A 1 95  ? 22.255 -51.645 -12.271 1.00 29.65 ? 95  LEU A CD1 1 
ATOM   704  C CD2 . LEU A 1 95  ? 21.350 -49.601 -11.141 1.00 30.29 ? 95  LEU A CD2 1 
ATOM   705  N N   . HIS A 1 96  ? 22.348 -53.135 -7.874  1.00 30.52 ? 96  HIS A N   1 
ATOM   706  C CA  . HIS A 1 96  ? 23.529 -53.164 -7.020  1.00 30.40 ? 96  HIS A CA  1 
ATOM   707  C C   . HIS A 1 96  ? 24.126 -54.570 -6.942  1.00 30.55 ? 96  HIS A C   1 
ATOM   708  O O   . HIS A 1 96  ? 25.350 -54.730 -6.954  1.00 29.91 ? 96  HIS A O   1 
ATOM   709  C CB  . HIS A 1 96  ? 23.221 -52.632 -5.619  1.00 31.13 ? 96  HIS A CB  1 
ATOM   710  C CG  . HIS A 1 96  ? 24.434 -52.152 -4.890  1.00 30.78 ? 96  HIS A CG  1 
ATOM   711  N ND1 . HIS A 1 96  ? 25.263 -52.999 -4.186  1.00 30.92 ? 96  HIS A ND1 1 
ATOM   712  C CD2 . HIS A 1 96  ? 24.978 -50.917 -4.781  1.00 30.48 ? 96  HIS A CD2 1 
ATOM   713  C CE1 . HIS A 1 96  ? 26.256 -52.303 -3.661  1.00 30.65 ? 96  HIS A CE1 1 
ATOM   714  N NE2 . HIS A 1 96  ? 26.106 -51.037 -4.006  1.00 30.29 ? 96  HIS A NE2 1 
ATOM   715  N N   . LYS A 1 97  ? 23.259 -55.577 -6.879  1.00 31.56 ? 97  LYS A N   1 
ATOM   716  C CA  . LYS A 1 97  ? 23.685 -56.975 -6.909  1.00 32.15 ? 97  LYS A CA  1 
ATOM   717  C C   . LYS A 1 97  ? 24.412 -57.307 -8.210  1.00 31.28 ? 97  LYS A C   1 
ATOM   718  O O   . LYS A 1 97  ? 25.462 -57.938 -8.183  1.00 30.89 ? 97  LYS A O   1 
ATOM   719  C CB  . LYS A 1 97  ? 22.486 -57.913 -6.744  1.00 33.72 ? 97  LYS A CB  1 
ATOM   720  C CG  . LYS A 1 97  ? 22.853 -59.388 -6.656  1.00 34.72 ? 97  LYS A CG  1 
ATOM   721  C CD  . LYS A 1 97  ? 21.611 -60.265 -6.670  1.00 36.62 ? 97  LYS A CD  1 
ATOM   722  C CE  . LYS A 1 97  ? 21.961 -61.745 -6.596  1.00 37.70 ? 97  LYS A CE  1 
ATOM   723  N NZ  . LYS A 1 97  ? 20.761 -62.612 -6.775  1.00 39.33 ? 97  LYS A NZ  1 
ATOM   724  N N   . LEU A 1 98  ? 23.840 -56.887 -9.337  1.00 31.01 ? 98  LEU A N   1 
ATOM   725  C CA  . LEU A 1 98  ? 24.451 -57.103 -10.655 1.00 30.62 ? 98  LEU A CA  1 
ATOM   726  C C   . LEU A 1 98  ? 25.886 -56.588 -10.702 1.00 29.70 ? 98  LEU A C   1 
ATOM   727  O O   . LEU A 1 98  ? 26.806 -57.309 -11.087 1.00 29.35 ? 98  LEU A O   1 
ATOM   728  C CB  . LEU A 1 98  ? 23.634 -56.397 -11.743 1.00 30.54 ? 98  LEU A CB  1 
ATOM   729  C CG  . LEU A 1 98  ? 24.212 -56.408 -13.162 1.00 30.06 ? 98  LEU A CG  1 
ATOM   730  C CD1 . LEU A 1 98  ? 24.180 -57.810 -13.750 1.00 30.73 ? 98  LEU A CD1 1 
ATOM   731  C CD2 . LEU A 1 98  ? 23.460 -55.425 -14.041 1.00 30.12 ? 98  LEU A CD2 1 
ATOM   732  N N   . LEU A 1 99  ? 26.061 -55.335 -10.295 1.00 29.46 ? 99  LEU A N   1 
ATOM   733  C CA  . LEU A 1 99  ? 27.335 -54.647 -10.430 1.00 28.94 ? 99  LEU A CA  1 
ATOM   734  C C   . LEU A 1 99  ? 28.365 -55.164 -9.434  1.00 29.18 ? 99  LEU A C   1 
ATOM   735  O O   . LEU A 1 99  ? 29.548 -55.273 -9.759  1.00 28.68 ? 99  LEU A O   1 
ATOM   736  C CB  . LEU A 1 99  ? 27.137 -53.141 -10.271 1.00 28.70 ? 99  LEU A CB  1 
ATOM   737  C CG  . LEU A 1 99  ? 26.187 -52.508 -11.293 1.00 28.82 ? 99  LEU A CG  1 
ATOM   738  C CD1 . LEU A 1 99  ? 26.009 -51.025 -11.011 1.00 28.87 ? 99  LEU A CD1 1 
ATOM   739  C CD2 . LEU A 1 99  ? 26.675 -52.741 -12.714 1.00 28.41 ? 99  LEU A CD2 1 
ATOM   740  N N   . THR A 1 100 ? 27.909 -55.490 -8.228  1.00 30.16 ? 100 THR A N   1 
ATOM   741  C CA  . THR A 1 100 ? 28.770 -56.084 -7.214  1.00 30.81 ? 100 THR A CA  1 
ATOM   742  C C   . THR A 1 100 ? 29.279 -57.459 -7.642  1.00 30.48 ? 100 THR A C   1 
ATOM   743  O O   . THR A 1 100 ? 30.431 -57.804 -7.393  1.00 30.27 ? 100 THR A O   1 
ATOM   744  C CB  . THR A 1 100 ? 28.024 -56.225 -5.872  1.00 32.31 ? 100 THR A CB  1 
ATOM   745  O OG1 . THR A 1 100 ? 27.638 -54.926 -5.413  1.00 33.41 ? 100 THR A OG1 1 
ATOM   746  C CG2 . THR A 1 100 ? 28.909 -56.884 -4.822  1.00 33.15 ? 100 THR A CG2 1 
ATOM   747  N N   . ASN A 1 101 ? 28.420 -58.228 -8.302  1.00 30.49 ? 101 ASN A N   1 
ATOM   748  C CA  . ASN A 1 101 ? 28.727 -59.618 -8.631  1.00 31.07 ? 101 ASN A CA  1 
ATOM   749  C C   . ASN A 1 101 ? 29.728 -59.755 -9.789  1.00 30.23 ? 101 ASN A C   1 
ATOM   750  O O   . ASN A 1 101 ? 30.237 -60.844 -10.046 1.00 30.39 ? 101 ASN A O   1 
ATOM   751  C CB  . ASN A 1 101 ? 27.420 -60.364 -8.934  1.00 32.01 ? 101 ASN A CB  1 
ATOM   752  C CG  . ASN A 1 101 ? 27.494 -61.853 -8.636  1.00 33.24 ? 101 ASN A CG  1 
ATOM   753  O OD1 . ASN A 1 101 ? 28.532 -62.496 -8.797  1.00 33.77 ? 101 ASN A OD1 1 
ATOM   754  N ND2 . ASN A 1 101 ? 26.377 -62.408 -8.202  1.00 34.20 ? 101 ASN A ND2 1 
ATOM   755  N N   . MET A 1 102 ? 30.015 -58.650 -10.474 1.00 29.24 ? 102 MET A N   1 
ATOM   756  C CA  . MET A 1 102 ? 30.996 -58.644 -11.564 1.00 28.77 ? 102 MET A CA  1 
ATOM   757  C C   . MET A 1 102 ? 32.320 -57.979 -11.156 1.00 27.99 ? 102 MET A C   1 
ATOM   758  O O   . MET A 1 102 ? 33.228 -57.849 -11.978 1.00 27.45 ? 102 MET A O   1 
ATOM   759  C CB  . MET A 1 102 ? 30.408 -57.980 -12.822 1.00 28.54 ? 102 MET A CB  1 
ATOM   760  C CG  . MET A 1 102 ? 29.800 -56.602 -12.606 1.00 28.32 ? 102 MET A CG  1 
ATOM   761  S SD  . MET A 1 102 ? 29.171 -55.850 -14.122 1.00 28.18 ? 102 MET A SD  1 
ATOM   762  C CE  . MET A 1 102 ? 30.709 -55.255 -14.822 1.00 27.45 ? 102 MET A CE  1 
ATOM   763  N N   . ILE A 1 103 ? 32.429 -57.581 -9.888  1.00 27.95 ? 103 ILE A N   1 
ATOM   764  C CA  . ILE A 1 103 ? 33.648 -56.961 -9.353  1.00 27.60 ? 103 ILE A CA  1 
ATOM   765  C C   . ILE A 1 103 ? 34.872 -57.845 -9.575  1.00 27.09 ? 103 ILE A C   1 
ATOM   766  O O   . ILE A 1 103 ? 35.916 -57.373 -10.032 1.00 26.41 ? 103 ILE A O   1 
ATOM   767  C CB  . ILE A 1 103 ? 33.498 -56.657 -7.840  1.00 28.60 ? 103 ILE A CB  1 
ATOM   768  C CG1 . ILE A 1 103 ? 32.654 -55.397 -7.645  1.00 28.72 ? 103 ILE A CG1 1 
ATOM   769  C CG2 . ILE A 1 103 ? 34.855 -56.481 -7.166  1.00 28.79 ? 103 ILE A CG2 1 
ATOM   770  C CD1 . ILE A 1 103 ? 32.207 -55.190 -6.209  1.00 29.72 ? 103 ILE A CD1 1 
ATOM   771  N N   . GLY A 1 104 ? 34.740 -59.121 -9.235  1.00 27.18 ? 104 GLY A N   1 
ATOM   772  C CA  . GLY A 1 104 ? 35.823 -60.080 -9.400  1.00 27.47 ? 104 GLY A CA  1 
ATOM   773  C C   . GLY A 1 104 ? 36.171 -60.337 -10.856 1.00 26.99 ? 104 GLY A C   1 
ATOM   774  O O   . GLY A 1 104 ? 37.337 -60.478 -11.214 1.00 26.76 ? 104 GLY A O   1 
ATOM   775  N N   . ASP A 1 105 ? 35.155 -60.389 -11.703 1.00 26.95 ? 105 ASP A N   1 
ATOM   776  C CA  . ASP A 1 105 ? 35.365 -60.654 -13.123 1.00 26.80 ? 105 ASP A CA  1 
ATOM   777  C C   . ASP A 1 105 ? 36.182 -59.545 -13.769 1.00 26.17 ? 105 ASP A C   1 
ATOM   778  O O   . ASP A 1 105 ? 37.148 -59.814 -14.482 1.00 26.34 ? 105 ASP A O   1 
ATOM   779  C CB  . ASP A 1 105 ? 34.024 -60.807 -13.832 1.00 26.99 ? 105 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 105 ? 33.189 -61.920 -13.245 1.00 27.84 ? 105 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 105 ? 33.705 -63.046 -13.104 1.00 28.41 ? 105 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 105 ? 32.020 -61.666 -12.904 1.00 27.95 ? 105 ASP A OD2 1 
ATOM   783  N N   . ALA A 1 106 ? 35.802 -58.300 -13.495 1.00 25.69 ? 106 ALA A N   1 
ATOM   784  C CA  . ALA A 1 106 ? 36.450 -57.138 -14.100 1.00 25.06 ? 106 ALA A CA  1 
ATOM   785  C C   . ALA A 1 106 ? 37.714 -56.719 -13.359 1.00 24.90 ? 106 ALA A C   1 
ATOM   786  O O   . ALA A 1 106 ? 38.699 -56.318 -13.981 1.00 24.68 ? 106 ALA A O   1 
ATOM   787  C CB  . ALA A 1 106 ? 35.473 -55.975 -14.163 1.00 24.89 ? 106 ALA A CB  1 
ATOM   788  N N   . GLY A 1 107 ? 37.680 -56.798 -12.032 1.00 25.02 ? 107 GLY A N   1 
ATOM   789  C CA  . GLY A 1 107 ? 38.787 -56.332 -11.210 1.00 24.99 ? 107 GLY A CA  1 
ATOM   790  C C   . GLY A 1 107 ? 39.919 -57.327 -11.088 1.00 25.42 ? 107 GLY A C   1 
ATOM   791  O O   . GLY A 1 107 ? 41.088 -56.940 -11.016 1.00 25.33 ? 107 GLY A O   1 
ATOM   792  N N   . ASP A 1 108 ? 39.575 -58.611 -11.066 1.00 25.98 ? 108 ASP A N   1 
ATOM   793  C CA  . ASP A 1 108 ? 40.551 -59.656 -10.795 1.00 26.64 ? 108 ASP A CA  1 
ATOM   794  C C   . ASP A 1 108 ? 40.821 -60.509 -12.035 1.00 26.77 ? 108 ASP A C   1 
ATOM   795  O O   . ASP A 1 108 ? 41.923 -60.472 -12.573 1.00 26.63 ? 108 ASP A O   1 
ATOM   796  C CB  . ASP A 1 108 ? 40.086 -60.511 -9.614  1.00 27.53 ? 108 ASP A CB  1 
ATOM   797  C CG  . ASP A 1 108 ? 41.064 -61.613 -9.260  1.00 28.42 ? 108 ASP A CG  1 
ATOM   798  O OD1 . ASP A 1 108 ? 42.230 -61.569 -9.705  1.00 28.37 ? 108 ASP A OD1 1 
ATOM   799  O OD2 . ASP A 1 108 ? 40.653 -62.542 -8.538  1.00 29.31 ? 108 ASP A OD2 1 
ATOM   800  N N   . LEU A 1 109 ? 39.823 -61.266 -12.489 1.00 26.91 ? 109 LEU A N   1 
ATOM   801  C CA  . LEU A 1 109 ? 40.016 -62.179 -13.619 1.00 27.31 ? 109 LEU A CA  1 
ATOM   802  C C   . LEU A 1 109 ? 40.551 -61.473 -14.862 1.00 26.60 ? 109 LEU A C   1 
ATOM   803  O O   . LEU A 1 109 ? 41.458 -61.976 -15.515 1.00 26.77 ? 109 LEU A O   1 
ATOM   804  C CB  . LEU A 1 109 ? 38.714 -62.898 -13.977 1.00 27.79 ? 109 LEU A CB  1 
ATOM   805  C CG  . LEU A 1 109 ? 38.188 -63.928 -12.984 1.00 28.80 ? 109 LEU A CG  1 
ATOM   806  C CD1 . LEU A 1 109 ? 36.865 -64.482 -13.487 1.00 29.31 ? 109 LEU A CD1 1 
ATOM   807  C CD2 . LEU A 1 109 ? 39.186 -65.055 -12.758 1.00 29.81 ? 109 LEU A CD2 1 
ATOM   808  N N   . ALA A 1 110 ? 40.000 -60.303 -15.171 1.00 25.77 ? 110 ALA A N   1 
ATOM   809  C CA  . ALA A 1 110 ? 40.383 -59.576 -16.375 1.00 25.54 ? 110 ALA A CA  1 
ATOM   810  C C   . ALA A 1 110 ? 41.782 -58.942 -16.291 1.00 25.35 ? 110 ALA A C   1 
ATOM   811  O O   . ALA A 1 110 ? 42.319 -58.524 -17.313 1.00 25.29 ? 110 ALA A O   1 
ATOM   812  C CB  . ALA A 1 110 ? 39.340 -58.514 -16.697 1.00 25.05 ? 110 ALA A CB  1 
ATOM   813  N N   . THR A 1 111 ? 42.361 -58.865 -15.090 1.00 25.50 ? 111 THR A N   1 
ATOM   814  C CA  . THR A 1 111 ? 43.655 -58.201 -14.884 1.00 25.43 ? 111 THR A CA  1 
ATOM   815  C C   . THR A 1 111 ? 44.780 -59.107 -14.385 1.00 25.99 ? 111 THR A C   1 
ATOM   816  O O   . THR A 1 111 ? 45.947 -58.718 -14.446 1.00 25.94 ? 111 THR A O   1 
ATOM   817  C CB  . THR A 1 111 ? 43.534 -57.071 -13.844 1.00 25.27 ? 111 THR A CB  1 
ATOM   818  O OG1 . THR A 1 111 ? 43.243 -57.633 -12.557 1.00 26.07 ? 111 THR A OG1 1 
ATOM   819  C CG2 . THR A 1 111 ? 42.447 -56.084 -14.228 1.00 24.79 ? 111 THR A CG2 1 
ATOM   820  N N   . ARG A 1 112 ? 44.438 -60.300 -13.899 1.00 26.35 ? 112 ARG A N   1 
ATOM   821  C CA  . ARG A 1 112 ? 45.352 -61.087 -13.067 1.00 27.10 ? 112 ARG A CA  1 
ATOM   822  C C   . ARG A 1 112 ? 46.628 -61.503 -13.783 1.00 27.28 ? 112 ARG A C   1 
ATOM   823  O O   . ARG A 1 112 ? 47.712 -61.417 -13.210 1.00 27.70 ? 112 ARG A O   1 
ATOM   824  C CB  . ARG A 1 112 ? 44.653 -62.338 -12.521 1.00 27.99 ? 112 ARG A CB  1 
ATOM   825  C CG  . ARG A 1 112 ? 45.384 -62.991 -11.361 1.00 28.99 ? 112 ARG A CG  1 
ATOM   826  C CD  . ARG A 1 112 ? 44.752 -64.318 -10.996 1.00 30.11 ? 112 ARG A CD  1 
ATOM   827  N NE  . ARG A 1 112 ? 43.390 -64.152 -10.489 1.00 29.96 ? 112 ARG A NE  1 
ATOM   828  C CZ  . ARG A 1 112 ? 42.444 -65.091 -10.524 1.00 30.74 ? 112 ARG A CZ  1 
ATOM   829  N NH1 . ARG A 1 112 ? 42.680 -66.284 -11.060 1.00 31.65 ? 112 ARG A NH1 1 
ATOM   830  N NH2 . ARG A 1 112 ? 41.241 -64.832 -10.025 1.00 30.69 ? 112 ARG A NH2 1 
ATOM   831  N N   . GLY A 1 113 ? 46.491 -61.977 -15.019 1.00 27.33 ? 113 GLY A N   1 
ATOM   832  C CA  . GLY A 1 113 ? 47.635 -62.455 -15.787 1.00 27.79 ? 113 GLY A CA  1 
ATOM   833  C C   . GLY A 1 113 ? 48.691 -61.381 -15.963 1.00 27.31 ? 113 GLY A C   1 
ATOM   834  O O   . GLY A 1 113 ? 49.860 -61.590 -15.648 1.00 27.42 ? 113 GLY A O   1 
ATOM   835  N N   . ALA A 1 114 ? 48.268 -60.226 -16.463 1.00 26.71 ? 114 ALA A N   1 
ATOM   836  C CA  . ALA A 1 114 ? 49.166 -59.091 -16.651 1.00 26.57 ? 114 ALA A CA  1 
ATOM   837  C C   . ALA A 1 114 ? 49.671 -58.542 -15.313 1.00 26.87 ? 114 ALA A C   1 
ATOM   838  O O   . ALA A 1 114 ? 50.853 -58.237 -15.178 1.00 26.91 ? 114 ALA A O   1 
ATOM   839  C CB  . ALA A 1 114 ? 48.472 -57.996 -17.453 1.00 25.71 ? 114 ALA A CB  1 
ATOM   840  N N   . LYS A 1 115 ? 48.779 -58.410 -14.334 1.00 27.46 ? 115 LYS A N   1 
ATOM   841  C CA  . LYS A 1 115 ? 49.168 -57.917 -13.008 1.00 28.50 ? 115 LYS A CA  1 
ATOM   842  C C   . LYS A 1 115 ? 50.332 -58.702 -12.432 1.00 29.46 ? 115 LYS A C   1 
ATOM   843  O O   . LYS A 1 115 ? 51.342 -58.124 -12.026 1.00 29.31 ? 115 LYS A O   1 
ATOM   844  C CB  . LYS A 1 115 ? 48.006 -57.979 -12.019 1.00 29.27 ? 115 LYS A CB  1 
ATOM   845  C CG  . LYS A 1 115 ? 47.141 -56.737 -11.991 1.00 29.59 ? 115 LYS A CG  1 
ATOM   846  C CD  . LYS A 1 115 ? 46.165 -56.795 -10.826 1.00 30.47 ? 115 LYS A CD  1 
ATOM   847  C CE  . LYS A 1 115 ? 45.347 -55.518 -10.722 1.00 30.33 ? 115 LYS A CE  1 
ATOM   848  N NZ  . LYS A 1 115 ? 46.197 -54.369 -10.318 1.00 30.61 ? 115 LYS A NZ  1 
ATOM   849  N N   . GLU A 1 116 ? 50.181 -60.020 -12.396 1.00 30.45 ? 116 GLU A N   1 
ATOM   850  C CA  . GLU A 1 116 ? 51.163 -60.876 -11.740 1.00 32.05 ? 116 GLU A CA  1 
ATOM   851  C C   . GLU A 1 116 ? 52.455 -61.023 -12.538 1.00 32.19 ? 116 GLU A C   1 
ATOM   852  O O   . GLU A 1 116 ? 53.516 -61.229 -11.954 1.00 32.73 ? 116 GLU A O   1 
ATOM   853  C CB  . GLU A 1 116 ? 50.556 -62.243 -11.419 1.00 33.54 ? 116 GLU A CB  1 
ATOM   854  C CG  . GLU A 1 116 ? 49.444 -62.150 -10.386 1.00 34.14 ? 116 GLU A CG  1 
ATOM   855  C CD  . GLU A 1 116 ? 48.984 -63.499 -9.863  1.00 35.86 ? 116 GLU A CD  1 
ATOM   856  O OE1 . GLU A 1 116 ? 49.667 -64.514 -10.110 1.00 37.82 ? 116 GLU A OE1 1 
ATOM   857  O OE2 . GLU A 1 116 ? 47.935 -63.538 -9.189  1.00 36.70 ? 116 GLU A OE2 1 
ATOM   858  N N   . LYS A 1 117 ? 52.376 -60.901 -13.860 1.00 31.67 ? 117 LYS A N   1 
ATOM   859  C CA  . LYS A 1 117 ? 53.571 -60.996 -14.692 1.00 32.16 ? 117 LYS A CA  1 
ATOM   860  C C   . LYS A 1 117 ? 54.485 -59.791 -14.498 1.00 30.81 ? 117 LYS A C   1 
ATOM   861  O O   . LYS A 1 117 ? 55.686 -59.945 -14.305 1.00 31.11 ? 117 LYS A O   1 
ATOM   862  C CB  . LYS A 1 117 ? 53.207 -61.125 -16.174 1.00 33.01 ? 117 LYS A CB  1 
ATOM   863  C CG  . LYS A 1 117 ? 54.398 -61.419 -17.081 1.00 34.78 ? 117 LYS A CG  1 
ATOM   864  C CD  . LYS A 1 117 ? 55.062 -62.737 -16.713 1.00 37.03 ? 117 LYS A CD  1 
ATOM   865  C CE  . LYS A 1 117 ? 55.888 -63.298 -17.859 1.00 38.96 ? 117 LYS A CE  1 
ATOM   866  N NZ  . LYS A 1 117 ? 56.851 -62.294 -18.401 1.00 39.42 ? 117 LYS A NZ  1 
ATOM   867  N N   . TYR A 1 118 ? 53.914 -58.593 -14.550 1.00 28.71 ? 118 TYR A N   1 
ATOM   868  C CA  . TYR A 1 118 ? 54.718 -57.379 -14.517 1.00 27.99 ? 118 TYR A CA  1 
ATOM   869  C C   . TYR A 1 118 ? 54.952 -56.847 -13.104 1.00 27.58 ? 118 TYR A C   1 
ATOM   870  O O   . TYR A 1 118 ? 55.974 -56.201 -12.858 1.00 27.85 ? 118 TYR A O   1 
ATOM   871  C CB  . TYR A 1 118 ? 54.081 -56.308 -15.398 1.00 27.00 ? 118 TYR A CB  1 
ATOM   872  C CG  . TYR A 1 118 ? 53.919 -56.756 -16.833 1.00 27.07 ? 118 TYR A CG  1 
ATOM   873  C CD1 . TYR A 1 118 ? 55.031 -56.995 -17.634 1.00 27.79 ? 118 TYR A CD1 1 
ATOM   874  C CD2 . TYR A 1 118 ? 52.660 -56.944 -17.388 1.00 26.56 ? 118 TYR A CD2 1 
ATOM   875  C CE1 . TYR A 1 118 ? 54.893 -57.408 -18.948 1.00 27.94 ? 118 TYR A CE1 1 
ATOM   876  C CE2 . TYR A 1 118 ? 52.511 -57.355 -18.702 1.00 26.81 ? 118 TYR A CE2 1 
ATOM   877  C CZ  . TYR A 1 118 ? 53.630 -57.586 -19.476 1.00 27.33 ? 118 TYR A CZ  1 
ATOM   878  O OH  . TYR A 1 118 ? 53.494 -57.991 -20.781 1.00 27.46 ? 118 TYR A OH  1 
ATOM   879  N N   . MET A 1 119 ? 54.023 -57.121 -12.186 1.00 38.02 ? 119 MET A N   1 
ATOM   880  C CA  . MET A 1 119 ? 54.099 -56.608 -10.814 1.00 37.63 ? 119 MET A CA  1 
ATOM   881  C C   . MET A 1 119 ? 54.619 -55.174 -10.807 1.00 33.77 ? 119 MET A C   1 
ATOM   882  O O   . MET A 1 119 ? 55.521 -54.821 -10.047 1.00 32.70 ? 119 MET A O   1 
ATOM   883  C CB  . MET A 1 119 ? 54.990 -57.507 -9.944  1.00 40.22 ? 119 MET A CB  1 
ATOM   884  C CG  . MET A 1 119 ? 54.405 -58.878 -9.651  1.00 44.72 ? 119 MET A CG  1 
ATOM   885  S SD  . MET A 1 119 ? 52.791 -58.824 -8.843  1.00 47.95 ? 119 MET A SD  1 
ATOM   886  C CE  . MET A 1 119 ? 53.201 -58.037 -7.288  1.00 47.92 ? 119 MET A CE  1 
ATOM   887  N N   . ARG A 1 120 ? 54.017 -54.345 -11.654 1.00 31.39 ? 120 ARG A N   1 
ATOM   888  C CA  . ARG A 1 120 ? 54.519 -53.010 -11.893 1.00 28.55 ? 120 ARG A CA  1 
ATOM   889  C C   . ARG A 1 120 ? 54.426 -52.148 -10.646 1.00 28.13 ? 120 ARG A C   1 
ATOM   890  O O   . ARG A 1 120 ? 53.422 -52.175 -9.938  1.00 28.93 ? 120 ARG A O   1 
ATOM   891  C CB  . ARG A 1 120 ? 53.747 -52.343 -13.024 1.00 27.40 ? 120 ARG A CB  1 
ATOM   892  C CG  . ARG A 1 120 ? 54.365 -51.038 -13.480 1.00 25.15 ? 120 ARG A CG  1 
ATOM   893  C CD  . ARG A 1 120 ? 53.455 -50.310 -14.445 1.00 24.85 ? 120 ARG A CD  1 
ATOM   894  N NE  . ARG A 1 120 ? 54.131 -49.175 -15.060 1.00 23.49 ? 120 ARG A NE  1 
ATOM   895  C CZ  . ARG A 1 120 ? 53.549 -48.311 -15.888 1.00 23.43 ? 120 ARG A CZ  1 
ATOM   896  N NH1 . ARG A 1 120 ? 52.257 -48.421 -16.193 1.00 24.09 ? 120 ARG A NH1 1 
ATOM   897  N NH2 . ARG A 1 120 ? 54.264 -47.317 -16.397 1.00 22.86 ? 120 ARG A NH2 1 
ATOM   898  N N   . ILE A 1 121 ? 55.482 -51.381 -10.401 1.00 27.00 ? 121 ILE A N   1 
ATOM   899  C CA  A ILE A 1 121 ? 55.522 -50.463 -9.269  0.50 26.96 ? 121 ILE A CA  1 
ATOM   900  C CA  B ILE A 1 121 ? 55.525 -50.467 -9.269  0.50 27.00 ? 121 ILE A CA  1 
ATOM   901  C C   . ILE A 1 121 ? 54.550 -49.316 -9.517  1.00 25.87 ? 121 ILE A C   1 
ATOM   902  O O   . ILE A 1 121 ? 54.453 -48.807 -10.631 1.00 24.61 ? 121 ILE A O   1 
ATOM   903  C CB  A ILE A 1 121 ? 56.948 -49.916 -9.005  0.50 26.38 ? 121 ILE A CB  1 
ATOM   904  C CB  B ILE A 1 121 ? 56.964 -49.957 -9.032  0.50 26.47 ? 121 ILE A CB  1 
ATOM   905  C CG1 A ILE A 1 121 ? 57.003 -49.218 -7.641  0.50 27.14 ? 121 ILE A CG1 1 
ATOM   906  C CG1 B ILE A 1 121 ? 57.856 -51.130 -8.602  0.50 28.25 ? 121 ILE A CG1 1 
ATOM   907  C CG2 A ILE A 1 121 ? 57.404 -48.971 -10.111 0.50 24.62 ? 121 ILE A CG2 1 
ATOM   908  C CG2 B ILE A 1 121 ? 56.998 -48.871 -7.967  0.50 26.47 ? 121 ILE A CG2 1 
ATOM   909  C CD1 A ILE A 1 121 ? 58.406 -48.909 -7.168  0.50 27.45 ? 121 ILE A CD1 1 
ATOM   910  C CD1 B ILE A 1 121 ? 59.311 -50.767 -8.416  0.50 28.21 ? 121 ILE A CD1 1 
ATOM   911  N N   . ARG A 1 122 ? 53.822 -48.926 -8.475  1.00 26.81 ? 122 ARG A N   1 
ATOM   912  C CA  A ARG A 1 122 ? 52.823 -47.859 -8.576  0.50 26.19 ? 122 ARG A CA  1 
ATOM   913  C CA  B ARG A 1 122 ? 52.820 -47.869 -8.597  0.50 26.33 ? 122 ARG A CA  1 
ATOM   914  C C   . ARG A 1 122 ? 53.496 -46.504 -8.424  1.00 24.98 ? 122 ARG A C   1 
ATOM   915  O O   . ARG A 1 122 ? 54.582 -46.417 -7.846  1.00 25.14 ? 122 ARG A O   1 
ATOM   916  C CB  A ARG A 1 122 ? 51.748 -48.033 -7.507  0.50 28.02 ? 122 ARG A CB  1 
ATOM   917  C CB  B ARG A 1 122 ? 51.679 -48.086 -7.590  0.50 28.38 ? 122 ARG A CB  1 
ATOM   918  C CG  A ARG A 1 122 ? 50.887 -49.262 -7.721  0.50 29.87 ? 122 ARG A CG  1 
ATOM   919  C CG  B ARG A 1 122 ? 51.229 -49.542 -7.501  0.50 30.75 ? 122 ARG A CG  1 
ATOM   920  C CD  A ARG A 1 122 ? 50.146 -49.636 -6.456  0.50 32.49 ? 122 ARG A CD  1 
ATOM   921  C CD  B ARG A 1 122 ? 49.728 -49.741 -7.386  0.50 32.66 ? 122 ARG A CD  1 
ATOM   922  N NE  A ARG A 1 122 ? 48.879 -48.927 -6.320  0.50 32.97 ? 122 ARG A NE  1 
ATOM   923  N NE  B ARG A 1 122 ? 49.248 -49.541 -6.027  0.50 34.63 ? 122 ARG A NE  1 
ATOM   924  C CZ  A ARG A 1 122 ? 47.723 -49.387 -6.780  0.50 34.26 ? 122 ARG A CZ  1 
ATOM   925  C CZ  B ARG A 1 122 ? 48.112 -50.047 -5.558  0.50 37.29 ? 122 ARG A CZ  1 
ATOM   926  N NH1 A ARG A 1 122 ? 46.612 -48.688 -6.601  0.50 34.75 ? 122 ARG A NH1 1 
ATOM   927  N NH1 B ARG A 1 122 ? 47.347 -50.808 -6.331  0.50 38.66 ? 122 ARG A NH1 1 
ATOM   928  N NH2 A ARG A 1 122 ? 47.681 -50.545 -7.423  0.50 35.53 ? 122 ARG A NH2 1 
ATOM   929  N NH2 B ARG A 1 122 ? 47.750 -49.806 -4.308  0.50 39.10 ? 122 ARG A NH2 1 
ATOM   930  N N   . PRO A 1 123 ? 52.859 -45.430 -8.934  1.00 24.11 ? 123 PRO A N   1 
ATOM   931  C CA  . PRO A 1 123 ? 53.519 -44.119 -8.891  1.00 23.25 ? 123 PRO A CA  1 
ATOM   932  C C   . PRO A 1 123 ? 54.000 -43.671 -7.515  1.00 23.81 ? 123 PRO A C   1 
ATOM   933  O O   . PRO A 1 123 ? 55.162 -43.316 -7.369  1.00 23.62 ? 123 PRO A O   1 
ATOM   934  C CB  . PRO A 1 123 ? 52.450 -43.157 -9.424  1.00 23.13 ? 123 PRO A CB  1 
ATOM   935  C CG  . PRO A 1 123 ? 51.537 -43.995 -10.232 1.00 23.50 ? 123 PRO A CG  1 
ATOM   936  C CD  . PRO A 1 123 ? 51.553 -45.367 -9.624  1.00 24.43 ? 123 PRO A CD  1 
ATOM   937  N N   . PHE A 1 124 ? 53.123 -43.683 -6.516  1.00 24.71 ? 124 PHE A N   1 
ATOM   938  C CA  . PHE A 1 124 ? 53.513 -43.214 -5.185  1.00 25.82 ? 124 PHE A CA  1 
ATOM   939  C C   . PHE A 1 124 ? 54.746 -43.964 -4.665  1.00 26.52 ? 124 PHE A C   1 
ATOM   940  O O   . PHE A 1 124 ? 55.617 -43.368 -4.035  1.00 27.24 ? 124 PHE A O   1 
ATOM   941  C CB  . PHE A 1 124 ? 52.343 -43.289 -4.191  1.00 27.36 ? 124 PHE A CB  1 
ATOM   942  C CG  . PHE A 1 124 ? 52.022 -44.677 -3.720  1.00 29.04 ? 124 PHE A CG  1 
ATOM   943  C CD1 . PHE A 1 124 ? 51.113 -45.468 -4.410  1.00 29.13 ? 124 PHE A CD1 1 
ATOM   944  C CD2 . PHE A 1 124 ? 52.623 -45.193 -2.582  1.00 31.14 ? 124 PHE A CD2 1 
ATOM   945  C CE1 . PHE A 1 124 ? 50.817 -46.745 -3.974  1.00 31.17 ? 124 PHE A CE1 1 
ATOM   946  C CE2 . PHE A 1 124 ? 52.330 -46.471 -2.142  1.00 33.34 ? 124 PHE A CE2 1 
ATOM   947  C CZ  . PHE A 1 124 ? 51.429 -47.248 -2.840  1.00 33.33 ? 124 PHE A CZ  1 
ATOM   948  N N   . ALA A 1 125 ? 54.816 -45.262 -4.948  1.00 26.79 ? 125 ALA A N   1 
ATOM   949  C CA  . ALA A 1 125 ? 55.949 -46.087 -4.532  1.00 27.98 ? 125 ALA A CA  1 
ATOM   950  C C   . ALA A 1 125 ? 57.207 -45.743 -5.324  1.00 26.61 ? 125 ALA A C   1 
ATOM   951  O O   . ALA A 1 125 ? 58.297 -45.702 -4.766  1.00 27.48 ? 125 ALA A O   1 
ATOM   952  C CB  . ALA A 1 125 ? 55.615 -47.563 -4.685  1.00 29.14 ? 125 ALA A CB  1 
ATOM   953  N N   . PHE A 1 126 ? 57.053 -45.493 -6.621  1.00 24.91 ? 126 PHE A N   1 
ATOM   954  C CA  . PHE A 1 126 ? 58.177 -45.091 -7.467  1.00 24.05 ? 126 PHE A CA  1 
ATOM   955  C C   . PHE A 1 126 ? 58.831 -43.817 -6.924  1.00 24.42 ? 126 PHE A C   1 
ATOM   956  O O   . PHE A 1 126 ? 60.056 -43.731 -6.842  1.00 24.95 ? 126 PHE A O   1 
ATOM   957  C CB  . PHE A 1 126 ? 57.708 -44.892 -8.917  1.00 22.76 ? 126 PHE A CB  1 
ATOM   958  C CG  . PHE A 1 126 ? 58.786 -44.421 -9.851  1.00 22.49 ? 126 PHE A CG  1 
ATOM   959  C CD1 . PHE A 1 126 ? 59.048 -43.066 -10.006 1.00 22.73 ? 126 PHE A CD1 1 
ATOM   960  C CD2 . PHE A 1 126 ? 59.531 -45.329 -10.591 1.00 22.66 ? 126 PHE A CD2 1 
ATOM   961  C CE1 . PHE A 1 126 ? 60.040 -42.626 -10.867 1.00 22.97 ? 126 PHE A CE1 1 
ATOM   962  C CE2 . PHE A 1 126 ? 60.523 -44.893 -11.459 1.00 22.67 ? 126 PHE A CE2 1 
ATOM   963  C CZ  . PHE A 1 126 ? 60.778 -43.543 -11.594 1.00 22.85 ? 126 PHE A CZ  1 
ATOM   964  N N   . TYR A 1 127 ? 58.008 -42.842 -6.544  1.00 24.32 ? 127 TYR A N   1 
ATOM   965  C CA  . TYR A 1 127 ? 58.501 -41.560 -6.042  1.00 25.22 ? 127 TYR A CA  1 
ATOM   966  C C   . TYR A 1 127 ? 58.803 -41.552 -4.541  1.00 27.08 ? 127 TYR A C   1 
ATOM   967  O O   . TYR A 1 127 ? 59.374 -40.589 -4.032  1.00 28.12 ? 127 TYR A O   1 
ATOM   968  C CB  . TYR A 1 127 ? 57.507 -40.444 -6.388  1.00 24.98 ? 127 TYR A CB  1 
ATOM   969  C CG  . TYR A 1 127 ? 57.380 -40.220 -7.878  1.00 23.90 ? 127 TYR A CG  1 
ATOM   970  C CD1 . TYR A 1 127 ? 58.378 -39.563 -8.588  1.00 24.56 ? 127 TYR A CD1 1 
ATOM   971  C CD2 . TYR A 1 127 ? 56.276 -40.683 -8.578  1.00 23.22 ? 127 TYR A CD2 1 
ATOM   972  C CE1 . TYR A 1 127 ? 58.272 -39.365 -9.957  1.00 24.17 ? 127 TYR A CE1 1 
ATOM   973  C CE2 . TYR A 1 127 ? 56.158 -40.495 -9.946  1.00 22.81 ? 127 TYR A CE2 1 
ATOM   974  C CZ  . TYR A 1 127 ? 57.157 -39.837 -10.630 1.00 23.25 ? 127 TYR A CZ  1 
ATOM   975  O OH  . TYR A 1 127 ? 57.038 -39.637 -11.982 1.00 23.37 ? 127 TYR A OH  1 
ATOM   976  N N   . GLY A 1 128 ? 58.433 -42.618 -3.838  1.00 27.87 ? 128 GLY A N   1 
ATOM   977  C CA  . GLY A 1 128 ? 58.671 -42.708 -2.398  1.00 30.38 ? 128 GLY A CA  1 
ATOM   978  C C   . GLY A 1 128 ? 57.849 -41.707 -1.610  1.00 31.30 ? 128 GLY A C   1 
ATOM   979  O O   . GLY A 1 128 ? 58.323 -41.148 -0.631  1.00 33.19 ? 128 GLY A O   1 
ATOM   980  N N   . VAL A 1 129 ? 56.606 -41.489 -2.037  1.00 30.28 ? 129 VAL A N   1 
ATOM   981  C CA  . VAL A 1 129 ? 55.718 -40.518 -1.393  1.00 31.41 ? 129 VAL A CA  1 
ATOM   982  C C   . VAL A 1 129 ? 54.351 -41.145 -1.127  1.00 31.84 ? 129 VAL A C   1 
ATOM   983  O O   . VAL A 1 129 ? 54.129 -42.311 -1.439  1.00 31.69 ? 129 VAL A O   1 
ATOM   984  C CB  . VAL A 1 129 ? 55.565 -39.235 -2.244  1.00 30.10 ? 129 VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 129 ? 56.905 -38.519 -2.363  1.00 30.80 ? 129 VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 129 ? 54.994 -39.549 -3.621  1.00 27.95 ? 129 VAL A CG2 1 
ATOM   987  N N   . SER A 1 130 ? 53.447 -40.379 -0.530  1.00 33.04 ? 130 SER A N   1 
ATOM   988  C CA  . SER A 1 130 ? 52.084 -40.848 -0.325  1.00 33.96 ? 130 SER A CA  1 
ATOM   989  C C   . SER A 1 130 ? 51.238 -40.534 -1.554  1.00 31.82 ? 130 SER A C   1 
ATOM   990  O O   . SER A 1 130 ? 51.703 -39.901 -2.508  1.00 29.86 ? 130 SER A O   1 
ATOM   991  C CB  . SER A 1 130 ? 51.476 -40.219 0.929   1.00 36.77 ? 130 SER A CB  1 
ATOM   992  O OG  . SER A 1 130 ? 51.306 -38.819 0.777   1.00 36.66 ? 130 SER A OG  1 
ATOM   993  N N   . THR A 1 131 ? 50.002 -41.010 -1.529  1.00 32.35 ? 131 THR A N   1 
ATOM   994  C CA  . THR A 1 131 ? 49.020 -40.686 -2.548  1.00 31.22 ? 131 THR A CA  1 
ATOM   995  C C   . THR A 1 131 ? 48.288 -39.428 -2.099  1.00 32.34 ? 131 THR A C   1 
ATOM   996  O O   . THR A 1 131 ? 48.574 -38.887 -1.031  1.00 33.51 ? 131 THR A O   1 
ATOM   997  C CB  . THR A 1 131 ? 48.017 -41.837 -2.721  1.00 31.80 ? 131 THR A CB  1 
ATOM   998  O OG1 . THR A 1 131 ? 47.324 -42.052 -1.489  1.00 34.09 ? 131 THR A OG1 1 
ATOM   999  C CG2 . THR A 1 131 ? 48.737 -43.113 -3.130  1.00 31.53 ? 131 THR A CG2 1 
ATOM   1000 N N   . CYS A 1 132 ? 47.329 -38.972 -2.898  1.00 32.19 ? 132 CYS A N   1 
ATOM   1001 C CA  . CYS A 1 132 ? 46.604 -37.746 -2.580  1.00 33.49 ? 132 CYS A CA  1 
ATOM   1002 C C   . CYS A 1 132 ? 45.652 -37.887 -1.389  1.00 35.99 ? 132 CYS A C   1 
ATOM   1003 O O   . CYS A 1 132 ? 45.318 -36.892 -0.754  1.00 36.96 ? 132 CYS A O   1 
ATOM   1004 C CB  . CYS A 1 132 ? 45.834 -37.254 -3.805  1.00 32.79 ? 132 CYS A CB  1 
ATOM   1005 S SG  . CYS A 1 132 ? 44.245 -38.053 -4.088  1.00 34.16 ? 132 CYS A SG  1 
ATOM   1006 N N   . ASN A 1 133 ? 45.221 -39.112 -1.088  1.00 37.55 ? 133 ASN A N   1 
ATOM   1007 C CA  . ASN A 1 133 ? 44.248 -39.351 -0.018  1.00 40.99 ? 133 ASN A CA  1 
ATOM   1008 C C   . ASN A 1 133 ? 44.798 -40.134 1.181   1.00 44.26 ? 133 ASN A C   1 
ATOM   1009 O O   . ASN A 1 133 ? 44.026 -40.578 2.031   1.00 46.69 ? 133 ASN A O   1 
ATOM   1010 C CB  . ASN A 1 133 ? 43.013 -40.067 -0.582  1.00 41.31 ? 133 ASN A CB  1 
ATOM   1011 C CG  . ASN A 1 133 ? 43.298 -41.502 -0.995  1.00 40.99 ? 133 ASN A CG  1 
ATOM   1012 O OD1 . ASN A 1 133 ? 44.447 -41.905 -1.149  1.00 39.57 ? 133 ASN A OD1 1 
ATOM   1013 N ND2 . ASN A 1 133 ? 42.245 -42.275 -1.184  1.00 42.74 ? 133 ASN A ND2 1 
ATOM   1014 N N   . THR A 1 134 ? 46.116 -40.313 1.238   1.00 45.04 ? 134 THR A N   1 
ATOM   1015 C CA  . THR A 1 134 ? 46.759 -41.031 2.338   1.00 49.24 ? 134 THR A CA  1 
ATOM   1016 C C   . THR A 1 134 ? 48.017 -40.313 2.807   1.00 50.73 ? 134 THR A C   1 
ATOM   1017 O O   . THR A 1 134 ? 48.606 -39.527 2.068   1.00 48.23 ? 134 THR A O   1 
ATOM   1018 C CB  . THR A 1 134 ? 47.188 -42.458 1.930   1.00 49.21 ? 134 THR A CB  1 
ATOM   1019 O OG1 . THR A 1 134 ? 48.156 -42.390 0.875   1.00 46.68 ? 134 THR A OG1 1 
ATOM   1020 C CG2 . THR A 1 134 ? 45.999 -43.291 1.478   1.00 49.90 ? 134 THR A CG2 1 
ATOM   1021 N N   . THR A 1 135 ? 48.405 -40.590 4.048   1.00 56.08 ? 135 THR A N   1 
ATOM   1022 C CA  . THR A 1 135 ? 49.747 -40.306 4.539   1.00 58.80 ? 135 THR A CA  1 
ATOM   1023 C C   . THR A 1 135 ? 50.472 -41.648 4.629   1.00 61.96 ? 135 THR A C   1 
ATOM   1024 O O   . THR A 1 135 ? 49.886 -42.692 4.330   1.00 62.33 ? 135 THR A O   1 
ATOM   1025 C CB  . THR A 1 135 ? 49.710 -39.627 5.919   1.00 62.36 ? 135 THR A CB  1 
ATOM   1026 O OG1 . THR A 1 135 ? 48.986 -40.449 6.840   1.00 65.93 ? 135 THR A OG1 1 
ATOM   1027 C CG2 . THR A 1 135 ? 49.037 -38.265 5.830   1.00 61.66 ? 135 THR A CG2 1 
ATOM   1028 N N   . GLU A 1 136 ? 51.737 -41.632 5.042   1.00 65.86 ? 136 GLU A N   1 
ATOM   1029 C CA  . GLU A 1 136 ? 52.519 -42.871 5.147   1.00 69.47 ? 136 GLU A CA  1 
ATOM   1030 C C   . GLU A 1 136 ? 52.145 -43.743 6.360   1.00 75.23 ? 136 GLU A C   1 
ATOM   1031 O O   . GLU A 1 136 ? 52.647 -44.862 6.487   1.00 77.26 ? 136 GLU A O   1 
ATOM   1032 C CB  . GLU A 1 136 ? 54.026 -42.568 5.149   1.00 70.27 ? 136 GLU A CB  1 
ATOM   1033 C CG  . GLU A 1 136 ? 54.541 -41.886 3.883   1.00 66.99 ? 136 GLU A CG  1 
ATOM   1034 C CD  . GLU A 1 136 ? 54.680 -42.821 2.686   1.00 65.39 ? 136 GLU A CD  1 
ATOM   1035 O OE1 . GLU A 1 136 ? 54.031 -43.891 2.655   1.00 67.03 ? 136 GLU A OE1 1 
ATOM   1036 O OE2 . GLU A 1 136 ? 55.446 -42.480 1.755   1.00 63.36 ? 136 GLU A OE2 1 
ATOM   1037 N N   . GLN A 1 137 ? 51.274 -43.244 7.242   1.00 78.92 ? 137 GLN A N   1 
ATOM   1038 C CA  . GLN A 1 137 ? 50.700 -44.072 8.312   1.00 84.61 ? 137 GLN A CA  1 
ATOM   1039 C C   . GLN A 1 137 ? 49.733 -45.110 7.727   1.00 84.99 ? 137 GLN A C   1 
ATOM   1040 O O   . GLN A 1 137 ? 49.536 -46.179 8.309   1.00 89.14 ? 137 GLN A O   1 
ATOM   1041 C CB  . GLN A 1 137 ? 49.992 -43.210 9.375   1.00 87.86 ? 137 GLN A CB  1 
ATOM   1042 C CG  . GLN A 1 137 ? 48.534 -42.878 9.074   1.00 87.07 ? 137 GLN A CG  1 
ATOM   1043 C CD  . GLN A 1 137 ? 47.955 -41.828 10.006  1.00 89.69 ? 137 GLN A CD  1 
ATOM   1044 O OE1 . GLN A 1 137 ? 48.390 -41.683 11.151  1.00 93.82 ? 137 GLN A OE1 1 
ATOM   1045 N NE2 . GLN A 1 137 ? 46.957 -41.095 9.521   1.00 87.62 ? 137 GLN A NE2 1 
ATOM   1046 N N   . ASP A 1 138 ? 49.126 -44.778 6.586   1.00 70.33 ? 138 ASP A N   1 
ATOM   1047 C CA  . ASP A 1 138 ? 48.284 -45.715 5.842   1.00 69.52 ? 138 ASP A CA  1 
ATOM   1048 C C   . ASP A 1 138 ? 49.186 -46.546 4.941   1.00 67.94 ? 138 ASP A C   1 
ATOM   1049 O O   . ASP A 1 138 ? 50.216 -46.053 4.467   1.00 67.75 ? 138 ASP A O   1 
ATOM   1050 C CB  . ASP A 1 138 ? 47.253 -44.974 4.980   1.00 68.39 ? 138 ASP A CB  1 
ATOM   1051 C CG  . ASP A 1 138 ? 46.550 -43.853 5.728   1.00 70.45 ? 138 ASP A CG  1 
ATOM   1052 O OD1 . ASP A 1 138 ? 46.300 -43.998 6.947   1.00 72.99 ? 138 ASP A OD1 1 
ATOM   1053 O OD2 . ASP A 1 138 ? 46.249 -42.822 5.088   1.00 69.72 ? 138 ASP A OD2 1 
ATOM   1054 N N   . LYS A 1 139 ? 48.802 -47.797 4.696   1.00 66.58 ? 139 LYS A N   1 
ATOM   1055 C CA  . LYS A 1 139 ? 49.621 -48.686 3.876   1.00 64.37 ? 139 LYS A CA  1 
ATOM   1056 C C   . LYS A 1 139 ? 48.853 -49.243 2.686   1.00 60.69 ? 139 LYS A C   1 
ATOM   1057 O O   . LYS A 1 139 ? 47.733 -49.740 2.819   1.00 61.28 ? 139 LYS A O   1 
ATOM   1058 C CB  . LYS A 1 139 ? 50.210 -49.820 4.722   1.00 67.19 ? 139 LYS A CB  1 
ATOM   1059 C CG  . LYS A 1 139 ? 51.636 -50.197 4.338   1.00 67.56 ? 139 LYS A CG  1 
ATOM   1060 C CD  . LYS A 1 139 ? 52.578 -49.006 4.467   1.00 67.87 ? 139 LYS A CD  1 
ATOM   1061 C CE  . LYS A 1 139 ? 54.034 -49.430 4.498   1.00 69.15 ? 139 LYS A CE  1 
ATOM   1062 N NZ  . LYS A 1 139 ? 54.932 -48.244 4.551   1.00 69.29 ? 139 LYS A NZ  1 
ATOM   1063 N N   . LEU A 1 140 ? 49.480 -49.141 1.519   1.00 56.42 ? 140 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 140 ? 48.909 -49.598 0.268   1.00 52.62 ? 140 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 140 ? 49.891 -50.553 -0.378  1.00 49.83 ? 140 LEU A C   1 
ATOM   1066 O O   . LEU A 1 140 ? 51.094 -50.468 -0.140  1.00 49.96 ? 140 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 140 ? 48.690 -48.409 -0.668  1.00 51.60 ? 140 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 140 ? 47.893 -47.215 -0.140  1.00 52.41 ? 140 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 140 ? 48.122 -46.003 -1.032  1.00 51.47 ? 140 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 140 ? 46.413 -47.548 -0.052  1.00 52.54 ? 140 LEU A CD2 1 
ATOM   1071 N N   . SER A 1 141 ? 49.383 -51.463 -1.197  1.00 47.01 ? 141 SER A N   1 
ATOM   1072 C CA  . SER A 1 141 ? 50.248 -52.317 -1.996  1.00 45.52 ? 141 SER A CA  1 
ATOM   1073 C C   . SER A 1 141 ? 51.069 -51.421 -2.918  1.00 42.30 ? 141 SER A C   1 
ATOM   1074 O O   . SER A 1 141 ? 50.538 -50.467 -3.481  1.00 40.18 ? 141 SER A O   1 
ATOM   1075 C CB  . SER A 1 141 ? 49.427 -53.305 -2.817  1.00 45.39 ? 141 SER A CB  1 
ATOM   1076 O OG  . SER A 1 141 ? 50.281 -54.184 -3.529  1.00 46.77 ? 141 SER A OG  1 
ATOM   1077 N N   . LYS A 1 142 ? 52.359 -51.718 -3.049  1.00 41.17 ? 142 LYS A N   1 
ATOM   1078 C CA  . LYS A 1 142 ? 53.275 -50.888 -3.837  1.00 39.48 ? 142 LYS A CA  1 
ATOM   1079 C C   . LYS A 1 142 ? 53.393 -51.322 -5.302  1.00 37.12 ? 142 LYS A C   1 
ATOM   1080 O O   . LYS A 1 142 ? 53.882 -50.558 -6.130  1.00 35.50 ? 142 LYS A O   1 
ATOM   1081 C CB  . LYS A 1 142 ? 54.668 -50.904 -3.210  1.00 41.20 ? 142 LYS A CB  1 
ATOM   1082 C CG  . LYS A 1 142 ? 54.763 -50.181 -1.880  1.00 42.94 ? 142 LYS A CG  1 
ATOM   1083 C CD  . LYS A 1 142 ? 56.157 -50.317 -1.290  1.00 44.89 ? 142 LYS A CD  1 
ATOM   1084 C CE  . LYS A 1 142 ? 56.421 -49.277 -0.213  1.00 46.45 ? 142 LYS A CE  1 
ATOM   1085 N NZ  . LYS A 1 142 ? 55.323 -49.202 0.790   1.00 47.54 ? 142 LYS A NZ  1 
ATOM   1086 N N   . ASN A 1 143 ? 52.939 -52.537 -5.608  1.00 36.42 ? 143 ASN A N   1 
ATOM   1087 C CA  A ASN A 1 143 ? 53.124 -53.120 -6.935  0.50 35.41 ? 143 ASN A CA  1 
ATOM   1088 C CA  B ASN A 1 143 ? 53.134 -53.149 -6.921  0.50 35.52 ? 143 ASN A CA  1 
ATOM   1089 C C   . ASN A 1 143 ? 51.824 -53.709 -7.491  1.00 34.44 ? 143 ASN A C   1 
ATOM   1090 O O   . ASN A 1 143 ? 50.768 -53.589 -6.871  1.00 34.78 ? 143 ASN A O   1 
ATOM   1091 C CB  A ASN A 1 143 ? 54.251 -54.160 -6.902  0.50 36.74 ? 143 ASN A CB  1 
ATOM   1092 C CB  B ASN A 1 143 ? 54.190 -54.256 -6.820  0.50 37.03 ? 143 ASN A CB  1 
ATOM   1093 C CG  A ASN A 1 143 ? 54.082 -55.178 -5.792  0.50 38.56 ? 143 ASN A CG  1 
ATOM   1094 C CG  B ASN A 1 143 ? 55.569 -53.720 -6.483  0.50 37.88 ? 143 ASN A CG  1 
ATOM   1095 O OD1 A ASN A 1 143 ? 53.033 -55.251 -5.151  0.50 38.78 ? 143 ASN A OD1 1 
ATOM   1096 O OD1 B ASN A 1 143 ? 56.273 -53.194 -7.345  0.50 37.42 ? 143 ASN A OD1 1 
ATOM   1097 N ND2 A ASN A 1 143 ? 55.117 -55.975 -5.564  0.50 40.11 ? 143 ASN A ND2 1 
ATOM   1098 N ND2 B ASN A 1 143 ? 55.967 -53.863 -5.226  0.50 39.41 ? 143 ASN A ND2 1 
ATOM   1099 N N   . GLY A 1 144 ? 51.894 -54.313 -8.677  1.00 33.00 ? 144 GLY A N   1 
ATOM   1100 C CA  . GLY A 1 144 ? 50.715 -54.865 -9.343  1.00 31.55 ? 144 GLY A CA  1 
ATOM   1101 C C   . GLY A 1 144 ? 49.893 -53.763 -9.989  1.00 29.39 ? 144 GLY A C   1 
ATOM   1102 O O   . GLY A 1 144 ? 48.677 -53.880 -10.116 1.00 28.39 ? 144 GLY A O   1 
ATOM   1103 N N   . SER A 1 145 ? 50.572 -52.700 -10.417 1.00 28.09 ? 145 SER A N   1 
ATOM   1104 C CA  . SER A 1 145 ? 49.917 -51.484 -10.898 1.00 26.77 ? 145 SER A CA  1 
ATOM   1105 C C   . SER A 1 145 ? 49.191 -51.667 -12.230 1.00 25.45 ? 145 SER A C   1 
ATOM   1106 O O   . SER A 1 145 ? 48.174 -51.014 -12.482 1.00 24.33 ? 145 SER A O   1 
ATOM   1107 C CB  . SER A 1 145 ? 50.949 -50.361 -11.051 1.00 26.60 ? 145 SER A CB  1 
ATOM   1108 O OG  . SER A 1 145 ? 50.338 -49.093 -10.922 1.00 26.55 ? 145 SER A OG  1 
ATOM   1109 N N   . TYR A 1 146 ? 49.717 -52.559 -13.066 1.00 25.41 ? 146 TYR A N   1 
ATOM   1110 C CA  . TYR A 1 146 ? 49.310 -52.687 -14.460 1.00 24.81 ? 146 TYR A CA  1 
ATOM   1111 C C   . TYR A 1 146 ? 48.643 -54.030 -14.754 1.00 25.04 ? 146 TYR A C   1 
ATOM   1112 O O   . TYR A 1 146 ? 49.260 -55.067 -14.534 1.00 26.19 ? 146 TYR A O   1 
ATOM   1113 C CB  . TYR A 1 146 ? 50.555 -52.573 -15.333 1.00 24.92 ? 146 TYR A CB  1 
ATOM   1114 C CG  . TYR A 1 146 ? 50.300 -52.580 -16.821 1.00 24.50 ? 146 TYR A CG  1 
ATOM   1115 C CD1 . TYR A 1 146 ? 49.980 -51.408 -17.497 1.00 23.81 ? 146 TYR A CD1 1 
ATOM   1116 C CD2 . TYR A 1 146 ? 50.415 -53.752 -17.561 1.00 25.06 ? 146 TYR A CD2 1 
ATOM   1117 C CE1 . TYR A 1 146 ? 49.770 -51.405 -18.864 1.00 23.73 ? 146 TYR A CE1 1 
ATOM   1118 C CE2 . TYR A 1 146 ? 50.207 -53.757 -18.929 1.00 24.99 ? 146 TYR A CE2 1 
ATOM   1119 C CZ  . TYR A 1 146 ? 49.883 -52.578 -19.574 1.00 24.33 ? 146 TYR A CZ  1 
ATOM   1120 O OH  . TYR A 1 146 ? 49.680 -52.577 -20.933 1.00 24.54 ? 146 TYR A OH  1 
ATOM   1121 N N   . PRO A 1 147 ? 47.404 -54.041 -15.246 1.00 24.89 ? 147 PRO A N   1 
ATOM   1122 C CA  . PRO A 1 147 ? 46.534 -52.868 -15.368 1.00 24.21 ? 147 PRO A CA  1 
ATOM   1123 C C   . PRO A 1 147 ? 45.819 -52.577 -14.050 1.00 24.55 ? 147 PRO A C   1 
ATOM   1124 O O   . PRO A 1 147 ? 45.921 -53.366 -13.110 1.00 25.76 ? 147 PRO A O   1 
ATOM   1125 C CB  . PRO A 1 147 ? 45.517 -53.312 -16.418 1.00 23.92 ? 147 PRO A CB  1 
ATOM   1126 C CG  . PRO A 1 147 ? 45.400 -54.782 -16.202 1.00 24.57 ? 147 PRO A CG  1 
ATOM   1127 C CD  . PRO A 1 147 ? 46.789 -55.240 -15.844 1.00 25.35 ? 147 PRO A CD  1 
ATOM   1128 N N   . SER A 1 148 ? 45.097 -51.462 -13.992 1.00 24.10 ? 148 SER A N   1 
ATOM   1129 C CA  . SER A 1 148 ? 44.329 -51.089 -12.800 1.00 24.49 ? 148 SER A CA  1 
ATOM   1130 C C   . SER A 1 148 ? 43.034 -51.904 -12.681 1.00 24.80 ? 148 SER A C   1 
ATOM   1131 O O   . SER A 1 148 ? 42.143 -51.795 -13.524 1.00 23.79 ? 148 SER A O   1 
ATOM   1132 C CB  . SER A 1 148 ? 43.988 -49.597 -12.823 1.00 24.10 ? 148 SER A CB  1 
ATOM   1133 O OG  . SER A 1 148 ? 43.061 -49.266 -11.799 1.00 24.57 ? 148 SER A OG  1 
ATOM   1134 N N   . GLY A 1 149 ? 42.938 -52.712 -11.630 1.00 25.67 ? 149 GLY A N   1 
ATOM   1135 C CA  . GLY A 1 149 ? 41.720 -53.467 -11.348 1.00 26.29 ? 149 GLY A CA  1 
ATOM   1136 C C   . GLY A 1 149 ? 40.525 -52.562 -11.115 1.00 26.25 ? 149 GLY A C   1 
ATOM   1137 O O   . GLY A 1 149 ? 39.455 -52.778 -11.686 1.00 25.61 ? 149 GLY A O   1 
ATOM   1138 N N   . HIS A 1 150 ? 40.711 -51.537 -10.285 1.00 26.94 ? 150 HIS A N   1 
ATOM   1139 C CA  . HIS A 1 150 ? 39.643 -50.581 -9.983  1.00 27.42 ? 150 HIS A CA  1 
ATOM   1140 C C   . HIS A 1 150 ? 39.103 -49.917 -11.246 1.00 26.20 ? 150 HIS A C   1 
ATOM   1141 O O   . HIS A 1 150 ? 37.888 -49.768 -11.411 1.00 26.12 ? 150 HIS A O   1 
ATOM   1142 C CB  . HIS A 1 150 ? 40.130 -49.502 -9.014  1.00 28.62 ? 150 HIS A CB  1 
ATOM   1143 C CG  . HIS A 1 150 ? 39.104 -48.450 -8.727  1.00 29.47 ? 150 HIS A CG  1 
ATOM   1144 N ND1 . HIS A 1 150 ? 38.199 -48.556 -7.692  1.00 31.18 ? 150 HIS A ND1 1 
ATOM   1145 C CD2 . HIS A 1 150 ? 38.827 -47.280 -9.352  1.00 29.66 ? 150 HIS A CD2 1 
ATOM   1146 C CE1 . HIS A 1 150 ? 37.414 -47.492 -7.687  1.00 31.35 ? 150 HIS A CE1 1 
ATOM   1147 N NE2 . HIS A 1 150 ? 37.773 -46.703 -8.685  1.00 30.49 ? 150 HIS A NE2 1 
ATOM   1148 N N   . THR A 1 151 ? 40.012 -49.515 -12.128 1.00 25.19 ? 151 THR A N   1 
ATOM   1149 C CA  . THR A 1 151 ? 39.643 -48.874 -13.380 1.00 24.43 ? 151 THR A CA  1 
ATOM   1150 C C   . THR A 1 151 ? 38.906 -49.839 -14.301 1.00 23.96 ? 151 THR A C   1 
ATOM   1151 O O   . THR A 1 151 ? 37.959 -49.443 -14.980 1.00 23.38 ? 151 THR A O   1 
ATOM   1152 C CB  . THR A 1 151 ? 40.883 -48.318 -14.093 1.00 24.25 ? 151 THR A CB  1 
ATOM   1153 O OG1 . THR A 1 151 ? 41.524 -47.370 -13.234 1.00 24.85 ? 151 THR A OG1 1 
ATOM   1154 C CG2 . THR A 1 151 ? 40.515 -47.646 -15.409 1.00 24.02 ? 151 THR A CG2 1 
ATOM   1155 N N   . SER A 1 152 ? 39.342 -51.098 -14.327 1.00 23.71 ? 152 SER A N   1 
ATOM   1156 C CA  . SER A 1 152 ? 38.652 -52.110 -15.105 1.00 23.48 ? 152 SER A CA  1 
ATOM   1157 C C   . SER A 1 152 ? 37.215 -52.280 -14.601 1.00 23.63 ? 152 SER A C   1 
ATOM   1158 O O   . SER A 1 152 ? 36.284 -52.349 -15.399 1.00 23.10 ? 152 SER A O   1 
ATOM   1159 C CB  . SER A 1 152 ? 39.400 -53.442 -15.069 1.00 23.92 ? 152 SER A CB  1 
ATOM   1160 O OG  . SER A 1 152 ? 38.723 -54.412 -15.854 1.00 24.00 ? 152 SER A OG  1 
ATOM   1161 N N   . ILE A 1 153 ? 37.039 -52.327 -13.282 1.00 24.27 ? 153 ILE A N   1 
ATOM   1162 C CA  . ILE A 1 153 ? 35.700 -52.395 -12.695 1.00 24.99 ? 153 ILE A CA  1 
ATOM   1163 C C   . ILE A 1 153 ? 34.900 -51.159 -13.096 1.00 24.76 ? 153 ILE A C   1 
ATOM   1164 O O   . ILE A 1 153 ? 33.754 -51.269 -13.528 1.00 24.80 ? 153 ILE A O   1 
ATOM   1165 C CB  . ILE A 1 153 ? 35.729 -52.509 -11.156 1.00 25.98 ? 153 ILE A CB  1 
ATOM   1166 C CG1 . ILE A 1 153 ? 36.375 -53.831 -10.725 1.00 26.68 ? 153 ILE A CG1 1 
ATOM   1167 C CG2 . ILE A 1 153 ? 34.314 -52.423 -10.584 1.00 26.66 ? 153 ILE A CG2 1 
ATOM   1168 C CD1 . ILE A 1 153 ? 36.809 -53.855 -9.273  1.00 27.82 ? 153 ILE A CD1 1 
ATOM   1169 N N   . GLY A 1 154 ? 35.514 -49.987 -12.954 1.00 24.57 ? 154 GLY A N   1 
ATOM   1170 C CA  . GLY A 1 154 ? 34.875 -48.729 -13.325 1.00 24.52 ? 154 GLY A CA  1 
ATOM   1171 C C   . GLY A 1 154 ? 34.361 -48.721 -14.755 1.00 24.11 ? 154 GLY A C   1 
ATOM   1172 O O   . GLY A 1 154 ? 33.208 -48.367 -15.005 1.00 24.31 ? 154 GLY A O   1 
ATOM   1173 N N   . TRP A 1 155 ? 35.204 -49.134 -15.694 1.00 23.47 ? 155 TRP A N   1 
ATOM   1174 C CA  . TRP A 1 155 ? 34.832 -49.093 -17.101 1.00 23.36 ? 155 TRP A CA  1 
ATOM   1175 C C   . TRP A 1 155 ? 33.805 -50.175 -17.446 1.00 23.50 ? 155 TRP A C   1 
ATOM   1176 O O   . TRP A 1 155 ? 32.820 -49.898 -18.126 1.00 23.61 ? 155 TRP A O   1 
ATOM   1177 C CB  . TRP A 1 155 ? 36.067 -49.205 -17.997 1.00 23.14 ? 155 TRP A CB  1 
ATOM   1178 C CG  . TRP A 1 155 ? 35.778 -48.899 -19.429 1.00 23.14 ? 155 TRP A CG  1 
ATOM   1179 C CD1 . TRP A 1 155 ? 35.914 -49.743 -20.492 1.00 23.23 ? 155 TRP A CD1 1 
ATOM   1180 C CD2 . TRP A 1 155 ? 35.283 -47.664 -19.957 1.00 23.50 ? 155 TRP A CD2 1 
ATOM   1181 N NE1 . TRP A 1 155 ? 35.544 -49.106 -21.653 1.00 23.61 ? 155 TRP A NE1 1 
ATOM   1182 C CE2 . TRP A 1 155 ? 35.155 -47.828 -21.353 1.00 23.64 ? 155 TRP A CE2 1 
ATOM   1183 C CE3 . TRP A 1 155 ? 34.947 -46.430 -19.389 1.00 23.83 ? 155 TRP A CE3 1 
ATOM   1184 C CZ2 . TRP A 1 155 ? 34.693 -46.811 -22.185 1.00 24.19 ? 155 TRP A CZ2 1 
ATOM   1185 C CZ3 . TRP A 1 155 ? 34.490 -45.419 -20.220 1.00 24.44 ? 155 TRP A CZ3 1 
ATOM   1186 C CH2 . TRP A 1 155 ? 34.368 -45.617 -21.604 1.00 24.53 ? 155 TRP A CH2 1 
ATOM   1187 N N   . ALA A 1 156 ? 34.028 -51.397 -16.967 1.00 23.52 ? 156 ALA A N   1 
ATOM   1188 C CA  . ALA A 1 156 ? 33.062 -52.477 -17.162 1.00 23.69 ? 156 ALA A CA  1 
ATOM   1189 C C   . ALA A 1 156 ? 31.695 -52.088 -16.605 1.00 24.02 ? 156 ALA A C   1 
ATOM   1190 O O   . ALA A 1 156 ? 30.674 -52.280 -17.263 1.00 24.18 ? 156 ALA A O   1 
ATOM   1191 C CB  . ALA A 1 156 ? 33.552 -53.760 -16.512 1.00 23.98 ? 156 ALA A CB  1 
ATOM   1192 N N   . THR A 1 157 ? 31.689 -51.535 -15.396 1.00 24.21 ? 157 THR A N   1 
ATOM   1193 C CA  . THR A 1 157 ? 30.465 -51.067 -14.762 1.00 24.72 ? 157 THR A CA  1 
ATOM   1194 C C   . THR A 1 157 ? 29.784 -49.978 -15.595 1.00 24.80 ? 157 THR A C   1 
ATOM   1195 O O   . THR A 1 157 ? 28.565 -49.989 -15.748 1.00 25.41 ? 157 THR A O   1 
ATOM   1196 C CB  . THR A 1 157 ? 30.743 -50.555 -13.336 1.00 25.24 ? 157 THR A CB  1 
ATOM   1197 O OG1 . THR A 1 157 ? 31.257 -51.629 -12.542 1.00 25.25 ? 157 THR A OG1 1 
ATOM   1198 C CG2 . THR A 1 157 ? 29.476 -50.015 -12.681 1.00 26.23 ? 157 THR A CG2 1 
ATOM   1199 N N   . ALA A 1 158 ? 30.568 -49.050 -16.135 1.00 24.24 ? 158 ALA A N   1 
ATOM   1200 C CA  . ALA A 1 158 ? 30.032 -48.001 -17.005 1.00 24.52 ? 158 ALA A CA  1 
ATOM   1201 C C   . ALA A 1 158 ? 29.337 -48.573 -18.243 1.00 24.50 ? 158 ALA A C   1 
ATOM   1202 O O   . ALA A 1 158 ? 28.260 -48.111 -18.627 1.00 24.87 ? 158 ALA A O   1 
ATOM   1203 C CB  . ALA A 1 158 ? 31.135 -47.043 -17.426 1.00 24.24 ? 158 ALA A CB  1 
ATOM   1204 N N   . LEU A 1 159 ? 29.956 -49.574 -18.862 1.00 24.05 ? 159 LEU A N   1 
ATOM   1205 C CA  . LEU A 1 159 ? 29.408 -50.181 -20.070 1.00 24.26 ? 159 LEU A CA  1 
ATOM   1206 C C   . LEU A 1 159 ? 28.092 -50.900 -19.784 1.00 24.83 ? 159 LEU A C   1 
ATOM   1207 O O   . LEU A 1 159 ? 27.158 -50.836 -20.583 1.00 25.18 ? 159 LEU A O   1 
ATOM   1208 C CB  . LEU A 1 159 ? 30.418 -51.149 -20.689 1.00 23.96 ? 159 LEU A CB  1 
ATOM   1209 C CG  . LEU A 1 159 ? 31.712 -50.502 -21.197 1.00 23.69 ? 159 LEU A CG  1 
ATOM   1210 C CD1 . LEU A 1 159 ? 32.741 -51.569 -21.525 1.00 23.44 ? 159 LEU A CD1 1 
ATOM   1211 C CD2 . LEU A 1 159 ? 31.448 -49.604 -22.397 1.00 24.09 ? 159 LEU A CD2 1 
ATOM   1212 N N   . VAL A 1 160 ? 28.021 -51.572 -18.639 1.00 25.04 ? 160 VAL A N   1 
ATOM   1213 C CA  . VAL A 1 160 ? 26.801 -52.262 -18.232 1.00 25.76 ? 160 VAL A CA  1 
ATOM   1214 C C   . VAL A 1 160 ? 25.718 -51.236 -17.900 1.00 26.47 ? 160 VAL A C   1 
ATOM   1215 O O   . VAL A 1 160 ? 24.593 -51.332 -18.396 1.00 26.89 ? 160 VAL A O   1 
ATOM   1216 C CB  . VAL A 1 160 ? 27.066 -53.223 -17.055 1.00 26.02 ? 160 VAL A CB  1 
ATOM   1217 C CG1 . VAL A 1 160 ? 25.766 -53.803 -16.506 1.00 26.89 ? 160 VAL A CG1 1 
ATOM   1218 C CG2 . VAL A 1 160 ? 27.984 -54.348 -17.511 1.00 25.77 ? 160 VAL A CG2 1 
ATOM   1219 N N   . LEU A 1 161 ? 26.069 -50.240 -17.090 1.00 26.52 ? 161 LEU A N   1 
ATOM   1220 C CA  . LEU A 1 161 ? 25.140 -49.165 -16.739 1.00 27.29 ? 161 LEU A CA  1 
ATOM   1221 C C   . LEU A 1 161 ? 24.616 -48.398 -17.953 1.00 27.51 ? 161 LEU A C   1 
ATOM   1222 O O   . LEU A 1 161 ? 23.450 -47.997 -17.978 1.00 28.15 ? 161 LEU A O   1 
ATOM   1223 C CB  . LEU A 1 161 ? 25.788 -48.183 -15.759 1.00 27.48 ? 161 LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 161 ? 25.870 -48.628 -14.297 1.00 27.90 ? 161 LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 161 ? 26.631 -47.595 -13.482 1.00 28.15 ? 161 LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 161 ? 24.485 -48.856 -13.712 1.00 28.96 ? 161 LEU A CD2 1 
ATOM   1227 N N   . ALA A 1 162 ? 25.477 -48.186 -18.945 1.00 26.98 ? 162 ALA A N   1 
ATOM   1228 C CA  . ALA A 1 162 ? 25.085 -47.486 -20.168 1.00 27.49 ? 162 ALA A CA  1 
ATOM   1229 C C   . ALA A 1 162 ? 24.021 -48.278 -20.930 1.00 27.85 ? 162 ALA A C   1 
ATOM   1230 O O   . ALA A 1 162 ? 23.101 -47.699 -21.509 1.00 28.77 ? 162 ALA A O   1 
ATOM   1231 C CB  . ALA A 1 162 ? 26.300 -47.234 -21.049 1.00 27.01 ? 162 ALA A CB  1 
ATOM   1232 N N   . GLU A 1 163 ? 24.147 -49.602 -20.916 1.00 27.33 ? 163 GLU A N   1 
ATOM   1233 C CA  . GLU A 1 163 ? 23.145 -50.474 -21.519 1.00 27.73 ? 163 GLU A CA  1 
ATOM   1234 C C   . GLU A 1 163 ? 21.807 -50.412 -20.774 1.00 28.37 ? 163 GLU A C   1 
ATOM   1235 O O   . GLU A 1 163 ? 20.749 -50.490 -21.394 1.00 28.94 ? 163 GLU A O   1 
ATOM   1236 C CB  . GLU A 1 163 ? 23.645 -51.921 -21.565 1.00 27.31 ? 163 GLU A CB  1 
ATOM   1237 C CG  . GLU A 1 163 ? 22.695 -52.864 -22.285 1.00 27.91 ? 163 GLU A CG  1 
ATOM   1238 C CD  . GLU A 1 163 ? 23.135 -54.309 -22.240 1.00 27.82 ? 163 GLU A CD  1 
ATOM   1239 O OE1 . GLU A 1 163 ? 22.245 -55.184 -22.287 1.00 28.37 ? 163 GLU A OE1 1 
ATOM   1240 O OE2 . GLU A 1 163 ? 24.353 -54.578 -22.176 1.00 27.46 ? 163 GLU A OE2 1 
ATOM   1241 N N   . ILE A 1 164 ? 21.854 -50.280 -19.452 1.00 28.16 ? 164 ILE A N   1 
ATOM   1242 C CA  . ILE A 1 164 ? 20.634 -50.240 -18.644 1.00 29.12 ? 164 ILE A CA  1 
ATOM   1243 C C   . ILE A 1 164 ? 19.920 -48.891 -18.788 1.00 29.98 ? 164 ILE A C   1 
ATOM   1244 O O   . ILE A 1 164 ? 18.691 -48.837 -18.836 1.00 30.64 ? 164 ILE A O   1 
ATOM   1245 C CB  . ILE A 1 164 ? 20.933 -50.551 -17.158 1.00 29.15 ? 164 ILE A CB  1 
ATOM   1246 C CG1 . ILE A 1 164 ? 21.510 -51.968 -17.024 1.00 28.58 ? 164 ILE A CG1 1 
ATOM   1247 C CG2 . ILE A 1 164 ? 19.672 -50.437 -16.310 1.00 30.42 ? 164 ILE A CG2 1 
ATOM   1248 C CD1 . ILE A 1 164 ? 22.132 -52.266 -15.675 1.00 28.65 ? 164 ILE A CD1 1 
ATOM   1249 N N   . ASN A 1 165 ? 20.694 -47.808 -18.870 1.00 29.82 ? 165 ASN A N   1 
ATOM   1250 C CA  . ASN A 1 165 ? 20.133 -46.462 -18.984 1.00 31.15 ? 165 ASN A CA  1 
ATOM   1251 C C   . ASN A 1 165 ? 20.790 -45.697 -20.138 1.00 31.19 ? 165 ASN A C   1 
ATOM   1252 O O   . ASN A 1 165 ? 21.599 -44.795 -19.911 1.00 30.84 ? 165 ASN A O   1 
ATOM   1253 C CB  . ASN A 1 165 ? 20.299 -45.719 -17.653 1.00 31.65 ? 165 ASN A CB  1 
ATOM   1254 C CG  . ASN A 1 165 ? 19.562 -44.390 -17.616 1.00 33.19 ? 165 ASN A CG  1 
ATOM   1255 O OD1 . ASN A 1 165 ? 18.777 -44.066 -18.506 1.00 34.07 ? 165 ASN A OD1 1 
ATOM   1256 N ND2 . ASN A 1 165 ? 19.804 -43.619 -16.565 1.00 33.93 ? 165 ASN A ND2 1 
ATOM   1257 N N   . PRO A 1 166 ? 20.444 -46.061 -21.388 1.00 31.75 ? 166 PRO A N   1 
ATOM   1258 C CA  . PRO A 1 166 ? 21.049 -45.423 -22.562 1.00 32.11 ? 166 PRO A CA  1 
ATOM   1259 C C   . PRO A 1 166 ? 20.779 -43.920 -22.666 1.00 33.76 ? 166 PRO A C   1 
ATOM   1260 O O   . PRO A 1 166 ? 21.582 -43.202 -23.256 1.00 33.86 ? 166 PRO A O   1 
ATOM   1261 C CB  . PRO A 1 166 ? 20.421 -46.176 -23.745 1.00 32.34 ? 166 PRO A CB  1 
ATOM   1262 C CG  . PRO A 1 166 ? 19.194 -46.815 -23.200 1.00 32.72 ? 166 PRO A CG  1 
ATOM   1263 C CD  . PRO A 1 166 ? 19.525 -47.145 -21.776 1.00 31.93 ? 166 PRO A CD  1 
ATOM   1264 N N   . GLN A 1 167 ? 19.676 -43.451 -22.086 1.00 35.29 ? 167 GLN A N   1 
ATOM   1265 C CA  . GLN A 1 167 ? 19.374 -42.019 -22.056 1.00 37.19 ? 167 GLN A CA  1 
ATOM   1266 C C   . GLN A 1 167 ? 20.446 -41.189 -21.342 1.00 36.43 ? 167 GLN A C   1 
ATOM   1267 O O   . GLN A 1 167 ? 20.577 -39.994 -21.606 1.00 37.45 ? 167 GLN A O   1 
ATOM   1268 C CB  . GLN A 1 167 ? 18.007 -41.768 -21.417 1.00 39.49 ? 167 GLN A CB  1 
ATOM   1269 C CG  . GLN A 1 167 ? 16.845 -42.137 -22.321 1.00 41.30 ? 167 GLN A CG  1 
ATOM   1270 C CD  . GLN A 1 167 ? 15.500 -41.964 -21.640 1.00 43.58 ? 167 GLN A CD  1 
ATOM   1271 O OE1 . GLN A 1 167 ? 15.181 -42.674 -20.682 1.00 44.29 ? 167 GLN A OE1 1 
ATOM   1272 N NE2 . GLN A 1 167 ? 14.698 -41.026 -22.134 1.00 45.75 ? 167 GLN A NE2 1 
ATOM   1273 N N   . ARG A 1 168 ? 21.203 -41.812 -20.442 1.00 34.48 ? 168 ARG A N   1 
ATOM   1274 C CA  . ARG A 1 168 ? 22.322 -41.134 -19.791 1.00 33.83 ? 168 ARG A CA  1 
ATOM   1275 C C   . ARG A 1 168 ? 23.654 -41.845 -20.035 1.00 31.43 ? 168 ARG A C   1 
ATOM   1276 O O   . ARG A 1 168 ? 24.575 -41.759 -19.222 1.00 30.47 ? 168 ARG A O   1 
ATOM   1277 C CB  . ARG A 1 168 ? 22.029 -40.964 -18.299 1.00 34.59 ? 168 ARG A CB  1 
ATOM   1278 C CG  . ARG A 1 168 ? 20.909 -39.961 -18.053 1.00 36.86 ? 168 ARG A CG  1 
ATOM   1279 C CD  . ARG A 1 168 ? 20.642 -39.745 -16.578 1.00 37.98 ? 168 ARG A CD  1 
ATOM   1280 N NE  . ARG A 1 168 ? 21.790 -39.156 -15.885 1.00 38.02 ? 168 ARG A NE  1 
ATOM   1281 C CZ  . ARG A 1 168 ? 22.027 -37.851 -15.749 1.00 39.26 ? 168 ARG A CZ  1 
ATOM   1282 N NH1 . ARG A 1 168 ? 21.211 -36.943 -16.270 1.00 40.94 ? 168 ARG A NH1 1 
ATOM   1283 N NH2 . ARG A 1 168 ? 23.105 -37.452 -15.083 1.00 39.03 ? 168 ARG A NH2 1 
ATOM   1284 N N   . GLN A 1 169 ? 23.766 -42.510 -21.183 1.00 30.37 ? 169 GLN A N   1 
ATOM   1285 C CA  . GLN A 1 169 ? 24.967 -43.285 -21.503 1.00 28.78 ? 169 GLN A CA  1 
ATOM   1286 C C   . GLN A 1 169 ? 26.227 -42.425 -21.479 1.00 28.26 ? 169 GLN A C   1 
ATOM   1287 O O   . GLN A 1 169 ? 27.270 -42.868 -21.017 1.00 27.05 ? 169 GLN A O   1 
ATOM   1288 C CB  . GLN A 1 169 ? 24.836 -43.995 -22.859 1.00 28.68 ? 169 GLN A CB  1 
ATOM   1289 C CG  . GLN A 1 169 ? 24.761 -43.088 -24.081 1.00 29.79 ? 169 GLN A CG  1 
ATOM   1290 C CD  . GLN A 1 169 ? 24.609 -43.869 -25.378 1.00 29.96 ? 169 GLN A CD  1 
ATOM   1291 O OE1 . GLN A 1 169 ? 24.767 -45.090 -25.403 1.00 29.24 ? 169 GLN A OE1 1 
ATOM   1292 N NE2 . GLN A 1 169 ? 24.315 -43.165 -26.463 1.00 31.15 ? 169 GLN A NE2 1 
ATOM   1293 N N   . ASN A 1 170 ? 26.124 -41.193 -21.963 1.00 29.22 ? 170 ASN A N   1 
ATOM   1294 C CA  . ASN A 1 170 ? 27.296 -40.332 -22.060 1.00 29.35 ? 170 ASN A CA  1 
ATOM   1295 C C   . ASN A 1 170 ? 27.767 -39.838 -20.697 1.00 29.14 ? 170 ASN A C   1 
ATOM   1296 O O   . ASN A 1 170 ? 28.962 -39.827 -20.427 1.00 28.18 ? 170 ASN A O   1 
ATOM   1297 C CB  . ASN A 1 170 ? 27.033 -39.190 -23.034 1.00 30.85 ? 170 ASN A CB  1 
ATOM   1298 C CG  . ASN A 1 170 ? 26.911 -39.688 -24.462 1.00 31.11 ? 170 ASN A CG  1 
ATOM   1299 O OD1 . ASN A 1 170 ? 27.761 -40.448 -24.936 1.00 30.35 ? 170 ASN A OD1 1 
ATOM   1300 N ND2 . ASN A 1 170 ? 25.852 -39.296 -25.141 1.00 32.56 ? 170 ASN A ND2 1 
ATOM   1301 N N   . GLU A 1 171 ? 26.826 -39.471 -19.833 1.00 30.04 ? 171 GLU A N   1 
ATOM   1302 C CA  . GLU A 1 171 ? 27.150 -39.126 -18.448 1.00 30.20 ? 171 GLU A CA  1 
ATOM   1303 C C   . GLU A 1 171 ? 27.771 -40.332 -17.741 1.00 28.61 ? 171 GLU A C   1 
ATOM   1304 O O   . GLU A 1 171 ? 28.776 -40.204 -17.041 1.00 28.04 ? 171 GLU A O   1 
ATOM   1305 C CB  . GLU A 1 171 ? 25.904 -38.658 -17.691 1.00 31.82 ? 171 GLU A CB  1 
ATOM   1306 C CG  . GLU A 1 171 ? 25.331 -37.329 -18.168 1.00 33.88 ? 171 GLU A CG  1 
ATOM   1307 C CD  . GLU A 1 171 ? 24.368 -37.452 -19.340 1.00 34.74 ? 171 GLU A CD  1 
ATOM   1308 O OE1 . GLU A 1 171 ? 24.212 -38.554 -19.910 1.00 33.96 ? 171 GLU A OE1 1 
ATOM   1309 O OE2 . GLU A 1 171 ? 23.758 -36.428 -19.698 1.00 37.19 ? 171 GLU A OE2 1 
ATOM   1310 N N   . ILE A 1 172 ? 27.177 -41.505 -17.945 1.00 28.01 ? 172 ILE A N   1 
ATOM   1311 C CA  . ILE A 1 172 ? 27.674 -42.740 -17.336 1.00 26.92 ? 172 ILE A CA  1 
ATOM   1312 C C   . ILE A 1 172 ? 29.088 -43.065 -17.811 1.00 26.09 ? 172 ILE A C   1 
ATOM   1313 O O   . ILE A 1 172 ? 29.974 -43.352 -17.003 1.00 25.15 ? 172 ILE A O   1 
ATOM   1314 C CB  . ILE A 1 172 ? 26.727 -43.924 -17.630 1.00 26.70 ? 172 ILE A CB  1 
ATOM   1315 C CG1 . ILE A 1 172 ? 25.412 -43.744 -16.859 1.00 27.75 ? 172 ILE A CG1 1 
ATOM   1316 C CG2 . ILE A 1 172 ? 27.375 -45.253 -17.265 1.00 25.61 ? 172 ILE A CG2 1 
ATOM   1317 C CD1 . ILE A 1 172 ? 24.240 -44.498 -17.454 1.00 28.08 ? 172 ILE A CD1 1 
ATOM   1318 N N   . LEU A 1 173 ? 29.298 -43.014 -19.122 1.00 26.23 ? 173 LEU A N   1 
ATOM   1319 C CA  . LEU A 1 173 ? 30.605 -43.320 -19.687 1.00 25.99 ? 173 LEU A CA  1 
ATOM   1320 C C   . LEU A 1 173 ? 31.666 -42.320 -19.221 1.00 26.48 ? 173 LEU A C   1 
ATOM   1321 O O   . LEU A 1 173 ? 32.785 -42.717 -18.894 1.00 25.75 ? 173 LEU A O   1 
ATOM   1322 C CB  . LEU A 1 173 ? 30.536 -43.370 -21.213 1.00 26.14 ? 173 LEU A CB  1 
ATOM   1323 C CG  . LEU A 1 173 ? 29.727 -44.542 -21.788 1.00 26.14 ? 173 LEU A CG  1 
ATOM   1324 C CD1 . LEU A 1 173 ? 29.350 -44.258 -23.237 1.00 26.96 ? 173 LEU A CD1 1 
ATOM   1325 C CD2 . LEU A 1 173 ? 30.477 -45.860 -21.664 1.00 25.22 ? 173 LEU A CD2 1 
ATOM   1326 N N   . LYS A 1 174 ? 31.317 -41.036 -19.181 1.00 28.06 ? 174 LYS A N   1 
ATOM   1327 C CA  . LYS A 1 174 ? 32.246 -40.019 -18.688 1.00 29.16 ? 174 LYS A CA  1 
ATOM   1328 C C   . LYS A 1 174 ? 32.631 -40.318 -17.243 1.00 28.58 ? 174 LYS A C   1 
ATOM   1329 O O   . LYS A 1 174 ? 33.799 -40.231 -16.878 1.00 27.76 ? 174 LYS A O   1 
ATOM   1330 C CB  . LYS A 1 174 ? 31.648 -38.614 -18.778 1.00 31.49 ? 174 LYS A CB  1 
ATOM   1331 C CG  . LYS A 1 174 ? 31.591 -38.042 -20.189 1.00 33.41 ? 174 LYS A CG  1 
ATOM   1332 C CD  . LYS A 1 174 ? 30.948 -36.657 -20.197 1.00 35.89 ? 174 LYS A CD  1 
ATOM   1333 C CE  . LYS A 1 174 ? 29.804 -36.575 -21.191 1.00 37.42 ? 174 LYS A CE  1 
ATOM   1334 N NZ  . LYS A 1 174 ? 28.979 -35.358 -20.981 1.00 39.86 ? 174 LYS A NZ  1 
ATOM   1335 N N   . ARG A 1 175 ? 31.645 -40.682 -16.429 1.00 28.71 ? 175 ARG A N   1 
ATOM   1336 C CA  . ARG A 1 175 ? 31.901 -40.999 -15.028 1.00 28.71 ? 175 ARG A CA  1 
ATOM   1337 C C   . ARG A 1 175 ? 32.852 -42.184 -14.894 1.00 27.54 ? 175 ARG A C   1 
ATOM   1338 O O   . ARG A 1 175 ? 33.805 -42.134 -14.119 1.00 26.89 ? 175 ARG A O   1 
ATOM   1339 C CB  . ARG A 1 175 ? 30.590 -41.272 -14.280 1.00 29.51 ? 175 ARG A CB  1 
ATOM   1340 C CG  . ARG A 1 175 ? 30.752 -41.581 -12.798 1.00 29.96 ? 175 ARG A CG  1 
ATOM   1341 C CD  . ARG A 1 175 ? 31.582 -40.531 -12.077 1.00 30.84 ? 175 ARG A CD  1 
ATOM   1342 N NE  . ARG A 1 175 ? 31.692 -40.826 -10.651 1.00 31.78 ? 175 ARG A NE  1 
ATOM   1343 C CZ  . ARG A 1 175 ? 32.757 -40.568 -9.891  1.00 32.14 ? 175 ARG A CZ  1 
ATOM   1344 N NH1 . ARG A 1 175 ? 33.853 -40.005 -10.400 1.00 31.70 ? 175 ARG A NH1 1 
ATOM   1345 N NH2 . ARG A 1 175 ? 32.728 -40.893 -8.603  1.00 33.13 ? 175 ARG A NH2 1 
ATOM   1346 N N   . GLY A 1 176 ? 32.594 -43.240 -15.662 1.00 27.08 ? 176 GLY A N   1 
ATOM   1347 C CA  . GLY A 1 176 ? 33.450 -44.420 -15.666 1.00 26.67 ? 176 GLY A CA  1 
ATOM   1348 C C   . GLY A 1 176 ? 34.872 -44.095 -16.079 1.00 26.66 ? 176 GLY A C   1 
ATOM   1349 O O   . GLY A 1 176 ? 35.827 -44.570 -15.471 1.00 25.88 ? 176 GLY A O   1 
ATOM   1350 N N   . TYR A 1 177 ? 35.001 -43.276 -17.117 1.00 27.41 ? 177 TYR A N   1 
ATOM   1351 C CA  . TYR A 1 177 ? 36.297 -42.785 -17.565 1.00 27.79 ? 177 TYR A CA  1 
ATOM   1352 C C   . TYR A 1 177 ? 37.004 -42.015 -16.444 1.00 27.71 ? 177 TYR A C   1 
ATOM   1353 O O   . TYR A 1 177 ? 38.185 -42.241 -16.169 1.00 26.37 ? 177 TYR A O   1 
ATOM   1354 C CB  . TYR A 1 177 ? 36.118 -41.876 -18.787 1.00 29.17 ? 177 TYR A CB  1 
ATOM   1355 C CG  . TYR A 1 177 ? 37.414 -41.518 -19.469 1.00 30.30 ? 177 TYR A CG  1 
ATOM   1356 C CD1 . TYR A 1 177 ? 37.944 -42.337 -20.455 1.00 30.57 ? 177 TYR A CD1 1 
ATOM   1357 C CD2 . TYR A 1 177 ? 38.113 -40.361 -19.129 1.00 31.73 ? 177 TYR A CD2 1 
ATOM   1358 C CE1 . TYR A 1 177 ? 39.135 -42.021 -21.082 1.00 31.43 ? 177 TYR A CE1 1 
ATOM   1359 C CE2 . TYR A 1 177 ? 39.308 -40.038 -19.757 1.00 32.52 ? 177 TYR A CE2 1 
ATOM   1360 C CZ  . TYR A 1 177 ? 39.810 -40.879 -20.732 1.00 32.46 ? 177 TYR A CZ  1 
ATOM   1361 O OH  . TYR A 1 177 ? 40.991 -40.593 -21.378 1.00 35.03 ? 177 TYR A OH  1 
ATOM   1362 N N   . GLU A 1 178 ? 36.275 -41.113 -15.796 1.00 28.23 ? 178 GLU A N   1 
ATOM   1363 C CA  . GLU A 1 178 ? 36.878 -40.263 -14.773 1.00 29.17 ? 178 GLU A CA  1 
ATOM   1364 C C   . GLU A 1 178 ? 37.312 -41.025 -13.517 1.00 28.08 ? 178 GLU A C   1 
ATOM   1365 O O   . GLU A 1 178 ? 38.262 -40.615 -12.857 1.00 27.71 ? 178 GLU A O   1 
ATOM   1366 C CB  . GLU A 1 178 ? 35.963 -39.090 -14.409 1.00 31.27 ? 178 GLU A CB  1 
ATOM   1367 C CG  . GLU A 1 178 ? 35.846 -38.027 -15.500 1.00 33.05 ? 178 GLU A CG  1 
ATOM   1368 C CD  . GLU A 1 178 ? 37.167 -37.355 -15.879 1.00 34.32 ? 178 GLU A CD  1 
ATOM   1369 O OE1 . GLU A 1 178 ? 38.186 -37.486 -15.155 1.00 34.35 ? 178 GLU A OE1 1 
ATOM   1370 O OE2 . GLU A 1 178 ? 37.184 -36.679 -16.932 1.00 36.06 ? 178 GLU A OE2 1 
ATOM   1371 N N   . LEU A 1 179 ? 36.644 -42.133 -13.198 1.00 27.18 ? 179 LEU A N   1 
ATOM   1372 C CA  . LEU A 1 179 ? 37.098 -42.994 -12.094 1.00 26.92 ? 179 LEU A CA  1 
ATOM   1373 C C   . LEU A 1 179 ? 38.539 -43.441 -12.331 1.00 25.90 ? 179 LEU A C   1 
ATOM   1374 O O   . LEU A 1 179 ? 39.349 -43.445 -11.409 1.00 25.96 ? 179 LEU A O   1 
ATOM   1375 C CB  . LEU A 1 179 ? 36.199 -44.220 -11.924 1.00 26.89 ? 179 LEU A CB  1 
ATOM   1376 C CG  . LEU A 1 179 ? 34.832 -43.978 -11.281 1.00 27.81 ? 179 LEU A CG  1 
ATOM   1377 C CD1 . LEU A 1 179 ? 33.986 -45.237 -11.381 1.00 27.82 ? 179 LEU A CD1 1 
ATOM   1378 C CD2 . LEU A 1 179 ? 34.978 -43.541 -9.831  1.00 28.84 ? 179 LEU A CD2 1 
ATOM   1379 N N   . GLY A 1 180 ? 38.847 -43.807 -13.571 1.00 24.78 ? 180 GLY A N   1 
ATOM   1380 C CA  . GLY A 1 180 ? 40.211 -44.140 -13.954 1.00 24.42 ? 180 GLY A CA  1 
ATOM   1381 C C   . GLY A 1 180 ? 41.154 -42.962 -13.786 1.00 24.61 ? 180 GLY A C   1 
ATOM   1382 O O   . GLY A 1 180 ? 42.201 -43.085 -13.162 1.00 24.93 ? 180 GLY A O   1 
ATOM   1383 N N   . GLU A 1 181 ? 40.769 -41.808 -14.317 1.00 24.86 ? 181 GLU A N   1 
ATOM   1384 C CA  . GLU A 1 181 ? 41.623 -40.624 -14.249 1.00 25.39 ? 181 GLU A CA  1 
ATOM   1385 C C   . GLU A 1 181 ? 41.864 -40.162 -12.810 1.00 25.45 ? 181 GLU A C   1 
ATOM   1386 O O   . GLU A 1 181 ? 42.944 -39.665 -12.496 1.00 25.39 ? 181 GLU A O   1 
ATOM   1387 C CB  . GLU A 1 181 ? 41.055 -39.485 -15.107 1.00 26.50 ? 181 GLU A CB  1 
ATOM   1388 C CG  . GLU A 1 181 ? 40.988 -39.813 -16.598 1.00 26.89 ? 181 GLU A CG  1 
ATOM   1389 C CD  . GLU A 1 181 ? 42.293 -40.381 -17.145 1.00 27.04 ? 181 GLU A CD  1 
ATOM   1390 O OE1 . GLU A 1 181 ? 43.367 -39.786 -16.875 1.00 28.31 ? 181 GLU A OE1 1 
ATOM   1391 O OE2 . GLU A 1 181 ? 42.256 -41.429 -17.831 1.00 26.54 ? 181 GLU A OE2 1 
ATOM   1392 N N   . SER A 1 182 ? 40.875 -40.342 -11.938 1.00 25.34 ? 182 SER A N   1 
ATOM   1393 C CA  . SER A 1 182 ? 41.047 -40.032 -10.514 1.00 26.05 ? 182 SER A CA  1 
ATOM   1394 C C   . SER A 1 182 ? 42.227 -40.786 -9.895  1.00 25.78 ? 182 SER A C   1 
ATOM   1395 O O   . SER A 1 182 ? 42.946 -40.241 -9.063  1.00 26.45 ? 182 SER A O   1 
ATOM   1396 C CB  . SER A 1 182 ? 39.769 -40.340 -9.738  1.00 26.44 ? 182 SER A CB  1 
ATOM   1397 O OG  . SER A 1 182 ? 38.773 -39.370 -10.002 1.00 26.96 ? 182 SER A OG  1 
ATOM   1398 N N   . ARG A 1 183 ? 42.427 -42.031 -10.316 1.00 25.31 ? 183 ARG A N   1 
ATOM   1399 C CA  . ARG A 1 183 ? 43.534 -42.845 -9.817  1.00 25.62 ? 183 ARG A CA  1 
ATOM   1400 C C   . ARG A 1 183 ? 44.891 -42.344 -10.320 1.00 25.04 ? 183 ARG A C   1 
ATOM   1401 O O   . ARG A 1 183 ? 45.900 -42.489 -9.632  1.00 25.26 ? 183 ARG A O   1 
ATOM   1402 C CB  . ARG A 1 183 ? 43.335 -44.310 -10.200 1.00 25.82 ? 183 ARG A CB  1 
ATOM   1403 C CG  . ARG A 1 183 ? 42.075 -44.927 -9.607  1.00 26.98 ? 183 ARG A CG  1 
ATOM   1404 C CD  . ARG A 1 183 ? 42.269 -45.315 -8.153  1.00 28.56 ? 183 ARG A CD  1 
ATOM   1405 N NE  . ARG A 1 183 ? 41.000 -45.373 -7.421  1.00 29.76 ? 183 ARG A NE  1 
ATOM   1406 C CZ  . ARG A 1 183 ? 40.704 -46.251 -6.462  1.00 30.82 ? 183 ARG A CZ  1 
ATOM   1407 N NH1 . ARG A 1 183 ? 41.568 -47.197 -6.102  1.00 31.26 ? 183 ARG A NH1 1 
ATOM   1408 N NH2 . ARG A 1 183 ? 39.522 -46.190 -5.861  1.00 31.82 ? 183 ARG A NH2 1 
ATOM   1409 N N   . VAL A 1 184 ? 44.905 -41.753 -11.514 1.00 24.03 ? 184 VAL A N   1 
ATOM   1410 C CA  . VAL A 1 184 ? 46.110 -41.121 -12.050 1.00 23.88 ? 184 VAL A CA  1 
ATOM   1411 C C   . VAL A 1 184 ? 46.419 -39.847 -11.267 1.00 24.43 ? 184 VAL A C   1 
ATOM   1412 O O   . VAL A 1 184 ? 47.563 -39.595 -10.895 1.00 24.37 ? 184 VAL A O   1 
ATOM   1413 C CB  . VAL A 1 184 ? 45.956 -40.795 -13.558 1.00 23.63 ? 184 VAL A CB  1 
ATOM   1414 C CG1 . VAL A 1 184 ? 47.166 -40.035 -14.082 1.00 24.06 ? 184 VAL A CG1 1 
ATOM   1415 C CG2 . VAL A 1 184 ? 45.744 -42.070 -14.356 1.00 22.98 ? 184 VAL A CG2 1 
ATOM   1416 N N   . ILE A 1 185 ? 45.383 -39.054 -11.012 1.00 24.79 ? 185 ILE A N   1 
ATOM   1417 C CA  . ILE A 1 185 ? 45.525 -37.813 -10.261 1.00 25.95 ? 185 ILE A CA  1 
ATOM   1418 C C   . ILE A 1 185 ? 46.030 -38.069 -8.839  1.00 26.81 ? 185 ILE A C   1 
ATOM   1419 O O   . ILE A 1 185 ? 46.832 -37.294 -8.311  1.00 27.00 ? 185 ILE A O   1 
ATOM   1420 C CB  . ILE A 1 185 ? 44.187 -37.039 -10.224 1.00 26.50 ? 185 ILE A CB  1 
ATOM   1421 C CG1 . ILE A 1 185 ? 43.875 -36.478 -11.619 1.00 26.33 ? 185 ILE A CG1 1 
ATOM   1422 C CG2 . ILE A 1 185 ? 44.219 -35.920 -9.191  1.00 27.86 ? 185 ILE A CG2 1 
ATOM   1423 C CD1 . ILE A 1 185 ? 42.429 -36.071 -11.810 1.00 26.83 ? 185 ILE A CD1 1 
ATOM   1424 N N   . CYS A 1 186 ? 45.565 -39.160 -8.231  1.00 27.06 ? 186 CYS A N   1 
ATOM   1425 C CA  . CYS A 1 186 ? 45.864 -39.431 -6.828  1.00 28.47 ? 186 CYS A CA  1 
ATOM   1426 C C   . CYS A 1 186 ? 47.199 -40.154 -6.618  1.00 28.07 ? 186 CYS A C   1 
ATOM   1427 O O   . CYS A 1 186 ? 47.694 -40.218 -5.495  1.00 29.03 ? 186 CYS A O   1 
ATOM   1428 C CB  . CYS A 1 186 ? 44.718 -40.216 -6.184  1.00 29.39 ? 186 CYS A CB  1 
ATOM   1429 S SG  . CYS A 1 186 ? 44.646 -40.039 -4.387  1.00 32.83 ? 186 CYS A SG  1 
ATOM   1430 N N   . GLY A 1 187 ? 47.786 -40.678 -7.692  1.00 26.83 ? 187 GLY A N   1 
ATOM   1431 C CA  . GLY A 1 187 ? 49.080 -41.359 -7.617  1.00 26.92 ? 187 GLY A CA  1 
ATOM   1432 C C   . GLY A 1 187 ? 48.997 -42.863 -7.382  1.00 26.76 ? 187 GLY A C   1 
ATOM   1433 O O   . GLY A 1 187 ? 50.016 -43.504 -7.130  1.00 26.71 ? 187 GLY A O   1 
ATOM   1434 N N   . TYR A 1 188 ? 47.789 -43.419 -7.468  1.00 26.61 ? 188 TYR A N   1 
ATOM   1435 C CA  . TYR A 1 188 ? 47.563 -44.864 -7.319  1.00 27.06 ? 188 TYR A CA  1 
ATOM   1436 C C   . TYR A 1 188 ? 48.050 -45.651 -8.530  1.00 25.94 ? 188 TYR A C   1 
ATOM   1437 O O   . TYR A 1 188 ? 48.510 -46.787 -8.403  1.00 25.90 ? 188 TYR A O   1 
ATOM   1438 C CB  . TYR A 1 188 ? 46.065 -45.155 -7.132  1.00 27.68 ? 188 TYR A CB  1 
ATOM   1439 C CG  . TYR A 1 188 ? 45.562 -45.003 -5.716  1.00 29.61 ? 188 TYR A CG  1 
ATOM   1440 C CD1 . TYR A 1 188 ? 45.784 -43.837 -4.999  1.00 30.87 ? 188 TYR A CD1 1 
ATOM   1441 C CD2 . TYR A 1 188 ? 44.836 -46.024 -5.100  1.00 30.80 ? 188 TYR A CD2 1 
ATOM   1442 C CE1 . TYR A 1 188 ? 45.318 -43.693 -3.703  1.00 32.44 ? 188 TYR A CE1 1 
ATOM   1443 C CE2 . TYR A 1 188 ? 44.367 -45.887 -3.802  1.00 32.37 ? 188 TYR A CE2 1 
ATOM   1444 C CZ  . TYR A 1 188 ? 44.614 -44.720 -3.109  1.00 33.24 ? 188 TYR A CZ  1 
ATOM   1445 O OH  . TYR A 1 188 ? 44.155 -44.573 -1.821  1.00 35.13 ? 188 TYR A OH  1 
ATOM   1446 N N   . HIS A 1 189 ? 47.917 -45.046 -9.707  1.00 24.92 ? 189 HIS A N   1 
ATOM   1447 C CA  . HIS A 1 189 ? 48.221 -45.711 -10.962 1.00 24.25 ? 189 HIS A CA  1 
ATOM   1448 C C   . HIS A 1 189 ? 48.836 -44.752 -11.961 1.00 23.71 ? 189 HIS A C   1 
ATOM   1449 O O   . HIS A 1 189 ? 48.611 -43.541 -11.895 1.00 23.81 ? 189 HIS A O   1 
ATOM   1450 C CB  . HIS A 1 189 ? 46.944 -46.283 -11.574 1.00 24.09 ? 189 HIS A CB  1 
ATOM   1451 C CG  . HIS A 1 189 ? 46.438 -47.504 -10.878 1.00 24.94 ? 189 HIS A CG  1 
ATOM   1452 N ND1 . HIS A 1 189 ? 47.052 -48.731 -10.996 1.00 25.45 ? 189 HIS A ND1 1 
ATOM   1453 C CD2 . HIS A 1 189 ? 45.377 -47.690 -10.058 1.00 25.79 ? 189 HIS A CD2 1 
ATOM   1454 C CE1 . HIS A 1 189 ? 46.391 -49.622 -10.277 1.00 26.26 ? 189 HIS A CE1 1 
ATOM   1455 N NE2 . HIS A 1 189 ? 45.372 -49.015 -9.696  1.00 26.38 ? 189 HIS A NE2 1 
ATOM   1456 N N   . TRP A 1 190 ? 49.615 -45.313 -12.879 1.00 23.19 ? 190 TRP A N   1 
ATOM   1457 C CA  . TRP A 1 190 ? 50.116 -44.579 -14.033 1.00 22.93 ? 190 TRP A CA  1 
ATOM   1458 C C   . TRP A 1 190 ? 49.004 -44.514 -15.070 1.00 22.71 ? 190 TRP A C   1 
ATOM   1459 O O   . TRP A 1 190 ? 48.137 -45.391 -15.111 1.00 22.03 ? 190 TRP A O   1 
ATOM   1460 C CB  . TRP A 1 190 ? 51.313 -45.298 -14.652 1.00 22.70 ? 190 TRP A CB  1 
ATOM   1461 C CG  . TRP A 1 190 ? 52.448 -45.573 -13.712 1.00 22.94 ? 190 TRP A CG  1 
ATOM   1462 C CD1 . TRP A 1 190 ? 52.747 -46.768 -13.117 1.00 23.16 ? 190 TRP A CD1 1 
ATOM   1463 C CD2 . TRP A 1 190 ? 53.445 -44.647 -13.272 1.00 23.29 ? 190 TRP A CD2 1 
ATOM   1464 N NE1 . TRP A 1 190 ? 53.870 -46.642 -12.336 1.00 23.82 ? 190 TRP A NE1 1 
ATOM   1465 C CE2 . TRP A 1 190 ? 54.318 -45.349 -12.410 1.00 23.93 ? 190 TRP A CE2 1 
ATOM   1466 C CE3 . TRP A 1 190 ? 53.685 -43.291 -13.516 1.00 23.37 ? 190 TRP A CE3 1 
ATOM   1467 C CZ2 . TRP A 1 190 ? 55.411 -44.743 -11.802 1.00 24.63 ? 190 TRP A CZ2 1 
ATOM   1468 C CZ3 . TRP A 1 190 ? 54.770 -42.688 -12.906 1.00 24.05 ? 190 TRP A CZ3 1 
ATOM   1469 C CH2 . TRP A 1 190 ? 55.618 -43.412 -12.055 1.00 24.59 ? 190 TRP A CH2 1 
ATOM   1470 N N   . GLN A 1 191 ? 49.046 -43.491 -15.922 1.00 23.10 ? 191 GLN A N   1 
ATOM   1471 C CA  . GLN A 1 191 ? 48.062 -43.347 -16.990 1.00 23.13 ? 191 GLN A CA  1 
ATOM   1472 C C   . GLN A 1 191 ? 47.928 -44.635 -17.799 1.00 22.56 ? 191 GLN A C   1 
ATOM   1473 O O   . GLN A 1 191 ? 46.814 -45.059 -18.109 1.00 22.10 ? 191 GLN A O   1 
ATOM   1474 C CB  . GLN A 1 191 ? 48.431 -42.184 -17.919 1.00 24.18 ? 191 GLN A CB  1 
ATOM   1475 C CG  . GLN A 1 191 ? 47.424 -41.916 -19.030 1.00 24.67 ? 191 GLN A CG  1 
ATOM   1476 C CD  . GLN A 1 191 ? 46.056 -41.554 -18.492 1.00 25.11 ? 191 GLN A CD  1 
ATOM   1477 O OE1 . GLN A 1 191 ? 45.922 -40.639 -17.682 1.00 26.59 ? 191 GLN A OE1 1 
ATOM   1478 N NE2 . GLN A 1 191 ? 45.034 -42.268 -18.938 1.00 25.03 ? 191 GLN A NE2 1 
ATOM   1479 N N   . SER A 1 192 ? 49.057 -45.259 -18.132 1.00 22.41 ? 192 SER A N   1 
ATOM   1480 C CA  . SER A 1 192 ? 49.039 -46.489 -18.924 1.00 22.48 ? 192 SER A CA  1 
ATOM   1481 C C   . SER A 1 192 ? 48.331 -47.657 -18.215 1.00 22.28 ? 192 SER A C   1 
ATOM   1482 O O   . SER A 1 192 ? 47.750 -48.507 -18.885 1.00 22.29 ? 192 SER A O   1 
ATOM   1483 C CB  . SER A 1 192 ? 50.452 -46.894 -19.348 1.00 22.87 ? 192 SER A CB  1 
ATOM   1484 O OG  . SER A 1 192 ? 51.323 -46.956 -18.240 1.00 22.87 ? 192 SER A OG  1 
ATOM   1485 N N   . ASP A 1 193 ? 48.382 -47.701 -16.881 1.00 22.30 ? 193 ASP A N   1 
ATOM   1486 C CA  . ASP A 1 193 ? 47.637 -48.712 -16.105 1.00 22.43 ? 193 ASP A CA  1 
ATOM   1487 C C   . ASP A 1 193 ? 46.143 -48.576 -16.347 1.00 22.40 ? 193 ASP A C   1 
ATOM   1488 O O   . ASP A 1 193 ? 45.415 -49.565 -16.472 1.00 22.23 ? 193 ASP A O   1 
ATOM   1489 C CB  . ASP A 1 193 ? 47.855 -48.540 -14.600 1.00 22.62 ? 193 ASP A CB  1 
ATOM   1490 C CG  . ASP A 1 193 ? 49.295 -48.709 -14.180 1.00 23.09 ? 193 ASP A CG  1 
ATOM   1491 O OD1 . ASP A 1 193 ? 50.039 -49.453 -14.845 1.00 23.07 ? 193 ASP A OD1 1 
ATOM   1492 O OD2 . ASP A 1 193 ? 49.671 -48.099 -13.157 1.00 23.68 ? 193 ASP A OD2 1 
ATOM   1493 N N   . VAL A 1 194 ? 45.705 -47.323 -16.377 1.00 22.79 ? 194 VAL A N   1 
ATOM   1494 C CA  . VAL A 1 194 ? 44.312 -46.968 -16.555 1.00 23.34 ? 194 VAL A CA  1 
ATOM   1495 C C   . VAL A 1 194 ? 43.878 -47.212 -18.000 1.00 23.55 ? 194 VAL A C   1 
ATOM   1496 O O   . VAL A 1 194 ? 42.800 -47.764 -18.236 1.00 23.37 ? 194 VAL A O   1 
ATOM   1497 C CB  . VAL A 1 194 ? 44.097 -45.504 -16.099 1.00 23.74 ? 194 VAL A CB  1 
ATOM   1498 C CG1 . VAL A 1 194 ? 42.793 -44.920 -16.612 1.00 24.15 ? 194 VAL A CG1 1 
ATOM   1499 C CG2 . VAL A 1 194 ? 44.178 -45.438 -14.580 1.00 24.05 ? 194 VAL A CG2 1 
ATOM   1500 N N   . ASP A 1 195 ? 44.716 -46.823 -18.960 1.00 24.24 ? 195 ASP A N   1 
ATOM   1501 C CA  . ASP A 1 195 ? 44.434 -47.077 -20.374 1.00 24.98 ? 195 ASP A CA  1 
ATOM   1502 C C   . ASP A 1 195 ? 44.241 -48.574 -20.616 1.00 24.85 ? 195 ASP A C   1 
ATOM   1503 O O   . ASP A 1 195 ? 43.256 -48.994 -21.223 1.00 24.60 ? 195 ASP A O   1 
ATOM   1504 C CB  . ASP A 1 195 ? 45.577 -46.585 -21.270 1.00 26.27 ? 195 ASP A CB  1 
ATOM   1505 C CG  . ASP A 1 195 ? 45.741 -45.075 -21.258 1.00 27.24 ? 195 ASP A CG  1 
ATOM   1506 O OD1 . ASP A 1 195 ? 44.781 -44.356 -20.929 1.00 27.88 ? 195 ASP A OD1 1 
ATOM   1507 O OD2 . ASP A 1 195 ? 46.852 -44.611 -21.593 1.00 28.77 ? 195 ASP A OD2 1 
ATOM   1508 N N   . ALA A 1 196 ? 45.191 -49.370 -20.129 1.00 24.85 ? 196 ALA A N   1 
ATOM   1509 C CA  . ALA A 1 196 ? 45.145 -50.822 -20.291 1.00 25.10 ? 196 ALA A CA  1 
ATOM   1510 C C   . ALA A 1 196 ? 43.913 -51.432 -19.623 1.00 24.95 ? 196 ALA A C   1 
ATOM   1511 O O   . ALA A 1 196 ? 43.328 -52.379 -20.147 1.00 25.31 ? 196 ALA A O   1 
ATOM   1512 C CB  . ALA A 1 196 ? 46.413 -51.462 -19.742 1.00 25.55 ? 196 ALA A CB  1 
ATOM   1513 N N   . ALA A 1 197 ? 43.526 -50.889 -18.471 1.00 24.60 ? 197 ALA A N   1 
ATOM   1514 C CA  . ALA A 1 197 ? 42.373 -51.390 -17.718 1.00 24.60 ? 197 ALA A CA  1 
ATOM   1515 C C   . ALA A 1 197 ? 41.058 -51.299 -18.498 1.00 24.44 ? 197 ALA A C   1 
ATOM   1516 O O   . ALA A 1 197 ? 40.199 -52.175 -18.386 1.00 24.05 ? 197 ALA A O   1 
ATOM   1517 C CB  . ALA A 1 197 ? 42.245 -50.645 -16.401 1.00 24.42 ? 197 ALA A CB  1 
ATOM   1518 N N   . ARG A 1 198 ? 40.906 -50.243 -19.291 1.00 24.31 ? 198 ARG A N   1 
ATOM   1519 C CA  . ARG A 1 198 ? 39.693 -50.055 -20.080 1.00 24.39 ? 198 ARG A CA  1 
ATOM   1520 C C   . ARG A 1 198 ? 39.594 -51.073 -21.209 1.00 24.28 ? 198 ARG A C   1 
ATOM   1521 O O   . ARG A 1 198 ? 38.495 -51.434 -21.616 1.00 24.13 ? 198 ARG A O   1 
ATOM   1522 C CB  . ARG A 1 198 ? 39.620 -48.629 -20.622 1.00 25.01 ? 198 ARG A CB  1 
ATOM   1523 C CG  . ARG A 1 198 ? 39.624 -47.598 -19.508 1.00 25.62 ? 198 ARG A CG  1 
ATOM   1524 C CD  . ARG A 1 198 ? 39.168 -46.236 -19.987 1.00 26.46 ? 198 ARG A CD  1 
ATOM   1525 N NE  . ARG A 1 198 ? 39.287 -45.242 -18.921 1.00 27.27 ? 198 ARG A NE  1 
ATOM   1526 C CZ  . ARG A 1 198 ? 40.253 -44.331 -18.817 1.00 27.94 ? 198 ARG A CZ  1 
ATOM   1527 N NH1 . ARG A 1 198 ? 41.223 -44.250 -19.719 1.00 28.30 ? 198 ARG A NH1 1 
ATOM   1528 N NH2 . ARG A 1 198 ? 40.242 -43.480 -17.797 1.00 28.48 ? 198 ARG A NH2 1 
ATOM   1529 N N   . ILE A 1 199 ? 40.735 -51.548 -21.701 1.00 24.16 ? 199 ILE A N   1 
ATOM   1530 C CA  A ILE A 1 199 ? 40.745 -52.595 -22.721 0.50 24.52 ? 199 ILE A CA  1 
ATOM   1531 C CA  B ILE A 1 199 ? 40.743 -52.598 -22.716 0.50 24.70 ? 199 ILE A CA  1 
ATOM   1532 C C   . ILE A 1 199 ? 40.159 -53.888 -22.149 1.00 24.57 ? 199 ILE A C   1 
ATOM   1533 O O   . ILE A 1 199 ? 39.207 -54.444 -22.707 1.00 24.73 ? 199 ILE A O   1 
ATOM   1534 C CB  A ILE A 1 199 ? 42.167 -52.845 -23.270 0.50 24.88 ? 199 ILE A CB  1 
ATOM   1535 C CB  B ILE A 1 199 ? 42.162 -52.867 -23.242 0.50 25.28 ? 199 ILE A CB  1 
ATOM   1536 C CG1 A ILE A 1 199 ? 42.651 -51.625 -24.057 0.50 24.92 ? 199 ILE A CG1 1 
ATOM   1537 C CG1 B ILE A 1 199 ? 42.685 -51.638 -23.977 0.50 25.55 ? 199 ILE A CG1 1 
ATOM   1538 C CG2 A ILE A 1 199 ? 42.206 -54.073 -24.170 0.50 25.53 ? 199 ILE A CG2 1 
ATOM   1539 C CG2 B ILE A 1 199 ? 42.189 -54.069 -24.176 0.50 25.92 ? 199 ILE A CG2 1 
ATOM   1540 C CD1 A ILE A 1 199 ? 41.752 -51.259 -25.217 0.50 25.17 ? 199 ILE A CD1 1 
ATOM   1541 C CD1 B ILE A 1 199 ? 43.871 -51.951 -24.849 0.50 26.47 ? 199 ILE A CD1 1 
ATOM   1542 N N   . VAL A 1 200 ? 40.727 -54.357 -21.040 1.00 24.42 ? 200 VAL A N   1 
ATOM   1543 C CA  . VAL A 1 200 ? 40.268 -55.606 -20.421 1.00 24.78 ? 200 VAL A CA  1 
ATOM   1544 C C   . VAL A 1 200 ? 38.885 -55.454 -19.786 1.00 24.51 ? 200 VAL A C   1 
ATOM   1545 O O   . VAL A 1 200 ? 38.098 -56.398 -19.779 1.00 24.96 ? 200 VAL A O   1 
ATOM   1546 C CB  . VAL A 1 200 ? 41.279 -56.192 -19.405 1.00 25.24 ? 200 VAL A CB  1 
ATOM   1547 C CG1 . VAL A 1 200 ? 42.589 -56.536 -20.102 1.00 25.62 ? 200 VAL A CG1 1 
ATOM   1548 C CG2 . VAL A 1 200 ? 41.516 -55.259 -18.221 1.00 24.93 ? 200 VAL A CG2 1 
ATOM   1549 N N   . GLY A 1 201 ? 38.592 -54.265 -19.268 1.00 24.09 ? 201 GLY A N   1 
ATOM   1550 C CA  . GLY A 1 201 ? 37.270 -53.959 -18.734 1.00 24.09 ? 201 GLY A CA  1 
ATOM   1551 C C   . GLY A 1 201 ? 36.180 -54.082 -19.780 1.00 24.05 ? 201 GLY A C   1 
ATOM   1552 O O   . GLY A 1 201 ? 35.098 -54.596 -19.502 1.00 24.68 ? 201 GLY A O   1 
ATOM   1553 N N   . SER A 1 202 ? 36.460 -53.609 -20.989 1.00 23.96 ? 202 SER A N   1 
ATOM   1554 C CA  . SER A 1 202 ? 35.511 -53.754 -22.082 1.00 24.34 ? 202 SER A CA  1 
ATOM   1555 C C   . SER A 1 202 ? 35.409 -55.220 -22.510 1.00 24.29 ? 202 SER A C   1 
ATOM   1556 O O   . SER A 1 202 ? 34.309 -55.716 -22.761 1.00 24.27 ? 202 SER A O   1 
ATOM   1557 C CB  . SER A 1 202 ? 35.873 -52.837 -23.257 1.00 24.79 ? 202 SER A CB  1 
ATOM   1558 O OG  . SER A 1 202 ? 37.037 -53.277 -23.925 1.00 26.50 ? 202 SER A OG  1 
ATOM   1559 N N   . ALA A 1 203 ? 36.547 -55.911 -22.561 1.00 24.05 ? 203 ALA A N   1 
ATOM   1560 C CA  . ALA A 1 203 ? 36.587 -57.319 -22.959 1.00 24.46 ? 203 ALA A CA  1 
ATOM   1561 C C   . ALA A 1 203 ? 35.731 -58.217 -22.054 1.00 24.46 ? 203 ALA A C   1 
ATOM   1562 O O   . ALA A 1 203 ? 34.976 -59.057 -22.546 1.00 24.99 ? 203 ALA A O   1 
ATOM   1563 C CB  . ALA A 1 203 ? 38.025 -57.820 -22.988 1.00 24.81 ? 203 ALA A CB  1 
ATOM   1564 N N   . VAL A 1 204 ? 35.848 -58.038 -20.741 1.00 23.89 ? 204 VAL A N   1 
ATOM   1565 C CA  . VAL A 1 204 ? 35.118 -58.883 -19.791 1.00 24.21 ? 204 VAL A CA  1 
ATOM   1566 C C   . VAL A 1 204 ? 33.600 -58.699 -19.902 1.00 24.08 ? 204 VAL A C   1 
ATOM   1567 O O   . VAL A 1 204 ? 32.845 -59.632 -19.645 1.00 24.38 ? 204 VAL A O   1 
ATOM   1568 C CB  . VAL A 1 204 ? 35.589 -58.667 -18.329 1.00 24.19 ? 204 VAL A CB  1 
ATOM   1569 C CG1 . VAL A 1 204 ? 35.199 -57.289 -17.810 1.00 23.64 ? 204 VAL A CG1 1 
ATOM   1570 C CG2 . VAL A 1 204 ? 35.028 -59.751 -17.416 1.00 25.13 ? 204 VAL A CG2 1 
ATOM   1571 N N   . VAL A 1 205 ? 33.156 -57.505 -20.290 1.00 23.52 ? 205 VAL A N   1 
ATOM   1572 C CA  . VAL A 1 205 ? 31.725 -57.253 -20.453 1.00 23.81 ? 205 VAL A CA  1 
ATOM   1573 C C   . VAL A 1 205 ? 31.146 -58.122 -21.571 1.00 24.31 ? 205 VAL A C   1 
ATOM   1574 O O   . VAL A 1 205 ? 30.005 -58.576 -21.474 1.00 24.69 ? 205 VAL A O   1 
ATOM   1575 C CB  . VAL A 1 205 ? 31.419 -55.757 -20.680 1.00 23.33 ? 205 VAL A CB  1 
ATOM   1576 C CG1 . VAL A 1 205 ? 29.954 -55.541 -21.047 1.00 23.65 ? 205 VAL A CG1 1 
ATOM   1577 C CG2 . VAL A 1 205 ? 31.748 -54.972 -19.420 1.00 23.15 ? 205 VAL A CG2 1 
ATOM   1578 N N   . ALA A 1 206 ? 31.938 -58.372 -22.614 1.00 24.54 ? 206 ALA A N   1 
ATOM   1579 C CA  . ALA A 1 206 ? 31.529 -59.289 -23.677 1.00 25.18 ? 206 ALA A CA  1 
ATOM   1580 C C   . ALA A 1 206 ? 31.356 -60.707 -23.133 1.00 26.02 ? 206 ALA A C   1 
ATOM   1581 O O   . ALA A 1 206 ? 30.357 -61.368 -23.423 1.00 26.59 ? 206 ALA A O   1 
ATOM   1582 C CB  . ALA A 1 206 ? 32.535 -59.277 -24.815 1.00 25.32 ? 206 ALA A CB  1 
ATOM   1583 N N   . THR A 1 207 ? 32.322 -61.165 -22.338 1.00 26.27 ? 207 THR A N   1 
ATOM   1584 C CA  . THR A 1 207 ? 32.231 -62.482 -21.708 1.00 27.32 ? 207 THR A CA  1 
ATOM   1585 C C   . THR A 1 207 ? 30.996 -62.572 -20.827 1.00 27.56 ? 207 THR A C   1 
ATOM   1586 O O   . THR A 1 207 ? 30.258 -63.552 -20.885 1.00 28.21 ? 207 THR A O   1 
ATOM   1587 C CB  . THR A 1 207 ? 33.462 -62.803 -20.839 1.00 27.62 ? 207 THR A CB  1 
ATOM   1588 O OG1 . THR A 1 207 ? 34.654 -62.359 -21.494 1.00 27.15 ? 207 THR A OG1 1 
ATOM   1589 C CG2 . THR A 1 207 ? 33.557 -64.301 -20.575 1.00 29.09 ? 207 THR A CG2 1 
ATOM   1590 N N   . LEU A 1 208 ? 30.775 -61.543 -20.015 1.00 27.02 ? 208 LEU A N   1 
ATOM   1591 C CA  . LEU A 1 208 ? 29.638 -61.525 -19.100 1.00 27.49 ? 208 LEU A CA  1 
ATOM   1592 C C   . LEU A 1 208 ? 28.310 -61.684 -19.839 1.00 27.81 ? 208 LEU A C   1 
ATOM   1593 O O   . LEU A 1 208 ? 27.410 -62.365 -19.350 1.00 28.37 ? 208 LEU A O   1 
ATOM   1594 C CB  . LEU A 1 208 ? 29.639 -60.248 -18.258 1.00 26.88 ? 208 LEU A CB  1 
ATOM   1595 C CG  . LEU A 1 208 ? 30.732 -60.189 -17.186 1.00 26.91 ? 208 LEU A CG  1 
ATOM   1596 C CD1 . LEU A 1 208 ? 30.805 -58.793 -16.586 1.00 26.27 ? 208 LEU A CD1 1 
ATOM   1597 C CD2 . LEU A 1 208 ? 30.510 -61.235 -16.101 1.00 28.24 ? 208 LEU A CD2 1 
ATOM   1598 N N   . HIS A 1 209 ? 28.203 -61.090 -21.028 1.00 27.32 ? 209 HIS A N   1 
ATOM   1599 C CA  . HIS A 1 209 ? 26.995 -61.227 -21.840 1.00 27.74 ? 209 HIS A CA  1 
ATOM   1600 C C   . HIS A 1 209 ? 26.714 -62.664 -22.306 1.00 28.46 ? 209 HIS A C   1 
ATOM   1601 O O   . HIS A 1 209 ? 25.590 -62.974 -22.703 1.00 28.77 ? 209 HIS A O   1 
ATOM   1602 C CB  . HIS A 1 209 ? 27.036 -60.273 -23.037 1.00 27.53 ? 209 HIS A CB  1 
ATOM   1603 C CG  . HIS A 1 209 ? 26.643 -58.871 -22.696 1.00 27.27 ? 209 HIS A CG  1 
ATOM   1604 N ND1 . HIS A 1 209 ? 27.538 -57.936 -22.223 1.00 26.90 ? 209 HIS A ND1 1 
ATOM   1605 C CD2 . HIS A 1 209 ? 25.443 -58.248 -22.751 1.00 27.70 ? 209 HIS A CD2 1 
ATOM   1606 C CE1 . HIS A 1 209 ? 26.906 -56.797 -22.004 1.00 26.85 ? 209 HIS A CE1 1 
ATOM   1607 N NE2 . HIS A 1 209 ? 25.633 -56.959 -22.315 1.00 27.25 ? 209 HIS A NE2 1 
ATOM   1608 N N   . THR A 1 210 ? 27.723 -63.533 -22.251 1.00 28.61 ? 210 THR A N   1 
ATOM   1609 C CA  . THR A 1 210 ? 27.546 -64.953 -22.576 1.00 29.68 ? 210 THR A CA  1 
ATOM   1610 C C   . THR A 1 210 ? 27.091 -65.794 -21.376 1.00 30.49 ? 210 THR A C   1 
ATOM   1611 O O   . THR A 1 210 ? 26.728 -66.950 -21.542 1.00 31.36 ? 210 THR A O   1 
ATOM   1612 C CB  . THR A 1 210 ? 28.847 -65.585 -23.112 1.00 30.01 ? 210 THR A CB  1 
ATOM   1613 O OG1 . THR A 1 210 ? 29.755 -65.829 -22.029 1.00 29.97 ? 210 THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 210 ? 29.512 -64.683 -24.150 1.00 29.26 ? 210 THR A CG2 1 
ATOM   1615 N N   . ASN A 1 211 ? 27.120 -65.213 -20.179 1.00 30.06 ? 211 ASN A N   1 
ATOM   1616 C CA  . ASN A 1 211 ? 26.885 -65.951 -18.940 1.00 31.11 ? 211 ASN A CA  1 
ATOM   1617 C C   . ASN A 1 211 ? 25.413 -65.892 -18.527 1.00 31.48 ? 211 ASN A C   1 
ATOM   1618 O O   . ASN A 1 211 ? 24.885 -64.799 -18.308 1.00 30.44 ? 211 ASN A O   1 
ATOM   1619 C CB  . ASN A 1 211 ? 27.757 -65.367 -17.829 1.00 30.91 ? 211 ASN A CB  1 
ATOM   1620 C CG  . ASN A 1 211 ? 27.597 -66.095 -16.514 1.00 32.25 ? 211 ASN A CG  1 
ATOM   1621 O OD1 . ASN A 1 211 ? 26.906 -65.622 -15.617 1.00 32.70 ? 211 ASN A OD1 1 
ATOM   1622 N ND2 . ASN A 1 211 ? 28.226 -67.255 -16.396 1.00 33.57 ? 211 ASN A ND2 1 
ATOM   1623 N N   . PRO A 1 212 ? 24.748 -67.064 -18.406 1.00 34.74 ? 212 PRO A N   1 
ATOM   1624 C CA  . PRO A 1 212 ? 23.326 -67.087 -18.038 1.00 35.24 ? 212 PRO A CA  1 
ATOM   1625 C C   . PRO A 1 212 ? 22.982 -66.299 -16.771 1.00 33.74 ? 212 PRO A C   1 
ATOM   1626 O O   . PRO A 1 212 ? 22.018 -65.538 -16.773 1.00 32.71 ? 212 PRO A O   1 
ATOM   1627 C CB  . PRO A 1 212 ? 23.033 -68.581 -17.840 1.00 38.61 ? 212 PRO A CB  1 
ATOM   1628 C CG  . PRO A 1 212 ? 24.024 -69.278 -18.701 1.00 40.05 ? 212 PRO A CG  1 
ATOM   1629 C CD  . PRO A 1 212 ? 25.260 -68.417 -18.698 1.00 37.61 ? 212 PRO A CD  1 
ATOM   1630 N N   . ALA A 1 213 ? 23.758 -66.476 -15.705 1.00 34.32 ? 213 ALA A N   1 
ATOM   1631 C CA  . ALA A 1 213 ? 23.478 -65.781 -14.445 1.00 34.22 ? 213 ALA A CA  1 
ATOM   1632 C C   . ALA A 1 213 ? 23.554 -64.263 -14.622 1.00 32.06 ? 213 ALA A C   1 
ATOM   1633 O O   . ALA A 1 213 ? 22.699 -63.528 -14.118 1.00 31.53 ? 213 ALA A O   1 
ATOM   1634 C CB  . ALA A 1 213 ? 24.427 -66.245 -13.353 1.00 36.14 ? 213 ALA A CB  1 
ATOM   1635 N N   . PHE A 1 214 ? 24.564 -63.796 -15.354 1.00 31.48 ? 214 PHE A N   1 
ATOM   1636 C CA  . PHE A 1 214 ? 24.690 -62.367 -15.641 1.00 30.39 ? 214 PHE A CA  1 
ATOM   1637 C C   . PHE A 1 214 ? 23.507 -61.870 -16.467 1.00 29.87 ? 214 PHE A C   1 
ATOM   1638 O O   . PHE A 1 214 ? 22.927 -60.828 -16.157 1.00 29.36 ? 214 PHE A O   1 
ATOM   1639 C CB  . PHE A 1 214 ? 25.997 -62.063 -16.376 1.00 30.73 ? 214 PHE A CB  1 
ATOM   1640 C CG  . PHE A 1 214 ? 26.143 -60.621 -16.782 1.00 30.25 ? 214 PHE A CG  1 
ATOM   1641 C CD1 . PHE A 1 214 ? 26.668 -59.689 -15.899 1.00 31.00 ? 214 PHE A CD1 1 
ATOM   1642 C CD2 . PHE A 1 214 ? 25.754 -60.196 -18.045 1.00 30.15 ? 214 PHE A CD2 1 
ATOM   1643 C CE1 . PHE A 1 214 ? 26.810 -58.362 -16.270 1.00 31.32 ? 214 PHE A CE1 1 
ATOM   1644 C CE2 . PHE A 1 214 ? 25.890 -58.871 -18.421 1.00 30.58 ? 214 PHE A CE2 1 
ATOM   1645 C CZ  . PHE A 1 214 ? 26.417 -57.953 -17.531 1.00 31.13 ? 214 PHE A CZ  1 
ATOM   1646 N N   . GLN A 1 215 ? 23.163 -62.616 -17.515 1.00 31.06 ? 215 GLN A N   1 
ATOM   1647 C CA  . GLN A 1 215 ? 22.032 -62.278 -18.384 1.00 31.70 ? 215 GLN A CA  1 
ATOM   1648 C C   . GLN A 1 215 ? 20.746 -62.112 -17.580 1.00 32.12 ? 215 GLN A C   1 
ATOM   1649 O O   . GLN A 1 215 ? 20.007 -61.146 -17.771 1.00 31.72 ? 215 GLN A O   1 
ATOM   1650 C CB  . GLN A 1 215 ? 21.820 -63.365 -19.440 1.00 33.97 ? 215 GLN A CB  1 
ATOM   1651 C CG  . GLN A 1 215 ? 22.906 -63.459 -20.500 1.00 34.84 ? 215 GLN A CG  1 
ATOM   1652 C CD  . GLN A 1 215 ? 22.845 -64.763 -21.277 1.00 37.85 ? 215 GLN A CD  1 
ATOM   1653 O OE1 . GLN A 1 215 ? 21.973 -65.598 -21.042 1.00 39.52 ? 215 GLN A OE1 1 
ATOM   1654 N NE2 . GLN A 1 215 ? 23.773 -64.943 -22.208 1.00 39.32 ? 215 GLN A NE2 1 
ATOM   1655 N N   . GLN A 1 216 ? 20.485 -63.062 -16.685 1.00 33.67 ? 216 GLN A N   1 
ATOM   1656 C CA  . GLN A 1 216 ? 19.288 -63.021 -15.844 1.00 35.18 ? 216 GLN A CA  1 
ATOM   1657 C C   . GLN A 1 216 ? 19.299 -61.811 -14.925 1.00 33.60 ? 216 GLN A C   1 
ATOM   1658 O O   . GLN A 1 216 ? 18.310 -61.082 -14.835 1.00 33.65 ? 216 GLN A O   1 
ATOM   1659 C CB  . GLN A 1 216 ? 19.183 -64.276 -14.983 1.00 38.34 ? 216 GLN A CB  1 
ATOM   1660 C CG  . GLN A 1 216 ? 18.837 -65.540 -15.739 1.00 41.70 ? 216 GLN A CG  1 
ATOM   1661 C CD  . GLN A 1 216 ? 18.767 -66.739 -14.815 1.00 45.57 ? 216 GLN A CD  1 
ATOM   1662 O OE1 . GLN A 1 216 ? 17.794 -66.908 -14.075 1.00 49.00 ? 216 GLN A OE1 1 
ATOM   1663 N NE2 . GLN A 1 216 ? 19.800 -67.577 -14.845 1.00 46.53 ? 216 GLN A NE2 1 
ATOM   1664 N N   . GLN A 1 217 ? 20.418 -61.611 -14.232 1.00 32.49 ? 217 GLN A N   1 
ATOM   1665 C CA  . GLN A 1 217 ? 20.517 -60.528 -13.265 1.00 32.15 ? 217 GLN A CA  1 
ATOM   1666 C C   . GLN A 1 217 ? 20.466 -59.176 -13.966 1.00 30.70 ? 217 GLN A C   1 
ATOM   1667 O O   . GLN A 1 217 ? 19.898 -58.220 -13.434 1.00 31.20 ? 217 GLN A O   1 
ATOM   1668 C CB  . GLN A 1 217 ? 21.789 -60.651 -12.423 1.00 32.62 ? 217 GLN A CB  1 
ATOM   1669 C CG  . GLN A 1 217 ? 21.823 -59.711 -11.228 1.00 33.93 ? 217 GLN A CG  1 
ATOM   1670 C CD  . GLN A 1 217 ? 20.636 -59.907 -10.299 1.00 35.89 ? 217 GLN A CD  1 
ATOM   1671 O OE1 . GLN A 1 217 ? 20.206 -61.033 -10.059 1.00 37.31 ? 217 GLN A OE1 1 
ATOM   1672 N NE2 . GLN A 1 217 ? 20.100 -58.811 -9.778  1.00 36.52 ? 217 GLN A NE2 1 
ATOM   1673 N N   . LEU A 1 218 ? 21.055 -59.102 -15.158 1.00 29.70 ? 218 LEU A N   1 
ATOM   1674 C CA  . LEU A 1 218 ? 20.999 -57.887 -15.962 1.00 29.30 ? 218 LEU A CA  1 
ATOM   1675 C C   . LEU A 1 218 ? 19.556 -57.539 -16.302 1.00 29.84 ? 218 LEU A C   1 
ATOM   1676 O O   . LEU A 1 218 ? 19.155 -56.383 -16.198 1.00 30.20 ? 218 LEU A O   1 
ATOM   1677 C CB  . LEU A 1 218 ? 21.816 -58.040 -17.244 1.00 29.33 ? 218 LEU A CB  1 
ATOM   1678 C CG  . LEU A 1 218 ? 21.747 -56.876 -18.236 1.00 30.04 ? 218 LEU A CG  1 
ATOM   1679 C CD1 . LEU A 1 218 ? 22.192 -55.574 -17.586 1.00 30.34 ? 218 LEU A CD1 1 
ATOM   1680 C CD2 . LEU A 1 218 ? 22.585 -57.183 -19.467 1.00 31.24 ? 218 LEU A CD2 1 
ATOM   1681 N N   . GLN A 1 219 ? 18.780 -58.540 -16.704 1.00 30.87 ? 219 GLN A N   1 
ATOM   1682 C CA  . GLN A 1 219 ? 17.368 -58.323 -17.002 1.00 32.54 ? 219 GLN A CA  1 
ATOM   1683 C C   . GLN A 1 219 ? 16.604 -57.857 -15.760 1.00 32.84 ? 219 GLN A C   1 
ATOM   1684 O O   . GLN A 1 219 ? 15.765 -56.961 -15.845 1.00 33.87 ? 219 GLN A O   1 
ATOM   1685 C CB  . GLN A 1 219 ? 16.722 -59.587 -17.581 1.00 34.83 ? 219 GLN A CB  1 
ATOM   1686 C CG  . GLN A 1 219 ? 15.327 -59.360 -18.150 1.00 37.72 ? 219 GLN A CG  1 
ATOM   1687 C CD  . GLN A 1 219 ? 15.289 -58.238 -19.176 1.00 38.31 ? 219 GLN A CD  1 
ATOM   1688 O OE1 . GLN A 1 219 ? 15.990 -58.287 -20.182 1.00 38.84 ? 219 GLN A OE1 1 
ATOM   1689 N NE2 . GLN A 1 219 ? 14.478 -57.217 -18.919 1.00 39.31 ? 219 GLN A NE2 1 
ATOM   1690 N N   . LYS A 1 220 ? 16.896 -58.459 -14.612 1.00 32.81 ? 220 LYS A N   1 
ATOM   1691 C CA  . LYS A 1 220 ? 16.282 -58.025 -13.357 1.00 34.17 ? 220 LYS A CA  1 
ATOM   1692 C C   . LYS A 1 220 ? 16.601 -56.561 -13.066 1.00 33.05 ? 220 LYS A C   1 
ATOM   1693 O O   . LYS A 1 220 ? 15.723 -55.802 -12.656 1.00 34.18 ? 220 LYS A O   1 
ATOM   1694 C CB  . LYS A 1 220 ? 16.726 -58.909 -12.193 1.00 35.72 ? 220 LYS A CB  1 
ATOM   1695 C CG  . LYS A 1 220 ? 16.122 -60.302 -12.235 1.00 38.22 ? 220 LYS A CG  1 
ATOM   1696 C CD  . LYS A 1 220 ? 16.662 -61.185 -11.128 1.00 40.50 ? 220 LYS A CD  1 
ATOM   1697 C CE  . LYS A 1 220 ? 16.158 -62.609 -11.285 1.00 43.64 ? 220 LYS A CE  1 
ATOM   1698 N NZ  . LYS A 1 220 ? 16.744 -63.520 -10.266 1.00 46.53 ? 220 LYS A NZ  1 
ATOM   1699 N N   . ALA A 1 221 ? 17.853 -56.167 -13.297 1.00 31.26 ? 221 ALA A N   1 
ATOM   1700 C CA  . ALA A 1 221 ? 18.267 -54.776 -13.112 1.00 31.14 ? 221 ALA A CA  1 
ATOM   1701 C C   . ALA A 1 221 ? 17.517 -53.837 -14.054 1.00 31.01 ? 221 ALA A C   1 
ATOM   1702 O O   . ALA A 1 221 ? 17.135 -52.740 -13.655 1.00 32.38 ? 221 ALA A O   1 
ATOM   1703 C CB  . ALA A 1 221 ? 19.771 -54.632 -13.311 1.00 30.61 ? 221 ALA A CB  1 
ATOM   1704 N N   . LYS A 1 222 ? 17.315 -54.270 -15.296 1.00 30.26 ? 222 LYS A N   1 
ATOM   1705 C CA  . LYS A 1 222 ? 16.560 -53.490 -16.277 1.00 31.33 ? 222 LYS A CA  1 
ATOM   1706 C C   . LYS A 1 222 ? 15.080 -53.376 -15.903 1.00 32.94 ? 222 LYS A C   1 
ATOM   1707 O O   . LYS A 1 222 ? 14.492 -52.300 -16.009 1.00 34.34 ? 222 LYS A O   1 
ATOM   1708 C CB  . LYS A 1 222 ? 16.688 -54.102 -17.675 1.00 31.58 ? 222 LYS A CB  1 
ATOM   1709 C CG  . LYS A 1 222 ? 18.076 -53.977 -18.282 1.00 30.94 ? 222 LYS A CG  1 
ATOM   1710 C CD  . LYS A 1 222 ? 18.102 -54.479 -19.715 1.00 32.18 ? 222 LYS A CD  1 
ATOM   1711 C CE  . LYS A 1 222 ? 19.500 -54.387 -20.299 1.00 32.32 ? 222 LYS A CE  1 
ATOM   1712 N NZ  . LYS A 1 222 ? 19.569 -55.039 -21.630 1.00 34.17 ? 222 LYS A NZ  1 
ATOM   1713 N N   . ASP A 1 223 ? 14.485 -54.490 -15.478 1.00 33.35 ? 223 ASP A N   1 
ATOM   1714 C CA  . ASP A 1 223 ? 13.097 -54.496 -15.003 1.00 35.75 ? 223 ASP A CA  1 
ATOM   1715 C C   . ASP A 1 223 ? 12.942 -53.537 -13.828 1.00 36.03 ? 223 ASP A C   1 
ATOM   1716 O O   . ASP A 1 223 ? 12.019 -52.722 -13.795 1.00 37.97 ? 223 ASP A O   1 
ATOM   1717 C CB  . ASP A 1 223 ? 12.670 -55.907 -14.574 1.00 37.35 ? 223 ASP A CB  1 
ATOM   1718 C CG  . ASP A 1 223 ? 12.582 -56.883 -15.739 1.00 38.33 ? 223 ASP A CG  1 
ATOM   1719 O OD1 . ASP A 1 223 ? 12.612 -56.444 -16.910 1.00 38.80 ? 223 ASP A OD1 1 
ATOM   1720 O OD2 . ASP A 1 223 ? 12.477 -58.101 -15.480 1.00 39.90 ? 223 ASP A OD2 1 
ATOM   1721 N N   . GLU A 1 224 ? 13.858 -53.645 -12.870 1.00 34.62 ? 224 GLU A N   1 
ATOM   1722 C CA  . GLU A 1 224 ? 13.892 -52.762 -11.703 1.00 35.90 ? 224 GLU A CA  1 
ATOM   1723 C C   . GLU A 1 224 ? 13.994 -51.291 -12.107 1.00 36.19 ? 224 GLU A C   1 
ATOM   1724 O O   . GLU A 1 224 ? 13.288 -50.441 -11.566 1.00 38.26 ? 224 GLU A O   1 
ATOM   1725 C CB  . GLU A 1 224 ? 15.078 -53.142 -10.814 1.00 35.29 ? 224 GLU A CB  1 
ATOM   1726 C CG  . GLU A 1 224 ? 15.242 -52.315 -9.553  1.00 37.74 ? 224 GLU A CG  1 
ATOM   1727 C CD  . GLU A 1 224 ? 16.474 -52.730 -8.776  1.00 38.18 ? 224 GLU A CD  1 
ATOM   1728 O OE1 . GLU A 1 224 ? 17.598 -52.419 -9.228  1.00 36.51 ? 224 GLU A OE1 1 
ATOM   1729 O OE2 . GLU A 1 224 ? 16.323 -53.378 -7.720  1.00 40.42 ? 224 GLU A OE2 1 
ATOM   1730 N N   . PHE A 1 225 ? 14.881 -50.999 -13.056 1.00 34.66 ? 225 PHE A N   1 
ATOM   1731 C CA  . PHE A 1 225 ? 15.072 -49.633 -13.536 1.00 35.89 ? 225 PHE A CA  1 
ATOM   1732 C C   . PHE A 1 225 ? 13.811 -49.093 -14.206 1.00 38.08 ? 225 PHE A C   1 
ATOM   1733 O O   . PHE A 1 225 ? 13.459 -47.928 -14.025 1.00 39.90 ? 225 PHE A O   1 
ATOM   1734 C CB  . PHE A 1 225 ? 16.252 -49.554 -14.508 1.00 34.43 ? 225 PHE A CB  1 
ATOM   1735 C CG  . PHE A 1 225 ? 16.494 -48.171 -15.041 1.00 36.36 ? 225 PHE A CG  1 
ATOM   1736 C CD1 . PHE A 1 225 ? 16.832 -47.140 -14.180 1.00 38.46 ? 225 PHE A CD1 1 
ATOM   1737 C CD2 . PHE A 1 225 ? 16.366 -47.894 -16.396 1.00 37.12 ? 225 PHE A CD2 1 
ATOM   1738 C CE1 . PHE A 1 225 ? 17.051 -45.860 -14.659 1.00 41.25 ? 225 PHE A CE1 1 
ATOM   1739 C CE2 . PHE A 1 225 ? 16.586 -46.616 -16.882 1.00 39.99 ? 225 PHE A CE2 1 
ATOM   1740 C CZ  . PHE A 1 225 ? 16.926 -45.597 -16.011 1.00 41.99 ? 225 PHE A CZ  1 
ATOM   1741 N N   . ALA A 1 226 ? 13.140 -49.942 -14.981 1.00 38.73 ? 226 ALA A N   1 
ATOM   1742 C CA  . ALA A 1 226 ? 11.881 -49.565 -15.620 1.00 42.31 ? 226 ALA A CA  1 
ATOM   1743 C C   . ALA A 1 226 ? 10.839 -49.138 -14.585 1.00 45.68 ? 226 ALA A C   1 
ATOM   1744 O O   . ALA A 1 226 ? 10.100 -48.182 -14.811 1.00 48.32 ? 226 ALA A O   1 
ATOM   1745 C CB  . ALA A 1 226 ? 11.348 -50.707 -16.475 1.00 42.58 ? 226 ALA A CB  1 
ATOM   1746 N N   . LYS A 1 227 ? 10.793 -49.837 -13.452 1.00 46.88 ? 227 LYS A N   1 
ATOM   1747 C CA  . LYS A 1 227 ? 9.891  -49.468 -12.356 1.00 51.31 ? 227 LYS A CA  1 
ATOM   1748 C C   . LYS A 1 227 ? 10.326 -48.158 -11.704 1.00 53.46 ? 227 LYS A C   1 
ATOM   1749 O O   . LYS A 1 227 ? 9.493  -47.308 -11.403 1.00 56.77 ? 227 LYS A O   1 
ATOM   1750 C CB  . LYS A 1 227 ? 9.825  -50.574 -11.303 1.00 52.07 ? 227 LYS A CB  1 
ATOM   1751 C CG  . LYS A 1 227 ? 9.204  -51.868 -11.798 1.00 52.85 ? 227 LYS A CG  1 
ATOM   1752 C CD  . LYS A 1 227 ? 9.243  -52.942 -10.720 1.00 54.39 ? 227 LYS A CD  1 
ATOM   1753 C CE  . LYS A 1 227 ? 9.019  -54.331 -11.299 1.00 54.76 ? 227 LYS A CE  1 
ATOM   1754 N NZ  . LYS A 1 227 ? 9.386  -55.394 -10.322 1.00 55.92 ? 227 LYS A NZ  1 
ATOM   1755 N N   . THR A 1 228 ? 11.632 -48.004 -11.492 1.00 53.06 ? 228 THR A N   1 
ATOM   1756 C CA  . THR A 1 228 ? 12.196 -46.762 -10.959 1.00 56.02 ? 228 THR A CA  1 
ATOM   1757 C C   . THR A 1 228 ? 11.805 -45.562 -11.825 1.00 58.86 ? 228 THR A C   1 
ATOM   1758 O O   . THR A 1 228 ? 11.443 -44.506 -11.305 1.00 62.40 ? 228 THR A O   1 
ATOM   1759 C CB  . THR A 1 228 ? 13.736 -46.845 -10.854 1.00 54.56 ? 228 THR A CB  1 
ATOM   1760 O OG1 . THR A 1 228 ? 14.098 -47.871 -9.923  1.00 54.21 ? 228 THR A OG1 1 
ATOM   1761 C CG2 . THR A 1 228 ? 14.339 -45.517 -10.393 1.00 57.61 ? 228 THR A CG2 1 
ATOM   1762 N N   . GLN A 1 229 ? 11.874 -45.734 -13.143 1.00 58.62 ? 229 GLN A N   1 
ATOM   1763 C CA  . GLN A 1 229 ? 11.463 -44.688 -14.082 1.00 62.09 ? 229 GLN A CA  1 
ATOM   1764 C C   . GLN A 1 229 ? 9.973  -44.355 -13.969 1.00 66.11 ? 229 GLN A C   1 
ATOM   1765 O O   . GLN A 1 229 ? 9.596  -43.184 -13.987 1.00 69.44 ? 229 GLN A O   1 
ATOM   1766 C CB  . GLN A 1 229 ? 11.796 -45.089 -15.522 1.00 60.99 ? 229 GLN A CB  1 
ATOM   1767 C CG  . GLN A 1 229 ? 13.260 -44.918 -15.888 1.00 59.84 ? 229 GLN A CG  1 
ATOM   1768 C CD  . GLN A 1 229 ? 13.518 -45.166 -17.362 1.00 60.25 ? 229 GLN A CD  1 
ATOM   1769 O OE1 . GLN A 1 229 ? 13.359 -46.285 -17.851 1.00 58.58 ? 229 GLN A OE1 1 
ATOM   1770 N NE2 . GLN A 1 229 ? 13.920 -44.120 -18.080 1.00 63.34 ? 229 GLN A NE2 1 
ATOM   1771 N N   . LYS A 1 230 ? 9.135  -45.383 -13.856 1.00 66.86 ? 230 LYS A N   1 
ATOM   1772 C CA  . LYS A 1 230 ? 7.686  -45.187 -13.738 1.00 71.54 ? 230 LYS A CA  1 
ATOM   1773 C C   . LYS A 1 230 ? 7.317  -44.389 -12.489 1.00 75.11 ? 230 LYS A C   1 
ATOM   1774 O O   . LYS A 1 230 ? 6.495  -43.474 -12.556 1.00 79.16 ? 230 LYS A O   1 
ATOM   1775 C CB  . LYS A 1 230 ? 6.955  -46.533 -13.731 1.00 71.74 ? 230 LYS A CB  1 
ATOM   1776 C CG  . LYS A 1 230 ? 6.945  -47.234 -15.080 1.00 71.21 ? 230 LYS A CG  1 
ATOM   1777 C CD  . LYS A 1 230 ? 6.659  -48.723 -14.943 1.00 70.84 ? 230 LYS A CD  1 
ATOM   1778 C CE  . LYS A 1 230 ? 6.874  -49.458 -16.259 1.00 70.33 ? 230 LYS A CE  1 
ATOM   1779 N NZ  . LYS A 1 230 ? 7.062  -50.922 -16.059 1.00 69.00 ? 230 LYS A NZ  1 
ATOM   1780 N N   . HIS A 1 231 ? 7.929  -44.734 -11.358 1.00 74.83 ? 231 HIS A N   1 
ATOM   1781 C CA  . HIS A 1 231 ? 7.654  -44.050 -10.090 1.00 79.06 ? 231 HIS A CA  1 
ATOM   1782 C C   . HIS A 1 231 ? 8.216  -42.628 -10.045 1.00 81.41 ? 231 HIS A C   1 
ATOM   1783 O O   . HIS A 1 231 ? 7.640  -41.761 -9.388  1.00 85.74 ? 231 HIS A O   1 
ATOM   1784 C CB  . HIS A 1 231 ? 8.173  -44.870 -8.901  1.00 78.73 ? 231 HIS A CB  1 
ATOM   1785 C CG  . HIS A 1 231 ? 7.297  -46.033 -8.545  1.00 79.98 ? 231 HIS A CG  1 
ATOM   1786 N ND1 . HIS A 1 231 ? 6.130  -45.892 -7.824  1.00 84.89 ? 231 HIS A ND1 1 
ATOM   1787 C CD2 . HIS A 1 231 ? 7.415  -47.356 -8.813  1.00 77.62 ? 231 HIS A CD2 1 
ATOM   1788 C CE1 . HIS A 1 231 ? 5.568  -47.076 -7.663  1.00 85.70 ? 231 HIS A CE1 1 
ATOM   1789 N NE2 . HIS A 1 231 ? 6.328  -47.982 -8.253  1.00 81.40 ? 231 HIS A NE2 1 
ATOM   1790 N N   . HIS A 1 232 ? 9.332  -42.388 -10.733 1.00 79.64 ? 232 HIS A N   1 
ATOM   1791 C CA  . HIS A 1 232 ? 9.875  -41.030 -10.858 1.00 82.88 ? 232 HIS A CA  1 
ATOM   1792 C C   . HIS A 1 232 ? 8.978  -40.153 -11.738 1.00 86.27 ? 232 HIS A C   1 
ATOM   1793 O O   . HIS A 1 232 ? 8.735  -38.989 -11.412 1.00 90.77 ? 232 HIS A O   1 
ATOM   1794 C CB  . HIS A 1 232 ? 11.309 -41.043 -11.410 1.00 80.69 ? 232 HIS A CB  1 
ATOM   1795 C CG  . HIS A 1 232 ? 12.351 -41.399 -10.392 1.00 80.25 ? 232 HIS A CG  1 
ATOM   1796 N ND1 . HIS A 1 232 ? 12.397 -40.824 -9.139  1.00 84.29 ? 232 HIS A ND1 1 
ATOM   1797 C CD2 . HIS A 1 232 ? 13.401 -42.253 -10.451 1.00 77.06 ? 232 HIS A CD2 1 
ATOM   1798 C CE1 . HIS A 1 232 ? 13.421 -41.320 -8.466  1.00 83.60 ? 232 HIS A CE1 1 
ATOM   1799 N NE2 . HIS A 1 232 ? 14.047 -42.188 -9.240  1.00 79.07 ? 232 HIS A NE2 1 
ATOM   1800 N N   . HIS A 1 233 ? 8.492  -40.714 -12.845 1.00 85.01 ? 233 HIS A N   1 
ATOM   1801 C CA  . HIS A 1 233 ? 7.578  -40.005 -13.745 1.00 88.73 ? 233 HIS A CA  1 
ATOM   1802 C C   . HIS A 1 233 ? 6.131  -40.253 -13.336 1.00 91.15 ? 233 HIS A C   1 
ATOM   1803 O O   . HIS A 1 233 ? 5.486  -39.389 -12.745 1.00 95.27 ? 233 HIS A O   1 
ATOM   1804 C CB  . HIS A 1 233 ? 7.787  -40.452 -15.195 1.00 87.47 ? 233 HIS A CB  1 
ATOM   1805 C CG  . HIS A 1 233 ? 9.176  -40.219 -15.708 1.00 86.12 ? 233 HIS A CG  1 
ATOM   1806 N ND1 . HIS A 1 233 ? 9.762  -38.972 -15.734 1.00 89.49 ? 233 HIS A ND1 1 
ATOM   1807 C CD2 . HIS A 1 233 ? 10.089 -41.075 -16.227 1.00 82.50 ? 233 HIS A CD2 1 
ATOM   1808 C CE1 . HIS A 1 233 ? 10.979 -39.070 -16.238 1.00 88.06 ? 233 HIS A CE1 1 
ATOM   1809 N NE2 . HIS A 1 233 ? 11.202 -40.336 -16.545 1.00 83.73 ? 233 HIS A NE2 1 
HETATM 1810 P P   . PO4 B 2 .   ? 43.975 -52.063 -8.312  1.00 45.98 ? 301 PO4 A P   1 
HETATM 1811 O O1  . PO4 B 2 .   ? 44.832 -52.308 -9.528  1.00 44.46 ? 301 PO4 A O1  1 
HETATM 1812 O O2  . PO4 B 2 .   ? 43.427 -53.381 -7.824  1.00 47.55 ? 301 PO4 A O2  1 
HETATM 1813 O O3  . PO4 B 2 .   ? 44.800 -51.426 -7.217  1.00 45.71 ? 301 PO4 A O3  1 
HETATM 1814 O O4  . PO4 B 2 .   ? 42.832 -51.153 -8.688  1.00 45.31 ? 301 PO4 A O4  1 
HETATM 1815 P P   . PO4 C 2 .   ? 58.575 -34.830 -8.061  1.00 76.41 ? 302 PO4 A P   1 
HETATM 1816 O O1  . PO4 C 2 .   ? 58.738 -33.990 -6.815  1.00 75.22 ? 302 PO4 A O1  1 
HETATM 1817 O O2  . PO4 C 2 .   ? 59.526 -36.001 -8.012  1.00 76.07 ? 302 PO4 A O2  1 
HETATM 1818 O O3  . PO4 C 2 .   ? 57.158 -35.347 -8.138  1.00 73.52 ? 302 PO4 A O3  1 
HETATM 1819 O O4  . PO4 C 2 .   ? 58.882 -33.983 -9.274  1.00 74.67 ? 302 PO4 A O4  1 
HETATM 1820 P P   . PO4 D 2 .   ? 62.671 -40.697 -17.424 0.80 32.64 ? 303 PO4 A P   1 
HETATM 1821 O O1  . PO4 D 2 .   ? 63.719 -40.721 -18.519 0.80 30.34 ? 303 PO4 A O1  1 
HETATM 1822 O O2  . PO4 D 2 .   ? 61.291 -40.836 -18.017 0.80 28.53 ? 303 PO4 A O2  1 
HETATM 1823 O O3  . PO4 D 2 .   ? 62.941 -41.828 -16.448 0.80 30.02 ? 303 PO4 A O3  1 
HETATM 1824 O O4  . PO4 D 2 .   ? 62.731 -39.374 -16.695 0.80 30.70 ? 303 PO4 A O4  1 
HETATM 1825 P P   . PO4 E 2 .   ? 40.651 -55.256 -7.415  1.00 93.70 ? 304 PO4 A P   1 
HETATM 1826 O O1  . PO4 E 2 .   ? 41.111 -55.572 -6.012  1.00 93.70 ? 304 PO4 A O1  1 
HETATM 1827 O O2  . PO4 E 2 .   ? 41.719 -55.672 -8.398  1.00 92.99 ? 304 PO4 A O2  1 
HETATM 1828 O O3  . PO4 E 2 .   ? 39.377 -56.011 -7.711  1.00 93.28 ? 304 PO4 A O3  1 
HETATM 1829 O O4  . PO4 E 2 .   ? 40.399 -53.772 -7.541  1.00 92.75 ? 304 PO4 A O4  1 
HETATM 1830 P P   . PO4 F 2 .   ? 45.301 -36.244 -16.127 1.00 82.98 ? 305 PO4 A P   1 
HETATM 1831 O O1  . PO4 F 2 .   ? 44.102 -36.756 -15.365 1.00 82.06 ? 305 PO4 A O1  1 
HETATM 1832 O O2  . PO4 F 2 .   ? 44.963 -34.915 -16.760 1.00 81.75 ? 305 PO4 A O2  1 
HETATM 1833 O O3  . PO4 F 2 .   ? 46.466 -36.069 -15.181 1.00 81.14 ? 305 PO4 A O3  1 
HETATM 1834 O O4  . PO4 F 2 .   ? 45.670 -37.236 -17.204 1.00 82.06 ? 305 PO4 A O4  1 
HETATM 1835 P P   . PO4 G 2 .   ? 20.968 -39.004 -7.399  1.00 97.94 ? 306 PO4 A P   1 
HETATM 1836 O O1  . PO4 G 2 .   ? 21.904 -39.247 -6.238  1.00 97.59 ? 306 PO4 A O1  1 
HETATM 1837 O O2  . PO4 G 2 .   ? 19.539 -39.102 -6.922  1.00 97.80 ? 306 PO4 A O2  1 
HETATM 1838 O O3  . PO4 G 2 .   ? 21.216 -37.630 -7.973  1.00 97.12 ? 306 PO4 A O3  1 
HETATM 1839 O O4  . PO4 G 2 .   ? 21.214 -40.042 -8.465  1.00 96.97 ? 306 PO4 A O4  1 
HETATM 1840 P P   . PO4 H 2 .   ? 57.795 -48.575 -14.883 1.00 61.23 ? 307 PO4 A P   1 
HETATM 1841 O O1  . PO4 H 2 .   ? 56.809 -48.239 -15.977 1.00 55.67 ? 307 PO4 A O1  1 
HETATM 1842 O O2  . PO4 H 2 .   ? 57.050 -49.005 -13.637 1.00 58.20 ? 307 PO4 A O2  1 
HETATM 1843 O O3  . PO4 H 2 .   ? 58.710 -49.688 -15.343 1.00 60.82 ? 307 PO4 A O3  1 
HETATM 1844 O O4  . PO4 H 2 .   ? 58.608 -47.347 -14.560 1.00 61.06 ? 307 PO4 A O4  1 
HETATM 1845 C C1  . GOL I 3 .   ? 51.506 -44.970 -23.317 1.00 51.43 ? 308 GOL A C1  1 
HETATM 1846 O O1  . GOL I 3 .   ? 51.387 -46.323 -22.864 1.00 52.58 ? 308 GOL A O1  1 
HETATM 1847 C C2  . GOL I 3 .   ? 51.777 -44.056 -22.127 1.00 50.87 ? 308 GOL A C2  1 
HETATM 1848 O O2  . GOL I 3 .   ? 52.650 -43.002 -22.540 1.00 51.74 ? 308 GOL A O2  1 
HETATM 1849 C C3  . GOL I 3 .   ? 50.481 -43.456 -21.589 1.00 50.41 ? 308 GOL A C3  1 
HETATM 1850 O O3  . GOL I 3 .   ? 50.775 -42.464 -20.597 1.00 48.78 ? 308 GOL A O3  1 
HETATM 1851 C C1  . GOL J 3 .   ? 48.307 -49.711 -22.800 1.00 59.65 ? 309 GOL A C1  1 
HETATM 1852 O O1  . GOL J 3 .   ? 48.772 -48.789 -21.809 1.00 58.30 ? 309 GOL A O1  1 
HETATM 1853 C C2  . GOL J 3 .   ? 47.429 -48.986 -23.809 1.00 59.91 ? 309 GOL A C2  1 
HETATM 1854 O O2  . GOL J 3 .   ? 48.237 -48.492 -24.884 1.00 60.83 ? 309 GOL A O2  1 
HETATM 1855 C C3  . GOL J 3 .   ? 46.376 -49.947 -24.345 1.00 60.31 ? 309 GOL A C3  1 
HETATM 1856 O O3  . GOL J 3 .   ? 45.849 -49.459 -25.586 1.00 61.84 ? 309 GOL A O3  1 
HETATM 1857 C C1  . GOL K 3 .   ? 42.512 -69.346 -18.987 1.00 62.74 ? 310 GOL A C1  1 
HETATM 1858 O O1  . GOL K 3 .   ? 42.295 -68.641 -17.761 1.00 61.62 ? 310 GOL A O1  1 
HETATM 1859 C C2  . GOL K 3 .   ? 42.400 -68.385 -20.164 1.00 62.98 ? 310 GOL A C2  1 
HETATM 1860 O O2  . GOL K 3 .   ? 42.684 -69.088 -21.379 1.00 63.88 ? 310 GOL A O2  1 
HETATM 1861 C C3  . GOL K 3 .   ? 43.382 -67.229 -19.996 1.00 62.63 ? 310 GOL A C3  1 
HETATM 1862 O O3  . GOL K 3 .   ? 42.718 -66.095 -19.429 1.00 62.25 ? 310 GOL A O3  1 
HETATM 1863 O O   . HOH L 4 .   ? 64.239 -39.773 -14.705 1.00 24.92 ? 401 HOH A O   1 
HETATM 1864 O O   . HOH L 4 .   ? 58.098 -37.382 -12.529 1.00 24.40 ? 402 HOH A O   1 
HETATM 1865 O O   . HOH L 4 .   ? 55.780 -36.966 -6.103  1.00 33.11 ? 403 HOH A O   1 
HETATM 1866 O O   . HOH L 4 .   ? 48.827 -46.308 -22.716 1.00 39.82 ? 404 HOH A O   1 
HETATM 1867 O O   . HOH L 4 .   ? 50.958 -58.114 -21.434 1.00 28.45 ? 405 HOH A O   1 
HETATM 1868 O O   . HOH L 4 .   ? 34.545 -72.603 -17.186 1.00 49.12 ? 406 HOH A O   1 
HETATM 1869 O O   . HOH L 4 .   ? 50.606 -41.384 -14.812 1.00 20.46 ? 407 HOH A O   1 
HETATM 1870 O O   . HOH L 4 .   ? 52.191 -35.345 -22.756 1.00 20.93 ? 408 HOH A O   1 
HETATM 1871 O O   . HOH L 4 .   ? 22.350 -57.698 -23.170 1.00 29.21 ? 409 HOH A O   1 
HETATM 1872 O O   . HOH L 4 .   ? 43.983 -61.980 -16.631 1.00 25.47 ? 410 HOH A O   1 
HETATM 1873 O O   . HOH L 4 .   ? 18.399 -46.372 -9.307  1.00 44.69 ? 411 HOH A O   1 
HETATM 1874 O O   . HOH L 4 .   ? 46.824 -63.731 -18.873 1.00 29.34 ? 412 HOH A O   1 
HETATM 1875 O O   . HOH L 4 .   ? 37.188 -74.208 -7.247  1.00 55.46 ? 413 HOH A O   1 
HETATM 1876 O O   . HOH L 4 .   ? 61.327 -43.170 -19.342 1.00 20.72 ? 414 HOH A O   1 
HETATM 1877 O O   . HOH L 4 .   ? 28.375 -49.407 -4.250  1.00 31.04 ? 415 HOH A O   1 
HETATM 1878 O O   . HOH L 4 .   ? 24.662 -55.557 -3.549  1.00 39.86 ? 416 HOH A O   1 
HETATM 1879 O O   . HOH L 4 .   ? 14.626 -50.845 -18.291 1.00 41.14 ? 417 HOH A O   1 
HETATM 1880 O O   . HOH L 4 .   ? 18.178 -42.955 -13.217 1.00 40.64 ? 418 HOH A O   1 
HETATM 1881 O O   . HOH L 4 .   ? 38.812 -50.707 -6.150  1.00 47.90 ? 419 HOH A O   1 
HETATM 1882 O O   . HOH L 4 .   ? 25.283 -64.798 -8.895  1.00 50.62 ? 420 HOH A O   1 
HETATM 1883 O O   . HOH L 4 .   ? 32.687 -37.933 -4.698  1.00 43.76 ? 421 HOH A O   1 
HETATM 1884 O O   . HOH L 4 .   ? 19.219 -63.446 -11.412 1.00 46.53 ? 422 HOH A O   1 
HETATM 1885 O O   . HOH L 4 .   ? 37.811 -46.139 -16.497 1.00 29.67 ? 423 HOH A O   1 
HETATM 1886 O O   . HOH L 4 .   ? 47.993 -53.443 -6.028  1.00 63.54 ? 424 HOH A O   1 
HETATM 1887 O O   . HOH L 4 .   ? 18.182 -53.393 -23.313 1.00 32.90 ? 425 HOH A O   1 
HETATM 1888 O O   . HOH L 4 .   ? 30.305 -68.485 -21.663 1.00 49.29 ? 426 HOH A O   1 
HETATM 1889 O O   . HOH L 4 .   ? 23.575 -47.372 -24.185 1.00 43.68 ? 427 HOH A O   1 
HETATM 1890 O O   . HOH L 4 .   ? 19.896 -60.126 -20.309 1.00 35.78 ? 428 HOH A O   1 
HETATM 1891 O O   . HOH L 4 .   ? 52.042 -56.019 -2.513  1.00 73.97 ? 429 HOH A O   1 
HETATM 1892 O O   . HOH L 4 .   ? 33.999 -41.856 -2.567  1.00 39.36 ? 430 HOH A O   1 
HETATM 1893 O O   . HOH L 4 .   ? 64.145 -37.319 -15.551 1.00 32.94 ? 431 HOH A O   1 
HETATM 1894 O O   . HOH L 4 .   ? 26.821 -53.450 -21.764 1.00 26.40 ? 432 HOH A O   1 
HETATM 1895 O O   . HOH L 4 .   ? 24.049 -50.472 1.255   1.00 38.79 ? 433 HOH A O   1 
HETATM 1896 O O   . HOH L 4 .   ? 29.230 -68.651 -18.859 1.00 39.89 ? 434 HOH A O   1 
HETATM 1897 O O   . HOH L 4 .   ? 17.135 -51.051 -19.345 1.00 32.56 ? 435 HOH A O   1 
HETATM 1898 O O   . HOH L 4 .   ? 18.105 -50.925 -22.032 1.00 37.47 ? 436 HOH A O   1 
HETATM 1899 O O   . HOH L 4 .   ? 40.206 -72.666 -11.318 1.00 50.63 ? 437 HOH A O   1 
HETATM 1900 O O   . HOH L 4 .   ? 51.829 -39.592 -5.368  1.00 28.37 ? 438 HOH A O   1 
HETATM 1901 O O   . HOH L 4 .   ? 23.295 -61.700 -23.551 1.00 34.46 ? 439 HOH A O   1 
HETATM 1902 O O   . HOH L 4 .   ? 27.662 -67.403 -13.239 1.00 36.39 ? 440 HOH A O   1 
HETATM 1903 O O   . HOH L 4 .   ? 58.518 -49.272 -23.047 1.00 26.17 ? 441 HOH A O   1 
HETATM 1904 O O   . HOH L 4 .   ? 41.898 -64.251 -6.660  1.00 33.49 ? 442 HOH A O   1 
HETATM 1905 O O   . HOH L 4 .   ? 30.680 -69.018 -15.109 1.00 30.13 ? 443 HOH A O   1 
HETATM 1906 O O   . HOH L 4 .   ? 21.811 -55.343 -3.631  1.00 33.57 ? 444 HOH A O   1 
HETATM 1907 O O   . HOH L 4 .   ? 43.974 -59.562 -10.525 1.00 26.60 ? 445 HOH A O   1 
HETATM 1908 O O   . HOH L 4 .   ? 23.900 -61.890 -9.625  1.00 40.45 ? 446 HOH A O   1 
HETATM 1909 O O   . HOH L 4 .   ? 17.773 -50.834 -11.516 1.00 30.36 ? 447 HOH A O   1 
HETATM 1910 O O   . HOH L 4 .   ? 52.043 -37.127 -2.693  1.00 40.23 ? 448 HOH A O   1 
HETATM 1911 O O   . HOH L 4 .   ? 37.328 -72.974 -11.724 1.00 44.74 ? 449 HOH A O   1 
HETATM 1912 O O   . HOH L 4 .   ? 38.662 -52.808 -3.112  1.00 36.31 ? 450 HOH A O   1 
HETATM 1913 O O   . HOH L 4 .   ? 39.154 -67.193 -21.593 1.00 36.86 ? 451 HOH A O   1 
HETATM 1914 O O   . HOH L 4 .   ? 48.766 -65.310 -17.494 1.00 40.26 ? 452 HOH A O   1 
HETATM 1915 O O   . HOH L 4 .   ? 30.760 -52.713 -10.018 1.00 27.12 ? 453 HOH A O   1 
HETATM 1916 O O   . HOH L 4 .   ? 13.732 -54.154 -7.029  1.00 37.98 ? 454 HOH A O   1 
HETATM 1917 O O   . HOH L 4 .   ? 43.551 -48.566 -7.512  1.00 36.35 ? 455 HOH A O   1 
HETATM 1918 O O   . HOH L 4 .   ? 36.211 -62.649 -19.140 1.00 27.26 ? 456 HOH A O   1 
HETATM 1919 O O   . HOH L 4 .   ? 50.217 -27.752 -16.716 1.00 34.73 ? 457 HOH A O   1 
HETATM 1920 O O   . HOH L 4 .   ? 50.885 -64.192 -15.482 1.00 36.60 ? 458 HOH A O   1 
HETATM 1921 O O   . HOH L 4 .   ? 38.630 -62.073 -4.634  1.00 46.98 ? 459 HOH A O   1 
HETATM 1922 O O   . HOH L 4 .   ? 48.206 -66.307 -8.356  1.00 45.54 ? 460 HOH A O   1 
HETATM 1923 O O   . HOH L 4 .   ? 38.782 -44.084 -8.718  1.00 32.04 ? 461 HOH A O   1 
HETATM 1924 O O   . HOH L 4 .   ? 18.821 -57.608 -20.768 1.00 34.36 ? 462 HOH A O   1 
HETATM 1925 O O   . HOH L 4 .   ? 26.765 -59.583 -5.133  1.00 41.28 ? 463 HOH A O   1 
HETATM 1926 O O   . HOH L 4 .   ? 39.039 -45.839 1.820   1.00 48.12 ? 464 HOH A O   1 
HETATM 1927 O O   . HOH L 4 .   ? 30.290 -45.150 -3.437  1.00 35.86 ? 465 HOH A O   1 
HETATM 1928 O O   . HOH L 4 .   ? 33.662 -40.584 -5.036  1.00 37.45 ? 466 HOH A O   1 
HETATM 1929 O O   . HOH L 4 .   ? 49.828 -40.987 -11.974 1.00 21.87 ? 467 HOH A O   1 
HETATM 1930 O O   . HOH L 4 .   ? 17.319 -44.950 -20.765 1.00 41.01 ? 468 HOH A O   1 
HETATM 1931 O O   . HOH L 4 .   ? 46.079 -62.081 -7.621  1.00 65.27 ? 469 HOH A O   1 
HETATM 1932 O O   . HOH L 4 .   ? 54.721 -51.389 -24.458 1.00 46.41 ? 470 HOH A O   1 
HETATM 1933 O O   . HOH L 4 .   ? 57.366 -51.905 -22.816 1.00 39.74 ? 471 HOH A O   1 
HETATM 1934 O O   . HOH L 4 .   ? 51.550 -55.330 -12.862 1.00 22.28 ? 472 HOH A O   1 
HETATM 1935 O O   . HOH L 4 .   ? 13.082 -48.720 -19.305 1.00 54.03 ? 473 HOH A O   1 
HETATM 1936 O O   . HOH L 4 .   ? 43.179 -71.186 -8.560  1.00 50.43 ? 474 HOH A O   1 
HETATM 1937 O O   . HOH L 4 .   ? 53.548 -53.757 -1.440  1.00 38.16 ? 475 HOH A O   1 
HETATM 1938 O O   . HOH L 4 .   ? 21.771 -36.741 -11.302 1.00 60.10 ? 476 HOH A O   1 
HETATM 1939 O O   . HOH L 4 .   ? 49.535 -37.934 -9.421  1.00 22.53 ? 477 HOH A O   1 
HETATM 1940 O O   . HOH L 4 .   ? 51.298 -50.131 -21.973 1.00 47.85 ? 478 HOH A O   1 
HETATM 1941 O O   . HOH L 4 .   ? 57.755 -51.740 -12.111 1.00 28.20 ? 479 HOH A O   1 
HETATM 1942 O O   . HOH L 4 .   ? 29.264 -37.689 -15.744 1.00 37.77 ? 480 HOH A O   1 
HETATM 1943 O O   . HOH L 4 .   ? 46.638 -55.470 -7.702  1.00 52.85 ? 481 HOH A O   1 
HETATM 1944 O O   . HOH L 4 .   ? 62.134 -39.895 -12.763 1.00 27.18 ? 482 HOH A O   1 
HETATM 1945 O O   . HOH L 4 .   ? 44.494 -64.650 -17.683 1.00 35.07 ? 483 HOH A O   1 
HETATM 1946 O O   . HOH L 4 .   ? 43.666 -34.763 -4.291  1.00 42.80 ? 484 HOH A O   1 
HETATM 1947 O O   . HOH L 4 .   ? 32.728 -64.007 -0.939  1.00 63.70 ? 485 HOH A O   1 
HETATM 1948 O O   . HOH L 4 .   ? 28.086 -40.486 -10.714 1.00 26.18 ? 486 HOH A O   1 
HETATM 1949 O O   . HOH L 4 .   ? 12.477 -59.117 -12.770 1.00 59.56 ? 487 HOH A O   1 
HETATM 1950 O O   . HOH L 4 .   ? 30.840 -51.947 -7.332  1.00 25.15 ? 488 HOH A O   1 
HETATM 1951 O O   . HOH L 4 .   ? 39.136 -25.989 -8.572  1.00 45.20 ? 489 HOH A O   1 
HETATM 1952 O O   . HOH L 4 .   ? 21.497 -49.027 0.883   1.00 43.96 ? 490 HOH A O   1 
HETATM 1953 O O   . HOH L 4 .   ? 31.963 -54.977 -24.297 1.00 26.34 ? 491 HOH A O   1 
HETATM 1954 O O   . HOH L 4 .   ? 43.715 -57.774 -8.218  1.00 59.27 ? 492 HOH A O   1 
HETATM 1955 O O   . HOH L 4 .   ? 16.871 -48.293 -10.752 1.00 41.27 ? 493 HOH A O   1 
HETATM 1956 O O   . HOH L 4 .   ? 38.147 -58.439 -6.640  1.00 79.97 ? 494 HOH A O   1 
HETATM 1957 O O   . HOH L 4 .   ? 44.142 -37.852 -19.621 1.00 68.28 ? 495 HOH A O   1 
HETATM 1958 O O   . HOH L 4 .   ? 27.221 -40.257 -7.538  1.00 38.53 ? 496 HOH A O   1 
HETATM 1959 O O   . HOH L 4 .   ? 15.872 -62.662 -15.282 1.00 60.11 ? 497 HOH A O   1 
HETATM 1960 O O   . HOH L 4 .   ? 23.668 -39.500 -22.643 1.00 30.65 ? 498 HOH A O   1 
HETATM 1961 O O   . HOH L 4 .   ? 25.577 -68.723 -15.126 1.00 43.34 ? 499 HOH A O   1 
HETATM 1962 O O   . HOH L 4 .   ? 38.901 -28.507 -10.722 1.00 38.15 ? 500 HOH A O   1 
HETATM 1963 O O   . HOH L 4 .   ? 14.166 -56.581 -5.469  1.00 45.91 ? 501 HOH A O   1 
HETATM 1964 O O   . HOH L 4 .   ? 13.729 -57.135 -10.916 1.00 55.33 ? 502 HOH A O   1 
HETATM 1965 O O   . HOH L 4 .   ? 55.886 -44.601 -0.741  1.00 47.59 ? 503 HOH A O   1 
HETATM 1966 O O   . HOH L 4 .   ? 21.559 -64.947 -11.769 1.00 57.73 ? 504 HOH A O   1 
HETATM 1967 O O   . HOH L 4 .   ? 24.294 -49.263 -1.178  1.00 36.59 ? 505 HOH A O   1 
HETATM 1968 O O   . HOH L 4 .   ? 54.191 -37.746 0.665   1.00 46.87 ? 506 HOH A O   1 
HETATM 1969 O O   . HOH L 4 .   ? 33.473 -33.621 -5.000  1.00 58.52 ? 507 HOH A O   1 
HETATM 1970 O O   . HOH L 4 .   ? 53.093 -33.076 -3.908  1.00 45.21 ? 508 HOH A O   1 
HETATM 1971 O O   . HOH L 4 .   ? 13.545 -60.873 -15.073 1.00 67.91 ? 509 HOH A O   1 
HETATM 1972 O O   . HOH L 4 .   ? 38.097 -72.545 -14.466 1.00 34.53 ? 510 HOH A O   1 
HETATM 1973 O O   . HOH L 4 .   ? 12.248 -55.042 -9.461  1.00 57.68 ? 511 HOH A O   1 
HETATM 1974 O O   . HOH L 4 .   ? 23.381 -67.370 -23.967 1.00 55.47 ? 512 HOH A O   1 
HETATM 1975 O O   . HOH L 4 .   ? 40.502 -71.560 -20.805 1.00 69.56 ? 513 HOH A O   1 
HETATM 1976 O O   . HOH L 4 .   ? 48.019 -27.459 -13.508 1.00 56.14 ? 514 HOH A O   1 
HETATM 1977 O O   . HOH L 4 .   ? 24.939 -61.820 -5.602  1.00 47.94 ? 515 HOH A O   1 
HETATM 1978 O O   . HOH L 4 .   ? 49.097 -35.099 -2.275  1.00 35.35 ? 516 HOH A O   1 
HETATM 1979 O O   . HOH L 4 .   ? 37.857 -50.145 -24.320 0.50 46.93 ? 517 HOH A O   1 
HETATM 1980 O O   . HOH L 4 .   ? 27.581 -66.241 -9.851  1.00 52.97 ? 518 HOH A O   1 
HETATM 1981 O O   . HOH L 4 .   ? 37.944 -61.599 -17.131 1.00 25.51 ? 519 HOH A O   1 
HETATM 1982 O O   . HOH L 4 .   ? 33.646 -37.727 -12.550 1.00 40.77 ? 520 HOH A O   1 
HETATM 1983 O O   . HOH L 4 .   ? 22.969 -34.389 -14.294 1.00 65.63 ? 521 HOH A O   1 
HETATM 1984 O O   . HOH L 4 .   ? 42.490 -71.551 -16.474 1.00 60.71 ? 522 HOH A O   1 
HETATM 1985 O O   . HOH L 4 .   ? 31.032 -41.158 -5.854  1.00 44.35 ? 523 HOH A O   1 
HETATM 1986 O O   . HOH L 4 .   ? 17.551 -41.199 -16.663 1.00 48.48 ? 524 HOH A O   1 
HETATM 1987 O O   . HOH L 4 .   ? 29.590 -56.533 -24.430 1.00 24.61 ? 525 HOH A O   1 
HETATM 1988 O O   . HOH L 4 .   ? 16.408 -40.732 -14.023 1.00 69.53 ? 526 HOH A O   1 
HETATM 1989 O O   . HOH L 4 .   ? 52.016 -65.028 -12.820 1.00 62.28 ? 527 HOH A O   1 
HETATM 1990 O O   . HOH L 4 .   ? 52.149 -49.984 -24.795 1.00 80.35 ? 528 HOH A O   1 
HETATM 1991 O O   . HOH L 4 .   ? 26.715 -36.631 -14.366 1.00 55.11 ? 529 HOH A O   1 
HETATM 1992 O O   . HOH L 4 .   ? 60.891 -37.550 -11.842 1.00 32.06 ? 530 HOH A O   1 
HETATM 1993 O O   . HOH L 4 .   ? 40.800 -73.456 -14.977 1.00 53.93 ? 531 HOH A O   1 
HETATM 1994 O O   . HOH L 4 .   ? 31.982 -37.030 -14.823 1.00 66.46 ? 532 HOH A O   1 
HETATM 1995 O O   . HOH L 4 .   ? 46.542 -59.750 -9.171  1.00 55.11 ? 533 HOH A O   1 
HETATM 1996 O O   . HOH L 4 .   ? 54.608 -48.464 -24.226 1.00 48.71 ? 534 HOH A O   1 
HETATM 1997 O O   . HOH L 4 .   ? 17.141 -63.701 -19.235 1.00 62.91 ? 535 HOH A O   1 
HETATM 1998 O O   . HOH L 4 .   ? 36.377 -74.485 -15.841 1.00 56.85 ? 536 HOH A O   1 
HETATM 1999 O O   . HOH L 4 .   ? 54.354 -35.763 -3.747  1.00 55.20 ? 537 HOH A O   1 
HETATM 2000 O O   . HOH L 4 .   ? 57.297 -47.924 -25.386 1.00 46.71 ? 538 HOH A O   1 
HETATM 2001 O O   . HOH L 4 .   ? 48.888 -25.481 -10.759 1.00 68.81 ? 539 HOH A O   1 
HETATM 2002 O O   . HOH L 4 .   ? 25.725 -58.135 -2.711  1.00 64.76 ? 540 HOH A O   1 
HETATM 2003 O O   . HOH L 4 .   ? 37.836 -59.317 -3.907  1.00 67.12 ? 541 HOH A O   1 
HETATM 2004 O O   . HOH L 4 .   ? 22.387 -60.013 -21.582 1.00 37.81 ? 542 HOH A O   1 
HETATM 2005 O O   . HOH L 4 .   ? 28.238 -69.402 -25.493 1.00 53.45 ? 543 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 2   ? 0.7426 0.9984 0.7213 -0.0110 0.1275  -0.0542 2   ALA A N   
2    C CA  . ALA A 2   ? 0.7126 0.9073 0.7390 0.0081  0.1142  -0.0461 2   ALA A CA  
3    C C   . ALA A 2   ? 0.7015 0.8297 0.7140 0.0047  0.0910  -0.0474 2   ALA A C   
4    O O   . ALA A 2   ? 0.7000 0.8296 0.6792 -0.0133 0.0768  -0.0328 2   ALA A O   
5    C CB  . ALA A 2   ? 0.6752 0.8892 0.7356 0.0050  0.1042  -0.0022 2   ALA A CB  
6    N N   . LEU A 3   ? 0.7017 0.7782 0.7442 0.0236  0.0888  -0.0596 3   LEU A N   
7    C CA  . LEU A 3   ? 0.6876 0.7046 0.7228 0.0207  0.0685  -0.0547 3   LEU A CA  
8    C C   . LEU A 3   ? 0.6362 0.6503 0.6832 0.0170  0.0441  -0.0149 3   LEU A C   
9    O O   . LEU A 3   ? 0.6210 0.6631 0.6998 0.0238  0.0433  0.0020  3   LEU A O   
10   C CB  . LEU A 3   ? 0.7196 0.6862 0.7896 0.0434  0.0780  -0.0722 3   LEU A CB  
11   C CG  . LEU A 3   ? 0.7815 0.7317 0.8490 0.0454  0.1079  -0.1241 3   LEU A CG  
12   C CD1 . LEU A 3   ? 0.8166 0.7291 0.9459 0.0795  0.1280  -0.1318 3   LEU A CD1 
13   C CD2 . LEU A 3   ? 0.8037 0.7187 0.8337 0.0202  0.1021  -0.1479 3   LEU A CD2 
14   N N   . VAL A 4   ? 0.6124 0.5979 0.6369 0.0041  0.0262  -0.0049 4   VAL A N   
15   C CA  . VAL A 4   ? 0.5721 0.5516 0.6074 -0.0010 0.0073  0.0219  4   VAL A CA  
16   C C   . VAL A 4   ? 0.5595 0.5272 0.6257 0.0150  -0.0003 0.0278  4   VAL A C   
17   O O   . VAL A 4   ? 0.5773 0.5157 0.6504 0.0290  0.0036  0.0197  4   VAL A O   
18   C CB  . VAL A 4   ? 0.5655 0.5203 0.5740 -0.0150 -0.0058 0.0283  4   VAL A CB  
19   C CG1 . VAL A 4   ? 0.5800 0.4933 0.5820 -0.0110 -0.0117 0.0179  4   VAL A CG1 
20   C CG2 . VAL A 4   ? 0.5420 0.4981 0.5633 -0.0231 -0.0165 0.0484  4   VAL A CG2 
21   N N   . PRO A 5   ? 0.5279 0.5236 0.6172 0.0118  -0.0102 0.0435  5   PRO A N   
22   C CA  . PRO A 5   ? 0.5219 0.5274 0.6368 0.0251  -0.0221 0.0553  5   PRO A CA  
23   C C   . PRO A 5   ? 0.5190 0.4896 0.6137 0.0233  -0.0358 0.0625  5   PRO A C   
24   O O   . PRO A 5   ? 0.5098 0.4543 0.5744 0.0078  -0.0384 0.0565  5   PRO A O   
25   C CB  . PRO A 5   ? 0.5030 0.5555 0.6382 0.0098  -0.0315 0.0623  5   PRO A CB  
26   C CG  . PRO A 5   ? 0.5003 0.5655 0.6376 -0.0024 -0.0161 0.0572  5   PRO A CG  
27   C CD  . PRO A 5   ? 0.5102 0.5370 0.6099 -0.0050 -0.0084 0.0513  5   PRO A CD  
28   N N   . PRO A 6   ? 0.5275 0.5051 0.6428 0.0403  -0.0437 0.0811  6   PRO A N   
29   C CA  . PRO A 6   ? 0.5309 0.4842 0.6284 0.0375  -0.0550 0.0950  6   PRO A CA  
30   C C   . PRO A 6   ? 0.5030 0.4708 0.5724 0.0121  -0.0684 0.0903  6   PRO A C   
31   O O   . PRO A 6   ? 0.4867 0.4938 0.5632 -0.0007 -0.0735 0.0831  6   PRO A O   
32   C CB  . PRO A 6   ? 0.5495 0.5367 0.6817 0.0600  -0.0632 0.1280  6   PRO A CB  
33   C CG  . PRO A 6   ? 0.5617 0.5649 0.7356 0.0829  -0.0486 0.1261  6   PRO A CG  
34   C CD  . PRO A 6   ? 0.5380 0.5557 0.6990 0.0645  -0.0416 0.0972  6   PRO A CD  
35   N N   . GLY A 7   ? 0.4997 0.4356 0.5427 0.0036  -0.0708 0.0911  7   GLY A N   
36   C CA  . GLY A 7   ? 0.4824 0.4316 0.5040 -0.0167 -0.0786 0.0838  7   GLY A CA  
37   C C   . GLY A 7   ? 0.4824 0.3971 0.4797 -0.0240 -0.0766 0.0836  7   GLY A C   
38   O O   . GLY A 7   ? 0.4970 0.3769 0.4931 -0.0175 -0.0711 0.0894  7   GLY A O   
39   N N   . ASN A 8   ? 0.4694 0.3954 0.4526 -0.0394 -0.0784 0.0732  8   ASN A N   
40   C CA  . ASN A 8   ? 0.4702 0.3767 0.4352 -0.0469 -0.0757 0.0734  8   ASN A CA  
41   C C   . ASN A 8   ? 0.4598 0.3377 0.4240 -0.0482 -0.0673 0.0657  8   ASN A C   
42   O O   . ASN A 8   ? 0.4460 0.3246 0.4201 -0.0463 -0.0623 0.0590  8   ASN A O   
43   C CB  . ASN A 8   ? 0.4701 0.4026 0.4269 -0.0605 -0.0751 0.0596  8   ASN A CB  
44   C CG  . ASN A 8   ? 0.4876 0.4663 0.4327 -0.0649 -0.0851 0.0684  8   ASN A CG  
45   O OD1 . ASN A 8   ? 0.5035 0.4859 0.4380 -0.0607 -0.0896 0.0941  8   ASN A OD1 
46   N ND2 . ASN A 8   ? 0.4921 0.5125 0.4411 -0.0761 -0.0881 0.0486  8   ASN A ND2 
47   N N   . ASP A 9   ? 0.4657 0.3287 0.4190 -0.0535 -0.0663 0.0699  9   ASP A N   
48   C CA  . ASP A 9   ? 0.4611 0.3182 0.4118 -0.0590 -0.0619 0.0642  9   ASP A CA  
49   C C   . ASP A 9   ? 0.4684 0.3279 0.4120 -0.0694 -0.0623 0.0690  9   ASP A C   
50   O O   . ASP A 9   ? 0.4700 0.3382 0.4094 -0.0717 -0.0632 0.0753  9   ASP A O   
51   C CB  . ASP A 9   ? 0.4726 0.3157 0.4224 -0.0574 -0.0586 0.0563  9   ASP A CB  
52   C CG  . ASP A 9   ? 0.5004 0.3137 0.4512 -0.0603 -0.0563 0.0557  9   ASP A CG  
53   O OD1 . ASP A 9   ? 0.5075 0.3140 0.4594 -0.0623 -0.0592 0.0710  9   ASP A OD1 
54   O OD2 . ASP A 9   ? 0.5181 0.3153 0.4717 -0.0615 -0.0487 0.0393  9   ASP A OD2 
55   N N   . VAL A 10  ? 0.4747 0.3390 0.4167 -0.0779 -0.0615 0.0661  10  VAL A N   
56   C CA  . VAL A 10  ? 0.4817 0.3579 0.4231 -0.0905 -0.0616 0.0709  10  VAL A CA  
57   C C   . VAL A 10  ? 0.5085 0.3631 0.4462 -0.0991 -0.0608 0.0786  10  VAL A C   
58   O O   . VAL A 10  ? 0.5120 0.3821 0.4496 -0.1074 -0.0589 0.0882  10  VAL A O   
59   C CB  . VAL A 10  ? 0.4852 0.3841 0.4269 -0.1029 -0.0638 0.0653  10  VAL A CB  
60   C CG1 . VAL A 10  ? 0.5146 0.3901 0.4485 -0.1152 -0.0627 0.0470  10  VAL A CG1 
61   C CG2 . VAL A 10  ? 0.4856 0.4139 0.4353 -0.1151 -0.0642 0.0730  10  VAL A CG2 
62   N N   . THR A 11  ? 0.5316 0.3529 0.4722 -0.0955 -0.0595 0.0784  11  THR A N   
63   C CA  . THR A 11  ? 0.5666 0.3613 0.5149 -0.1002 -0.0557 0.0961  11  THR A CA  
64   C C   . THR A 11  ? 0.5679 0.3845 0.5103 -0.0909 -0.0595 0.1223  11  THR A C   
65   O O   . THR A 11  ? 0.5951 0.4089 0.5408 -0.0972 -0.0565 0.1478  11  THR A O   
66   C CB  . THR A 11  ? 0.6005 0.3488 0.5667 -0.0935 -0.0481 0.0911  11  THR A CB  
67   O OG1 . THR A 11  ? 0.5882 0.3425 0.5584 -0.0701 -0.0512 0.0971  11  THR A OG1 
68   C CG2 . THR A 11  ? 0.6125 0.3497 0.5784 -0.1077 -0.0423 0.0552  11  THR A CG2 
69   N N   . THR A 12  ? 0.5210 0.4215 0.4686 -0.1454 -0.0427 0.0929  12  THR A N   
70   C CA  . THR A 12  ? 0.5359 0.4369 0.4677 -0.1545 -0.0457 0.1019  12  THR A CA  
71   C C   . THR A 12  ? 0.5333 0.4502 0.4515 -0.1597 -0.0348 0.0954  12  THR A C   
72   O O   . THR A 12  ? 0.5481 0.4673 0.4501 -0.1731 -0.0340 0.1011  12  THR A O   
73   C CB  . THR A 12  ? 0.5361 0.4307 0.4717 -0.1476 -0.0536 0.1066  12  THR A CB  
74   O OG1 . THR A 12  ? 0.5170 0.4200 0.4581 -0.1355 -0.0477 0.0956  12  THR A OG1 
75   C CG2 . THR A 12  ? 0.5431 0.4214 0.4957 -0.1431 -0.0640 0.1134  12  THR A CG2 
76   N N   . LYS A 13  ? 0.5145 0.4423 0.4401 -0.1500 -0.0264 0.0836  13  LYS A N   
77   C CA  . LYS A 13  ? 0.5103 0.4529 0.4290 -0.1530 -0.0151 0.0763  13  LYS A CA  
78   C C   . LYS A 13  ? 0.4945 0.4483 0.4258 -0.1476 -0.0068 0.0667  13  LYS A C   
79   O O   . LYS A 13  ? 0.4737 0.4352 0.4143 -0.1373 -0.0026 0.0593  13  LYS A O   
80   C CB  . LYS A 13  ? 0.5064 0.4518 0.4230 -0.1462 -0.0142 0.0732  13  LYS A CB  
81   C CG  . LYS A 13  ? 0.5247 0.4619 0.4279 -0.1532 -0.0224 0.0830  13  LYS A CG  
82   C CD  . LYS A 13  ? 0.5194 0.4601 0.4211 -0.1465 -0.0210 0.0790  13  LYS A CD  
83   C CE  . LYS A 13  ? 0.5385 0.4737 0.4252 -0.1561 -0.0290 0.0891  13  LYS A CE  
84   N NZ  . LYS A 13  ? 0.5338 0.4728 0.4189 -0.1502 -0.0276 0.0848  13  LYS A NZ  
85   N N   . PRO A 14  ? 0.5013 0.4567 0.4334 -0.1553 -0.0049 0.0678  14  PRO A N   
86   C CA  . PRO A 14  ? 0.4895 0.4560 0.4351 -0.1512 0.0010  0.0605  14  PRO A CA  
87   C C   . PRO A 14  ? 0.4795 0.4630 0.4304 -0.1496 0.0125  0.0524  14  PRO A C   
88   O O   . PRO A 14  ? 0.4696 0.4636 0.4353 -0.1440 0.0161  0.0472  14  PRO A O   
89   C CB  . PRO A 14  ? 0.5024 0.4662 0.4449 -0.1627 0.0003  0.0648  14  PRO A CB  
90   C CG  . PRO A 14  ? 0.5215 0.4791 0.4464 -0.1752 -0.0013 0.0725  14  PRO A CG  
91   C CD  . PRO A 14  ? 0.5227 0.4707 0.4429 -0.1695 -0.0086 0.0767  14  PRO A CD  
92   N N   . ASP A 15  ? 0.4839 0.4702 0.4240 -0.1553 0.0180  0.0515  15  ASP A N   
93   C CA  A ASP A 15  ? 0.4770 0.4778 0.4239 -0.1540 0.0302  0.0427  15  ASP A CA  
94   C CA  B ASP A 15  ? 0.4758 0.4769 0.4233 -0.1538 0.0302  0.0426  15  ASP A CA  
95   C C   . ASP A 15  ? 0.4596 0.4620 0.4147 -0.1409 0.0301  0.0385  15  ASP A C   
96   O O   . ASP A 15  ? 0.4481 0.4620 0.4152 -0.1366 0.0392  0.0313  15  ASP A O   
97   C CB  A ASP A 15  ? 0.4971 0.5003 0.4275 -0.1683 0.0380  0.0418  15  ASP A CB  
98   C CB  B ASP A 15  ? 0.4945 0.4987 0.4265 -0.1680 0.0385  0.0413  15  ASP A CB  
99   C CG  A ASP A 15  ? 0.5119 0.5030 0.4225 -0.1731 0.0302  0.0487  15  ASP A CG  
100  C CG  B ASP A 15  ? 0.5092 0.5165 0.4363 -0.1816 0.0420  0.0433  15  ASP A CG  
101  O OD1 A ASP A 15  ? 0.5162 0.4946 0.4234 -0.1710 0.0177  0.0577  15  ASP A OD1 
102  O OD1 B ASP A 15  ? 0.5026 0.5156 0.4441 -0.1787 0.0426  0.0421  15  ASP A OD1 
103  O OD2 A ASP A 15  ? 0.5207 0.5153 0.4202 -0.1796 0.0368  0.0450  15  ASP A OD2 
104  O OD2 B ASP A 15  ? 0.5311 0.5358 0.4392 -0.1962 0.0439  0.0464  15  ASP A OD2 
105  N N   . LEU A 16  ? 0.4529 0.4436 0.4031 -0.1348 0.0202  0.0431  16  LEU A N   
106  C CA  . LEU A 16  ? 0.4373 0.4284 0.3933 -0.1232 0.0193  0.0398  16  LEU A CA  
107  C C   . LEU A 16  ? 0.4154 0.4030 0.3825 -0.1120 0.0117  0.0404  16  LEU A C   
108  O O   . LEU A 16  ? 0.3975 0.3874 0.3712 -0.1026 0.0117  0.0372  16  LEU A O   
109  C CB  . LEU A 16  ? 0.4522 0.4349 0.3926 -0.1265 0.0157  0.0433  16  LEU A CB  
110  C CG  . LEU A 16  ? 0.4688 0.4575 0.3979 -0.1368 0.0255  0.0394  16  LEU A CG  
111  C CD1 . LEU A 16  ? 0.4865 0.4661 0.3961 -0.1444 0.0192  0.0458  16  LEU A CD1 
112  C CD2 . LEU A 16  ? 0.4587 0.4576 0.4001 -0.1292 0.0356  0.0297  16  LEU A CD2 
113  N N   . TYR A 17  ? 0.4113 0.3933 0.3799 -0.1140 0.0060  0.0438  17  TYR A N   
114  C CA  . TYR A 17  ? 0.3977 0.3771 0.3760 -0.1060 0.0003  0.0426  17  TYR A CA  
115  C C   . TYR A 17  ? 0.3980 0.3821 0.3831 -0.1100 0.0007  0.0420  17  TYR A C   
116  O O   . TYR A 17  ? 0.4061 0.3876 0.3860 -0.1192 0.0011  0.0452  17  TYR A O   
117  C CB  . TYR A 17  ? 0.4029 0.3664 0.3766 -0.1047 -0.0085 0.0469  17  TYR A CB  
118  C CG  . TYR A 17  ? 0.4036 0.3606 0.3704 -0.1020 -0.0115 0.0495  17  TYR A CG  
119  C CD1 . TYR A 17  ? 0.4155 0.3704 0.3696 -0.1103 -0.0109 0.0543  17  TYR A CD1 
120  C CD2 . TYR A 17  ? 0.3926 0.3457 0.3650 -0.0926 -0.0153 0.0474  17  TYR A CD2 
121  C CE1 . TYR A 17  ? 0.4176 0.3674 0.3649 -0.1092 -0.0146 0.0575  17  TYR A CE1 
122  C CE2 . TYR A 17  ? 0.3961 0.3440 0.3635 -0.0904 -0.0186 0.0503  17  TYR A CE2 
123  C CZ  . TYR A 17  ? 0.4073 0.3536 0.3622 -0.0987 -0.0187 0.0556  17  TYR A CZ  
124  O OH  . TYR A 17  ? 0.4086 0.3508 0.3579 -0.0978 -0.0228 0.0591  17  TYR A OH  
125  N N   . TYR A 18  ? 0.3867 0.3782 0.3829 -0.1042 0.0001  0.0385  18  TYR A N   
126  C CA  . TYR A 18  ? 0.3891 0.3835 0.3910 -0.1080 -0.0018 0.0379  18  TYR A CA  
127  C C   . TYR A 18  ? 0.3922 0.3731 0.3919 -0.1071 -0.0084 0.0374  18  TYR A C   
128  O O   . TYR A 18  ? 0.3989 0.3762 0.3995 -0.1129 -0.0103 0.0374  18  TYR A O   
129  C CB  . TYR A 18  ? 0.3784 0.3889 0.3932 -0.1042 0.0000  0.0352  18  TYR A CB  
130  C CG  . TYR A 18  ? 0.3755 0.4007 0.3994 -0.1057 0.0071  0.0352  18  TYR A CG  
131  C CD1 . TYR A 18  ? 0.3835 0.4158 0.4116 -0.1137 0.0101  0.0361  18  TYR A CD1 
132  C CD2 . TYR A 18  ? 0.3683 0.4006 0.3988 -0.0992 0.0115  0.0336  18  TYR A CD2 
133  C CE1 . TYR A 18  ? 0.3819 0.4285 0.4218 -0.1150 0.0178  0.0350  18  TYR A CE1 
134  C CE2 . TYR A 18  ? 0.3672 0.4128 0.4101 -0.1003 0.0193  0.0324  18  TYR A CE2 
135  C CZ  . TYR A 18  ? 0.3739 0.4270 0.4223 -0.1080 0.0227  0.0329  18  TYR A CZ  
136  O OH  . TYR A 18  ? 0.3772 0.4441 0.4413 -0.1090 0.0316  0.0307  18  TYR A OH  
137  N N   . LEU A 19  ? 0.3872 0.3608 0.3857 -0.1000 -0.0112 0.0362  19  LEU A N   
138  C CA  . LEU A 19  ? 0.3899 0.3534 0.3908 -0.0977 -0.0156 0.0331  19  LEU A CA  
139  C C   . LEU A 19  ? 0.4018 0.3479 0.4001 -0.0980 -0.0200 0.0367  19  LEU A C   
140  O O   . LEU A 19  ? 0.4034 0.3458 0.3957 -0.0986 -0.0209 0.0422  19  LEU A O   
141  C CB  . LEU A 19  ? 0.3795 0.3486 0.3841 -0.0898 -0.0155 0.0285  19  LEU A CB  
142  C CG  . LEU A 19  ? 0.3682 0.3548 0.3778 -0.0889 -0.0130 0.0269  19  LEU A CG  
143  C CD1 . LEU A 19  ? 0.3583 0.3485 0.3698 -0.0819 -0.0137 0.0237  19  LEU A CD1 
144  C CD2 . LEU A 19  ? 0.3719 0.3643 0.3846 -0.0960 -0.0137 0.0252  19  LEU A CD2 
145  N N   . THR A 20  ? 0.4093 0.3449 0.4131 -0.0984 -0.0227 0.0336  20  THR A N   
146  C CA  . THR A 20  ? 0.4221 0.3406 0.4294 -0.0975 -0.0275 0.0370  20  THR A CA  
147  C C   . THR A 20  ? 0.4176 0.3332 0.4302 -0.0885 -0.0286 0.0334  20  THR A C   
148  O O   . THR A 20  ? 0.4056 0.3311 0.4185 -0.0840 -0.0255 0.0270  20  THR A O   
149  C CB  . THR A 20  ? 0.4340 0.3411 0.4488 -0.1022 -0.0289 0.0342  20  THR A CB  
150  O OG1 . THR A 20  ? 0.4294 0.3400 0.4497 -0.1000 -0.0258 0.0235  20  THR A OG1 
151  C CG2 . THR A 20  ? 0.4423 0.3521 0.4522 -0.1118 -0.0279 0.0375  20  THR A CG2 
152  N N   . ASN A 21  ? 0.4283 0.3307 0.4462 -0.0864 -0.0336 0.0382  21  ASN A N   
153  C CA  . ASN A 21  ? 0.4242 0.3228 0.4506 -0.0781 -0.0348 0.0348  21  ASN A CA  
154  C C   . ASN A 21  ? 0.4217 0.3206 0.4569 -0.0757 -0.0307 0.0227  21  ASN A C   
155  O O   . ASN A 21  ? 0.4140 0.3188 0.4505 -0.0700 -0.0284 0.0168  21  ASN A O   
156  C CB  . ASN A 21  ? 0.4357 0.3192 0.4712 -0.0773 -0.0418 0.0429  21  ASN A CB  
157  C CG  . ASN A 21  ? 0.4388 0.3241 0.4636 -0.0793 -0.0463 0.0542  21  ASN A CG  
158  O OD1 . ASN A 21  ? 0.4267 0.3228 0.4421 -0.0768 -0.0436 0.0530  21  ASN A OD1 
159  N ND2 . ASN A 21  ? 0.4539 0.3286 0.4802 -0.0849 -0.0533 0.0653  21  ASN A ND2 
160  N N   . ALA A 22  ? 0.4297 0.3227 0.4696 -0.0813 -0.0294 0.0186  22  ALA A N   
161  C CA  . ALA A 22  ? 0.4328 0.3263 0.4791 -0.0820 -0.0245 0.0058  22  ALA A CA  
162  C C   . ALA A 22  ? 0.4205 0.3319 0.4564 -0.0832 -0.0205 0.0001  22  ALA A C   
163  O O   . ALA A 22  ? 0.4196 0.3343 0.4576 -0.0832 -0.0168 -0.0098 22  ALA A O   
164  C CB  . ALA A 22  ? 0.4471 0.3307 0.4994 -0.0895 -0.0237 0.0027  22  ALA A CB  
165  N N   . GLN A 23  ? 0.4135 0.3363 0.4393 -0.0849 -0.0212 0.0068  23  GLN A N   
166  C CA  . GLN A 23  ? 0.4040 0.3442 0.4234 -0.0859 -0.0188 0.0043  23  GLN A CA  
167  C C   . GLN A 23  ? 0.3895 0.3375 0.4066 -0.0782 -0.0187 0.0059  23  GLN A C   
168  O O   . GLN A 23  ? 0.3794 0.3413 0.3932 -0.0783 -0.0175 0.0053  23  GLN A O   
169  C CB  . GLN A 23  ? 0.4047 0.3540 0.4191 -0.0915 -0.0188 0.0100  23  GLN A CB  
170  C CG  . GLN A 23  ? 0.4202 0.3651 0.4358 -0.1004 -0.0187 0.0078  23  GLN A CG  
171  C CD  . GLN A 23  ? 0.4224 0.3764 0.4346 -0.1059 -0.0186 0.0141  23  GLN A CD  
172  O OE1 . GLN A 23  ? 0.4239 0.3754 0.4337 -0.1053 -0.0191 0.0211  23  GLN A OE1 
173  N NE2 . GLN A 23  ? 0.4269 0.3924 0.4389 -0.1123 -0.0178 0.0115  23  GLN A NE2 
174  N N   . ALA A 24  ? 0.3876 0.3268 0.4071 -0.0722 -0.0205 0.0088  24  ALA A N   
175  C CA  . ALA A 24  ? 0.3771 0.3226 0.3943 -0.0655 -0.0203 0.0103  24  ALA A CA  
176  C C   . ALA A 24  ? 0.3707 0.3225 0.3894 -0.0633 -0.0180 0.0024  24  ALA A C   
177  O O   . ALA A 24  ? 0.3793 0.3259 0.4028 -0.0653 -0.0165 -0.0052 24  ALA A O   
178  C CB  . ALA A 24  ? 0.3811 0.3159 0.4010 -0.0610 -0.0235 0.0151  24  ALA A CB  
179  N N   . ILE A 25  ? 0.3612 0.3242 0.3762 -0.0599 -0.0173 0.0041  25  ILE A N   
180  C CA  . ILE A 25  ? 0.3571 0.3261 0.3722 -0.0580 -0.0158 -0.0016 25  ILE A CA  
181  C C   . ILE A 25  ? 0.3603 0.3188 0.3810 -0.0526 -0.0158 -0.0051 25  ILE A C   
182  O O   . ILE A 25  ? 0.3593 0.3117 0.3815 -0.0481 -0.0180 0.0003  25  ILE A O   
183  C CB  . ILE A 25  ? 0.3471 0.3286 0.3591 -0.0549 -0.0157 0.0027  25  ILE A CB  
184  C CG1 . ILE A 25  ? 0.3464 0.3393 0.3575 -0.0596 -0.0160 0.0070  25  ILE A CG1 
185  C CG2 . ILE A 25  ? 0.3471 0.3341 0.3582 -0.0536 -0.0147 -0.0021 25  ILE A CG2 
186  C CD1 . ILE A 25  ? 0.3520 0.3502 0.3620 -0.0678 -0.0165 0.0030  25  ILE A CD1 
187  N N   . ASP A 26  ? 0.3624 0.3196 0.3868 -0.0541 -0.0131 -0.0143 26  ASP A N   
188  C CA  . ASP A 26  ? 0.3660 0.3149 0.3996 -0.0490 -0.0122 -0.0189 26  ASP A CA  
189  C C   . ASP A 26  ? 0.3508 0.3077 0.3807 -0.0439 -0.0121 -0.0174 26  ASP A C   
190  O O   . ASP A 26  ? 0.3469 0.3102 0.3752 -0.0454 -0.0090 -0.0242 26  ASP A O   
191  C CB  . ASP A 26  ? 0.3796 0.3248 0.4198 -0.0535 -0.0073 -0.0314 26  ASP A CB  
192  C CG  . ASP A 26  ? 0.3882 0.3237 0.4436 -0.0479 -0.0056 -0.0368 26  ASP A CG  
193  O OD1 . ASP A 26  ? 0.3832 0.3173 0.4421 -0.0408 -0.0089 -0.0307 26  ASP A OD1 
194  O OD2 . ASP A 26  ? 0.4009 0.3305 0.4662 -0.0512 -0.0007 -0.0477 26  ASP A OD2 
195  N N   . SER A 27  ? 0.3420 0.2984 0.3696 -0.0392 -0.0153 -0.0088 27  SER A N   
196  C CA  . SER A 27  ? 0.3335 0.2971 0.3574 -0.0347 -0.0152 -0.0066 27  SER A CA  
197  C C   . SER A 27  ? 0.3334 0.2941 0.3643 -0.0306 -0.0140 -0.0123 27  SER A C   
198  O O   . SER A 27  ? 0.3274 0.2957 0.3552 -0.0294 -0.0123 -0.0145 27  SER A O   
199  C CB  . SER A 27  ? 0.3304 0.2929 0.3503 -0.0320 -0.0178 0.0022  27  SER A CB  
200  O OG  . SER A 27  ? 0.3352 0.2869 0.3597 -0.0307 -0.0212 0.0058  27  SER A OG  
201  N N   . LEU A 28  ? 0.3409 0.2910 0.3832 -0.0287 -0.0151 -0.0141 28  LEU A N   
202  C CA  . LEU A 28  ? 0.3433 0.2908 0.3968 -0.0247 -0.0135 -0.0200 28  LEU A CA  
203  C C   . LEU A 28  ? 0.3453 0.2984 0.3993 -0.0286 -0.0070 -0.0322 28  LEU A C   
204  O O   . LEU A 28  ? 0.3418 0.3002 0.3967 -0.0269 -0.0044 -0.0367 28  LEU A O   
205  C CB  . LEU A 28  ? 0.3550 0.2898 0.4252 -0.0222 -0.0164 -0.0188 28  LEU A CB  
206  C CG  . LEU A 28  ? 0.3587 0.2904 0.4465 -0.0173 -0.0150 -0.0244 28  LEU A CG  
207  C CD1 . LEU A 28  ? 0.3506 0.2890 0.4339 -0.0129 -0.0169 -0.0204 28  LEU A CD1 
208  C CD2 . LEU A 28  ? 0.3689 0.2879 0.4763 -0.0147 -0.0197 -0.0200 28  LEU A CD2 
209  N N   . ALA A 29  ? 0.3496 0.3022 0.4018 -0.0353 -0.0042 -0.0377 29  ALA A N   
210  C CA  . ALA A 29  ? 0.3553 0.3139 0.4051 -0.0420 0.0023  -0.0498 29  ALA A CA  
211  C C   . ALA A 29  ? 0.3494 0.3223 0.3827 -0.0466 0.0021  -0.0475 29  ALA A C   
212  O O   . ALA A 29  ? 0.3482 0.3282 0.3779 -0.0508 0.0063  -0.0550 29  ALA A O   
213  C CB  . ALA A 29  ? 0.3663 0.3194 0.4191 -0.0491 0.0054  -0.0568 29  ALA A CB  
214  N N   . LEU A 30  ? 0.3440 0.3214 0.3688 -0.0464 -0.0026 -0.0369 30  LEU A N   
215  C CA  . LEU A 30  ? 0.3403 0.3311 0.3535 -0.0508 -0.0039 -0.0328 30  LEU A CA  
216  C C   . LEU A 30  ? 0.3344 0.3304 0.3458 -0.0455 -0.0049 -0.0287 30  LEU A C   
217  O O   . LEU A 30  ? 0.3351 0.3405 0.3403 -0.0500 -0.0039 -0.0304 30  LEU A O   
218  C CB  . LEU A 30  ? 0.3356 0.3294 0.3450 -0.0519 -0.0079 -0.0234 30  LEU A CB  
219  C CG  . LEU A 30  ? 0.3313 0.3393 0.3336 -0.0562 -0.0105 -0.0170 30  LEU A CG  
220  C CD1 . LEU A 30  ? 0.3407 0.3572 0.3359 -0.0670 -0.0091 -0.0233 30  LEU A CD1 
221  C CD2 . LEU A 30  ? 0.3294 0.3396 0.3327 -0.0568 -0.0135 -0.0090 30  LEU A CD2 
222  N N   . LEU A 31  ? 0.3303 0.3204 0.3462 -0.0372 -0.0071 -0.0230 31  LEU A N   
223  C CA  . LEU A 31  ? 0.3247 0.3190 0.3390 -0.0324 -0.0080 -0.0188 31  LEU A CA  
224  C C   . LEU A 31  ? 0.3320 0.3251 0.3508 -0.0306 -0.0050 -0.0262 31  LEU A C   
225  O O   . LEU A 31  ? 0.3363 0.3218 0.3642 -0.0294 -0.0030 -0.0326 31  LEU A O   
226  C CB  . LEU A 31  ? 0.3196 0.3084 0.3357 -0.0262 -0.0108 -0.0111 31  LEU A CB  
227  C CG  . LEU A 31  ? 0.3166 0.3074 0.3294 -0.0276 -0.0124 -0.0041 31  LEU A CG  
228  C CD1 . LEU A 31  ? 0.3159 0.3006 0.3292 -0.0235 -0.0139 0.0012  31  LEU A CD1 
229  C CD2 . LEU A 31  ? 0.3123 0.3144 0.3220 -0.0296 -0.0126 -0.0002 31  LEU A CD2 
230  N N   . PRO A 32  ? 0.3321 0.3325 0.3465 -0.0304 -0.0046 -0.0251 32  PRO A N   
231  C CA  . PRO A 32  ? 0.3361 0.3351 0.3561 -0.0275 -0.0019 -0.0310 32  PRO A CA  
232  C C   . PRO A 32  ? 0.3313 0.3225 0.3588 -0.0193 -0.0048 -0.0264 32  PRO A C   
233  O O   . PRO A 32  ? 0.3326 0.3207 0.3575 -0.0170 -0.0082 -0.0186 32  PRO A O   
234  C CB  . PRO A 32  ? 0.3346 0.3435 0.3467 -0.0299 -0.0017 -0.0286 32  PRO A CB  
235  C CG  . PRO A 32  ? 0.3312 0.3437 0.3380 -0.0297 -0.0057 -0.0183 32  PRO A CG  
236  C CD  . PRO A 32  ? 0.3313 0.3407 0.3385 -0.0319 -0.0069 -0.0174 32  PRO A CD  
237  N N   . PRO A 33  ? 0.3339 0.3226 0.3709 -0.0159 -0.0033 -0.0312 33  PRO A N   
238  C CA  . PRO A 33  ? 0.3304 0.3137 0.3727 -0.0096 -0.0074 -0.0250 33  PRO A CA  
239  C C   . PRO A 33  ? 0.3213 0.3095 0.3538 -0.0083 -0.0090 -0.0184 33  PRO A C   
240  O O   . PRO A 33  ? 0.3188 0.3144 0.3444 -0.0111 -0.0068 -0.0193 33  PRO A O   
241  C CB  . PRO A 33  ? 0.3317 0.3140 0.3881 -0.0069 -0.0053 -0.0319 33  PRO A CB  
242  C CG  . PRO A 33  ? 0.3407 0.3260 0.4001 -0.0120 0.0012  -0.0433 33  PRO A CG  
243  C CD  . PRO A 33  ? 0.3391 0.3309 0.3821 -0.0185 0.0022  -0.0421 33  PRO A CD  
244  N N   . PRO A 34  ? 0.3146 0.2985 0.3466 -0.0050 -0.0128 -0.0117 34  PRO A N   
245  C CA  . PRO A 34  ? 0.3086 0.2962 0.3331 -0.0041 -0.0129 -0.0074 34  PRO A CA  
246  C C   . PRO A 34  ? 0.3036 0.2954 0.3309 -0.0027 -0.0113 -0.0110 34  PRO A C   
247  O O   . PRO A 34  ? 0.3030 0.2940 0.3397 -0.0016 -0.0107 -0.0161 34  PRO A O   
248  C CB  . PRO A 34  ? 0.3121 0.2939 0.3352 -0.0030 -0.0166 -0.0012 34  PRO A CB  
249  C CG  . PRO A 34  ? 0.3173 0.2931 0.3506 -0.0019 -0.0200 -0.0017 34  PRO A CG  
250  C CD  . PRO A 34  ? 0.3205 0.2964 0.3593 -0.0031 -0.0171 -0.0079 34  PRO A CD  
251  N N   . PRO A 35  ? 0.3003 0.2964 0.3213 -0.0029 -0.0101 -0.0086 35  PRO A N   
252  C CA  . PRO A 35  ? 0.2975 0.2973 0.3204 -0.0021 -0.0088 -0.0114 35  PRO A CA  
253  C C   . PRO A 35  ? 0.2988 0.2951 0.3292 0.0008  -0.0115 -0.0115 35  PRO A C   
254  O O   . PRO A 35  ? 0.3014 0.2931 0.3302 0.0016  -0.0150 -0.0064 35  PRO A O   
255  C CB  . PRO A 35  ? 0.2953 0.2974 0.3112 -0.0024 -0.0082 -0.0067 35  PRO A CB  
256  C CG  . PRO A 35  ? 0.2960 0.2989 0.3085 -0.0042 -0.0079 -0.0032 35  PRO A CG  
257  C CD  . PRO A 35  ? 0.2977 0.2955 0.3120 -0.0039 -0.0096 -0.0035 35  PRO A CD  
258  N N   . ALA A 36  ? 0.2959 0.2952 0.3350 0.0016  -0.0099 -0.0171 36  ALA A N   
259  C CA  . ALA A 36  ? 0.2960 0.2938 0.3455 0.0044  -0.0131 -0.0166 36  ALA A CA  
260  C C   . ALA A 36  ? 0.2909 0.2918 0.3349 0.0044  -0.0135 -0.0141 36  ALA A C   
261  O O   . ALA A 36  ? 0.2830 0.2882 0.3198 0.0025  -0.0099 -0.0157 36  ALA A O   
262  C CB  . ALA A 36  ? 0.2995 0.2998 0.3646 0.0054  -0.0101 -0.0247 36  ALA A CB  
263  N N   . VAL A 37  ? 0.2892 0.2881 0.3368 0.0055  -0.0184 -0.0098 37  VAL A N   
264  C CA  . VAL A 37  ? 0.2867 0.2888 0.3309 0.0047  -0.0188 -0.0087 37  VAL A CA  
265  C C   . VAL A 37  ? 0.2798 0.2884 0.3321 0.0053  -0.0148 -0.0154 37  VAL A C   
266  O O   . VAL A 37  ? 0.2813 0.2915 0.3481 0.0070  -0.0141 -0.0200 37  VAL A O   
267  C CB  . VAL A 37  ? 0.2924 0.2927 0.3408 0.0044  -0.0257 -0.0030 37  VAL A CB  
268  C CG1 . VAL A 37  ? 0.2932 0.2979 0.3396 0.0029  -0.0259 -0.0031 37  VAL A CG1 
269  C CG2 . VAL A 37  ? 0.2993 0.2940 0.3362 0.0014  -0.0289 0.0033  37  VAL A CG2 
270  N N   . GLY A 38  ? 0.2716 0.2838 0.3157 0.0033  -0.0115 -0.0164 38  GLY A N   
271  C CA  . GLY A 38  ? 0.2701 0.2891 0.3188 0.0021  -0.0070 -0.0227 38  GLY A CA  
272  C C   . GLY A 38  ? 0.2677 0.2896 0.3093 -0.0011 -0.0022 -0.0259 38  GLY A C   
273  O O   . GLY A 38  ? 0.2724 0.3005 0.3141 -0.0043 0.0018  -0.0306 38  GLY A O   
274  N N   . SER A 39  ? 0.2625 0.2807 0.2976 -0.0015 -0.0028 -0.0230 39  SER A N   
275  C CA  . SER A 39  ? 0.2629 0.2846 0.2903 -0.0058 0.0000  -0.0239 39  SER A CA  
276  C C   . SER A 39  ? 0.2602 0.2820 0.2782 -0.0073 -0.0006 -0.0172 39  SER A C   
277  O O   . SER A 39  ? 0.2543 0.2714 0.2709 -0.0046 -0.0025 -0.0125 39  SER A O   
278  C CB  . SER A 39  ? 0.2637 0.2823 0.2908 -0.0060 -0.0005 -0.0240 39  SER A CB  
279  O OG  . SER A 39  ? 0.2584 0.2713 0.2813 -0.0036 -0.0039 -0.0170 39  SER A OG  
280  N N   . ILE A 40  ? 0.2609 0.2883 0.2735 -0.0124 0.0010  -0.0166 40  ILE A N   
281  C CA  . ILE A 40  ? 0.2629 0.2903 0.2704 -0.0138 -0.0003 -0.0088 40  ILE A CA  
282  C C   . ILE A 40  ? 0.2601 0.2829 0.2677 -0.0112 -0.0023 -0.0038 40  ILE A C   
283  O O   . ILE A 40  ? 0.2533 0.2728 0.2620 -0.0092 -0.0028 0.0014  40  ILE A O   
284  C CB  . ILE A 40  ? 0.2700 0.3051 0.2719 -0.0213 0.0001  -0.0070 40  ILE A CB  
285  C CG1 . ILE A 40  ? 0.2763 0.3172 0.2770 -0.0257 0.0033  -0.0133 40  ILE A CG1 
286  C CG2 . ILE A 40  ? 0.2702 0.3048 0.2714 -0.0221 -0.0024 0.0028  40  ILE A CG2 
287  C CD1 . ILE A 40  ? 0.2763 0.3151 0.2805 -0.0226 0.0038  -0.0132 40  ILE A CD1 
288  N N   . ALA A 41  ? 0.2612 0.2839 0.2690 -0.0117 -0.0027 -0.0062 41  ALA A N   
289  C CA  . ALA A 41  ? 0.2606 0.2798 0.2688 -0.0098 -0.0043 -0.0020 41  ALA A CA  
290  C C   . ALA A 41  ? 0.2585 0.2706 0.2686 -0.0051 -0.0045 -0.0007 41  ALA A C   
291  O O   . ALA A 41  ? 0.2604 0.2702 0.2712 -0.0041 -0.0042 0.0036  41  ALA A O   
292  C CB  . ALA A 41  ? 0.2655 0.2851 0.2736 -0.0116 -0.0044 -0.0058 41  ALA A CB  
293  N N   . PHE A 42  ? 0.2567 0.2659 0.2685 -0.0031 -0.0050 -0.0044 42  PHE A N   
294  C CA  . PHE A 42  ? 0.2588 0.2624 0.2698 -0.0011 -0.0059 -0.0026 42  PHE A CA  
295  C C   . PHE A 42  ? 0.2570 0.2600 0.2663 -0.0013 -0.0040 -0.0009 42  PHE A C   
296  O O   . PHE A 42  ? 0.2597 0.2587 0.2671 -0.0014 -0.0027 0.0006  42  PHE A O   
297  C CB  . PHE A 42  ? 0.2596 0.2612 0.2743 0.0001  -0.0085 -0.0050 42  PHE A CB  
298  C CG  . PHE A 42  ? 0.2646 0.2615 0.2759 -0.0001 -0.0106 -0.0021 42  PHE A CG  
299  C CD1 . PHE A 42  ? 0.2670 0.2599 0.2739 -0.0013 -0.0108 0.0006  42  PHE A CD1 
300  C CD2 . PHE A 42  ? 0.2662 0.2634 0.2775 -0.0007 -0.0120 -0.0022 42  PHE A CD2 
301  C CE1 . PHE A 42  ? 0.2742 0.2635 0.2754 -0.0039 -0.0120 0.0028  42  PHE A CE1 
302  C CE2 . PHE A 42  ? 0.2709 0.2646 0.2766 -0.0034 -0.0141 0.0004  42  PHE A CE2 
303  C CZ  . PHE A 42  ? 0.2773 0.2670 0.2771 -0.0055 -0.0139 0.0028  42  PHE A CZ  
304  N N   . LEU A 43  ? 0.2575 0.2643 0.2676 -0.0023 -0.0031 -0.0020 43  LEU A N   
305  C CA  . LEU A 43  ? 0.2600 0.2657 0.2697 -0.0029 -0.0010 -0.0002 43  LEU A CA  
306  C C   . LEU A 43  ? 0.2632 0.2672 0.2753 -0.0028 0.0007  0.0041  43  LEU A C   
307  O O   . LEU A 43  ? 0.2660 0.2657 0.2797 -0.0025 0.0035  0.0046  43  LEU A O   
308  C CB  . LEU A 43  ? 0.2590 0.2697 0.2692 -0.0049 -0.0006 -0.0013 43  LEU A CB  
309  C CG  . LEU A 43  ? 0.2606 0.2696 0.2712 -0.0060 0.0012  0.0005  43  LEU A CG  
310  C CD1 . LEU A 43  ? 0.2623 0.2669 0.2715 -0.0055 0.0019  -0.0021 43  LEU A CD1 
311  C CD2 . LEU A 43  ? 0.2602 0.2753 0.2705 -0.0091 0.0012  0.0000  43  LEU A CD2 
312  N N   . ASN A 44  ? 0.2668 0.2745 0.2806 -0.0035 -0.0006 0.0070  44  ASN A N   
313  C CA  . ASN A 44  ? 0.2696 0.2771 0.2893 -0.0030 0.0001  0.0122  44  ASN A CA  
314  C C   . ASN A 44  ? 0.2655 0.2682 0.2861 -0.0013 0.0023  0.0108  44  ASN A C   
315  O O   . ASN A 44  ? 0.2624 0.2625 0.2896 -0.0005 0.0058  0.0123  44  ASN A O   
316  C CB  . ASN A 44  ? 0.2745 0.2886 0.2952 -0.0056 -0.0029 0.0164  44  ASN A CB  
317  C CG  . ASN A 44  ? 0.2801 0.2956 0.3109 -0.0052 -0.0033 0.0237  44  ASN A CG  
318  O OD1 . ASN A 44  ? 0.3007 0.3182 0.3342 -0.0053 -0.0044 0.0257  44  ASN A OD1 
319  N ND2 . ASN A 44  ? 0.2795 0.2937 0.3179 -0.0046 -0.0022 0.0276  44  ASN A ND2 
320  N N   . ASP A 45  ? 0.2653 0.2668 0.2804 -0.0013 0.0008  0.0079  45  ASP A N   
321  C CA  . ASP A 45  ? 0.2681 0.2651 0.2812 -0.0014 0.0026  0.0067  45  ASP A CA  
322  C C   . ASP A 45  ? 0.2710 0.2635 0.2822 -0.0024 0.0063  0.0042  45  ASP A C   
323  O O   . ASP A 45  ? 0.2766 0.2664 0.2894 -0.0036 0.0108  0.0032  45  ASP A O   
324  C CB  . ASP A 45  ? 0.2710 0.2664 0.2787 -0.0019 -0.0008 0.0050  45  ASP A CB  
325  C CG  . ASP A 45  ? 0.2721 0.2697 0.2814 -0.0021 -0.0026 0.0063  45  ASP A CG  
326  O OD1 . ASP A 45  ? 0.2737 0.2742 0.2873 -0.0023 -0.0013 0.0091  45  ASP A OD1 
327  O OD2 . ASP A 45  ? 0.2759 0.2722 0.2835 -0.0022 -0.0054 0.0046  45  ASP A OD2 
328  N N   . GLN A 46  ? 0.2672 0.2594 0.2752 -0.0029 0.0052  0.0024  46  GLN A N   
329  C CA  . GLN A 46  ? 0.2713 0.2597 0.2761 -0.0052 0.0086  -0.0004 46  GLN A CA  
330  C C   . GLN A 46  ? 0.2726 0.2593 0.2856 -0.0047 0.0142  -0.0003 46  GLN A C   
331  O O   . GLN A 46  ? 0.2777 0.2603 0.2909 -0.0071 0.0199  -0.0038 46  GLN A O   
332  C CB  . GLN A 46  ? 0.2714 0.2608 0.2722 -0.0061 0.0053  -0.0018 46  GLN A CB  
333  C CG  . GLN A 46  ? 0.2723 0.2625 0.2691 -0.0066 -0.0001 -0.0015 46  GLN A CG  
334  C CD  . GLN A 46  ? 0.2742 0.2660 0.2698 -0.0078 -0.0034 -0.0025 46  GLN A CD  
335  O OE1 . GLN A 46  ? 0.2862 0.2763 0.2761 -0.0117 -0.0052 -0.0023 46  GLN A OE1 
336  N NE2 . GLN A 46  ? 0.2662 0.2622 0.2671 -0.0056 -0.0041 -0.0033 46  GLN A NE2 
337  N N   . ALA A 47  ? 0.2680 0.2580 0.2886 -0.0025 0.0127  0.0035  47  ALA A N   
338  C CA  . ALA A 47  ? 0.2708 0.2594 0.3035 -0.0015 0.0167  0.0058  47  ALA A CA  
339  C C   . ALA A 47  ? 0.2732 0.2603 0.3148 -0.0007 0.0212  0.0058  47  ALA A C   
340  O O   . ALA A 47  ? 0.2699 0.2528 0.3204 -0.0010 0.0279  0.0031  47  ALA A O   
341  C CB  . ALA A 47  ? 0.2688 0.2624 0.3073 -0.0006 0.0124  0.0125  47  ALA A CB  
342  N N   . MET A 48  ? 0.2737 0.2644 0.3140 0.0000  0.0182  0.0080  48  MET A N   
343  C CA  . MET A 48  ? 0.2792 0.2699 0.3284 0.0003  0.0224  0.0080  48  MET A CA  
344  C C   . MET A 48  ? 0.2798 0.2654 0.3218 -0.0030 0.0289  0.0005  48  MET A C   
345  O O   . MET A 48  ? 0.2808 0.2648 0.3328 -0.0037 0.0364  -0.0025 48  MET A O   
346  C CB  . MET A 48  ? 0.2846 0.2805 0.3324 0.0008  0.0173  0.0121  48  MET A CB  
347  C CG  . MET A 48  ? 0.2903 0.2926 0.3436 0.0017  0.0111  0.0194  48  MET A CG  
348  S SD  . MET A 48  ? 0.3116 0.3161 0.3870 0.0036  0.0120  0.0269  48  MET A SD  
349  C CE  . MET A 48  ? 0.3146 0.3156 0.3868 0.0031  0.0120  0.0263  48  MET A CE  
350  N N   . TYR A 49  ? 0.2772 0.2610 0.3031 -0.0060 0.0261  -0.0022 49  TYR A N   
351  C CA  . TYR A 49  ? 0.2869 0.2668 0.3028 -0.0117 0.0309  -0.0082 49  TYR A CA  
352  C C   . TYR A 49  ? 0.2968 0.2725 0.3175 -0.0140 0.0391  -0.0139 49  TYR A C   
353  O O   . TYR A 49  ? 0.3021 0.2752 0.3242 -0.0182 0.0477  -0.0200 49  TYR A O   
354  C CB  . TYR A 49  ? 0.2867 0.2662 0.2868 -0.0147 0.0243  -0.0078 49  TYR A CB  
355  C CG  . TYR A 49  ? 0.2994 0.2758 0.2872 -0.0228 0.0278  -0.0127 49  TYR A CG  
356  C CD1 . TYR A 49  ? 0.3054 0.2812 0.2850 -0.0283 0.0291  -0.0135 49  TYR A CD1 
357  C CD2 . TYR A 49  ? 0.3034 0.2778 0.2863 -0.0263 0.0296  -0.0163 49  TYR A CD2 
358  C CE1 . TYR A 49  ? 0.3209 0.2948 0.2866 -0.0381 0.0321  -0.0175 49  TYR A CE1 
359  C CE2 . TYR A 49  ? 0.3170 0.2894 0.2866 -0.0358 0.0325  -0.0207 49  TYR A CE2 
360  C CZ  . TYR A 49  ? 0.3243 0.2967 0.2848 -0.0421 0.0336  -0.0212 49  TYR A CZ  
361  O OH  . TYR A 49  ? 0.3426 0.3140 0.2874 -0.0538 0.0361  -0.0251 49  TYR A OH  
362  N N   . GLU A 50  ? 0.2974 0.2725 0.3206 -0.0120 0.0370  -0.0127 50  GLU A N   
363  C CA  . GLU A 50  ? 0.3081 0.2783 0.3363 -0.0143 0.0446  -0.0182 50  GLU A CA  
364  C C   . GLU A 50  ? 0.3118 0.2802 0.3616 -0.0113 0.0523  -0.0189 50  GLU A C   
365  O O   . GLU A 50  ? 0.3122 0.2760 0.3674 -0.0149 0.0625  -0.0268 50  GLU A O   
366  C CB  . GLU A 50  ? 0.3068 0.2770 0.3336 -0.0131 0.0401  -0.0159 50  GLU A CB  
367  C CG  . GLU A 50  ? 0.3099 0.2822 0.3197 -0.0161 0.0333  -0.0159 50  GLU A CG  
368  C CD  . GLU A 50  ? 0.3257 0.2952 0.3221 -0.0243 0.0368  -0.0224 50  GLU A CD  
369  O OE1 . GLU A 50  ? 0.3326 0.2979 0.3309 -0.0287 0.0461  -0.0289 50  GLU A OE1 
370  O OE2 . GLU A 50  ? 0.3366 0.3085 0.3212 -0.0272 0.0301  -0.0209 50  GLU A OE2 
371  N N   . GLN A 51  ? 0.3079 0.2805 0.3711 -0.0053 0.0475  -0.0107 51  GLN A N   
372  C CA  A GLN A 51  ? 0.3138 0.2863 0.4015 -0.0017 0.0525  -0.0086 51  GLN A CA  
373  C CA  B GLN A 51  ? 0.3102 0.2824 0.3981 -0.0019 0.0530  -0.0090 51  GLN A CA  
374  C C   . GLN A 51  ? 0.3169 0.2889 0.4081 -0.0045 0.0614  -0.0157 51  GLN A C   
375  O O   . GLN A 51  ? 0.3189 0.2872 0.4267 -0.0051 0.0719  -0.0218 51  GLN A O   
376  C CB  A GLN A 51  ? 0.3122 0.2917 0.4085 0.0028  0.0433  0.0028  51  GLN A CB  
377  C CB  B GLN A 51  ? 0.3039 0.2824 0.4036 0.0030  0.0445  0.0026  51  GLN A CB  
378  C CG  A GLN A 51  ? 0.3199 0.3004 0.4436 0.0068  0.0438  0.0099  51  GLN A CG  
379  C CG  B GLN A 51  ? 0.3071 0.2863 0.4364 0.0067  0.0486  0.0065  51  GLN A CG  
380  C CD  A GLN A 51  ? 0.3185 0.3070 0.4448 0.0087  0.0326  0.0223  51  GLN A CD  
381  C CD  B GLN A 51  ? 0.3148 0.2868 0.4604 0.0073  0.0554  0.0037  51  GLN A CD  
382  O OE1 A GLN A 51  ? 0.3209 0.3153 0.4480 0.0091  0.0294  0.0256  51  GLN A OE1 
383  O OE1 B GLN A 51  ? 0.3155 0.2868 0.4646 0.0085  0.0500  0.0104  51  GLN A OE1 
384  N NE2 A GLN A 51  ? 0.3227 0.3120 0.4491 0.0085  0.0268  0.0290  51  GLN A NE2 
385  N NE2 B GLN A 51  ? 0.3225 0.2891 0.4782 0.0057  0.0679  -0.0067 51  GLN A NE2 
386  N N   . GLY A 52  ? 0.3133 0.2888 0.3895 -0.0065 0.0574  -0.0151 52  GLY A N   
387  C CA  . GLY A 52  ? 0.3224 0.2983 0.3977 -0.0106 0.0649  -0.0213 52  GLY A CA  
388  C C   . GLY A 52  ? 0.3345 0.3048 0.4019 -0.0183 0.0758  -0.0330 52  GLY A C   
389  O O   . GLY A 52  ? 0.3408 0.3098 0.4204 -0.0210 0.0874  -0.0407 52  GLY A O   
390  N N   . ARG A 53  ? 0.3408 0.3084 0.3886 -0.0227 0.0723  -0.0348 53  ARG A N   
391  C CA  . ARG A 53  ? 0.3588 0.3218 0.3945 -0.0323 0.0810  -0.0455 53  ARG A CA  
392  C C   . ARG A 53  ? 0.3655 0.3235 0.4216 -0.0321 0.0937  -0.0536 53  ARG A C   
393  O O   . ARG A 53  ? 0.3692 0.3246 0.4259 -0.0397 0.1065  -0.0650 53  ARG A O   
394  C CB  . ARG A 53  ? 0.3651 0.3274 0.3804 -0.0358 0.0728  -0.0435 53  ARG A CB  
395  C CG  . ARG A 53  ? 0.3866 0.3465 0.3824 -0.0485 0.0782  -0.0523 53  ARG A CG  
396  C CD  . ARG A 53  ? 0.3877 0.3492 0.3646 -0.0515 0.0668  -0.0472 53  ARG A CD  
397  N NE  . ARG A 53  ? 0.3824 0.3426 0.3670 -0.0457 0.0635  -0.0448 53  ARG A NE  
398  C CZ  . ARG A 53  ? 0.3901 0.3461 0.3754 -0.0500 0.0699  -0.0515 53  ARG A CZ  
399  N NH1 . ARG A 53  ? 0.3837 0.3390 0.3761 -0.0446 0.0658  -0.0480 53  ARG A NH1 
400  N NH2 . ARG A 53  ? 0.4059 0.3586 0.3842 -0.0606 0.0807  -0.0623 53  ARG A NH2 
401  N N   . LEU A 54  ? 0.3598 0.3163 0.4337 -0.0242 0.0906  -0.0480 54  LEU A N   
402  C CA  . LEU A 54  ? 0.3696 0.3204 0.4678 -0.0228 0.1017  -0.0540 54  LEU A CA  
403  C C   . LEU A 54  ? 0.3704 0.3226 0.4960 -0.0193 0.1106  -0.0563 54  LEU A C   
404  O O   . LEU A 54  ? 0.3825 0.3296 0.5288 -0.0202 0.1234  -0.0651 54  LEU A O   
405  C CB  . LEU A 54  ? 0.3646 0.3136 0.4752 -0.0158 0.0946  -0.0452 54  LEU A CB  
406  C CG  . LEU A 54  ? 0.3666 0.3141 0.4559 -0.0189 0.0876  -0.0440 54  LEU A CG  
407  C CD1 . LEU A 54  ? 0.3648 0.3091 0.4704 -0.0137 0.0847  -0.0378 54  LEU A CD1 
408  C CD2 . LEU A 54  ? 0.3811 0.3243 0.4521 -0.0296 0.0957  -0.0566 54  LEU A CD2 
409  N N   . LEU A 55  ? 0.3630 0.3222 0.4903 -0.0155 0.1044  -0.0488 55  LEU A N   
410  C CA  . LEU A 55  ? 0.3655 0.3278 0.5186 -0.0127 0.1122  -0.0505 55  LEU A CA  
411  C C   . LEU A 55  ? 0.3764 0.3389 0.5202 -0.0221 0.1249  -0.0639 55  LEU A C   
412  O O   . LEU A 55  ? 0.3769 0.3416 0.5438 -0.0212 0.1349  -0.0687 55  LEU A O   
413  C CB  . LEU A 55  ? 0.3563 0.3269 0.5151 -0.0060 0.1001  -0.0369 55  LEU A CB  
414  C CG  . LEU A 55  ? 0.3515 0.3242 0.5283 0.0023  0.0895  -0.0230 55  LEU A CG  
415  C CD1 . LEU A 55  ? 0.3433 0.3248 0.5158 0.0055  0.0771  -0.0113 55  LEU A CD1 
416  C CD2 . LEU A 55  ? 0.3570 0.3279 0.5733 0.0072  0.0971  -0.0226 55  LEU A CD2 
417  N N   . ARG A 56  ? 0.4308 0.3479 0.5189 -0.0562 0.0466  -0.0764 56  ARG A N   
418  C CA  . ARG A 56  ? 0.4369 0.3622 0.5071 -0.0590 0.0433  -0.0878 56  ARG A CA  
419  C C   . ARG A 56  ? 0.4638 0.3798 0.5386 -0.0603 0.0518  -0.1032 56  ARG A C   
420  O O   . ARG A 56  ? 0.4637 0.3849 0.5258 -0.0585 0.0532  -0.1084 56  ARG A O   
421  C CB  . ARG A 56  ? 0.4292 0.3669 0.4883 -0.0673 0.0330  -0.0942 56  ARG A CB  
422  C CG  . ARG A 56  ? 0.4066 0.3554 0.4572 -0.0646 0.0244  -0.0802 56  ARG A CG  
423  C CD  . ARG A 56  ? 0.4032 0.3644 0.4468 -0.0718 0.0143  -0.0850 56  ARG A CD  
424  N NE  . ARG A 56  ? 0.3833 0.3526 0.4238 -0.0684 0.0073  -0.0716 56  ARG A NE  
425  C CZ  . ARG A 56  ? 0.3784 0.3599 0.4137 -0.0720 -0.0022 -0.0714 56  ARG A CZ  
426  N NH1 . ARG A 56  ? 0.3903 0.3794 0.4209 -0.0796 -0.0072 -0.0834 56  ARG A NH1 
427  N NH2 . ARG A 56  ? 0.3643 0.3512 0.3992 -0.0677 -0.0069 -0.0596 56  ARG A NH2 
428  N N   . ASN A 57  ? 0.4879 0.3901 0.5819 -0.0636 0.0582  -0.1105 57  ASN A N   
429  C CA  . ASN A 57  ? 0.5209 0.4112 0.6232 -0.0646 0.0677  -0.1265 57  ASN A CA  
430  C C   . ASN A 57  ? 0.5218 0.3973 0.6418 -0.0545 0.0787  -0.1180 57  ASN A C   
431  O O   . ASN A 57  ? 0.5509 0.4100 0.6895 -0.0552 0.0877  -0.1267 57  ASN A O   
432  C CB  . ASN A 57  ? 0.5498 0.4331 0.6637 -0.0754 0.0684  -0.1427 57  ASN A CB  
433  C CG  . ASN A 57  ? 0.5751 0.4692 0.6723 -0.0842 0.0640  -0.1631 57  ASN A CG  
434  O OD1 . ASN A 57  ? 0.5848 0.4968 0.6611 -0.0864 0.0542  -0.1609 57  ASN A OD1 
435  N ND2 . ASN A 57  ? 0.6058 0.4894 0.7121 -0.0891 0.0715  -0.1829 57  ASN A ND2 
436  N N   . THR A 58  ? 0.4978 0.3793 0.6130 -0.0453 0.0777  -0.1011 58  THR A N   
437  C CA  . THR A 58  ? 0.4947 0.3668 0.6242 -0.0347 0.0866  -0.0916 58  THR A CA  
438  C C   . THR A 58  ? 0.4866 0.3709 0.6017 -0.0287 0.0861  -0.0897 58  THR A C   
439  O O   . THR A 58  ? 0.4735 0.3718 0.5678 -0.0331 0.0790  -0.0939 58  THR A O   
440  C CB  . THR A 58  ? 0.4797 0.3502 0.6193 -0.0290 0.0856  -0.0700 58  THR A CB  
441  O OG1 . THR A 58  ? 0.4560 0.3433 0.5778 -0.0276 0.0764  -0.0589 58  THR A OG1 
442  C CG2 . THR A 58  ? 0.4842 0.3453 0.6375 -0.0357 0.0858  -0.0698 58  THR A CG2 
443  N N   . GLU A 59  ? 0.4910 0.3706 0.6180 -0.0187 0.0937  -0.0823 59  GLU A N   
444  C CA  . GLU A 59  ? 0.4866 0.3792 0.6031 -0.0126 0.0936  -0.0785 59  GLU A CA  
445  C C   . GLU A 59  ? 0.4517 0.3598 0.5520 -0.0127 0.0831  -0.0643 59  GLU A C   
446  O O   . GLU A 59  ? 0.4403 0.3614 0.5234 -0.0143 0.0790  -0.0663 59  GLU A O   
447  C CB  . GLU A 59  ? 0.5079 0.3942 0.6439 -0.0009 0.1027  -0.0702 59  GLU A CB  
448  C CG  . GLU A 59  ? 0.5223 0.4212 0.6518 0.0046  0.1052  -0.0713 59  GLU A CG  
449  C CD  . GLU A 59  ? 0.5508 0.4508 0.6718 -0.0003 0.1101  -0.0927 59  GLU A CD  
450  O OE1 . GLU A 59  ? 0.5842 0.4709 0.7121 -0.0052 0.1149  -0.1081 59  GLU A OE1 
451  O OE2 . GLU A 59  ? 0.5627 0.4776 0.6702 0.0001  0.1094  -0.0945 59  GLU A OE2 
452  N N   . ARG A 60  ? 0.4281 0.3344 0.5342 -0.0114 0.0794  -0.0505 60  ARG A N   
453  C CA  . ARG A 60  ? 0.4020 0.3215 0.4941 -0.0118 0.0700  -0.0388 60  ARG A CA  
454  C C   . ARG A 60  ? 0.3908 0.3176 0.4649 -0.0210 0.0618  -0.0474 60  ARG A C   
455  O O   . ARG A 60  ? 0.3771 0.3158 0.4361 -0.0216 0.0552  -0.0429 60  ARG A O   
456  C CB  . ARG A 60  ? 0.3930 0.3098 0.4949 -0.0090 0.0687  -0.0238 60  ARG A CB  
457  C CG  . ARG A 60  ? 0.3762 0.3063 0.4647 -0.0091 0.0598  -0.0132 60  ARG A CG  
458  C CD  . ARG A 60  ? 0.3669 0.3087 0.4481 -0.0034 0.0582  -0.0067 60  ARG A CD  
459  N NE  . ARG A 60  ? 0.3529 0.3065 0.4210 -0.0046 0.0499  0.0006  60  ARG A NE  
460  C CZ  . ARG A 60  ? 0.3471 0.3078 0.3995 -0.0096 0.0435  -0.0045 60  ARG A CZ  
461  N NH1 . ARG A 60  ? 0.3528 0.3122 0.3981 -0.0146 0.0438  -0.0164 60  ARG A NH1 
462  N NH2 . ARG A 60  ? 0.3400 0.3093 0.3838 -0.0098 0.0369  0.0025  60  ARG A NH2 
463  N N   . GLY A 61  ? 0.3975 0.3173 0.4744 -0.0282 0.0622  -0.0594 61  GLY A N   
464  C CA  . GLY A 61  ? 0.3977 0.3255 0.4586 -0.0369 0.0543  -0.0684 61  GLY A CA  
465  C C   . GLY A 61  ? 0.4012 0.3380 0.4457 -0.0387 0.0539  -0.0774 61  GLY A C   
466  O O   . GLY A 61  ? 0.3902 0.3382 0.4178 -0.0423 0.0460  -0.0761 61  GLY A O   
467  N N   . LYS A 62  ? 0.4167 0.3484 0.4668 -0.0359 0.0629  -0.0861 62  LYS A N   
468  C CA  . LYS A 62  ? 0.4261 0.3675 0.4613 -0.0370 0.0645  -0.0941 62  LYS A CA  
469  C C   . LYS A 62  ? 0.4076 0.3607 0.4328 -0.0327 0.0604  -0.0802 62  LYS A C   
470  O O   . LYS A 62  ? 0.4024 0.3668 0.4095 -0.0369 0.0553  -0.0810 62  LYS A O   
471  C CB  . LYS A 62  ? 0.4481 0.3818 0.4948 -0.0330 0.0765  -0.1051 62  LYS A CB  
472  C CG  . LYS A 62  ? 0.4635 0.4082 0.4954 -0.0344 0.0799  -0.1150 62  LYS A CG  
473  C CD  . LYS A 62  ? 0.4870 0.4232 0.5326 -0.0305 0.0927  -0.1285 62  LYS A CD  
474  C CE  . LYS A 62  ? 0.5023 0.4512 0.5333 -0.0316 0.0975  -0.1390 62  LYS A CE  
475  N NZ  . LYS A 62  ? 0.4925 0.4540 0.5185 -0.0261 0.0967  -0.1246 62  LYS A NZ  
476  N N   . LEU A 63  ? 0.3954 0.3462 0.4326 -0.0249 0.0625  -0.0672 63  LEU A N   
477  C CA  . LEU A 63  ? 0.3804 0.3421 0.4103 -0.0216 0.0581  -0.0544 63  LEU A CA  
478  C C   . LEU A 63  ? 0.3653 0.3328 0.3820 -0.0266 0.0474  -0.0484 63  LEU A C   
479  O O   . LEU A 63  ? 0.3577 0.3349 0.3614 -0.0282 0.0430  -0.0445 63  LEU A O   
480  C CB  . LEU A 63  ? 0.3756 0.3352 0.4211 -0.0127 0.0611  -0.0416 63  LEU A CB  
481  C CG  . LEU A 63  ? 0.3658 0.3376 0.4053 -0.0099 0.0560  -0.0291 63  LEU A CG  
482  C CD1 . LEU A 63  ? 0.3702 0.3526 0.4010 -0.0105 0.0581  -0.0326 63  LEU A CD1 
483  C CD2 . LEU A 63  ? 0.3644 0.3361 0.4188 -0.0015 0.0581  -0.0167 63  LEU A CD2 
484  N N   . ALA A 64  ? 0.3589 0.3203 0.3804 -0.0290 0.0437  -0.0476 64  ALA A N   
485  C CA  . ALA A 64  ? 0.3498 0.3165 0.3616 -0.0329 0.0341  -0.0425 64  ALA A CA  
486  C C   . ALA A 64  ? 0.3546 0.3287 0.3493 -0.0396 0.0289  -0.0497 64  ALA A C   
487  O O   . ALA A 64  ? 0.3470 0.3283 0.3306 -0.0407 0.0224  -0.0431 64  ALA A O   
488  C CB  . ALA A 64  ? 0.3479 0.3080 0.3699 -0.0345 0.0323  -0.0416 64  ALA A CB  
489  N N   . ALA A 65  ? 0.3723 0.3447 0.3651 -0.0441 0.0319  -0.0631 65  ALA A N   
490  C CA  . ALA A 65  ? 0.3869 0.3685 0.3620 -0.0506 0.0273  -0.0702 65  ALA A CA  
491  C C   . ALA A 65  ? 0.3903 0.3806 0.3528 -0.0494 0.0287  -0.0663 65  ALA A C   
492  O O   . ALA A 65  ? 0.3913 0.3903 0.3390 -0.0528 0.0221  -0.0620 65  ALA A O   
493  C CB  . ALA A 65  ? 0.4042 0.3832 0.3799 -0.0557 0.0316  -0.0873 65  ALA A CB  
494  N N   . GLU A 66  ? 0.3962 0.3844 0.3660 -0.0444 0.0375  -0.0668 66  GLU A N   
495  C CA  . GLU A 66  ? 0.3993 0.3966 0.3605 -0.0431 0.0400  -0.0627 66  GLU A CA  
496  C C   . GLU A 66  ? 0.3848 0.3859 0.3436 -0.0414 0.0335  -0.0478 66  GLU A C   
497  O O   . GLU A 66  ? 0.3844 0.3935 0.3303 -0.0446 0.0302  -0.0434 66  GLU A O   
498  C CB  . GLU A 66  ? 0.4063 0.4014 0.3800 -0.0371 0.0509  -0.0663 66  GLU A CB  
499  C CG  . GLU A 66  ? 0.4297 0.4218 0.4045 -0.0391 0.0587  -0.0831 66  GLU A CG  
500  C CD  . GLU A 66  ? 0.4382 0.4241 0.4312 -0.0316 0.0698  -0.0868 66  GLU A CD  
501  O OE1 . GLU A 66  ? 0.4591 0.4418 0.4544 -0.0326 0.0775  -0.1018 66  GLU A OE1 
502  O OE2 . GLU A 66  ? 0.4316 0.4165 0.4371 -0.0246 0.0709  -0.0753 66  GLU A OE2 
503  N N   . ASP A 67  ? 0.3736 0.3688 0.3449 -0.0369 0.0318  -0.0403 67  ASP A N   
504  C CA  . ASP A 67  ? 0.3635 0.3614 0.3331 -0.0356 0.0255  -0.0283 67  ASP A CA  
505  C C   . ASP A 67  ? 0.3650 0.3648 0.3229 -0.0408 0.0165  -0.0261 67  ASP A C   
506  O O   . ASP A 67  ? 0.3564 0.3604 0.3072 -0.0420 0.0122  -0.0188 67  ASP A O   
507  C CB  . ASP A 67  ? 0.3542 0.3466 0.3379 -0.0303 0.0254  -0.0221 67  ASP A CB  
508  C CG  . ASP A 67  ? 0.3555 0.3493 0.3506 -0.0240 0.0321  -0.0187 67  ASP A CG  
509  O OD1 . ASP A 67  ? 0.3636 0.3632 0.3571 -0.0234 0.0368  -0.0210 67  ASP A OD1 
510  O OD2 . ASP A 67  ? 0.3457 0.3363 0.3519 -0.0193 0.0327  -0.0129 67  ASP A OD2 
511  N N   . ALA A 68  ? 0.3698 0.3666 0.3274 -0.0437 0.0137  -0.0322 68  ALA A N   
512  C CA  . ALA A 68  ? 0.3728 0.3728 0.3213 -0.0478 0.0047  -0.0300 68  ALA A CA  
513  C C   . ALA A 68  ? 0.3846 0.3929 0.3162 -0.0525 0.0024  -0.0305 68  ALA A C   
514  O O   . ALA A 68  ? 0.3861 0.3980 0.3099 -0.0546 -0.0051 -0.0242 68  ALA A O   
515  C CB  . ALA A 68  ? 0.3795 0.3767 0.3334 -0.0503 0.0024  -0.0372 68  ALA A CB  
516  N N   . ASN A 69  ? 0.3936 0.4055 0.3201 -0.0538 0.0095  -0.0375 69  ASN A N   
517  C CA  . ASN A 69  ? 0.4072 0.4287 0.3168 -0.0582 0.0091  -0.0370 69  ASN A CA  
518  C C   . ASN A 69  ? 0.4031 0.4273 0.3097 -0.0573 0.0086  -0.0250 69  ASN A C   
519  O O   . ASN A 69  ? 0.4115 0.4430 0.3046 -0.0612 0.0067  -0.0205 69  ASN A O   
520  C CB  . ASN A 69  ? 0.4209 0.4465 0.3267 -0.0596 0.0183  -0.0491 69  ASN A CB  
521  C CG  . ASN A 69  ? 0.4354 0.4609 0.3390 -0.0634 0.0181  -0.0630 69  ASN A CG  
522  O OD1 . ASN A 69  ? 0.4372 0.4635 0.3380 -0.0664 0.0099  -0.0629 69  ASN A OD1 
523  N ND2 . ASN A 69  ? 0.4466 0.4717 0.3523 -0.0633 0.0275  -0.0758 69  ASN A ND2 
524  N N   . LEU A 70  ? 0.3897 0.4088 0.3091 -0.0525 0.0106  -0.0199 70  LEU A N   
525  C CA  . LEU A 70  ? 0.3874 0.4093 0.3064 -0.0523 0.0106  -0.0103 70  LEU A CA  
526  C C   . LEU A 70  ? 0.3875 0.4079 0.3006 -0.0547 0.0018  -0.0009 70  LEU A C   
527  O O   . LEU A 70  ? 0.3793 0.3942 0.2968 -0.0530 -0.0041 0.0006  70  LEU A O   
528  C CB  . LEU A 70  ? 0.3773 0.3959 0.3115 -0.0468 0.0135  -0.0077 70  LEU A CB  
529  C CG  . LEU A 70  ? 0.3793 0.3993 0.3231 -0.0428 0.0225  -0.0140 70  LEU A CG  
530  C CD1 . LEU A 70  ? 0.3695 0.3874 0.3277 -0.0370 0.0229  -0.0091 70  LEU A CD1 
531  C CD2 . LEU A 70  ? 0.3915 0.4210 0.3304 -0.0447 0.0290  -0.0153 70  LEU A CD2 
532  N N   . SER A 71  ? 0.3955 0.4208 0.2998 -0.0584 0.0017  0.0057  71  SER A N   
533  C CA  . SER A 71  ? 0.3967 0.4185 0.2990 -0.0599 -0.0051 0.0163  71  SER A CA  
534  C C   . SER A 71  ? 0.3841 0.4019 0.2984 -0.0576 -0.0040 0.0200  71  SER A C   
535  O O   . SER A 71  ? 0.3737 0.3939 0.2959 -0.0550 0.0016  0.0158  71  SER A O   
536  C CB  . SER A 71  ? 0.4126 0.4408 0.3012 -0.0655 -0.0050 0.0230  71  SER A CB  
537  O OG  . SER A 71  ? 0.4155 0.4501 0.3043 -0.0673 0.0030  0.0226  71  SER A OG  
538  N N   . ALA A 72  ? 0.3834 0.3956 0.2998 -0.0583 -0.0095 0.0277  72  ALA A N   
539  C CA  . ALA A 72  ? 0.3771 0.3864 0.3040 -0.0572 -0.0091 0.0300  72  ALA A CA  
540  C C   . ALA A 72  ? 0.3795 0.3967 0.3079 -0.0600 -0.0026 0.0306  72  ALA A C   
541  O O   . ALA A 72  ? 0.3716 0.3916 0.3098 -0.0579 0.0000  0.0284  72  ALA A O   
542  C CB  . ALA A 72  ? 0.3830 0.3844 0.3114 -0.0586 -0.0152 0.0372  72  ALA A CB  
543  N N   . GLY A 73  ? 0.3889 0.4113 0.3075 -0.0648 0.0000  0.0339  73  GLY A N   
544  C CA  . GLY A 73  ? 0.3926 0.4243 0.3124 -0.0682 0.0069  0.0349  73  GLY A CA  
545  C C   . GLY A 73  ? 0.3887 0.4289 0.3128 -0.0647 0.0143  0.0266  73  GLY A C   
546  O O   . GLY A 73  ? 0.3876 0.4364 0.3182 -0.0656 0.0199  0.0267  73  GLY A O   
547  N N   . GLY A 74  ? 0.3888 0.4267 0.3108 -0.0607 0.0146  0.0194  74  GLY A N   
548  C CA  . GLY A 74  ? 0.3854 0.4285 0.3133 -0.0565 0.0220  0.0111  74  GLY A CA  
549  C C   . GLY A 74  ? 0.3723 0.4130 0.3153 -0.0503 0.0220  0.0097  74  GLY A C   
550  O O   . GLY A 74  ? 0.3695 0.4145 0.3208 -0.0459 0.0282  0.0049  74  GLY A O   
551  N N   . VAL A 75  ? 0.3660 0.4006 0.3130 -0.0495 0.0153  0.0141  75  VAL A N   
552  C CA  . VAL A 75  ? 0.3558 0.3896 0.3149 -0.0439 0.0146  0.0136  75  VAL A CA  
553  C C   . VAL A 75  ? 0.3523 0.3972 0.3215 -0.0423 0.0192  0.0149  75  VAL A C   
554  O O   . VAL A 75  ? 0.3454 0.3935 0.3241 -0.0364 0.0229  0.0128  75  VAL A O   
555  C CB  . VAL A 75  ? 0.3516 0.3787 0.3118 -0.0440 0.0071  0.0173  75  VAL A CB  
556  C CG1 . VAL A 75  ? 0.3434 0.3733 0.3144 -0.0389 0.0067  0.0177  75  VAL A CG1 
557  C CG2 . VAL A 75  ? 0.3544 0.3724 0.3086 -0.0437 0.0030  0.0157  75  VAL A CG2 
558  N N   . ALA A 76  ? 0.3537 0.4048 0.3222 -0.0475 0.0191  0.0187  76  ALA A N   
559  C CA  . ALA A 76  ? 0.3520 0.4162 0.3314 -0.0469 0.0227  0.0200  76  ALA A CA  
560  C C   . ALA A 76  ? 0.3546 0.4266 0.3401 -0.0420 0.0310  0.0159  76  ALA A C   
561  O O   . ALA A 76  ? 0.3493 0.4278 0.3472 -0.0358 0.0328  0.0160  76  ALA A O   
562  C CB  . ALA A 76  ? 0.3587 0.4283 0.3360 -0.0549 0.0228  0.0241  76  ALA A CB  
563  N N   . ASN A 77  ? 0.3629 0.4345 0.3396 -0.0443 0.0361  0.0123  77  ASN A N   
564  C CA  . ASN A 77  ? 0.3689 0.4472 0.3511 -0.0398 0.0452  0.0065  77  ASN A CA  
565  C C   . ASN A 77  ? 0.3627 0.4330 0.3519 -0.0320 0.0464  0.0019  77  ASN A C   
566  O O   . ASN A 77  ? 0.3591 0.4345 0.3601 -0.0258 0.0531  -0.0009 77  ASN A O   
567  C CB  . ASN A 77  ? 0.3859 0.4658 0.3546 -0.0448 0.0502  0.0022  77  ASN A CB  
568  C CG  . ASN A 77  ? 0.3976 0.4831 0.3715 -0.0401 0.0604  -0.0062 77  ASN A CG  
569  O OD1 . ASN A 77  ? 0.4132 0.4913 0.3812 -0.0387 0.0625  -0.0141 77  ASN A OD1 
570  N ND2 . ASN A 77  ? 0.3981 0.4970 0.3846 -0.0376 0.0668  -0.0054 77  ASN A ND2 
571  N N   . ALA A 78  ? 0.3578 0.4157 0.3413 -0.0321 0.0402  0.0019  78  ALA A N   
572  C CA  . ALA A 78  ? 0.3537 0.4028 0.3440 -0.0259 0.0412  -0.0014 78  ALA A CA  
573  C C   . ALA A 78  ? 0.3423 0.3955 0.3483 -0.0187 0.0413  0.0037  78  ALA A C   
574  O O   . ALA A 78  ? 0.3457 0.3927 0.3603 -0.0127 0.0439  0.0025  78  ALA A O   
575  C CB  . ALA A 78  ? 0.3528 0.3901 0.3343 -0.0285 0.0343  -0.0016 78  ALA A CB  
576  N N   . PHE A 79  ? 0.3292 0.3930 0.3391 -0.0196 0.0382  0.0099  79  PHE A N   
577  C CA  . PHE A 79  ? 0.3192 0.3912 0.3431 -0.0132 0.0375  0.0155  79  PHE A CA  
578  C C   . PHE A 79  ? 0.3183 0.4034 0.3559 -0.0081 0.0447  0.0156  79  PHE A C   
579  O O   . PHE A 79  ? 0.3114 0.4056 0.3618 -0.0020 0.0440  0.0212  79  PHE A O   
580  C CB  . PHE A 79  ? 0.3106 0.3894 0.3325 -0.0171 0.0298  0.0208  79  PHE A CB  
581  C CG  . PHE A 79  ? 0.3042 0.3730 0.3195 -0.0179 0.0230  0.0222  79  PHE A CG  
582  C CD1 . PHE A 79  ? 0.3056 0.3642 0.3086 -0.0241 0.0192  0.0199  79  PHE A CD1 
583  C CD2 . PHE A 79  ? 0.2990 0.3700 0.3209 -0.0122 0.0207  0.0265  79  PHE A CD2 
584  C CE1 . PHE A 79  ? 0.3017 0.3523 0.3004 -0.0242 0.0136  0.0208  79  PHE A CE1 
585  C CE2 . PHE A 79  ? 0.2953 0.3586 0.3112 -0.0129 0.0155  0.0273  79  PHE A CE2 
586  C CZ  . PHE A 79  ? 0.2982 0.3514 0.3033 -0.0188 0.0121  0.0239  79  PHE A CZ  
587  N N   . SER A 80  ? 0.3220 0.4094 0.3571 -0.0104 0.0516  0.0097  80  SER A N   
588  C CA  . SER A 80  ? 0.3239 0.4262 0.3723 -0.0064 0.0590  0.0093  80  SER A CA  
589  C C   . SER A 80  ? 0.3239 0.4279 0.3909 0.0048  0.0632  0.0114  80  SER A C   
590  O O   . SER A 80  ? 0.3162 0.4358 0.3975 0.0095  0.0633  0.0172  80  SER A O   
591  C CB  . SER A 80  ? 0.3344 0.4375 0.3757 -0.0101 0.0672  0.0010  80  SER A CB  
592  O OG  . SER A 80  ? 0.3365 0.4426 0.3636 -0.0201 0.0640  0.0022  80  SER A OG  
593  N N   . SER A 81  ? 0.3291 0.4176 0.3968 0.0090  0.0665  0.0071  81  SER A N   
594  C CA  A SER A 81  ? 0.3328 0.4196 0.4193 0.0200  0.0714  0.0098  81  SER A CA  
595  C CA  B SER A 81  ? 0.3335 0.4202 0.4200 0.0200  0.0713  0.0098  81  SER A CA  
596  C C   . SER A 81  ? 0.3247 0.4171 0.4186 0.0246  0.0640  0.0219  81  SER A C   
597  O O   . SER A 81  ? 0.3245 0.4281 0.4356 0.0330  0.0659  0.0286  81  SER A O   
598  C CB  A SER A 81  ? 0.3417 0.4085 0.4273 0.0217  0.0760  0.0023  81  SER A CB  
599  C CB  B SER A 81  ? 0.3430 0.4096 0.4284 0.0217  0.0758  0.0024  81  SER A CB  
600  O OG  A SER A 81  ? 0.3510 0.4155 0.4319 0.0189  0.0840  -0.0099 81  SER A OG  
601  O OG  B SER A 81  ? 0.3495 0.4127 0.4551 0.0323  0.0820  0.0049  81  SER A OG  
602  N N   . ALA A 82  ? 0.3196 0.4056 0.4008 0.0193  0.0558  0.0247  82  ALA A N   
603  C CA  . ALA A 82  ? 0.3151 0.4079 0.3998 0.0225  0.0486  0.0350  82  ALA A CA  
604  C C   . ALA A 82  ? 0.3117 0.4267 0.4010 0.0215  0.0445  0.0400  82  ALA A C   
605  O O   . ALA A 82  ? 0.3129 0.4407 0.4132 0.0278  0.0418  0.0487  82  ALA A O   
606  C CB  . ALA A 82  ? 0.3109 0.3929 0.3801 0.0163  0.0415  0.0348  82  ALA A CB  
607  N N   . PHE A 83  ? 0.3118 0.4320 0.3931 0.0131  0.0439  0.0348  83  PHE A N   
608  C CA  . PHE A 83  ? 0.3075 0.4482 0.3934 0.0098  0.0402  0.0379  83  PHE A CA  
609  C C   . PHE A 83  ? 0.3120 0.4702 0.4173 0.0170  0.0462  0.0404  83  PHE A C   
610  O O   . PHE A 83  ? 0.3057 0.4843 0.4206 0.0177  0.0422  0.0457  83  PHE A O   
611  C CB  . PHE A 83  ? 0.3087 0.4473 0.3816 -0.0015 0.0394  0.0322  83  PHE A CB  
612  C CG  . PHE A 83  ? 0.3064 0.4629 0.3827 -0.0075 0.0348  0.0346  83  PHE A CG  
613  C CD1 . PHE A 83  ? 0.3024 0.4627 0.3753 -0.0107 0.0257  0.0375  83  PHE A CD1 
614  C CD2 . PHE A 83  ? 0.3110 0.4811 0.3944 -0.0108 0.0400  0.0330  83  PHE A CD2 
615  C CE1 . PHE A 83  ? 0.3021 0.4786 0.3791 -0.0174 0.0213  0.0382  83  PHE A CE1 
616  C CE2 . PHE A 83  ? 0.3090 0.4959 0.3973 -0.0176 0.0358  0.0349  83  PHE A CE2 
617  C CZ  . PHE A 83  ? 0.3054 0.4950 0.3907 -0.0212 0.0262  0.0371  83  PHE A CZ  
618  N N   . GLY A 84  ? 0.3208 0.4717 0.4324 0.0223  0.0558  0.0358  84  GLY A N   
619  C CA  . GLY A 84  ? 0.3275 0.4932 0.4596 0.0307  0.0630  0.0373  84  GLY A CA  
620  C C   . GLY A 84  ? 0.3335 0.5098 0.4666 0.0256  0.0698  0.0306  84  GLY A C   
621  O O   . GLY A 84  ? 0.3361 0.5257 0.4868 0.0324  0.0770  0.0305  84  GLY A O   
622  N N   . SER A 85  ? 0.3358 0.5072 0.4509 0.0140  0.0678  0.0257  85  SER A N   
623  C CA  . SER A 85  ? 0.3426 0.5236 0.4559 0.0078  0.0745  0.0203  85  SER A CA  
624  C C   . SER A 85  ? 0.3461 0.5124 0.4359 -0.0030 0.0731  0.0152  85  SER A C   
625  O O   . SER A 85  ? 0.3387 0.4915 0.4160 -0.0067 0.0650  0.0170  85  SER A O   
626  C CB  . SER A 85  ? 0.3395 0.5451 0.4638 0.0041  0.0715  0.0257  85  SER A CB  
627  O OG  . SER A 85  ? 0.3354 0.5400 0.4504 -0.0035 0.0604  0.0299  85  SER A OG  
628  N N   . PRO A 86  ? 0.3524 0.5224 0.4364 -0.0078 0.0812  0.0093  86  PRO A N   
629  C CA  . PRO A 86  ? 0.3559 0.5128 0.4174 -0.0171 0.0801  0.0055  86  PRO A CA  
630  C C   . PRO A 86  ? 0.3479 0.5039 0.3995 -0.0270 0.0706  0.0118  86  PRO A C   
631  O O   . PRO A 86  ? 0.3470 0.5183 0.4058 -0.0318 0.0699  0.0160  86  PRO A O   
632  C CB  . PRO A 86  ? 0.3682 0.5354 0.4275 -0.0200 0.0912  -0.0003 86  PRO A CB  
633  C CG  . PRO A 86  ? 0.3709 0.5510 0.4521 -0.0098 0.0997  -0.0026 86  PRO A CG  
634  C CD  . PRO A 86  ? 0.3598 0.5472 0.4575 -0.0045 0.0920  0.0060  86  PRO A CD  
635  N N   . ILE A 87  ? 0.3440 0.4823 0.3810 -0.0299 0.0637  0.0119  87  ILE A N   
636  C CA  . ILE A 87  ? 0.3402 0.4741 0.3669 -0.0391 0.0558  0.0166  87  ILE A CA  
637  C C   . ILE A 87  ? 0.3503 0.4782 0.3597 -0.0465 0.0588  0.0147  87  ILE A C   
638  O O   . ILE A 87  ? 0.3528 0.4660 0.3487 -0.0473 0.0559  0.0125  87  ILE A O   
639  C CB  . ILE A 87  ? 0.3322 0.4523 0.3547 -0.0374 0.0463  0.0185  87  ILE A CB  
640  C CG1 . ILE A 87  ? 0.3240 0.4523 0.3621 -0.0297 0.0437  0.0213  87  ILE A CG1 
641  C CG2 . ILE A 87  ? 0.3322 0.4474 0.3463 -0.0465 0.0390  0.0224  87  ILE A CG2 
642  C CD1 . ILE A 87  ? 0.3196 0.4354 0.3539 -0.0263 0.0366  0.0226  87  ILE A CD1 
643  N N   . THR A 88  ? 0.3540 0.4952 0.3646 -0.0520 0.0648  0.0161  88  THR A N   
644  C CA  . THR A 88  ? 0.3688 0.5086 0.3632 -0.0591 0.0690  0.0157  88  THR A CA  
645  C C   . THR A 88  ? 0.3743 0.5229 0.3692 -0.0690 0.0687  0.0233  88  THR A C   
646  O O   . THR A 88  ? 0.3648 0.5241 0.3750 -0.0702 0.0674  0.0264  88  THR A O   
647  C CB  . THR A 88  ? 0.3777 0.5272 0.3722 -0.0555 0.0808  0.0081  88  THR A CB  
648  O OG1 . THR A 88  ? 0.3736 0.5422 0.3863 -0.0535 0.0873  0.0088  88  THR A OG1 
649  C CG2 . THR A 88  ? 0.3768 0.5160 0.3724 -0.0463 0.0821  -0.0003 88  THR A CG2 
650  N N   . GLU A 89  ? 0.3893 0.5343 0.3679 -0.0765 0.0701  0.0266  89  GLU A N   
651  C CA  . GLU A 89  ? 0.4015 0.5540 0.3803 -0.0867 0.0716  0.0348  89  GLU A CA  
652  C C   . GLU A 89  ? 0.4071 0.5819 0.3974 -0.0873 0.0827  0.0331  89  GLU A C   
653  O O   . GLU A 89  ? 0.4070 0.5929 0.4087 -0.0938 0.0838  0.0385  89  GLU A O   
654  C CB  . GLU A 89  ? 0.4177 0.5614 0.3755 -0.0935 0.0708  0.0402  89  GLU A CB  
655  C CG  . GLU A 89  ? 0.4162 0.5394 0.3655 -0.0928 0.0596  0.0428  89  GLU A CG  
656  C CD  . GLU A 89  ? 0.4342 0.5501 0.3640 -0.0987 0.0579  0.0498  89  GLU A CD  
657  O OE1 . GLU A 89  ? 0.4453 0.5475 0.3728 -0.1016 0.0497  0.0568  89  GLU A OE1 
658  O OE2 . GLU A 89  ? 0.4438 0.5683 0.3608 -0.1002 0.0647  0.0485  89  GLU A OE2 
659  N N   . LYS A 90  ? 0.4154 0.5967 0.4043 -0.0806 0.0910  0.0248  90  LYS A N   
660  C CA  . LYS A 90  ? 0.4235 0.6265 0.4249 -0.0790 0.1027  0.0214  90  LYS A CA  
661  C C   . LYS A 90  ? 0.4068 0.6221 0.4340 -0.0742 0.1014  0.0219  90  LYS A C   
662  O O   . LYS A 90  ? 0.4061 0.6396 0.4463 -0.0791 0.1057  0.0257  90  LYS A O   
663  C CB  . LYS A 90  ? 0.4367 0.6404 0.4324 -0.0711 0.1113  0.0102  90  LYS A CB  
664  C CG  . LYS A 90  ? 0.4476 0.6729 0.4574 -0.0673 0.1246  0.0046  90  LYS A CG  
665  C CD  . LYS A 90  ? 0.4644 0.6873 0.4665 -0.0604 0.1332  -0.0082 90  LYS A CD  
666  C CE  . LYS A 90  ? 0.4727 0.7141 0.4950 -0.0527 0.1458  -0.0155 90  LYS A CE  
667  N NZ  . LYS A 90  ? 0.4644 0.7044 0.5112 -0.0419 0.1419  -0.0155 90  LYS A NZ  
668  N N   . ASP A 91  ? 0.3892 0.5958 0.4237 -0.0650 0.0954  0.0186  91  ASP A N   
669  C CA  . ASP A 91  ? 0.3767 0.5967 0.4351 -0.0576 0.0947  0.0185  91  ASP A CA  
670  C C   . ASP A 91  ? 0.3618 0.5811 0.4280 -0.0611 0.0831  0.0247  91  ASP A C   
671  O O   . ASP A 91  ? 0.3532 0.5901 0.4389 -0.0593 0.0823  0.0267  91  ASP A O   
672  C CB  . ASP A 91  ? 0.3741 0.5862 0.4371 -0.0446 0.0958  0.0121  91  ASP A CB  
673  C CG  . ASP A 91  ? 0.3879 0.5990 0.4438 -0.0409 0.1072  0.0032  91  ASP A CG  
674  O OD1 . ASP A 91  ? 0.3965 0.6259 0.4626 -0.0397 0.1178  0.0005  91  ASP A OD1 
675  O OD2 . ASP A 91  ? 0.3927 0.5859 0.4332 -0.0395 0.1058  -0.0017 91  ASP A OD2 
676  N N   . ALA A 92  ? 0.3562 0.5565 0.4079 -0.0658 0.0743  0.0271  92  ALA A N   
677  C CA  . ALA A 92  ? 0.3444 0.5421 0.4019 -0.0689 0.0635  0.0309  92  ALA A CA  
678  C C   . ALA A 92  ? 0.3467 0.5284 0.3895 -0.0793 0.0580  0.0348  92  ALA A C   
679  O O   . ALA A 92  ? 0.3394 0.5038 0.3735 -0.0779 0.0501  0.0345  92  ALA A O   
680  C CB  . ALA A 92  ? 0.3364 0.5256 0.3961 -0.0587 0.0572  0.0287  92  ALA A CB  
681  N N   . PRO A 93  ? 0.3544 0.5422 0.3957 -0.0894 0.0626  0.0390  93  PRO A N   
682  C CA  . PRO A 93  ? 0.3613 0.5332 0.3895 -0.0989 0.0586  0.0444  93  PRO A CA  
683  C C   . PRO A 93  ? 0.3545 0.5156 0.3869 -0.1023 0.0479  0.0455  93  PRO A C   
684  O O   . PRO A 93  ? 0.3541 0.4956 0.3746 -0.1038 0.0424  0.0473  93  PRO A O   
685  C CB  . PRO A 93  ? 0.3728 0.5582 0.4047 -0.1090 0.0665  0.0498  93  PRO A CB  
686  C CG  . PRO A 93  ? 0.3671 0.5773 0.4186 -0.1060 0.0722  0.0466  93  PRO A CG  
687  C CD  . PRO A 93  ? 0.3582 0.5684 0.4108 -0.0923 0.0725  0.0397  93  PRO A CD  
688  N N   . GLN A 94  ? 0.3484 0.5234 0.3981 -0.1035 0.0450  0.0438  94  GLN A N   
689  C CA  . GLN A 94  ? 0.3483 0.5153 0.4023 -0.1074 0.0353  0.0427  94  GLN A CA  
690  C C   . GLN A 94  ? 0.3380 0.4915 0.3841 -0.0980 0.0285  0.0388  94  GLN A C   
691  O O   . GLN A 94  ? 0.3363 0.4730 0.3761 -0.1005 0.0220  0.0384  94  GLN A O   
692  C CB  . GLN A 94  ? 0.3480 0.5367 0.4220 -0.1109 0.0333  0.0406  94  GLN A CB  
693  C CG  . GLN A 94  ? 0.3604 0.5645 0.4455 -0.1216 0.0398  0.0444  94  GLN A CG  
694  C CD  . GLN A 94  ? 0.3782 0.5658 0.4568 -0.1336 0.0401  0.0496  94  GLN A CD  
695  O OE1 . GLN A 94  ? 0.3834 0.5515 0.4561 -0.1360 0.0329  0.0488  94  GLN A OE1 
696  N NE2 . GLN A 94  ? 0.3919 0.5876 0.4722 -0.1410 0.0487  0.0554  94  GLN A NE2 
697  N N   . LEU A 95  ? 0.3309 0.4914 0.3786 -0.0873 0.0307  0.0361  95  LEU A N   
698  C CA  . LEU A 95  ? 0.3257 0.4742 0.3666 -0.0784 0.0257  0.0334  95  LEU A CA  
699  C C   . LEU A 95  ? 0.3306 0.4578 0.3541 -0.0781 0.0256  0.0341  95  LEU A C   
700  O O   . LEU A 95  ? 0.3280 0.4405 0.3449 -0.0770 0.0192  0.0332  95  LEU A O   
701  C CB  . LEU A 95  ? 0.3202 0.4801 0.3683 -0.0672 0.0294  0.0317  95  LEU A CB  
702  C CG  . LEU A 95  ? 0.3151 0.4636 0.3579 -0.0579 0.0255  0.0300  95  LEU A CG  
703  C CD1 . LEU A 95  ? 0.3121 0.4586 0.3557 -0.0591 0.0163  0.0296  95  LEU A CD1 
704  C CD2 . LEU A 95  ? 0.3125 0.4724 0.3658 -0.0473 0.0302  0.0298  95  LEU A CD2 
705  N N   . HIS A 96  ? 0.3387 0.4658 0.3549 -0.0792 0.0328  0.0354  96  HIS A N   
706  C CA  . HIS A 96  ? 0.3484 0.4587 0.3478 -0.0791 0.0324  0.0362  96  HIS A CA  
707  C C   . HIS A 96  ? 0.3569 0.4535 0.3502 -0.0869 0.0268  0.0410  96  HIS A C   
708  O O   . HIS A 96  ? 0.3572 0.4382 0.3410 -0.0849 0.0218  0.0413  96  HIS A O   
709  C CB  . HIS A 96  ? 0.3583 0.4745 0.3501 -0.0796 0.0413  0.0361  96  HIS A CB  
710  C CG  . HIS A 96  ? 0.3635 0.4667 0.3393 -0.0765 0.0407  0.0341  96  HIS A CG  
711  N ND1 . HIS A 96  ? 0.3737 0.4654 0.3357 -0.0818 0.0373  0.0390  96  HIS A ND1 
712  C CD2 . HIS A 96  ? 0.3617 0.4620 0.3344 -0.0688 0.0427  0.0278  96  HIS A CD2 
713  C CE1 . HIS A 96  ? 0.3765 0.4609 0.3271 -0.0777 0.0367  0.0354  96  HIS A CE1 
714  N NE2 . HIS A 96  ? 0.3684 0.4572 0.3253 -0.0703 0.0401  0.0279  96  HIS A NE2 
715  N N   . LYS A 97  ? 0.3653 0.4678 0.3658 -0.0958 0.0278  0.0450  97  LYS A N   
716  C CA  . LYS A 97  ? 0.3781 0.4667 0.3767 -0.1035 0.0229  0.0497  97  LYS A CA  
717  C C   . LYS A 97  ? 0.3692 0.4474 0.3716 -0.1007 0.0145  0.0453  97  LYS A C   
718  O O   . LYS A 97  ? 0.3722 0.4332 0.3680 -0.1010 0.0099  0.0471  97  LYS A O   
719  C CB  . LYS A 97  ? 0.3911 0.4892 0.4006 -0.1141 0.0262  0.0537  97  LYS A CB  
720  C CG  . LYS A 97  ? 0.4092 0.4912 0.4187 -0.1228 0.0225  0.0595  97  LYS A CG  
721  C CD  . LYS A 97  ? 0.4253 0.5170 0.4489 -0.1341 0.0257  0.0623  97  LYS A CD  
722  C CE  . LYS A 97  ? 0.4444 0.5175 0.4702 -0.1430 0.0226  0.0681  97  LYS A CE  
723  N NZ  . LYS A 97  ? 0.4566 0.5385 0.4991 -0.1550 0.0252  0.0693  97  LYS A NZ  
724  N N   . LEU A 98  ? 0.3582 0.4483 0.3715 -0.0978 0.0126  0.0397  98  LEU A N   
725  C CA  . LEU A 98  ? 0.3545 0.4385 0.3704 -0.0948 0.0052  0.0346  98  LEU A CA  
726  C C   . LEU A 98  ? 0.3513 0.4208 0.3561 -0.0869 0.0024  0.0335  98  LEU A C   
727  O O   . LEU A 98  ? 0.3527 0.4078 0.3546 -0.0875 -0.0024 0.0325  98  LEU A O   
728  C CB  . LEU A 98  ? 0.3435 0.4466 0.3702 -0.0909 0.0042  0.0301  98  LEU A CB  
729  C CG  . LEU A 98  ? 0.3377 0.4389 0.3654 -0.0869 -0.0027 0.0247  98  LEU A CG  
730  C CD1 . LEU A 98  ? 0.3468 0.4420 0.3789 -0.0957 -0.0075 0.0211  98  LEU A CD1 
731  C CD2 . LEU A 98  ? 0.3287 0.4507 0.3647 -0.0809 -0.0031 0.0230  98  LEU A CD2 
732  N N   . LEU A 99  ? 0.3485 0.4222 0.3486 -0.0797 0.0061  0.0332  99  LEU A N   
733  C CA  . LEU A 99  ? 0.3481 0.4111 0.3402 -0.0722 0.0038  0.0314  99  LEU A CA  
734  C C   . LEU A 99  ? 0.3600 0.4077 0.3408 -0.0743 0.0027  0.0348  99  LEU A C   
735  O O   . LEU A 99  ? 0.3589 0.3950 0.3355 -0.0710 -0.0017 0.0337  99  LEU A O   
736  C CB  . LEU A 99  ? 0.3420 0.4135 0.3348 -0.0646 0.0086  0.0295  99  LEU A CB  
737  C CG  . LEU A 99  ? 0.3341 0.4216 0.3391 -0.0606 0.0092  0.0278  99  LEU A CG  
738  C CD1 . LEU A 99  ? 0.3320 0.4252 0.3395 -0.0526 0.0149  0.0268  99  LEU A CD1 
739  C CD2 . LEU A 99  ? 0.3286 0.4145 0.3361 -0.0583 0.0026  0.0258  99  LEU A CD2 
740  N N   . THR A 100 ? 0.3734 0.4228 0.3495 -0.0797 0.0068  0.0395  100 THR A N   
741  C CA  . THR A 100 ? 0.3893 0.4268 0.3544 -0.0823 0.0053  0.0449  100 THR A CA  
742  C C   . THR A 100 ? 0.3886 0.4125 0.3568 -0.0862 -0.0003 0.0481  100 THR A C   
743  O O   . THR A 100 ? 0.3920 0.4036 0.3542 -0.0842 -0.0044 0.0506  100 THR A O   
744  C CB  . THR A 100 ? 0.4079 0.4527 0.3671 -0.0881 0.0115  0.0504  100 THR A CB  
745  O OG1 . THR A 100 ? 0.4188 0.4751 0.3752 -0.0838 0.0175  0.0458  100 THR A OG1 
746  C CG2 . THR A 100 ? 0.4262 0.4603 0.3730 -0.0908 0.0092  0.0579  100 THR A CG2 
747  N N   . ASN A 101 ? 0.3842 0.4110 0.3631 -0.0916 -0.0005 0.0474  101 ASN A N   
748  C CA  . ASN A 101 ? 0.3944 0.4075 0.3784 -0.0966 -0.0046 0.0497  101 ASN A CA  
749  C C   . ASN A 101 ? 0.3860 0.3896 0.3727 -0.0912 -0.0105 0.0432  101 ASN A C   
750  O O   . ASN A 101 ? 0.3915 0.3812 0.3820 -0.0935 -0.0138 0.0439  101 ASN A O   
751  C CB  . ASN A 101 ? 0.4000 0.4204 0.3957 -0.1055 -0.0025 0.0495  101 ASN A CB  
752  C CG  . ASN A 101 ? 0.4190 0.4244 0.4192 -0.1136 -0.0037 0.0555  101 ASN A CG  
753  O OD1 . ASN A 101 ? 0.4318 0.4203 0.4310 -0.1114 -0.0080 0.0564  101 ASN A OD1 
754  N ND2 . ASN A 101 ? 0.4269 0.4386 0.4338 -0.1228 0.0004  0.0599  101 ASN A ND2 
755  N N   . MET A 102 ? 0.3716 0.3825 0.3568 -0.0839 -0.0110 0.0371  102 MET A N   
756  C CA  . MET A 102 ? 0.3674 0.3718 0.3539 -0.0783 -0.0155 0.0312  102 MET A CA  
757  C C   . MET A 102 ? 0.3624 0.3600 0.3407 -0.0713 -0.0168 0.0325  102 MET A C   
758  O O   . MET A 102 ? 0.3567 0.3501 0.3360 -0.0662 -0.0197 0.0282  102 MET A O   
759  C CB  . MET A 102 ? 0.3580 0.3762 0.3500 -0.0756 -0.0157 0.0243  102 MET A CB  
760  C CG  . MET A 102 ? 0.3509 0.3835 0.3416 -0.0715 -0.0117 0.0251  102 MET A CG  
761  S SD  . MET A 102 ? 0.3411 0.3906 0.3389 -0.0672 -0.0128 0.0198  102 MET A SD  
762  C CE  . MET A 102 ? 0.3366 0.3774 0.3287 -0.0588 -0.0153 0.0174  102 MET A CE  
763  N N   . ILE A 103 ? 0.3645 0.3624 0.3349 -0.0716 -0.0146 0.0380  103 ILE A N   
764  C CA  . ILE A 103 ? 0.3642 0.3574 0.3269 -0.0664 -0.0163 0.0389  103 ILE A CA  
765  C C   . ILE A 103 ? 0.3617 0.3415 0.3259 -0.0645 -0.0216 0.0404  103 ILE A C   
766  O O   . ILE A 103 ? 0.3539 0.3314 0.3182 -0.0588 -0.0239 0.0370  103 ILE A O   
767  C CB  . ILE A 103 ? 0.3791 0.3755 0.3319 -0.0689 -0.0135 0.0445  103 ILE A CB  
768  C CG1 . ILE A 103 ? 0.3768 0.3862 0.3282 -0.0676 -0.0076 0.0405  103 ILE A CG1 
769  C CG2 . ILE A 103 ? 0.3861 0.3765 0.3313 -0.0656 -0.0173 0.0467  103 ILE A CG2 
770  C CD1 . ILE A 103 ? 0.3906 0.4059 0.3325 -0.0713 -0.0033 0.0443  103 ILE A CD1 
771  N N   . GLY A 104 ? 0.3649 0.3358 0.3318 -0.0693 -0.0231 0.0459  104 GLY A N   
772  C CA  . GLY A 104 ? 0.3719 0.3290 0.3428 -0.0671 -0.0277 0.0479  104 GLY A CA  
773  C C   . GLY A 104 ? 0.3640 0.3177 0.3436 -0.0639 -0.0293 0.0389  104 GLY A C   
774  O O   . GLY A 104 ? 0.3624 0.3097 0.3445 -0.0585 -0.0322 0.0371  104 GLY A O   
775  N N   . ASP A 105 ? 0.3599 0.3197 0.3443 -0.0673 -0.0272 0.0330  105 ASP A N   
776  C CA  . ASP A 105 ? 0.3559 0.3152 0.3470 -0.0652 -0.0286 0.0235  105 ASP A CA  
777  C C   . ASP A 105 ? 0.3468 0.3128 0.3345 -0.0576 -0.0288 0.0191  105 ASP A C   
778  O O   . ASP A 105 ? 0.3497 0.3106 0.3405 -0.0533 -0.0306 0.0147  105 ASP A O   
779  C CB  . ASP A 105 ? 0.3535 0.3223 0.3493 -0.0710 -0.0270 0.0184  105 ASP A CB  
780  C CG  . ASP A 105 ? 0.3647 0.3270 0.3658 -0.0797 -0.0262 0.0225  105 ASP A CG  
781  O OD1 . ASP A 105 ? 0.3755 0.3220 0.3818 -0.0813 -0.0278 0.0240  105 ASP A OD1 
782  O OD2 . ASP A 105 ? 0.3625 0.3355 0.3639 -0.0848 -0.0235 0.0247  105 ASP A OD2 
783  N N   . ALA A 106 ? 0.3388 0.3160 0.3212 -0.0560 -0.0265 0.0206  106 ALA A N   
784  C CA  . ALA A 106 ? 0.3293 0.3129 0.3097 -0.0495 -0.0258 0.0174  106 ALA A CA  
785  C C   . ALA A 106 ? 0.3303 0.3084 0.3073 -0.0455 -0.0271 0.0206  106 ALA A C   
786  O O   . ALA A 106 ? 0.3270 0.3051 0.3056 -0.0406 -0.0278 0.0176  106 ALA A O   
787  C CB  . ALA A 106 ? 0.3234 0.3202 0.3022 -0.0491 -0.0224 0.0176  106 ALA A CB  
788  N N   . GLY A 107 ? 0.3344 0.3095 0.3065 -0.0480 -0.0274 0.0266  107 GLY A N   
789  C CA  . GLY A 107 ? 0.3362 0.3090 0.3041 -0.0452 -0.0292 0.0293  107 GLY A CA  
790  C C   . GLY A 107 ? 0.3436 0.3067 0.3152 -0.0432 -0.0338 0.0320  107 GLY A C   
791  O O   . GLY A 107 ? 0.3423 0.3054 0.3147 -0.0390 -0.0360 0.0316  107 GLY A O   
792  N N   . ASP A 108 ? 0.3523 0.3070 0.3277 -0.0462 -0.0351 0.0349  108 ASP A N   
793  C CA  . ASP A 108 ? 0.3626 0.3065 0.3430 -0.0440 -0.0392 0.0392  108 ASP A CA  
794  C C   . ASP A 108 ? 0.3632 0.2997 0.3541 -0.0418 -0.0393 0.0326  108 ASP A C   
795  O O   . ASP A 108 ? 0.3601 0.2955 0.3561 -0.0361 -0.0407 0.0291  108 ASP A O   
796  C CB  . ASP A 108 ? 0.3768 0.3147 0.3542 -0.0488 -0.0403 0.0494  108 ASP A CB  
797  C CG  . ASP A 108 ? 0.3898 0.3161 0.3738 -0.0458 -0.0448 0.0562  108 ASP A CG  
798  O OD1 . ASP A 108 ? 0.3877 0.3126 0.3775 -0.0395 -0.0473 0.0532  108 ASP A OD1 
799  O OD2 . ASP A 108 ? 0.4035 0.3221 0.3879 -0.0497 -0.0454 0.0653  108 ASP A OD2 
800  N N   . LEU A 109 ? 0.3650 0.2976 0.3596 -0.0467 -0.0376 0.0300  109 LEU A N   
801  C CA  . LEU A 109 ? 0.3693 0.2944 0.3737 -0.0457 -0.0375 0.0220  109 LEU A CA  
802  C C   . LEU A 109 ? 0.3574 0.2910 0.3622 -0.0406 -0.0362 0.0122  109 LEU A C   
803  O O   . LEU A 109 ? 0.3589 0.2873 0.3707 -0.0361 -0.0367 0.0071  109 LEU A O   
804  C CB  . LEU A 109 ? 0.3750 0.2979 0.3827 -0.0533 -0.0357 0.0186  109 LEU A CB  
805  C CG  . LEU A 109 ? 0.3905 0.3019 0.4015 -0.0592 -0.0360 0.0277  109 LEU A CG  
806  C CD1 . LEU A 109 ? 0.3953 0.3075 0.4109 -0.0676 -0.0339 0.0225  109 LEU A CD1 
807  C CD2 . LEU A 109 ? 0.4061 0.3002 0.4263 -0.0557 -0.0384 0.0315  109 LEU A CD2 
808  N N   . ALA A 110 ? 0.3446 0.2917 0.3426 -0.0411 -0.0342 0.0103  110 ALA A N   
809  C CA  . ALA A 110 ? 0.3387 0.2953 0.3363 -0.0369 -0.0325 0.0029  110 ALA A CA  
810  C C   . ALA A 110 ? 0.3356 0.2934 0.3340 -0.0304 -0.0330 0.0043  110 ALA A C   
811  O O   . ALA A 110 ? 0.3323 0.2964 0.3319 -0.0266 -0.0312 -0.0011 110 ALA A O   
812  C CB  . ALA A 110 ? 0.3298 0.3001 0.3216 -0.0388 -0.0302 0.0025  110 ALA A CB  
813  N N   . THR A 111 ? 0.3392 0.2925 0.3368 -0.0296 -0.0354 0.0117  111 THR A N   
814  C CA  . THR A 111 ? 0.3368 0.2931 0.3360 -0.0245 -0.0364 0.0131  111 THR A CA  
815  C C   . THR A 111 ? 0.3442 0.2922 0.3510 -0.0210 -0.0401 0.0164  111 THR A C   
816  O O   . THR A 111 ? 0.3408 0.2926 0.3521 -0.0164 -0.0411 0.0161  111 THR A O   
817  C CB  . THR A 111 ? 0.3353 0.2975 0.3272 -0.0262 -0.0366 0.0182  111 THR A CB  
818  O OG1 . THR A 111 ? 0.3485 0.3053 0.3367 -0.0294 -0.0395 0.0254  111 THR A OG1 
819  C CG2 . THR A 111 ? 0.3283 0.2986 0.3147 -0.0285 -0.0327 0.0160  111 THR A CG2 
820  N N   . ARG A 112 ? 0.3514 0.2884 0.3612 -0.0230 -0.0422 0.0203  112 ARG A N   
821  C CA  . ARG A 112 ? 0.3614 0.2907 0.3775 -0.0198 -0.0465 0.0276  112 ARG A CA  
822  C C   . ARG A 112 ? 0.3602 0.2876 0.3885 -0.0126 -0.0469 0.0230  112 ARG A C   
823  O O   . ARG A 112 ? 0.3631 0.2930 0.3961 -0.0082 -0.0504 0.0280  112 ARG A O   
824  C CB  . ARG A 112 ? 0.3763 0.2924 0.3946 -0.0236 -0.0477 0.0335  112 ARG A CB  
825  C CG  . ARG A 112 ? 0.3898 0.2997 0.4118 -0.0210 -0.0527 0.0454  112 ARG A CG  
826  C CD  . ARG A 112 ? 0.4074 0.3022 0.4344 -0.0243 -0.0529 0.0518  112 ARG A CD  
827  N NE  . ARG A 112 ? 0.4084 0.3050 0.4250 -0.0328 -0.0508 0.0552  112 ARG A NE  
828  C CZ  . ARG A 112 ? 0.4205 0.3064 0.4409 -0.0385 -0.0487 0.0567  112 ARG A CZ  
829  N NH1 . ARG A 112 ? 0.4325 0.3031 0.4669 -0.0368 -0.0484 0.0543  112 ARG A NH1 
830  N NH2 . ARG A 112 ? 0.4212 0.3119 0.4327 -0.0461 -0.0464 0.0600  112 ARG A NH2 
831  N N   . GLY A 113 ? 0.3600 0.2845 0.3939 -0.0114 -0.0432 0.0132  113 GLY A N   
832  C CA  . GLY A 113 ? 0.3622 0.2852 0.4083 -0.0044 -0.0422 0.0072  113 GLY A CA  
833  C C   . GLY A 113 ? 0.3513 0.2878 0.3982 -0.0002 -0.0418 0.0065  113 GLY A C   
834  O O   . GLY A 113 ? 0.3492 0.2865 0.4060 0.0054  -0.0443 0.0095  113 GLY A O   
835  N N   . ALA A 114 ? 0.3432 0.2906 0.3809 -0.0029 -0.0387 0.0031  114 ALA A N   
836  C CA  . ALA A 114 ? 0.3370 0.2968 0.3756 -0.0003 -0.0376 0.0027  114 ALA A CA  
837  C C   . ALA A 114 ? 0.3403 0.3029 0.3777 -0.0009 -0.0425 0.0114  114 ALA A C   
838  O O   . ALA A 114 ? 0.3359 0.3051 0.3813 0.0027  -0.0440 0.0124  114 ALA A O   
839  C CB  . ALA A 114 ? 0.3261 0.2950 0.3555 -0.0033 -0.0330 -0.0011 114 ALA A CB  
840  N N   . LYS A 115 ? 0.3520 0.3115 0.3797 -0.0060 -0.0449 0.0171  115 LYS A N   
841  C CA  . LYS A 115 ? 0.3651 0.3286 0.3893 -0.0074 -0.0497 0.0244  115 LYS A CA  
842  C C   . LYS A 115 ? 0.3740 0.3363 0.4087 -0.0025 -0.0553 0.0297  115 LYS A C   
843  O O   . LYS A 115 ? 0.3676 0.3393 0.4066 -0.0008 -0.0583 0.0311  115 LYS A O   
844  C CB  . LYS A 115 ? 0.3800 0.3396 0.3924 -0.0132 -0.0511 0.0299  115 LYS A CB  
845  C CG  . LYS A 115 ? 0.3855 0.3513 0.3875 -0.0178 -0.0474 0.0270  115 LYS A CG  
846  C CD  . LYS A 115 ? 0.4007 0.3649 0.3919 -0.0230 -0.0486 0.0327  115 LYS A CD  
847  C CE  . LYS A 115 ? 0.3996 0.3703 0.3824 -0.0266 -0.0444 0.0293  115 LYS A CE  
848  N NZ  . LYS A 115 ? 0.4006 0.3789 0.3834 -0.0262 -0.0452 0.0273  115 LYS A NZ  
849  N N   . GLU A 116 ? 0.3885 0.3394 0.4288 -0.0004 -0.0567 0.0328  116 GLU A N   
850  C CA  . GLU A 116 ? 0.4060 0.3543 0.4571 0.0049  -0.0624 0.0404  116 GLU A CA  
851  C C   . GLU A 116 ? 0.4008 0.3538 0.4682 0.0124  -0.0615 0.0352  116 GLU A C   
852  O O   . GLU A 116 ? 0.4026 0.3610 0.4797 0.0172  -0.0667 0.0411  116 GLU A O   
853  C CB  . GLU A 116 ? 0.4293 0.3619 0.4829 0.0047  -0.0636 0.0465  116 GLU A CB  
854  C CG  . GLU A 116 ? 0.4427 0.3730 0.4814 -0.0025 -0.0652 0.0543  116 GLU A CG  
855  C CD  . GLU A 116 ? 0.4682 0.3836 0.5106 -0.0030 -0.0670 0.0635  116 GLU A CD  
856  O OE1 . GLU A 116 ? 0.4911 0.3972 0.5486 0.0032  -0.0683 0.0655  116 GLU A OE1 
857  O OE2 . GLU A 116 ? 0.4835 0.3963 0.5145 -0.0096 -0.0665 0.0691  116 GLU A OE2 
858  N N   . LYS A 117 ? 0.3932 0.3464 0.4635 0.0136  -0.0548 0.0245  117 LYS A N   
859  C CA  . LYS A 117 ? 0.3924 0.3519 0.4777 0.0205  -0.0524 0.0187  117 LYS A CA  
860  C C   . LYS A 117 ? 0.3691 0.3452 0.4561 0.0205  -0.0535 0.0193  117 LYS A C   
861  O O   . LYS A 117 ? 0.3658 0.3493 0.4668 0.0259  -0.0564 0.0214  117 LYS A O   
862  C CB  . LYS A 117 ? 0.4036 0.3614 0.4890 0.0210  -0.0444 0.0068  117 LYS A CB  
863  C CG  . LYS A 117 ? 0.4188 0.3825 0.5200 0.0286  -0.0406 0.0000  117 LYS A CG  
864  C CD  . LYS A 117 ? 0.4449 0.3990 0.5628 0.0358  -0.0437 0.0030  117 LYS A CD  
865  C CE  . LYS A 117 ? 0.4638 0.4197 0.5968 0.0433  -0.0375 -0.0075 117 LYS A CE  
866  N NZ  . LYS A 117 ? 0.4618 0.4369 0.5990 0.0452  -0.0340 -0.0109 117 LYS A NZ  
867  N N   . TYR A 118 ? 0.3447 0.3268 0.4193 0.0143  -0.0512 0.0173  118 TYR A N   
868  C CA  . TYR A 118 ? 0.3298 0.3261 0.4072 0.0131  -0.0508 0.0163  118 TYR A CA  
869  C C   . TYR A 118 ? 0.3242 0.3261 0.3975 0.0096  -0.0580 0.0231  118 TYR A C   
870  O O   . TYR A 118 ? 0.3208 0.3349 0.4022 0.0098  -0.0602 0.0231  118 TYR A O   
871  C CB  . TYR A 118 ? 0.3192 0.3188 0.3878 0.0090  -0.0438 0.0106  118 TYR A CB  
872  C CG  . TYR A 118 ? 0.3199 0.3178 0.3909 0.0121  -0.0369 0.0035  118 TYR A CG  
873  C CD1 . TYR A 118 ? 0.3220 0.3271 0.4065 0.0177  -0.0335 -0.0007 118 TYR A CD1 
874  C CD2 . TYR A 118 ? 0.3193 0.3104 0.3792 0.0093  -0.0337 0.0005  118 TYR A CD2 
875  C CE1 . TYR A 118 ? 0.3237 0.3290 0.4090 0.0203  -0.0269 -0.0084 118 TYR A CE1 
876  C CE2 . TYR A 118 ? 0.3220 0.3137 0.3827 0.0115  -0.0280 -0.0070 118 TYR A CE2 
877  C CZ  . TYR A 118 ? 0.3224 0.3210 0.3949 0.0170  -0.0244 -0.0118 118 TYR A CZ  
878  O OH  . TYR A 118 ? 0.3235 0.3243 0.3954 0.0190  -0.0183 -0.0204 118 TYR A OH  
879  N N   . MET A 119 ? 0.5489 0.2889 0.6067 -0.0848 -0.0072 -0.0091 119 MET A N   
880  C CA  . MET A 119 ? 0.5725 0.2828 0.5742 -0.0888 0.0048  0.0268  119 MET A CA  
881  C C   . MET A 119 ? 0.5230 0.2708 0.4893 -0.0755 -0.0084 0.0293  119 MET A C   
882  O O   . MET A 119 ? 0.5290 0.2610 0.4524 -0.0639 -0.0169 0.0496  119 MET A O   
883  C CB  . MET A 119 ? 0.6367 0.2851 0.6062 -0.0804 0.0028  0.0576  119 MET A CB  
884  C CG  . MET A 119 ? 0.7013 0.2964 0.7012 -0.0957 0.0252  0.0663  119 MET A CG  
885  S SD  . MET A 119 ? 0.7430 0.3270 0.7519 -0.1266 0.0689  0.0759  119 MET A SD  
886  C CE  . MET A 119 ? 0.7810 0.3448 0.6949 -0.1152 0.0745  0.1208  119 MET A CE  
887  N N   . ARG A 120 ? 0.4689 0.2668 0.4569 -0.0755 -0.0098 0.0066  120 ARG A N   
888  C CA  . ARG A 120 ? 0.4288 0.2600 0.3958 -0.0621 -0.0198 0.0073  120 ARG A CA  
889  C C   . ARG A 120 ? 0.4386 0.2612 0.3689 -0.0671 -0.0109 0.0267  120 ARG A C   
890  O O   . ARG A 120 ? 0.4522 0.2677 0.3794 -0.0827 0.0069  0.0309  120 ARG A O   
891  C CB  . ARG A 120 ? 0.3890 0.2698 0.3823 -0.0574 -0.0205 -0.0167 120 ARG A CB  
892  C CG  . ARG A 120 ? 0.3568 0.2652 0.3334 -0.0408 -0.0276 -0.0125 120 ARG A CG  
893  C CD  . ARG A 120 ? 0.3335 0.2852 0.3252 -0.0319 -0.0259 -0.0297 120 ARG A CD  
894  N NE  . ARG A 120 ? 0.3146 0.2854 0.2922 -0.0133 -0.0287 -0.0212 120 ARG A NE  
895  C CZ  . ARG A 120 ? 0.3026 0.3060 0.2813 0.0021  -0.0269 -0.0271 120 ARG A CZ  
896  N NH1 . ARG A 120 ? 0.2975 0.3254 0.2921 0.0026  -0.0269 -0.0475 120 ARG A NH1 
897  N NH2 . ARG A 120 ? 0.2973 0.3080 0.2632 0.0183  -0.0236 -0.0129 120 ARG A NH2 
898  N N   . ILE A 121 ? 0.4299 0.2578 0.3382 -0.0536 -0.0227 0.0341  121 ILE A N   
899  C CA  A ILE A 121 ? 0.4385 0.2678 0.3181 -0.0540 -0.0185 0.0444  121 ILE A CA  
900  C CA  B ILE A 121 ? 0.4389 0.2682 0.3186 -0.0540 -0.0186 0.0444  121 ILE A CA  
901  C C   . ILE A 121 ? 0.4081 0.2718 0.3027 -0.0604 -0.0086 0.0336  121 ILE A C   
902  O O   . ILE A 121 ? 0.3757 0.2656 0.2936 -0.0539 -0.0118 0.0218  121 ILE A O   
903  C CB  A ILE A 121 ? 0.4340 0.2668 0.3015 -0.0371 -0.0349 0.0453  121 ILE A CB  
904  C CB  B ILE A 121 ? 0.4351 0.2673 0.3030 -0.0369 -0.0352 0.0453  121 ILE A CB  
905  C CG1 A ILE A 121 ? 0.4528 0.2872 0.2912 -0.0349 -0.0335 0.0508  121 ILE A CG1 
906  C CG1 B ILE A 121 ? 0.4760 0.2730 0.3243 -0.0269 -0.0475 0.0553  121 ILE A CG1 
907  C CG2 A ILE A 121 ? 0.3912 0.2562 0.2878 -0.0297 -0.0386 0.0323  121 ILE A CG2 
908  C CG2 B ILE A 121 ? 0.4366 0.2820 0.2869 -0.0351 -0.0333 0.0458  121 ILE A CG2 
909  C CD1 A ILE A 121 ? 0.4582 0.2962 0.2884 -0.0165 -0.0518 0.0453  121 ILE A CD1 
910  C CD1 B ILE A 121 ? 0.4741 0.2788 0.3189 -0.0082 -0.0667 0.0485  121 ILE A CD1 
911  N N   . ARG A 122 ? 0.4255 0.2894 0.3038 -0.0703 0.0036  0.0382  122 ARG A N   
912  C CA  A ARG A 122 ? 0.4016 0.2973 0.2959 -0.0760 0.0124  0.0258  122 ARG A CA  
913  C CA  B ARG A 122 ? 0.4033 0.2990 0.2979 -0.0760 0.0123  0.0257  122 ARG A CA  
914  C C   . ARG A 122 ? 0.3800 0.2942 0.2749 -0.0645 0.0047  0.0228  122 ARG A C   
915  O O   . ARG A 122 ? 0.3901 0.2949 0.2699 -0.0559 -0.0046 0.0279  122 ARG A O   
916  C CB  A ARG A 122 ? 0.4304 0.3220 0.3119 -0.0925 0.0312  0.0285  122 ARG A CB  
917  C CB  B ARG A 122 ? 0.4340 0.3260 0.3182 -0.0933 0.0317  0.0276  122 ARG A CB  
918  C CG  A ARG A 122 ? 0.4538 0.3290 0.3518 -0.1085 0.0462  0.0271  122 ARG A CG  
919  C CG  B ARG A 122 ? 0.4734 0.3349 0.3599 -0.1068 0.0451  0.0350  122 ARG A CG  
920  C CD  A ARG A 122 ? 0.4998 0.3583 0.3762 -0.1248 0.0708  0.0391  122 ARG A CD  
921  C CD  B ARG A 122 ? 0.4850 0.3586 0.3972 -0.1274 0.0681  0.0221  122 ARG A CD  
922  N NE  A ARG A 122 ? 0.4872 0.3799 0.3854 -0.1375 0.0852  0.0202  122 ARG A NE  
923  N NE  B ARG A 122 ? 0.5220 0.3895 0.4040 -0.1378 0.0882  0.0344  122 ARG A NE  
924  C CZ  A ARG A 122 ? 0.4856 0.3901 0.4258 -0.1539 0.1006  0.0012  122 ARG A CZ  
925  C CZ  B ARG A 122 ? 0.5527 0.4162 0.4478 -0.1593 0.1169  0.0321  122 ARG A CZ  
926  N NH1 A ARG A 122 ? 0.4733 0.4128 0.4343 -0.1631 0.1118  -0.0193 122 ARG A NH1 
927  N NH1 B ARG A 122 ? 0.5527 0.4174 0.4986 -0.1735 0.1271  0.0140  122 ARG A NH1 
928  N NH2 A ARG A 122 ? 0.4991 0.3837 0.4671 -0.1602 0.1038  -0.0023 122 ARG A NH2 
929  N NH2 B ARG A 122 ? 0.5877 0.4493 0.4485 -0.1659 0.1366  0.0450  122 ARG A NH2 
930  N N   . PRO A 123 ? 0.3525 0.2934 0.2698 -0.0626 0.0084  0.0121  123 PRO A N   
931  C CA  . PRO A 123 ? 0.3334 0.2866 0.2632 -0.0524 0.0049  0.0091  123 PRO A CA  
932  C C   . PRO A 123 ? 0.3444 0.2984 0.2616 -0.0532 0.0024  0.0059  123 PRO A C   
933  O O   . PRO A 123 ? 0.3398 0.2930 0.2646 -0.0440 -0.0060 0.0031  123 PRO A O   
934  C CB  . PRO A 123 ? 0.3171 0.2931 0.2686 -0.0506 0.0118  0.0002  123 PRO A CB  
935  C CG  . PRO A 123 ? 0.3190 0.3005 0.2732 -0.0529 0.0133  -0.0044 123 PRO A CG  
936  C CD  . PRO A 123 ? 0.3433 0.3040 0.2806 -0.0667 0.0154  0.0000  123 PRO A CD  
937  N N   . PHE A 124 ? 0.3590 0.3197 0.2598 -0.0626 0.0102  0.0026  124 PHE A N   
938  C CA  . PHE A 124 ? 0.3752 0.3457 0.2599 -0.0585 0.0067  -0.0043 124 PHE A CA  
939  C C   . PHE A 124 ? 0.3997 0.3521 0.2558 -0.0471 -0.0063 0.0036  124 PHE A C   
940  O O   . PHE A 124 ? 0.4027 0.3695 0.2629 -0.0347 -0.0180 -0.0100 124 PHE A O   
941  C CB  . PHE A 124 ? 0.3982 0.3798 0.2612 -0.0695 0.0205  -0.0066 124 PHE A CB  
942  C CG  . PHE A 124 ? 0.4420 0.3967 0.2643 -0.0773 0.0312  0.0132  124 PHE A CG  
943  C CD1 . PHE A 124 ? 0.4433 0.3855 0.2777 -0.0925 0.0448  0.0188  124 PHE A CD1 
944  C CD2 . PHE A 124 ? 0.4889 0.4307 0.2633 -0.0673 0.0286  0.0252  124 PHE A CD2 
945  C CE1 . PHE A 124 ? 0.4883 0.4001 0.2957 -0.1020 0.0598  0.0374  124 PHE A CE1 
946  C CE2 . PHE A 124 ? 0.5410 0.4493 0.2762 -0.0729 0.0430  0.0499  124 PHE A CE2 
947  C CZ  . PHE A 124 ? 0.5401 0.4304 0.2957 -0.0925 0.0608  0.0568  124 PHE A CZ  
948  N N   . ALA A 125 ? 0.4207 0.3435 0.2537 -0.0493 -0.0056 0.0216  125 ALA A N   
949  C CA  . ALA A 125 ? 0.4524 0.3536 0.2569 -0.0351 -0.0198 0.0306  125 ALA A CA  
950  C C   . ALA A 125 ? 0.4221 0.3296 0.2594 -0.0240 -0.0353 0.0192  125 ALA A C   
951  O O   . ALA A 125 ? 0.4339 0.3455 0.2647 -0.0080 -0.0512 0.0103  125 ALA A O   
952  C CB  . ALA A 125 ? 0.4879 0.3512 0.2679 -0.0414 -0.0124 0.0528  125 ALA A CB  
953  N N   . PHE A 126 ? 0.3874 0.2990 0.2598 -0.0302 -0.0299 0.0177  126 PHE A N   
954  C CA  . PHE A 126 ? 0.3630 0.2818 0.2688 -0.0215 -0.0370 0.0091  126 PHE A CA  
955  C C   . PHE A 126 ? 0.3500 0.2925 0.2851 -0.0155 -0.0397 -0.0106 126 PHE A C   
956  O O   . PHE A 126 ? 0.3487 0.2968 0.3021 -0.0054 -0.0504 -0.0238 126 PHE A O   
957  C CB  . PHE A 126 ? 0.3371 0.2604 0.2671 -0.0257 -0.0263 0.0136  126 PHE A CB  
958  C CG  . PHE A 126 ? 0.3207 0.2514 0.2823 -0.0171 -0.0258 0.0093  126 PHE A CG  
959  C CD1 . PHE A 126 ? 0.3073 0.2521 0.3040 -0.0157 -0.0152 0.0026  126 PHE A CD1 
960  C CD2 . PHE A 126 ? 0.3257 0.2485 0.2864 -0.0111 -0.0327 0.0115  126 PHE A CD2 
961  C CE1 . PHE A 126 ? 0.2984 0.2470 0.3274 -0.0097 -0.0074 0.0013  126 PHE A CE1 
962  C CE2 . PHE A 126 ? 0.3128 0.2454 0.3030 -0.0041 -0.0277 0.0073  126 PHE A CE2 
963  C CZ  . PHE A 126 ? 0.3001 0.2444 0.3237 -0.0041 -0.0129 0.0039  126 PHE A CZ  
964  N N   . TYR A 127 ? 0.3396 0.2982 0.2862 -0.0218 -0.0301 -0.0174 127 TYR A N   
965  C CA  . TYR A 127 ? 0.3296 0.3121 0.3164 -0.0176 -0.0308 -0.0410 127 TYR A CA  
966  C C   . TYR A 127 ? 0.3541 0.3542 0.3204 -0.0078 -0.0453 -0.0597 127 TYR A C   
967  O O   . TYR A 127 ? 0.3456 0.3715 0.3514 -0.0015 -0.0504 -0.0883 127 TYR A O   
968  C CB  . TYR A 127 ? 0.3138 0.3060 0.3291 -0.0255 -0.0151 -0.0425 127 TYR A CB  
969  C CG  . TYR A 127 ? 0.2974 0.2774 0.3332 -0.0263 -0.0019 -0.0262 127 TYR A CG  
970  C CD1 . TYR A 127 ? 0.2921 0.2699 0.3711 -0.0216 0.0060  -0.0284 127 TYR A CD1 
971  C CD2 . TYR A 127 ? 0.2988 0.2722 0.3112 -0.0297 0.0036  -0.0103 127 TYR A CD2 
972  C CE1 . TYR A 127 ? 0.2879 0.2549 0.3753 -0.0178 0.0209  -0.0091 127 TYR A CE1 
973  C CE2 . TYR A 127 ? 0.2917 0.2600 0.3147 -0.0233 0.0130  0.0029  127 TYR A CE2 
974  C CZ  . TYR A 127 ? 0.2883 0.2520 0.3431 -0.0161 0.0222  0.0066  127 TYR A CZ  
975  O OH  . TYR A 127 ? 0.2910 0.2500 0.3468 -0.0054 0.0343  0.0240  127 TYR A OH  
976  N N   . GLY A 128 ? 0.3886 0.3756 0.2948 -0.0045 -0.0507 -0.0448 128 GLY A N   
977  C CA  . GLY A 128 ? 0.4266 0.4305 0.2970 0.0111  -0.0638 -0.0573 128 GLY A CA  
978  C C   . GLY A 128 ? 0.4250 0.4604 0.3037 0.0076  -0.0567 -0.0751 128 GLY A C   
979  O O   . GLY A 128 ? 0.4364 0.5048 0.3199 0.0233  -0.0698 -0.1036 128 GLY A O   
980  N N   . VAL A 129 ? 0.4121 0.4424 0.2956 -0.0107 -0.0378 -0.0631 129 VAL A N   
981  C CA  . VAL A 129 ? 0.4115 0.4728 0.3089 -0.0154 -0.0301 -0.0817 129 VAL A CA  
982  C C   . VAL A 129 ? 0.4341 0.4866 0.2887 -0.0289 -0.0126 -0.0616 129 VAL A C   
983  O O   . VAL A 129 ? 0.4544 0.4750 0.2745 -0.0351 -0.0055 -0.0341 129 VAL A O   
984  C CB  . VAL A 129 ? 0.3677 0.4389 0.3369 -0.0233 -0.0234 -0.0971 129 VAL A CB  
985  C CG1 . VAL A 129 ? 0.3551 0.4371 0.3779 -0.0129 -0.0341 -0.1212 129 VAL A CG1 
986  C CG2 . VAL A 129 ? 0.3476 0.3908 0.3236 -0.0351 -0.0107 -0.0715 129 VAL A CG2 
987  N N   . SER A 130 ? 0.4363 0.5188 0.3001 -0.0338 -0.0042 -0.0787 130 SER A N   
988  C CA  . SER A 130 ? 0.4577 0.5380 0.2945 -0.0495 0.0163  -0.0657 130 SER A CA  
989  C C   . SER A 130 ? 0.4181 0.4919 0.2988 -0.0647 0.0256  -0.0645 130 SER A C   
990  O O   . SER A 130 ? 0.3805 0.4498 0.3042 -0.0607 0.0178  -0.0692 130 SER A O   
991  C CB  . SER A 130 ? 0.4839 0.6053 0.3078 -0.0460 0.0214  -0.0876 130 SER A CB  
992  O OG  . SER A 130 ? 0.4512 0.6047 0.3368 -0.0455 0.0154  -0.1205 130 SER A OG  
993  N N   . THR A 131 ? 0.4287 0.5028 0.2976 -0.0801 0.0438  -0.0583 131 THR A N   
994  C CA  . THR A 131 ? 0.3994 0.4786 0.3081 -0.0900 0.0504  -0.0649 131 THR A CA  
995  C C   . THR A 131 ? 0.3903 0.5079 0.3304 -0.0895 0.0519  -0.0934 131 THR A C   
996  O O   . THR A 131 ? 0.4000 0.5408 0.3324 -0.0829 0.0484  -0.1086 131 THR A O   
997  C CB  . THR A 131 ? 0.4160 0.4825 0.3095 -0.1075 0.0693  -0.0533 131 THR A CB  
998  O OG1 . THR A 131 ? 0.4494 0.5309 0.3149 -0.1171 0.0880  -0.0559 131 THR A OG1 
999  C CG2 . THR A 131 ? 0.4343 0.4608 0.3026 -0.1075 0.0677  -0.0274 131 THR A CG2 
1000 N N   . CYS A 132 ? 0.3729 0.5010 0.3492 -0.0932 0.0553  -0.1040 132 CYS A N   
1001 C CA  . CYS A 132 ? 0.3658 0.5282 0.3783 -0.0904 0.0548  -0.1324 132 CYS A CA  
1002 C C   . CYS A 132 ? 0.3924 0.5867 0.3880 -0.1027 0.0702  -0.1488 132 CYS A C   
1003 O O   . CYS A 132 ? 0.3857 0.6138 0.4046 -0.0985 0.0680  -0.1758 132 CYS A O   
1004 C CB  . CYS A 132 ? 0.3435 0.5076 0.3946 -0.0851 0.0519  -0.1384 132 CYS A CB  
1005 S SG  . CYS A 132 ? 0.3539 0.5360 0.4077 -0.1001 0.0659  -0.1495 132 CYS A SG  
1006 N N   . ASN A 133 ? 0.4280 0.6115 0.3870 -0.1177 0.0883  -0.1330 133 ASN A N   
1007 C CA  . ASN A 133 ? 0.4683 0.6793 0.4096 -0.1315 0.1112  -0.1440 133 ASN A CA  
1008 C C   . ASN A 133 ? 0.5351 0.7356 0.4110 -0.1309 0.1235  -0.1225 133 ASN A C   
1009 O O   . ASN A 133 ? 0.5697 0.7842 0.4197 -0.1431 0.1500  -0.1214 133 ASN A O   
1010 C CB  . ASN A 133 ? 0.4653 0.6768 0.4272 -0.1513 0.1311  -0.1474 133 ASN A CB  
1011 C CG  . ASN A 133 ? 0.4839 0.6519 0.4214 -0.1615 0.1422  -0.1169 133 ASN A CG  
1012 O OD1 . ASN A 133 ? 0.4866 0.6212 0.3955 -0.1511 0.1297  -0.0922 133 ASN A OD1 
1013 N ND2 . ASN A 133 ? 0.4990 0.6692 0.4556 -0.1821 0.1659  -0.1227 133 ASN A ND2 
1014 N N   . THR A 134 ? 0.5620 0.7386 0.4105 -0.1148 0.1058  -0.1053 134 THR A N   
1015 C CA  . THR A 134 ? 0.6415 0.8073 0.4219 -0.1051 0.1116  -0.0843 134 THR A CA  
1016 C C   . THR A 134 ? 0.6570 0.8387 0.4315 -0.0790 0.0832  -0.0983 134 THR A C   
1017 O O   . THR A 134 ? 0.6082 0.7915 0.4328 -0.0725 0.0621  -0.1140 134 THR A O   
1018 C CB  . THR A 134 ? 0.6711 0.7816 0.4169 -0.1098 0.1194  -0.0447 134 THR A CB  
1019 O OG1 . THR A 134 ? 0.6378 0.7255 0.4102 -0.1010 0.0941  -0.0415 134 THR A OG1 
1020 C CG2 . THR A 134 ? 0.6801 0.7743 0.4415 -0.1366 0.1492  -0.0351 134 THR A CG2 
1021 N N   . THR A 135 ? 0.7402 0.9355 0.4548 -0.0626 0.0848  -0.0938 135 THR A N   
1022 C CA  . THR A 135 ? 0.7766 0.9826 0.4748 -0.0338 0.0566  -0.1044 135 THR A CA  
1023 C C   . THR A 135 ? 0.8540 1.0123 0.4878 -0.0237 0.0574  -0.0634 135 THR A C   
1024 O O   . THR A 135 ? 0.8803 0.9979 0.4897 -0.0411 0.0817  -0.0288 135 THR A O   
1025 C CB  . THR A 135 ? 0.8105 1.0750 0.4837 -0.0135 0.0522  -0.1351 135 THR A CB  
1026 O OG1 . THR A 135 ? 0.8812 1.1446 0.4790 -0.0145 0.0813  -0.1093 135 THR A OG1 
1027 C CG2 . THR A 135 ? 0.7620 1.0732 0.5075 -0.0222 0.0493  -0.1796 135 THR A CG2 
1028 N N   . GLU A 136 ? 0.9087 1.0726 0.5210 0.0051  0.0307  -0.0703 136 GLU A N   
1029 C CA  . GLU A 136 ? 0.9896 1.1084 0.5414 0.0206  0.0266  -0.0337 136 GLU A CA  
1030 C C   . GLU A 136 ? 1.0974 1.2071 0.5538 0.0351  0.0480  -0.0021 136 GLU A C   
1031 O O   . GLU A 136 ? 1.1571 1.2206 0.5575 0.0485  0.0497  0.0353  136 GLU A O   
1032 C CB  . GLU A 136 ? 0.9911 1.1223 0.5566 0.0495  -0.0110 -0.0563 136 GLU A CB  
1033 C CG  . GLU A 136 ? 0.9211 1.0490 0.5751 0.0356  -0.0254 -0.0773 136 GLU A CG  
1034 C CD  . GLU A 136 ? 0.9172 0.9884 0.5787 0.0195  -0.0193 -0.0437 136 GLU A CD  
1035 O OE1 . GLU A 136 ? 0.9650 0.9983 0.5835 0.0082  0.0016  -0.0071 136 GLU A OE1 
1036 O OE2 . GLU A 136 ? 0.8753 0.9414 0.5906 0.0179  -0.0337 -0.0558 136 GLU A OE2 
1037 N N   . GLN A 137 ? 1.1365 1.2884 0.5735 0.0340  0.0660  -0.0155 137 GLN A N   
1038 C CA  . GLN A 137 ? 1.2425 1.3828 0.5892 0.0426  0.0981  0.0205  137 GLN A CA  
1039 C C   . GLN A 137 ? 1.2665 1.3480 0.6147 0.0062  0.1399  0.0631  137 GLN A C   
1040 O O   . GLN A 137 ? 1.3562 1.3971 0.6333 0.0112  0.1690  0.1086  137 GLN A O   
1041 C CB  . GLN A 137 ? 1.2663 1.4747 0.5970 0.0500  0.1087  -0.0096 137 GLN A CB  
1042 C CG  . GLN A 137 ? 1.2360 1.4577 0.6143 0.0100  0.1428  -0.0183 137 GLN A CG  
1043 C CD  . GLN A 137 ? 1.2428 1.5413 0.6235 0.0185  0.1452  -0.0605 137 GLN A CD  
1044 O OE1 . GLN A 137 ? 1.3035 1.6408 0.6202 0.0545  0.1363  -0.0692 137 GLN A OE1 
1045 N NE2 . GLN A 137 ? 1.1835 1.5077 0.6379 -0.0114 0.1559  -0.0897 137 GLN A NE2 
1046 N N   . ASP A 138 ? 0.8762 1.1618 0.6339 -0.1556 -0.0782 -0.0754 138 ASP A N   
1047 C CA  . ASP A 138 ? 0.8751 1.1345 0.6316 -0.1502 -0.0790 -0.0527 138 ASP A CA  
1048 C C   . ASP A 138 ? 0.8603 1.0868 0.6341 -0.1349 -0.0959 -0.0324 138 ASP A C   
1049 O O   . ASP A 138 ? 0.8534 1.0709 0.6499 -0.1236 -0.0980 -0.0435 138 ASP A O   
1050 C CB  . ASP A 138 ? 0.8583 1.1051 0.6351 -0.1416 -0.0563 -0.0698 138 ASP A CB  
1051 C CG  . ASP A 138 ? 0.8747 1.1532 0.6486 -0.1527 -0.0374 -0.0994 138 ASP A CG  
1052 O OD1 . ASP A 138 ? 0.9050 1.2179 0.6504 -0.1717 -0.0391 -0.1007 138 ASP A OD1 
1053 O OD2 . ASP A 138 ? 0.8591 1.1290 0.6608 -0.1427 -0.0210 -0.1215 138 ASP A OD2 
1054 N N   . LYS A 139 ? 0.8516 1.0610 0.6170 -0.1349 -0.1073 -0.0044 139 LYS A N   
1055 C CA  . LYS A 139 ? 0.8271 1.0070 0.6117 -0.1209 -0.1240 0.0132  139 LYS A CA  
1056 C C   . LYS A 139 ? 0.7856 0.9359 0.5845 -0.1104 -0.1176 0.0222  139 LYS A C   
1057 O O   . LYS A 139 ? 0.7981 0.9486 0.5817 -0.1184 -0.1132 0.0332  139 LYS A O   
1058 C CB  . LYS A 139 ? 0.8665 1.0520 0.6342 -0.1297 -0.1503 0.0404  139 LYS A CB  
1059 C CG  . LYS A 139 ? 0.8678 1.0392 0.6597 -0.1167 -0.1691 0.0454  139 LYS A CG  
1060 C CD  . LYS A 139 ? 0.8625 1.0497 0.6662 -0.1130 -0.1631 0.0185  139 LYS A CD  
1061 C CE  . LYS A 139 ? 0.8739 1.0581 0.6952 -0.1054 -0.1852 0.0248  139 LYS A CE  
1062 N NZ  . LYS A 139 ? 0.8662 1.0653 0.7011 -0.1021 -0.1777 -0.0028 139 LYS A NZ  
1063 N N   . LEU A 140 ? 0.7292 0.8567 0.5578 -0.0935 -0.1167 0.0161  140 LEU A N   
1064 C CA  . LEU A 140 ? 0.6842 0.7857 0.5292 -0.0827 -0.1108 0.0214  140 LEU A CA  
1065 C C   . LEU A 140 ? 0.6487 0.7298 0.5146 -0.0718 -0.1282 0.0335  140 LEU A C   
1066 O O   . LEU A 140 ? 0.6456 0.7312 0.5212 -0.0684 -0.1397 0.0301  140 LEU A O   
1067 C CB  . LEU A 140 ? 0.6668 0.7631 0.5305 -0.0733 -0.0903 -0.0011 140 LEU A CB  
1068 C CG  . LEU A 140 ? 0.6736 0.7894 0.5282 -0.0809 -0.0719 -0.0198 140 LEU A CG  
1069 C CD1 . LEU A 140 ? 0.6559 0.7641 0.5356 -0.0703 -0.0573 -0.0405 140 LEU A CD1 
1070 C CD2 . LEU A 140 ? 0.6792 0.7974 0.5195 -0.0878 -0.0633 -0.0130 140 LEU A CD2 
1071 N N   . SER A 141 ? 0.6168 0.6772 0.4921 -0.0663 -0.1302 0.0457  141 SER A N   
1072 C CA  . SER A 141 ? 0.5953 0.6366 0.4974 -0.0545 -0.1438 0.0518  141 SER A CA  
1073 C C   . SER A 141 ? 0.5473 0.5866 0.4732 -0.0428 -0.1339 0.0300  141 SER A C   
1074 O O   . SER A 141 ? 0.5198 0.5604 0.4464 -0.0409 -0.1148 0.0158  141 SER A O   
1075 C CB  . SER A 141 ? 0.5977 0.6192 0.5076 -0.0512 -0.1434 0.0634  141 SER A CB  
1076 O OG  . SER A 141 ? 0.6109 0.6161 0.5497 -0.0404 -0.1571 0.0669  141 SER A OG  
1077 N N   . LYS A 142 ? 0.5269 0.5639 0.4734 -0.0357 -0.1475 0.0279  142 LYS A N   
1078 C CA  . LYS A 142 ? 0.4977 0.5358 0.4666 -0.0267 -0.1392 0.0074  142 LYS A CA  
1079 C C   . LYS A 142 ? 0.4644 0.4865 0.4594 -0.0159 -0.1347 0.0027  142 LYS A C   
1080 O O   . LYS A 142 ? 0.4383 0.4617 0.4485 -0.0106 -0.1233 -0.0135 142 LYS A O   
1081 C CB  . LYS A 142 ? 0.5123 0.5609 0.4918 -0.0253 -0.1552 0.0042  142 LYS A CB  
1082 C CG  . LYS A 142 ? 0.5350 0.6053 0.4910 -0.0362 -0.1568 0.0018  142 LYS A CG  
1083 C CD  . LYS A 142 ? 0.5521 0.6336 0.5199 -0.0346 -0.1752 0.0002  142 LYS A CD  
1084 C CE  . LYS A 142 ? 0.5695 0.6761 0.5194 -0.0445 -0.1719 -0.0111 142 LYS A CE  
1085 N NZ  . LYS A 142 ? 0.5907 0.7098 0.5055 -0.0586 -0.1685 -0.0020 142 LYS A NZ  
1086 N N   . ASN A 143 ? 0.4583 0.4668 0.4586 -0.0140 -0.1435 0.0167  143 ASN A N   
1087 C CA  A ASN A 143 ? 0.4405 0.4369 0.4677 -0.0046 -0.1416 0.0109  143 ASN A CA  
1088 C CA  B ASN A 143 ? 0.4419 0.4381 0.4693 -0.0046 -0.1421 0.0112  143 ASN A CA  
1089 C C   . ASN A 143 ? 0.4343 0.4194 0.4547 -0.0062 -0.1349 0.0197  143 ASN A C   
1090 O O   . ASN A 143 ? 0.4466 0.4332 0.4417 -0.0144 -0.1304 0.0297  143 ASN A O   
1091 C CB  A ASN A 143 ? 0.4496 0.4414 0.5048 0.0019  -0.1625 0.0136  143 ASN A CB  
1092 C CB  B ASN A 143 ? 0.4539 0.4449 0.5079 0.0014  -0.1640 0.0157  143 ASN A CB  
1093 C CG  A ASN A 143 ? 0.4773 0.4638 0.5237 -0.0031 -0.1837 0.0365  143 ASN A CG  
1094 C CG  B ASN A 143 ? 0.4561 0.4596 0.5235 0.0046  -0.1706 0.0041  143 ASN A CG  
1095 O OD1 A ASN A 143 ? 0.4897 0.4756 0.5082 -0.0126 -0.1815 0.0509  143 ASN A OD1 
1096 O OD1 B ASN A 143 ? 0.4422 0.4504 0.5291 0.0104  -0.1614 -0.0144 143 ASN A OD1 
1097 N ND2 A ASN A 143 ? 0.4896 0.4730 0.5612 0.0024  -0.2047 0.0406  143 ASN A ND2 
1098 N ND2 B ASN A 143 ? 0.4766 0.4873 0.5332 -0.0001 -0.1869 0.0152  143 ASN A ND2 
1099 N N   . GLY A 144 ? 0.4112 0.3876 0.4548 0.0008  -0.1332 0.0138  144 GLY A N   
1100 C CA  . GLY A 144 ? 0.3970 0.3644 0.4373 -0.0003 -0.1263 0.0193  144 GLY A CA  
1101 C C   . GLY A 144 ? 0.3723 0.3456 0.3987 -0.0019 -0.1049 0.0110  144 GLY A C   
1102 O O   . GLY A 144 ? 0.3650 0.3354 0.3781 -0.0058 -0.0979 0.0177  144 GLY A O   
1103 N N   . SER A 145 ? 0.3512 0.3330 0.3831 0.0008  -0.0955 -0.0032 145 SER A N   
1104 C CA  . SER A 145 ? 0.3365 0.3235 0.3571 -0.0009 -0.0773 -0.0096 145 SER A CA  
1105 C C   . SER A 145 ? 0.3187 0.3028 0.3452 0.0011  -0.0674 -0.0117 145 SER A C   
1106 O O   . SER A 145 ? 0.3082 0.2936 0.3225 -0.0011 -0.0558 -0.0098 145 SER A O   
1107 C CB  . SER A 145 ? 0.3289 0.3241 0.3575 0.0006  -0.0713 -0.0231 145 SER A CB  
1108 O OG  . SER A 145 ? 0.3313 0.3304 0.3470 -0.0027 -0.0577 -0.0259 145 SER A OG  
1109 N N   . TYR A 146 ? 0.3121 0.2941 0.3592 0.0054  -0.0727 -0.0166 146 TYR A N   
1110 C CA  . TYR A 146 ? 0.3009 0.2855 0.3562 0.0068  -0.0633 -0.0227 146 TYR A CA  
1111 C C   . TYR A 146 ? 0.3039 0.2813 0.3660 0.0072  -0.0698 -0.0175 146 TYR A C   
1112 O O   . TYR A 146 ? 0.3143 0.2862 0.3944 0.0100  -0.0828 -0.0180 146 TYR A O   
1113 C CB  . TYR A 146 ? 0.2921 0.2854 0.3690 0.0100  -0.0617 -0.0382 146 TYR A CB  
1114 C CG  . TYR A 146 ? 0.2817 0.2835 0.3656 0.0092  -0.0511 -0.0464 146 TYR A CG  
1115 C CD1 . TYR A 146 ? 0.2742 0.2833 0.3470 0.0058  -0.0374 -0.0470 146 TYR A CD1 
1116 C CD2 . TYR A 146 ? 0.2816 0.2856 0.3850 0.0112  -0.0555 -0.0541 146 TYR A CD2 
1117 C CE1 . TYR A 146 ? 0.2682 0.2882 0.3449 0.0033  -0.0287 -0.0527 146 TYR A CE1 
1118 C CE2 . TYR A 146 ? 0.2749 0.2913 0.3833 0.0089  -0.0455 -0.0633 146 TYR A CE2 
1119 C CZ  . TYR A 146 ? 0.2687 0.2940 0.3616 0.0044  -0.0323 -0.0616 146 TYR A CZ  
1120 O OH  . TYR A 146 ? 0.2656 0.3059 0.3608 0.0003  -0.0234 -0.0688 146 TYR A OH  
1121 N N   . PRO A 147 ? 0.3057 0.2830 0.3570 0.0045  -0.0616 -0.0128 147 PRO A N   
1122 C CA  . PRO A 147 ? 0.3016 0.2838 0.3342 0.0018  -0.0486 -0.0098 147 PRO A CA  
1123 C C   . PRO A 147 ? 0.3138 0.2921 0.3269 -0.0021 -0.0501 0.0011  147 PRO A C   
1124 O O   . PRO A 147 ? 0.3319 0.3041 0.3425 -0.0041 -0.0613 0.0087  147 PRO A O   
1125 C CB  . PRO A 147 ? 0.2968 0.2817 0.3303 0.0008  -0.0429 -0.0094 147 PRO A CB  
1126 C CG  . PRO A 147 ? 0.3043 0.2809 0.3483 0.0009  -0.0539 -0.0063 147 PRO A CG  
1127 C CD  . PRO A 147 ? 0.3094 0.2827 0.3711 0.0045  -0.0650 -0.0120 147 PRO A CD  
1128 N N   . SER A 148 ? 0.3107 0.2936 0.3113 -0.0039 -0.0392 0.0016  148 SER A N   
1129 C CA  . SER A 148 ? 0.3209 0.3049 0.3044 -0.0086 -0.0379 0.0080  148 SER A CA  
1130 C C   . SER A 148 ? 0.3283 0.3103 0.3036 -0.0126 -0.0383 0.0171  148 SER A C   
1131 O O   . SER A 148 ? 0.3141 0.2986 0.2910 -0.0117 -0.0309 0.0168  148 SER A O   
1132 C CB  . SER A 148 ? 0.3153 0.3053 0.2951 -0.0084 -0.0259 0.0026  148 SER A CB  
1133 O OG  . SER A 148 ? 0.3243 0.3187 0.2906 -0.0133 -0.0225 0.0053  148 SER A OG  
1134 N N   . GLY A 149 ? 0.3433 0.3220 0.3099 -0.0179 -0.0476 0.0261  149 GLY A N   
1135 C CA  . GLY A 149 ? 0.3546 0.3321 0.3120 -0.0241 -0.0479 0.0358  149 GLY A CA  
1136 C C   . GLY A 149 ? 0.3546 0.3424 0.3002 -0.0275 -0.0352 0.0337  149 GLY A C   
1137 O O   . GLY A 149 ? 0.3455 0.3352 0.2922 -0.0281 -0.0297 0.0350  149 GLY A O   
1138 N N   . HIS A 150 ? 0.3634 0.3594 0.3006 -0.0295 -0.0308 0.0285  150 HIS A N   
1139 C CA  . HIS A 150 ? 0.3677 0.3751 0.2990 -0.0321 -0.0187 0.0230  150 HIS A CA  
1140 C C   . HIS A 150 ? 0.3478 0.3551 0.2926 -0.0247 -0.0097 0.0177  150 HIS A C   
1141 O O   . HIS A 150 ? 0.3448 0.3582 0.2894 -0.0260 -0.0029 0.0176  150 HIS A O   
1142 C CB  . HIS A 150 ? 0.3815 0.3981 0.3076 -0.0344 -0.0152 0.0141  150 HIS A CB  
1143 C CG  . HIS A 150 ? 0.3879 0.4168 0.3147 -0.0361 -0.0025 0.0046  150 HIS A CG  
1144 N ND1 . HIS A 150 ? 0.4094 0.4523 0.3227 -0.0459 0.0012  0.0040  150 HIS A ND1 
1145 C CD2 . HIS A 150 ? 0.3850 0.4150 0.3269 -0.0294 0.0067  -0.0048 150 HIS A CD2 
1146 C CE1 . HIS A 150 ? 0.4051 0.4581 0.3277 -0.0443 0.0128  -0.0080 150 HIS A CE1 
1147 N NE2 . HIS A 150 ? 0.3911 0.4350 0.3321 -0.0338 0.0155  -0.0126 150 HIS A NE2 
1148 N N   . THR A 151 ? 0.3328 0.3346 0.2893 -0.0178 -0.0102 0.0136  151 THR A N   
1149 C CA  . THR A 151 ? 0.3193 0.3218 0.2871 -0.0122 -0.0035 0.0113  151 THR A CA  
1150 C C   . THR A 151 ? 0.3128 0.3148 0.2826 -0.0120 -0.0050 0.0168  151 THR A C   
1151 O O   . THR A 151 ? 0.3023 0.3095 0.2762 -0.0102 0.0006  0.0173  151 THR A O   
1152 C CB  . THR A 151 ? 0.3149 0.3137 0.2927 -0.0076 -0.0039 0.0067  151 THR A CB  
1153 O OG1 . THR A 151 ? 0.3222 0.3220 0.2999 -0.0082 -0.0020 0.0003  151 THR A OG1 
1154 C CG2 . THR A 151 ? 0.3081 0.3091 0.2953 -0.0039 0.0020  0.0073  151 THR A CG2 
1155 N N   . SER A 152 ? 0.3116 0.3079 0.2811 -0.0137 -0.0134 0.0202  152 SER A N   
1156 C CA  . SER A 152 ? 0.3075 0.3036 0.2809 -0.0146 -0.0150 0.0234  152 SER A CA  
1157 C C   . SER A 152 ? 0.3104 0.3116 0.2756 -0.0196 -0.0112 0.0281  152 SER A C   
1158 O O   . SER A 152 ? 0.3004 0.3075 0.2698 -0.0189 -0.0071 0.0281  152 SER A O   
1159 C CB  . SER A 152 ? 0.3141 0.3013 0.2933 -0.0156 -0.0256 0.0252  152 SER A CB  
1160 O OG  . SER A 152 ? 0.3127 0.3002 0.2988 -0.0168 -0.0267 0.0259  152 SER A OG  
1161 N N   . ILE A 153 ? 0.3221 0.3240 0.2758 -0.0257 -0.0123 0.0314  153 ILE A N   
1162 C CA  . ILE A 153 ? 0.3310 0.3416 0.2767 -0.0322 -0.0071 0.0340  153 ILE A CA  
1163 C C   . ILE A 153 ? 0.3224 0.3435 0.2745 -0.0278 0.0032  0.0268  153 ILE A C   
1164 O O   . ILE A 153 ? 0.3193 0.3476 0.2752 -0.0284 0.0074  0.0271  153 ILE A O   
1165 C CB  . ILE A 153 ? 0.3477 0.3618 0.2776 -0.0416 -0.0090 0.0376  153 ILE A CB  
1166 C CG1 . ILE A 153 ? 0.3618 0.3646 0.2870 -0.0468 -0.0217 0.0487  153 ILE A CG1 
1167 C CG2 . ILE A 153 ? 0.3541 0.3821 0.2768 -0.0494 -0.0009 0.0371  153 ILE A CG2 
1168 C CD1 . ILE A 153 ? 0.3807 0.3870 0.2894 -0.0556 -0.0267 0.0542  153 ILE A CD1 
1169 N N   . GLY A 154 ? 0.3185 0.3403 0.2745 -0.0233 0.0065  0.0205  154 GLY A N   
1170 C CA  . GLY A 154 ? 0.3118 0.3407 0.2791 -0.0182 0.0147  0.0143  154 GLY A CA  
1171 C C   . GLY A 154 ? 0.3027 0.3324 0.2807 -0.0127 0.0151  0.0176  154 GLY A C   
1172 O O   . GLY A 154 ? 0.2999 0.3384 0.2852 -0.0114 0.0194  0.0168  154 GLY A O   
1173 N N   . TRP A 155 ? 0.2963 0.3194 0.2760 -0.0100 0.0102  0.0207  155 TRP A N   
1174 C CA  . TRP A 155 ? 0.2908 0.3182 0.2783 -0.0065 0.0103  0.0236  155 TRP A CA  
1175 C C   . TRP A 155 ? 0.2912 0.3246 0.2771 -0.0099 0.0090  0.0261  155 TRP A C   
1176 O O   . TRP A 155 ? 0.2873 0.3300 0.2794 -0.0081 0.0113  0.0276  155 TRP A O   
1177 C CB  . TRP A 155 ? 0.2888 0.3119 0.2784 -0.0047 0.0069  0.0234  155 TRP A CB  
1178 C CG  . TRP A 155 ? 0.2841 0.3154 0.2796 -0.0027 0.0078  0.0265  155 TRP A CG  
1179 C CD1 . TRP A 155 ? 0.2831 0.3206 0.2788 -0.0046 0.0052  0.0260  155 TRP A CD1 
1180 C CD2 . TRP A 155 ? 0.2845 0.3205 0.2876 0.0005  0.0107  0.0310  155 TRP A CD2 
1181 N NE1 . TRP A 155 ? 0.2833 0.3314 0.2823 -0.0038 0.0065  0.0305  155 TRP A NE1 
1182 C CE2 . TRP A 155 ? 0.2827 0.3286 0.2867 -0.0003 0.0090  0.0354  155 TRP A CE2 
1183 C CE3 . TRP A 155 ? 0.2870 0.3202 0.2982 0.0039  0.0140  0.0313  155 TRP A CE3 
1184 C CZ2 . TRP A 155 ? 0.2852 0.3375 0.2960 0.0016  0.0091  0.0436  155 TRP A CZ2 
1185 C CZ3 . TRP A 155 ? 0.2896 0.3268 0.3120 0.0072  0.0142  0.0382  155 TRP A CZ3 
1186 C CH2 . TRP A 155 ? 0.2882 0.3345 0.3092 0.0059  0.0111  0.0459  155 TRP A CH2 
1187 N N   . ALA A 156 ? 0.2954 0.3233 0.2748 -0.0149 0.0046  0.0271  156 ALA A N   
1188 C CA  . ALA A 156 ? 0.2963 0.3282 0.2755 -0.0196 0.0034  0.0291  156 ALA A CA  
1189 C C   . ALA A 156 ? 0.2972 0.3395 0.2757 -0.0221 0.0094  0.0291  156 ALA A C   
1190 O O   . ALA A 156 ? 0.2941 0.3462 0.2784 -0.0223 0.0111  0.0291  156 ALA A O   
1191 C CB  . ALA A 156 ? 0.3050 0.3263 0.2796 -0.0253 -0.0031 0.0320  156 ALA A CB  
1192 N N   . THR A 157 ? 0.3015 0.3443 0.2741 -0.0246 0.0127  0.0275  157 THR A N   
1193 C CA  . THR A 157 ? 0.3031 0.3589 0.2773 -0.0276 0.0197  0.0239  157 THR A CA  
1194 C C   . THR A 157 ? 0.2958 0.3606 0.2859 -0.0194 0.0235  0.0204  157 THR A C   
1195 O O   . THR A 157 ? 0.2969 0.3740 0.2945 -0.0201 0.0268  0.0185  157 THR A O   
1196 C CB  . THR A 157 ? 0.3118 0.3696 0.2773 -0.0323 0.0231  0.0196  157 THR A CB  
1197 O OG1 . THR A 157 ? 0.3194 0.3703 0.2694 -0.0412 0.0176  0.0262  157 THR A OG1 
1198 C CG2 . THR A 157 ? 0.3170 0.3924 0.2872 -0.0359 0.0319  0.0119  157 THR A CG2 
1199 N N   . ALA A 158 ? 0.2884 0.3473 0.2853 -0.0120 0.0225  0.0204  158 ALA A N   
1200 C CA  . ALA A 158 ? 0.2843 0.3494 0.2978 -0.0044 0.0236  0.0208  158 ALA A CA  
1201 C C   . ALA A 158 ? 0.2803 0.3533 0.2973 -0.0036 0.0202  0.0263  158 ALA A C   
1202 O O   . ALA A 158 ? 0.2769 0.3612 0.3068 -0.0003 0.0211  0.0264  158 ALA A O   
1203 C CB  . ALA A 158 ? 0.2824 0.3379 0.3005 0.0010  0.0220  0.0226  158 ALA A CB  
1204 N N   . LEU A 159 ? 0.2791 0.3477 0.2868 -0.0065 0.0159  0.0293  159 LEU A N   
1205 C CA  . LEU A 159 ? 0.2776 0.3561 0.2879 -0.0071 0.0128  0.0321  159 LEU A CA  
1206 C C   . LEU A 159 ? 0.2806 0.3695 0.2931 -0.0116 0.0146  0.0298  159 LEU A C   
1207 O O   . LEU A 159 ? 0.2777 0.3804 0.2985 -0.0101 0.0136  0.0310  159 LEU A O   
1208 C CB  . LEU A 159 ? 0.2779 0.3510 0.2811 -0.0101 0.0087  0.0316  159 LEU A CB  
1209 C CG  . LEU A 159 ? 0.2769 0.3441 0.2790 -0.0070 0.0074  0.0328  159 LEU A CG  
1210 C CD1 . LEU A 159 ? 0.2766 0.3390 0.2749 -0.0103 0.0042  0.0283  159 LEU A CD1 
1211 C CD2 . LEU A 159 ? 0.2762 0.3547 0.2840 -0.0039 0.0065  0.0386  159 LEU A CD2 
1212 N N   . VAL A 160 ? 0.2876 0.3712 0.2924 -0.0179 0.0168  0.0274  160 VAL A N   
1213 C CA  . VAL A 160 ? 0.2929 0.3865 0.2989 -0.0244 0.0196  0.0254  160 VAL A CA  
1214 C C   . VAL A 160 ? 0.2933 0.4010 0.3113 -0.0211 0.0250  0.0211  160 VAL A C   
1215 O O   . VAL A 160 ? 0.2903 0.4127 0.3186 -0.0209 0.0256  0.0196  160 VAL A O   
1216 C CB  . VAL A 160 ? 0.3036 0.3880 0.2969 -0.0341 0.0199  0.0265  160 VAL A CB  
1217 C CG1 . VAL A 160 ? 0.3104 0.4068 0.3043 -0.0429 0.0243  0.0249  160 VAL A CG1 
1218 C CG2 . VAL A 160 ? 0.3062 0.3773 0.2953 -0.0364 0.0130  0.0298  160 VAL A CG2 
1219 N N   . LEU A 161 ? 0.2944 0.3989 0.3141 -0.0181 0.0286  0.0176  161 LEU A N   
1220 C CA  . LEU A 161 ? 0.2941 0.4117 0.3311 -0.0139 0.0338  0.0105  161 LEU A CA  
1221 C C   . LEU A 161 ? 0.2880 0.4127 0.3443 -0.0041 0.0297  0.0138  161 LEU A C   
1222 O O   . LEU A 161 ? 0.2852 0.4251 0.3592 -0.0015 0.0317  0.0091  161 LEU A O   
1223 C CB  . LEU A 161 ? 0.2980 0.4100 0.3361 -0.0120 0.0380  0.0042  161 LEU A CB  
1224 C CG  . LEU A 161 ? 0.3074 0.4222 0.3304 -0.0228 0.0436  -0.0017 161 LEU A CG  
1225 C CD1 . LEU A 161 ? 0.3112 0.4222 0.3361 -0.0206 0.0469  -0.0092 161 LEU A CD1 
1226 C CD2 . LEU A 161 ? 0.3120 0.4473 0.3410 -0.0296 0.0506  -0.0098 161 LEU A CD2 
1227 N N   . ALA A 162 ? 0.2854 0.4007 0.3388 0.0004  0.0236  0.0223  162 ALA A N   
1228 C CA  . ALA A 162 ? 0.2845 0.4070 0.3528 0.0078  0.0179  0.0294  162 ALA A CA  
1229 C C   . ALA A 162 ? 0.2827 0.4218 0.3535 0.0053  0.0150  0.0307  162 ALA A C   
1230 O O   . ALA A 162 ? 0.2840 0.4362 0.3726 0.0106  0.0116  0.0331  162 ALA A O   
1231 C CB  . ALA A 162 ? 0.2848 0.3966 0.3449 0.0097  0.0128  0.0384  162 ALA A CB  
1232 N N   . GLU A 163 ? 0.2815 0.4199 0.3369 -0.0028 0.0157  0.0289  163 GLU A N   
1233 C CA  . GLU A 163 ? 0.2803 0.4346 0.3384 -0.0069 0.0140  0.0276  163 GLU A CA  
1234 C C   . GLU A 163 ? 0.2795 0.4477 0.3507 -0.0084 0.0191  0.0202  163 GLU A C   
1235 O O   . GLU A 163 ? 0.2767 0.4625 0.3602 -0.0074 0.0167  0.0194  163 GLU A O   
1236 C CB  . GLU A 163 ? 0.2825 0.4300 0.3251 -0.0157 0.0138  0.0259  163 GLU A CB  
1237 C CG  . GLU A 163 ? 0.2833 0.4469 0.3302 -0.0207 0.0120  0.0231  163 GLU A CG  
1238 C CD  . GLU A 163 ? 0.2882 0.4434 0.3255 -0.0296 0.0117  0.0198  163 GLU A CD  
1239 O OE1 . GLU A 163 ? 0.2904 0.4552 0.3322 -0.0362 0.0127  0.0156  163 GLU A OE1 
1240 O OE2 . GLU A 163 ? 0.2918 0.4311 0.3202 -0.0299 0.0101  0.0210  163 GLU A OE2 
1241 N N   . ILE A 164 ? 0.2795 0.4424 0.3480 -0.0118 0.0263  0.0138  164 ILE A N   
1242 C CA  . ILE A 164 ? 0.2824 0.4615 0.3624 -0.0154 0.0330  0.0043  164 ILE A CA  
1243 C C   . ILE A 164 ? 0.2801 0.4712 0.3877 -0.0047 0.0327  0.0000  164 ILE A C   
1244 O O   . ILE A 164 ? 0.2759 0.4866 0.4015 -0.0041 0.0342  -0.0063 164 ILE A O   
1245 C CB  . ILE A 164 ? 0.2892 0.4628 0.3553 -0.0249 0.0411  -0.0013 164 ILE A CB  
1246 C CG1 . ILE A 164 ? 0.2936 0.4549 0.3372 -0.0356 0.0392  0.0049  164 ILE A CG1 
1247 C CG2 . ILE A 164 ? 0.2943 0.4891 0.3725 -0.0304 0.0497  -0.0131 164 ILE A CG2 
1248 C CD1 . ILE A 164 ? 0.3034 0.4554 0.3294 -0.0448 0.0435  0.0047  164 ILE A CD1 
1249 N N   . ASN A 165 ? 0.2801 0.4592 0.3937 0.0037  0.0301  0.0033  165 ASN A N   
1250 C CA  . ASN A 165 ? 0.2843 0.4706 0.4285 0.0147  0.0284  0.0000  165 ASN A CA  
1251 C C   . ASN A 165 ? 0.2866 0.4621 0.4361 0.0236  0.0181  0.0145  165 ASN A C   
1252 O O   . ASN A 165 ? 0.2854 0.4467 0.4394 0.0284  0.0180  0.0161  165 ASN A O   
1253 C CB  . ASN A 165 ? 0.2885 0.4728 0.4412 0.0146  0.0373  -0.0135 165 ASN A CB  
1254 C CG  . ASN A 165 ? 0.2918 0.4854 0.4835 0.0256  0.0366  -0.0216 165 ASN A CG  
1255 O OD1 . ASN A 165 ? 0.2925 0.4957 0.5063 0.0332  0.0290  -0.0163 165 ASN A OD1 
1256 N ND2 . ASN A 165 ? 0.2981 0.4901 0.5007 0.0263  0.0441  -0.0355 165 ASN A ND2 
1257 N N   . PRO A 166 ? 0.2912 0.4754 0.4397 0.0246  0.0096  0.0252  166 PRO A N   
1258 C CA  . PRO A 166 ? 0.2975 0.4754 0.4470 0.0301  -0.0003 0.0411  166 PRO A CA  
1259 C C   . PRO A 166 ? 0.3087 0.4843 0.4897 0.0412  -0.0057 0.0457  166 PRO A C   
1260 O O   . PRO A 166 ? 0.3141 0.4774 0.4948 0.0444  -0.0117 0.0585  166 PRO A O   
1261 C CB  . PRO A 166 ? 0.2962 0.4918 0.4406 0.0271  -0.0075 0.0482  166 PRO A CB  
1262 C CG  . PRO A 166 ? 0.2924 0.5047 0.4460 0.0241  -0.0025 0.0356  166 PRO A CG  
1263 C CD  . PRO A 166 ? 0.2890 0.4908 0.4333 0.0187  0.0091  0.0229  166 PRO A CD  
1264 N N   . GLN A 167 ? 0.3144 0.5018 0.5245 0.0465  -0.0036 0.0347  167 GLN A N   
1265 C CA  . GLN A 167 ? 0.3272 0.5113 0.5746 0.0580  -0.0087 0.0359  167 GLN A CA  
1266 C C   . GLN A 167 ? 0.3240 0.4866 0.5733 0.0599  -0.0038 0.0323  167 GLN A C   
1267 O O   . GLN A 167 ? 0.3313 0.4843 0.6073 0.0684  -0.0104 0.0391  167 GLN A O   
1268 C CB  . GLN A 167 ? 0.3387 0.5420 0.6198 0.0627  -0.0051 0.0191  167 GLN A CB  
1269 C CG  . GLN A 167 ? 0.3502 0.5756 0.6432 0.0648  -0.0141 0.0252  167 GLN A CG  
1270 C CD  . GLN A 167 ? 0.3606 0.6074 0.6878 0.0687  -0.0094 0.0059  167 GLN A CD  
1271 O OE1 . GLN A 167 ? 0.3696 0.6261 0.6868 0.0603  0.0035  -0.0118 167 GLN A OE1 
1272 N NE2 . GLN A 167 ? 0.3712 0.6268 0.7403 0.0807  -0.0204 0.0096  167 GLN A NE2 
1273 N N   . ARG A 168 ? 0.3108 0.4656 0.5337 0.0516  0.0067  0.0222  168 ARG A N   
1274 C CA  . ARG A 168 ? 0.3095 0.4455 0.5302 0.0520  0.0111  0.0185  168 ARG A CA  
1275 C C   . ARG A 168 ? 0.2964 0.4183 0.4794 0.0443  0.0116  0.0274  168 ARG A C   
1276 O O   . ARG A 168 ? 0.2918 0.4021 0.4636 0.0410  0.0178  0.0203  168 ARG A O   
1277 C CB  . ARG A 168 ? 0.3138 0.4559 0.5445 0.0499  0.0232  -0.0049 168 ARG A CB  
1278 C CG  . ARG A 168 ? 0.3231 0.4773 0.5999 0.0592  0.0230  -0.0169 168 ARG A CG  
1279 C CD  . ARG A 168 ? 0.3302 0.4950 0.6177 0.0556  0.0363  -0.0434 168 ARG A CD  
1280 N NE  . ARG A 168 ? 0.3377 0.4867 0.6199 0.0541  0.0411  -0.0496 168 ARG A NE  
1281 C CZ  . ARG A 168 ? 0.3451 0.4847 0.6615 0.0626  0.0397  -0.0558 168 ARG A CZ  
1282 N NH1 . ARG A 168 ? 0.3507 0.4930 0.7118 0.0743  0.0325  -0.0552 168 ARG A NH1 
1283 N NH2 . ARG A 168 ? 0.3494 0.4764 0.6572 0.0594  0.0448  -0.0627 168 ARG A NH2 
1284 N N   . GLN A 169 ? 0.2876 0.4126 0.4535 0.0416  0.0046  0.0420  169 GLN A N   
1285 C CA  . GLN A 169 ? 0.2815 0.3968 0.4153 0.0343  0.0050  0.0479  169 GLN A CA  
1286 C C   . GLN A 169 ? 0.2811 0.3781 0.4143 0.0359  0.0046  0.0528  169 GLN A C   
1287 O O   . GLN A 169 ? 0.2757 0.3628 0.3890 0.0308  0.0090  0.0486  169 GLN A O   
1288 C CB  . GLN A 169 ? 0.2811 0.4067 0.4016 0.0310  -0.0024 0.0605  169 GLN A CB  
1289 C CG  . GLN A 169 ? 0.2900 0.4185 0.4232 0.0357  -0.0129 0.0779  169 GLN A CG  
1290 C CD  . GLN A 169 ? 0.2922 0.4366 0.4093 0.0302  -0.0194 0.0879  169 GLN A CD  
1291 O OE1 . GLN A 169 ? 0.2880 0.4378 0.3849 0.0231  -0.0155 0.0806  169 GLN A OE1 
1292 N NE2 . GLN A 169 ? 0.3012 0.4538 0.4283 0.0326  -0.0299 0.1046  169 GLN A NE2 
1293 N N   . ASN A 170 ? 0.2868 0.3791 0.4440 0.0428  -0.0013 0.0619  170 ASN A N   
1294 C CA  . ASN A 170 ? 0.2938 0.3688 0.4525 0.0433  -0.0022 0.0683  170 ASN A CA  
1295 C C   . ASN A 170 ? 0.2920 0.3562 0.4588 0.0444  0.0064  0.0514  170 ASN A C   
1296 O O   . ASN A 170 ? 0.2886 0.3411 0.4410 0.0405  0.0095  0.0500  170 ASN A O   
1297 C CB  . ASN A 170 ? 0.3057 0.3780 0.4884 0.0490  -0.0125 0.0860  170 ASN A CB  
1298 C CG  . ASN A 170 ? 0.3104 0.3947 0.4770 0.0447  -0.0213 0.1045  170 ASN A CG  
1299 O OD1 . ASN A 170 ? 0.3099 0.3959 0.4474 0.0366  -0.0197 0.1075  170 ASN A OD1 
1300 N ND2 . ASN A 170 ? 0.3183 0.4137 0.5048 0.0497  -0.0309 0.1155  170 ASN A ND2 
1301 N N   . GLU A 171 ? 0.2934 0.3646 0.4832 0.0489  0.0106  0.0370  171 GLU A N   
1302 C CA  . GLU A 171 ? 0.2947 0.3623 0.4902 0.0478  0.0201  0.0173  171 GLU A CA  
1303 C C   . GLU A 171 ? 0.2860 0.3553 0.4455 0.0382  0.0264  0.0104  171 GLU A C   
1304 O O   . GLU A 171 ? 0.2852 0.3456 0.4346 0.0348  0.0306  0.0037  171 GLU A O   
1305 C CB  . GLU A 171 ? 0.3005 0.3817 0.5268 0.0527  0.0245  0.0004  171 GLU A CB  
1306 C CG  . GLU A 171 ? 0.3129 0.3903 0.5839 0.0636  0.0177  0.0041  171 GLU A CG  
1307 C CD  . GLU A 171 ? 0.3173 0.4035 0.5990 0.0685  0.0069  0.0206  171 GLU A CD  
1308 O OE1 . GLU A 171 ? 0.3140 0.4091 0.5671 0.0631  0.0049  0.0296  171 GLU A OE1 
1309 O OE2 . GLU A 171 ? 0.3356 0.4204 0.6569 0.0780  -0.0003 0.0245  171 GLU A OE2 
1310 N N   . ILE A 172 ? 0.2805 0.3611 0.4224 0.0338  0.0261  0.0127  172 ILE A N   
1311 C CA  . ILE A 172 ? 0.2770 0.3581 0.3877 0.0246  0.0301  0.0089  172 ILE A CA  
1312 C C   . ILE A 172 ? 0.2780 0.3449 0.3682 0.0218  0.0266  0.0180  172 ILE A C   
1313 O O   . ILE A 172 ? 0.2732 0.3336 0.3488 0.0172  0.0296  0.0121  172 ILE A O   
1314 C CB  . ILE A 172 ? 0.2731 0.3676 0.3734 0.0202  0.0293  0.0111  172 ILE A CB  
1315 C CG1 . ILE A 172 ? 0.2751 0.3863 0.3929 0.0203  0.0353  -0.0019 172 ILE A CG1 
1316 C CG2 . ILE A 172 ? 0.2707 0.3610 0.3411 0.0110  0.0303  0.0120  172 ILE A CG2 
1317 C CD1 . ILE A 172 ? 0.2736 0.3999 0.3934 0.0191  0.0330  0.0013  172 ILE A CD1 
1318 N N   . LEU A 173 ? 0.2807 0.3453 0.3707 0.0240  0.0199  0.0318  173 LEU A N   
1319 C CA  . LEU A 173 ? 0.2864 0.3416 0.3593 0.0208  0.0173  0.0387  173 LEU A CA  
1320 C C   . LEU A 173 ? 0.2949 0.3368 0.3743 0.0222  0.0194  0.0357  173 LEU A C   
1321 O O   . LEU A 173 ? 0.2929 0.3279 0.3573 0.0183  0.0206  0.0327  173 LEU A O   
1322 C CB  . LEU A 173 ? 0.2869 0.3476 0.3587 0.0210  0.0106  0.0530  173 LEU A CB  
1323 C CG  . LEU A 173 ? 0.2854 0.3603 0.3475 0.0178  0.0084  0.0545  173 LEU A CG  
1324 C CD1 . LEU A 173 ? 0.2908 0.3762 0.3571 0.0186  0.0014  0.0681  173 LEU A CD1 
1325 C CD2 . LEU A 173 ? 0.2815 0.3543 0.3222 0.0112  0.0097  0.0494  173 LEU A CD2 
1326 N N   . LYS A 174 ? 0.3076 0.3462 0.4123 0.0280  0.0193  0.0359  174 LYS A N   
1327 C CA  . LYS A 174 ? 0.3223 0.3482 0.4374 0.0292  0.0217  0.0311  174 LYS A CA  
1328 C C   . LYS A 174 ? 0.3178 0.3441 0.4237 0.0256  0.0285  0.0140  174 LYS A C   
1329 O O   . LYS A 174 ? 0.3131 0.3314 0.4103 0.0226  0.0298  0.0106  174 LYS A O   
1330 C CB  . LYS A 174 ? 0.3415 0.3633 0.4914 0.0364  0.0203  0.0321  174 LYS A CB  
1331 C CG  . LYS A 174 ? 0.3638 0.3817 0.5237 0.0387  0.0117  0.0529  174 LYS A CG  
1332 C CD  . LYS A 174 ? 0.3840 0.3957 0.5838 0.0466  0.0083  0.0547  174 LYS A CD  
1333 C CE  . LYS A 174 ? 0.3959 0.4166 0.6092 0.0511  -0.0006 0.0699  174 LYS A CE  
1334 N NZ  . LYS A 174 ? 0.4134 0.4298 0.6713 0.0604  -0.0042 0.0676  174 LYS A NZ  
1335 N N   . ARG A 175 ? 0.3151 0.3530 0.4225 0.0248  0.0326  0.0035  175 ARG A N   
1336 C CA  . ARG A 175 ? 0.3174 0.3600 0.4135 0.0191  0.0387  -0.0114 175 ARG A CA  
1337 C C   . ARG A 175 ? 0.3140 0.3528 0.3796 0.0124  0.0362  -0.0067 175 ARG A C   
1338 O O   . ARG A 175 ? 0.3100 0.3449 0.3668 0.0089  0.0375  -0.0132 175 ARG A O   
1339 C CB  . ARG A 175 ? 0.3202 0.3796 0.4213 0.0172  0.0439  -0.0221 175 ARG A CB  
1340 C CG  . ARG A 175 ? 0.3273 0.3962 0.4146 0.0088  0.0504  -0.0369 175 ARG A CG  
1341 C CD  . ARG A 175 ? 0.3362 0.4009 0.4344 0.0093  0.0540  -0.0495 175 ARG A CD  
1342 N NE  . ARG A 175 ? 0.3485 0.4270 0.4317 -0.0002 0.0600  -0.0639 175 ARG A NE  
1343 C CZ  . ARG A 175 ? 0.3567 0.4332 0.4311 -0.0044 0.0609  -0.0714 175 ARG A CZ  
1344 N NH1 . ARG A 175 ? 0.3546 0.4146 0.4351 0.0002  0.0570  -0.0668 175 ARG A NH1 
1345 N NH2 . ARG A 175 ? 0.3690 0.4621 0.4276 -0.0147 0.0656  -0.0831 175 ARG A NH2 
1346 N N   . GLY A 176 ? 0.3119 0.3524 0.3644 0.0109  0.0319  0.0036  176 GLY A N   
1347 C CA  . GLY A 176 ? 0.3159 0.3519 0.3456 0.0056  0.0282  0.0078  176 GLY A CA  
1348 C C   . GLY A 176 ? 0.3199 0.3450 0.3478 0.0067  0.0255  0.0105  176 GLY A C   
1349 O O   . GLY A 176 ? 0.3155 0.3363 0.3314 0.0031  0.0240  0.0073  176 GLY A O   
1350 N N   . TYR A 177 ? 0.3264 0.3480 0.3670 0.0110  0.0244  0.0171  177 TYR A N   
1351 C CA  . TYR A 177 ? 0.3338 0.3467 0.3751 0.0108  0.0231  0.0194  177 TYR A CA  
1352 C C   . TYR A 177 ? 0.3328 0.3402 0.3797 0.0105  0.0265  0.0085  177 TYR A C   
1353 O O   . TYR A 177 ? 0.3200 0.3232 0.3585 0.0078  0.0254  0.0053  177 TYR A O   
1354 C CB  . TYR A 177 ? 0.3472 0.3587 0.4024 0.0138  0.0214  0.0304  177 TYR A CB  
1355 C CG  . TYR A 177 ? 0.3639 0.3697 0.4174 0.0112  0.0204  0.0350  177 TYR A CG  
1356 C CD1 . TYR A 177 ? 0.3698 0.3813 0.4102 0.0072  0.0177  0.0404  177 TYR A CD1 
1357 C CD2 . TYR A 177 ? 0.3807 0.3771 0.4475 0.0118  0.0227  0.0321  177 TYR A CD2 
1358 C CE1 . TYR A 177 ? 0.3817 0.3914 0.4208 0.0033  0.0179  0.0429  177 TYR A CE1 
1359 C CE2 . TYR A 177 ? 0.3925 0.3850 0.4578 0.0079  0.0224  0.0362  177 TYR A CE2 
1360 C CZ  . TYR A 177 ? 0.3942 0.3942 0.4449 0.0035  0.0203  0.0416  177 TYR A CZ  
1361 O OH  . TYR A 177 ? 0.4272 0.4272 0.4766 -0.0017 0.0211  0.0441  177 TYR A OH  
1362 N N   . GLU A 178 ? 0.3334 0.3427 0.3965 0.0131  0.0307  0.0011  178 GLU A N   
1363 C CA  . GLU A 178 ? 0.3432 0.3498 0.4150 0.0123  0.0347  -0.0118 178 GLU A CA  
1364 C C   . GLU A 178 ? 0.3338 0.3466 0.3863 0.0063  0.0355  -0.0215 178 GLU A C   
1365 O O   . GLU A 178 ? 0.3298 0.3406 0.3822 0.0041  0.0365  -0.0299 178 GLU A O   
1366 C CB  . GLU A 178 ? 0.3600 0.3689 0.4590 0.0166  0.0393  -0.0204 178 GLU A CB  
1367 C CG  . GLU A 178 ? 0.3777 0.3766 0.5013 0.0223  0.0368  -0.0100 178 GLU A CG  
1368 C CD  . GLU A 178 ? 0.3966 0.3829 0.5243 0.0208  0.0357  -0.0063 178 GLU A CD  
1369 O OE1 . GLU A 178 ? 0.4007 0.3862 0.5180 0.0167  0.0378  -0.0160 178 GLU A OE1 
1370 O OE2 . GLU A 178 ? 0.4168 0.3949 0.5584 0.0230  0.0322  0.0072  178 GLU A OE2 
1371 N N   . LEU A 179 ? 0.3251 0.3459 0.3616 0.0029  0.0343  -0.0192 179 LEU A N   
1372 C CA  . LEU A 179 ? 0.3270 0.3529 0.3428 -0.0041 0.0325  -0.0233 179 LEU A CA  
1373 C C   . LEU A 179 ? 0.3202 0.3371 0.3267 -0.0047 0.0263  -0.0189 179 LEU A C   
1374 O O   . LEU A 179 ? 0.3227 0.3415 0.3219 -0.0086 0.0247  -0.0252 179 LEU A O   
1375 C CB  . LEU A 179 ? 0.3293 0.3621 0.3302 -0.0085 0.0308  -0.0173 179 LEU A CB  
1376 C CG  . LEU A 179 ? 0.3345 0.3815 0.3404 -0.0111 0.0377  -0.0251 179 LEU A CG  
1377 C CD1 . LEU A 179 ? 0.3374 0.3894 0.3300 -0.0158 0.0355  -0.0166 179 LEU A CD1 
1378 C CD2 . LEU A 179 ? 0.3451 0.4041 0.3466 -0.0179 0.0425  -0.0393 179 LEU A CD2 
1379 N N   . GLY A 180 ? 0.3078 0.3177 0.3158 -0.0015 0.0226  -0.0092 180 GLY A N   
1380 C CA  . GLY A 180 ? 0.3066 0.3101 0.3111 -0.0016 0.0177  -0.0075 180 GLY A CA  
1381 C C   . GLY A 180 ? 0.3064 0.3062 0.3221 -0.0007 0.0205  -0.0147 180 GLY A C   
1382 O O   . GLY A 180 ? 0.3121 0.3117 0.3234 -0.0030 0.0176  -0.0202 180 GLY A O   
1383 N N   . GLU A 181 ? 0.3050 0.3020 0.3373 0.0023  0.0254  -0.0144 181 GLU A N   
1384 C CA  . GLU A 181 ? 0.3088 0.3004 0.3554 0.0025  0.0283  -0.0205 181 GLU A CA  
1385 C C   . GLU A 181 ? 0.3076 0.3039 0.3555 0.0000  0.0310  -0.0356 181 GLU A C   
1386 O O   . GLU A 181 ? 0.3059 0.3001 0.3585 -0.0017 0.0311  -0.0428 181 GLU A O   
1387 C CB  . GLU A 181 ? 0.3180 0.3038 0.3850 0.0060  0.0316  -0.0146 181 GLU A CB  
1388 C CG  . GLU A 181 ? 0.3244 0.3088 0.3885 0.0064  0.0286  0.0008  181 GLU A CG  
1389 C CD  . GLU A 181 ? 0.3296 0.3143 0.3835 0.0026  0.0261  0.0024  181 GLU A CD  
1390 O OE1 . GLU A 181 ? 0.3448 0.3257 0.4050 0.0005  0.0276  -0.0037 181 GLU A OE1 
1391 O OE2 . GLU A 181 ? 0.3254 0.3155 0.3673 0.0016  0.0230  0.0079  181 GLU A OE2 
1392 N N   . SER A 182 ? 0.3046 0.3099 0.3483 -0.0013 0.0334  -0.0414 182 SER A N   
1393 C CA  . SER A 182 ? 0.3110 0.3264 0.3520 -0.0061 0.0361  -0.0568 182 SER A CA  
1394 C C   . SER A 182 ? 0.3129 0.3311 0.3356 -0.0108 0.0295  -0.0574 182 SER A C   
1395 O O   . SER A 182 ? 0.3187 0.3423 0.3436 -0.0141 0.0305  -0.0695 182 SER A O   
1396 C CB  . SER A 182 ? 0.3136 0.3423 0.3485 -0.0091 0.0398  -0.0618 182 SER A CB  
1397 O OG  . SER A 182 ? 0.3121 0.3413 0.3710 -0.0046 0.0464  -0.0676 182 SER A OG  
1398 N N   . ARG A 183 ? 0.3130 0.3280 0.3204 -0.0110 0.0222  -0.0449 183 ARG A N   
1399 C CA  . ARG A 183 ? 0.3209 0.3373 0.3152 -0.0142 0.0135  -0.0436 183 ARG A CA  
1400 C C   . ARG A 183 ? 0.3118 0.3219 0.3175 -0.0118 0.0120  -0.0472 183 ARG A C   
1401 O O   . ARG A 183 ? 0.3145 0.3289 0.3161 -0.0145 0.0067  -0.0524 183 ARG A O   
1402 C CB  . ARG A 183 ? 0.3289 0.3418 0.3103 -0.0142 0.0057  -0.0303 183 ARG A CB  
1403 C CG  . ARG A 183 ? 0.3456 0.3655 0.3141 -0.0187 0.0065  -0.0259 183 ARG A CG  
1404 C CD  . ARG A 183 ? 0.3675 0.3984 0.3192 -0.0272 0.0019  -0.0281 183 ARG A CD  
1405 N NE  . ARG A 183 ? 0.3818 0.4250 0.3237 -0.0337 0.0075  -0.0296 183 ARG A NE  
1406 C CZ  . ARG A 183 ? 0.3989 0.4512 0.3209 -0.0432 0.0024  -0.0231 183 ARG A CZ  
1407 N NH1 . ARG A 183 ? 0.4096 0.4578 0.3202 -0.0463 -0.0102 -0.0127 183 ARG A NH1 
1408 N NH2 . ARG A 183 ? 0.4094 0.4756 0.3240 -0.0502 0.0096  -0.0266 183 ARG A NH2 
1409 N N   . VAL A 184 ? 0.2971 0.2989 0.3170 -0.0077 0.0164  -0.0438 184 VAL A N   
1410 C CA  . VAL A 184 ? 0.2925 0.2899 0.3246 -0.0073 0.0171  -0.0473 184 VAL A CA  
1411 C C   . VAL A 184 ? 0.2948 0.2941 0.3393 -0.0093 0.0225  -0.0610 184 VAL A C   
1412 O O   . VAL A 184 ? 0.2920 0.2937 0.3401 -0.0116 0.0207  -0.0691 184 VAL A O   
1413 C CB  . VAL A 184 ? 0.2885 0.2787 0.3305 -0.0048 0.0205  -0.0379 184 VAL A CB  
1414 C CG1 . VAL A 184 ? 0.2907 0.2778 0.3453 -0.0067 0.0227  -0.0414 184 VAL A CG1 
1415 C CG2 . VAL A 184 ? 0.2834 0.2747 0.3147 -0.0037 0.0157  -0.0280 184 VAL A CG2 
1416 N N   . ILE A 185 ? 0.2961 0.2955 0.3500 -0.0085 0.0291  -0.0651 185 ILE A N   
1417 C CA  . ILE A 185 ? 0.3045 0.3064 0.3751 -0.0103 0.0351  -0.0809 185 ILE A CA  
1418 C C   . ILE A 185 ? 0.3146 0.3310 0.3728 -0.0159 0.0326  -0.0944 185 ILE A C   
1419 O O   . ILE A 185 ? 0.3124 0.3323 0.3812 -0.0187 0.0345  -0.1080 185 ILE A O   
1420 C CB  . ILE A 185 ? 0.3063 0.3075 0.3929 -0.0076 0.0419  -0.0845 185 ILE A CB  
1421 C CG1 . ILE A 185 ? 0.3033 0.2898 0.4071 -0.0027 0.0432  -0.0710 185 ILE A CG1 
1422 C CG2 . ILE A 185 ? 0.3153 0.3233 0.4199 -0.0102 0.0483  -0.1059 185 ILE A CG2 
1423 C CD1 . ILE A 185 ? 0.3053 0.2910 0.4231 0.0016  0.0465  -0.0690 185 ILE A CD1 
1424 N N   . CYS A 186 ? 0.3222 0.3480 0.3579 -0.0185 0.0277  -0.0897 186 CYS A N   
1425 C CA  . CYS A 186 ? 0.3394 0.3821 0.3601 -0.0257 0.0244  -0.0996 186 CYS A CA  
1426 C C   . CYS A 186 ? 0.3374 0.3817 0.3472 -0.0274 0.0136  -0.0958 186 CYS A C   
1427 O O   . CYS A 186 ? 0.3481 0.4069 0.3477 -0.0337 0.0094  -0.1040 186 CYS A O   
1428 C CB  . CYS A 186 ? 0.3538 0.4075 0.3554 -0.0300 0.0240  -0.0952 186 CYS A CB  
1429 S SG  . CYS A 186 ? 0.3932 0.4741 0.3801 -0.0418 0.0253  -0.1121 186 CYS A SG  
1430 N N   . GLY A 187 ? 0.3248 0.3565 0.3380 -0.0223 0.0088  -0.0844 187 GLY A N   
1431 C CA  . GLY A 187 ? 0.3268 0.3598 0.3362 -0.0225 -0.0017 -0.0822 187 GLY A CA  
1432 C C   . GLY A 187 ? 0.3302 0.3643 0.3220 -0.0230 -0.0136 -0.0687 187 GLY A C   
1433 O O   . GLY A 187 ? 0.3293 0.3660 0.3196 -0.0230 -0.0246 -0.0669 187 GLY A O   
1434 N N   . TYR A 188 ? 0.3326 0.3646 0.3139 -0.0233 -0.0121 -0.0593 188 TYR A N   
1435 C CA  . TYR A 188 ? 0.3436 0.3739 0.3106 -0.0244 -0.0230 -0.0449 188 TYR A CA  
1436 C C   . TYR A 188 ? 0.3300 0.3481 0.3074 -0.0178 -0.0281 -0.0372 188 TYR A C   
1437 O O   . TYR A 188 ? 0.3312 0.3469 0.3059 -0.0173 -0.0404 -0.0292 188 TYR A O   
1438 C CB  . TYR A 188 ? 0.3547 0.3871 0.3098 -0.0277 -0.0180 -0.0385 188 TYR A CB  
1439 C CG  . TYR A 188 ? 0.3792 0.4283 0.3175 -0.0374 -0.0171 -0.0429 188 TYR A CG  
1440 C CD1 . TYR A 188 ? 0.3896 0.4512 0.3318 -0.0409 -0.0101 -0.0598 188 TYR A CD1 
1441 C CD2 . TYR A 188 ? 0.3989 0.4532 0.3179 -0.0444 -0.0227 -0.0309 188 TYR A CD2 
1442 C CE1 . TYR A 188 ? 0.4080 0.4898 0.3345 -0.0513 -0.0082 -0.0665 188 TYR A CE1 
1443 C CE2 . TYR A 188 ? 0.4183 0.4920 0.3195 -0.0557 -0.0210 -0.0350 188 TYR A CE2 
1444 C CZ  . TYR A 188 ? 0.4231 0.5120 0.3277 -0.0592 -0.0135 -0.0537 188 TYR A CZ  
1445 O OH  . TYR A 188 ? 0.4450 0.5579 0.3318 -0.0719 -0.0109 -0.0606 188 TYR A OH  
1446 N N   . HIS A 189 ? 0.3150 0.3264 0.3054 -0.0133 -0.0190 -0.0396 189 HIS A N   
1447 C CA  . HIS A 189 ? 0.3058 0.3101 0.3055 -0.0087 -0.0212 -0.0347 189 HIS A CA  
1448 C C   . HIS A 189 ? 0.2944 0.2971 0.3092 -0.0067 -0.0132 -0.0413 189 HIS A C   
1449 O O   . HIS A 189 ? 0.2941 0.2968 0.3136 -0.0079 -0.0045 -0.0462 189 HIS A O   
1450 C CB  . HIS A 189 ? 0.3071 0.3071 0.3011 -0.0078 -0.0184 -0.0252 189 HIS A CB  
1451 C CG  . HIS A 189 ? 0.3221 0.3217 0.3036 -0.0104 -0.0274 -0.0162 189 HIS A CG  
1452 N ND1 . HIS A 189 ? 0.3287 0.3241 0.3141 -0.0089 -0.0391 -0.0113 189 HIS A ND1 
1453 C CD2 . HIS A 189 ? 0.3365 0.3397 0.3034 -0.0153 -0.0265 -0.0111 189 HIS A CD2 
1454 C CE1 . HIS A 189 ? 0.3433 0.3374 0.3167 -0.0130 -0.0459 -0.0013 189 HIS A CE1 
1455 N NE2 . HIS A 189 ? 0.3473 0.3472 0.3075 -0.0176 -0.0379 -0.0009 189 HIS A NE2 
1456 N N   . TRP A 190 ? 0.2848 0.2870 0.3092 -0.0044 -0.0163 -0.0417 190 TRP A N   
1457 C CA  . TRP A 190 ? 0.2772 0.2801 0.3137 -0.0047 -0.0084 -0.0454 190 TRP A CA  
1458 C C   . TRP A 190 ? 0.2764 0.2765 0.3099 -0.0043 -0.0018 -0.0368 190 TRP A C   
1459 O O   . TRP A 190 ? 0.2709 0.2696 0.2964 -0.0029 -0.0050 -0.0302 190 TRP A O   
1460 C CB  . TRP A 190 ? 0.2687 0.2767 0.3168 -0.0036 -0.0135 -0.0513 190 TRP A CB  
1461 C CG  . TRP A 190 ? 0.2686 0.2806 0.3225 -0.0029 -0.0229 -0.0591 190 TRP A CG  
1462 C CD1 . TRP A 190 ? 0.2710 0.2831 0.3256 -0.0001 -0.0361 -0.0574 190 TRP A CD1 
1463 C CD2 . TRP A 190 ? 0.2686 0.2855 0.3306 -0.0051 -0.0210 -0.0690 190 TRP A CD2 
1464 N NE1 . TRP A 190 ? 0.2751 0.2929 0.3369 -0.0001 -0.0434 -0.0650 190 TRP A NE1 
1465 C CE2 . TRP A 190 ? 0.2738 0.2955 0.3398 -0.0033 -0.0338 -0.0733 190 TRP A CE2 
1466 C CE3 . TRP A 190 ? 0.2676 0.2849 0.3354 -0.0088 -0.0105 -0.0742 190 TRP A CE3 
1467 C CZ2 . TRP A 190 ? 0.2774 0.3066 0.3519 -0.0050 -0.0359 -0.0840 190 TRP A CZ2 
1468 C CZ3 . TRP A 190 ? 0.2711 0.2943 0.3482 -0.0110 -0.0117 -0.0853 190 TRP A CZ3 
1469 C CH2 . TRP A 190 ? 0.2747 0.3049 0.3544 -0.0090 -0.0241 -0.0908 190 TRP A CH2 
1470 N N   . GLN A 191 ? 0.2790 0.2790 0.3196 -0.0063 0.0064  -0.0358 191 GLN A N   
1471 C CA  . GLN A 191 ? 0.2802 0.2796 0.3187 -0.0066 0.0113  -0.0261 191 GLN A CA  
1472 C C   . GLN A 191 ? 0.2724 0.2775 0.3071 -0.0060 0.0075  -0.0239 191 GLN A C   
1473 O O   . GLN A 191 ? 0.2689 0.2737 0.2970 -0.0049 0.0075  -0.0167 191 GLN A O   
1474 C CB  . GLN A 191 ? 0.2905 0.2902 0.3380 -0.0106 0.0185  -0.0234 191 GLN A CB  
1475 C CG  . GLN A 191 ? 0.2972 0.2976 0.3425 -0.0117 0.0220  -0.0108 191 GLN A CG  
1476 C CD  . GLN A 191 ? 0.3055 0.2990 0.3493 -0.0077 0.0223  -0.0050 191 GLN A CD  
1477 O OE1 . GLN A 191 ? 0.3239 0.3107 0.3754 -0.0064 0.0246  -0.0085 191 GLN A OE1 
1478 N NE2 . GLN A 191 ? 0.3058 0.3028 0.3421 -0.0059 0.0205  0.0018  191 GLN A NE2 
1479 N N   . SER A 192 ? 0.2660 0.2775 0.3077 -0.0069 0.0044  -0.0320 192 SER A N   
1480 C CA  . SER A 192 ? 0.2639 0.2824 0.3075 -0.0065 0.0012  -0.0341 192 SER A CA  
1481 C C   . SER A 192 ? 0.2652 0.2775 0.3037 -0.0027 -0.0069 -0.0310 192 SER A C   
1482 O O   . SER A 192 ? 0.2644 0.2799 0.3025 -0.0026 -0.0079 -0.0294 192 SER A O   
1483 C CB  . SER A 192 ? 0.2610 0.2893 0.3186 -0.0078 -0.0003 -0.0469 192 SER A CB  
1484 O OG  . SER A 192 ? 0.2602 0.2844 0.3240 -0.0050 -0.0070 -0.0532 192 SER A OG  
1485 N N   . ASP A 193 ? 0.2693 0.2742 0.3035 -0.0008 -0.0127 -0.0300 193 ASP A N   
1486 C CA  . ASP A 193 ? 0.2755 0.2745 0.3023 0.0004  -0.0204 -0.0238 193 ASP A CA  
1487 C C   . ASP A 193 ? 0.2791 0.2767 0.2952 -0.0005 -0.0149 -0.0152 193 ASP A C   
1488 O O   . ASP A 193 ? 0.2783 0.2744 0.2919 -0.0006 -0.0184 -0.0108 193 ASP A O   
1489 C CB  . ASP A 193 ? 0.2815 0.2766 0.3011 -0.0001 -0.0262 -0.0226 193 ASP A CB  
1490 C CG  . ASP A 193 ? 0.2832 0.2804 0.3135 0.0011  -0.0339 -0.0303 193 ASP A CG  
1491 O OD1 . ASP A 193 ? 0.2774 0.2769 0.3223 0.0034  -0.0384 -0.0358 193 ASP A OD1 
1492 O OD2 . ASP A 193 ? 0.2919 0.2903 0.3173 -0.0004 -0.0356 -0.0322 193 ASP A OD2 
1493 N N   . VAL A 194 ? 0.2849 0.2830 0.2979 -0.0013 -0.0067 -0.0134 194 VAL A N   
1494 C CA  . VAL A 194 ? 0.2938 0.2920 0.3008 -0.0014 -0.0015 -0.0064 194 VAL A CA  
1495 C C   . VAL A 194 ? 0.2937 0.2976 0.3034 -0.0018 0.0012  -0.0028 194 VAL A C   
1496 O O   . VAL A 194 ? 0.2923 0.2978 0.2975 -0.0017 0.0009  0.0020  194 VAL A O   
1497 C CB  . VAL A 194 ? 0.2987 0.2952 0.3079 -0.0014 0.0049  -0.0074 194 VAL A CB  
1498 C CG1 . VAL A 194 ? 0.3032 0.3007 0.3137 -0.0004 0.0104  -0.0008 194 VAL A CG1 
1499 C CG2 . VAL A 194 ? 0.3050 0.3004 0.3083 -0.0027 0.0025  -0.0119 194 VAL A CG2 
1500 N N   . ASP A 195 ? 0.2984 0.3077 0.3147 -0.0033 0.0040  -0.0059 195 ASP A N   
1501 C CA  . ASP A 195 ? 0.3041 0.3236 0.3211 -0.0058 0.0066  -0.0035 195 ASP A CA  
1502 C C   . ASP A 195 ? 0.3010 0.3242 0.3188 -0.0055 0.0015  -0.0078 195 ASP A C   
1503 O O   . ASP A 195 ? 0.2971 0.3258 0.3115 -0.0064 0.0022  -0.0037 195 ASP A O   
1504 C CB  . ASP A 195 ? 0.3155 0.3436 0.3387 -0.0099 0.0103  -0.0081 195 ASP A CB  
1505 C CG  . ASP A 195 ? 0.3287 0.3526 0.3537 -0.0117 0.0154  -0.0022 195 ASP A CG  
1506 O OD1 . ASP A 195 ? 0.3395 0.3565 0.3631 -0.0095 0.0167  0.0061  195 ASP A OD1 
1507 O OD2 . ASP A 195 ? 0.3447 0.3728 0.3754 -0.0156 0.0181  -0.0068 195 ASP A OD2 
1508 N N   . ALA A 196 ? 0.2995 0.3199 0.3246 -0.0041 -0.0042 -0.0162 196 ALA A N   
1509 C CA  . ALA A 196 ? 0.3001 0.3215 0.3321 -0.0034 -0.0104 -0.0213 196 ALA A CA  
1510 C C   . ALA A 196 ? 0.3035 0.3166 0.3276 -0.0027 -0.0139 -0.0129 196 ALA A C   
1511 O O   . ALA A 196 ? 0.3059 0.3221 0.3335 -0.0037 -0.0157 -0.0141 196 ALA A O   
1512 C CB  . ALA A 196 ? 0.3026 0.3202 0.3479 -0.0010 -0.0180 -0.0304 196 ALA A CB  
1513 N N   . ALA A 197 ? 0.3052 0.3098 0.3195 -0.0021 -0.0144 -0.0058 197 ALA A N   
1514 C CA  . ALA A 197 ? 0.3099 0.3092 0.3155 -0.0033 -0.0167 0.0018  197 ALA A CA  
1515 C C   . ALA A 197 ? 0.3068 0.3129 0.3087 -0.0045 -0.0110 0.0060  197 ALA A C   
1516 O O   . ALA A 197 ? 0.3028 0.3079 0.3029 -0.0063 -0.0134 0.0092  197 ALA A O   
1517 C CB  . ALA A 197 ? 0.3124 0.3071 0.3081 -0.0041 -0.0160 0.0056  197 ALA A CB  
1518 N N   . ARG A 198 ? 0.3028 0.3161 0.3046 -0.0039 -0.0043 0.0068  198 ARG A N   
1519 C CA  . ARG A 198 ? 0.3017 0.3234 0.3014 -0.0046 -0.0004 0.0119  198 ARG A CA  
1520 C C   . ARG A 198 ? 0.2956 0.3271 0.2996 -0.0068 -0.0020 0.0077  198 ARG A C   
1521 O O   . ARG A 198 ? 0.2922 0.3299 0.2945 -0.0081 -0.0013 0.0106  198 ARG A O   
1522 C CB  . ARG A 198 ? 0.3079 0.3338 0.3085 -0.0036 0.0049  0.0164  198 ARG A CB  
1523 C CG  . ARG A 198 ? 0.3185 0.3357 0.3191 -0.0014 0.0071  0.0175  198 ARG A CG  
1524 C CD  . ARG A 198 ? 0.3266 0.3456 0.3330 0.0001  0.0114  0.0236  198 ARG A CD  
1525 N NE  . ARG A 198 ? 0.3379 0.3491 0.3489 0.0021  0.0140  0.0208  198 ARG A NE  
1526 C CZ  . ARG A 198 ? 0.3460 0.3522 0.3630 0.0021  0.0158  0.0184  198 ARG A CZ  
1527 N NH1 . ARG A 198 ? 0.3495 0.3579 0.3676 -0.0003 0.0157  0.0195  198 ARG A NH1 
1528 N NH2 . ARG A 198 ? 0.3527 0.3536 0.3757 0.0035  0.0184  0.0133  198 ARG A NH2 
1529 N N   . ILE A 199 ? 0.2906 0.3251 0.3021 -0.0076 -0.0038 -0.0011 199 ILE A N   
1530 C CA  A ILE A 199 ? 0.2888 0.3347 0.3081 -0.0103 -0.0049 -0.0097 199 ILE A CA  
1531 C CA  B ILE A 199 ? 0.2910 0.3369 0.3103 -0.0103 -0.0049 -0.0096 199 ILE A CA  
1532 C C   . ILE A 199 ? 0.2907 0.3281 0.3147 -0.0102 -0.0107 -0.0105 199 ILE A C   
1533 O O   . ILE A 199 ? 0.2900 0.3349 0.3145 -0.0126 -0.0100 -0.0109 199 ILE A O   
1534 C CB  A ILE A 199 ? 0.2873 0.3400 0.3179 -0.0113 -0.0052 -0.0225 199 ILE A CB  
1535 C CB  B ILE A 199 ? 0.2924 0.3447 0.3232 -0.0112 -0.0054 -0.0225 199 ILE A CB  
1536 C CG1 A ILE A 199 ? 0.2857 0.3502 0.3108 -0.0143 0.0014  -0.0206 199 ILE A CG1 
1537 C CG1 B ILE A 199 ? 0.2940 0.3573 0.3194 -0.0140 0.0011  -0.0207 199 ILE A CG1 
1538 C CG2 A ILE A 199 ? 0.2873 0.3521 0.3306 -0.0140 -0.0066 -0.0357 199 ILE A CG2 
1539 C CG2 B ILE A 199 ? 0.2922 0.3572 0.3354 -0.0140 -0.0065 -0.0356 199 ILE A CG2 
1540 C CD1 A ILE A 199 ? 0.2860 0.3672 0.3030 -0.0190 0.0056  -0.0149 199 ILE A CD1 
1541 C CD1 B ILE A 199 ? 0.2971 0.3754 0.3332 -0.0177 0.0031  -0.0353 199 ILE A CD1 
1542 N N   . VAL A 200 ? 0.2925 0.3149 0.3203 -0.0083 -0.0171 -0.0100 200 VAL A N   
1543 C CA  . VAL A 200 ? 0.2988 0.3107 0.3320 -0.0095 -0.0241 -0.0079 200 VAL A CA  
1544 C C   . VAL A 200 ? 0.3009 0.3099 0.3205 -0.0120 -0.0220 0.0033  200 VAL A C   
1545 O O   . VAL A 200 ? 0.3060 0.3132 0.3290 -0.0152 -0.0244 0.0048  200 VAL A O   
1546 C CB  . VAL A 200 ? 0.3067 0.3039 0.3482 -0.0076 -0.0339 -0.0076 200 VAL A CB  
1547 C CG1 . VAL A 200 ? 0.3034 0.3055 0.3644 -0.0048 -0.0364 -0.0220 200 VAL A CG1 
1548 C CG2 . VAL A 200 ? 0.3100 0.3004 0.3369 -0.0069 -0.0340 0.0010  200 VAL A CG2 
1549 N N   . GLY A 201 ? 0.2995 0.3092 0.3064 -0.0111 -0.0170 0.0097  201 GLY A N   
1550 C CA  . GLY A 201 ? 0.3023 0.3137 0.2992 -0.0133 -0.0133 0.0173  201 GLY A CA  
1551 C C   . GLY A 201 ? 0.2969 0.3208 0.2960 -0.0144 -0.0093 0.0165  201 GLY A C   
1552 O O   . GLY A 201 ? 0.3051 0.3303 0.3023 -0.0178 -0.0090 0.0198  201 GLY A O   
1553 N N   . SER A 202 ? 0.2908 0.3258 0.2936 -0.0127 -0.0065 0.0124  202 SER A N   
1554 C CA  . SER A 202 ? 0.2901 0.3402 0.2945 -0.0145 -0.0041 0.0117  202 SER A CA  
1555 C C   . SER A 202 ? 0.2856 0.3378 0.2992 -0.0181 -0.0078 0.0038  202 SER A C   
1556 O O   . SER A 202 ? 0.2827 0.3418 0.2974 -0.0210 -0.0073 0.0043  202 SER A O   
1557 C CB  . SER A 202 ? 0.2914 0.3552 0.2951 -0.0138 -0.0010 0.0115  202 SER A CB  
1558 O OG  . SER A 202 ? 0.3097 0.3779 0.3191 -0.0154 -0.0019 0.0019  202 SER A OG  
1559 N N   . ALA A 203 ? 0.2813 0.3277 0.3046 -0.0179 -0.0117 -0.0043 203 ALA A N   
1560 C CA  . ALA A 203 ? 0.2814 0.3281 0.3198 -0.0207 -0.0159 -0.0143 203 ALA A CA  
1561 C C   . ALA A 203 ? 0.2852 0.3188 0.3252 -0.0238 -0.0200 -0.0078 203 ALA A C   
1562 O O   . ALA A 203 ? 0.2873 0.3267 0.3353 -0.0276 -0.0203 -0.0125 203 ALA A O   
1563 C CB  . ALA A 203 ? 0.2829 0.3237 0.3360 -0.0186 -0.0204 -0.0246 203 ALA A CB  
1564 N N   . VAL A 204 ? 0.2859 0.3039 0.3178 -0.0234 -0.0230 0.0027  204 VAL A N   
1565 C CA  . VAL A 204 ? 0.2941 0.3004 0.3251 -0.0287 -0.0271 0.0111  204 VAL A CA  
1566 C C   . VAL A 204 ? 0.2916 0.3088 0.3146 -0.0327 -0.0209 0.0149  204 VAL A C   
1567 O O   . VAL A 204 ? 0.2951 0.3086 0.3225 -0.0387 -0.0230 0.0175  204 VAL A O   
1568 C CB  . VAL A 204 ? 0.3023 0.2939 0.3229 -0.0295 -0.0316 0.0222  204 VAL A CB  
1569 C CG1 . VAL A 204 ? 0.2990 0.2977 0.3016 -0.0283 -0.0242 0.0272  204 VAL A CG1 
1570 C CG2 . VAL A 204 ? 0.3180 0.2975 0.3391 -0.0372 -0.0379 0.0322  204 VAL A CG2 
1571 N N   . VAL A 205 ? 0.2830 0.3137 0.2967 -0.0296 -0.0140 0.0155  205 VAL A N   
1572 C CA  . VAL A 205 ? 0.2837 0.3271 0.2936 -0.0321 -0.0088 0.0180  205 VAL A CA  
1573 C C   . VAL A 205 ? 0.2825 0.3375 0.3036 -0.0351 -0.0093 0.0101  205 VAL A C   
1574 O O   . VAL A 205 ? 0.2849 0.3453 0.3075 -0.0400 -0.0078 0.0113  205 VAL A O   
1575 C CB  . VAL A 205 ? 0.2763 0.3307 0.2794 -0.0269 -0.0032 0.0206  205 VAL A CB  
1576 C CG1 . VAL A 205 ? 0.2746 0.3447 0.2792 -0.0282 0.0005  0.0216  205 VAL A CG1 
1577 C CG2 . VAL A 205 ? 0.2802 0.3249 0.2744 -0.0255 -0.0017 0.0259  205 VAL A CG2 
1578 N N   . ALA A 206 ? 0.2806 0.3414 0.3102 -0.0333 -0.0109 0.0004  206 ALA A N   
1579 C CA  . ALA A 206 ? 0.2803 0.3542 0.3223 -0.0372 -0.0114 -0.0106 206 ALA A CA  
1580 C C   . ALA A 206 ? 0.2913 0.3507 0.3466 -0.0425 -0.0163 -0.0128 206 ALA A C   
1581 O O   . ALA A 206 ? 0.2939 0.3607 0.3557 -0.0478 -0.0154 -0.0159 206 ALA A O   
1582 C CB  . ALA A 206 ? 0.2758 0.3615 0.3247 -0.0356 -0.0114 -0.0230 206 ALA A CB  
1583 N N   . THR A 207 ? 0.2995 0.3382 0.3603 -0.0414 -0.0221 -0.0101 207 THR A N   
1584 C CA  . THR A 207 ? 0.3140 0.3350 0.3889 -0.0468 -0.0289 -0.0080 207 THR A CA  
1585 C C   . THR A 207 ? 0.3218 0.3394 0.3856 -0.0537 -0.0270 0.0047  207 THR A C   
1586 O O   . THR A 207 ? 0.3270 0.3427 0.4019 -0.0606 -0.0284 0.0034  207 THR A O   
1587 C CB  . THR A 207 ? 0.3233 0.3222 0.4040 -0.0441 -0.0375 -0.0028 207 THR A CB  
1588 O OG1 . THR A 207 ? 0.3134 0.3181 0.4000 -0.0371 -0.0374 -0.0137 207 THR A OG1 
1589 C CG2 . THR A 207 ? 0.3398 0.3212 0.4443 -0.0488 -0.0468 -0.0035 207 THR A CG2 
1590 N N   . LEU A 208 ? 0.3215 0.3399 0.3650 -0.0526 -0.0231 0.0156  208 LEU A N   
1591 C CA  . LEU A 208 ? 0.3310 0.3501 0.3632 -0.0600 -0.0198 0.0260  208 LEU A CA  
1592 C C   . LEU A 208 ? 0.3274 0.3647 0.3645 -0.0637 -0.0142 0.0199  208 LEU A C   
1593 O O   . LEU A 208 ? 0.3345 0.3704 0.3731 -0.0728 -0.0136 0.0244  208 LEU A O   
1594 C CB  . LEU A 208 ? 0.3286 0.3511 0.3415 -0.0574 -0.0150 0.0332  208 LEU A CB  
1595 C CG  . LEU A 208 ? 0.3371 0.3429 0.3423 -0.0572 -0.0209 0.0415  208 LEU A CG  
1596 C CD1 . LEU A 208 ? 0.3319 0.3449 0.3214 -0.0535 -0.0149 0.0435  208 LEU A CD1 
1597 C CD2 . LEU A 208 ? 0.3593 0.3514 0.3623 -0.0682 -0.0269 0.0535  208 LEU A CD2 
1598 N N   . HIS A 209 ? 0.3142 0.3697 0.3540 -0.0577 -0.0107 0.0104  209 HIS A N   
1599 C CA  . HIS A 209 ? 0.3108 0.3866 0.3563 -0.0607 -0.0069 0.0041  209 HIS A CA  
1600 C C   . HIS A 209 ? 0.3146 0.3885 0.3781 -0.0679 -0.0101 -0.0043 209 HIS A C   
1601 O O   . HIS A 209 ? 0.3118 0.4004 0.3807 -0.0729 -0.0073 -0.0085 209 HIS A O   
1602 C CB  . HIS A 209 ? 0.3020 0.3985 0.3454 -0.0536 -0.0045 -0.0018 209 HIS A CB  
1603 C CG  . HIS A 209 ? 0.3003 0.4040 0.3318 -0.0482 -0.0005 0.0061  209 HIS A CG  
1604 N ND1 . HIS A 209 ? 0.3017 0.3956 0.3244 -0.0422 -0.0002 0.0116  209 HIS A ND1 
1605 C CD2 . HIS A 209 ? 0.3004 0.4204 0.3314 -0.0477 0.0031  0.0083  209 HIS A CD2 
1606 C CE1 . HIS A 209 ? 0.2997 0.4024 0.3178 -0.0382 0.0034  0.0164  209 HIS A CE1 
1607 N NE2 . HIS A 209 ? 0.2977 0.4162 0.3215 -0.0411 0.0052  0.0146  209 HIS A NE2 
1608 N N   . THR A 210 ? 0.3182 0.3745 0.3942 -0.0682 -0.0164 -0.0078 210 THR A N   
1609 C CA  . THR A 210 ? 0.3262 0.3766 0.4249 -0.0750 -0.0205 -0.0164 210 THR A CA  
1610 C C   . THR A 210 ? 0.3426 0.3723 0.4436 -0.0846 -0.0241 -0.0030 210 THR A C   
1611 O O   . THR A 210 ? 0.3491 0.3726 0.4697 -0.0919 -0.0272 -0.0078 210 THR A O   
1612 C CB  . THR A 210 ? 0.3269 0.3679 0.4453 -0.0709 -0.0266 -0.0285 210 THR A CB  
1613 O OG1 . THR A 210 ? 0.3350 0.3493 0.4542 -0.0696 -0.0339 -0.0168 210 THR A OG1 
1614 C CG2 . THR A 210 ? 0.3128 0.3736 0.4253 -0.0631 -0.0229 -0.0394 210 THR A CG2 
1615 N N   . ASN A 211 ? 0.3467 0.3671 0.4281 -0.0857 -0.0236 0.0133  211 ASN A N   
1616 C CA  . ASN A 211 ? 0.3671 0.3684 0.4463 -0.0963 -0.0280 0.0290  211 ASN A CA  
1617 C C   . ASN A 211 ? 0.3704 0.3851 0.4402 -0.1066 -0.0204 0.0340  211 ASN A C   
1618 O O   . ASN A 211 ? 0.3575 0.3890 0.4100 -0.1041 -0.0126 0.0351  211 ASN A O   
1619 C CB  . ASN A 211 ? 0.3749 0.3630 0.4365 -0.0939 -0.0317 0.0430  211 ASN A CB  
1620 C CG  . ASN A 211 ? 0.3996 0.3700 0.4554 -0.1065 -0.0375 0.0619  211 ASN A CG  
1621 O OD1 . ASN A 211 ? 0.4095 0.3880 0.4447 -0.1142 -0.0319 0.0718  211 ASN A OD1 
1622 N ND2 . ASN A 211 ? 0.4173 0.3651 0.4929 -0.1095 -0.0492 0.0667  211 ASN A ND2 
1623 N N   . PRO A 212 ? 0.4176 0.4103 0.4920 -0.0476 0.0154  0.0355  212 PRO A N   
1624 C CA  . PRO A 212 ? 0.4166 0.4049 0.5175 -0.0670 0.0111  0.0305  212 PRO A CA  
1625 C C   . PRO A 212 ? 0.3926 0.4022 0.4870 -0.0735 0.0175  0.0599  212 PRO A C   
1626 O O   . PRO A 212 ? 0.3726 0.3995 0.4706 -0.0848 0.0110  0.0524  212 PRO A O   
1627 C CB  . PRO A 212 ? 0.4561 0.4024 0.6084 -0.0707 0.0243  0.0285  212 PRO A CB  
1628 C CG  . PRO A 212 ? 0.4854 0.4107 0.6253 -0.0521 0.0232  0.0102  212 PRO A CG  
1629 C CD  . PRO A 212 ? 0.4588 0.4165 0.5535 -0.0353 0.0248  0.0281  212 PRO A CD  
1630 N N   . ALA A 213 ? 0.4048 0.4140 0.4850 -0.0600 0.0273  0.0901  213 ALA A N   
1631 C CA  . ALA A 213 ? 0.4063 0.4317 0.4622 -0.0561 0.0308  0.1126  213 ALA A CA  
1632 C C   . ALA A 213 ? 0.3747 0.4343 0.4091 -0.0615 0.0126  0.0975  213 ALA A C   
1633 O O   . ALA A 213 ? 0.3675 0.4370 0.3933 -0.0671 0.0144  0.0983  213 ALA A O   
1634 C CB  . ALA A 213 ? 0.4410 0.4618 0.4703 -0.0287 0.0337  0.1413  213 ALA A CB  
1635 N N   . PHE A 214 ? 0.3628 0.4368 0.3964 -0.0587 0.0015  0.0854  214 PHE A N   
1636 C CA  . PHE A 214 ? 0.3437 0.4395 0.3714 -0.0651 -0.0075 0.0748  214 PHE A CA  
1637 C C   . PHE A 214 ? 0.3408 0.4310 0.3631 -0.0752 -0.0073 0.0628  214 PHE A C   
1638 O O   . PHE A 214 ? 0.3331 0.4328 0.3493 -0.0796 -0.0111 0.0609  214 PHE A O   
1639 C CB  . PHE A 214 ? 0.3382 0.4462 0.3832 -0.0604 -0.0055 0.0709  214 PHE A CB  
1640 C CG  . PHE A 214 ? 0.3255 0.4449 0.3787 -0.0682 -0.0036 0.0659  214 PHE A CG  
1641 C CD1 . PHE A 214 ? 0.3196 0.4598 0.3983 -0.0724 -0.0160 0.0607  214 PHE A CD1 
1642 C CD2 . PHE A 214 ? 0.3355 0.4403 0.3698 -0.0670 0.0096  0.0652  214 PHE A CD2 
1643 C CE1 . PHE A 214 ? 0.3152 0.4566 0.4180 -0.0821 -0.0091 0.0564  214 PHE A CE1 
1644 C CE2 . PHE A 214 ? 0.3384 0.4429 0.3804 -0.0701 0.0201  0.0700  214 PHE A CE2 
1645 C CZ  . PHE A 214 ? 0.3258 0.4461 0.4107 -0.0812 0.0136  0.0664  214 PHE A CZ  
1646 N N   . GLN A 215 ? 0.3601 0.4351 0.3848 -0.0740 -0.0072 0.0501  215 GLN A N   
1647 C CA  . GLN A 215 ? 0.3700 0.4450 0.3895 -0.0753 -0.0185 0.0317  215 GLN A CA  
1648 C C   . GLN A 215 ? 0.3622 0.4479 0.4104 -0.0871 -0.0201 0.0324  215 GLN A C   
1649 O O   . GLN A 215 ? 0.3539 0.4532 0.3981 -0.0858 -0.0285 0.0271  215 GLN A O   
1650 C CB  . GLN A 215 ? 0.4035 0.4610 0.4259 -0.0685 -0.0276 0.0064  215 GLN A CB  
1651 C CG  . GLN A 215 ? 0.4322 0.4779 0.4133 -0.0479 -0.0210 0.0019  215 GLN A CG  
1652 C CD  . GLN A 215 ? 0.4777 0.4995 0.4608 -0.0381 -0.0294 -0.0285 215 GLN A CD  
1653 O OE1 . GLN A 215 ? 0.4861 0.4992 0.5163 -0.0515 -0.0424 -0.0484 215 GLN A OE1 
1654 N NE2 . GLN A 215 ? 0.5151 0.5239 0.4550 -0.0138 -0.0182 -0.0340 215 GLN A NE2 
1655 N N   . GLN A 216 ? 0.3742 0.4512 0.4536 -0.0946 -0.0060 0.0433  216 GLN A N   
1656 C CA  . GLN A 216 ? 0.3786 0.4646 0.4935 -0.1035 0.0072  0.0511  216 GLN A CA  
1657 C C   . GLN A 216 ? 0.3653 0.4663 0.4449 -0.0964 0.0125  0.0648  216 GLN A C   
1658 O O   . GLN A 216 ? 0.3552 0.4727 0.4505 -0.0983 0.0129  0.0589  216 GLN A O   
1659 C CB  . GLN A 216 ? 0.4154 0.4785 0.5626 -0.1069 0.0358  0.0731  216 GLN A CB  
1660 C CG  . GLN A 216 ? 0.4437 0.4859 0.6546 -0.1189 0.0346  0.0536  216 GLN A CG  
1661 C CD  . GLN A 216 ? 0.4913 0.4993 0.7406 -0.1210 0.0737  0.0853  216 GLN A CD  
1662 O OE1 . GLN A 216 ? 0.5183 0.5260 0.8173 -0.1294 0.1059  0.1045  216 GLN A OE1 
1663 N NE2 . GLN A 216 ? 0.5206 0.4973 0.7500 -0.1094 0.0776  0.0957  216 GLN A NE2 
1664 N N   . GLN A 217 ? 0.3664 0.4634 0.4046 -0.0855 0.0131  0.0780  217 GLN A N   
1665 C CA  . GLN A 217 ? 0.3697 0.4775 0.3741 -0.0757 0.0116  0.0804  217 GLN A CA  
1666 C C   . GLN A 217 ? 0.3480 0.4652 0.3529 -0.0802 -0.0036 0.0625  217 GLN A C   
1667 O O   . GLN A 217 ? 0.3552 0.4780 0.3519 -0.0759 -0.0021 0.0572  217 GLN A O   
1668 C CB  . GLN A 217 ? 0.3874 0.4949 0.3570 -0.0594 0.0028  0.0875  217 GLN A CB  
1669 C CG  . GLN A 217 ? 0.4148 0.5310 0.3432 -0.0425 -0.0045 0.0809  217 GLN A CG  
1670 C CD  . GLN A 217 ? 0.4503 0.5590 0.3542 -0.0298 0.0250  0.0981  217 GLN A CD  
1671 O OE1 . GLN A 217 ? 0.4709 0.5647 0.3817 -0.0263 0.0536  0.1256  217 GLN A OE1 
1672 N NE2 . GLN A 217 ? 0.4632 0.5786 0.3457 -0.0219 0.0247  0.0834  217 GLN A NE2 
1673 N N   . LEU A 218 ? 0.3348 0.4481 0.3454 -0.0839 -0.0129 0.0560  218 LEU A N   
1674 C CA  . LEU A 218 ? 0.3315 0.4430 0.3385 -0.0825 -0.0180 0.0497  218 LEU A CA  
1675 C C   . LEU A 218 ? 0.3334 0.4510 0.3492 -0.0794 -0.0215 0.0436  218 LEU A C   
1676 O O   . LEU A 218 ? 0.3391 0.4559 0.3524 -0.0740 -0.0219 0.0420  218 LEU A O   
1677 C CB  . LEU A 218 ? 0.3377 0.4393 0.3371 -0.0783 -0.0160 0.0519  218 LEU A CB  
1678 C CG  . LEU A 218 ? 0.3560 0.4452 0.3402 -0.0683 -0.0109 0.0571  218 LEU A CG  
1679 C CD1 . LEU A 218 ? 0.3545 0.4387 0.3596 -0.0746 -0.0039 0.0600  218 LEU A CD1 
1680 C CD2 . LEU A 218 ? 0.3828 0.4588 0.3450 -0.0558 0.0022  0.0654  218 LEU A CD2 
1681 N N   . GLN A 219 ? 0.3366 0.4612 0.3748 -0.0820 -0.0261 0.0366  219 GLN A N   
1682 C CA  . GLN A 219 ? 0.3411 0.4838 0.4115 -0.0788 -0.0355 0.0246  219 GLN A CA  
1683 C C   . GLN A 219 ? 0.3333 0.4889 0.4256 -0.0807 -0.0172 0.0316  219 GLN A C   
1684 O O   . GLN A 219 ? 0.3375 0.5061 0.4431 -0.0714 -0.0215 0.0261  219 GLN A O   
1685 C CB  . GLN A 219 ? 0.3516 0.5033 0.4684 -0.0854 -0.0476 0.0061  219 GLN A CB  
1686 C CG  . GLN A 219 ? 0.3618 0.5430 0.5283 -0.0790 -0.0707 -0.0169 219 GLN A CG  
1687 C CD  . GLN A 219 ? 0.3868 0.5678 0.5007 -0.0515 -0.0953 -0.0214 219 GLN A CD  
1688 O OE1 . GLN A 219 ? 0.4194 0.5810 0.4752 -0.0353 -0.1078 -0.0244 219 GLN A OE1 
1689 N NE2 . GLN A 219 ? 0.3885 0.5865 0.5184 -0.0408 -0.0965 -0.0177 219 GLN A NE2 
1690 N N   . LYS A 220 ? 0.3361 0.4860 0.4243 -0.0857 0.0052  0.0456  220 LYS A N   
1691 C CA  . LYS A 220 ? 0.3520 0.5086 0.4375 -0.0778 0.0297  0.0547  220 LYS A CA  
1692 C C   . LYS A 220 ? 0.3532 0.5037 0.3986 -0.0656 0.0208  0.0456  220 LYS A C   
1693 O O   . LYS A 220 ? 0.3611 0.5207 0.4167 -0.0556 0.0311  0.0409  220 LYS A O   
1694 C CB  . LYS A 220 ? 0.3849 0.5279 0.4440 -0.0727 0.0556  0.0766  220 LYS A CB  
1695 C CG  . LYS A 220 ? 0.3977 0.5385 0.5160 -0.0845 0.0798  0.0911  220 LYS A CG  
1696 C CD  . LYS A 220 ? 0.4478 0.5638 0.5271 -0.0712 0.1102  0.1232  220 LYS A CD  
1697 C CE  . LYS A 220 ? 0.4677 0.5692 0.6211 -0.0862 0.1391  0.1401  220 LYS A CE  
1698 N NZ  . LYS A 220 ? 0.5309 0.5980 0.6389 -0.0663 0.1727  0.1807  220 LYS A NZ  
1699 N N   . ALA A 221 ? 0.3463 0.4811 0.3601 -0.0669 0.0043  0.0411  221 ALA A N   
1700 C CA  . ALA A 221 ? 0.3541 0.4766 0.3524 -0.0607 -0.0042 0.0279  221 ALA A CA  
1701 C C   . ALA A 221 ? 0.3468 0.4656 0.3658 -0.0559 -0.0077 0.0258  221 ALA A C   
1702 O O   . ALA A 221 ? 0.3671 0.4768 0.3864 -0.0458 -0.0045 0.0164  221 ALA A O   
1703 C CB  . ALA A 221 ? 0.3528 0.4643 0.3457 -0.0679 -0.0176 0.0235  221 ALA A CB  
1704 N N   . LYS A 222 ? 0.3323 0.4553 0.3620 -0.0569 -0.0165 0.0325  222 LYS A N   
1705 C CA  . LYS A 222 ? 0.3445 0.4655 0.3804 -0.0409 -0.0254 0.0336  222 LYS A CA  
1706 C C   . LYS A 222 ? 0.3428 0.4919 0.4165 -0.0313 -0.0249 0.0257  222 LYS A C   
1707 O O   . LYS A 222 ? 0.3602 0.5045 0.4398 -0.0136 -0.0257 0.0248  222 LYS A O   
1708 C CB  . LYS A 222 ? 0.3525 0.4737 0.3734 -0.0338 -0.0409 0.0370  222 LYS A CB  
1709 C CG  . LYS A 222 ? 0.3654 0.4577 0.3525 -0.0349 -0.0315 0.0505  222 LYS A CG  
1710 C CD  . LYS A 222 ? 0.3945 0.4824 0.3456 -0.0155 -0.0429 0.0532  222 LYS A CD  
1711 C CE  . LYS A 222 ? 0.4152 0.4754 0.3371 -0.0138 -0.0202 0.0718  222 LYS A CE  
1712 N NZ  . LYS A 222 ? 0.4583 0.5123 0.3276 0.0118  -0.0277 0.0713  222 LYS A NZ  
1713 N N   . ASP A 223 ? 0.3265 0.5036 0.4368 -0.0421 -0.0188 0.0219  223 ASP A N   
1714 C CA  . ASP A 223 ? 0.3256 0.5366 0.4959 -0.0365 -0.0076 0.0163  223 ASP A CA  
1715 C C   . ASP A 223 ? 0.3391 0.5399 0.4899 -0.0247 0.0180  0.0182  223 ASP A C   
1716 O O   . ASP A 223 ? 0.3494 0.5638 0.5294 -0.0072 0.0211  0.0124  223 ASP A O   
1717 C CB  . ASP A 223 ? 0.3204 0.5532 0.5452 -0.0547 0.0097  0.0186  223 ASP A CB  
1718 C CG  . ASP A 223 ? 0.3162 0.5612 0.5789 -0.0648 -0.0204 0.0034  223 ASP A CG  
1719 O OD1 . ASP A 223 ? 0.3289 0.5746 0.5704 -0.0499 -0.0568 -0.0097 223 ASP A OD1 
1720 O OD2 . ASP A 223 ? 0.3189 0.5681 0.6290 -0.0834 -0.0061 0.0043  223 ASP A OD2 
1721 N N   . GLU A 224 ? 0.3462 0.5238 0.4454 -0.0291 0.0325  0.0221  224 GLU A N   
1722 C CA  . GLU A 224 ? 0.3799 0.5423 0.4417 -0.0124 0.0494  0.0135  224 GLU A CA  
1723 C C   . GLU A 224 ? 0.3932 0.5314 0.4501 -0.0011 0.0344  -0.0007 224 GLU A C   
1724 O O   . GLU A 224 ? 0.4185 0.5543 0.4806 0.0183  0.0477  -0.0115 224 GLU A O   
1725 C CB  . GLU A 224 ? 0.3992 0.5420 0.3993 -0.0137 0.0492  0.0122  224 GLU A CB  
1726 C CG  . GLU A 224 ? 0.4539 0.5800 0.3999 0.0098  0.0562  -0.0078 224 GLU A CG  
1727 C CD  . GLU A 224 ? 0.4836 0.5979 0.3691 0.0147  0.0411  -0.0152 224 GLU A CD  
1728 O OE1 . GLU A 224 ? 0.4634 0.5668 0.3570 0.0004  0.0096  -0.0296 224 GLU A OE1 
1729 O OE2 . GLU A 224 ? 0.5284 0.6456 0.3615 0.0367  0.0627  -0.0040 224 GLU A OE2 
1730 N N   . PHE A 225 ? 0.3838 0.4994 0.4336 -0.0110 0.0133  0.0022  225 PHE A N   
1731 C CA  . PHE A 225 ? 0.4099 0.4909 0.4628 -0.0010 0.0077  -0.0019 225 PHE A CA  
1732 C C   . PHE A 225 ? 0.4240 0.5161 0.5067 0.0217  0.0068  0.0053  225 PHE A C   
1733 O O   . PHE A 225 ? 0.4525 0.5203 0.5430 0.0401  0.0134  -0.0013 225 PHE A O   
1734 C CB  . PHE A 225 ? 0.4025 0.4571 0.4483 -0.0137 -0.0011 0.0106  225 PHE A CB  
1735 C CG  . PHE A 225 ? 0.4382 0.4470 0.4961 -0.0036 0.0052  0.0162  225 PHE A CG  
1736 C CD1 . PHE A 225 ? 0.4699 0.4474 0.5438 -0.0049 0.0103  -0.0080 225 PHE A CD1 
1737 C CD2 . PHE A 225 ? 0.4559 0.4477 0.5066 0.0119  0.0070  0.0451  225 PHE A CD2 
1738 C CE1 . PHE A 225 ? 0.5135 0.4393 0.6146 0.0022  0.0222  -0.0015 225 PHE A CE1 
1739 C CE2 . PHE A 225 ? 0.5063 0.4456 0.5675 0.0256  0.0231  0.0606  225 PHE A CE2 
1740 C CZ  . PHE A 225 ? 0.5318 0.4360 0.6277 0.0173  0.0332  0.0384  225 PHE A CZ  
1741 N N   . ALA A 226 ? 0.4123 0.5414 0.5176 0.0232  -0.0054 0.0144  226 ALA A N   
1742 C CA  . ALA A 226 ? 0.4362 0.5910 0.5805 0.0495  -0.0173 0.0154  226 ALA A CA  
1743 C C   . ALA A 226 ? 0.4577 0.6347 0.6431 0.0626  0.0047  0.0035  226 ALA A C   
1744 O O   . ALA A 226 ? 0.4842 0.6595 0.6920 0.0910  0.0023  0.0027  226 ALA A O   
1745 C CB  . ALA A 226 ? 0.4140 0.6139 0.5899 0.0465  -0.0427 0.0126  226 ALA A CB  
1746 N N   . LYS A 227 ? 0.4657 0.6599 0.6554 0.0480  0.0307  -0.0020 227 LYS A N   
1747 C CA  . LYS A 227 ? 0.5080 0.7190 0.7223 0.0655  0.0643  -0.0101 227 LYS A CA  
1748 C C   . LYS A 227 ? 0.5688 0.7293 0.7331 0.0833  0.0727  -0.0256 227 LYS A C   
1749 O O   . LYS A 227 ? 0.6021 0.7640 0.7909 0.1104  0.0872  -0.0347 227 LYS A O   
1750 C CB  . LYS A 227 ? 0.5114 0.7429 0.7239 0.0531  0.0992  -0.0035 227 LYS A CB  
1751 C CG  . LYS A 227 ? 0.4790 0.7581 0.7708 0.0337  0.1000  0.0074  227 LYS A CG  
1752 C CD  . LYS A 227 ? 0.4989 0.7822 0.7851 0.0237  0.1460  0.0246  227 LYS A CD  
1753 C CE  . LYS A 227 ? 0.4688 0.7796 0.8319 -0.0044 0.1424  0.0334  227 LYS A CE  
1754 N NZ  . LYS A 227 ? 0.4980 0.7917 0.8347 -0.0126 0.1876  0.0594  227 LYS A NZ  
1755 N N   . THR A 228 ? 0.5974 0.7148 0.7036 0.0686  0.0618  -0.0331 228 THR A N   
1756 C CA  . THR A 228 ? 0.6623 0.7277 0.7383 0.0797  0.0609  -0.0582 228 THR A CA  
1757 C C   . THR A 228 ? 0.6966 0.7322 0.8074 0.0973  0.0545  -0.0531 228 THR A C   
1758 O O   . THR A 228 ? 0.7496 0.7561 0.8651 0.1202  0.0660  -0.0735 228 THR A O   
1759 C CB  . THR A 228 ? 0.6661 0.6997 0.7070 0.0557  0.0414  -0.0691 228 THR A CB  
1760 O OG1 . THR A 228 ? 0.6685 0.7249 0.6661 0.0505  0.0456  -0.0736 228 THR A OG1 
1761 C CG2 . THR A 228 ? 0.7236 0.7031 0.7620 0.0622  0.0346  -0.1041 228 THR A CG2 
1762 N N   . GLN A 229 ? 0.6873 0.7258 0.8142 0.0929  0.0373  -0.0254 229 GLN A N   
1763 C CA  . GLN A 229 ? 0.7347 0.7431 0.8812 0.1199  0.0326  -0.0091 229 GLN A CA  
1764 C C   . GLN A 229 ? 0.7594 0.8033 0.9491 0.1550  0.0378  -0.0120 229 GLN A C   
1765 O O   . GLN A 229 ? 0.8091 0.8161 1.0129 0.1841  0.0458  -0.0137 229 GLN A O   
1766 C CB  . GLN A 229 ? 0.7256 0.7342 0.8576 0.1195  0.0133  0.0232  229 GLN A CB  
1767 C CG  . GLN A 229 ? 0.7374 0.6943 0.8419 0.0966  0.0193  0.0348  229 GLN A CG  
1768 C CD  . GLN A 229 ? 0.7552 0.7038 0.8299 0.1096  0.0105  0.0714  229 GLN A CD  
1769 O OE1 . GLN A 229 ? 0.7244 0.7182 0.7829 0.1056  -0.0089 0.0733  229 GLN A OE1 
1770 N NE2 . GLN A 229 ? 0.8189 0.7041 0.8836 0.1290  0.0283  0.1007  229 GLN A NE2 
1771 N N   . LYS A 230 ? 0.7335 0.8485 0.9580 0.1522  0.0357  -0.0130 230 LYS A N   
1772 C CA  . LYS A 230 ? 0.7535 0.9184 1.0460 0.1830  0.0424  -0.0177 230 LYS A CA  
1773 C C   . LYS A 230 ? 0.8048 0.9507 1.0983 0.2017  0.0797  -0.0390 230 LYS A C   
1774 O O   . LYS A 230 ? 0.8443 0.9878 1.1754 0.2385  0.0855  -0.0420 230 LYS A O   
1775 C CB  . LYS A 230 ? 0.7086 0.9537 1.0632 0.1673  0.0406  -0.0185 230 LYS A CB  
1776 C CG  . LYS A 230 ? 0.6870 0.9611 1.0574 0.1626  -0.0053 -0.0099 230 LYS A CG  
1777 C CD  . LYS A 230 ? 0.6440 0.9766 1.0707 0.1313  -0.0049 -0.0173 230 LYS A CD  
1778 C CE  . LYS A 230 ? 0.6332 0.9820 1.0569 0.1261  -0.0554 -0.0195 230 LYS A CE  
1779 N NZ  . LYS A 230 ? 0.5963 0.9719 1.0535 0.0869  -0.0502 -0.0268 230 LYS A NZ  
1780 N N   . HIS A 231 ? 0.8225 0.9533 1.0674 0.1833  0.1031  -0.0552 231 HIS A N   
1781 C CA  . HIS A 231 ? 0.8909 1.0003 1.1127 0.2077  0.1376  -0.0824 231 HIS A CA  
1782 C C   . HIS A 231 ? 0.9562 0.9864 1.1504 0.2227  0.1290  -0.1051 231 HIS A C   
1783 O O   . HIS A 231 ? 1.0159 1.0264 1.2153 0.2561  0.1512  -0.1287 231 HIS A O   
1784 C CB  . HIS A 231 ? 0.9064 1.0207 1.0643 0.1946  0.1602  -0.0933 231 HIS A CB  
1785 C CG  . HIS A 231 ? 0.8861 1.0680 1.0849 0.1929  0.1949  -0.0719 231 HIS A CG  
1786 N ND1 . HIS A 231 ? 0.9240 1.1393 1.1620 0.2247  0.2435  -0.0732 231 HIS A ND1 
1787 C CD2 . HIS A 231 ? 0.8368 1.0558 1.0566 0.1631  0.1941  -0.0478 231 HIS A CD2 
1788 C CE1 . HIS A 231 ? 0.8982 1.1693 1.1885 0.2116  0.2748  -0.0478 231 HIS A CE1 
1789 N NE2 . HIS A 231 ? 0.8470 1.1183 1.1274 0.1736  0.2435  -0.0337 231 HIS A NE2 
1790 N N   . HIS A 232 ? 0.9562 0.9387 1.1308 0.1986  0.1021  -0.0986 232 HIS A N   
1791 C CA  . HIS A 232 ? 1.0235 0.9248 1.2005 0.2075  0.0984  -0.1146 232 HIS A CA  
1792 C C   . HIS A 232 ? 1.0554 0.9415 1.2807 0.2440  0.1012  -0.0898 232 HIS A C   
1793 O O   . HIS A 232 ? 1.1248 0.9574 1.3664 0.2711  0.1148  -0.1095 232 HIS A O   
1794 C CB  . HIS A 232 ? 1.0144 0.8724 1.1789 0.1708  0.0793  -0.1073 232 HIS A CB  
1795 C CG  . HIS A 232 ? 1.0235 0.8751 1.1502 0.1451  0.0701  -0.1468 232 HIS A CG  
1796 N ND1 . HIS A 232 ? 1.0915 0.9178 1.1934 0.1611  0.0733  -0.2013 232 HIS A ND1 
1797 C CD2 . HIS A 232 ? 0.9846 0.8522 1.0911 0.1112  0.0532  -0.1430 232 HIS A CD2 
1798 C CE1 . HIS A 232 ? 1.0937 0.9244 1.1580 0.1404  0.0532  -0.2302 232 HIS A CE1 
1799 N NE2 . HIS A 232 ? 1.0250 0.8817 1.0974 0.1088  0.0420  -0.1936 232 HIS A NE2 
1800 N N   . HIS A 233 ? 1.0175 0.9489 1.2633 0.2495  0.0846  -0.0501 233 HIS A N   
1801 C CA  . HIS A 233 ? 1.0529 0.9818 1.3364 0.2944  0.0779  -0.0239 233 HIS A CA  
1802 C C   . HIS A 233 ? 1.0387 1.0453 1.3793 0.3243  0.0852  -0.0346 233 HIS A C   
1803 O O   . HIS A 233 ? 1.0875 1.0770 1.4553 0.3578  0.1077  -0.0524 233 HIS A O   
1804 C CB  . HIS A 233 ? 1.0388 0.9788 1.3058 0.2963  0.0484  0.0184  233 HIS A CB  
1805 C CG  . HIS A 233 ? 1.0610 0.9285 1.2827 0.2707  0.0523  0.0378  233 HIS A CG  
1806 N ND1 . HIS A 233 ? 1.1338 0.9069 1.3592 0.2785  0.0749  0.0444  233 HIS A ND1 
1807 C CD2 . HIS A 233 ? 1.0244 0.9000 1.2100 0.2380  0.0417  0.0523  233 HIS A CD2 
1808 C CE1 . HIS A 233 ? 1.1375 0.8682 1.3400 0.2492  0.0811  0.0642  233 HIS A CE1 
1809 N NE2 . HIS A 233 ? 1.0719 0.8649 1.2446 0.2265  0.0611  0.0694  233 HIS A NE2 
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