data_9MS6
# 
_entry.id   9MS6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9MS6         pdb_00009ms6 10.2210/pdb9ms6/pdb 
WWPDB D_1000291613 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MS6 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              csmith@slac.stanford.edu 
_pdbx_contact_author.name_first         Clyde 
_pdbx_contact_author.name_last          Smith 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1885-1511 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smith, C.A.'  1 ? 
'Buchko, G.W.' 2 ? 
'Wu, R.'       3 ? 
'Cort, J.R.'   4 ? 
# 
_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                     
'Crystal structures of two phage endolysins identified from a metagenomic survey of south-central Washington soil' 
_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 'Buchko, G.W.'    1 ? 
primary 'Smith, C.A.'     2 ? 
primary 'Wu, R.'          3 ? 
primary 'Alfaro, T.D.'    4 ? 
primary 'McClure, R.S.'   5 ? 
primary 'Cort, J.R.'      6 ? 
primary 'Hofmockel, K.F.' 7 ? 
# 
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 'PWe1 endolysin' 23724.861 1  ? ? ? ? 
2 non-polymer syn 'SULFATE ION'    96.063    1  ? ? ? ? 
3 non-polymer syn 'BROMIDE ION'    79.904    2  ? ? ? ? 
4 water       nat water            18.015    22 ? ? ? ? 
# 
_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       
;MITDLLRAVAPNCKDPEGWGEQLTPAMEKFGIRDREDIAAFIAQLMVESGELNRVVENLSYSTKRLREVWPKRFPDDRTA
MRYANNPQALANYVYANRIGNGNEASGDGWRFRGRGPIQTTGRANYLQLERALGIPVTRKPELLETQALGALAAAKFWYD
NKLTSLALDIAGDDQEADWVTITRRINGGTEGLARRRQYRDKARKHLGLV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MITDLLRAVAPNCKDPEGWGEQLTPAMEKFGIRDREDIAAFIAQLMVESGELNRVVENLSYSTKRLREVWPKRFPDDRTA
MRYANNPQALANYVYANRIGNGNEASGDGWRFRGRGPIQTTGRANYLQLERALGIPVTRKPELLETQALGALAAAKFWYD
NKLTSLALDIAGDDQEADWVTITRRINGGTEGLARRRQYRDKARKHLGLV
;
_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 'SULFATE ION' SO4 
3 'BROMIDE ION' BR  
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   ILE n 
1 3   THR n 
1 4   ASP n 
1 5   LEU n 
1 6   LEU n 
1 7   ARG n 
1 8   ALA n 
1 9   VAL n 
1 10  ALA n 
1 11  PRO n 
1 12  ASN n 
1 13  CYS n 
1 14  LYS n 
1 15  ASP n 
1 16  PRO n 
1 17  GLU n 
1 18  GLY n 
1 19  TRP n 
1 20  GLY n 
1 21  GLU n 
1 22  GLN n 
1 23  LEU n 
1 24  THR n 
1 25  PRO n 
1 26  ALA n 
1 27  MET n 
1 28  GLU n 
1 29  LYS n 
1 30  PHE n 
1 31  GLY n 
1 32  ILE n 
1 33  ARG n 
1 34  ASP n 
1 35  ARG n 
1 36  GLU n 
1 37  ASP n 
1 38  ILE n 
1 39  ALA n 
1 40  ALA n 
1 41  PHE n 
1 42  ILE n 
1 43  ALA n 
1 44  GLN n 
1 45  LEU n 
1 46  MET n 
1 47  VAL n 
1 48  GLU n 
1 49  SER n 
1 50  GLY n 
1 51  GLU n 
1 52  LEU n 
1 53  ASN n 
1 54  ARG n 
1 55  VAL n 
1 56  VAL n 
1 57  GLU n 
1 58  ASN n 
1 59  LEU n 
1 60  SER n 
1 61  TYR n 
1 62  SER n 
1 63  THR n 
1 64  LYS n 
1 65  ARG n 
1 66  LEU n 
1 67  ARG n 
1 68  GLU n 
1 69  VAL n 
1 70  TRP n 
1 71  PRO n 
1 72  LYS n 
1 73  ARG n 
1 74  PHE n 
1 75  PRO n 
1 76  ASP n 
1 77  ASP n 
1 78  ARG n 
1 79  THR n 
1 80  ALA n 
1 81  MET n 
1 82  ARG n 
1 83  TYR n 
1 84  ALA n 
1 85  ASN n 
1 86  ASN n 
1 87  PRO n 
1 88  GLN n 
1 89  ALA n 
1 90  LEU n 
1 91  ALA n 
1 92  ASN n 
1 93  TYR n 
1 94  VAL n 
1 95  TYR n 
1 96  ALA n 
1 97  ASN n 
1 98  ARG n 
1 99  ILE n 
1 100 GLY n 
1 101 ASN n 
1 102 GLY n 
1 103 ASN n 
1 104 GLU n 
1 105 ALA n 
1 106 SER n 
1 107 GLY n 
1 108 ASP n 
1 109 GLY n 
1 110 TRP n 
1 111 ARG n 
1 112 PHE n 
1 113 ARG n 
1 114 GLY n 
1 115 ARG n 
1 116 GLY n 
1 117 PRO n 
1 118 ILE n 
1 119 GLN n 
1 120 THR n 
1 121 THR n 
1 122 GLY n 
1 123 ARG n 
1 124 ALA n 
1 125 ASN n 
1 126 TYR n 
1 127 LEU n 
1 128 GLN n 
1 129 LEU n 
1 130 GLU n 
1 131 ARG n 
1 132 ALA n 
1 133 LEU n 
1 134 GLY n 
1 135 ILE n 
1 136 PRO n 
1 137 VAL n 
1 138 THR n 
1 139 ARG n 
1 140 LYS n 
1 141 PRO n 
1 142 GLU n 
1 143 LEU n 
1 144 LEU n 
1 145 GLU n 
1 146 THR n 
1 147 GLN n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 ALA n 
1 152 LEU n 
1 153 ALA n 
1 154 ALA n 
1 155 ALA n 
1 156 LYS n 
1 157 PHE n 
1 158 TRP n 
1 159 TYR n 
1 160 ASP n 
1 161 ASN n 
1 162 LYS n 
1 163 LEU n 
1 164 THR n 
1 165 SER n 
1 166 LEU n 
1 167 ALA n 
1 168 LEU n 
1 169 ASP n 
1 170 ILE n 
1 171 ALA n 
1 172 GLY n 
1 173 ASP n 
1 174 ASP n 
1 175 GLN n 
1 176 GLU n 
1 177 ALA n 
1 178 ASP n 
1 179 TRP n 
1 180 VAL n 
1 181 THR n 
1 182 ILE n 
1 183 THR n 
1 184 ARG n 
1 185 ARG n 
1 186 ILE n 
1 187 ASN n 
1 188 GLY n 
1 189 GLY n 
1 190 THR n 
1 191 GLU n 
1 192 GLY n 
1 193 LEU n 
1 194 ALA n 
1 195 ARG n 
1 196 ARG n 
1 197 ARG n 
1 198 GLN n 
1 199 TYR n 
1 200 ARG n 
1 201 ASP n 
1 202 LYS n 
1 203 ALA n 
1 204 ARG n 
1 205 LYS n 
1 206 HIS n 
1 207 LEU n 
1 208 GLY n 
1 209 LEU n 
1 210 VAL 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                   210 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      metagenome 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     256318 
_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 
BR  non-polymer         . 'BROMIDE ION'   ? 'Br -1'          79.904  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   1   MET MET A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  TRP 19  19  19  TRP TRP A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  MET 27  27  27  MET MET A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  MET 46  46  46  MET MET A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  TRP 70  70  70  TRP TRP A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  ARG 78  78  78  ARG ALA A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 SER 106 106 106 SER SER 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 GLY 109 109 109 GLY GLY A . n 
A 1 110 TRP 110 110 110 TRP TRP A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 TRP 158 158 158 TRP TRP A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 ASP 173 173 ?   ?   ?   A . n 
A 1 174 ASP 174 174 ?   ?   ?   A . n 
A 1 175 GLN 175 175 ?   ?   ?   A . n 
A 1 176 GLU 176 176 ?   ?   ?   A . n 
A 1 177 ALA 177 177 ?   ?   ?   A . n 
A 1 178 ASP 178 178 ?   ?   ?   A . n 
A 1 179 TRP 179 179 ?   ?   ?   A . n 
A 1 180 VAL 180 180 ?   ?   ?   A . n 
A 1 181 THR 181 181 ?   ?   ?   A . n 
A 1 182 ILE 182 182 ?   ?   ?   A . n 
A 1 183 THR 183 183 ?   ?   ?   A . n 
A 1 184 ARG 184 184 ?   ?   ?   A . n 
A 1 185 ARG 185 185 ?   ?   ?   A . n 
A 1 186 ILE 186 186 ?   ?   ?   A . n 
A 1 187 ASN 187 187 ?   ?   ?   A . n 
A 1 188 GLY 188 188 ?   ?   ?   A . n 
A 1 189 GLY 189 189 ?   ?   ?   A . n 
A 1 190 THR 190 190 ?   ?   ?   A . n 
A 1 191 GLU 191 191 ?   ?   ?   A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 GLN 198 198 198 GLN GLN A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 HIS 206 206 206 HIS HIS A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 GLY 208 208 ?   ?   ?   A . n 
A 1 209 LEU 209 209 ?   ?   ?   A . n 
A 1 210 VAL 210 210 ?   ?   ?   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 SO4 1  301 1  SO4 SO4 A . 
C 3 BR  1  302 1  BR  BR  A . 
D 3 BR  1  303 2  BR  BR  A . 
E 4 HOH 1  401 7  HOH HOH A . 
E 4 HOH 2  402 20 HOH HOH A . 
E 4 HOH 3  403 13 HOH HOH A . 
E 4 HOH 4  404 9  HOH HOH A . 
E 4 HOH 5  405 1  HOH HOH A . 
E 4 HOH 6  406 25 HOH HOH A . 
E 4 HOH 7  407 14 HOH HOH A . 
E 4 HOH 8  408 27 HOH HOH A . 
E 4 HOH 9  409 16 HOH HOH A . 
E 4 HOH 10 410 10 HOH HOH A . 
E 4 HOH 11 411 4  HOH HOH A . 
E 4 HOH 12 412 2  HOH HOH A . 
E 4 HOH 13 413 3  HOH HOH A . 
E 4 HOH 14 414 18 HOH HOH A . 
E 4 HOH 15 415 22 HOH HOH A . 
E 4 HOH 16 416 28 HOH HOH A . 
E 4 HOH 17 417 11 HOH HOH A . 
E 4 HOH 18 418 8  HOH HOH A . 
E 4 HOH 19 419 6  HOH HOH A . 
E 4 HOH 20 420 17 HOH HOH A . 
E 4 HOH 21 421 24 HOH HOH A . 
E 4 HOH 22 422 26 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 78 ? CG  ? A ARG 78 CG  
2 1 Y 1 A ARG 78 ? CD  ? A ARG 78 CD  
3 1 Y 1 A ARG 78 ? NE  ? A ARG 78 NE  
4 1 Y 1 A ARG 78 ? CZ  ? A ARG 78 CZ  
5 1 Y 1 A ARG 78 ? NH1 ? A ARG 78 NH1 
6 1 Y 1 A ARG 78 ? NH2 ? A ARG 78 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21.2_5419: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_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                     9MS6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.842 
_cell.length_a_esd                 ? 
_cell.length_b                     64.842 
_cell.length_b_esd                 ? 
_cell.length_c                     85.573 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9MS6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MS6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.81 
_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              ? 
_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    '0.1 M Hepes, sodium pH 7.5, 2% v/v PEG 400, 2.0 M ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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         2023-08-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.91966 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91966 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MS6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               34.03 
_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                                     11764 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                39.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.092 
_reflns.pdbx_Rpim_I_all                                0.015 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.15 
_reflns_shell.d_res_low                                     2.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             971 
_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                               0.531 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.725 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MS6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.15 
_refine.ls_d_res_low                             34.03 
_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                     11720 
_refine.ls_number_reflns_R_free                  616 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.26 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2147 
_refine.ls_R_factor_R_free                       0.2718 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2119 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.41 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1492 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_refine_hist.number_atoms_solvent             22 
_refine_hist.number_atoms_total               1521 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        34.03 
# 
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' ? 0.008  ? 1520 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.974  ? 2052 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.410 ? 579  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 217  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 272  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.37  . . 177 2680 100.00 . . . . 0.2982 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 2.37 2.71  . . 166 2726 100.00 . . . . 0.2299 . . . . . . . . . . . 0.3078 
'X-RAY DIFFRACTION' 2.71 3.41  . . 141 2787 100.00 . . . . 0.2814 . . . . . . . . . . . 0.3304 
'X-RAY DIFFRACTION' 3.42 34.03 . . 132 2911 100.00 . . . . 0.1785 . . . . . . . . . . . 0.2370 
# 
_struct.entry_id                     9MS6 
_struct.title                        
'Crystal structure of a putative phage endolysin identified from a metagenomic survey of Prosser, Washington soil (PWe1)' 
_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        9MS6 
_struct_keywords.text            'endolysin, carbohydrate-metabolizing, soil phage enzyme, 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 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9MS6 
_struct_ref.pdbx_db_accession          9MS6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MS6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 210 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9MS6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  210 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       210 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 MET A 1   ? ALA A 10  ? MET A 1   ALA A 10  1 ? 10 
HELX_P HELX_P2  AA2 ASP A 15  ? PHE A 30  ? ASP A 15  PHE A 30  1 ? 16 
HELX_P HELX_P3  AA3 ASP A 34  ? SER A 49  ? ASP A 34  SER A 49  1 ? 16 
HELX_P HELX_P4  AA4 SER A 62  ? TRP A 70  ? SER A 62  TRP A 70  1 ? 9  
HELX_P HELX_P5  AA5 ASP A 76  ? ALA A 84  ? ASP A 76  ALA A 84  1 ? 9  
HELX_P HELX_P6  AA6 ASN A 86  ? TYR A 95  ? ASN A 86  TYR A 95  1 ? 10 
HELX_P HELX_P7  AA7 GLY A 107 ? PHE A 112 ? GLY A 107 PHE A 112 1 ? 6  
HELX_P HELX_P8  AA8 GLY A 122 ? GLY A 134 ? GLY A 122 GLY A 134 1 ? 13 
HELX_P HELX_P9  AA9 LYS A 140 ? GLU A 145 ? LYS A 140 GLU A 145 5 ? 6  
HELX_P HELX_P10 AB1 THR A 146 ? ALA A 171 ? THR A 146 ALA A 171 1 ? 26 
HELX_P HELX_P11 AB2 LEU A 193 ? HIS A 206 ? LEU A 193 HIS A 206 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9MS6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O1 A SO4 301 ? ? 1_555 O3 A SO4 301 ? ? 6_554 1.16 
2 1 O1 A SO4 301 ? ? 1_555 O4 A SO4 301 ? ? 6_554 1.43 
3 1 S  A SO4 301 ? ? 1_555 O2 A SO4 301 ? ? 6_554 1.51 
4 1 S  A SO4 301 ? ? 1_555 O3 A SO4 301 ? ? 6_554 1.52 
5 1 S  A SO4 301 ? ? 1_555 O1 A SO4 301 ? ? 6_554 1.52 
6 1 S  A SO4 301 ? ? 1_555 O4 A SO4 301 ? ? 6_554 1.52 
7 1 O2 A SO4 301 ? ? 1_555 O4 A SO4 301 ? ? 6_554 1.61 
8 1 O1 A SO4 301 ? ? 1_555 O2 A SO4 301 ? ? 6_554 1.84 
9 1 O3 A SO4 301 ? ? 1_555 O3 A SO4 301 ? ? 6_554 2.03 
# 
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 ILE A 99  ? ? 34.69  50.02 
2 1 ALA A 171 ? ? -99.53 45.40 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 65  ? ? 0.258 'SIDE CHAIN' 
2 1 ARG A 67  ? ? 0.283 'SIDE CHAIN' 
3 1 ARG A 73  ? ? 0.254 'SIDE CHAIN' 
4 1 ARG A 139 ? ? 0.175 'SIDE CHAIN' 
# 
_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    SO4 
_pdbx_struct_special_symmetry.auth_seq_id     301 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   B 
_pdbx_struct_special_symmetry.label_comp_id   SO4 
_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 -4.7823  1.5907  -3.3363  0.9541 ? 0.8644  ? 0.0088  ? 1.4031 ? 0.2945  ? 0.6386 ? 1.7436 ? 
1.1845  ? 3.7255  ? 6.4097 ? 2.6695  ? 7.8859 ? -0.2662 ? 1.0507  ? -0.2703 ? -0.7880 ? 0.8367  ? -3.2734 ? 1.1796  ? 4.3581  ? 
0.6525  ? 
2  'X-RAY DIFFRACTION' ? refined -12.7110 6.4514  2.6248   0.6159 ? 0.2433  ? 0.1069  ? 0.8328 ? 0.1276  ? 0.6177 ? 0.2941 ? 
-0.2614 ? 0.1485  ? 1.2569 ? 0.7080  ? 0.7237 ? 0.1143  ? 0.1773  ? -0.1451 ? 0.8519  ? -0.3928 ? -0.4826 ? 0.9858  ? 0.8923  ? 
0.0090  ? 
3  'X-RAY DIFFRACTION' ? refined -17.7289 -1.1073 -4.4054  1.0104 ? 0.1755  ? 0.1042  ? 0.6470 ? 0.0024  ? 0.7496 ? 0.8517 ? 
-0.5736 ? 0.6107  ? 1.1200 ? 0.2198  ? 0.6834 ? 0.0839  ? 0.3446  ? -0.5170 ? -0.3963 ? -0.1954 ? -0.0119 ? 1.8480  ? 0.0297  ? 
-0.0008 ? 
4  'X-RAY DIFFRACTION' ? refined -11.7122 12.2236 -17.4804 0.6297 ? 0.1872  ? 0.0441  ? 0.7845 ? 0.0189  ? 0.7317 ? 0.7652 ? 
0.0793  ? 0.0332  ? 0.1319 ? -0.3941 ? 0.6720 ? 0.0490  ? 0.4155  ? 0.0276  ? -0.5079 ? -0.6772 ? 0.3607  ? 2.2259  ? 1.2146  ? 
-0.0048 ? 
5  'X-RAY DIFFRACTION' ? refined -21.5348 12.2382 -32.6230 1.0383 ? -0.0359 ? -0.1071 ? 0.7929 ? -0.1832 ? 1.1295 ? 0.4896 ? 
0.4351  ? -0.2419 ? 0.3784 ? -0.2111 ? 0.4677 ? -1.0800 ? 0.8072  ? -1.1981 ? -1.5540 ? -0.0120 ? 0.8645  ? 1.0762  ? 0.6155  ? 
-0.0023 ? 
6  'X-RAY DIFFRACTION' ? refined -17.9761 20.7859 -33.8122 0.7432 ? -0.1993 ? -0.0163 ? 1.1317 ? -0.2277 ? 0.6904 ? 0.1271 ? 
0.1210  ? 0.2379  ? 0.1243 ? 0.2994  ? 0.5146 ? -0.0339 ? 2.6602  ? -0.7914 ? -1.2958 ? 0.4615  ? -0.0686 ? -0.1676 ? 1.1758  ? 
-0.0073 ? 
7  'X-RAY DIFFRACTION' ? refined -23.6934 20.1594 -18.5811 0.3958 ? -0.0203 ? -0.0740 ? 0.4260 ? 0.0042  ? 0.5560 ? 1.8296 ? 
-1.4908 ? -1.8408 ? 1.1092 ? 0.9728  ? 2.0308 ? 0.2054  ? 0.0695  ? -0.2005 ? -0.1608 ? -0.1762 ? 0.3381  ? 0.1192  ? -0.1605 ? 
0.0010  ? 
8  'X-RAY DIFFRACTION' ? refined -24.1657 19.9397 -5.1815  0.4775 ? -0.0529 ? -0.0144 ? 0.4495 ? 0.0342  ? 0.5440 ? 1.3091 ? 
-0.6436 ? -0.2252 ? 1.2695 ? -1.1156 ? 2.6580 ? -0.0054 ? -0.2931 ? 0.0912  ? 0.2308  ? 0.0278  ? 0.0423  ? -0.4544 ? -0.1676 ? 
-0.0010 ? 
9  'X-RAY DIFFRACTION' ? refined -26.7098 3.7541  -4.8691  0.7691 ? 0.0306  ? 0.0885  ? 0.6080 ? 0.0510  ? 0.6112 ? 0.9144 ? 
-0.5380 ? -0.7699 ? 1.2266 ? -0.8179 ? 2.0275 ? 0.1297  ? 0.1846  ? -0.6513 ? -0.0276 ? -0.0139 ? -0.2334 ? 1.0817  ? 0.2030  ? 
-0.0018 ? 
10 'X-RAY DIFFRACTION' ? refined -12.3775 -6.2892 -11.9732 1.4909 ? 0.2538  ? 0.0280  ? 0.9550 ? -0.0579 ? 1.0474 ? 0.2019 ? 
0.3492  ? 0.2041  ? 0.4107 ? 0.4537  ? 0.2874 ? -1.2276 ? -0.7433 ? -0.0299 ? -0.2806 ? 0.7063  ? 0.0490  ? 1.2344  ? -0.1769 ? 
-0.0151 ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 15 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 16 through 29 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 30 through 48 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 49 through 62 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 63 through 76 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 86 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 87 through 122 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 123 through 146 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 147 through 171 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 172 through 206 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 173 ? A ASP 173 
2  1 Y 1 A ASP 174 ? A ASP 174 
3  1 Y 1 A GLN 175 ? A GLN 175 
4  1 Y 1 A GLU 176 ? A GLU 176 
5  1 Y 1 A ALA 177 ? A ALA 177 
6  1 Y 1 A ASP 178 ? A ASP 178 
7  1 Y 1 A TRP 179 ? A TRP 179 
8  1 Y 1 A VAL 180 ? A VAL 180 
9  1 Y 1 A THR 181 ? A THR 181 
10 1 Y 1 A ILE 182 ? A ILE 182 
11 1 Y 1 A THR 183 ? A THR 183 
12 1 Y 1 A ARG 184 ? A ARG 184 
13 1 Y 1 A ARG 185 ? A ARG 185 
14 1 Y 1 A ILE 186 ? A ILE 186 
15 1 Y 1 A ASN 187 ? A ASN 187 
16 1 Y 1 A GLY 188 ? A GLY 188 
17 1 Y 1 A GLY 189 ? A GLY 189 
18 1 Y 1 A THR 190 ? A THR 190 
19 1 Y 1 A GLU 191 ? A GLU 191 
20 1 Y 1 A GLY 208 ? A GLY 208 
21 1 Y 1 A LEU 209 ? A LEU 209 
22 1 Y 1 A VAL 210 ? A VAL 210 
# 
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  
BR  BR   BR N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
SO4 S    S  N N 305 
SO4 O1   O  N N 306 
SO4 O2   O  N N 307 
SO4 O3   O  N N 308 
SO4 O4   O  N N 309 
THR N    N  N N 310 
THR CA   C  N S 311 
THR C    C  N N 312 
THR O    O  N N 313 
THR CB   C  N R 314 
THR OG1  O  N N 315 
THR CG2  C  N N 316 
THR OXT  O  N N 317 
THR H    H  N N 318 
THR H2   H  N N 319 
THR HA   H  N N 320 
THR HB   H  N N 321 
THR HG1  H  N N 322 
THR HG21 H  N N 323 
THR HG22 H  N N 324 
THR HG23 H  N N 325 
THR HXT  H  N N 326 
TRP N    N  N N 327 
TRP CA   C  N S 328 
TRP C    C  N N 329 
TRP O    O  N N 330 
TRP CB   C  N N 331 
TRP CG   C  Y N 332 
TRP CD1  C  Y N 333 
TRP CD2  C  Y N 334 
TRP NE1  N  Y N 335 
TRP CE2  C  Y N 336 
TRP CE3  C  Y N 337 
TRP CZ2  C  Y N 338 
TRP CZ3  C  Y N 339 
TRP CH2  C  Y N 340 
TRP OXT  O  N N 341 
TRP H    H  N N 342 
TRP H2   H  N N 343 
TRP HA   H  N N 344 
TRP HB2  H  N N 345 
TRP HB3  H  N N 346 
TRP HD1  H  N N 347 
TRP HE1  H  N N 348 
TRP HE3  H  N N 349 
TRP HZ2  H  N N 350 
TRP HZ3  H  N N 351 
TRP HH2  H  N N 352 
TRP HXT  H  N N 353 
TYR N    N  N N 354 
TYR CA   C  N S 355 
TYR C    C  N N 356 
TYR O    O  N N 357 
TYR CB   C  N N 358 
TYR CG   C  Y N 359 
TYR CD1  C  Y N 360 
TYR CD2  C  Y N 361 
TYR CE1  C  Y N 362 
TYR CE2  C  Y N 363 
TYR CZ   C  Y N 364 
TYR OH   O  N N 365 
TYR OXT  O  N N 366 
TYR H    H  N N 367 
TYR H2   H  N N 368 
TYR HA   H  N N 369 
TYR HB2  H  N N 370 
TYR HB3  H  N N 371 
TYR HD1  H  N N 372 
TYR HD2  H  N N 373 
TYR HE1  H  N N 374 
TYR HE2  H  N N 375 
TYR HH   H  N N 376 
TYR HXT  H  N N 377 
VAL N    N  N N 378 
VAL CA   C  N S 379 
VAL C    C  N N 380 
VAL O    O  N N 381 
VAL CB   C  N N 382 
VAL CG1  C  N N 383 
VAL CG2  C  N N 384 
VAL OXT  O  N N 385 
VAL H    H  N N 386 
VAL H2   H  N N 387 
VAL HA   H  N N 388 
VAL HB   H  N N 389 
VAL HG11 H  N N 390 
VAL HG12 H  N N 391 
VAL HG13 H  N N 392 
VAL HG21 H  N N 393 
VAL HG22 H  N N 394 
VAL HG23 H  N N 395 
VAL HXT  H  N N 396 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             '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                    9MS6 
_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]   0.015422 
_atom_sites.fract_transf_matrix[1][2]   0.008904 
_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]   0.017808 
_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]   0.011686 
_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 
BR 
C  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 1   ? -8.912  -2.983  4.743   1.00 71.00  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? -8.668  -1.560  4.624   1.00 68.16  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? -8.779  -1.195  3.169   1.00 78.40  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? -8.157  -1.820  2.300   1.00 81.05  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? -7.301  -1.168  5.174   1.00 80.93  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? -7.114  0.317   5.396   1.00 73.41  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? -6.333  0.699   6.983   1.00 104.43 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? -7.777  1.046   7.996   1.00 78.21  ? 1   MET A CE  1 
ATOM   9    N  N   . ILE A 1 2   ? -9.606  -0.184  2.912   1.00 71.76  ? 2   ILE A N   1 
ATOM   10   C  CA  . ILE A 1 2   ? -9.841  0.261   1.544   1.00 73.29  ? 2   ILE A CA  1 
ATOM   11   C  C   . ILE A 1 2   ? -8.552  0.779   0.937   1.00 70.90  ? 2   ILE A C   1 
ATOM   12   O  O   . ILE A 1 2   ? -8.308  0.631   -0.265  1.00 78.71  ? 2   ILE A O   1 
ATOM   13   C  CB  . ILE A 1 2   ? -10.952 1.328   1.521   1.00 70.17  ? 2   ILE A CB  1 
ATOM   14   C  CG1 . ILE A 1 2   ? -12.236 0.712   2.046   1.00 60.71  ? 2   ILE A CG1 1 
ATOM   15   C  CG2 . ILE A 1 2   ? -11.175 1.883   0.091   1.00 55.02  ? 2   ILE A CG2 1 
ATOM   16   C  CD1 . ILE A 1 2   ? -12.697 -0.470  1.175   1.00 67.35  ? 2   ILE A CD1 1 
ATOM   17   N  N   . THR A 1 3   ? -7.711  1.403   1.758   1.00 72.00  ? 3   THR A N   1 
ATOM   18   C  CA  . THR A 1 3   ? -6.483  1.981   1.240   1.00 78.39  ? 3   THR A CA  1 
ATOM   19   C  C   . THR A 1 3   ? -5.584  0.907   0.650   1.00 80.31  ? 3   THR A C   1 
ATOM   20   O  O   . THR A 1 3   ? -5.074  1.054   -0.470  1.00 80.79  ? 3   THR A O   1 
ATOM   21   C  CB  . THR A 1 3   ? -5.777  2.755   2.343   1.00 77.22  ? 3   THR A CB  1 
ATOM   22   O  OG1 . THR A 1 3   ? -6.273  4.094   2.319   1.00 72.07  ? 3   THR A OG1 1 
ATOM   23   C  CG2 . THR A 1 3   ? -4.279  2.782   2.101   1.00 78.41  ? 3   THR A CG2 1 
ATOM   24   N  N   . ASP A 1 4   ? -5.408  -0.204  1.372   1.00 79.77  ? 4   ASP A N   1 
ATOM   25   C  CA  . ASP A 1 4   ? -4.583  -1.283  0.840   1.00 86.40  ? 4   ASP A CA  1 
ATOM   26   C  C   . ASP A 1 4   ? -5.303  -2.050  -0.272  1.00 85.32  ? 4   ASP A C   1 
ATOM   27   O  O   . ASP A 1 4   ? -4.640  -2.662  -1.116  1.00 86.04  ? 4   ASP A O   1 
ATOM   28   C  CB  . ASP A 1 4   ? -4.123  -2.205  1.980   1.00 89.11  ? 4   ASP A CB  1 
ATOM   29   C  CG  . ASP A 1 4   ? -3.236  -1.474  3.009   1.00 94.29  ? 4   ASP A CG  1 
ATOM   30   O  OD1 . ASP A 1 4   ? -2.649  -0.427  2.652   1.00 98.37  ? 4   ASP A OD1 1 
ATOM   31   O  OD2 . ASP A 1 4   ? -3.127  -1.931  4.172   1.00 101.41 ? 4   ASP A OD2 1 
ATOM   32   N  N   . LEU A 1 5   ? -6.637  -1.982  -0.329  1.00 80.96  ? 5   LEU A N   1 
ATOM   33   C  CA  . LEU A 1 5   ? -7.354  -2.523  -1.484  1.00 82.53  ? 5   LEU A CA  1 
ATOM   34   C  C   . LEU A 1 5   ? -7.133  -1.664  -2.724  1.00 78.09  ? 5   LEU A C   1 
ATOM   35   O  O   . LEU A 1 5   ? -6.906  -2.190  -3.820  1.00 76.23  ? 5   LEU A O   1 
ATOM   36   C  CB  . LEU A 1 5   ? -8.851  -2.632  -1.187  1.00 76.93  ? 5   LEU A CB  1 
ATOM   37   C  CG  . LEU A 1 5   ? -9.649  -3.058  -2.422  1.00 75.72  ? 5   LEU A CG  1 
ATOM   38   C  CD1 . LEU A 1 5   ? -9.304  -4.469  -2.844  1.00 85.16  ? 5   LEU A CD1 1 
ATOM   39   C  CD2 . LEU A 1 5   ? -11.144 -2.908  -2.200  1.00 76.59  ? 5   LEU A CD2 1 
ATOM   40   N  N   . LEU A 1 6   ? -7.206  -0.337  -2.578  1.00 76.47  ? 6   LEU A N   1 
ATOM   41   C  CA  . LEU A 1 6   ? -6.946  0.533   -3.723  1.00 75.15  ? 6   LEU A CA  1 
ATOM   42   C  C   . LEU A 1 6   ? -5.555  0.303   -4.305  1.00 89.13  ? 6   LEU A C   1 
ATOM   43   O  O   . LEU A 1 6   ? -5.355  0.520   -5.506  1.00 88.44  ? 6   LEU A O   1 
ATOM   44   C  CB  . LEU A 1 6   ? -7.120  2.009   -3.349  1.00 68.41  ? 6   LEU A CB  1 
ATOM   45   C  CG  . LEU A 1 6   ? -8.497  2.460   -2.834  1.00 72.01  ? 6   LEU A CG  1 
ATOM   46   C  CD1 . LEU A 1 6   ? -8.403  3.825   -2.161  1.00 70.98  ? 6   LEU A CD1 1 
ATOM   47   C  CD2 . LEU A 1 6   ? -9.581  2.473   -3.916  1.00 67.91  ? 6   LEU A CD2 1 
ATOM   48   N  N   . ARG A 1 7   ? -4.605  -0.179  -3.497  1.00 83.19  ? 7   ARG A N   1 
ATOM   49   C  CA  . ARG A 1 7   ? -3.261  -0.455  -3.997  1.00 94.03  ? 7   ARG A CA  1 
ATOM   50   C  C   . ARG A 1 7   ? -3.188  -1.800  -4.704  1.00 98.19  ? 7   ARG A C   1 
ATOM   51   O  O   . ARG A 1 7   ? -2.543  -1.924  -5.750  1.00 105.32 ? 7   ARG A O   1 
ATOM   52   C  CB  . ARG A 1 7   ? -2.253  -0.412  -2.852  1.00 99.55  ? 7   ARG A CB  1 
ATOM   53   C  CG  . ARG A 1 7   ? -2.044  0.966   -2.310  1.00 97.99  ? 7   ARG A CG  1 
ATOM   54   C  CD  . ARG A 1 7   ? -0.566  1.255   -2.210  1.00 108.84 ? 7   ARG A CD  1 
ATOM   55   N  NE  . ARG A 1 7   ? -0.321  2.460   -1.430  1.00 107.67 ? 7   ARG A NE  1 
ATOM   56   C  CZ  . ARG A 1 7   ? -0.501  2.559   -0.117  1.00 105.19 ? 7   ARG A CZ  1 
ATOM   57   N  NH1 . ARG A 1 7   ? -0.961  1.546   0.607   1.00 100.95 ? 7   ARG A NH1 1 
ATOM   58   N  NH2 . ARG A 1 7   ? -0.207  3.703   0.491   1.00 107.27 ? 7   ARG A NH2 1 
ATOM   59   N  N   . ALA A 1 8   ? -3.818  -2.825  -4.136  1.00 94.47  ? 8   ALA A N   1 
ATOM   60   C  CA  . ALA A 1 8   ? -3.794  -4.142  -4.763  1.00 98.45  ? 8   ALA A CA  1 
ATOM   61   C  C   . ALA A 1 8   ? -4.484  -4.143  -6.120  1.00 95.73  ? 8   ALA A C   1 
ATOM   62   O  O   . ALA A 1 8   ? -4.109  -4.915  -7.010  1.00 101.85 ? 8   ALA A O   1 
ATOM   63   C  CB  . ALA A 1 8   ? -4.461  -5.161  -3.851  1.00 97.15  ? 8   ALA A CB  1 
ATOM   64   N  N   . VAL A 1 9   ? -5.509  -3.313  -6.282  1.00 93.57  ? 9   VAL A N   1 
ATOM   65   C  CA  . VAL A 1 9   ? -6.242  -3.217  -7.534  1.00 88.16  ? 9   VAL A CA  1 
ATOM   66   C  C   . VAL A 1 9   ? -5.562  -2.269  -8.515  1.00 93.94  ? 9   VAL A C   1 
ATOM   67   O  O   . VAL A 1 9   ? -5.631  -2.481  -9.730  1.00 101.25 ? 9   VAL A O   1 
ATOM   68   C  CB  . VAL A 1 9   ? -7.679  -2.772  -7.222  1.00 88.91  ? 9   VAL A CB  1 
ATOM   69   C  CG1 . VAL A 1 9   ? -8.511  -2.634  -8.492  1.00 92.83  ? 9   VAL A CG1 1 
ATOM   70   C  CG2 . VAL A 1 9   ? -8.297  -3.748  -6.277  1.00 88.99  ? 9   VAL A CG2 1 
ATOM   71   N  N   . ALA A 1 10  ? -4.895  -1.232  -8.007  1.00 97.62  ? 10  ALA A N   1 
ATOM   72   C  CA  . ALA A 1 10  ? -4.273  -0.209  -8.849  1.00 104.49 ? 10  ALA A CA  1 
ATOM   73   C  C   . ALA A 1 10  ? -3.035  0.333   -8.150  1.00 113.16 ? 10  ALA A C   1 
ATOM   74   O  O   . ALA A 1 10  ? -3.049  1.439   -7.600  1.00 104.94 ? 10  ALA A O   1 
ATOM   75   C  CB  . ALA A 1 10  ? -5.250  0.930   -9.145  1.00 97.76  ? 10  ALA A CB  1 
ATOM   76   N  N   . PRO A 1 11  ? -1.924  -0.424  -8.181  1.00 129.08 ? 11  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 11  ? -0.721  0.014   -7.439  1.00 138.76 ? 11  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 11  ? -0.242  1.390   -7.847  1.00 138.91 ? 11  PRO A C   1 
ATOM   79   O  O   . PRO A 1 11  ? 0.561   2.004   -7.131  1.00 150.29 ? 11  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 11  ? 0.324   -1.066  -7.775  1.00 138.73 ? 11  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 11  ? -0.464  -2.245  -8.267  1.00 134.32 ? 11  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 11  ? -1.690  -1.664  -8.937  1.00 128.81 ? 11  PRO A CD  1 
ATOM   83   N  N   . ASN A 1 12  ? -0.736  1.897   -8.969  1.00 121.69 ? 12  ASN A N   1 
ATOM   84   C  CA  . ASN A 1 12  ? -0.386  3.205   -9.485  1.00 124.69 ? 12  ASN A CA  1 
ATOM   85   C  C   . ASN A 1 12  ? -1.499  4.225   -9.302  1.00 114.21 ? 12  ASN A C   1 
ATOM   86   O  O   . ASN A 1 12  ? -1.411  5.325   -9.859  1.00 115.80 ? 12  ASN A O   1 
ATOM   87   C  CB  . ASN A 1 12  ? -0.039  3.073   -10.962 1.00 132.07 ? 12  ASN A CB  1 
ATOM   88   C  CG  . ASN A 1 12  ? -0.898  2.048   -11.659 1.00 132.66 ? 12  ASN A CG  1 
ATOM   89   O  OD1 . ASN A 1 12  ? -1.666  1.321   -11.016 1.00 125.68 ? 12  ASN A OD1 1 
ATOM   90   N  ND2 . ASN A 1 12  ? -0.769  1.969   -12.976 1.00 134.44 ? 12  ASN A ND2 1 
ATOM   91   N  N   . CYS A 1 13  ? -2.553  3.889   -8.557  1.00 109.18 ? 13  CYS A N   1 
ATOM   92   C  CA  . CYS A 1 13  ? -3.615  4.859   -8.332  1.00 96.85  ? 13  CYS A CA  1 
ATOM   93   C  C   . CYS A 1 13  ? -3.082  6.016   -7.500  1.00 95.95  ? 13  CYS A C   1 
ATOM   94   O  O   . CYS A 1 13  ? -2.152  5.861   -6.701  1.00 101.15 ? 13  CYS A O   1 
ATOM   95   C  CB  . CYS A 1 13  ? -4.815  4.206   -7.644  1.00 84.63  ? 13  CYS A CB  1 
ATOM   96   S  SG  . CYS A 1 13  ? -4.508  3.618   -5.944  1.00 88.46  ? 13  CYS A SG  1 
ATOM   97   N  N   . LYS A 1 14  ? -3.665  7.188   -7.719  1.00 91.67  ? 14  LYS A N   1 
ATOM   98   C  CA  . LYS A 1 14  ? -3.222  8.399   -7.050  1.00 92.98  ? 14  LYS A CA  1 
ATOM   99   C  C   . LYS A 1 14  ? -3.682  8.387   -5.597  1.00 87.11  ? 14  LYS A C   1 
ATOM   100  O  O   . LYS A 1 14  ? -4.846  8.099   -5.314  1.00 86.25  ? 14  LYS A O   1 
ATOM   101  C  CB  . LYS A 1 14  ? -3.775  9.623   -7.779  1.00 90.74  ? 14  LYS A CB  1 
ATOM   102  C  CG  . LYS A 1 14  ? -3.210  10.953  -7.311  1.00 93.88  ? 14  LYS A CG  1 
ATOM   103  C  CD  . LYS A 1 14  ? -1.850  11.224  -7.933  1.00 106.03 ? 14  LYS A CD  1 
ATOM   104  C  CE  . LYS A 1 14  ? -1.228  12.514  -7.392  1.00 112.91 ? 14  LYS A CE  1 
ATOM   105  N  NZ  . LYS A 1 14  ? -2.111  13.712  -7.566  1.00 104.38 ? 14  LYS A NZ  1 
ATOM   106  N  N   . ASP A 1 15  ? -2.749  8.662   -4.674  1.00 94.80  ? 15  ASP A N   1 
ATOM   107  C  CA  . ASP A 1 15  ? -3.001  8.911   -3.254  1.00 85.66  ? 15  ASP A CA  1 
ATOM   108  C  C   . ASP A 1 15  ? -3.994  7.924   -2.648  1.00 77.66  ? 15  ASP A C   1 
ATOM   109  O  O   . ASP A 1 15  ? -5.085  8.319   -2.221  1.00 69.38  ? 15  ASP A O   1 
ATOM   110  C  CB  . ASP A 1 15  ? -3.509  10.337  -3.059  1.00 81.42  ? 15  ASP A CB  1 
ATOM   111  C  CG  . ASP A 1 15  ? -3.725  10.691  -1.586  1.00 83.05  ? 15  ASP A CG  1 
ATOM   112  O  OD1 . ASP A 1 15  ? -3.087  10.072  -0.701  1.00 80.33  ? 15  ASP A OD1 1 
ATOM   113  O  OD2 . ASP A 1 15  ? -4.553  11.585  -1.303  1.00 82.48  ? 15  ASP A OD2 1 
ATOM   114  N  N   . PRO A 1 16  ? -3.671  6.638   -2.572  1.00 76.82  ? 16  PRO A N   1 
ATOM   115  C  CA  . PRO A 1 16  ? -4.650  5.675   -2.046  1.00 76.75  ? 16  PRO A CA  1 
ATOM   116  C  C   . PRO A 1 16  ? -4.906  5.834   -0.561  1.00 79.65  ? 16  PRO A C   1 
ATOM   117  O  O   . PRO A 1 16  ? -5.899  5.292   -0.063  1.00 71.80  ? 16  PRO A O   1 
ATOM   118  C  CB  . PRO A 1 16  ? -4.010  4.316   -2.353  1.00 75.55  ? 16  PRO A CB  1 
ATOM   119  C  CG  . PRO A 1 16  ? -2.552  4.604   -2.363  1.00 86.36  ? 16  PRO A CG  1 
ATOM   120  C  CD  . PRO A 1 16  ? -2.396  5.981   -2.939  1.00 83.16  ? 16  PRO A CD  1 
ATOM   121  N  N   . GLU A 1 17  ? -4.061  6.573   0.157   1.00 76.73  ? 17  GLU A N   1 
ATOM   122  C  CA  . GLU A 1 17  ? -4.293  6.739   1.585   1.00 82.80  ? 17  GLU A CA  1 
ATOM   123  C  C   . GLU A 1 17  ? -5.221  7.899   1.876   1.00 74.86  ? 17  GLU A C   1 
ATOM   124  O  O   . GLU A 1 17  ? -6.023  7.819   2.806   1.00 73.71  ? 17  GLU A O   1 
ATOM   125  C  CB  . GLU A 1 17  ? -2.968  6.926   2.319   1.00 77.60  ? 17  GLU A CB  1 
ATOM   126  C  CG  . GLU A 1 17  ? -1.985  5.841   1.973   1.00 93.49  ? 17  GLU A CG  1 
ATOM   127  C  CD  . GLU A 1 17  ? -0.630  6.027   2.623   1.00 109.68 ? 17  GLU A CD  1 
ATOM   128  O  OE1 . GLU A 1 17  ? -0.474  5.638   3.802   1.00 109.36 ? 17  GLU A OE1 1 
ATOM   129  O  OE2 . GLU A 1 17  ? 0.281   6.558   1.949   1.00 111.92 ? 17  GLU A OE2 1 
ATOM   130  N  N   . GLY A 1 18  ? -5.132  8.974   1.092   1.00 79.09  ? 18  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 18  ? -6.075  10.069  1.246   1.00 69.16  ? 18  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 18  ? -7.480  9.678   0.823   1.00 71.77  ? 18  GLY A C   1 
ATOM   133  O  O   . GLY A 1 18  ? -8.453  9.986   1.513   1.00 64.31  ? 18  GLY A O   1 
ATOM   134  N  N   . TRP A 1 19  ? -7.603  9.013   -0.333  1.00 72.71  ? 19  TRP A N   1 
ATOM   135  C  CA  . TRP A 1 19  ? -8.905  8.507   -0.765  1.00 69.42  ? 19  TRP A CA  1 
ATOM   136  C  C   . TRP A 1 19  ? -9.397  7.397   0.157   1.00 64.22  ? 19  TRP A C   1 
ATOM   137  O  O   . TRP A 1 19  ? -10.604 7.259   0.392   1.00 56.73  ? 19  TRP A O   1 
ATOM   138  C  CB  . TRP A 1 19  ? -8.827  7.995   -2.206  1.00 60.25  ? 19  TRP A CB  1 
ATOM   139  C  CG  . TRP A 1 19  ? -8.866  9.081   -3.235  1.00 69.21  ? 19  TRP A CG  1 
ATOM   140  C  CD1 . TRP A 1 19  ? -7.834  9.519   -4.011  1.00 64.73  ? 19  TRP A CD1 1 
ATOM   141  C  CD2 . TRP A 1 19  ? -10.006 9.864   -3.602  1.00 57.29  ? 19  TRP A CD2 1 
ATOM   142  N  NE1 . TRP A 1 19  ? -8.265  10.534  -4.837  1.00 66.21  ? 19  TRP A NE1 1 
ATOM   143  C  CE2 . TRP A 1 19  ? -9.595  10.764  -4.599  1.00 69.64  ? 19  TRP A CE2 1 
ATOM   144  C  CE3 . TRP A 1 19  ? -11.332 9.894   -3.180  1.00 56.81  ? 19  TRP A CE3 1 
ATOM   145  C  CZ2 . TRP A 1 19  ? -10.472 11.686  -5.183  1.00 69.29  ? 19  TRP A CZ2 1 
ATOM   146  C  CZ3 . TRP A 1 19  ? -12.199 10.816  -3.758  1.00 63.98  ? 19  TRP A CZ3 1 
ATOM   147  C  CH2 . TRP A 1 19  ? -11.768 11.692  -4.740  1.00 59.75  ? 19  TRP A CH2 1 
ATOM   148  N  N   . GLY A 1 20  ? -8.479  6.566   0.647   1.00 58.74  ? 20  GLY A N   1 
ATOM   149  C  CA  . GLY A 1 20  ? -8.877  5.506   1.556   1.00 66.19  ? 20  GLY A CA  1 
ATOM   150  C  C   . GLY A 1 20  ? -9.526  6.043   2.811   1.00 59.91  ? 20  GLY A C   1 
ATOM   151  O  O   . GLY A 1 20  ? -10.570 5.543   3.245   1.00 62.75  ? 20  GLY A O   1 
ATOM   152  N  N   . GLU A 1 21  ? -8.947  7.100   3.387   1.00 63.79  ? 21  GLU A N   1 
ATOM   153  C  CA  . GLU A 1 21  ? -9.531  7.701   4.585   1.00 65.90  ? 21  GLU A CA  1 
ATOM   154  C  C   . GLU A 1 21  ? -10.931 8.222   4.314   1.00 61.09  ? 21  GLU A C   1 
ATOM   155  O  O   . GLU A 1 21  ? -11.803 8.142   5.186   1.00 60.45  ? 21  GLU A O   1 
ATOM   156  C  CB  . GLU A 1 21  ? -8.654  8.835   5.114   1.00 65.53  ? 21  GLU A CB  1 
ATOM   157  C  CG  . GLU A 1 21  ? -7.621  8.370   6.128   1.00 83.24  ? 21  GLU A CG  1 
ATOM   158  C  CD  . GLU A 1 21  ? -6.308  9.134   6.035   1.00 94.57  ? 21  GLU A CD  1 
ATOM   159  O  OE1 . GLU A 1 21  ? -6.328  10.381  6.170   1.00 95.52  ? 21  GLU A OE1 1 
ATOM   160  O  OE2 . GLU A 1 21  ? -5.257  8.484   5.822   1.00 99.81  ? 21  GLU A OE2 1 
ATOM   161  N  N   . GLN A 1 22  ? -11.168 8.778   3.124   1.00 59.33  ? 22  GLN A N   1 
ATOM   162  C  CA  . GLN A 1 22  ? -12.483 9.355   2.836   1.00 62.21  ? 22  GLN A CA  1 
ATOM   163  C  C   . GLN A 1 22  ? -13.480 8.300   2.376   1.00 52.92  ? 22  GLN A C   1 
ATOM   164  O  O   . GLN A 1 22  ? -14.648 8.350   2.758   1.00 53.74  ? 22  GLN A O   1 
ATOM   165  C  CB  . GLN A 1 22  ? -12.374 10.468  1.784   1.00 57.09  ? 22  GLN A CB  1 
ATOM   166  C  CG  . GLN A 1 22  ? -11.630 11.705  2.262   1.00 57.89  ? 22  GLN A CG  1 
ATOM   167  C  CD  . GLN A 1 22  ? -12.027 12.108  3.690   1.00 67.63  ? 22  GLN A CD  1 
ATOM   168  O  OE1 . GLN A 1 22  ? -13.181 12.459  3.967   1.00 58.31  ? 22  GLN A OE1 1 
ATOM   169  N  NE2 . GLN A 1 22  ? -11.067 12.052  4.598   1.00 66.98  ? 22  GLN A NE2 1 
ATOM   170  N  N   . LEU A 1 23  ? -13.042 7.342   1.561   1.00 54.43  ? 23  LEU A N   1 
ATOM   171  C  CA  . LEU A 1 23  ? -13.961 6.333   1.055   1.00 52.56  ? 23  LEU A CA  1 
ATOM   172  C  C   . LEU A 1 23  ? -14.540 5.474   2.169   1.00 54.32  ? 23  LEU A C   1 
ATOM   173  O  O   . LEU A 1 23  ? -15.707 5.074   2.087   1.00 56.14  ? 23  LEU A O   1 
ATOM   174  C  CB  . LEU A 1 23  ? -13.250 5.449   0.025   1.00 57.08  ? 23  LEU A CB  1 
ATOM   175  C  CG  . LEU A 1 23  ? -13.045 5.957   -1.408  1.00 59.79  ? 23  LEU A CG  1 
ATOM   176  C  CD1 . LEU A 1 23  ? -12.052 5.075   -2.182  1.00 53.91  ? 23  LEU A CD1 1 
ATOM   177  C  CD2 . LEU A 1 23  ? -14.373 6.031   -2.143  1.00 58.98  ? 23  LEU A CD2 1 
ATOM   178  N  N   . THR A 1 24  ? -13.749 5.185   3.223   1.00 56.92  ? 24  THR A N   1 
ATOM   179  C  CA  . THR A 1 24  ? -14.170 4.187   4.205   1.00 56.04  ? 24  THR A CA  1 
ATOM   180  C  C   . THR A 1 24  ? -15.431 4.593   4.954   1.00 57.43  ? 24  THR A C   1 
ATOM   181  O  O   . THR A 1 24  ? -16.354 3.769   5.052   1.00 55.45  ? 24  THR A O   1 
ATOM   182  C  CB  . THR A 1 24  ? -13.033 3.862   5.186   1.00 59.00  ? 24  THR A CB  1 
ATOM   183  O  OG1 . THR A 1 24  ? -11.847 3.470   4.480   1.00 59.90  ? 24  THR A OG1 1 
ATOM   184  C  CG2 . THR A 1 24  ? -13.445 2.714   6.064   1.00 60.07  ? 24  THR A CG2 1 
ATOM   185  N  N   . PRO A 1 25  ? -15.538 5.795   5.525   1.00 61.89  ? 25  PRO A N   1 
ATOM   186  C  CA  . PRO A 1 25  ? -16.808 6.125   6.183   1.00 61.22  ? 25  PRO A CA  1 
ATOM   187  C  C   . PRO A 1 25  ? -17.942 6.321   5.191   1.00 54.60  ? 25  PRO A C   1 
ATOM   188  O  O   . PRO A 1 25  ? -19.094 5.983   5.499   1.00 57.81  ? 25  PRO A O   1 
ATOM   189  C  CB  . PRO A 1 25  ? -16.488 7.414   6.958   1.00 57.98  ? 25  PRO A CB  1 
ATOM   190  C  CG  . PRO A 1 25  ? -14.989 7.559   6.899   1.00 60.76  ? 25  PRO A CG  1 
ATOM   191  C  CD  . PRO A 1 25  ? -14.589 6.914   5.621   1.00 57.81  ? 25  PRO A CD  1 
ATOM   192  N  N   . ALA A 1 26  ? -17.657 6.840   4.002   1.00 56.03  ? 26  ALA A N   1 
ATOM   193  C  CA  . ALA A 1 26  ? -18.712 6.966   2.999   1.00 58.64  ? 26  ALA A CA  1 
ATOM   194  C  C   . ALA A 1 26  ? -19.276 5.597   2.633   1.00 59.23  ? 26  ALA A C   1 
ATOM   195  O  O   . ALA A 1 26  ? -20.496 5.434   2.518   1.00 59.63  ? 26  ALA A O   1 
ATOM   196  C  CB  . ALA A 1 26  ? -18.174 7.681   1.758   1.00 52.46  ? 26  ALA A CB  1 
ATOM   197  N  N   . MET A 1 27  ? -18.401 4.598   2.462   1.00 54.32  ? 27  MET A N   1 
ATOM   198  C  CA  . MET A 1 27  ? -18.865 3.245   2.167   1.00 62.43  ? 27  MET A CA  1 
ATOM   199  C  C   . MET A 1 27  ? -19.649 2.672   3.336   1.00 60.45  ? 27  MET A C   1 
ATOM   200  O  O   . MET A 1 27  ? -20.765 2.170   3.161   1.00 63.07  ? 27  MET A O   1 
ATOM   201  C  CB  . MET A 1 27  ? -17.681 2.349   1.819   1.00 60.12  ? 27  MET A CB  1 
ATOM   202  C  CG  . MET A 1 27  ? -17.009 2.779   0.532   1.00 55.73  ? 27  MET A CG  1 
ATOM   203  S  SD  . MET A 1 27  ? -15.505 1.904   0.189   1.00 63.83  ? 27  MET A SD  1 
ATOM   204  C  CE  . MET A 1 27  ? -16.149 0.344   -0.399  1.00 61.59  ? 27  MET A CE  1 
ATOM   205  N  N   . GLU A 1 28  ? -19.094 2.779   4.544   1.00 55.10  ? 28  GLU A N   1 
ATOM   206  C  CA  . GLU A 1 28  ? -19.749 2.223   5.720   1.00 63.89  ? 28  GLU A CA  1 
ATOM   207  C  C   . GLU A 1 28  ? -21.115 2.865   5.933   1.00 66.90  ? 28  GLU A C   1 
ATOM   208  O  O   . GLU A 1 28  ? -22.099 2.181   6.223   1.00 70.73  ? 28  GLU A O   1 
ATOM   209  C  CB  . GLU A 1 28  ? -18.851 2.427   6.939   1.00 66.46  ? 28  GLU A CB  1 
ATOM   210  C  CG  . GLU A 1 28  ? -18.807 1.256   7.890   1.00 71.34  ? 28  GLU A CG  1 
ATOM   211  C  CD  . GLU A 1 28  ? -19.995 1.246   8.830   1.00 88.54  ? 28  GLU A CD  1 
ATOM   212  O  OE1 . GLU A 1 28  ? -20.602 2.335   9.026   1.00 87.28  ? 28  GLU A OE1 1 
ATOM   213  O  OE2 . GLU A 1 28  ? -20.318 0.153   9.363   1.00 86.61  ? 28  GLU A OE2 1 
ATOM   214  N  N   . LYS A 1 29  ? -21.199 4.182   5.762   1.00 64.82  ? 29  LYS A N   1 
ATOM   215  C  CA  . LYS A 1 29  ? -22.473 4.852   5.972   1.00 65.47  ? 29  LYS A CA  1 
ATOM   216  C  C   . LYS A 1 29  ? -23.494 4.453   4.912   1.00 67.65  ? 29  LYS A C   1 
ATOM   217  O  O   . LYS A 1 29  ? -24.670 4.250   5.228   1.00 68.53  ? 29  LYS A O   1 
ATOM   218  C  CB  . LYS A 1 29  ? -22.271 6.364   5.990   1.00 61.59  ? 29  LYS A CB  1 
ATOM   219  C  CG  . LYS A 1 29  ? -21.709 6.932   7.307   1.00 56.16  ? 29  LYS A CG  1 
ATOM   220  C  CD  . LYS A 1 29  ? -21.332 8.395   7.065   1.00 64.15  ? 29  LYS A CD  1 
ATOM   221  C  CE  . LYS A 1 29  ? -19.921 8.708   7.525   1.00 69.21  ? 29  LYS A CE  1 
ATOM   222  N  NZ  . LYS A 1 29  ? -19.940 8.983   8.976   1.00 63.01  ? 29  LYS A NZ  1 
ATOM   223  N  N   . PHE A 1 30  ? -23.075 4.326   3.656   1.00 59.30  ? 30  PHE A N   1 
ATOM   224  C  CA  . PHE A 1 30  ? -24.018 3.989   2.596   1.00 63.03  ? 30  PHE A CA  1 
ATOM   225  C  C   . PHE A 1 30  ? -24.189 2.484   2.396   1.00 71.42  ? 30  PHE A C   1 
ATOM   226  O  O   . PHE A 1 30  ? -24.762 2.066   1.383   1.00 69.06  ? 30  PHE A O   1 
ATOM   227  C  CB  . PHE A 1 30  ? -23.607 4.674   1.286   1.00 62.61  ? 30  PHE A CB  1 
ATOM   228  C  CG  . PHE A 1 30  ? -24.135 6.072   1.168   1.00 54.43  ? 30  PHE A CG  1 
ATOM   229  C  CD1 . PHE A 1 30  ? -25.496 6.291   1.073   1.00 49.66  ? 30  PHE A CD1 1 
ATOM   230  C  CD2 . PHE A 1 30  ? -23.288 7.159   1.205   1.00 52.88  ? 30  PHE A CD2 1 
ATOM   231  C  CE1 . PHE A 1 30  ? -26.009 7.563   0.993   1.00 47.77  ? 30  PHE A CE1 1 
ATOM   232  C  CE2 . PHE A 1 30  ? -23.801 8.438   1.122   1.00 54.89  ? 30  PHE A CE2 1 
ATOM   233  C  CZ  . PHE A 1 30  ? -25.171 8.635   1.021   1.00 50.56  ? 30  PHE A CZ  1 
ATOM   234  N  N   . GLY A 1 31  ? -23.745 1.671   3.352   1.00 70.94  ? 31  GLY A N   1 
ATOM   235  C  CA  . GLY A 1 31  ? -23.974 0.242   3.286   1.00 72.87  ? 31  GLY A CA  1 
ATOM   236  C  C   . GLY A 1 31  ? -23.172 -0.503  2.252   1.00 78.23  ? 31  GLY A C   1 
ATOM   237  O  O   . GLY A 1 31  ? -23.599 -1.574  1.790   1.00 80.43  ? 31  GLY A O   1 
ATOM   238  N  N   . ILE A 1 32  ? -22.022 0.031   1.860   1.00 75.58  ? 32  ILE A N   1 
ATOM   239  C  CA  . ILE A 1 32  ? -21.149 -0.682  0.928   1.00 76.17  ? 32  ILE A CA  1 
ATOM   240  C  C   . ILE A 1 32  ? -20.214 -1.523  1.808   1.00 80.50  ? 32  ILE A C   1 
ATOM   241  O  O   . ILE A 1 32  ? -19.103 -1.134  2.154   1.00 77.42  ? 32  ILE A O   1 
ATOM   242  C  CB  . ILE A 1 32  ? -20.405 0.269   -0.011  1.00 73.37  ? 32  ILE A CB  1 
ATOM   243  C  CG1 . ILE A 1 32  ? -21.429 1.144   -0.757  1.00 69.94  ? 32  ILE A CG1 1 
ATOM   244  C  CG2 . ILE A 1 32  ? -19.570 -0.495  -0.997  1.00 68.42  ? 32  ILE A CG2 1 
ATOM   245  C  CD1 . ILE A 1 32  ? -20.902 2.477   -1.210  1.00 66.55  ? 32  ILE A CD1 1 
ATOM   246  N  N   . ARG A 1 33  ? -20.726 -2.695  2.197   1.00 87.72  ? 33  ARG A N   1 
ATOM   247  C  CA  . ARG A 1 33  ? -20.089 -3.505  3.234   1.00 90.51  ? 33  ARG A CA  1 
ATOM   248  C  C   . ARG A 1 33  ? -19.769 -4.924  2.769   1.00 100.33 ? 33  ARG A C   1 
ATOM   249  O  O   . ARG A 1 33  ? -18.805 -5.519  3.256   1.00 103.75 ? 33  ARG A O   1 
ATOM   250  C  CB  . ARG A 1 33  ? -20.975 -3.563  4.490   1.00 93.26  ? 33  ARG A CB  1 
ATOM   251  C  CG  . ARG A 1 33  ? -21.252 -2.211  5.192   1.00 93.06  ? 33  ARG A CG  1 
ATOM   252  C  CD  . ARG A 1 33  ? -22.289 -2.360  6.334   1.00 94.89  ? 33  ARG A CD  1 
ATOM   253  N  NE  . ARG A 1 33  ? -22.810 -1.082  6.822   1.00 94.69  ? 33  ARG A NE  1 
ATOM   254  C  CZ  . ARG A 1 33  ? -24.024 -0.908  7.334   1.00 92.69  ? 33  ARG A CZ  1 
ATOM   255  N  NH1 . ARG A 1 33  ? -24.886 -1.910  7.427   1.00 92.71  ? 33  ARG A NH1 1 
ATOM   256  N  NH2 . ARG A 1 33  ? -24.387 0.303   7.754   1.00 86.99  ? 33  ARG A NH2 1 
ATOM   257  N  N   . ASP A 1 34  ? -20.563 -5.488  1.859   1.00 92.51  ? 34  ASP A N   1 
ATOM   258  C  CA  . ASP A 1 34  ? -20.411 -6.900  1.521   1.00 93.46  ? 34  ASP A CA  1 
ATOM   259  C  C   . ASP A 1 34  ? -19.254 -7.117  0.549   1.00 88.99  ? 34  ASP A C   1 
ATOM   260  O  O   . ASP A 1 34  ? -18.852 -6.220  -0.193  1.00 79.34  ? 34  ASP A O   1 
ATOM   261  C  CB  . ASP A 1 34  ? -21.710 -7.470  0.940   1.00 91.31  ? 34  ASP A CB  1 
ATOM   262  C  CG  . ASP A 1 34  ? -22.751 -7.762  2.019   1.00 97.96  ? 34  ASP A CG  1 
ATOM   263  O  OD1 . ASP A 1 34  ? -22.490 -8.631  2.881   1.00 102.92 ? 34  ASP A OD1 1 
ATOM   264  O  OD2 . ASP A 1 34  ? -23.816 -7.106  2.017   1.00 94.84  ? 34  ASP A OD2 1 
ATOM   265  N  N   . ARG A 1 35  ? -18.736 -8.348  0.558   1.00 86.64  ? 35  ARG A N   1 
ATOM   266  C  CA  . ARG A 1 35  ? -17.490 -8.674  -0.130  1.00 84.43  ? 35  ARG A CA  1 
ATOM   267  C  C   . ARG A 1 35  ? -17.542 -8.301  -1.604  1.00 84.93  ? 35  ARG A C   1 
ATOM   268  O  O   . ARG A 1 35  ? -16.758 -7.471  -2.071  1.00 84.00  ? 35  ARG A O   1 
ATOM   269  C  CB  . ARG A 1 35  ? -17.179 -10.165 0.021   1.00 94.28  ? 35  ARG A CB  1 
ATOM   270  C  CG  . ARG A 1 35  ? -17.220 -10.678 1.446   1.00 95.88  ? 35  ARG A CG  1 
ATOM   271  C  CD  . ARG A 1 35  ? -18.507 -11.430 1.688   1.00 96.57  ? 35  ARG A CD  1 
ATOM   272  N  NE  . ARG A 1 35  ? -18.599 -11.937 3.049   1.00 97.81  ? 35  ARG A NE  1 
ATOM   273  C  CZ  . ARG A 1 35  ? -19.205 -11.303 4.040   1.00 99.94  ? 35  ARG A CZ  1 
ATOM   274  N  NH1 . ARG A 1 35  ? -19.741 -10.105 3.869   1.00 91.70  ? 35  ARG A NH1 1 
ATOM   275  N  NH2 . ARG A 1 35  ? -19.285 -11.890 5.231   1.00 103.86 ? 35  ARG A NH2 1 
ATOM   276  N  N   . GLU A 1 36  ? -18.448 -8.923  -2.362  1.00 88.96  ? 36  GLU A N   1 
ATOM   277  C  CA  . GLU A 1 36  ? -18.549 -8.610  -3.787  1.00 88.68  ? 36  GLU A CA  1 
ATOM   278  C  C   . GLU A 1 36  ? -18.941 -7.151  -3.990  1.00 81.73  ? 36  GLU A C   1 
ATOM   279  O  O   . GLU A 1 36  ? -18.378 -6.459  -4.845  1.00 79.34  ? 36  GLU A O   1 
ATOM   280  C  CB  . GLU A 1 36  ? -19.557 -9.543  -4.472  1.00 90.80  ? 36  GLU A CB  1 
ATOM   281  C  CG  . GLU A 1 36  ? -19.205 -11.033 -4.420  1.00 92.60  ? 36  GLU A CG  1 
ATOM   282  C  CD  . GLU A 1 36  ? -18.447 -11.514 -5.654  1.00 100.13 ? 36  GLU A CD  1 
ATOM   283  O  OE1 . GLU A 1 36  ? -18.332 -10.751 -6.640  1.00 100.67 ? 36  GLU A OE1 1 
ATOM   284  O  OE2 . GLU A 1 36  ? -17.964 -12.663 -5.636  1.00 101.25 ? 36  GLU A OE2 1 
ATOM   285  N  N   . ASP A 1 37  ? -19.905 -6.671  -3.201  1.00 78.65  ? 37  ASP A N   1 
ATOM   286  C  CA  . ASP A 1 37  ? -20.346 -5.279  -3.252  1.00 83.90  ? 37  ASP A CA  1 
ATOM   287  C  C   . ASP A 1 37  ? -19.164 -4.310  -3.271  1.00 79.75  ? 37  ASP A C   1 
ATOM   288  O  O   . ASP A 1 37  ? -19.072 -3.438  -4.141  1.00 78.69  ? 37  ASP A O   1 
ATOM   289  C  CB  . ASP A 1 37  ? -21.262 -5.004  -2.052  1.00 86.50  ? 37  ASP A CB  1 
ATOM   290  C  CG  . ASP A 1 37  ? -22.286 -3.911  -2.322  1.00 90.47  ? 37  ASP A CG  1 
ATOM   291  O  OD1 . ASP A 1 37  ? -22.876 -3.906  -3.421  1.00 93.56  ? 37  ASP A OD1 1 
ATOM   292  O  OD2 . ASP A 1 37  ? -22.507 -3.056  -1.430  1.00 86.26  ? 37  ASP A OD2 1 
ATOM   293  N  N   . ILE A 1 38  ? -18.223 -4.485  -2.341  1.00 81.81  ? 38  ILE A N   1 
ATOM   294  C  CA  . ILE A 1 38  ? -17.062 -3.597  -2.260  1.00 80.47  ? 38  ILE A CA  1 
ATOM   295  C  C   . ILE A 1 38  ? -16.195 -3.726  -3.511  1.00 76.76  ? 38  ILE A C   1 
ATOM   296  O  O   . ILE A 1 38  ? -15.667 -2.725  -4.025  1.00 72.55  ? 38  ILE A O   1 
ATOM   297  C  CB  . ILE A 1 38  ? -16.259 -3.887  -0.974  1.00 78.32  ? 38  ILE A CB  1 
ATOM   298  C  CG1 . ILE A 1 38  ? -17.131 -3.679  0.257   1.00 78.35  ? 38  ILE A CG1 1 
ATOM   299  C  CG2 . ILE A 1 38  ? -15.038 -2.984  -0.855  1.00 71.71  ? 38  ILE A CG2 1 
ATOM   300  C  CD1 . ILE A 1 38  ? -16.406 -3.980  1.523   1.00 76.54  ? 38  ILE A CD1 1 
ATOM   301  N  N   . ALA A 1 39  ? -16.044 -4.953  -4.031  1.00 76.61  ? 39  ALA A N   1 
ATOM   302  C  CA  . ALA A 1 39  ? -15.150 -5.185  -5.164  1.00 76.05  ? 39  ALA A CA  1 
ATOM   303  C  C   . ALA A 1 39  ? -15.662 -4.498  -6.420  1.00 72.39  ? 39  ALA A C   1 
ATOM   304  O  O   . ALA A 1 39  ? -14.893 -3.859  -7.145  1.00 71.61  ? 39  ALA A O   1 
ATOM   305  C  CB  . ALA A 1 39  ? -14.974 -6.685  -5.412  1.00 81.94  ? 39  ALA A CB  1 
ATOM   306  N  N   . ALA A 1 40  ? -16.962 -4.640  -6.700  1.00 73.63  ? 40  ALA A N   1 
ATOM   307  C  CA  . ALA A 1 40  ? -17.549 -3.994  -7.872  1.00 76.22  ? 40  ALA A CA  1 
ATOM   308  C  C   . ALA A 1 40  ? -17.499 -2.479  -7.745  1.00 72.18  ? 40  ALA A C   1 
ATOM   309  O  O   . ALA A 1 40  ? -17.154 -1.779  -8.705  1.00 68.50  ? 40  ALA A O   1 
ATOM   310  C  CB  . ALA A 1 40  ? -18.989 -4.463  -8.073  1.00 78.41  ? 40  ALA A CB  1 
ATOM   311  N  N   . PHE A 1 41  ? -17.860 -1.951  -6.568  1.00 70.37  ? 41  PHE A N   1 
ATOM   312  C  CA  . PHE A 1 41  ? -17.794 -0.510  -6.346  1.00 63.44  ? 41  PHE A CA  1 
ATOM   313  C  C   . PHE A 1 41  ? -16.412 0.016   -6.680  1.00 67.19  ? 41  PHE A C   1 
ATOM   314  O  O   . PHE A 1 41  ? -16.253 0.910   -7.524  1.00 61.72  ? 41  PHE A O   1 
ATOM   315  C  CB  . PHE A 1 41  ? -18.136 -0.177  -4.899  1.00 67.18  ? 41  PHE A CB  1 
ATOM   316  C  CG  . PHE A 1 41  ? -17.931 1.268   -4.543  1.00 67.58  ? 41  PHE A CG  1 
ATOM   317  C  CD1 . PHE A 1 41  ? -18.746 2.243   -5.073  1.00 56.62  ? 41  PHE A CD1 1 
ATOM   318  C  CD2 . PHE A 1 41  ? -16.936 1.645   -3.658  1.00 67.22  ? 41  PHE A CD2 1 
ATOM   319  C  CE1 . PHE A 1 41  ? -18.569 3.567   -4.733  1.00 60.08  ? 41  PHE A CE1 1 
ATOM   320  C  CE2 . PHE A 1 41  ? -16.761 2.965   -3.318  1.00 58.81  ? 41  PHE A CE2 1 
ATOM   321  C  CZ  . PHE A 1 41  ? -17.587 3.926   -3.855  1.00 53.03  ? 41  PHE A CZ  1 
ATOM   322  N  N   . ILE A 1 42  ? -15.396 -0.574  -6.056  1.00 63.58  ? 42  ILE A N   1 
ATOM   323  C  CA  . ILE A 1 42  ? -14.032 -0.122  -6.268  1.00 62.99  ? 42  ILE A CA  1 
ATOM   324  C  C   . ILE A 1 42  ? -13.663 -0.209  -7.744  1.00 66.77  ? 42  ILE A C   1 
ATOM   325  O  O   . ILE A 1 42  ? -13.056 0.720   -8.295  1.00 63.66  ? 42  ILE A O   1 
ATOM   326  C  CB  . ILE A 1 42  ? -13.077 -0.927  -5.370  1.00 64.17  ? 42  ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 42  ? -13.295 -0.565  -3.895  1.00 66.63  ? 42  ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 42  ? -11.630 -0.748  -5.811  1.00 64.62  ? 42  ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 42  ? -12.965 0.883   -3.535  1.00 66.08  ? 42  ILE A CD1 1 
ATOM   330  N  N   . ALA A 1 43  ? -14.059 -1.299  -8.419  1.00 67.22  ? 43  ALA A N   1 
ATOM   331  C  CA  . ALA A 1 43  ? -13.742 -1.460  -9.840  1.00 70.95  ? 43  ALA A CA  1 
ATOM   332  C  C   . ALA A 1 43  ? -14.342 -0.335  -10.670 1.00 67.96  ? 43  ALA A C   1 
ATOM   333  O  O   . ALA A 1 43  ? -13.656 0.277   -11.493 1.00 68.91  ? 43  ALA A O   1 
ATOM   334  C  CB  . ALA A 1 43  ? -14.240 -2.810  -10.364 1.00 72.12  ? 43  ALA A CB  1 
ATOM   335  N  N   . GLN A 1 44  ? -15.640 -0.082  -10.486 1.00 66.17  ? 44  GLN A N   1 
ATOM   336  C  CA  . GLN A 1 44  ? -16.302 1.026   -11.167 1.00 70.25  ? 44  GLN A CA  1 
ATOM   337  C  C   . GLN A 1 44  ? -15.630 2.352   -10.836 1.00 64.26  ? 44  GLN A C   1 
ATOM   338  O  O   . GLN A 1 44  ? -15.387 3.177   -11.727 1.00 64.55  ? 44  GLN A O   1 
ATOM   339  C  CB  . GLN A 1 44  ? -17.780 1.051   -10.782 1.00 63.74  ? 44  GLN A CB  1 
ATOM   340  C  CG  . GLN A 1 44  ? -18.501 2.318   -11.148 1.00 71.62  ? 44  GLN A CG  1 
ATOM   341  C  CD  . GLN A 1 44  ? -18.870 2.383   -12.621 1.00 73.97  ? 44  GLN A CD  1 
ATOM   342  O  OE1 . GLN A 1 44  ? -18.007 2.509   -13.488 1.00 73.34  ? 44  GLN A OE1 1 
ATOM   343  N  NE2 . GLN A 1 44  ? -20.166 2.303   -12.906 1.00 75.65  ? 44  GLN A NE2 1 
ATOM   344  N  N   . LEU A 1 45  ? -15.291 2.553   -9.565  1.00 61.16  ? 45  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 45  ? -14.563 3.747   -9.150  1.00 59.90  ? 45  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 45  ? -13.235 3.864   -9.887  1.00 63.26  ? 45  LEU A C   1 
ATOM   347  O  O   . LEU A 1 45  ? -12.817 4.969   -10.265 1.00 59.08  ? 45  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 45  ? -14.333 3.692   -7.638  1.00 61.68  ? 45  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 45  ? -13.934 4.858   -6.722  1.00 59.69  ? 45  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 45  ? -12.607 5.437   -7.122  1.00 62.43  ? 45  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 45  ? -15.011 5.960   -6.653  1.00 61.56  ? 45  LEU A CD2 1 
ATOM   352  N  N   . MET A 1 46  ? -12.554 2.733   -10.091 1.00 60.70  ? 46  MET A N   1 
ATOM   353  C  CA  . MET A 1 46  ? -11.201 2.770   -10.627 1.00 65.85  ? 46  MET A CA  1 
ATOM   354  C  C   . MET A 1 46  ? -11.200 3.072   -12.116 1.00 67.76  ? 46  MET A C   1 
ATOM   355  O  O   . MET A 1 46  ? -10.284 3.731   -12.613 1.00 66.58  ? 46  MET A O   1 
ATOM   356  C  CB  . MET A 1 46  ? -10.478 1.448   -10.354 1.00 73.82  ? 46  MET A CB  1 
ATOM   357  C  CG  . MET A 1 46  ? -9.921  1.290   -8.948  1.00 76.81  ? 46  MET A CG  1 
ATOM   358  S  SD  . MET A 1 46  ? -8.602  2.471   -8.587  1.00 75.42  ? 46  MET A SD  1 
ATOM   359  C  CE  . MET A 1 46  ? -9.548  3.764   -7.825  1.00 74.75  ? 46  MET A CE  1 
ATOM   360  N  N   . VAL A 1 47  ? -12.203 2.588   -12.847 1.00 64.38  ? 47  VAL A N   1 
ATOM   361  C  CA  . VAL A 1 47  ? -12.221 2.843   -14.276 1.00 71.52  ? 47  VAL A CA  1 
ATOM   362  C  C   . VAL A 1 47  ? -12.786 4.226   -14.556 1.00 65.74  ? 47  VAL A C   1 
ATOM   363  O  O   . VAL A 1 47  ? -12.306 4.928   -15.449 1.00 72.26  ? 47  VAL A O   1 
ATOM   364  C  CB  . VAL A 1 47  ? -12.986 1.730   -15.024 1.00 77.70  ? 47  VAL A CB  1 
ATOM   365  C  CG1 . VAL A 1 47  ? -14.386 1.560   -14.473 1.00 68.17  ? 47  VAL A CG1 1 
ATOM   366  C  CG2 . VAL A 1 47  ? -13.005 2.015   -16.520 1.00 79.57  ? 47  VAL A CG2 1 
ATOM   367  N  N   . GLU A 1 48  ? -13.771 4.674   -13.769 1.00 67.30  ? 48  GLU A N   1 
ATOM   368  C  CA  . GLU A 1 48  ? -14.364 5.979   -14.043 1.00 66.46  ? 48  GLU A CA  1 
ATOM   369  C  C   . GLU A 1 48  ? -13.422 7.129   -13.683 1.00 69.33  ? 48  GLU A C   1 
ATOM   370  O  O   . GLU A 1 48  ? -13.473 8.183   -14.328 1.00 69.79  ? 48  GLU A O   1 
ATOM   371  C  CB  . GLU A 1 48  ? -15.703 6.145   -13.314 1.00 62.80  ? 48  GLU A CB  1 
ATOM   372  C  CG  . GLU A 1 48  ? -16.580 7.264   -13.921 1.00 58.08  ? 48  GLU A CG  1 
ATOM   373  C  CD  . GLU A 1 48  ? -18.009 7.314   -13.355 1.00 65.85  ? 48  GLU A CD  1 
ATOM   374  O  OE1 . GLU A 1 48  ? -18.543 6.247   -12.976 1.00 63.28  ? 48  GLU A OE1 1 
ATOM   375  O  OE2 . GLU A 1 48  ? -18.601 8.422   -13.283 1.00 67.00  ? 48  GLU A OE2 1 
ATOM   376  N  N   . SER A 1 49  ? -12.546 6.952   -12.692 1.00 64.62  ? 49  SER A N   1 
ATOM   377  C  CA  . SER A 1 49  ? -11.662 8.025   -12.238 1.00 63.32  ? 49  SER A CA  1 
ATOM   378  C  C   . SER A 1 49  ? -10.246 7.926   -12.814 1.00 62.61  ? 49  SER A C   1 
ATOM   379  O  O   . SER A 1 49  ? -9.382  8.724   -12.439 1.00 61.35  ? 49  SER A O   1 
ATOM   380  C  CB  . SER A 1 49  ? -11.588 8.052   -10.702 1.00 59.60  ? 49  SER A CB  1 
ATOM   381  O  OG  . SER A 1 49  ? -10.808 6.974   -10.199 1.00 62.08  ? 49  SER A OG  1 
ATOM   382  N  N   . GLY A 1 50  ? -9.986  6.982   -13.710 1.00 65.54  ? 50  GLY A N   1 
ATOM   383  C  CA  . GLY A 1 50  ? -8.634  6.825   -14.228 1.00 70.35  ? 50  GLY A CA  1 
ATOM   384  C  C   . GLY A 1 50  ? -7.659  6.509   -13.103 1.00 67.97  ? 50  GLY A C   1 
ATOM   385  O  O   . GLY A 1 50  ? -6.592  7.123   -12.989 1.00 67.48  ? 50  GLY A O   1 
ATOM   386  N  N   . GLU A 1 51  ? -8.058  5.566   -12.247 1.00 68.95  ? 51  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 51  ? -7.310  5.199   -11.038 1.00 70.06  ? 51  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 51  ? -7.061  6.427   -10.168 1.00 66.29  ? 51  GLU A C   1 
ATOM   389  O  O   . GLU A 1 51  ? -5.932  6.722   -9.783  1.00 66.33  ? 51  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 51  ? -5.999  4.491   -11.398 1.00 72.32  ? 51  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 51  ? -6.217  3.407   -12.447 1.00 82.83  ? 51  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 51  ? -5.011  2.491   -12.662 1.00 96.72  ? 51  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 51  ? -3.857  2.965   -12.557 1.00 99.34  ? 51  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 51  ? -5.225  1.290   -12.950 1.00 90.66  ? 51  GLU A OE2 1 
ATOM   395  N  N   . LEU A 1 52  ? -8.140  7.167   -9.889  1.00 63.61  ? 52  LEU A N   1 
ATOM   396  C  CA  . LEU A 1 52  ? -8.199  8.284   -8.944  1.00 61.25  ? 52  LEU A CA  1 
ATOM   397  C  C   . LEU A 1 52  ? -7.532  9.557   -9.447  1.00 61.33  ? 52  LEU A C   1 
ATOM   398  O  O   . LEU A 1 52  ? -7.384  10.500  -8.659  1.00 62.38  ? 52  LEU A O   1 
ATOM   399  C  CB  . LEU A 1 52  ? -7.591  7.899   -7.587  1.00 70.23  ? 52  LEU A CB  1 
ATOM   400  C  CG  . LEU A 1 52  ? -8.433  6.812   -6.932  1.00 67.14  ? 52  LEU A CG  1 
ATOM   401  C  CD1 . LEU A 1 52  ? -7.980  6.465   -5.514  1.00 74.55  ? 52  LEU A CD1 1 
ATOM   402  C  CD2 . LEU A 1 52  ? -9.875  7.296   -6.934  1.00 67.02  ? 52  LEU A CD2 1 
ATOM   403  N  N   . ASN A 1 53  ? -7.146  9.637   -10.727 1.00 68.31  ? 53  ASN A N   1 
ATOM   404  C  CA  . ASN A 1 53  ? -6.569  10.864  -11.270 1.00 64.51  ? 53  ASN A CA  1 
ATOM   405  C  C   . ASN A 1 53  ? -7.605  11.824  -11.868 1.00 62.22  ? 53  ASN A C   1 
ATOM   406  O  O   . ASN A 1 53  ? -7.308  13.016  -11.998 1.00 65.09  ? 53  ASN A O   1 
ATOM   407  C  CB  . ASN A 1 53  ? -5.513  10.534  -12.333 1.00 65.34  ? 53  ASN A CB  1 
ATOM   408  C  CG  . ASN A 1 53  ? -4.257  9.890   -11.739 1.00 74.21  ? 53  ASN A CG  1 
ATOM   409  O  OD1 . ASN A 1 53  ? -3.481  10.544  -11.034 1.00 69.31  ? 53  ASN A OD1 1 
ATOM   410  N  ND2 . ASN A 1 53  ? -4.043  8.606   -12.043 1.00 70.64  ? 53  ASN A ND2 1 
ATOM   411  N  N   . ARG A 1 54  ? -8.809  11.361  -12.218 1.00 60.85  ? 54  ARG A N   1 
ATOM   412  C  CA  . ARG A 1 54  ? -9.828  12.201  -12.849 1.00 56.63  ? 54  ARG A CA  1 
ATOM   413  C  C   . ARG A 1 54  ? -10.982 12.425  -11.885 1.00 52.13  ? 54  ARG A C   1 
ATOM   414  O  O   . ARG A 1 54  ? -11.589 11.460  -11.402 1.00 56.89  ? 54  ARG A O   1 
ATOM   415  C  CB  . ARG A 1 54  ? -10.375 11.578  -14.135 1.00 61.21  ? 54  ARG A CB  1 
ATOM   416  C  CG  . ARG A 1 54  ? -11.709 12.232  -14.570 1.00 64.25  ? 54  ARG A CG  1 
ATOM   417  C  CD  . ARG A 1 54  ? -12.254 11.753  -15.928 1.00 59.57  ? 54  ARG A CD  1 
ATOM   418  N  NE  . ARG A 1 54  ? -11.255 11.042  -16.708 1.00 73.69  ? 54  ARG A NE  1 
ATOM   419  C  CZ  . ARG A 1 54  ? -10.484 11.589  -17.641 1.00 80.08  ? 54  ARG A CZ  1 
ATOM   420  N  NH1 . ARG A 1 54  ? -10.579 12.875  -17.953 1.00 76.74  ? 54  ARG A NH1 1 
ATOM   421  N  NH2 . ARG A 1 54  ? -9.593  10.825  -18.274 1.00 76.98  ? 54  ARG A NH2 1 
ATOM   422  N  N   . VAL A 1 55  ? -11.312 13.689  -11.635 1.00 49.20  ? 55  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 55  ? -12.501 14.003  -10.853 1.00 54.95  ? 55  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 55  ? -13.426 14.971  -11.586 1.00 52.28  ? 55  VAL A C   1 
ATOM   425  O  O   . VAL A 1 55  ? -14.413 15.439  -11.010 1.00 52.53  ? 55  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 55  ? -12.103 14.552  -9.472  1.00 55.57  ? 55  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 55  ? -11.636 13.403  -8.620  1.00 59.86  ? 55  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 55  ? -10.985 15.608  -9.608  1.00 52.12  ? 55  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 56  ? -13.133 15.267  -12.861 1.00 52.80  ? 56  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 56  ? -13.979 16.117  -13.706 1.00 47.84  ? 56  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 56  ? -14.128 15.465  -15.075 1.00 51.26  ? 56  VAL A C   1 
ATOM   432  O  O   . VAL A 1 56  ? -13.159 14.931  -15.623 1.00 50.71  ? 56  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 56  ? -13.389 17.537  -13.882 1.00 54.63  ? 56  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 56  ? -14.482 18.526  -14.273 1.00 47.94  ? 56  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 56  ? -12.659 17.996  -12.637 1.00 60.12  ? 56  VAL A CG2 1 
ATOM   436  N  N   . GLU A 1 57  ? -15.326 15.558  -15.653 1.00 54.08  ? 57  GLU A N   1 
ATOM   437  C  CA  . GLU A 1 57  ? -15.625 14.853  -16.893 1.00 53.61  ? 57  GLU A CA  1 
ATOM   438  C  C   . GLU A 1 57  ? -14.649 15.209  -18.016 1.00 53.32  ? 57  GLU A C   1 
ATOM   439  O  O   . GLU A 1 57  ? -14.230 16.362  -18.172 1.00 46.97  ? 57  GLU A O   1 
ATOM   440  C  CB  . GLU A 1 57  ? -17.055 15.152  -17.336 1.00 51.60  ? 57  GLU A CB  1 
ATOM   441  C  CG  . GLU A 1 57  ? -17.484 14.358  -18.589 1.00 52.09  ? 57  GLU A CG  1 
ATOM   442  C  CD  . GLU A 1 57  ? -18.944 14.612  -18.974 1.00 55.46  ? 57  GLU A CD  1 
ATOM   443  O  OE1 . GLU A 1 57  ? -19.654 15.244  -18.167 1.00 54.43  ? 57  GLU A OE1 1 
ATOM   444  O  OE2 . GLU A 1 57  ? -19.372 14.184  -20.072 1.00 54.68  ? 57  GLU A OE2 1 
ATOM   445  N  N   . ASN A 1 58  ? -14.259 14.193  -18.784 1.00 53.35  ? 58  ASN A N   1 
ATOM   446  C  CA  . ASN A 1 58  ? -13.478 14.424  -19.990 1.00 60.07  ? 58  ASN A CA  1 
ATOM   447  C  C   . ASN A 1 58  ? -14.413 14.919  -21.092 1.00 54.04  ? 58  ASN A C   1 
ATOM   448  O  O   . ASN A 1 58  ? -15.384 14.245  -21.438 1.00 53.07  ? 58  ASN A O   1 
ATOM   449  C  CB  . ASN A 1 58  ? -12.761 13.148  -20.414 1.00 67.01  ? 58  ASN A CB  1 
ATOM   450  C  CG  . ASN A 1 58  ? -11.622 13.410  -21.395 1.00 69.32  ? 58  ASN A CG  1 
ATOM   451  O  OD1 . ASN A 1 58  ? -11.751 14.207  -22.328 1.00 64.88  ? 58  ASN A OD1 1 
ATOM   452  N  ND2 . ASN A 1 58  ? -10.492 12.726  -21.183 1.00 71.84  ? 58  ASN A ND2 1 
ATOM   453  N  N   . LEU A 1 59  ? -14.132 16.092  -21.645 1.00 50.54  ? 59  LEU A N   1 
ATOM   454  C  CA  . LEU A 1 59  ? -14.975 16.638  -22.700 1.00 60.24  ? 59  LEU A CA  1 
ATOM   455  C  C   . LEU A 1 59  ? -14.177 17.005  -23.948 1.00 65.82  ? 59  LEU A C   1 
ATOM   456  O  O   . LEU A 1 59  ? -14.601 17.875  -24.722 1.00 61.28  ? 59  LEU A O   1 
ATOM   457  C  CB  . LEU A 1 59  ? -15.768 17.834  -22.174 1.00 47.69  ? 59  LEU A CB  1 
ATOM   458  C  CG  . LEU A 1 59  ? -17.124 17.472  -21.576 1.00 53.02  ? 59  LEU A CG  1 
ATOM   459  C  CD1 . LEU A 1 59  ? -17.516 18.481  -20.503 1.00 56.18  ? 59  LEU A CD1 1 
ATOM   460  C  CD2 . LEU A 1 59  ? -18.181 17.430  -22.648 1.00 57.09  ? 59  LEU A CD2 1 
ATOM   461  N  N   . SER A 1 60  ? -13.049 16.336  -24.173 1.00 65.47  ? 60  SER A N   1 
ATOM   462  C  CA  . SER A 1 60  ? -12.298 16.454  -25.420 1.00 70.86  ? 60  SER A CA  1 
ATOM   463  C  C   . SER A 1 60  ? -12.611 15.263  -26.325 1.00 71.28  ? 60  SER A C   1 
ATOM   464  O  O   . SER A 1 60  ? -12.226 14.129  -26.022 1.00 74.94  ? 60  SER A O   1 
ATOM   465  C  CB  . SER A 1 60  ? -10.798 16.531  -25.145 1.00 65.73  ? 60  SER A CB  1 
ATOM   466  O  OG  . SER A 1 60  ? -10.072 16.538  -26.363 1.00 77.06  ? 60  SER A OG  1 
ATOM   467  N  N   . TYR A 1 61  ? -13.285 15.523  -27.443 1.00 75.02  ? 61  TYR A N   1 
ATOM   468  C  CA  . TYR A 1 61  ? -13.717 14.481  -28.364 1.00 82.24  ? 61  TYR A CA  1 
ATOM   469  C  C   . TYR A 1 61  ? -13.274 14.797  -29.786 1.00 87.09  ? 61  TYR A C   1 
ATOM   470  O  O   . TYR A 1 61  ? -13.268 15.959  -30.203 1.00 83.42  ? 61  TYR A O   1 
ATOM   471  C  CB  . TYR A 1 61  ? -15.238 14.338  -28.358 1.00 77.57  ? 61  TYR A CB  1 
ATOM   472  C  CG  . TYR A 1 61  ? -15.798 13.663  -27.133 1.00 77.06  ? 61  TYR A CG  1 
ATOM   473  C  CD1 . TYR A 1 61  ? -15.928 14.352  -25.928 1.00 70.34  ? 61  TYR A CD1 1 
ATOM   474  C  CD2 . TYR A 1 61  ? -16.208 12.335  -27.179 1.00 80.59  ? 61  TYR A CD2 1 
ATOM   475  C  CE1 . TYR A 1 61  ? -16.445 13.733  -24.796 1.00 65.10  ? 61  TYR A CE1 1 
ATOM   476  C  CE2 . TYR A 1 61  ? -16.734 11.702  -26.048 1.00 77.55  ? 61  TYR A CE2 1 
ATOM   477  C  CZ  . TYR A 1 61  ? -16.849 12.411  -24.856 1.00 72.02  ? 61  TYR A CZ  1 
ATOM   478  O  OH  . TYR A 1 61  ? -17.366 11.804  -23.731 1.00 58.68  ? 61  TYR A OH  1 
ATOM   479  N  N   . SER A 1 62  ? -12.933 13.750  -30.538 1.00 85.87  ? 62  SER A N   1 
ATOM   480  C  CA  . SER A 1 62  ? -12.697 13.917  -31.964 1.00 90.98  ? 62  SER A CA  1 
ATOM   481  C  C   . SER A 1 62  ? -13.984 14.346  -32.664 1.00 90.29  ? 62  SER A C   1 
ATOM   482  O  O   . SER A 1 62  ? -15.081 14.240  -32.113 1.00 89.05  ? 62  SER A O   1 
ATOM   483  C  CB  . SER A 1 62  ? -12.188 12.621  -32.589 1.00 87.19  ? 62  SER A CB  1 
ATOM   484  O  OG  . SER A 1 62  ? -12.548 12.571  -33.961 1.00 91.39  ? 62  SER A OG  1 
ATOM   485  N  N   . THR A 1 63  ? -13.842 14.844  -33.898 1.00 93.18  ? 63  THR A N   1 
ATOM   486  C  CA  . THR A 1 63  ? -15.029 15.122  -34.705 1.00 88.53  ? 63  THR A CA  1 
ATOM   487  C  C   . THR A 1 63  ? -15.740 13.828  -35.060 1.00 93.64  ? 63  THR A C   1 
ATOM   488  O  O   . THR A 1 63  ? -16.976 13.761  -35.062 1.00 92.69  ? 63  THR A O   1 
ATOM   489  C  CB  . THR A 1 63  ? -14.660 15.893  -35.977 1.00 85.86  ? 63  THR A CB  1 
ATOM   490  O  OG1 . THR A 1 63  ? -14.019 17.131  -35.636 1.00 89.70  ? 63  THR A OG1 1 
ATOM   491  C  CG2 . THR A 1 63  ? -15.910 16.190  -36.791 1.00 89.50  ? 63  THR A CG2 1 
ATOM   492  N  N   . LYS A 1 64  ? -14.982 12.741  -35.077 1.00 101.70 ? 64  LYS A N   1 
ATOM   493  C  CA  . LYS A 1 64  ? -15.623 11.428  -35.321 1.00 102.34 ? 64  LYS A CA  1 
ATOM   494  C  C   . LYS A 1 64  ? -16.253 10.911  -34.031 1.00 98.76  ? 64  LYS A C   1 
ATOM   495  O  O   . LYS A 1 64  ? -17.453 10.601  -34.049 1.00 101.66 ? 64  LYS A O   1 
ATOM   496  C  CB  . LYS A 1 64  ? -14.572 10.434  -35.814 1.00 107.86 ? 64  LYS A CB  1 
ATOM   497  C  CG  . LYS A 1 64  ? -13.867 10.837  -37.101 1.00 110.20 ? 64  LYS A CG  1 
ATOM   498  C  CD  . LYS A 1 64  ? -12.392 11.119  -36.915 1.00 113.89 ? 64  LYS A CD  1 
ATOM   499  C  CE  . LYS A 1 64  ? -11.515 10.320  -37.855 1.00 109.84 ? 64  LYS A CE  1 
ATOM   500  N  NZ  . LYS A 1 64  ? -12.082 8.978   -38.125 1.00 110.17 ? 64  LYS A NZ  1 
ATOM   501  N  N   . ARG A 1 65  ? -15.473 10.814  -32.956 1.00 98.95  ? 65  ARG A N   1 
ATOM   502  C  CA  . ARG A 1 65  ? -15.993 10.200  -31.706 1.00 98.68  ? 65  ARG A CA  1 
ATOM   503  C  C   . ARG A 1 65  ? -17.386 10.739  -31.377 1.00 94.59  ? 65  ARG A C   1 
ATOM   504  O  O   . ARG A 1 65  ? -18.254 9.941   -31.015 1.00 92.12  ? 65  ARG A O   1 
ATOM   505  C  CB  . ARG A 1 65  ? -15.041 10.489  -30.548 1.00 98.16  ? 65  ARG A CB  1 
ATOM   506  C  CG  . ARG A 1 65  ? -15.275 9.611   -29.329 1.00 102.02 ? 65  ARG A CG  1 
ATOM   507  C  CD  . ARG A 1 65  ? -14.588 8.266   -29.455 1.00 114.13 ? 65  ARG A CD  1 
ATOM   508  N  NE  . ARG A 1 65  ? -14.671 7.491   -28.226 1.00 123.02 ? 65  ARG A NE  1 
ATOM   509  C  CZ  . ARG A 1 65  ? -13.722 7.448   -27.297 1.00 123.88 ? 65  ARG A CZ  1 
ATOM   510  N  NH1 . ARG A 1 65  ? -13.382 8.545   -26.645 1.00 121.34 ? 65  ARG A NH1 1 
ATOM   511  N  NH2 . ARG A 1 65  ? -13.120 6.305   -27.020 1.00 116.84 ? 65  ARG A NH2 1 
ATOM   512  N  N   . LEU A 1 66  ? -17.573 12.049  -31.468 1.00 92.95  ? 66  LEU A N   1 
ATOM   513  C  CA  . LEU A 1 66  ? -18.872 12.656  -31.094 1.00 87.68  ? 66  LEU A CA  1 
ATOM   514  C  C   . LEU A 1 66  ? -19.989 11.965  -31.869 1.00 91.60  ? 66  LEU A C   1 
ATOM   515  O  O   . LEU A 1 66  ? -20.957 11.514  -31.237 1.00 89.54  ? 66  LEU A O   1 
ATOM   516  C  CB  . LEU A 1 66  ? -18.817 14.143  -31.448 1.00 81.96  ? 66  LEU A CB  1 
ATOM   517  C  CG  . LEU A 1 66  ? -18.081 15.031  -30.450 1.00 79.96  ? 66  LEU A CG  1 
ATOM   518  C  CD1 . LEU A 1 66  ? -18.105 16.481  -30.897 1.00 74.82  ? 66  LEU A CD1 1 
ATOM   519  C  CD2 . LEU A 1 66  ? -18.691 14.894  -29.068 1.00 67.88  ? 66  LEU A CD2 1 
ATOM   520  N  N   . ARG A 1 67  ? -19.845 11.883  -33.190 1.00 89.72  ? 67  ARG A N   1 
ATOM   521  C  CA  . ARG A 1 67  ? -20.929 11.312  -34.030 1.00 93.49  ? 67  ARG A CA  1 
ATOM   522  C  C   . ARG A 1 67  ? -21.298 9.933   -33.485 1.00 90.43  ? 67  ARG A C   1 
ATOM   523  O  O   . ARG A 1 67  ? -22.471 9.573   -33.552 1.00 88.70  ? 67  ARG A O   1 
ATOM   524  C  CB  . ARG A 1 67  ? -20.499 11.306  -35.500 1.00 93.62  ? 67  ARG A CB  1 
ATOM   525  C  CG  . ARG A 1 67  ? -20.685 12.654  -36.182 1.00 98.33  ? 67  ARG A CG  1 
ATOM   526  C  CD  . ARG A 1 67  ? -19.713 12.947  -37.309 1.00 101.47 ? 67  ARG A CD  1 
ATOM   527  N  NE  . ARG A 1 67  ? -19.935 12.127  -38.491 1.00 109.81 ? 67  ARG A NE  1 
ATOM   528  C  CZ  . ARG A 1 67  ? -21.031 12.155  -39.240 1.00 111.35 ? 67  ARG A CZ  1 
ATOM   529  N  NH1 . ARG A 1 67  ? -22.122 11.523  -38.846 1.00 107.79 ? 67  ARG A NH1 1 
ATOM   530  N  NH2 . ARG A 1 67  ? -21.028 12.798  -40.394 1.00 108.14 ? 67  ARG A NH2 1 
ATOM   531  N  N   . GLU A 1 68  ? -20.326 9.205   -32.949 1.00 91.42  ? 68  GLU A N   1 
ATOM   532  C  CA  . GLU A 1 68  ? -20.630 7.894   -32.330 1.00 89.10  ? 68  GLU A CA  1 
ATOM   533  C  C   . GLU A 1 68  ? -21.315 8.093   -30.979 1.00 93.25  ? 68  GLU A C   1 
ATOM   534  O  O   . GLU A 1 68  ? -22.496 7.745   -30.866 1.00 92.83  ? 68  GLU A O   1 
ATOM   535  C  CB  . GLU A 1 68  ? -19.334 7.119   -32.120 1.00 96.83  ? 68  GLU A CB  1 
ATOM   536  C  CG  . GLU A 1 68  ? -18.313 7.336   -33.220 1.00 100.51 ? 68  GLU A CG  1 
ATOM   537  C  CD  . GLU A 1 68  ? -16.992 6.620   -33.000 1.00 103.12 ? 68  GLU A CD  1 
ATOM   538  O  OE1 . GLU A 1 68  ? -16.757 6.149   -31.871 1.00 101.06 ? 68  GLU A OE1 1 
ATOM   539  O  OE2 . GLU A 1 68  ? -16.203 6.533   -33.959 1.00 101.81 ? 68  GLU A OE2 1 
ATOM   540  N  N   . VAL A 1 69  ? -20.592 8.626   -29.995 1.00 90.21  ? 69  VAL A N   1 
ATOM   541  C  CA  . VAL A 1 69  ? -21.143 8.764   -28.615 1.00 86.06  ? 69  VAL A CA  1 
ATOM   542  C  C   . VAL A 1 69  ? -22.544 9.372   -28.661 1.00 87.65  ? 69  VAL A C   1 
ATOM   543  O  O   . VAL A 1 69  ? -23.441 8.809   -28.024 1.00 86.70  ? 69  VAL A O   1 
ATOM   544  C  CB  . VAL A 1 69  ? -20.196 9.602   -27.742 1.00 87.07  ? 69  VAL A CB  1 
ATOM   545  C  CG1 . VAL A 1 69  ? -20.611 9.581   -26.281 1.00 86.29  ? 69  VAL A CG1 1 
ATOM   546  C  CG2 . VAL A 1 69  ? -18.755 9.144   -27.893 1.00 89.27  ? 69  VAL A CG2 1 
ATOM   547  N  N   . TRP A 1 70  ? -22.708 10.494  -29.359 1.00 89.82  ? 70  TRP A N   1 
ATOM   548  C  CA  . TRP A 1 70  ? -24.024 11.176  -29.430 1.00 86.72  ? 70  TRP A CA  1 
ATOM   549  C  C   . TRP A 1 70  ? -24.430 11.339  -30.891 1.00 86.85  ? 70  TRP A C   1 
ATOM   550  O  O   . TRP A 1 70  ? -24.216 12.427  -31.457 1.00 86.61  ? 70  TRP A O   1 
ATOM   551  C  CB  . TRP A 1 70  ? -23.942 12.535  -28.730 1.00 84.09  ? 70  TRP A CB  1 
ATOM   552  C  CG  . TRP A 1 70  ? -23.675 12.467  -27.252 1.00 84.26  ? 70  TRP A CG  1 
ATOM   553  C  CD1 . TRP A 1 70  ? -24.540 12.073  -26.276 1.00 82.99  ? 70  TRP A CD1 1 
ATOM   554  C  CD2 . TRP A 1 70  ? -22.451 12.830  -26.580 1.00 80.32  ? 70  TRP A CD2 1 
ATOM   555  N  NE1 . TRP A 1 70  ? -23.941 12.155  -25.049 1.00 75.50  ? 70  TRP A NE1 1 
ATOM   556  C  CE2 . TRP A 1 70  ? -22.662 12.617  -25.202 1.00 76.64  ? 70  TRP A CE2 1 
ATOM   557  C  CE3 . TRP A 1 70  ? -21.208 13.307  -27.006 1.00 76.65  ? 70  TRP A CE3 1 
ATOM   558  C  CZ2 . TRP A 1 70  ? -21.675 12.866  -24.253 1.00 70.40  ? 70  TRP A CZ2 1 
ATOM   559  C  CZ3 . TRP A 1 70  ? -20.234 13.552  -26.065 1.00 72.01  ? 70  TRP A CZ3 1 
ATOM   560  C  CH2 . TRP A 1 70  ? -20.466 13.336  -24.709 1.00 66.97  ? 70  TRP A CH2 1 
ATOM   561  N  N   . PRO A 1 71  ? -25.024 10.314  -31.532 1.00 92.31  ? 71  PRO A N   1 
ATOM   562  C  CA  . PRO A 1 71  ? -25.327 10.382  -32.966 1.00 89.70  ? 71  PRO A CA  1 
ATOM   563  C  C   . PRO A 1 71  ? -26.486 11.311  -33.347 1.00 93.34  ? 71  PRO A C   1 
ATOM   564  O  O   . PRO A 1 71  ? -26.482 11.823  -34.440 1.00 91.78  ? 71  PRO A O   1 
ATOM   565  C  CB  . PRO A 1 71  ? -25.713 8.933   -33.281 1.00 94.03  ? 71  PRO A CB  1 
ATOM   566  C  CG  . PRO A 1 71  ? -26.278 8.403   -31.988 1.00 96.14  ? 71  PRO A CG  1 
ATOM   567  C  CD  . PRO A 1 71  ? -25.432 9.052   -30.917 1.00 91.34  ? 71  PRO A CD  1 
ATOM   568  N  N   . LYS A 1 72  ? -27.448 11.486  -32.446 1.00 96.39  ? 72  LYS A N   1 
ATOM   569  C  CA  . LYS A 1 72  ? -28.580 12.397  -32.727 1.00 96.55  ? 72  LYS A CA  1 
ATOM   570  C  C   . LYS A 1 72  ? -28.072 13.834  -32.632 1.00 92.80  ? 72  LYS A C   1 
ATOM   571  O  O   . LYS A 1 72  ? -28.224 14.574  -33.612 1.00 92.21  ? 72  LYS A O   1 
ATOM   572  C  CB  . LYS A 1 72  ? -29.706 12.171  -31.718 1.00 102.96 ? 72  LYS A CB  1 
ATOM   573  C  CG  . LYS A 1 72  ? -29.891 10.731  -31.260 1.00 98.68  ? 72  LYS A CG  1 
ATOM   574  C  CD  . LYS A 1 72  ? -30.733 9.912   -32.211 1.00 96.71  ? 72  LYS A CD  1 
ATOM   575  C  CE  . LYS A 1 72  ? -31.727 9.018   -31.503 1.00 99.73  ? 72  LYS A CE  1 
ATOM   576  N  NZ  . LYS A 1 72  ? -32.769 8.515   -32.429 1.00 96.53  ? 72  LYS A NZ  1 
ATOM   577  N  N   . ARG A 1 73  ? -27.485 14.196  -31.492 1.00 91.66  ? 73  ARG A N   1 
ATOM   578  C  CA  . ARG A 1 73  ? -26.991 15.581  -31.287 1.00 89.79  ? 73  ARG A CA  1 
ATOM   579  C  C   . ARG A 1 73  ? -25.956 15.911  -32.360 1.00 86.45  ? 73  ARG A C   1 
ATOM   580  O  O   . ARG A 1 73  ? -25.918 17.069  -32.796 1.00 79.93  ? 73  ARG A O   1 
ATOM   581  C  CB  . ARG A 1 73  ? -26.380 15.711  -29.894 1.00 80.97  ? 73  ARG A CB  1 
ATOM   582  C  CG  . ARG A 1 73  ? -27.401 15.727  -28.767 1.00 85.31  ? 73  ARG A CG  1 
ATOM   583  C  CD  . ARG A 1 73  ? -26.850 15.060  -27.523 1.00 86.96  ? 73  ARG A CD  1 
ATOM   584  N  NE  . ARG A 1 73  ? -27.904 14.604  -26.632 1.00 83.39  ? 73  ARG A NE  1 
ATOM   585  C  CZ  . ARG A 1 73  ? -28.398 13.372  -26.628 1.00 91.47  ? 73  ARG A CZ  1 
ATOM   586  N  NH1 . ARG A 1 73  ? -28.972 12.886  -27.713 1.00 87.28  ? 73  ARG A NH1 1 
ATOM   587  N  NH2 . ARG A 1 73  ? -28.311 12.629  -25.539 1.00 95.34  ? 73  ARG A NH2 1 
ATOM   588  N  N   . PHE A 1 74  ? -25.157 14.920  -32.757 1.00 89.91  ? 74  PHE A N   1 
ATOM   589  C  CA  . PHE A 1 74  ? -24.110 15.143  -33.781 1.00 86.49  ? 74  PHE A CA  1 
ATOM   590  C  C   . PHE A 1 74  ? -24.371 14.231  -34.974 1.00 89.32  ? 74  PHE A C   1 
ATOM   591  O  O   . PHE A 1 74  ? -23.793 13.142  -35.060 1.00 89.41  ? 74  PHE A O   1 
ATOM   592  C  CB  . PHE A 1 74  ? -22.723 14.898  -33.197 1.00 79.94  ? 74  PHE A CB  1 
ATOM   593  C  CG  . PHE A 1 74  ? -22.397 15.808  -32.048 1.00 80.56  ? 74  PHE A CG  1 
ATOM   594  C  CD1 . PHE A 1 74  ? -22.245 17.167  -32.252 1.00 76.70  ? 74  PHE A CD1 1 
ATOM   595  C  CD2 . PHE A 1 74  ? -22.274 15.310  -30.765 1.00 83.74  ? 74  PHE A CD2 1 
ATOM   596  C  CE1 . PHE A 1 74  ? -21.953 18.010  -31.197 1.00 69.69  ? 74  PHE A CE1 1 
ATOM   597  C  CE2 . PHE A 1 74  ? -21.983 16.155  -29.710 1.00 76.68  ? 74  PHE A CE2 1 
ATOM   598  C  CZ  . PHE A 1 74  ? -21.823 17.502  -29.929 1.00 67.59  ? 74  PHE A CZ  1 
ATOM   599  N  N   . PRO A 1 75  ? -25.249 14.672  -35.894 1.00 93.14  ? 75  PRO A N   1 
ATOM   600  C  CA  . PRO A 1 75  ? -25.537 13.871  -37.060 1.00 95.77  ? 75  PRO A CA  1 
ATOM   601  C  C   . PRO A 1 75  ? -24.544 13.869  -38.256 1.00 103.54 ? 75  PRO A C   1 
ATOM   602  O  O   . PRO A 1 75  ? -24.327 12.887  -38.825 1.00 103.31 ? 75  PRO A O   1 
ATOM   603  C  CB  . PRO A 1 75  ? -26.783 14.542  -37.652 1.00 90.07  ? 75  PRO A CB  1 
ATOM   604  C  CG  . PRO A 1 75  ? -27.238 15.544  -36.615 1.00 94.82  ? 75  PRO A CG  1 
ATOM   605  C  CD  . PRO A 1 75  ? -25.978 15.934  -35.878 1.00 87.09  ? 75  PRO A CD  1 
ATOM   606  N  N   . ASP A 1 76  ? -24.137 15.202  -38.572 1.00 107.41 ? 76  ASP A N   1 
ATOM   607  C  CA  . ASP A 1 76  ? -23.102 15.405  -39.617 1.00 114.52 ? 76  ASP A CA  1 
ATOM   608  C  C   . ASP A 1 76  ? -21.819 15.972  -39.010 1.00 110.04 ? 76  ASP A C   1 
ATOM   609  O  O   . ASP A 1 76  ? -21.841 16.360  -37.834 1.00 103.38 ? 76  ASP A O   1 
ATOM   610  C  CB  . ASP A 1 76  ? -23.627 16.332  -40.711 1.00 115.14 ? 76  ASP A CB  1 
ATOM   611  C  CG  . ASP A 1 76  ? -24.287 17.585  -40.167 1.00 115.71 ? 76  ASP A CG  1 
ATOM   612  O  OD1 . ASP A 1 76  ? -25.064 17.467  -39.202 1.00 112.55 ? 76  ASP A OD1 1 
ATOM   613  O  OD2 . ASP A 1 76  ? -24.022 18.667  -40.716 1.00 113.54 ? 76  ASP A OD2 1 
ATOM   614  N  N   . ASP A 1 77  ? -20.756 16.031  -39.810 1.00 121.78 ? 77  ASP A N   1 
ATOM   615  C  CA  . ASP A 1 77  ? -19.467 16.586  -39.333 1.00 116.61 ? 77  ASP A CA  1 
ATOM   616  C  C   . ASP A 1 77  ? -19.608 18.103  -39.209 1.00 106.43 ? 77  ASP A C   1 
ATOM   617  O  O   . ASP A 1 77  ? -19.148 18.641  -38.199 1.00 104.91 ? 77  ASP A O   1 
ATOM   618  C  CB  . ASP A 1 77  ? -18.316 16.166  -40.248 1.00 124.07 ? 77  ASP A CB  1 
ATOM   619  C  CG  . ASP A 1 77  ? -18.472 14.766  -40.810 1.00 125.61 ? 77  ASP A CG  1 
ATOM   620  O  OD1 . ASP A 1 77  ? -19.128 14.627  -41.861 1.00 127.74 ? 77  ASP A OD1 1 
ATOM   621  O  OD2 . ASP A 1 77  ? -17.943 13.827  -40.190 1.00 129.13 ? 77  ASP A OD2 1 
ATOM   622  N  N   . ARG A 1 78  ? -20.218 18.764  -40.191 1.00 104.61 ? 78  ARG A N   1 
ATOM   623  C  CA  . ARG A 1 78  ? -20.456 20.198  -40.041 1.00 97.66  ? 78  ARG A CA  1 
ATOM   624  C  C   . ARG A 1 78  ? -20.935 20.538  -38.639 1.00 96.16  ? 78  ARG A C   1 
ATOM   625  O  O   . ARG A 1 78  ? -20.611 21.609  -38.111 1.00 88.69  ? 78  ARG A O   1 
ATOM   626  C  CB  . ARG A 1 78  ? -21.477 20.683  -41.081 1.00 90.06  ? 78  ARG A CB  1 
ATOM   627  N  N   . THR A 1 79  ? -21.692 19.634  -38.020 1.00 90.12  ? 79  THR A N   1 
ATOM   628  C  CA  . THR A 1 79  ? -22.161 19.812  -36.653 1.00 91.67  ? 79  THR A CA  1 
ATOM   629  C  C   . THR A 1 79  ? -21.104 19.386  -35.637 1.00 84.97  ? 79  THR A C   1 
ATOM   630  O  O   . THR A 1 79  ? -20.711 20.176  -34.773 1.00 84.88  ? 79  THR A O   1 
ATOM   631  C  CB  . THR A 1 79  ? -23.456 19.026  -36.445 1.00 89.28  ? 79  THR A CB  1 
ATOM   632  O  OG1 . THR A 1 79  ? -24.407 19.422  -37.433 1.00 90.81  ? 79  THR A OG1 1 
ATOM   633  C  CG2 . THR A 1 79  ? -24.022 19.303  -35.077 1.00 78.71  ? 79  THR A CG2 1 
ATOM   634  N  N   . ALA A 1 80  ? -20.622 18.146  -35.738 1.00 87.41  ? 80  ALA A N   1 
ATOM   635  C  CA  . ALA A 1 80  ? -19.719 17.621  -34.719 1.00 77.24  ? 80  ALA A CA  1 
ATOM   636  C  C   . ALA A 1 80  ? -18.378 18.343  -34.686 1.00 82.06  ? 80  ALA A C   1 
ATOM   637  O  O   . ALA A 1 80  ? -17.654 18.224  -33.693 1.00 83.80  ? 80  ALA A O   1 
ATOM   638  C  CB  . ALA A 1 80  ? -19.500 16.123  -34.929 1.00 82.87  ? 80  ALA A CB  1 
ATOM   639  N  N   . MET A 1 81  ? -18.032 19.101  -35.730 1.00 77.40  ? 81  MET A N   1 
ATOM   640  C  CA  . MET A 1 81  ? -16.735 19.778  -35.740 1.00 83.63  ? 81  MET A CA  1 
ATOM   641  C  C   . MET A 1 81  ? -16.711 21.004  -34.834 1.00 72.57  ? 81  MET A C   1 
ATOM   642  O  O   . MET A 1 81  ? -15.675 21.312  -34.236 1.00 71.65  ? 81  MET A O   1 
ATOM   643  C  CB  . MET A 1 81  ? -16.370 20.198  -37.160 1.00 85.20  ? 81  MET A CB  1 
ATOM   644  C  CG  . MET A 1 81  ? -17.267 21.305  -37.708 1.00 89.39  ? 81  MET A CG  1 
ATOM   645  S  SD  . MET A 1 81  ? -16.348 22.828  -37.981 1.00 94.64  ? 81  MET A SD  1 
ATOM   646  C  CE  . MET A 1 81  ? -15.661 22.481  -39.613 1.00 90.47  ? 81  MET A CE  1 
ATOM   647  N  N   . ARG A 1 82  ? -17.830 21.728  -34.747 1.00 72.01  ? 82  ARG A N   1 
ATOM   648  C  CA  . ARG A 1 82  ? -17.848 22.969  -33.986 1.00 72.01  ? 82  ARG A CA  1 
ATOM   649  C  C   . ARG A 1 82  ? -17.668 22.706  -32.500 1.00 66.40  ? 82  ARG A C   1 
ATOM   650  O  O   . ARG A 1 82  ? -17.175 23.565  -31.766 1.00 60.83  ? 82  ARG A O   1 
ATOM   651  C  CB  . ARG A 1 82  ? -19.159 23.711  -34.240 1.00 66.10  ? 82  ARG A CB  1 
ATOM   652  C  CG  . ARG A 1 82  ? -19.477 23.880  -35.714 1.00 84.10  ? 82  ARG A CG  1 
ATOM   653  C  CD  . ARG A 1 82  ? -20.729 24.735  -35.926 1.00 85.73  ? 82  ARG A CD  1 
ATOM   654  N  NE  . ARG A 1 82  ? -21.958 23.965  -36.044 1.00 84.75  ? 82  ARG A NE  1 
ATOM   655  C  CZ  . ARG A 1 82  ? -22.973 24.044  -35.202 1.00 82.93  ? 82  ARG A CZ  1 
ATOM   656  N  NH1 . ARG A 1 82  ? -22.930 24.827  -34.122 1.00 81.81  ? 82  ARG A NH1 1 
ATOM   657  N  NH2 . ARG A 1 82  ? -24.063 23.336  -35.462 1.00 85.23  ? 82  ARG A NH2 1 
ATOM   658  N  N   . TYR A 1 83  ? -18.045 21.520  -32.051 1.00 65.55  ? 83  TYR A N   1 
ATOM   659  C  CA  . TYR A 1 83  ? -18.053 21.207  -30.640 1.00 64.70  ? 83  TYR A CA  1 
ATOM   660  C  C   . TYR A 1 83  ? -16.880 20.330  -30.226 1.00 65.56  ? 83  TYR A C   1 
ATOM   661  O  O   . TYR A 1 83  ? -16.538 20.291  -29.042 1.00 65.59  ? 83  TYR A O   1 
ATOM   662  C  CB  . TYR A 1 83  ? -19.390 20.545  -30.298 1.00 61.84  ? 83  TYR A CB  1 
ATOM   663  C  CG  . TYR A 1 83  ? -20.567 21.490  -30.489 1.00 61.36  ? 83  TYR A CG  1 
ATOM   664  C  CD1 . TYR A 1 83  ? -20.797 22.515  -29.585 1.00 58.09  ? 83  TYR A CD1 1 
ATOM   665  C  CD2 . TYR A 1 83  ? -21.441 21.362  -31.570 1.00 68.05  ? 83  TYR A CD2 1 
ATOM   666  C  CE1 . TYR A 1 83  ? -21.859 23.385  -29.732 1.00 58.57  ? 83  TYR A CE1 1 
ATOM   667  C  CE2 . TYR A 1 83  ? -22.518 22.237  -31.734 1.00 63.48  ? 83  TYR A CE2 1 
ATOM   668  C  CZ  . TYR A 1 83  ? -22.724 23.244  -30.802 1.00 63.50  ? 83  TYR A CZ  1 
ATOM   669  O  OH  . TYR A 1 83  ? -23.775 24.135  -30.917 1.00 63.53  ? 83  TYR A OH  1 
ATOM   670  N  N   . ALA A 1 84  ? -16.261 19.636  -31.171 1.00 68.00  ? 84  ALA A N   1 
ATOM   671  C  CA  . ALA A 1 84  ? -15.000 18.968  -30.909 1.00 67.98  ? 84  ALA A CA  1 
ATOM   672  C  C   . ALA A 1 84  ? -13.937 20.001  -30.588 1.00 66.99  ? 84  ALA A C   1 
ATOM   673  O  O   . ALA A 1 84  ? -13.858 21.056  -31.230 1.00 73.86  ? 84  ALA A O   1 
ATOM   674  C  CB  . ALA A 1 84  ? -14.573 18.142  -32.124 1.00 80.06  ? 84  ALA A CB  1 
ATOM   675  N  N   . ASN A 1 85  ? -13.114 19.691  -29.590 1.00 68.97  ? 85  ASN A N   1 
ATOM   676  C  CA  . ASN A 1 85  ? -12.063 20.594  -29.132 1.00 67.97  ? 85  ASN A CA  1 
ATOM   677  C  C   . ASN A 1 85  ? -12.634 21.922  -28.627 1.00 63.00  ? 85  ASN A C   1 
ATOM   678  O  O   . ASN A 1 85  ? -11.998 22.973  -28.750 1.00 66.30  ? 85  ASN A O   1 
ATOM   679  C  CB  . ASN A 1 85  ? -11.013 20.838  -30.223 1.00 64.40  ? 85  ASN A CB  1 
ATOM   680  C  CG  . ASN A 1 85  ? -10.116 19.627  -30.454 1.00 72.80  ? 85  ASN A CG  1 
ATOM   681  O  OD1 . ASN A 1 85  ? -9.263  19.301  -29.634 1.00 79.73  ? 85  ASN A OD1 1 
ATOM   682  N  ND2 . ASN A 1 85  ? -10.298 18.970  -31.575 1.00 69.52  ? 85  ASN A ND2 1 
ATOM   683  N  N   . ASN A 1 86  ? -13.843 21.895  -28.076 1.00 61.27  ? 86  ASN A N   1 
ATOM   684  C  CA  . ASN A 1 86  ? -14.409 23.055  -27.378 1.00 59.00  ? 86  ASN A CA  1 
ATOM   685  C  C   . ASN A 1 86  ? -15.208 22.517  -26.215 1.00 50.82  ? 86  ASN A C   1 
ATOM   686  O  O   . ASN A 1 86  ? -16.430 22.356  -26.287 1.00 48.24  ? 86  ASN A O   1 
ATOM   687  C  CB  . ASN A 1 86  ? -15.281 23.900  -28.319 1.00 60.56  ? 86  ASN A CB  1 
ATOM   688  C  CG  . ASN A 1 86  ? -15.534 25.301  -27.792 1.00 60.19  ? 86  ASN A CG  1 
ATOM   689  O  OD1 . ASN A 1 86  ? -15.812 25.499  -26.603 1.00 57.34  ? 86  ASN A OD1 1 
ATOM   690  N  ND2 . ASN A 1 86  ? -15.452 26.278  -28.674 1.00 59.57  ? 86  ASN A ND2 1 
ATOM   691  N  N   . PRO A 1 87  ? -14.540 22.192  -25.101 1.00 54.27  ? 87  PRO A N   1 
ATOM   692  C  CA  . PRO A 1 87  ? -15.227 21.450  -24.035 1.00 51.34  ? 87  PRO A CA  1 
ATOM   693  C  C   . PRO A 1 87  ? -16.455 22.164  -23.508 1.00 44.84  ? 87  PRO A C   1 
ATOM   694  O  O   . PRO A 1 87  ? -17.484 21.506  -23.290 1.00 45.78  ? 87  PRO A O   1 
ATOM   695  C  CB  . PRO A 1 87  ? -14.141 21.293  -22.958 1.00 52.62  ? 87  PRO A CB  1 
ATOM   696  C  CG  . PRO A 1 87  ? -12.846 21.485  -23.677 1.00 53.66  ? 87  PRO A CG  1 
ATOM   697  C  CD  . PRO A 1 87  ? -13.146 22.497  -24.752 1.00 53.59  ? 87  PRO A CD  1 
ATOM   698  N  N   . GLN A 1 88  ? -16.404 23.498  -23.372 1.00 40.44  ? 88  GLN A N   1 
ATOM   699  C  CA  . GLN A 1 88  ? -17.528 24.242  -22.802 1.00 47.68  ? 88  GLN A CA  1 
ATOM   700  C  C   . GLN A 1 88  ? -18.718 24.254  -23.752 1.00 45.43  ? 88  GLN A C   1 
ATOM   701  O  O   . GLN A 1 88  ? -19.856 23.999  -23.341 1.00 43.03  ? 88  GLN A O   1 
ATOM   702  C  CB  . GLN A 1 88  ? -17.106 25.679  -22.455 1.00 49.02  ? 88  GLN A CB  1 
ATOM   703  C  CG  . GLN A 1 88  ? -18.238 26.543  -21.832 1.00 42.39  ? 88  GLN A CG  1 
ATOM   704  C  CD  . GLN A 1 88  ? -17.723 27.873  -21.228 1.00 50.72  ? 88  GLN A CD  1 
ATOM   705  O  OE1 . GLN A 1 88  ? -16.613 28.318  -21.521 1.00 58.05  ? 88  GLN A OE1 1 
ATOM   706  N  NE2 . GLN A 1 88  ? -18.542 28.503  -20.396 1.00 47.79  ? 88  GLN A NE2 1 
ATOM   707  N  N   . ALA A 1 89  ? -18.488 24.597  -25.017 1.00 49.56  ? 89  ALA A N   1 
ATOM   708  C  CA  . ALA A 1 89  ? -19.578 24.558  -25.982 1.00 50.16  ? 89  ALA A CA  1 
ATOM   709  C  C   . ALA A 1 89  ? -20.169 23.159  -26.059 1.00 46.18  ? 89  ALA A C   1 
ATOM   710  O  O   . ALA A 1 89  ? -21.389 22.997  -26.053 1.00 46.15  ? 89  ALA A O   1 
ATOM   711  C  CB  . ALA A 1 89  ? -19.086 25.009  -27.351 1.00 48.70  ? 89  ALA A CB  1 
ATOM   712  N  N   . LEU A 1 90  ? -19.307 22.138  -26.039 1.00 47.20  ? 90  LEU A N   1 
ATOM   713  C  CA  . LEU A 1 90  ? -19.760 20.754  -26.135 1.00 48.67  ? 90  LEU A CA  1 
ATOM   714  C  C   . LEU A 1 90  ? -20.730 20.406  -25.009 1.00 53.48  ? 90  LEU A C   1 
ATOM   715  O  O   . LEU A 1 90  ? -21.852 19.941  -25.270 1.00 50.50  ? 90  LEU A O   1 
ATOM   716  C  CB  . LEU A 1 90  ? -18.542 19.827  -26.123 1.00 44.68  ? 90  LEU A CB  1 
ATOM   717  C  CG  . LEU A 1 90  ? -18.804 18.326  -26.072 1.00 54.24  ? 90  LEU A CG  1 
ATOM   718  C  CD1 . LEU A 1 90  ? -19.824 17.939  -27.114 1.00 57.53  ? 90  LEU A CD1 1 
ATOM   719  C  CD2 . LEU A 1 90  ? -17.518 17.546  -26.303 1.00 57.95  ? 90  LEU A CD2 1 
ATOM   720  N  N   . ALA A 1 91  ? -20.322 20.655  -23.749 1.00 42.46  ? 91  ALA A N   1 
ATOM   721  C  CA  . ALA A 1 91  ? -21.157 20.342  -22.589 1.00 48.69  ? 91  ALA A CA  1 
ATOM   722  C  C   . ALA A 1 91  ? -22.455 21.132  -22.616 1.00 50.39  ? 91  ALA A C   1 
ATOM   723  O  O   . ALA A 1 91  ? -23.531 20.584  -22.343 1.00 49.74  ? 91  ALA A O   1 
ATOM   724  C  CB  . ALA A 1 91  ? -20.398 20.614  -21.277 1.00 44.07  ? 91  ALA A CB  1 
ATOM   725  N  N   . ASN A 1 92  ? -22.378 22.420  -22.960 1.00 45.82  ? 92  ASN A N   1 
ATOM   726  C  CA  . ASN A 1 92  ? -23.582 23.236  -22.989 1.00 47.80  ? 92  ASN A CA  1 
ATOM   727  C  C   . ASN A 1 92  ? -24.558 22.753  -24.045 1.00 51.96  ? 92  ASN A C   1 
ATOM   728  O  O   . ASN A 1 92  ? -25.772 22.932  -23.895 1.00 51.56  ? 92  ASN A O   1 
ATOM   729  C  CB  . ASN A 1 92  ? -23.220 24.699  -23.235 1.00 44.19  ? 92  ASN A CB  1 
ATOM   730  C  CG  . ASN A 1 92  ? -22.641 25.356  -22.002 1.00 47.10  ? 92  ASN A CG  1 
ATOM   731  O  OD1 . ASN A 1 92  ? -22.981 24.986  -20.880 1.00 40.47  ? 92  ASN A OD1 1 
ATOM   732  N  ND2 . ASN A 1 92  ? -21.778 26.339  -22.201 1.00 45.99  ? 92  ASN A ND2 1 
ATOM   733  N  N   . TYR A 1 93  ? -24.059 22.144  -25.115 1.00 46.66  ? 93  TYR A N   1 
ATOM   734  C  CA  . TYR A 1 93  ? -24.993 21.707  -26.132 1.00 53.06  ? 93  TYR A CA  1 
ATOM   735  C  C   . TYR A 1 93  ? -25.535 20.314  -25.838 1.00 55.05  ? 93  TYR A C   1 
ATOM   736  O  O   . TYR A 1 93  ? -26.749 20.123  -25.804 1.00 55.07  ? 93  TYR A O   1 
ATOM   737  C  CB  . TYR A 1 93  ? -24.326 21.762  -27.505 1.00 48.54  ? 93  TYR A CB  1 
ATOM   738  C  CG  . TYR A 1 93  ? -25.130 21.083  -28.583 1.00 55.43  ? 93  TYR A CG  1 
ATOM   739  C  CD1 . TYR A 1 93  ? -26.398 21.535  -28.916 1.00 54.79  ? 93  TYR A CD1 1 
ATOM   740  C  CD2 . TYR A 1 93  ? -24.622 19.987  -29.268 1.00 59.14  ? 93  TYR A CD2 1 
ATOM   741  C  CE1 . TYR A 1 93  ? -27.138 20.919  -29.904 1.00 58.93  ? 93  TYR A CE1 1 
ATOM   742  C  CE2 . TYR A 1 93  ? -25.350 19.359  -30.258 1.00 57.99  ? 93  TYR A CE2 1 
ATOM   743  C  CZ  . TYR A 1 93  ? -26.608 19.825  -30.565 1.00 60.95  ? 93  TYR A CZ  1 
ATOM   744  O  OH  . TYR A 1 93  ? -27.331 19.200  -31.541 1.00 67.22  ? 93  TYR A OH  1 
ATOM   745  N  N   . VAL A 1 94  ? -24.661 19.347  -25.560 1.00 57.10  ? 94  VAL A N   1 
ATOM   746  C  CA  . VAL A 1 94  ? -25.142 17.974  -25.448 1.00 53.59  ? 94  VAL A CA  1 
ATOM   747  C  C   . VAL A 1 94  ? -25.944 17.758  -24.174 1.00 57.09  ? 94  VAL A C   1 
ATOM   748  O  O   . VAL A 1 94  ? -26.838 16.906  -24.136 1.00 57.07  ? 94  VAL A O   1 
ATOM   749  C  CB  . VAL A 1 94  ? -23.968 16.987  -25.560 1.00 55.36  ? 94  VAL A CB  1 
ATOM   750  C  CG1 . VAL A 1 94  ? -23.214 17.285  -26.797 1.00 58.41  ? 94  VAL A CG1 1 
ATOM   751  C  CG2 . VAL A 1 94  ? -23.048 17.079  -24.376 1.00 54.93  ? 94  VAL A CG2 1 
ATOM   752  N  N   . TYR A 1 95  ? -25.668 18.518  -23.121 1.00 48.46  ? 95  TYR A N   1 
ATOM   753  C  CA  . TYR A 1 95  ? -26.436 18.386  -21.897 1.00 47.57  ? 95  TYR A CA  1 
ATOM   754  C  C   . TYR A 1 95  ? -27.584 19.381  -21.809 1.00 52.31  ? 95  TYR A C   1 
ATOM   755  O  O   . TYR A 1 95  ? -28.241 19.462  -20.763 1.00 45.00  ? 95  TYR A O   1 
ATOM   756  C  CB  . TYR A 1 95  ? -25.507 18.510  -20.697 1.00 46.73  ? 95  TYR A CB  1 
ATOM   757  C  CG  . TYR A 1 95  ? -24.526 17.349  -20.666 1.00 53.43  ? 95  TYR A CG  1 
ATOM   758  C  CD1 . TYR A 1 95  ? -24.937 16.071  -21.015 1.00 54.68  ? 95  TYR A CD1 1 
ATOM   759  C  CD2 . TYR A 1 95  ? -23.198 17.535  -20.341 1.00 50.94  ? 95  TYR A CD2 1 
ATOM   760  C  CE1 . TYR A 1 95  ? -24.068 15.010  -21.011 1.00 54.80  ? 95  TYR A CE1 1 
ATOM   761  C  CE2 . TYR A 1 95  ? -22.307 16.467  -20.330 1.00 54.11  ? 95  TYR A CE2 1 
ATOM   762  C  CZ  . TYR A 1 95  ? -22.752 15.209  -20.664 1.00 52.32  ? 95  TYR A CZ  1 
ATOM   763  O  OH  . TYR A 1 95  ? -21.889 14.141  -20.652 1.00 50.77  ? 95  TYR A OH  1 
ATOM   764  N  N   . ALA A 1 96  ? -27.860 20.120  -22.882 1.00 51.51  ? 96  ALA A N   1 
ATOM   765  C  CA  . ALA A 1 96  ? -28.908 21.124  -22.803 1.00 50.57  ? 96  ALA A CA  1 
ATOM   766  C  C   . ALA A 1 96  ? -30.251 20.443  -22.597 1.00 50.67  ? 96  ALA A C   1 
ATOM   767  O  O   . ALA A 1 96  ? -30.496 19.354  -23.121 1.00 51.58  ? 96  ALA A O   1 
ATOM   768  C  CB  . ALA A 1 96  ? -28.931 21.988  -24.057 1.00 57.12  ? 96  ALA A CB  1 
ATOM   769  N  N   . ASN A 1 97  ? -31.089 21.054  -21.764 1.00 51.12  ? 97  ASN A N   1 
ATOM   770  C  CA  . ASN A 1 97  ? -32.467 20.628  -21.567 1.00 53.30  ? 97  ASN A CA  1 
ATOM   771  C  C   . ASN A 1 97  ? -32.580 19.158  -21.162 1.00 54.19  ? 97  ASN A C   1 
ATOM   772  O  O   . ASN A 1 97  ? -33.616 18.531  -21.396 1.00 55.71  ? 97  ASN A O   1 
ATOM   773  C  CB  . ASN A 1 97  ? -33.283 20.913  -22.831 1.00 53.83  ? 97  ASN A CB  1 
ATOM   774  C  CG  . ASN A 1 97  ? -32.969 22.278  -23.411 1.00 51.10  ? 97  ASN A CG  1 
ATOM   775  O  OD1 . ASN A 1 97  ? -33.264 23.292  -22.793 1.00 52.62  ? 97  ASN A OD1 1 
ATOM   776  N  ND2 . ASN A 1 97  ? -32.366 22.310  -24.600 1.00 52.49  ? 97  ASN A ND2 1 
ATOM   777  N  N   . ARG A 1 98  ? -31.521 18.599  -20.580 1.00 49.31  ? 98  ARG A N   1 
ATOM   778  C  CA  . ARG A 1 98  ? -31.495 17.234  -20.084 1.00 55.21  ? 98  ARG A CA  1 
ATOM   779  C  C   . ARG A 1 98  ? -31.130 17.261  -18.612 1.00 51.54  ? 98  ARG A C   1 
ATOM   780  O  O   . ARG A 1 98  ? -30.547 18.227  -18.119 1.00 48.21  ? 98  ARG A O   1 
ATOM   781  C  CB  . ARG A 1 98  ? -30.481 16.354  -20.844 1.00 57.24  ? 98  ARG A CB  1 
ATOM   782  C  CG  . ARG A 1 98  ? -30.889 16.039  -22.279 1.00 64.67  ? 98  ARG A CG  1 
ATOM   783  C  CD  . ARG A 1 98  ? -30.149 14.832  -22.851 1.00 67.71  ? 98  ARG A CD  1 
ATOM   784  N  NE  . ARG A 1 98  ? -30.889 14.260  -23.976 1.00 88.68  ? 98  ARG A NE  1 
ATOM   785  C  CZ  . ARG A 1 98  ? -31.848 13.345  -23.864 1.00 87.37  ? 98  ARG A CZ  1 
ATOM   786  N  NH1 . ARG A 1 98  ? -32.192 12.843  -22.686 1.00 84.00  ? 98  ARG A NH1 1 
ATOM   787  N  NH2 . ARG A 1 98  ? -32.485 12.929  -24.958 1.00 84.27  ? 98  ARG A NH2 1 
ATOM   788  N  N   . ILE A 1 99  ? -31.459 16.165  -17.927 1.00 54.97  ? 99  ILE A N   1 
ATOM   789  C  CA  . ILE A 1 99  ? -31.185 15.948  -16.504 1.00 52.59  ? 99  ILE A CA  1 
ATOM   790  C  C   . ILE A 1 99  ? -31.285 17.238  -15.701 1.00 50.15  ? 99  ILE A C   1 
ATOM   791  O  O   . ILE A 1 99  ? -30.366 17.591  -14.956 1.00 46.87  ? 99  ILE A O   1 
ATOM   792  C  CB  . ILE A 1 99  ? -29.809 15.279  -16.293 1.00 52.77  ? 99  ILE A CB  1 
ATOM   793  C  CG1 . ILE A 1 99  ? -28.764 15.813  -17.274 1.00 44.99  ? 99  ILE A CG1 1 
ATOM   794  C  CG2 . ILE A 1 99  ? -29.952 13.762  -16.388 1.00 59.98  ? 99  ILE A CG2 1 
ATOM   795  C  CD1 . ILE A 1 99  ? -27.413 15.182  -17.162 1.00 48.61  ? 99  ILE A CD1 1 
ATOM   796  N  N   . GLY A 1 100 ? -32.381 17.969  -15.875 1.00 52.19  ? 100 GLY A N   1 
ATOM   797  C  CA  . GLY A 1 100 ? -32.619 19.181  -15.124 1.00 46.84  ? 100 GLY A CA  1 
ATOM   798  C  C   . GLY A 1 100 ? -31.994 20.431  -15.689 1.00 46.71  ? 100 GLY A C   1 
ATOM   799  O  O   . GLY A 1 100 ? -32.352 21.539  -15.245 1.00 50.82  ? 100 GLY A O   1 
ATOM   800  N  N   . ASN A 1 101 ? -31.083 20.314  -16.655 1.00 47.03  ? 101 ASN A N   1 
ATOM   801  C  CA  . ASN A 1 101 ? -30.361 21.492  -17.129 1.00 44.29  ? 101 ASN A CA  1 
ATOM   802  C  C   . ASN A 1 101 ? -31.271 22.431  -17.913 1.00 46.33  ? 101 ASN A C   1 
ATOM   803  O  O   . ASN A 1 101 ? -32.250 22.014  -18.521 1.00 43.95  ? 101 ASN A O   1 
ATOM   804  C  CB  . ASN A 1 101 ? -29.195 21.087  -18.016 1.00 44.16  ? 101 ASN A CB  1 
ATOM   805  C  CG  . ASN A 1 101 ? -28.092 20.451  -17.250 1.00 47.90  ? 101 ASN A CG  1 
ATOM   806  O  OD1 . ASN A 1 101 ? -27.968 20.644  -16.022 1.00 45.42  ? 101 ASN A OD1 1 
ATOM   807  N  ND2 . ASN A 1 101 ? -27.255 19.687  -17.956 1.00 42.26  ? 101 ASN A ND2 1 
ATOM   808  N  N   . GLY A 1 102 ? -30.940 23.719  -17.882 1.00 46.07  ? 102 GLY A N   1 
ATOM   809  C  CA  . GLY A 1 102 ? -31.505 24.674  -18.812 1.00 51.69  ? 102 GLY A CA  1 
ATOM   810  C  C   . GLY A 1 102 ? -31.005 24.453  -20.232 1.00 49.64  ? 102 GLY A C   1 
ATOM   811  O  O   . GLY A 1 102 ? -30.368 23.447  -20.553 1.00 46.41  ? 102 GLY A O   1 
ATOM   812  N  N   . ASN A 1 103 ? -31.286 25.430  -21.101 1.00 46.65  ? 103 ASN A N   1 
ATOM   813  C  CA  . ASN A 1 103 ? -30.918 25.288  -22.503 1.00 48.32  ? 103 ASN A CA  1 
ATOM   814  C  C   . ASN A 1 103 ? -29.428 25.573  -22.701 1.00 49.11  ? 103 ASN A C   1 
ATOM   815  O  O   . ASN A 1 103 ? -28.653 25.753  -21.749 1.00 48.17  ? 103 ASN A O   1 
ATOM   816  C  CB  . ASN A 1 103 ? -31.813 26.164  -23.394 1.00 52.97  ? 103 ASN A CB  1 
ATOM   817  C  CG  . ASN A 1 103 ? -31.649 27.657  -23.142 1.00 55.05  ? 103 ASN A CG  1 
ATOM   818  O  OD1 . ASN A 1 103 ? -30.709 28.090  -22.488 1.00 57.37  ? 103 ASN A OD1 1 
ATOM   819  N  ND2 . ASN A 1 103 ? -32.571 28.452  -23.678 1.00 51.50  ? 103 ASN A ND2 1 
ATOM   820  N  N   . GLU A 1 104 ? -29.012 25.570  -23.966 1.00 50.79  ? 104 GLU A N   1 
ATOM   821  C  CA  . GLU A 1 104 ? -27.602 25.778  -24.279 1.00 49.50  ? 104 GLU A CA  1 
ATOM   822  C  C   . GLU A 1 104 ? -27.146 27.126  -23.759 1.00 44.72  ? 104 GLU A C   1 
ATOM   823  O  O   . GLU A 1 104 ? -26.053 27.243  -23.205 1.00 45.29  ? 104 GLU A O   1 
ATOM   824  C  CB  . GLU A 1 104 ? -27.353 25.671  -25.792 1.00 45.21  ? 104 GLU A CB  1 
ATOM   825  C  CG  . GLU A 1 104 ? -25.866 25.785  -26.186 1.00 43.12  ? 104 GLU A CG  1 
ATOM   826  C  CD  . GLU A 1 104 ? -25.636 25.617  -27.709 1.00 54.14  ? 104 GLU A CD  1 
ATOM   827  O  OE1 . GLU A 1 104 ? -26.555 25.929  -28.484 1.00 49.12  ? 104 GLU A OE1 1 
ATOM   828  O  OE2 . GLU A 1 104 ? -24.530 25.166  -28.145 1.00 55.17  ? 104 GLU A OE2 1 
ATOM   829  N  N   . ALA A 1 105 ? -27.999 28.141  -23.877 1.00 43.19  ? 105 ALA A N   1 
ATOM   830  C  CA  . ALA A 1 105 ? -27.606 29.485  -23.477 1.00 51.43  ? 105 ALA A CA  1 
ATOM   831  C  C   . ALA A 1 105 ? -27.398 29.570  -21.983 1.00 49.49  ? 105 ALA A C   1 
ATOM   832  O  O   . ALA A 1 105 ? -26.572 30.363  -21.518 1.00 45.68  ? 105 ALA A O   1 
ATOM   833  C  CB  . ALA A 1 105 ? -28.666 30.492  -23.910 1.00 44.38  ? 105 ALA A CB  1 
ATOM   834  N  N   . SER A 1 106 ? -28.113 28.733  -21.219 1.00 47.97  ? 106 SER A N   1 
ATOM   835  C  CA  . SER A 1 106 ? -28.069 28.818  -19.761 1.00 46.04  ? 106 SER A CA  1 
ATOM   836  C  C   . SER A 1 106 ? -26.691 28.469  -19.213 1.00 41.59  ? 106 SER A C   1 
ATOM   837  O  O   . SER A 1 106 ? -26.325 28.917  -18.122 1.00 46.30  ? 106 SER A O   1 
ATOM   838  C  CB  . SER A 1 106 ? -29.127 27.893  -19.136 1.00 46.13  ? 106 SER A CB  1 
ATOM   839  O  OG  . SER A 1 106 ? -28.675 26.530  -19.140 1.00 44.69  ? 106 SER A OG  1 
ATOM   840  N  N   . GLY A 1 107 ? -25.912 27.682  -19.937 1.00 41.26  ? 107 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 107 ? -24.629 27.271  -19.410 1.00 39.37  ? 107 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 107 ? -24.706 26.106  -18.449 1.00 48.28  ? 107 GLY A C   1 
ATOM   843  O  O   . GLY A 1 107 ? -23.662 25.676  -17.946 1.00 44.22  ? 107 GLY A O   1 
ATOM   844  N  N   . ASP A 1 108 ? -25.907 25.562  -18.202 1.00 41.25  ? 108 ASP A N   1 
ATOM   845  C  CA  . ASP A 1 108 ? -26.048 24.472  -17.239 1.00 46.81  ? 108 ASP A CA  1 
ATOM   846  C  C   . ASP A 1 108 ? -25.251 23.234  -17.624 1.00 44.56  ? 108 ASP A C   1 
ATOM   847  O  O   . ASP A 1 108 ? -24.750 22.531  -16.739 1.00 42.70  ? 108 ASP A O   1 
ATOM   848  C  CB  . ASP A 1 108 ? -27.519 24.093  -17.067 1.00 42.11  ? 108 ASP A CB  1 
ATOM   849  C  CG  . ASP A 1 108 ? -28.226 24.992  -16.081 1.00 42.47  ? 108 ASP A CG  1 
ATOM   850  O  OD1 . ASP A 1 108 ? -27.563 25.894  -15.521 1.00 46.19  ? 108 ASP A OD1 1 
ATOM   851  O  OD2 . ASP A 1 108 ? -29.438 24.792  -15.874 1.00 44.20  ? 108 ASP A OD2 1 
ATOM   852  N  N   . GLY A 1 109 ? -25.149 22.926  -18.922 1.00 42.43  ? 109 GLY A N   1 
ATOM   853  C  CA  . GLY A 1 109 ? -24.479 21.694  -19.324 1.00 43.78  ? 109 GLY A CA  1 
ATOM   854  C  C   . GLY A 1 109 ? -23.044 21.633  -18.838 1.00 43.33  ? 109 GLY A C   1 
ATOM   855  O  O   . GLY A 1 109 ? -22.602 20.627  -18.280 1.00 38.13  ? 109 GLY A O   1 
ATOM   856  N  N   . TRP A 1 110 ? -22.310 22.731  -19.017 1.00 43.97  ? 110 TRP A N   1 
ATOM   857  C  CA  . TRP A 1 110 ? -20.930 22.840  -18.548 1.00 42.06  ? 110 TRP A CA  1 
ATOM   858  C  C   . TRP A 1 110 ? -20.874 23.020  -17.032 1.00 44.45  ? 110 TRP A C   1 
ATOM   859  O  O   . TRP A 1 110 ? -20.075 22.370  -16.336 1.00 45.15  ? 110 TRP A O   1 
ATOM   860  C  CB  . TRP A 1 110 ? -20.295 24.024  -19.285 1.00 40.56  ? 110 TRP A CB  1 
ATOM   861  C  CG  . TRP A 1 110 ? -18.936 24.420  -18.828 1.00 39.71  ? 110 TRP A CG  1 
ATOM   862  C  CD1 . TRP A 1 110 ? -18.586 25.568  -18.163 1.00 47.80  ? 110 TRP A CD1 1 
ATOM   863  C  CD2 . TRP A 1 110 ? -17.734 23.674  -19.007 1.00 40.34  ? 110 TRP A CD2 1 
ATOM   864  N  NE1 . TRP A 1 110 ? -17.240 25.570  -17.922 1.00 48.50  ? 110 TRP A NE1 1 
ATOM   865  C  CE2 . TRP A 1 110 ? -16.692 24.421  -18.434 1.00 44.81  ? 110 TRP A CE2 1 
ATOM   866  C  CE3 . TRP A 1 110 ? -17.438 22.444  -19.602 1.00 44.36  ? 110 TRP A CE3 1 
ATOM   867  C  CZ2 . TRP A 1 110 ? -15.377 23.976  -18.428 1.00 43.80  ? 110 TRP A CZ2 1 
ATOM   868  C  CZ3 . TRP A 1 110 ? -16.121 22.002  -19.600 1.00 41.25  ? 110 TRP A CZ3 1 
ATOM   869  C  CH2 . TRP A 1 110 ? -15.114 22.765  -19.008 1.00 40.41  ? 110 TRP A CH2 1 
ATOM   870  N  N   . ARG A 1 111 ? -21.731 23.896  -16.501 1.00 41.40  ? 111 ARG A N   1 
ATOM   871  C  CA  . ARG A 1 111 ? -21.770 24.156  -15.060 1.00 44.36  ? 111 ARG A CA  1 
ATOM   872  C  C   . ARG A 1 111 ? -21.930 22.863  -14.263 1.00 43.17  ? 111 ARG A C   1 
ATOM   873  O  O   . ARG A 1 111 ? -21.266 22.658  -13.230 1.00 43.54  ? 111 ARG A O   1 
ATOM   874  C  CB  . ARG A 1 111 ? -22.918 25.136  -14.757 1.00 41.22  ? 111 ARG A CB  1 
ATOM   875  C  CG  . ARG A 1 111 ? -23.195 25.412  -13.258 1.00 48.54  ? 111 ARG A CG  1 
ATOM   876  C  CD  . ARG A 1 111 ? -24.316 26.482  -13.079 1.00 48.85  ? 111 ARG A CD  1 
ATOM   877  N  NE  . ARG A 1 111 ? -23.913 27.776  -13.627 1.00 55.07  ? 111 ARG A NE  1 
ATOM   878  C  CZ  . ARG A 1 111 ? -24.428 28.364  -14.710 1.00 60.06  ? 111 ARG A CZ  1 
ATOM   879  N  NH1 . ARG A 1 111 ? -25.509 27.890  -15.326 1.00 52.35  ? 111 ARG A NH1 1 
ATOM   880  N  NH2 . ARG A 1 111 ? -23.851 29.469  -15.183 1.00 58.13  ? 111 ARG A NH2 1 
ATOM   881  N  N   . PHE A 1 112 ? -22.776 21.961  -14.742 1.00 41.49  ? 112 PHE A N   1 
ATOM   882  C  CA  . PHE A 1 112 ? -23.092 20.737  -14.020 1.00 40.52  ? 112 PHE A CA  1 
ATOM   883  C  C   . PHE A 1 112 ? -22.572 19.505  -14.744 1.00 37.55  ? 112 PHE A C   1 
ATOM   884  O  O   . PHE A 1 112 ? -23.222 18.461  -14.761 1.00 43.40  ? 112 PHE A O   1 
ATOM   885  C  CB  . PHE A 1 112 ? -24.597 20.637  -13.791 1.00 42.57  ? 112 PHE A CB  1 
ATOM   886  C  CG  . PHE A 1 112 ? -25.128 21.715  -12.903 1.00 39.46  ? 112 PHE A CG  1 
ATOM   887  C  CD1 . PHE A 1 112 ? -24.738 21.775  -11.561 1.00 44.40  ? 112 PHE A CD1 1 
ATOM   888  C  CD2 . PHE A 1 112 ? -26.002 22.671  -13.394 1.00 38.83  ? 112 PHE A CD2 1 
ATOM   889  C  CE1 . PHE A 1 112 ? -25.231 22.768  -10.729 1.00 46.77  ? 112 PHE A CE1 1 
ATOM   890  C  CE2 . PHE A 1 112 ? -26.505 23.678  -12.577 1.00 47.79  ? 112 PHE A CE2 1 
ATOM   891  C  CZ  . PHE A 1 112 ? -26.120 23.732  -11.236 1.00 47.13  ? 112 PHE A CZ  1 
ATOM   892  N  N   . ARG A 1 113 ? -21.418 19.640  -15.403 1.00 41.91  ? 113 ARG A N   1 
ATOM   893  C  CA  . ARG A 1 113 ? -20.757 18.500  -16.025 1.00 41.50  ? 113 ARG A CA  1 
ATOM   894  C  C   . ARG A 1 113 ? -20.322 17.515  -14.944 1.00 43.02  ? 113 ARG A C   1 
ATOM   895  O  O   . ARG A 1 113 ? -20.303 17.840  -13.750 1.00 39.48  ? 113 ARG A O   1 
ATOM   896  C  CB  . ARG A 1 113 ? -19.554 18.957  -16.853 1.00 42.13  ? 113 ARG A CB  1 
ATOM   897  C  CG  . ARG A 1 113 ? -18.412 19.630  -16.049 1.00 39.22  ? 113 ARG A CG  1 
ATOM   898  C  CD  . ARG A 1 113 ? -17.381 20.166  -17.028 1.00 41.22  ? 113 ARG A CD  1 
ATOM   899  N  NE  . ARG A 1 113 ? -16.223 20.792  -16.399 1.00 36.21  ? 113 ARG A NE  1 
ATOM   900  C  CZ  . ARG A 1 113 ? -16.251 21.978  -15.811 1.00 46.68  ? 113 ARG A CZ  1 
ATOM   901  N  NH1 . ARG A 1 113 ? -17.378 22.674  -15.710 1.00 43.69  ? 113 ARG A NH1 1 
ATOM   902  N  NH2 . ARG A 1 113 ? -15.129 22.473  -15.295 1.00 48.09  ? 113 ARG A NH2 1 
ATOM   903  N  N   . GLY A 1 114 ? -20.004 16.288  -15.365 1.00 43.69  ? 114 GLY A N   1 
ATOM   904  C  CA  . GLY A 1 114 ? -19.608 15.238  -14.442 1.00 49.77  ? 114 GLY A CA  1 
ATOM   905  C  C   . GLY A 1 114 ? -18.481 15.628  -13.504 1.00 46.30  ? 114 GLY A C   1 
ATOM   906  O  O   . GLY A 1 114 ? -17.465 16.159  -13.955 1.00 43.39  ? 114 GLY A O   1 
ATOM   907  N  N   . ARG A 1 115 ? -18.650 15.386  -12.201 1.00 47.09  ? 115 ARG A N   1 
ATOM   908  C  CA  . ARG A 1 115 ? -17.632 15.688  -11.196 1.00 46.43  ? 115 ARG A CA  1 
ATOM   909  C  C   . ARG A 1 115 ? -17.642 14.642  -10.090 1.00 51.06  ? 115 ARG A C   1 
ATOM   910  O  O   . ARG A 1 115 ? -18.706 14.190  -9.644  1.00 44.08  ? 115 ARG A O   1 
ATOM   911  C  CB  . ARG A 1 115 ? -17.838 17.072  -10.556 1.00 48.04  ? 115 ARG A CB  1 
ATOM   912  C  CG  . ARG A 1 115 ? -17.300 18.283  -11.319 1.00 44.55  ? 115 ARG A CG  1 
ATOM   913  C  CD  . ARG A 1 115 ? -17.533 19.531  -10.460 1.00 53.53  ? 115 ARG A CD  1 
ATOM   914  N  NE  . ARG A 1 115 ? -17.363 20.795  -11.179 1.00 54.16  ? 115 ARG A NE  1 
ATOM   915  C  CZ  . ARG A 1 115 ? -18.262 21.334  -11.999 1.00 55.35  ? 115 ARG A CZ  1 
ATOM   916  N  NH1 . ARG A 1 115 ? -19.418 20.728  -12.275 1.00 41.34  ? 115 ARG A NH1 1 
ATOM   917  N  NH2 . ARG A 1 115 ? -17.989 22.505  -12.574 1.00 54.88  ? 115 ARG A NH2 1 
ATOM   918  N  N   . GLY A 1 116 ? -16.448 14.304  -9.606  1.00 56.87  ? 116 GLY A N   1 
ATOM   919  C  CA  . GLY A 1 116 ? -16.283 13.259  -8.623  1.00 44.63  ? 116 GLY A CA  1 
ATOM   920  C  C   . GLY A 1 116 ? -15.639 12.038  -9.254  1.00 55.35  ? 116 GLY A C   1 
ATOM   921  O  O   . GLY A 1 116 ? -15.697 11.849  -10.471 1.00 48.63  ? 116 GLY A O   1 
ATOM   922  N  N   . PRO A 1 117 ? -15.004 11.186  -8.441  1.00 52.13  ? 117 PRO A N   1 
ATOM   923  C  CA  . PRO A 1 117 ? -14.390 9.971   -9.009  1.00 49.33  ? 117 PRO A CA  1 
ATOM   924  C  C   . PRO A 1 117 ? -15.394 9.067   -9.704  1.00 56.62  ? 117 PRO A C   1 
ATOM   925  O  O   . PRO A 1 117 ? -15.098 8.551   -10.787 1.00 60.00  ? 117 PRO A O   1 
ATOM   926  C  CB  . PRO A 1 117 ? -13.751 9.297   -7.789  1.00 54.71  ? 117 PRO A CB  1 
ATOM   927  C  CG  . PRO A 1 117 ? -14.564 9.839   -6.597  1.00 54.07  ? 117 PRO A CG  1 
ATOM   928  C  CD  . PRO A 1 117 ? -14.872 11.258  -6.979  1.00 50.27  ? 117 PRO A CD  1 
ATOM   929  N  N   . ILE A 1 118 ? -16.568 8.849   -9.119  1.00 52.32  ? 118 ILE A N   1 
ATOM   930  C  CA  . ILE A 1 118 ? -17.756 8.422   -9.863  1.00 54.44  ? 118 ILE A CA  1 
ATOM   931  C  C   . ILE A 1 118 ? -18.652 9.651   -10.004 1.00 56.32  ? 118 ILE A C   1 
ATOM   932  O  O   . ILE A 1 118 ? -19.043 10.249  -8.991  1.00 53.84  ? 118 ILE A O   1 
ATOM   933  C  CB  . ILE A 1 118 ? -18.489 7.274   -9.149  1.00 52.21  ? 118 ILE A CB  1 
ATOM   934  C  CG1 . ILE A 1 118 ? -17.626 6.015   -9.120  1.00 56.77  ? 118 ILE A CG1 1 
ATOM   935  C  CG2 . ILE A 1 118 ? -19.824 6.981   -9.820  1.00 48.87  ? 118 ILE A CG2 1 
ATOM   936  C  CD1 . ILE A 1 118 ? -18.211 4.910   -8.263  1.00 60.82  ? 118 ILE A CD1 1 
ATOM   937  N  N   . GLN A 1 119 ? -18.998 10.021  -11.246 1.00 45.04  ? 119 GLN A N   1 
ATOM   938  C  CA  . GLN A 1 119 ? -19.427 11.388  -11.540 1.00 53.83  ? 119 GLN A CA  1 
ATOM   939  C  C   . GLN A 1 119 ? -20.913 11.619  -11.278 1.00 47.44  ? 119 GLN A C   1 
ATOM   940  O  O   . GLN A 1 119 ? -21.754 10.748  -11.515 1.00 46.41  ? 119 GLN A O   1 
ATOM   941  C  CB  . GLN A 1 119 ? -19.086 11.761  -12.984 1.00 49.52  ? 119 GLN A CB  1 
ATOM   942  C  CG  . GLN A 1 119 ? -17.586 11.749  -13.243 1.00 51.55  ? 119 GLN A CG  1 
ATOM   943  C  CD  . GLN A 1 119 ? -17.265 12.004  -14.689 1.00 55.17  ? 119 GLN A CD  1 
ATOM   944  O  OE1 . GLN A 1 119 ? -18.105 12.503  -15.446 1.00 55.96  ? 119 GLN A OE1 1 
ATOM   945  N  NE2 . GLN A 1 119 ? -16.052 11.663  -15.093 1.00 47.04  ? 119 GLN A NE2 1 
ATOM   946  N  N   . THR A 1 120 ? -21.215 12.792  -10.735 1.00 46.47  ? 120 THR A N   1 
ATOM   947  C  CA  . THR A 1 120 ? -22.572 13.316  -10.677 1.00 52.51  ? 120 THR A CA  1 
ATOM   948  C  C   . THR A 1 120 ? -22.698 14.334  -11.791 1.00 47.53  ? 120 THR A C   1 
ATOM   949  O  O   . THR A 1 120 ? -21.777 15.131  -12.008 1.00 47.01  ? 120 THR A O   1 
ATOM   950  C  CB  . THR A 1 120 ? -22.886 13.975  -9.326  1.00 46.95  ? 120 THR A CB  1 
ATOM   951  O  OG1 . THR A 1 120 ? -22.663 13.029  -8.278  1.00 52.48  ? 120 THR A OG1 1 
ATOM   952  C  CG2 . THR A 1 120 ? -24.359 14.417  -9.259  1.00 50.90  ? 120 THR A CG2 1 
ATOM   953  N  N   . THR A 1 121 ? -23.828 14.291  -12.511 1.00 44.32  ? 121 THR A N   1 
ATOM   954  C  CA  . THR A 1 121 ? -23.977 15.092  -13.719 1.00 48.76  ? 121 THR A CA  1 
ATOM   955  C  C   . THR A 1 121 ? -25.375 15.673  -13.834 1.00 45.38  ? 121 THR A C   1 
ATOM   956  O  O   . THR A 1 121 ? -26.359 14.946  -13.676 1.00 46.70  ? 121 THR A O   1 
ATOM   957  C  CB  . THR A 1 121 ? -23.667 14.237  -14.943 1.00 47.44  ? 121 THR A CB  1 
ATOM   958  O  OG1 . THR A 1 121 ? -22.450 13.503  -14.690 1.00 50.24  ? 121 THR A OG1 1 
ATOM   959  C  CG2 . THR A 1 121 ? -23.527 15.135  -16.189 1.00 40.30  ? 121 THR A CG2 1 
ATOM   960  N  N   . GLY A 1 122 ? -25.458 16.964  -14.124 1.00 45.81  ? 122 GLY A N   1 
ATOM   961  C  CA  . GLY A 1 122 ? -26.731 17.599  -14.449 1.00 42.67  ? 122 GLY A CA  1 
ATOM   962  C  C   . GLY A 1 122 ? -27.376 18.272  -13.257 1.00 44.14  ? 122 GLY A C   1 
ATOM   963  O  O   . GLY A 1 122 ? -27.286 17.804  -12.121 1.00 42.52  ? 122 GLY A O   1 
ATOM   964  N  N   . ARG A 1 123 ? -28.050 19.399  -13.532 1.00 40.90  ? 123 ARG A N   1 
ATOM   965  C  CA  . ARG A 1 123 ? -28.609 20.224  -12.462 1.00 41.25  ? 123 ARG A CA  1 
ATOM   966  C  C   . ARG A 1 123 ? -29.480 19.414  -11.510 1.00 45.24  ? 123 ARG A C   1 
ATOM   967  O  O   . ARG A 1 123 ? -29.462 19.640  -10.297 1.00 43.16  ? 123 ARG A O   1 
ATOM   968  C  CB  . ARG A 1 123 ? -29.431 21.381  -13.042 1.00 45.15  ? 123 ARG A CB  1 
ATOM   969  C  CG  . ARG A 1 123 ? -30.106 22.236  -11.948 1.00 41.68  ? 123 ARG A CG  1 
ATOM   970  C  CD  . ARG A 1 123 ? -30.872 23.432  -12.508 1.00 45.40  ? 123 ARG A CD  1 
ATOM   971  N  NE  . ARG A 1 123 ? -30.012 24.482  -13.055 1.00 44.63  ? 123 ARG A NE  1 
ATOM   972  C  CZ  . ARG A 1 123 ? -29.510 25.475  -12.328 1.00 54.67  ? 123 ARG A CZ  1 
ATOM   973  N  NH1 . ARG A 1 123 ? -29.719 25.548  -11.026 1.00 46.22  ? 123 ARG A NH1 1 
ATOM   974  N  NH2 . ARG A 1 123 ? -28.796 26.428  -12.924 1.00 48.12  ? 123 ARG A NH2 1 
ATOM   975  N  N   . ALA A 1 124 ? -30.251 18.470  -12.039 1.00 43.80  ? 124 ALA A N   1 
ATOM   976  C  CA  . ALA A 1 124 ? -31.199 17.747  -11.205 1.00 47.42  ? 124 ALA A CA  1 
ATOM   977  C  C   . ALA A 1 124 ? -30.481 16.807  -10.260 1.00 46.57  ? 124 ALA A C   1 
ATOM   978  O  O   . ALA A 1 124 ? -30.917 16.614  -9.120  1.00 51.37  ? 124 ALA A O   1 
ATOM   979  C  CB  . ALA A 1 124 ? -32.186 16.967  -12.081 1.00 47.05  ? 124 ALA A CB  1 
ATOM   980  N  N   . ASN A 1 125 ? -29.368 16.244  -10.697 1.00 44.08  ? 125 ASN A N   1 
ATOM   981  C  CA  . ASN A 1 125 ? -28.634 15.342  -9.821  1.00 47.83  ? 125 ASN A CA  1 
ATOM   982  C  C   . ASN A 1 125 ? -27.821 16.094  -8.767  1.00 50.35  ? 125 ASN A C   1 
ATOM   983  O  O   . ASN A 1 125 ? -27.759 15.659  -7.607  1.00 47.20  ? 125 ASN A O   1 
ATOM   984  C  CB  . ASN A 1 125 ? -27.755 14.442  -10.677 1.00 43.25  ? 125 ASN A CB  1 
ATOM   985  C  CG  . ASN A 1 125 ? -28.580 13.515  -11.527 1.00 52.91  ? 125 ASN A CG  1 
ATOM   986  O  OD1 . ASN A 1 125 ? -29.591 12.977  -11.071 1.00 52.14  ? 125 ASN A OD1 1 
ATOM   987  N  ND2 . ASN A 1 125 ? -28.177 13.341  -12.770 1.00 55.60  ? 125 ASN A ND2 1 
ATOM   988  N  N   . TYR A 1 126 ? -27.180 17.208  -9.147  1.00 43.65  ? 126 TYR A N   1 
ATOM   989  C  CA  . TYR A 1 126 ? -26.553 18.071  -8.144  1.00 47.60  ? 126 TYR A CA  1 
ATOM   990  C  C   . TYR A 1 126 ? -27.567 18.536  -7.115  1.00 41.13  ? 126 TYR A C   1 
ATOM   991  O  O   . TYR A 1 126 ? -27.282 18.565  -5.922  1.00 45.00  ? 126 TYR A O   1 
ATOM   992  C  CB  . TYR A 1 126 ? -25.902 19.277  -8.817  1.00 41.09  ? 126 TYR A CB  1 
ATOM   993  C  CG  . TYR A 1 126 ? -24.575 18.935  -9.420  1.00 40.95  ? 126 TYR A CG  1 
ATOM   994  C  CD1 . TYR A 1 126 ? -24.480 18.393  -10.697 1.00 41.94  ? 126 TYR A CD1 1 
ATOM   995  C  CD2 . TYR A 1 126 ? -23.409 19.127  -8.694  1.00 45.40  ? 126 TYR A CD2 1 
ATOM   996  C  CE1 . TYR A 1 126 ? -23.240 18.058  -11.229 1.00 43.94  ? 126 TYR A CE1 1 
ATOM   997  C  CE2 . TYR A 1 126 ? -22.184 18.803  -9.215  1.00 48.16  ? 126 TYR A CE2 1 
ATOM   998  C  CZ  . TYR A 1 126 ? -22.102 18.286  -10.476 1.00 42.12  ? 126 TYR A CZ  1 
ATOM   999  O  OH  . TYR A 1 126 ? -20.865 17.983  -10.941 1.00 38.68  ? 126 TYR A OH  1 
ATOM   1000 N  N   . LEU A 1 127 ? -28.755 18.924  -7.569  1.00 49.79  ? 127 LEU A N   1 
ATOM   1001 C  CA  . LEU A 1 127 ? -29.803 19.317  -6.644  1.00 51.31  ? 127 LEU A CA  1 
ATOM   1002 C  C   . LEU A 1 127 ? -30.130 18.167  -5.704  1.00 54.01  ? 127 LEU A C   1 
ATOM   1003 O  O   . LEU A 1 127 ? -30.244 18.349  -4.488  1.00 49.93  ? 127 LEU A O   1 
ATOM   1004 C  CB  . LEU A 1 127 ? -31.047 19.751  -7.426  1.00 49.74  ? 127 LEU A CB  1 
ATOM   1005 C  CG  . LEU A 1 127 ? -32.175 20.247  -6.526  1.00 58.14  ? 127 LEU A CG  1 
ATOM   1006 C  CD1 . LEU A 1 127 ? -31.782 21.604  -5.952  1.00 65.27  ? 127 LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A 1 127 ? -33.528 20.317  -7.234  1.00 57.38  ? 127 LEU A CD2 1 
ATOM   1008 N  N   . GLN A 1 128 ? -30.249 16.959  -6.253  1.00 50.06  ? 128 GLN A N   1 
ATOM   1009 C  CA  . GLN A 1 128 ? -30.569 15.823  -5.411  1.00 54.97  ? 128 GLN A CA  1 
ATOM   1010 C  C   . GLN A 1 128 ? -29.411 15.500  -4.498  1.00 50.96  ? 128 GLN A C   1 
ATOM   1011 O  O   . GLN A 1 128 ? -29.596 15.282  -3.299  1.00 51.45  ? 128 GLN A O   1 
ATOM   1012 C  CB  . GLN A 1 128 ? -30.922 14.625  -6.266  1.00 59.22  ? 128 GLN A CB  1 
ATOM   1013 C  CG  . GLN A 1 128 ? -32.214 14.043  -5.872  1.00 69.38  ? 128 GLN A CG  1 
ATOM   1014 C  CD  . GLN A 1 128 ? -32.607 12.919  -6.778  1.00 75.68  ? 128 GLN A CD  1 
ATOM   1015 O  OE1 . GLN A 1 128 ? -32.750 13.100  -8.001  1.00 84.17  ? 128 GLN A OE1 1 
ATOM   1016 N  NE2 . GLN A 1 128 ? -32.784 11.753  -6.204  1.00 75.73  ? 128 GLN A NE2 1 
ATOM   1017 N  N   . LEU A 1 129 ? -28.201 15.497  -5.048  1.00 50.04  ? 129 LEU A N   1 
ATOM   1018 C  CA  . LEU A 1 129 ? -27.031 15.394  -4.199  1.00 47.06  ? 129 LEU A CA  1 
ATOM   1019 C  C   . LEU A 1 129 ? -27.068 16.449  -3.098  1.00 54.18  ? 129 LEU A C   1 
ATOM   1020 O  O   . LEU A 1 129 ? -26.822 16.136  -1.927  1.00 53.03  ? 129 LEU A O   1 
ATOM   1021 C  CB  . LEU A 1 129 ? -25.770 15.525  -5.045  1.00 43.59  ? 129 LEU A CB  1 
ATOM   1022 C  CG  . LEU A 1 129 ? -24.520 14.943  -4.429  1.00 52.12  ? 129 LEU A CG  1 
ATOM   1023 C  CD1 . LEU A 1 129 ? -24.829 13.531  -3.971  1.00 55.86  ? 129 LEU A CD1 1 
ATOM   1024 C  CD2 . LEU A 1 129 ? -23.478 14.938  -5.505  1.00 53.19  ? 129 LEU A CD2 1 
ATOM   1025 N  N   . GLU A 1 130 ? -27.409 17.699  -3.442  1.00 45.94  ? 130 GLU A N   1 
ATOM   1026 C  CA  . GLU A 1 130 ? -27.476 18.746  -2.421  1.00 50.43  ? 130 GLU A CA  1 
ATOM   1027 C  C   . GLU A 1 130 ? -28.479 18.390  -1.325  1.00 55.68  ? 130 GLU A C   1 
ATOM   1028 O  O   . GLU A 1 130 ? -28.203 18.552  -0.127  1.00 51.74  ? 130 GLU A O   1 
ATOM   1029 C  CB  . GLU A 1 130 ? -27.836 20.094  -3.057  1.00 49.93  ? 130 GLU A CB  1 
ATOM   1030 C  CG  . GLU A 1 130 ? -28.381 21.084  -2.045  1.00 48.83  ? 130 GLU A CG  1 
ATOM   1031 C  CD  . GLU A 1 130 ? -28.082 22.534  -2.374  1.00 60.53  ? 130 GLU A CD  1 
ATOM   1032 O  OE1 . GLU A 1 130 ? -28.052 22.909  -3.564  1.00 53.00  ? 130 GLU A OE1 1 
ATOM   1033 O  OE2 . GLU A 1 130 ? -27.873 23.306  -1.422  1.00 69.71  ? 130 GLU A OE2 1 
ATOM   1034 N  N   . ARG A 1 131 ? -29.656 17.900  -1.715  1.00 54.77  ? 131 ARG A N   1 
ATOM   1035 C  CA  . ARG A 1 131 ? -30.675 17.614  -0.717  1.00 59.51  ? 131 ARG A CA  1 
ATOM   1036 C  C   . ARG A 1 131 ? -30.218 16.517  0.221   1.00 57.24  ? 131 ARG A C   1 
ATOM   1037 O  O   . ARG A 1 131 ? -30.414 16.605  1.434   1.00 60.73  ? 131 ARG A O   1 
ATOM   1038 C  CB  . ARG A 1 131 ? -31.980 17.202  -1.387  1.00 60.56  ? 131 ARG A CB  1 
ATOM   1039 C  CG  . ARG A 1 131 ? -32.489 18.187  -2.408  1.00 63.97  ? 131 ARG A CG  1 
ATOM   1040 C  CD  . ARG A 1 131 ? -33.992 18.078  -2.459  1.00 79.97  ? 131 ARG A CD  1 
ATOM   1041 N  NE  . ARG A 1 131 ? -34.605 19.089  -3.309  1.00 87.82  ? 131 ARG A NE  1 
ATOM   1042 C  CZ  . ARG A 1 131 ? -34.680 20.384  -3.024  1.00 92.51  ? 131 ARG A CZ  1 
ATOM   1043 N  NH1 . ARG A 1 131 ? -34.127 20.887  -1.929  1.00 94.25  ? 131 ARG A NH1 1 
ATOM   1044 N  NH2 . ARG A 1 131 ? -35.318 21.198  -3.865  1.00 86.27  ? 131 ARG A NH2 1 
ATOM   1045 N  N   . ALA A 1 132 ? -29.608 15.474  -0.323  1.00 52.20  ? 132 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 132 ? -29.229 14.312  0.468   1.00 54.82  ? 132 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 132 ? -27.992 14.552  1.331   1.00 59.06  ? 132 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 132 ? -27.899 14.009  2.443   1.00 54.45  ? 132 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 132 ? -28.983 13.125  -0.457  1.00 52.45  ? 132 ALA A CB  1 
ATOM   1050 N  N   . LEU A 1 133 ? -27.010 15.316  0.835   1.00 51.63  ? 133 LEU A N   1 
ATOM   1051 C  CA  . LEU A 1 133 ? -25.758 15.496  1.569   1.00 52.71  ? 133 LEU A CA  1 
ATOM   1052 C  C   . LEU A 1 133 ? -25.713 16.788  2.387   1.00 49.63  ? 133 LEU A C   1 
ATOM   1053 O  O   . LEU A 1 133 ? -24.826 16.931  3.229   1.00 48.39  ? 133 LEU A O   1 
ATOM   1054 C  CB  . LEU A 1 133 ? -24.558 15.443  0.602   1.00 53.90  ? 133 LEU A CB  1 
ATOM   1055 C  CG  . LEU A 1 133 ? -24.470 14.204  -0.301  1.00 55.48  ? 133 LEU A CG  1 
ATOM   1056 C  CD1 . LEU A 1 133 ? -23.115 14.073  -0.937  1.00 49.53  ? 133 LEU A CD1 1 
ATOM   1057 C  CD2 . LEU A 1 133 ? -24.774 12.964  0.509   1.00 59.91  ? 133 LEU A CD2 1 
ATOM   1058 N  N   . GLY A 1 134 ? -26.629 17.726  2.171   1.00 52.10  ? 134 GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 134 ? -26.625 18.982  2.923   1.00 45.96  ? 134 GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 134 ? -25.437 19.882  2.648   1.00 50.09  ? 134 GLY A C   1 
ATOM   1061 O  O   . GLY A 1 134 ? -24.906 20.526  3.570   1.00 47.58  ? 134 GLY A O   1 
ATOM   1062 N  N   . ILE A 1 135 ? -25.008 19.943  1.394   1.00 49.44  ? 135 ILE A N   1 
ATOM   1063 C  CA  . ILE A 1 135 ? -23.858 20.737  0.970   1.00 52.56  ? 135 ILE A CA  1 
ATOM   1064 C  C   . ILE A 1 135 ? -24.290 21.488  -0.284  1.00 53.23  ? 135 ILE A C   1 
ATOM   1065 O  O   . ILE A 1 135 ? -24.962 20.914  -1.154  1.00 52.40  ? 135 ILE A O   1 
ATOM   1066 C  CB  . ILE A 1 135 ? -22.624 19.854  0.713   1.00 54.83  ? 135 ILE A CB  1 
ATOM   1067 C  CG1 . ILE A 1 135 ? -22.832 19.011  -0.552  1.00 63.16  ? 135 ILE A CG1 1 
ATOM   1068 C  CG2 . ILE A 1 135 ? -22.389 18.901  1.872   1.00 50.28  ? 135 ILE A CG2 1 
ATOM   1069 C  CD1 . ILE A 1 135 ? -21.945 17.717  -0.650  1.00 60.28  ? 135 ILE A CD1 1 
ATOM   1070 N  N   . PRO A 1 136 ? -23.976 22.761  -0.412  1.00 53.67  ? 136 PRO A N   1 
ATOM   1071 C  CA  . PRO A 1 136 ? -24.574 23.544  -1.499  1.00 51.22  ? 136 PRO A CA  1 
ATOM   1072 C  C   . PRO A 1 136 ? -23.847 23.319  -2.824  1.00 49.52  ? 136 PRO A C   1 
ATOM   1073 O  O   . PRO A 1 136 ? -23.192 24.221  -3.363  1.00 48.60  ? 136 PRO A O   1 
ATOM   1074 C  CB  . PRO A 1 136 ? -24.443 24.980  -0.973  1.00 53.29  ? 136 PRO A CB  1 
ATOM   1075 C  CG  . PRO A 1 136 ? -23.135 24.955  -0.221  1.00 55.45  ? 136 PRO A CG  1 
ATOM   1076 C  CD  . PRO A 1 136 ? -23.022 23.560  0.382   1.00 57.18  ? 136 PRO A CD  1 
ATOM   1077 N  N   . VAL A 1 137 ? -23.937 22.084  -3.338  1.00 40.93  ? 137 VAL A N   1 
ATOM   1078 C  CA  . VAL A 1 137 ? -23.228 21.712  -4.555  1.00 45.43  ? 137 VAL A CA  1 
ATOM   1079 C  C   . VAL A 1 137 ? -23.966 22.173  -5.797  1.00 49.47  ? 137 VAL A C   1 
ATOM   1080 O  O   . VAL A 1 137 ? -23.438 22.034  -6.903  1.00 50.49  ? 137 VAL A O   1 
ATOM   1081 C  CB  . VAL A 1 137 ? -22.982 20.193  -4.669  1.00 48.90  ? 137 VAL A CB  1 
ATOM   1082 C  CG1 . VAL A 1 137 ? -21.984 19.771  -3.680  1.00 45.80  ? 137 VAL A CG1 1 
ATOM   1083 C  CG2 . VAL A 1 137 ? -24.289 19.381  -4.511  1.00 49.09  ? 137 VAL A CG2 1 
ATOM   1084 N  N   . THR A 1 138 ? -25.186 22.694  -5.650  1.00 49.80  ? 138 THR A N   1 
ATOM   1085 C  CA  . THR A 1 138 ? -25.838 23.346  -6.773  1.00 43.87  ? 138 THR A CA  1 
ATOM   1086 C  C   . THR A 1 138 ? -25.107 24.629  -7.114  1.00 52.05  ? 138 THR A C   1 
ATOM   1087 O  O   . THR A 1 138 ? -24.796 24.892  -8.281  1.00 48.03  ? 138 THR A O   1 
ATOM   1088 C  CB  . THR A 1 138 ? -27.301 23.651  -6.454  1.00 48.34  ? 138 THR A CB  1 
ATOM   1089 O  OG1 . THR A 1 138 ? -27.974 22.447  -6.057  1.00 60.06  ? 138 THR A OG1 1 
ATOM   1090 C  CG2 . THR A 1 138 ? -27.995 24.224  -7.692  1.00 56.60  ? 138 THR A CG2 1 
ATOM   1091 N  N   . ARG A 1 139 ? -24.784 25.419  -6.092  1.00 44.43  ? 139 ARG A N   1 
ATOM   1092 C  CA  . ARG A 1 139 ? -24.069 26.705  -6.293  1.00 49.12  ? 139 ARG A CA  1 
ATOM   1093 C  C   . ARG A 1 139 ? -22.566 26.457  -6.400  1.00 49.64  ? 139 ARG A C   1 
ATOM   1094 O  O   . ARG A 1 139 ? -21.900 27.180  -7.151  1.00 48.05  ? 139 ARG A O   1 
ATOM   1095 C  CB  . ARG A 1 139 ? -24.374 27.636  -5.119  1.00 44.72  ? 139 ARG A CB  1 
ATOM   1096 C  CG  . ARG A 1 139 ? -23.370 28.758  -4.901  1.00 53.96  ? 139 ARG A CG  1 
ATOM   1097 C  CD  . ARG A 1 139 ? -23.869 30.072  -5.464  1.00 73.99  ? 139 ARG A CD  1 
ATOM   1098 N  NE  . ARG A 1 139 ? -22.928 31.155  -5.225  1.00 83.32  ? 139 ARG A NE  1 
ATOM   1099 C  CZ  . ARG A 1 139 ? -22.603 31.614  -4.023  1.00 85.43  ? 139 ARG A CZ  1 
ATOM   1100 N  NH1 . ARG A 1 139 ? -23.520 31.698  -3.076  1.00 82.38  ? 139 ARG A NH1 1 
ATOM   1101 N  NH2 . ARG A 1 139 ? -21.360 31.989  -3.775  1.00 85.99  ? 139 ARG A NH2 1 
ATOM   1102 N  N   . LYS A 1 140 ? -22.060 25.457  -5.686  1.00 44.69  ? 140 LYS A N   1 
ATOM   1103 C  CA  . LYS A 1 140 ? -20.621 25.205  -5.682  1.00 54.00  ? 140 LYS A CA  1 
ATOM   1104 C  C   . LYS A 1 140 ? -20.383 23.769  -6.134  1.00 49.50  ? 140 LYS A C   1 
ATOM   1105 O  O   . LYS A 1 140 ? -20.010 22.910  -5.323  1.00 49.31  ? 140 LYS A O   1 
ATOM   1106 C  CB  . LYS A 1 140 ? -20.010 25.451  -4.295  1.00 53.57  ? 140 LYS A CB  1 
ATOM   1107 C  CG  . LYS A 1 140 ? -20.642 26.578  -3.462  1.00 53.13  ? 140 LYS A CG  1 
ATOM   1108 C  CD  . LYS A 1 140 ? -19.564 27.321  -2.661  1.00 60.64  ? 140 LYS A CD  1 
ATOM   1109 C  CE  . LYS A 1 140 ? -18.565 27.971  -3.652  1.00 63.36  ? 140 LYS A CE  1 
ATOM   1110 N  NZ  . LYS A 1 140 ? -17.407 28.684  -3.025  1.00 74.94  ? 140 LYS A NZ  1 
ATOM   1111 N  N   . PRO A 1 141 ? -20.586 23.471  -7.423  1.00 44.17  ? 141 PRO A N   1 
ATOM   1112 C  CA  . PRO A 1 141 ? -20.473 22.067  -7.858  1.00 43.40  ? 141 PRO A CA  1 
ATOM   1113 C  C   . PRO A 1 141 ? -19.051 21.555  -7.822  1.00 49.77  ? 141 PRO A C   1 
ATOM   1114 O  O   . PRO A 1 141 ? -18.850 20.341  -7.706  1.00 47.17  ? 141 PRO A O   1 
ATOM   1115 C  CB  . PRO A 1 141 ? -21.037 22.083  -9.289  1.00 46.62  ? 141 PRO A CB  1 
ATOM   1116 C  CG  . PRO A 1 141 ? -20.823 23.488  -9.770  1.00 47.55  ? 141 PRO A CG  1 
ATOM   1117 C  CD  . PRO A 1 141 ? -20.910 24.385  -8.538  1.00 44.82  ? 141 PRO A CD  1 
ATOM   1118 N  N   . GLU A 1 142 ? -18.058 22.436  -7.893  1.00 45.96  ? 142 GLU A N   1 
ATOM   1119 C  CA  . GLU A 1 142 ? -16.684 21.969  -7.833  1.00 50.38  ? 142 GLU A CA  1 
ATOM   1120 C  C   . GLU A 1 142 ? -16.309 21.414  -6.473  1.00 48.83  ? 142 GLU A C   1 
ATOM   1121 O  O   . GLU A 1 142 ? -15.185 20.933  -6.328  1.00 47.54  ? 142 GLU A O   1 
ATOM   1122 C  CB  . GLU A 1 142 ? -15.729 23.102  -8.216  1.00 48.45  ? 142 GLU A CB  1 
ATOM   1123 C  CG  . GLU A 1 142 ? -15.520 24.156  -7.128  1.00 47.90  ? 142 GLU A CG  1 
ATOM   1124 C  CD  . GLU A 1 142 ? -16.701 25.092  -6.939  1.00 53.21  ? 142 GLU A CD  1 
ATOM   1125 O  OE1 . GLU A 1 142 ? -17.682 24.997  -7.717  1.00 47.08  ? 142 GLU A OE1 1 
ATOM   1126 O  OE2 . GLU A 1 142 ? -16.639 25.933  -6.011  1.00 55.94  ? 142 GLU A OE2 1 
ATOM   1127 N  N   . LEU A 1 143 ? -17.198 21.446  -5.472  1.00 51.11  ? 143 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 143 ? -16.880 20.777  -4.209  1.00 49.04  ? 143 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 143 ? -16.843 19.262  -4.364  1.00 52.87  ? 143 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 143 ? -16.372 18.570  -3.453  1.00 47.43  ? 143 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 143 ? -17.885 21.150  -3.108  1.00 46.46  ? 143 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 143 ? -17.988 22.601  -2.642  1.00 51.46  ? 143 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 143 ? -19.178 22.792  -1.709  1.00 51.25  ? 143 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 143 ? -16.697 23.075  -1.977  1.00 56.18  ? 143 LEU A CD2 1 
ATOM   1135 N  N   . LEU A 1 144 ? -17.333 18.725  -5.482  1.00 45.41  ? 144 LEU A N   1 
ATOM   1136 C  CA  . LEU A 1 144 ? -17.226 17.289  -5.696  1.00 50.61  ? 144 LEU A CA  1 
ATOM   1137 C  C   . LEU A 1 144 ? -15.843 16.875  -6.202  1.00 50.77  ? 144 LEU A C   1 
ATOM   1138 O  O   . LEU A 1 144 ? -15.584 15.676  -6.369  1.00 51.42  ? 144 LEU A O   1 
ATOM   1139 C  CB  . LEU A 1 144 ? -18.309 16.816  -6.665  1.00 51.42  ? 144 LEU A CB  1 
ATOM   1140 C  CG  . LEU A 1 144 ? -19.751 16.924  -6.168  1.00 50.64  ? 144 LEU A CG  1 
ATOM   1141 C  CD1 . LEU A 1 144 ? -20.622 15.998  -6.974  1.00 53.19  ? 144 LEU A CD1 1 
ATOM   1142 C  CD2 . LEU A 1 144 ? -19.836 16.554  -4.723  1.00 50.97  ? 144 LEU A CD2 1 
ATOM   1143 N  N   . GLU A 1 145 ? -14.955 17.830  -6.458  1.00 46.54  ? 145 GLU A N   1 
ATOM   1144 C  CA  . GLU A 1 145 ? -13.577 17.496  -6.781  1.00 53.24  ? 145 GLU A CA  1 
ATOM   1145 C  C   . GLU A 1 145 ? -12.761 17.200  -5.536  1.00 57.22  ? 145 GLU A C   1 
ATOM   1146 O  O   . GLU A 1 145 ? -11.601 16.804  -5.658  1.00 58.14  ? 145 GLU A O   1 
ATOM   1147 C  CB  . GLU A 1 145 ? -12.913 18.632  -7.576  1.00 44.78  ? 145 GLU A CB  1 
ATOM   1148 C  CG  . GLU A 1 145 ? -13.630 18.922  -8.886  1.00 48.68  ? 145 GLU A CG  1 
ATOM   1149 C  CD  . GLU A 1 145 ? -12.888 19.903  -9.788  1.00 58.43  ? 145 GLU A CD  1 
ATOM   1150 O  OE1 . GLU A 1 145 ? -13.550 20.533  -10.653 1.00 57.95  ? 145 GLU A OE1 1 
ATOM   1151 O  OE2 . GLU A 1 145 ? -11.646 20.041  -9.650  1.00 49.97  ? 145 GLU A OE2 1 
ATOM   1152 N  N   . THR A 1 146 ? -13.330 17.391  -4.349  1.00 55.27  ? 146 THR A N   1 
ATOM   1153 C  CA  . THR A 1 146 ? -12.601 17.079  -3.133  1.00 58.60  ? 146 THR A CA  1 
ATOM   1154 C  C   . THR A 1 146 ? -12.633 15.580  -2.859  1.00 58.12  ? 146 THR A C   1 
ATOM   1155 O  O   . THR A 1 146 ? -13.530 14.847  -3.303  1.00 51.38  ? 146 THR A O   1 
ATOM   1156 C  CB  . THR A 1 146 ? -13.175 17.834  -1.943  1.00 56.73  ? 146 THR A CB  1 
ATOM   1157 O  OG1 . THR A 1 146 ? -14.510 17.387  -1.692  1.00 54.11  ? 146 THR A OG1 1 
ATOM   1158 C  CG2 . THR A 1 146 ? -13.202 19.307  -2.241  1.00 57.80  ? 146 THR A CG2 1 
ATOM   1159 N  N   . GLN A 1 147 ? -11.624 15.123  -2.124  1.00 53.18  ? 147 GLN A N   1 
ATOM   1160 C  CA  . GLN A 1 147 ? -11.637 13.741  -1.671  1.00 54.77  ? 147 GLN A CA  1 
ATOM   1161 C  C   . GLN A 1 147 ? -12.850 13.465  -0.798  1.00 51.53  ? 147 GLN A C   1 
ATOM   1162 O  O   . GLN A 1 147 ? -13.490 12.416  -0.931  1.00 51.74  ? 147 GLN A O   1 
ATOM   1163 C  CB  . GLN A 1 147 ? -10.357 13.424  -0.913  1.00 54.83  ? 147 GLN A CB  1 
ATOM   1164 C  CG  . GLN A 1 147 ? -9.097  13.601  -1.702  1.00 56.24  ? 147 GLN A CG  1 
ATOM   1165 C  CD  . GLN A 1 147 ? -8.047  12.641  -1.240  1.00 68.12  ? 147 GLN A CD  1 
ATOM   1166 O  OE1 . GLN A 1 147 ? -7.819  12.524  -0.026  1.00 75.93  ? 147 GLN A OE1 1 
ATOM   1167 N  NE2 . GLN A 1 147 ? -7.438  11.905  -2.168  1.00 61.83  ? 147 GLN A NE2 1 
ATOM   1168 N  N   . ALA A 1 148 ? -13.199 14.416  0.075   1.00 56.61  ? 148 ALA A N   1 
ATOM   1169 C  CA  . ALA A 1 148 ? -14.223 14.186  1.089   1.00 52.84  ? 148 ALA A CA  1 
ATOM   1170 C  C   . ALA A 1 148 ? -15.610 14.077  0.473   1.00 51.39  ? 148 ALA A C   1 
ATOM   1171 O  O   . ALA A 1 148 ? -16.362 13.143  0.772   1.00 48.10  ? 148 ALA A O   1 
ATOM   1172 C  CB  . ALA A 1 148 ? -14.195 15.308  2.128   1.00 63.05  ? 148 ALA A CB  1 
ATOM   1173 N  N   . LEU A 1 149 ? -15.977 15.018  -0.392  1.00 56.85  ? 149 LEU A N   1 
ATOM   1174 C  CA  . LEU A 1 149 ? -17.313 14.939  -0.958  1.00 53.23  ? 149 LEU A CA  1 
ATOM   1175 C  C   . LEU A 1 149 ? -17.355 14.121  -2.237  1.00 46.86  ? 149 LEU A C   1 
ATOM   1176 O  O   . LEU A 1 149 ? -18.415 13.589  -2.576  1.00 55.26  ? 149 LEU A O   1 
ATOM   1177 C  CB  . LEU A 1 149 ? -17.880 16.338  -1.202  1.00 52.15  ? 149 LEU A CB  1 
ATOM   1178 C  CG  . LEU A 1 149 ? -18.016 17.148  0.091   1.00 61.14  ? 149 LEU A CG  1 
ATOM   1179 C  CD1 . LEU A 1 149 ? -18.625 18.532  -0.209  1.00 66.61  ? 149 LEU A CD1 1 
ATOM   1180 C  CD2 . LEU A 1 149 ? -18.920 16.455  1.090   1.00 58.80  ? 149 LEU A CD2 1 
ATOM   1181 N  N   . GLY A 1 150 ? -16.237 13.996  -2.948  1.00 47.82  ? 150 GLY A N   1 
ATOM   1182 C  CA  . GLY A 1 150 ? -16.186 13.047  -4.058  1.00 54.99  ? 150 GLY A CA  1 
ATOM   1183 C  C   . GLY A 1 150 ? -16.415 11.615  -3.597  1.00 53.36  ? 150 GLY A C   1 
ATOM   1184 O  O   . GLY A 1 150 ? -17.209 10.879  -4.187  1.00 50.90  ? 150 GLY A O   1 
ATOM   1185 N  N   . ALA A 1 151 ? -15.737 11.210  -2.517  1.00 53.38  ? 151 ALA A N   1 
ATOM   1186 C  CA  . ALA A 1 151 ? -15.970 9.881   -1.948  1.00 55.05  ? 151 ALA A CA  1 
ATOM   1187 C  C   . ALA A 1 151 ? -17.414 9.714   -1.495  1.00 50.33  ? 151 ALA A C   1 
ATOM   1188 O  O   . ALA A 1 151 ? -18.044 8.685   -1.761  1.00 50.95  ? 151 ALA A O   1 
ATOM   1189 C  CB  . ALA A 1 151 ? -15.030 9.630   -0.762  1.00 53.02  ? 151 ALA A CB  1 
ATOM   1190 N  N   . LEU A 1 152 ? -17.950 10.705  -0.792  1.00 48.74  ? 152 LEU A N   1 
ATOM   1191 C  CA  . LEU A 1 152 ? -19.317 10.582  -0.299  1.00 53.02  ? 152 LEU A CA  1 
ATOM   1192 C  C   . LEU A 1 152 ? -20.310 10.531  -1.461  1.00 51.43  ? 152 LEU A C   1 
ATOM   1193 O  O   . LEU A 1 152 ? -21.285 9.767   -1.422  1.00 48.91  ? 152 LEU A O   1 
ATOM   1194 C  CB  . LEU A 1 152 ? -19.630 11.739  0.657   1.00 52.03  ? 152 LEU A CB  1 
ATOM   1195 C  CG  . LEU A 1 152 ? -20.633 11.582  1.801   1.00 58.20  ? 152 LEU A CG  1 
ATOM   1196 C  CD1 . LEU A 1 152 ? -20.185 10.543  2.811   1.00 54.69  ? 152 LEU A CD1 1 
ATOM   1197 C  CD2 . LEU A 1 152 ? -20.866 12.914  2.534   1.00 53.29  ? 152 LEU A CD2 1 
ATOM   1198 N  N   . ALA A 1 153 ? -20.058 11.319  -2.508  1.00 45.95  ? 153 ALA A N   1 
ATOM   1199 C  CA  . ALA A 1 153 ? -20.929 11.347  -3.681  1.00 55.23  ? 153 ALA A CA  1 
ATOM   1200 C  C   . ALA A 1 153 ? -20.757 10.102  -4.530  1.00 54.15  ? 153 ALA A C   1 
ATOM   1201 O  O   . ALA A 1 153 ? -21.744 9.556   -5.034  1.00 48.49  ? 153 ALA A O   1 
ATOM   1202 C  CB  . ALA A 1 153 ? -20.638 12.578  -4.531  1.00 45.25  ? 153 ALA A CB  1 
ATOM   1203 N  N   . ALA A 1 154 ? -19.506 9.679   -4.750  1.00 49.39  ? 154 ALA A N   1 
ATOM   1204 C  CA  . ALA A 1 154 ? -19.253 8.382   -5.369  1.00 51.38  ? 154 ALA A CA  1 
ATOM   1205 C  C   . ALA A 1 154 ? -20.000 7.264   -4.641  1.00 52.87  ? 154 ALA A C   1 
ATOM   1206 O  O   . ALA A 1 154 ? -20.670 6.441   -5.266  1.00 51.77  ? 154 ALA A O   1 
ATOM   1207 C  CB  . ALA A 1 154 ? -17.754 8.095   -5.386  1.00 51.90  ? 154 ALA A CB  1 
ATOM   1208 N  N   . ALA A 1 155 ? -19.900 7.220   -3.312  1.00 51.18  ? 155 ALA A N   1 
ATOM   1209 C  CA  . ALA A 1 155 ? -20.588 6.154   -2.585  1.00 53.67  ? 155 ALA A CA  1 
ATOM   1210 C  C   . ALA A 1 155 ? -22.098 6.331   -2.635  1.00 53.87  ? 155 ALA A C   1 
ATOM   1211 O  O   . ALA A 1 155 ? -22.835 5.345   -2.778  1.00 53.33  ? 155 ALA A O   1 
ATOM   1212 C  CB  . ALA A 1 155 ? -20.119 6.084   -1.134  1.00 52.58  ? 155 ALA A CB  1 
ATOM   1213 N  N   . LYS A 1 156 ? -22.588 7.570   -2.515  1.00 49.85  ? 156 LYS A N   1 
ATOM   1214 C  CA  . LYS A 1 156 ? -24.030 7.766   -2.621  1.00 58.28  ? 156 LYS A CA  1 
ATOM   1215 C  C   . LYS A 1 156 ? -24.539 7.397   -4.013  1.00 56.09  ? 156 LYS A C   1 
ATOM   1216 O  O   . LYS A 1 156 ? -25.649 6.870   -4.152  1.00 59.44  ? 156 LYS A O   1 
ATOM   1217 C  CB  . LYS A 1 156 ? -24.439 9.203   -2.291  1.00 62.83  ? 156 LYS A CB  1 
ATOM   1218 C  CG  . LYS A 1 156 ? -25.835 9.485   -2.861  1.00 63.12  ? 156 LYS A CG  1 
ATOM   1219 C  CD  . LYS A 1 156 ? -26.561 10.712  -2.371  1.00 58.90  ? 156 LYS A CD  1 
ATOM   1220 C  CE  . LYS A 1 156 ? -27.796 10.929  -3.282  1.00 63.74  ? 156 LYS A CE  1 
ATOM   1221 N  NZ  . LYS A 1 156 ? -28.985 10.028  -2.938  1.00 48.57  ? 156 LYS A NZ  1 
ATOM   1222 N  N   . PHE A 1 157 ? -23.746 7.652   -5.056  1.00 54.39  ? 157 PHE A N   1 
ATOM   1223 C  CA  . PHE A 1 157 ? -24.184 7.296   -6.405  1.00 54.03  ? 157 PHE A CA  1 
ATOM   1224 C  C   . PHE A 1 157 ? -24.351 5.787   -6.544  1.00 53.03  ? 157 PHE A C   1 
ATOM   1225 O  O   . PHE A 1 157 ? -25.298 5.317   -7.183  1.00 58.95  ? 157 PHE A O   1 
ATOM   1226 C  CB  . PHE A 1 157 ? -23.187 7.832   -7.431  1.00 61.65  ? 157 PHE A CB  1 
ATOM   1227 C  CG  . PHE A 1 157 ? -23.517 7.498   -8.868  1.00 59.22  ? 157 PHE A CG  1 
ATOM   1228 C  CD1 . PHE A 1 157 ? -23.260 6.236   -9.385  1.00 55.92  ? 157 PHE A CD1 1 
ATOM   1229 C  CD2 . PHE A 1 157 ? -24.036 8.472   -9.718  1.00 57.88  ? 157 PHE A CD2 1 
ATOM   1230 C  CE1 . PHE A 1 157 ? -23.547 5.942   -10.694 1.00 59.01  ? 157 PHE A CE1 1 
ATOM   1231 C  CE2 . PHE A 1 157 ? -24.321 8.189   -11.033 1.00 58.65  ? 157 PHE A CE2 1 
ATOM   1232 C  CZ  . PHE A 1 157 ? -24.074 6.920   -11.528 1.00 59.15  ? 157 PHE A CZ  1 
ATOM   1233 N  N   . TRP A 1 158 ? -23.433 5.011   -5.963  1.00 52.17  ? 158 TRP A N   1 
ATOM   1234 C  CA  . TRP A 1 158 ? -23.538 3.552   -6.027  1.00 57.55  ? 158 TRP A CA  1 
ATOM   1235 C  C   . TRP A 1 158 ? -24.717 3.059   -5.191  1.00 61.09  ? 158 TRP A C   1 
ATOM   1236 O  O   . TRP A 1 158 ? -25.449 2.147   -5.601  1.00 58.64  ? 158 TRP A O   1 
ATOM   1237 C  CB  . TRP A 1 158 ? -22.216 2.923   -5.558  1.00 56.08  ? 158 TRP A CB  1 
ATOM   1238 C  CG  . TRP A 1 158 ? -22.173 1.404   -5.542  1.00 65.73  ? 158 TRP A CG  1 
ATOM   1239 C  CD1 . TRP A 1 158 ? -22.571 0.576   -4.523  1.00 67.92  ? 158 TRP A CD1 1 
ATOM   1240 C  CD2 . TRP A 1 158 ? -21.681 0.540   -6.590  1.00 62.62  ? 158 TRP A CD2 1 
ATOM   1241 N  NE1 . TRP A 1 158 ? -22.363 -0.745  -4.878  1.00 73.76  ? 158 TRP A NE1 1 
ATOM   1242 C  CE2 . TRP A 1 158 ? -21.822 -0.791  -6.138  1.00 73.23  ? 158 TRP A CE2 1 
ATOM   1243 C  CE3 . TRP A 1 158 ? -21.144 0.764   -7.860  1.00 66.88  ? 158 TRP A CE3 1 
ATOM   1244 C  CZ2 . TRP A 1 158 ? -21.448 -1.892  -6.920  1.00 74.60  ? 158 TRP A CZ2 1 
ATOM   1245 C  CZ3 . TRP A 1 158 ? -20.772 -0.341  -8.640  1.00 74.08  ? 158 TRP A CZ3 1 
ATOM   1246 C  CH2 . TRP A 1 158 ? -20.929 -1.644  -8.165  1.00 72.56  ? 158 TRP A CH2 1 
ATOM   1247 N  N   . TYR A 1 159 ? -24.916 3.671   -4.022  1.00 56.42  ? 159 TYR A N   1 
ATOM   1248 C  CA  . TYR A 1 159 ? -26.071 3.381   -3.182  1.00 60.67  ? 159 TYR A CA  1 
ATOM   1249 C  C   . TYR A 1 159 ? -27.381 3.629   -3.916  1.00 59.53  ? 159 TYR A C   1 
ATOM   1250 O  O   . TYR A 1 159 ? -28.327 2.845   -3.798  1.00 54.85  ? 159 TYR A O   1 
ATOM   1251 C  CB  . TYR A 1 159 ? -25.995 4.251   -1.936  1.00 59.80  ? 159 TYR A CB  1 
ATOM   1252 C  CG  . TYR A 1 159 ? -27.208 4.245   -1.069  1.00 57.89  ? 159 TYR A CG  1 
ATOM   1253 C  CD1 . TYR A 1 159 ? -27.505 3.150   -0.263  1.00 63.70  ? 159 TYR A CD1 1 
ATOM   1254 C  CD2 . TYR A 1 159 ? -28.027 5.363   -0.993  1.00 60.24  ? 159 TYR A CD2 1 
ATOM   1255 C  CE1 . TYR A 1 159 ? -28.601 3.163   0.563   1.00 64.76  ? 159 TYR A CE1 1 
ATOM   1256 C  CE2 . TYR A 1 159 ? -29.117 5.385   -0.155  1.00 60.40  ? 159 TYR A CE2 1 
ATOM   1257 C  CZ  . TYR A 1 159 ? -29.402 4.287   0.609   1.00 61.64  ? 159 TYR A CZ  1 
ATOM   1258 O  OH  . TYR A 1 159 ? -30.499 4.309   1.432   1.00 68.86  ? 159 TYR A OH  1 
ATOM   1259 N  N   . ASP A 1 160 ? -27.471 4.747   -4.635  1.00 56.74  ? 160 ASP A N   1 
ATOM   1260 C  CA  . ASP A 1 160 ? -28.671 5.016   -5.417  1.00 64.86  ? 160 ASP A CA  1 
ATOM   1261 C  C   . ASP A 1 160 ? -28.922 3.905   -6.430  1.00 64.65  ? 160 ASP A C   1 
ATOM   1262 O  O   . ASP A 1 160 ? -30.070 3.505   -6.652  1.00 63.25  ? 160 ASP A O   1 
ATOM   1263 C  CB  . ASP A 1 160 ? -28.549 6.364   -6.131  1.00 65.86  ? 160 ASP A CB  1 
ATOM   1264 C  CG  . ASP A 1 160 ? -28.611 7.539   -5.174  1.00 65.11  ? 160 ASP A CG  1 
ATOM   1265 O  OD1 . ASP A 1 160 ? -29.037 7.341   -4.031  1.00 53.34  ? 160 ASP A OD1 1 
ATOM   1266 O  OD2 . ASP A 1 160 ? -28.238 8.667   -5.565  1.00 66.20  ? 160 ASP A OD2 1 
ATOM   1267 N  N   . ASN A 1 161 ? -27.855 3.399   -7.058  1.00 62.31  ? 161 ASN A N   1 
ATOM   1268 C  CA  . ASN A 1 161 ? -28.019 2.368   -8.078  1.00 67.28  ? 161 ASN A CA  1 
ATOM   1269 C  C   . ASN A 1 161 ? -28.500 1.062   -7.462  1.00 63.98  ? 161 ASN A C   1 
ATOM   1270 O  O   . ASN A 1 161 ? -29.256 0.320   -8.095  1.00 63.03  ? 161 ASN A O   1 
ATOM   1271 C  CB  . ASN A 1 161 ? -26.710 2.154   -8.840  1.00 56.06  ? 161 ASN A CB  1 
ATOM   1272 C  CG  . ASN A 1 161 ? -26.625 2.989   -10.110 1.00 72.11  ? 161 ASN A CG  1 
ATOM   1273 O  OD1 . ASN A 1 161 ? -27.532 3.762   -10.436 1.00 73.53  ? 161 ASN A OD1 1 
ATOM   1274 N  ND2 . ASN A 1 161 ? -25.527 2.832   -10.838 1.00 77.68  ? 161 ASN A ND2 1 
ATOM   1275 N  N   . LYS A 1 162 ? -28.087 0.766   -6.228  1.00 65.42  ? 162 LYS A N   1 
ATOM   1276 C  CA  . LYS A 1 162 ? -28.588 -0.443  -5.577  1.00 69.96  ? 162 LYS A CA  1 
ATOM   1277 C  C   . LYS A 1 162 ? -30.047 -0.287  -5.149  1.00 62.01  ? 162 LYS A C   1 
ATOM   1278 O  O   . LYS A 1 162 ? -30.803 -1.266  -5.175  1.00 65.64  ? 162 LYS A O   1 
ATOM   1279 C  CB  . LYS A 1 162 ? -27.711 -0.819  -4.377  1.00 69.73  ? 162 LYS A CB  1 
ATOM   1280 C  CG  . LYS A 1 162 ? -26.679 -1.936  -4.633  1.00 80.42  ? 162 LYS A CG  1 
ATOM   1281 C  CD  . LYS A 1 162 ? -27.267 -3.204  -5.310  1.00 82.09  ? 162 LYS A CD  1 
ATOM   1282 C  CE  . LYS A 1 162 ? -28.617 -3.690  -4.740  1.00 85.27  ? 162 LYS A CE  1 
ATOM   1283 N  NZ  . LYS A 1 162 ? -28.530 -4.423  -3.437  1.00 91.51  ? 162 LYS A NZ  1 
ATOM   1284 N  N   . LEU A 1 163 ? -30.458 0.921   -4.754  1.00 58.81  ? 163 LEU A N   1 
ATOM   1285 C  CA  . LEU A 1 163 ? -31.873 1.179   -4.502  1.00 63.19  ? 163 LEU A CA  1 
ATOM   1286 C  C   . LEU A 1 163 ? -32.722 0.868   -5.730  1.00 65.16  ? 163 LEU A C   1 
ATOM   1287 O  O   . LEU A 1 163 ? -33.742 0.176   -5.628  1.00 60.72  ? 163 LEU A O   1 
ATOM   1288 C  CB  . LEU A 1 163 ? -32.074 2.627   -4.082  1.00 56.87  ? 163 LEU A CB  1 
ATOM   1289 C  CG  . LEU A 1 163 ? -31.309 3.017   -2.821  1.00 70.97  ? 163 LEU A CG  1 
ATOM   1290 C  CD1 . LEU A 1 163 ? -31.722 4.411   -2.337  1.00 66.56  ? 163 LEU A CD1 1 
ATOM   1291 C  CD2 . LEU A 1 163 ? -31.476 1.967   -1.711  1.00 65.72  ? 163 LEU A CD2 1 
ATOM   1292 N  N   . THR A 1 164 ? -32.326 1.390   -6.900  1.00 63.59  ? 164 THR A N   1 
ATOM   1293 C  CA  . THR A 1 164 ? -33.056 1.090   -8.134  1.00 65.78  ? 164 THR A CA  1 
ATOM   1294 C  C   . THR A 1 164 ? -33.101 -0.411  -8.372  1.00 62.80  ? 164 THR A C   1 
ATOM   1295 O  O   . THR A 1 164 ? -34.179 -0.993  -8.551  1.00 63.51  ? 164 THR A O   1 
ATOM   1296 C  CB  . THR A 1 164 ? -32.412 1.776   -9.351  1.00 68.80  ? 164 THR A CB  1 
ATOM   1297 O  OG1 . THR A 1 164 ? -32.248 3.181   -9.129  1.00 71.10  ? 164 THR A OG1 1 
ATOM   1298 C  CG2 . THR A 1 164 ? -33.296 1.590   -10.560 1.00 65.87  ? 164 THR A CG2 1 
ATOM   1299 N  N   . SER A 1 165 ? -31.928 -1.057  -8.356  1.00 62.94  ? 165 SER A N   1 
ATOM   1300 C  CA  . SER A 1 165 ? -31.849 -2.502  -8.550  1.00 65.65  ? 165 SER A CA  1 
ATOM   1301 C  C   . SER A 1 165 ? -32.751 -3.235  -7.569  1.00 70.10  ? 165 SER A C   1 
ATOM   1302 O  O   . SER A 1 165 ? -33.534 -4.106  -7.961  1.00 68.10  ? 165 SER A O   1 
ATOM   1303 C  CB  . SER A 1 165 ? -30.399 -2.971  -8.402  1.00 70.79  ? 165 SER A CB  1 
ATOM   1304 O  OG  . SER A 1 165 ? -30.342 -4.324  -7.965  1.00 73.92  ? 165 SER A OG  1 
ATOM   1305 N  N   . LEU A 1 166 ? -32.653 -2.885  -6.283  1.00 68.88  ? 166 LEU A N   1 
ATOM   1306 C  CA  . LEU A 1 166 ? -33.538 -3.462  -5.278  1.00 70.27  ? 166 LEU A CA  1 
ATOM   1307 C  C   . LEU A 1 166 ? -35.004 -3.163  -5.585  1.00 72.25  ? 166 LEU A C   1 
ATOM   1308 O  O   . LEU A 1 166 ? -35.862 -4.045  -5.465  1.00 68.64  ? 166 LEU A O   1 
ATOM   1309 C  CB  . LEU A 1 166 ? -33.158 -2.931  -3.891  1.00 62.56  ? 166 LEU A CB  1 
ATOM   1310 C  CG  . LEU A 1 166 ? -34.084 -3.277  -2.728  1.00 67.60  ? 166 LEU A CG  1 
ATOM   1311 C  CD1 . LEU A 1 166 ? -34.417 -4.772  -2.669  1.00 69.58  ? 166 LEU A CD1 1 
ATOM   1312 C  CD2 . LEU A 1 166 ? -33.433 -2.829  -1.425  1.00 70.48  ? 166 LEU A CD2 1 
ATOM   1313 N  N   . ALA A 1 167 ? -35.317 -1.923  -5.980  1.00 68.16  ? 167 ALA A N   1 
ATOM   1314 C  CA  . ALA A 1 167 ? -36.719 -1.539  -6.160  1.00 74.08  ? 167 ALA A CA  1 
ATOM   1315 C  C   . ALA A 1 167 ? -37.388 -2.262  -7.328  1.00 78.33  ? 167 ALA A C   1 
ATOM   1316 O  O   . ALA A 1 167 ? -38.621 -2.370  -7.350  1.00 77.76  ? 167 ALA A O   1 
ATOM   1317 C  CB  . ALA A 1 167 ? -36.842 -0.027  -6.351  1.00 73.35  ? 167 ALA A CB  1 
ATOM   1318 N  N   . LEU A 1 168 ? -36.613 -2.763  -8.290  1.00 75.04  ? 168 LEU A N   1 
ATOM   1319 C  CA  . LEU A 1 168 ? -37.215 -3.528  -9.373  1.00 77.38  ? 168 LEU A CA  1 
ATOM   1320 C  C   . LEU A 1 168 ? -37.465 -4.977  -8.964  1.00 82.27  ? 168 LEU A C   1 
ATOM   1321 O  O   . LEU A 1 168 ? -38.523 -5.532  -9.280  1.00 89.33  ? 168 LEU A O   1 
ATOM   1322 C  CB  . LEU A 1 168 ? -36.337 -3.445  -10.630 1.00 75.53  ? 168 LEU A CB  1 
ATOM   1323 C  CG  . LEU A 1 168 ? -35.998 -2.028  -11.122 1.00 75.39  ? 168 LEU A CG  1 
ATOM   1324 C  CD1 . LEU A 1 168 ? -35.528 -2.026  -12.566 1.00 69.99  ? 168 LEU A CD1 1 
ATOM   1325 C  CD2 . LEU A 1 168 ? -37.170 -1.054  -10.930 1.00 80.79  ? 168 LEU A CD2 1 
ATOM   1326 N  N   . ASP A 1 169 ? -36.523 -5.600  -8.244  1.00 80.39  ? 169 ASP A N   1 
ATOM   1327 C  CA  . ASP A 1 169 ? -36.716 -6.985  -7.810  1.00 84.79  ? 169 ASP A CA  1 
ATOM   1328 C  C   . ASP A 1 169 ? -38.017 -7.143  -7.037  1.00 90.59  ? 169 ASP A C   1 
ATOM   1329 O  O   . ASP A 1 169 ? -38.712 -8.160  -7.169  1.00 96.96  ? 169 ASP A O   1 
ATOM   1330 C  CB  . ASP A 1 169 ? -35.546 -7.457  -6.937  1.00 83.30  ? 169 ASP A CB  1 
ATOM   1331 C  CG  . ASP A 1 169 ? -34.221 -7.509  -7.685  1.00 90.08  ? 169 ASP A CG  1 
ATOM   1332 O  OD1 . ASP A 1 169 ? -34.063 -8.361  -8.584  1.00 92.38  ? 169 ASP A OD1 1 
ATOM   1333 O  OD2 . ASP A 1 169 ? -33.327 -6.693  -7.365  1.00 87.12  ? 169 ASP A OD2 1 
ATOM   1334 N  N   . ILE A 1 170 ? -38.351 -6.148  -6.208  1.00 88.07  ? 170 ILE A N   1 
ATOM   1335 C  CA  . ILE A 1 170 ? -39.611 -6.168  -5.467  1.00 93.14  ? 170 ILE A CA  1 
ATOM   1336 C  C   . ILE A 1 170 ? -40.790 -6.268  -6.432  1.00 95.24  ? 170 ILE A C   1 
ATOM   1337 O  O   . ILE A 1 170 ? -41.715 -7.067  -6.229  1.00 95.99  ? 170 ILE A O   1 
ATOM   1338 C  CB  . ILE A 1 170 ? -39.711 -4.927  -4.555  1.00 84.64  ? 170 ILE A CB  1 
ATOM   1339 C  CG1 . ILE A 1 170 ? -38.869 -5.129  -3.289  1.00 84.66  ? 170 ILE A CG1 1 
ATOM   1340 C  CG2 . ILE A 1 170 ? -41.158 -4.623  -4.215  1.00 78.35  ? 170 ILE A CG2 1 
ATOM   1341 C  CD1 . ILE A 1 170 ? -38.701 -3.874  -2.443  1.00 77.35  ? 170 ILE A CD1 1 
ATOM   1342 N  N   . ALA A 1 171 ? -40.757 -5.488  -7.512  1.00 90.84  ? 171 ALA A N   1 
ATOM   1343 C  CA  . ALA A 1 171 ? -41.828 -5.480  -8.510  1.00 95.34  ? 171 ALA A CA  1 
ATOM   1344 C  C   . ALA A 1 171 ? -41.492 -6.321  -9.740  1.00 100.09 ? 171 ALA A C   1 
ATOM   1345 O  O   . ALA A 1 171 ? -41.711 -5.881  -10.872 1.00 105.20 ? 171 ALA A O   1 
ATOM   1346 C  CB  . ALA A 1 171 ? -42.152 -4.041  -8.906  1.00 90.47  ? 171 ALA A CB  1 
ATOM   1347 N  N   . GLY A 1 172 ? -40.968 -7.532  -9.549  1.00 105.01 ? 172 GLY A N   1 
ATOM   1348 C  CA  . GLY A 1 172 ? -40.525 -8.384  -10.647 1.00 107.32 ? 172 GLY A CA  1 
ATOM   1349 C  C   . GLY A 1 172 ? -41.439 -8.532  -11.854 1.00 110.69 ? 172 GLY A C   1 
ATOM   1350 O  O   . GLY A 1 172 ? -41.326 -7.781  -12.833 1.00 103.68 ? 172 GLY A O   1 
ATOM   1351 N  N   . GLY A 1 192 ? -11.913 -0.252  -22.032 1.00 98.23  ? 192 GLY A N   1 
ATOM   1352 C  CA  . GLY A 1 192 ? -13.351 -0.065  -21.934 1.00 107.44 ? 192 GLY A CA  1 
ATOM   1353 C  C   . GLY A 1 192 ? -14.034 -0.874  -20.836 1.00 113.10 ? 192 GLY A C   1 
ATOM   1354 O  O   . GLY A 1 192 ? -13.731 -0.714  -19.649 1.00 110.33 ? 192 GLY A O   1 
ATOM   1355 N  N   . LEU A 1 193 ? -14.977 -1.734  -21.235 1.00 113.19 ? 193 LEU A N   1 
ATOM   1356 C  CA  . LEU A 1 193 ? -15.652 -2.606  -20.280 1.00 109.74 ? 193 LEU A CA  1 
ATOM   1357 C  C   . LEU A 1 193 ? -14.761 -3.741  -19.804 1.00 110.88 ? 193 LEU A C   1 
ATOM   1358 O  O   . LEU A 1 193 ? -15.033 -4.328  -18.750 1.00 111.51 ? 193 LEU A O   1 
ATOM   1359 C  CB  . LEU A 1 193 ? -16.925 -3.174  -20.898 1.00 104.65 ? 193 LEU A CB  1 
ATOM   1360 C  CG  . LEU A 1 193 ? -18.155 -2.291  -20.718 1.00 105.35 ? 193 LEU A CG  1 
ATOM   1361 C  CD1 . LEU A 1 193 ? -19.067 -2.411  -21.936 1.00 105.75 ? 193 LEU A CD1 1 
ATOM   1362 C  CD2 . LEU A 1 193 ? -18.877 -2.679  -19.435 1.00 91.61  ? 193 LEU A CD2 1 
ATOM   1363 N  N   . ALA A 1 194 ? -13.719 -4.075  -20.567 1.00 117.67 ? 194 ALA A N   1 
ATOM   1364 C  CA  . ALA A 1 194 ? -12.717 -5.014  -20.078 1.00 117.73 ? 194 ALA A CA  1 
ATOM   1365 C  C   . ALA A 1 194 ? -11.889 -4.399  -18.956 1.00 116.83 ? 194 ALA A C   1 
ATOM   1366 O  O   . ALA A 1 194 ? -11.401 -5.121  -18.080 1.00 116.07 ? 194 ALA A O   1 
ATOM   1367 C  CB  . ALA A 1 194 ? -11.813 -5.466  -21.228 1.00 118.67 ? 194 ALA A CB  1 
ATOM   1368 N  N   . ARG A 1 195 ? -11.724 -3.073  -18.969 1.00 111.59 ? 195 ARG A N   1 
ATOM   1369 C  CA  . ARG A 1 195 ? -11.019 -2.376  -17.896 1.00 106.42 ? 195 ARG A CA  1 
ATOM   1370 C  C   . ARG A 1 195 ? -11.705 -2.598  -16.561 1.00 103.11 ? 195 ARG A C   1 
ATOM   1371 O  O   . ARG A 1 195 ? -11.067 -2.994  -15.578 1.00 101.54 ? 195 ARG A O   1 
ATOM   1372 C  CB  . ARG A 1 195 ? -10.935 -0.883  -18.216 1.00 107.62 ? 195 ARG A CB  1 
ATOM   1373 C  CG  . ARG A 1 195 ? -9.542  -0.394  -18.531 1.00 111.73 ? 195 ARG A CG  1 
ATOM   1374 C  CD  . ARG A 1 195 ? -8.785  0.001   -17.270 1.00 107.33 ? 195 ARG A CD  1 
ATOM   1375 N  NE  . ARG A 1 195 ? -7.464  0.502   -17.621 1.00 113.79 ? 195 ARG A NE  1 
ATOM   1376 C  CZ  . ARG A 1 195 ? -6.348  -0.212  -17.556 1.00 111.62 ? 195 ARG A CZ  1 
ATOM   1377 N  NH1 . ARG A 1 195 ? -6.321  -1.417  -17.003 1.00 106.88 ? 195 ARG A NH1 1 
ATOM   1378 N  NH2 . ARG A 1 195 ? -5.231  0.291   -18.065 1.00 115.54 ? 195 ARG A NH2 1 
ATOM   1379 N  N   . ARG A 1 196 ? -13.013 -2.344  -16.516 1.00 102.96 ? 196 ARG A N   1 
ATOM   1380 C  CA  . ARG A 1 196 ? -13.806 -2.623  -15.327 1.00 103.91 ? 196 ARG A CA  1 
ATOM   1381 C  C   . ARG A 1 196 ? -13.635 -4.066  -14.859 1.00 106.23 ? 196 ARG A C   1 
ATOM   1382 O  O   . ARG A 1 196 ? -13.713 -4.355  -13.662 1.00 103.95 ? 196 ARG A O   1 
ATOM   1383 C  CB  . ARG A 1 196 ? -15.269 -2.333  -15.636 1.00 104.83 ? 196 ARG A CB  1 
ATOM   1384 C  CG  . ARG A 1 196 ? -16.089 -1.975  -14.448 1.00 97.55  ? 196 ARG A CG  1 
ATOM   1385 C  CD  . ARG A 1 196 ? -17.540 -2.279  -14.719 1.00 102.96 ? 196 ARG A CD  1 
ATOM   1386 N  NE  . ARG A 1 196 ? -18.233 -2.369  -13.446 1.00 113.26 ? 196 ARG A NE  1 
ATOM   1387 C  CZ  . ARG A 1 196 ? -18.282 -3.463  -12.700 1.00 113.36 ? 196 ARG A CZ  1 
ATOM   1388 N  NH1 . ARG A 1 196 ? -17.796 -4.621  -13.136 1.00 111.11 ? 196 ARG A NH1 1 
ATOM   1389 N  NH2 . ARG A 1 196 ? -18.821 -3.392  -11.483 1.00 101.59 ? 196 ARG A NH2 1 
ATOM   1390 N  N   . ARG A 1 197 ? -13.386 -4.986  -15.790 1.00 103.55 ? 197 ARG A N   1 
ATOM   1391 C  CA  . ARG A 1 197 ? -13.246 -6.394  -15.423 1.00 105.08 ? 197 ARG A CA  1 
ATOM   1392 C  C   . ARG A 1 197 ? -11.913 -6.671  -14.736 1.00 104.49 ? 197 ARG A C   1 
ATOM   1393 O  O   . ARG A 1 197 ? -11.865 -7.409  -13.744 1.00 98.71  ? 197 ARG A O   1 
ATOM   1394 C  CB  . ARG A 1 197 ? -13.401 -7.293  -16.653 1.00 109.58 ? 197 ARG A CB  1 
ATOM   1395 C  CG  . ARG A 1 197 ? -14.810 -7.365  -17.190 1.00 108.06 ? 197 ARG A CG  1 
ATOM   1396 C  CD  . ARG A 1 197 ? -15.827 -7.670  -16.087 1.00 113.00 ? 197 ARG A CD  1 
ATOM   1397 N  NE  . ARG A 1 197 ? -15.649 -9.009  -15.535 1.00 114.76 ? 197 ARG A NE  1 
ATOM   1398 C  CZ  . ARG A 1 197 ? -15.230 -9.265  -14.301 1.00 113.60 ? 197 ARG A CZ  1 
ATOM   1399 N  NH1 . ARG A 1 197 ? -14.908 -8.288  -13.460 1.00 110.57 ? 197 ARG A NH1 1 
ATOM   1400 N  NH2 . ARG A 1 197 ? -15.144 -10.530 -13.893 1.00 115.95 ? 197 ARG A NH2 1 
ATOM   1401 N  N   . GLN A 1 198 ? -10.815 -6.125  -15.267 1.00 103.45 ? 198 GLN A N   1 
ATOM   1402 C  CA  . GLN A 1 198 ? -9.506  -6.286  -14.638 1.00 98.67  ? 198 GLN A CA  1 
ATOM   1403 C  C   . GLN A 1 198 ? -9.566  -5.950  -13.157 1.00 95.09  ? 198 GLN A C   1 
ATOM   1404 O  O   . GLN A 1 198 ? -9.340  -6.815  -12.302 1.00 93.26  ? 198 GLN A O   1 
ATOM   1405 C  CB  . GLN A 1 198 ? -8.460  -5.385  -15.280 1.00 96.54  ? 198 GLN A CB  1 
ATOM   1406 C  CG  . GLN A 1 198 ? -7.979  -5.821  -16.627 1.00 106.57 ? 198 GLN A CG  1 
ATOM   1407 C  CD  . GLN A 1 198 ? -7.320  -4.674  -17.348 1.00 108.57 ? 198 GLN A CD  1 
ATOM   1408 O  OE1 . GLN A 1 198 ? -6.134  -4.738  -17.705 1.00 105.52 ? 198 GLN A OE1 1 
ATOM   1409 N  NE2 . GLN A 1 198 ? -8.078  -3.597  -17.547 1.00 107.71 ? 198 GLN A NE2 1 
ATOM   1410 N  N   . TYR A 1 199 ? -9.864  -4.683  -12.859 1.00 94.47  ? 199 TYR A N   1 
ATOM   1411 C  CA  . TYR A 1 199 ? -9.967  -4.214  -11.484 1.00 94.54  ? 199 TYR A CA  1 
ATOM   1412 C  C   . TYR A 1 199 ? -10.791 -5.160  -10.620 1.00 90.95  ? 199 TYR A C   1 
ATOM   1413 O  O   . TYR A 1 199 ? -10.326 -5.635  -9.578  1.00 91.79  ? 199 TYR A O   1 
ATOM   1414 C  CB  . TYR A 1 199 ? -10.583 -2.820  -11.469 1.00 87.77  ? 199 TYR A CB  1 
ATOM   1415 C  CG  . TYR A 1 199 ? -9.739  -1.797  -12.166 1.00 86.15  ? 199 TYR A CG  1 
ATOM   1416 C  CD1 . TYR A 1 199 ? -8.461  -1.497  -11.717 1.00 86.24  ? 199 TYR A CD1 1 
ATOM   1417 C  CD2 . TYR A 1 199 ? -10.216 -1.123  -13.272 1.00 85.95  ? 199 TYR A CD2 1 
ATOM   1418 C  CE1 . TYR A 1 199 ? -7.681  -0.550  -12.352 1.00 87.51  ? 199 TYR A CE1 1 
ATOM   1419 C  CE2 . TYR A 1 199 ? -9.447  -0.170  -13.913 1.00 87.87  ? 199 TYR A CE2 1 
ATOM   1420 C  CZ  . TYR A 1 199 ? -8.181  0.113   -13.453 1.00 85.06  ? 199 TYR A CZ  1 
ATOM   1421 O  OH  . TYR A 1 199 ? -7.422  1.060   -14.104 1.00 81.78  ? 199 TYR A OH  1 
ATOM   1422 N  N   . ARG A 1 200 ? -12.017 -5.454  -11.068 1.00 91.28  ? 200 ARG A N   1 
ATOM   1423 C  CA  . ARG A 1 200 ? -12.971 -6.228  -10.278 1.00 96.81  ? 200 ARG A CA  1 
ATOM   1424 C  C   . ARG A 1 200 ? -12.371 -7.552  -9.820  1.00 97.66  ? 200 ARG A C   1 
ATOM   1425 O  O   . ARG A 1 200 ? -12.348 -7.858  -8.624  1.00 97.11  ? 200 ARG A O   1 
ATOM   1426 C  CB  . ARG A 1 200 ? -14.251 -6.457  -11.091 1.00 94.39  ? 200 ARG A CB  1 
ATOM   1427 C  CG  . ARG A 1 200 ? -15.413 -7.088  -10.313 1.00 94.28  ? 200 ARG A CG  1 
ATOM   1428 C  CD  . ARG A 1 200 ? -16.678 -7.168  -11.171 1.00 99.60  ? 200 ARG A CD  1 
ATOM   1429 N  NE  . ARG A 1 200 ? -17.843 -7.662  -10.440 1.00 102.13 ? 200 ARG A NE  1 
ATOM   1430 C  CZ  . ARG A 1 200 ? -18.982 -8.045  -11.006 1.00 107.26 ? 200 ARG A CZ  1 
ATOM   1431 N  NH1 . ARG A 1 200 ? -19.135 -8.047  -12.323 1.00 111.66 ? 200 ARG A NH1 1 
ATOM   1432 N  NH2 . ARG A 1 200 ? -19.994 -8.436  -10.231 1.00 103.43 ? 200 ARG A NH2 1 
ATOM   1433 N  N   . ASP A 1 201 ? -11.874 -8.350  -10.765 1.00 100.64 ? 201 ASP A N   1 
ATOM   1434 C  CA  . ASP A 1 201 ? -11.242 -9.609  -10.388 1.00 102.24 ? 201 ASP A CA  1 
ATOM   1435 C  C   . ASP A 1 201 ? -9.970  -9.369  -9.580  1.00 97.67  ? 201 ASP A C   1 
ATOM   1436 O  O   . ASP A 1 201 ? -9.712  -10.072 -8.599  1.00 99.36  ? 201 ASP A O   1 
ATOM   1437 C  CB  . ASP A 1 201 ? -10.942 -10.453 -11.629 1.00 101.00 ? 201 ASP A CB  1 
ATOM   1438 C  CG  . ASP A 1 201 ? -12.198 -10.788 -12.444 1.00 106.93 ? 201 ASP A CG  1 
ATOM   1439 O  OD1 . ASP A 1 201 ? -13.317 -10.732 -11.888 1.00 101.63 ? 201 ASP A OD1 1 
ATOM   1440 O  OD2 . ASP A 1 201 ? -12.042 -11.098 -13.647 1.00 110.21 ? 201 ASP A OD2 1 
ATOM   1441 N  N   . LYS A 1 202 ? -9.164  -8.377  -9.973  1.00 98.75  ? 202 LYS A N   1 
ATOM   1442 C  CA  . LYS A 1 202 ? -8.013  -7.998  -9.155  1.00 97.31  ? 202 LYS A CA  1 
ATOM   1443 C  C   . LYS A 1 202 ? -8.453  -7.602  -7.752  1.00 100.58 ? 202 LYS A C   1 
ATOM   1444 O  O   . LYS A 1 202 ? -7.784  -7.932  -6.766  1.00 101.13 ? 202 LYS A O   1 
ATOM   1445 C  CB  . LYS A 1 202 ? -7.236  -6.850  -9.811  1.00 98.56  ? 202 LYS A CB  1 
ATOM   1446 C  CG  . LYS A 1 202 ? -6.107  -7.270  -10.769 1.00 99.32  ? 202 LYS A CG  1 
ATOM   1447 C  CD  . LYS A 1 202 ? -5.375  -6.039  -11.324 1.00 98.05  ? 202 LYS A CD  1 
ATOM   1448 C  CE  . LYS A 1 202 ? -4.304  -6.411  -12.362 1.00 91.43  ? 202 LYS A CE  1 
ATOM   1449 N  NZ  . LYS A 1 202 ? -4.844  -6.568  -13.744 1.00 94.05  ? 202 LYS A NZ  1 
ATOM   1450 N  N   . ALA A 1 203 ? -9.589  -6.907  -7.645  1.00 98.93  ? 203 ALA A N   1 
ATOM   1451 C  CA  . ALA A 1 203 ? -10.165 -6.607  -6.338  1.00 100.36 ? 203 ALA A CA  1 
ATOM   1452 C  C   . ALA A 1 203 ? -10.782 -7.852  -5.718  1.00 105.68 ? 203 ALA A C   1 
ATOM   1453 O  O   . ALA A 1 203 ? -10.574 -8.138  -4.533  1.00 97.25  ? 203 ALA A O   1 
ATOM   1454 C  CB  . ALA A 1 203 ? -11.213 -5.496  -6.463  1.00 93.22  ? 203 ALA A CB  1 
ATOM   1455 N  N   . ARG A 1 204 ? -11.560 -8.599  -6.505  1.00 102.33 ? 204 ARG A N   1 
ATOM   1456 C  CA  . ARG A 1 204 ? -12.200 -9.804  -5.993  1.00 103.17 ? 204 ARG A CA  1 
ATOM   1457 C  C   . ARG A 1 204 ? -11.162 -10.809 -5.496  1.00 109.44 ? 204 ARG A C   1 
ATOM   1458 O  O   . ARG A 1 204 ? -11.444 -11.590 -4.581  1.00 109.19 ? 204 ARG A O   1 
ATOM   1459 C  CB  . ARG A 1 204 ? -13.093 -10.402 -7.086  1.00 102.74 ? 204 ARG A CB  1 
ATOM   1460 C  CG  . ARG A 1 204 ? -13.985 -11.559 -6.683  1.00 104.77 ? 204 ARG A CG  1 
ATOM   1461 C  CD  . ARG A 1 204 ? -14.769 -11.270 -5.414  1.00 108.71 ? 204 ARG A CD  1 
ATOM   1462 N  NE  . ARG A 1 204 ? -14.337 -12.144 -4.328  1.00 111.30 ? 204 ARG A NE  1 
ATOM   1463 C  CZ  . ARG A 1 204 ? -15.084 -12.495 -3.291  1.00 111.76 ? 204 ARG A CZ  1 
ATOM   1464 N  NH1 . ARG A 1 204 ? -16.328 -12.068 -3.160  1.00 109.19 ? 204 ARG A NH1 1 
ATOM   1465 N  NH2 . ARG A 1 204 ? -14.568 -13.297 -2.364  1.00 105.76 ? 204 ARG A NH2 1 
ATOM   1466 N  N   . LYS A 1 205 ? -9.946  -10.770 -6.058  1.00 116.84 ? 205 LYS A N   1 
ATOM   1467 C  CA  . LYS A 1 205 ? -8.857  -11.623 -5.579  1.00 119.29 ? 205 LYS A CA  1 
ATOM   1468 C  C   . LYS A 1 205 ? -8.587  -11.385 -4.102  1.00 118.41 ? 205 LYS A C   1 
ATOM   1469 O  O   . LYS A 1 205 ? -8.287  -12.324 -3.356  1.00 121.54 ? 205 LYS A O   1 
ATOM   1470 C  CB  . LYS A 1 205 ? -7.585  -11.373 -6.399  1.00 117.64 ? 205 LYS A CB  1 
ATOM   1471 C  CG  . LYS A 1 205 ? -7.021  -12.613 -7.081  1.00 126.71 ? 205 LYS A CG  1 
ATOM   1472 C  CD  . LYS A 1 205 ? -5.884  -12.274 -8.059  1.00 128.98 ? 205 LYS A CD  1 
ATOM   1473 C  CE  . LYS A 1 205 ? -6.378  -11.468 -9.264  1.00 119.43 ? 205 LYS A CE  1 
ATOM   1474 N  NZ  . LYS A 1 205 ? -5.311  -11.231 -10.281 1.00 115.40 ? 205 LYS A NZ  1 
ATOM   1475 N  N   . HIS A 1 206 ? -8.681  -10.132 -3.667  1.00 105.93 ? 206 HIS A N   1 
ATOM   1476 C  CA  . HIS A 1 206 ? -8.622  -9.809  -2.250  1.00 106.67 ? 206 HIS A CA  1 
ATOM   1477 C  C   . HIS A 1 206 ? -9.813  -10.421 -1.522  1.00 107.72 ? 206 HIS A C   1 
ATOM   1478 O  O   . HIS A 1 206 ? -10.926 -9.887  -1.588  1.00 106.86 ? 206 HIS A O   1 
ATOM   1479 C  CB  . HIS A 1 206 ? -8.590  -8.293  -2.051  1.00 105.11 ? 206 HIS A CB  1 
ATOM   1480 C  CG  . HIS A 1 206 ? -7.217  -7.744  -1.823  1.00 102.77 ? 206 HIS A CG  1 
ATOM   1481 N  ND1 . HIS A 1 206 ? -6.983  -6.637  -1.035  1.00 101.83 ? 206 HIS A ND1 1 
ATOM   1482 C  CD2 . HIS A 1 206 ? -6.008  -8.147  -2.277  1.00 105.29 ? 206 HIS A CD2 1 
ATOM   1483 C  CE1 . HIS A 1 206 ? -5.686  -6.387  -1.005  1.00 96.00  ? 206 HIS A CE1 1 
ATOM   1484 N  NE2 . HIS A 1 206 ? -5.075  -7.282  -1.757  1.00 99.08  ? 206 HIS A NE2 1 
ATOM   1485 N  N   . LEU A 1 207 ? -9.578  -11.532 -0.822  1.00 103.35 ? 207 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 207 ? -10.623 -12.318 -0.151  1.00 107.63 ? 207 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 207 ? -11.762 -12.658 -1.122  1.00 104.97 ? 207 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 207 ? -11.758 -13.711 -1.767  1.00 99.68  ? 207 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 207 ? -11.178 -11.589 1.094   1.00 103.04 ? 207 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 207 ? -10.431 -11.516 2.447   1.00 102.63 ? 207 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 207 ? -11.356 -10.970 3.534   1.00 99.63  ? 207 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 207 ? -9.823  -12.850 2.898   1.00 97.44  ? 207 LEU A CD2 1 
HETATM 1493 S  S   . SO4 B 2 .   ? -15.036 26.044  -14.262 1.00 96.68  ? 301 SO4 A S   1 
HETATM 1494 O  O1  . SO4 B 2 .   ? -15.765 25.393  -13.100 1.00 81.22  ? 301 SO4 A O1  1 
HETATM 1495 O  O2  . SO4 B 2 .   ? -14.071 27.086  -13.742 1.00 77.69  ? 301 SO4 A O2  1 
HETATM 1496 O  O3  . SO4 B 2 .   ? -14.237 25.207  -15.241 1.00 78.83  ? 301 SO4 A O3  1 
HETATM 1497 O  O4  . SO4 B 2 .   ? -15.467 26.799  -15.507 1.00 75.91  ? 301 SO4 A O4  1 
HETATM 1498 BR BR  . BR  C 3 .   ? -21.151 30.071  -12.645 0.79 112.81 ? 302 BR  A BR  1 
HETATM 1499 BR BR  . BR  D 3 .   ? -28.672 28.829  -9.643  0.70 103.95 ? 303 BR  A BR  1 
HETATM 1500 O  O   . HOH E 4 .   ? -31.329 6.544   1.537   1.00 52.07  ? 401 HOH A O   1 
HETATM 1501 O  O   . HOH E 4 .   ? -17.840 12.913  -21.439 1.00 55.69  ? 402 HOH A O   1 
HETATM 1502 O  O   . HOH E 4 .   ? -20.317 12.312  -7.982  1.00 51.54  ? 403 HOH A O   1 
HETATM 1503 O  O   . HOH E 4 .   ? -20.995 28.281  -19.964 1.00 39.82  ? 404 HOH A O   1 
HETATM 1504 O  O   . HOH E 4 .   ? -14.948 25.172  -4.246  1.00 47.69  ? 405 HOH A O   1 
HETATM 1505 O  O   . HOH E 4 .   ? -15.200 22.212  -11.672 1.00 56.30  ? 406 HOH A O   1 
HETATM 1506 O  O   . HOH E 4 .   ? -15.569 12.844  -39.744 1.00 98.36  ? 407 HOH A O   1 
HETATM 1507 O  O   . HOH E 4 .   ? -19.585 30.999  -5.419  1.00 75.20  ? 408 HOH A O   1 
HETATM 1508 O  O   . HOH E 4 .   ? -5.663  -8.636  -5.368  1.00 109.89 ? 409 HOH A O   1 
HETATM 1509 O  O   . HOH E 4 .   ? -17.389 28.599  -0.296  1.00 64.98  ? 410 HOH A O   1 
HETATM 1510 O  O   . HOH E 4 .   ? -27.282 11.321  -29.210 1.00 81.43  ? 411 HOH A O   1 
HETATM 1511 O  O   . HOH E 4 .   ? -24.528 18.896  -17.195 1.00 42.05  ? 412 HOH A O   1 
HETATM 1512 O  O   . HOH E 4 .   ? -26.773 23.774  -21.118 1.00 46.86  ? 413 HOH A O   1 
HETATM 1513 O  O   . HOH E 4 .   ? -14.460 10.710  -12.816 1.00 57.32  ? 414 HOH A O   1 
HETATM 1514 O  O   . HOH E 4 .   ? -4.741  -4.351  4.390   1.00 90.77  ? 415 HOH A O   1 
HETATM 1515 O  O   . HOH E 4 .   ? -17.761 26.440  -10.395 1.00 62.20  ? 416 HOH A O   1 
HETATM 1516 O  O   . HOH E 4 .   ? -33.343 14.021  -19.024 1.00 66.76  ? 417 HOH A O   1 
HETATM 1517 O  O   . HOH E 4 .   ? -14.937 11.224  -18.488 1.00 51.85  ? 418 HOH A O   1 
HETATM 1518 O  O   . HOH E 4 .   ? -32.948 28.015  -19.847 1.00 52.84  ? 419 HOH A O   1 
HETATM 1519 O  O   . HOH E 4 .   ? -31.644 23.610  -9.095  1.00 52.39  ? 420 HOH A O   1 
HETATM 1520 O  O   . HOH E 4 .   ? -32.304 31.750  -22.626 1.00 54.16  ? 421 HOH A O   1 
HETATM 1521 O  O   . HOH E 4 .   ? -20.113 27.739  -15.044 1.00 55.91  ? 422 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   . MET A 1   ? 1.2180 0.9159 0.5637 0.5707  -0.1357 0.0106  1   MET A N   
2    C CA  . MET A 1   ? 1.1246 0.9007 0.5642 0.5339  -0.1303 0.0400  1   MET A CA  
3    C C   . MET A 1   ? 1.2386 1.0503 0.6898 0.5279  -0.0908 0.0529  1   MET A C   
4    O O   . MET A 1   ? 1.2666 1.1074 0.7057 0.5687  -0.0789 0.0560  1   MET A O   
5    C CB  . MET A 1   ? 1.2279 1.0911 0.7560 0.5538  -0.1661 0.0622  1   MET A CB  
6    C CG  . MET A 1   ? 1.0818 1.0086 0.6989 0.5086  -0.1732 0.0907  1   MET A CG  
7    S SD  . MET A 1   ? 1.4458 1.3993 1.1229 0.5083  -0.2267 0.0985  1   MET A SD  
8    C CE  . MET A 1   ? 1.1683 1.0219 0.7814 0.4587  -0.2237 0.0811  1   MET A CE  
9    N N   . ILE A 2   ? 1.1499 0.9545 0.6221 0.4781  -0.0726 0.0582  2   ILE A N   
10   C CA  . ILE A 2   ? 1.1598 0.9844 0.6403 0.4669  -0.0372 0.0688  2   ILE A CA  
11   C C   . ILE A 2   ? 1.0715 0.9993 0.6229 0.4827  -0.0392 0.1039  2   ILE A C   
12   O O   . ILE A 2   ? 1.1648 1.1180 0.7079 0.5009  -0.0105 0.1126  2   ILE A O   
13   C CB  . ILE A 2   ? 1.1242 0.9191 0.6231 0.4105  -0.0305 0.0650  2   ILE A CB  
14   C CG1 . ILE A 2   ? 1.0573 0.7588 0.4905 0.4014  -0.0285 0.0246  2   ILE A CG1 
15   C CG2 . ILE A 2   ? 0.9233 0.7319 0.4353 0.3968  -0.0011 0.0766  2   ILE A CG2 
16   C CD1 . ILE A 2   ? 1.1860 0.8310 0.5420 0.4316  -0.0019 -0.0007 2   ILE A CD1 
17   N N   . THR A 3   ? 1.0401 1.0307 0.6651 0.4764  -0.0743 0.1229  3   THR A N   
18   C CA  . THR A 3   ? 1.0559 1.1573 0.7654 0.4888  -0.0818 0.1515  3   THR A CA  
19   C C   . THR A 3   ? 1.0638 1.2127 0.7748 0.5543  -0.0746 0.1435  3   THR A C   
20   O O   . THR A 3   ? 1.0369 1.2535 0.7790 0.5702  -0.0509 0.1566  3   THR A O   
21   C CB  . THR A 3   ? 0.9953 1.1507 0.7880 0.4720  -0.1270 0.1648  3   THR A CB  
22   O OG1 . THR A 3   ? 0.9254 1.0749 0.7380 0.4109  -0.1305 0.1838  3   THR A OG1 
23   C CG2 . THR A 3   ? 0.9334 1.2165 0.8293 0.5106  -0.1442 0.1740  3   THR A CG2 
24   N N   . ASP A 4   ? 1.0812 1.1929 0.7569 0.5942  -0.0957 0.1196  4   ASP A N   
25   C CA  . ASP A 4   ? 1.1522 1.3017 0.8291 0.6600  -0.0951 0.1062  4   ASP A CA  
26   C C   . ASP A 4   ? 1.1965 1.2780 0.7673 0.6732  -0.0546 0.0970  4   ASP A C   
27   O O   . ASP A 4   ? 1.1872 1.3147 0.7672 0.7209  -0.0434 0.0935  4   ASP A O   
28   C CB  . ASP A 4   ? 1.1972 1.3217 0.8670 0.6994  -0.1386 0.0829  4   ASP A CB  
29   C CG  . ASP A 4   ? 1.1977 1.4010 0.9838 0.6930  -0.1798 0.0919  4   ASP A CG  
30   O OD1 . ASP A 4   ? 1.1793 1.4864 1.0719 0.6735  -0.1757 0.1118  4   ASP A OD1 
31   O OD2 . ASP A 4   ? 1.3077 1.4683 1.0769 0.7060  -0.2173 0.0782  4   ASP A OD2 
32   N N   . LEU A 5   ? 1.2033 1.1845 0.6884 0.6323  -0.0317 0.0889  5   LEU A N   
33   C CA  . LEU A 5   ? 1.2716 1.1944 0.6697 0.6382  0.0095  0.0796  5   LEU A CA  
34   C C   . LEU A 5   ? 1.1807 1.1652 0.6211 0.6248  0.0441  0.1070  5   LEU A C   
35   O O   . LEU A 5   ? 1.1677 1.1589 0.5697 0.6564  0.0702  0.1104  5   LEU A O   
36   C CB  . LEU A 5   ? 1.2612 1.0732 0.5887 0.5997  0.0221  0.0525  5   LEU A CB  
37   C CG  . LEU A 5   ? 1.2804 1.0375 0.5589 0.5899  0.0567  0.0434  5   LEU A CG  
38   C CD1 . LEU A 5   ? 1.4301 1.1599 0.6457 0.6329  0.0506  0.0357  5   LEU A CD1 
39   C CD2 . LEU A 5   ? 1.3095 0.9943 0.6062 0.5206  0.0499  0.0279  5   LEU A CD2 
40   N N   . LEU A 6   ? 1.1228 1.1469 0.6358 0.5772  0.0418  0.1281  6   LEU A N   
41   C CA  . LEU A 6   ? 1.0756 1.1584 0.6215 0.5685  0.0715  0.1571  6   LEU A CA  
42   C C   . LEU A 6   ? 1.2035 1.4268 0.7562 0.6653  0.0919  0.1795  6   LEU A C   
43   O O   . LEU A 6   ? 1.1886 1.4663 0.7054 0.7049  0.1416  0.2066  6   LEU A O   
44   C CB  . LEU A 6   ? 0.9588 1.0663 0.5742 0.5043  0.0521  0.1795  6   LEU A CB  
45   C CG  . LEU A 6   ? 1.0453 1.0527 0.6381 0.4481  0.0434  0.1598  6   LEU A CG  
46   C CD1 . LEU A 6   ? 1.0010 1.0403 0.6555 0.3933  0.0091  0.1821  6   LEU A CD1 
47   C CD2 . LEU A 6   ? 1.0339 0.9629 0.5835 0.4313  0.0734  0.1454  6   LEU A CD2 
48   N N   . ARG A 7   ? 1.0826 1.3731 0.7052 0.7001  0.0526  0.1632  7   ARG A N   
49   C CA  . ARG A 7   ? 1.1388 1.5911 0.8430 0.7776  0.0649  0.1568  7   ARG A CA  
50   C C   . ARG A 7   ? 1.2304 1.6343 0.8660 0.8307  0.0777  0.1330  7   ARG A C   
51   O O   . ARG A 7   ? 1.2751 1.7800 0.9468 0.8761  0.1188  0.1278  7   ARG A O   
52   C CB  . ARG A 7   ? 1.1341 1.6784 0.9700 0.7878  0.0173  0.1338  7   ARG A CB  
53   C CG  . ARG A 7   ? 1.0558 1.6869 0.9806 0.7422  0.0042  0.1582  7   ARG A CG  
54   C CD  . ARG A 7   ? 1.0637 1.9112 1.1605 0.7755  0.0037  0.1376  7   ARG A CD  
55   N NE  . ARG A 7   ? 0.9962 1.9145 1.1803 0.7239  -0.0260 0.1577  7   ARG A NE  
56   C CZ  . ARG A 7   ? 0.9982 1.8157 1.1828 0.6907  -0.0868 0.1559  7   ARG A CZ  
57   N NH1 . ARG A 7   ? 1.0221 1.6791 1.1343 0.6948  -0.1186 0.1382  7   ARG A NH1 
58   N NH2 . ARG A 7   ? 0.9753 1.8611 1.2393 0.6440  -0.1135 0.1736  7   ARG A NH2 
59   N N   . ALA A 8   ? 1.2578 1.5193 0.8122 0.8162  0.0462  0.1124  8   ALA A N   
60   C CA  . ALA A 8   ? 1.3502 1.5590 0.8314 0.8631  0.0501  0.0929  8   ALA A CA  
61   C C   . ALA A 8   ? 1.3711 1.5235 0.7427 0.8619  0.0975  0.1165  8   ALA A C   
62   O O   . ALA A 8   ? 1.4527 1.6161 0.8010 0.9137  0.1119  0.1087  8   ALA A O   
63   C CB  . ALA A 8   ? 1.3988 1.4753 0.8171 0.8341  0.0111  0.0704  8   ALA A CB  
64   N N   . VAL A 9   ? 1.3860 1.4709 0.6983 0.8004  0.1223  0.1388  9   VAL A N   
65   C CA  . VAL A 9   ? 1.3603 1.3737 0.6155 0.7739  0.1577  0.1577  9   VAL A CA  
66   C C   . VAL A 9   ? 1.3877 1.5073 0.6741 0.8163  0.1926  0.2086  9   VAL A C   
67   O O   . VAL A 9   ? 1.4995 1.5867 0.7609 0.8390  0.2159  0.2285  9   VAL A O   
68   C CB  . VAL A 9   ? 1.3873 1.2956 0.6952 0.6596  0.1507  0.1294  9   VAL A CB  
69   C CG1 . VAL A 9   ? 1.4540 1.2942 0.7789 0.6150  0.1705  0.1263  9   VAL A CG1 
70   C CG2 . VAL A 9   ? 1.4226 1.2587 0.6998 0.6410  0.1197  0.0951  9   VAL A CG2 
71   N N   . ALA A 10  ? 1.3541 1.6122 0.7428 0.8181  0.1987  0.2185  10  ALA A N   
72   C CA  . ALA A 10  ? 1.3575 1.7568 0.8560 0.8000  0.2557  0.2255  10  ALA A CA  
73   C C   . ALA A 10  ? 1.3395 1.9566 1.0033 0.8033  0.2614  0.1991  10  ALA A C   
74   O O   . ALA A 10  ? 1.1946 1.8803 0.9124 0.7636  0.2574  0.2241  10  ALA A O   
75   C CB  . ALA A 10  ? 1.3135 1.6212 0.7797 0.7261  0.2629  0.2628  10  ALA A CB  
76   N N   . PRO A 11  ? 1.4704 2.2039 1.2300 0.8479  0.2664  0.1478  11  PRO A N   
77   C CA  . PRO A 11  ? 1.4682 2.4011 1.4030 0.8505  0.2566  0.1195  11  PRO A CA  
78   C C   . PRO A 11  ? 1.3789 2.4868 1.4121 0.7780  0.3163  0.1325  11  PRO A C   
79   O O   . PRO A 11  ? 1.4243 2.6884 1.5975 0.7603  0.2988  0.1238  11  PRO A O   
80   C CB  . PRO A 11  ? 1.4159 2.4318 1.4234 0.9087  0.2681  0.0592  11  PRO A CB  
81   C CG  . PRO A 11  ? 1.4744 2.3009 1.3282 0.9452  0.2549  0.0611  11  PRO A CG  
82   C CD  . PRO A 11  ? 1.4934 2.1866 1.2144 0.8952  0.2805  0.1129  11  PRO A CD  
83   N N   . ASN A 12  ? 1.2028 2.2674 1.1534 0.7160  0.3808  0.1538  12  ASN A N   
84   C CA  . ASN A 12  ? 1.1852 2.3697 1.1829 0.6089  0.4391  0.1702  12  ASN A CA  
85   C C   . ASN A 12  ? 1.1330 2.1855 1.0209 0.5336  0.4204  0.2322  12  ASN A C   
86   O O   . ASN A 12  ? 1.1471 2.2283 1.0247 0.4204  0.4559  0.2529  12  ASN A O   
87   C CB  . ASN A 12  ? 1.2855 2.4820 1.2506 0.5630  0.5193  0.1425  12  ASN A CB  
88   C CG  . ASN A 12  ? 1.4089 2.4022 1.2292 0.6077  0.5139  0.1390  12  ASN A CG  
89   O OD1 . ASN A 12  ? 1.3904 2.2429 1.1419 0.6776  0.4498  0.1544  12  ASN A OD1 
90   N ND2 . ASN A 12  ? 1.4543 2.4272 1.2268 0.5615  0.5779  0.1184  12  ASN A ND2 
91   N N   . CYS A 13  ? 1.1564 2.0416 0.9505 0.5830  0.3584  0.2598  13  CYS A N   
92   C CA  . CYS A 13  ? 1.0852 1.8202 0.7746 0.5018  0.3235  0.3118  13  CYS A CA  
93   C C   . CYS A 13  ? 0.9973 1.8466 0.8017 0.4317  0.2846  0.3277  13  CYS A C   
94   O O   . CYS A 13  ? 0.9601 1.9694 0.9139 0.4744  0.2604  0.3039  13  CYS A O   
95   C CB  . CYS A 13  ? 1.0324 1.5529 0.6301 0.5550  0.2474  0.3220  13  CYS A CB  
96   S SG  . CYS A 13  ? 1.0369 1.6086 0.7155 0.6553  0.1676  0.3158  13  CYS A SG  
97   N N   . LYS A 14  ? 0.9969 1.7582 0.7280 0.3236  0.2746  0.3664  14  LYS A N   
98   C CA  . LYS A 14  ? 0.9553 1.8030 0.7743 0.2433  0.2368  0.3849  14  LYS A CA  
99   C C   . LYS A 14  ? 0.8961 1.6784 0.7354 0.2874  0.1422  0.3962  14  LYS A C   
100  O O   . LYS A 14  ? 0.9851 1.5776 0.7146 0.3121  0.1016  0.4067  14  LYS A O   
101  C CB  . LYS A 14  ? 0.9973 1.7407 0.7097 0.1177  0.2475  0.4206  14  LYS A CB  
102  C CG  . LYS A 14  ? 0.9799 1.8165 0.7706 0.0197  0.2185  0.4411  14  LYS A CG  
103  C CD  . LYS A 14  ? 1.0201 2.0802 0.9284 -0.0331 0.2909  0.4212  14  LYS A CD  
104  C CE  . LYS A 14  ? 1.0458 2.2034 1.0407 -0.1325 0.2557  0.4405  14  LYS A CE  
105  N NZ  . LYS A 14  ? 1.0463 2.0167 0.9028 -0.2345 0.2133  0.4831  14  LYS A NZ  
106  N N   . ASP A 15  ? 0.8908 1.8307 0.8805 0.2945  0.1076  0.3849  15  ASP A N   
107  C CA  . ASP A 15  ? 0.7782 1.6784 0.7983 0.3153  0.0172  0.3974  15  ASP A CA  
108  C C   . ASP A 15  ? 0.7721 1.4768 0.7019 0.3844  -0.0164 0.3755  15  ASP A C   
109  O O   . ASP A 15  ? 0.7599 1.2528 0.6234 0.3159  -0.0439 0.3466  15  ASP A O   
110  C CB  . ASP A 15  ? 0.7664 1.5898 0.7373 0.2069  -0.0206 0.4351  15  ASP A CB  
111  C CG  . ASP A 15  ? 0.7971 1.5540 0.8044 0.2103  -0.1005 0.4231  15  ASP A CG  
112  O OD1 . ASP A 15  ? 0.7139 1.5293 0.8091 0.2696  -0.1223 0.3893  15  ASP A OD1 
113  O OD2 . ASP A 15  ? 0.8690 1.4525 0.8124 0.1388  -0.1259 0.4069  15  ASP A OD2 
114  N N   . PRO A 16  ? 0.6805 1.2840 0.9543 0.3701  0.0325  0.1804  16  PRO A N   
115  C CA  . PRO A 16  ? 0.7067 1.2681 0.9412 0.3881  0.0400  0.1794  16  PRO A CA  
116  C C   . PRO A 16  ? 0.7562 1.2987 0.9714 0.3941  0.0280  0.1900  16  PRO A C   
117  O O   . PRO A 16  ? 0.6848 1.1813 0.8622 0.4009  0.0366  0.1878  16  PRO A O   
118  C CB  . PRO A 16  ? 0.7035 1.2479 0.9191 0.4163  0.0361  0.1767  16  PRO A CB  
119  C CG  . PRO A 16  ? 0.8199 1.3979 1.0636 0.4174  0.0187  0.1813  16  PRO A CG  
120  C CD  . PRO A 16  ? 0.7540 1.3695 1.0360 0.3875  0.0223  0.1804  16  PRO A CD  
121  N N   . GLU A 17  ? 0.7053 1.2710 0.9391 0.3867  0.0084  0.1990  17  GLU A N   
122  C CA  . GLU A 17  ? 0.7979 1.3402 1.0079 0.3906  -0.0064 0.2100  17  GLU A CA  
123  C C   . GLU A 17  ? 0.6969 1.2355 0.9119 0.3527  0.0022  0.2068  17  GLU A C   
124  O O   . GLU A 17  ? 0.7193 1.1944 0.8869 0.3338  0.0035  0.2013  17  GLU A O   
125  C CB  . GLU A 17  ? 0.7245 1.2802 0.9439 0.3951  -0.0331 0.2174  17  GLU A CB  
126  C CG  . GLU A 17  ? 0.9301 1.4794 1.1425 0.4196  -0.0404 0.2136  17  GLU A CG  
127  C CD  . GLU A 17  ? 1.1253 1.6899 1.3522 0.4238  -0.0658 0.2183  17  GLU A CD  
128  O OE1 . GLU A 17  ? 1.1446 1.6738 1.3367 0.4371  -0.0848 0.2251  17  GLU A OE1 
129  O OE2 . GLU A 17  ? 1.1251 1.7322 1.3951 0.4138  -0.0669 0.2146  17  GLU A OE2 
130  N N   . GLY A 18  ? 0.7151 1.3100 0.9800 0.3355  0.0089  0.2070  18  GLY A N   
131  C CA  . GLY A 18  ? 0.5828 1.1853 0.8597 0.3060  0.0180  0.2058  18  GLY A CA  
132  C C   . GLY A 18  ? 0.6413 1.1980 0.8876 0.2933  0.0423  0.1904  18  GLY A C   
133  O O   . GLY A 18  ? 0.5723 1.0829 0.7881 0.2670  0.0477  0.1831  18  GLY A O   
134  N N   . TRP A 19  ? 0.6456 1.2158 0.9012 0.3117  0.0575  0.1847  19  TRP A N   
135  C CA  . TRP A 19  ? 0.6290 1.1539 0.8549 0.3029  0.0800  0.1688  19  TRP A CA  
136  C C   . TRP A 19  ? 0.6128 1.0543 0.7728 0.3054  0.0797  0.1617  19  TRP A C   
137  O O   . TRP A 19  ? 0.5464 0.9359 0.6730 0.2857  0.0944  0.1488  19  TRP A O   
138  C CB  . TRP A 19  ? 0.5041 1.0431 0.7419 0.3135  0.0915  0.1605  19  TRP A CB  
139  C CG  . TRP A 19  ? 0.6023 1.1617 0.8658 0.2828  0.0934  0.1531  19  TRP A CG  
140  C CD1 . TRP A 19  ? 0.5302 1.1141 0.8151 0.2773  0.0838  0.1542  19  TRP A CD1 
141  C CD2 . TRP A 19  ? 0.4543 1.0025 0.7199 0.2548  0.1052  0.1420  19  TRP A CD2 
142  N NE1 . TRP A 19  ? 0.5442 1.1299 0.8416 0.2501  0.0884  0.1456  19  TRP A NE1 
143  C CE2 . TRP A 19  ? 0.5989 1.1625 0.8847 0.2357  0.0997  0.1377  19  TRP A CE2 
144  C CE3 . TRP A 19  ? 0.4621 0.9844 0.7122 0.2438  0.1203  0.1337  19  TRP A CE3 
145  C CZ2 . TRP A 19  ? 0.5971 1.1487 0.8867 0.2083  0.1054  0.1258  19  TRP A CZ2 
146  C CZ3 . TRP A 19  ? 0.5536 1.0670 0.8104 0.2130  0.1258  0.1208  19  TRP A CZ3 
147  C CH2 . TRP A 19  ? 0.4891 1.0161 0.7649 0.1971  0.1169  0.1172  19  TRP A CH2 
148  N N   . GLY A 20  ? 0.5547 0.9819 0.6954 0.3303  0.0637  0.1694  20  GLY A N   
149  C CA  . GLY A 20  ? 0.6979 1.0436 0.7733 0.3335  0.0623  0.1638  20  GLY A CA  
150  C C   . GLY A 20  ? 0.6458 0.9432 0.6873 0.3033  0.0587  0.1618  20  GLY A C   
151  O O   . GLY A 20  ? 0.7201 0.9504 0.7138 0.2896  0.0716  0.1503  20  GLY A O   
152  N N   . GLU A 21  ? 0.6748 1.0067 0.7422 0.2914  0.0421  0.1724  21  GLU A N   
153  C CA  . GLU A 21  ? 0.7255 1.0152 0.7631 0.2621  0.0378  0.1709  21  GLU A CA  
154  C C   . GLU A 21  ? 0.6711 0.9438 0.7061 0.2318  0.0603  0.1571  21  GLU A C   
155  O O   . GLU A 21  ? 0.6987 0.9093 0.6889 0.2109  0.0660  0.1493  21  GLU A O   
156  C CB  . GLU A 21  ? 0.6928 1.0308 0.7661 0.2548  0.0163  0.1843  21  GLU A CB  
157  C CG  . GLU A 21  ? 0.9319 1.2500 0.9808 0.2730  -0.0092 0.1949  21  GLU A CG  
158  C CD  . GLU A 21  ? 1.0324 1.4245 1.1364 0.2838  -0.0304 0.2089  21  GLU A CD  
159  O OE1 . GLU A 21  ? 1.0207 1.4501 1.1587 0.2616  -0.0341 0.2128  21  GLU A OE1 
160  O OE2 . GLU A 21  ? 1.0884 1.5015 1.2024 0.3146  -0.0432 0.2155  21  GLU A OE2 
161  N N   . GLN A 22  ? 0.6150 0.9418 0.6975 0.2287  0.0733  0.1536  22  GLN A N   
162  C CA  . GLN A 22  ? 0.6551 0.9698 0.7390 0.2001  0.0932  0.1397  22  GLN A CA  
163  C C   . GLN A 22  ? 0.5654 0.8300 0.6153 0.2039  0.1147  0.1235  22  GLN A C   
164  O O   . GLN A 22  ? 0.6011 0.8183 0.6225 0.1800  0.1283  0.1101  22  GLN A O   
165  C CB  . GLN A 22  ? 0.5439 0.9345 0.6907 0.1936  0.0975  0.1422  22  GLN A CB  
166  C CG  . GLN A 22  ? 0.5266 0.9643 0.7085 0.1819  0.0792  0.1558  22  GLN A CG  
167  C CD  . GLN A 22  ? 0.6778 1.0676 0.8243 0.1573  0.0702  0.1553  22  GLN A CD  
168  O OE1 . GLN A 22  ? 0.5773 0.9331 0.7053 0.1308  0.0828  0.1432  22  GLN A OE1 
169  N NE2 . GLN A 22  ? 0.6737 1.0606 0.8106 0.1664  0.0483  0.1678  22  GLN A NE2 
170  N N   . LEU A 23  ? 0.5802 0.8547 0.6333 0.2334  0.1181  0.1238  23  LEU A N   
171  C CA  . LEU A 23  ? 0.5812 0.8110 0.6049 0.2382  0.1384  0.1081  23  LEU A CA  
172  C C   . LEU A 23  ? 0.6544 0.7976 0.6118 0.2309  0.1408  0.1012  23  LEU A C   
173  O O   . LEU A 23  ? 0.7017 0.7988 0.6326 0.2175  0.1601  0.0849  23  LEU A O   
174  C CB  . LEU A 23  ? 0.6239 0.8817 0.6631 0.2735  0.1391  0.1112  23  LEU A CB  
175  C CG  . LEU A 23  ? 0.6151 0.9453 0.7113 0.2826  0.1466  0.1116  23  LEU A CG  
176  C CD1 . LEU A 23  ? 0.5267 0.8855 0.6360 0.3203  0.1420  0.1184  23  LEU A CD1 
177  C CD2 . LEU A 23  ? 0.6095 0.9255 0.7061 0.2669  0.1700  0.0934  23  LEU A CD2 
178  N N   . THR A 24  ? 0.7048 0.8238 0.6342 0.2395  0.1215  0.1130  24  THR A N   
179  C CA  . THR A 24  ? 0.7444 0.7784 0.6064 0.2383  0.1235  0.1077  24  THR A CA  
180  C C   . THR A 24  ? 0.7894 0.7719 0.6208 0.2026  0.1368  0.0954  24  THR A C   
181  O O   . THR A 24  ? 0.7984 0.7199 0.5886 0.1971  0.1541  0.0816  24  THR A O   
182  C CB  . THR A 24  ? 0.7947 0.8142 0.6329 0.2553  0.0983  0.1230  24  THR A CB  
183  O OG1 . THR A 24  ? 0.7793 0.8485 0.6481 0.2892  0.0859  0.1333  24  THR A OG1 
184  C CG2 . THR A 24  ? 0.8620 0.7921 0.6283 0.2577  0.1016  0.1175  24  THR A CG2 
185  N N   . PRO A 25  ? 0.8341 0.8353 0.6821 0.1777  0.1301  0.0989  25  PRO A N   
186  C CA  . PRO A 25  ? 0.8522 0.8032 0.6709 0.1440  0.1448  0.0853  25  PRO A CA  
187  C C   . PRO A 25  ? 0.7569 0.7193 0.5984 0.1301  0.1688  0.0676  25  PRO A C   
188  O O   . PRO A 25  ? 0.8276 0.7339 0.6350 0.1114  0.1868  0.0516  25  PRO A O   
189  C CB  . PRO A 25  ? 0.7962 0.7736 0.6332 0.1240  0.1290  0.0950  25  PRO A CB  
190  C CG  . PRO A 25  ? 0.8048 0.8337 0.6701 0.1492  0.1044  0.1143  25  PRO A CG  
191  C CD  . PRO A 25  ? 0.7459 0.8117 0.6389 0.1771  0.1102  0.1141  25  PRO A CD  
192  N N   . ALA A 26  ? 0.7329 0.7653 0.6305 0.1391  0.1699  0.0694  26  ALA A N   
193  C CA  . ALA A 26  ? 0.7559 0.7982 0.6739 0.1290  0.1917  0.0521  26  ALA A CA  
194  C C   . ALA A 26  ? 0.7917 0.7837 0.6749 0.1424  0.2081  0.0390  26  ALA A C   
195  O O   . ALA A 26  ? 0.8137 0.7700 0.6821 0.1246  0.2279  0.0202  26  ALA A O   
196  C CB  . ALA A 26  ? 0.6289 0.7542 0.6100 0.1404  0.1887  0.0582  26  ALA A CB  
197  N N   . MET A 27  ? 0.7352 0.7233 0.6054 0.1736  0.2000  0.0482  27  MET A N   
198  C CA  . MET A 27  ? 0.8666 0.8043 0.7011 0.1878  0.2141  0.0368  27  MET A CA  
199  C C   . MET A 27  ? 0.8909 0.7427 0.6632 0.1696  0.2221  0.0278  27  MET A C   
200  O O   . MET A 27  ? 0.9453 0.7543 0.6967 0.1581  0.2429  0.0095  27  MET A O   
201  C CB  . MET A 27  ? 0.8329 0.7853 0.6662 0.2254  0.2012  0.0496  27  MET A CB  
202  C CG  . MET A 27  ? 0.7301 0.7642 0.6234 0.2443  0.1977  0.0559  27  MET A CG  
203  S SD  . MET A 27  ? 0.8221 0.8825 0.7206 0.2873  0.1804  0.0720  27  MET A SD  
204  C CE  . MET A 27  ? 0.8237 0.8307 0.6858 0.3052  0.1984  0.0567  27  MET A CE  
205  N N   . GLU A 28  ? 0.8417 0.6674 0.5843 0.1659  0.2059  0.0402  28  GLU A N   
206  C CA  . GLU A 28  ? 1.0023 0.7437 0.6815 0.1496  0.2126  0.0334  28  GLU A CA  
207  C C   . GLU A 28  ? 1.0482 0.7680 0.7257 0.1130  0.2318  0.0158  28  GLU A C   
208  O O   . GLU A 28  ? 1.1312 0.7875 0.7688 0.1007  0.2504  0.0004  28  GLU A O   
209  C CB  . GLU A 28  ? 1.0485 0.7748 0.7021 0.1517  0.1896  0.0508  28  GLU A CB  
210  C CG  . GLU A 28  ? 1.1610 0.8053 0.7445 0.1599  0.1882  0.0518  28  GLU A CG  
211  C CD  . GLU A 28  ? 1.4186 0.9911 0.9545 0.1277  0.2047  0.0386  28  GLU A CD  
212  O OE1 . GLU A 28  ? 1.3894 0.9800 0.9468 0.0991  0.2098  0.0330  28  GLU A OE1 
213  O OE2 . GLU A 28  ? 1.4384 0.9365 0.9158 0.1310  0.2129  0.0336  28  GLU A OE2 
214  N N   . LYS A 29  ? 0.9892 0.7621 0.7113 0.0954  0.2279  0.0171  29  LYS A N   
215  C CA  . LYS A 29  ? 1.0031 0.7583 0.7260 0.0608  0.2447  0.0000  29  LYS A CA  
216  C C   . LYS A 29  ? 1.0267 0.7802 0.7636 0.0588  0.2680  -0.0209 29  LYS A C   
217  O O   . LYS A 29  ? 1.0628 0.7667 0.7744 0.0366  0.2870  -0.0394 29  LYS A O   
218  C CB  . LYS A 29  ? 0.9189 0.7337 0.6877 0.0442  0.2335  0.0067  29  LYS A CB  
219  C CG  . LYS A 29  ? 0.8616 0.6627 0.6096 0.0333  0.2149  0.0210  29  LYS A CG  
220  C CD  . LYS A 29  ? 0.9206 0.7933 0.7237 0.0229  0.2024  0.0293  29  LYS A CD  
221  C CE  . LYS A 29  ? 0.9704 0.8756 0.7835 0.0392  0.1753  0.0524  29  LYS A CE  
222  N NZ  . LYS A 29  ? 0.9203 0.7803 0.6935 0.0214  0.1657  0.0569  29  LYS A NZ  
223  N N   . PHE A 30  ? 0.7183 0.7308 0.8040 -0.0164 0.0625  0.0681  30  PHE A N   
224  C CA  . PHE A 30  ? 0.7805 0.7720 0.8424 -0.0452 0.0586  0.0524  30  PHE A CA  
225  C C   . PHE A 30  ? 0.9420 0.8377 0.9337 -0.0534 0.0631  0.0450  30  PHE A C   
226  O O   . PHE A 30  ? 0.9307 0.7982 0.8951 -0.0700 0.0601  0.0309  30  PHE A O   
227  C CB  . PHE A 30  ? 0.7572 0.7854 0.8362 -0.0282 0.0567  0.0457  30  PHE A CB  
228  C CG  . PHE A 30  ? 0.6029 0.7199 0.7454 -0.0420 0.0478  0.0461  30  PHE A CG  
229  C CD1 . PHE A 30  ? 0.5324 0.6680 0.6863 -0.0837 0.0392  0.0369  30  PHE A CD1 
230  C CD2 . PHE A 30  ? 0.5452 0.7268 0.7372 -0.0138 0.0473  0.0558  30  PHE A CD2 
231  C CE1 . PHE A 30  ? 0.4623 0.6785 0.6740 -0.0966 0.0299  0.0366  30  PHE A CE1 
232  C CE2 . PHE A 30  ? 0.5245 0.7863 0.7747 -0.0273 0.0378  0.0561  30  PHE A CE2 
233  C CZ  . PHE A 30  ? 0.4611 0.7397 0.7203 -0.0687 0.0289  0.0462  30  PHE A CZ  
234  N N   . GLY A 31  ? 0.9627 0.8076 0.9251 -0.0429 0.0692  0.0539  31  GLY A N   
235  C CA  . GLY A 31  ? 1.0394 0.7926 0.9368 -0.0533 0.0724  0.0480  31  GLY A CA  
236  C C   . GLY A 31  ? 1.1407 0.8392 0.9922 -0.0261 0.0762  0.0397  31  GLY A C   
237  O O   . GLY A 31  ? 1.2091 0.8378 1.0091 -0.0406 0.0756  0.0294  31  GLY A O   
238  N N   . ILE A 32  ? 1.0914 0.8197 0.9606 0.0133  0.0800  0.0435  32  ILE A N   
239  C CA  . ILE A 32  ? 1.1304 0.8078 0.9559 0.0434  0.0849  0.0363  32  ILE A CA  
240  C C   . ILE A 32  ? 1.2143 0.8362 1.0080 0.0703  0.0917  0.0458  32  ILE A C   
241  O O   . ILE A 32  ? 1.1606 0.8062 0.9747 0.1061  0.0965  0.0556  32  ILE A O   
242  C CB  . ILE A 32  ? 1.0647 0.8000 0.9230 0.0715  0.0865  0.0353  32  ILE A CB  
243  C CG1 . ILE A 32  ? 0.9916 0.7830 0.8829 0.0419  0.0784  0.0268  32  ILE A CG1 
244  C CG2 . ILE A 32  ? 1.0353 0.7180 0.8465 0.1014  0.0921  0.0271  32  ILE A CG2 
245  C CD1 . ILE A 32  ? 0.9026 0.7768 0.8494 0.0613  0.0782  0.0318  32  ILE A CD1 
246  N N   . ARG A 33  ? 1.3474 0.8941 1.0915 0.0508  0.0913  0.0429  33  ARG A N   
247  C CA  . ARG A 33  ? 1.4106 0.9034 1.1250 0.0678  0.0961  0.0529  33  ARG A CA  
248  C C   . ARG A 33  ? 1.5905 0.9871 1.2344 0.0780  0.0980  0.0441  33  ARG A C   
249  O O   . ARG A 33  ? 1.6564 1.0111 1.2747 0.1082  0.1027  0.0503  33  ARG A O   
250  C CB  . ARG A 33  ? 1.4423 0.9355 1.1659 0.0349  0.0942  0.0620  33  ARG A CB  
251  C CG  . ARG A 33  ? 1.3863 0.9714 1.1784 0.0267  0.0918  0.0721  33  ARG A CG  
252  C CD  . ARG A 33  ? 1.4095 0.9910 1.2052 -0.0101 0.0902  0.0791  33  ARG A CD  
253  N NE  . ARG A 33  ? 1.3563 1.0259 1.2157 -0.0249 0.0861  0.0848  33  ARG A NE  
254  C CZ  . ARG A 33  ? 1.3195 1.0084 1.1941 -0.0651 0.0828  0.0852  33  ARG A CZ  
255  N NH1 . ARG A 33  ? 1.3538 0.9819 1.1869 -0.0968 0.0834  0.0809  33  ARG A NH1 
256  N NH2 . ARG A 33  ? 1.1999 0.9716 1.1338 -0.0737 0.0786  0.0899  33  ARG A NH2 
257  N N   . ASP A 34  ? 1.5143 0.8741 1.1265 0.0538  0.0935  0.0294  34  ASP A N   
258  C CA  . ASP A 34  ? 1.5811 0.8450 1.1251 0.0585  0.0934  0.0208  34  ASP A CA  
259  C C   . ASP A 34  ? 1.5379 0.7840 1.0593 0.1016  0.0972  0.0134  34  ASP A C   
260  O O   . ASP A 34  ? 1.3849 0.6904 0.9392 0.1190  0.0989  0.0111  34  ASP A O   
261  C CB  . ASP A 34  ? 1.5747 0.8023 1.0926 0.0163  0.0860  0.0073  34  ASP A CB  
262  C CG  . ASP A 34  ? 1.6633 0.8760 1.1829 -0.0242 0.0838  0.0147  34  ASP A CG  
263  O OD1 . ASP A 34  ? 1.7569 0.9105 1.2430 -0.0204 0.0867  0.0228  34  ASP A OD1 
264  O OD2 . ASP A 34  ? 1.5958 0.8570 1.1506 -0.0592 0.0795  0.0128  34  ASP A OD2 
265  N N   . ARG A 35  ? 1.5556 0.7174 1.0190 0.1183  0.0984  0.0097  35  ARG A N   
266  C CA  . ARG A 35  ? 1.5436 0.6820 0.9823 0.1639  0.1032  0.0046  35  ARG A CA  
267  C C   . ARG A 35  ? 1.5409 0.7044 0.9815 0.1695  0.1020  -0.0097 35  ARG A C   
268  O O   . ARG A 35  ? 1.4997 0.7196 0.9724 0.1983  0.1074  -0.0073 35  ARG A O   
269  C CB  . ARG A 35  ? 1.7253 0.7613 1.0957 0.1735  0.1020  -0.0001 35  ARG A CB  
270  C CG  . ARG A 35  ? 1.7611 0.7610 1.1207 0.1651  0.1025  0.0135  35  ARG A CG  
271  C CD  . ARG A 35  ? 1.7963 0.7455 1.1273 0.1188  0.0959  0.0098  35  ARG A CD  
272  N NE  . ARG A 35  ? 1.8281 0.7415 1.1467 0.1090  0.0970  0.0237  35  ARG A NE  
273  C CZ  . ARG A 35  ? 1.8271 0.7859 1.1843 0.0845  0.0981  0.0366  35  ARG A CZ  
274  N NH1 . ARG A 35  ? 1.6758 0.7195 1.0891 0.0681  0.0978  0.0375  35  ARG A NH1 
275  N NH2 . ARG A 35  ? 1.8970 0.8142 1.2350 0.0763  0.0994  0.0487  35  ARG A NH2 
276  N N   . GLU A 36  ? 1.6179 0.7387 1.0236 0.1429  0.0949  -0.0246 36  GLU A N   
277  C CA  . GLU A 36  ? 1.6084 0.7493 1.0118 0.1478  0.0930  -0.0391 36  GLU A CA  
278  C C   . GLU A 36  ? 1.4661 0.7049 0.9343 0.1355  0.0930  -0.0347 36  GLU A C   
279  O O   . GLU A 36  ? 1.4144 0.6986 0.9017 0.1592  0.0968  -0.0373 36  GLU A O   
280  C CB  . GLU A 36  ? 1.6726 0.7490 1.0285 0.1181  0.0833  -0.0562 36  GLU A CB  
281  C CG  . GLU A 36  ? 1.7518 0.7266 1.0400 0.1301  0.0814  -0.0628 36  GLU A CG  
282  C CD  . GLU A 36  ? 1.8719 0.8130 1.1196 0.1650  0.0823  -0.0775 36  GLU A CD  
283  O OE1 . GLU A 36  ? 1.8547 0.8474 1.1229 0.1757  0.0840  -0.0838 36  GLU A OE1 
284  O OE2 . GLU A 36  ? 1.9300 0.7927 1.1245 0.1823  0.0812  -0.0827 36  GLU A OE2 
285  N N   . ASP A 37  ? 1.4045 0.6766 0.9070 0.0986  0.0887  -0.0277 37  ASP A N   
286  C CA  . ASP A 37  ? 1.4188 0.7839 0.9851 0.0845  0.0872  -0.0229 37  ASP A CA  
287  C C   . ASP A 37  ? 1.3313 0.7602 0.9387 0.1238  0.0952  -0.0124 37  ASP A C   
288  O O   . ASP A 37  ? 1.2897 0.7744 0.9256 0.1313  0.0954  -0.0157 37  ASP A O   
289  C CB  . ASP A 37  ? 1.4347 0.8214 1.0306 0.0479  0.0837  -0.0132 37  ASP A CB  
290  C CG  . ASP A 37  ? 1.4440 0.9039 1.0896 0.0162  0.0773  -0.0159 37  ASP A CG  
291  O OD1 . ASP A 37  ? 1.4875 0.9454 1.1220 0.0024  0.0715  -0.0306 37  ASP A OD1 
292  O OD2 . ASP A 37  ? 1.3544 0.8734 1.0496 0.0055  0.0773  -0.0039 37  ASP A OD2 
293  N N   . ILE A 38  ? 1.3601 0.7789 0.9696 0.1503  0.1015  0.0004  38  ILE A N   
294  C CA  . ILE A 38  ? 1.3096 0.7873 0.9607 0.1881  0.1088  0.0112  38  ILE A CA  
295  C C   . ILE A 38  ? 1.2726 0.7417 0.9023 0.2226  0.1143  0.0024  38  ILE A C   
296  O O   . ILE A 38  ? 1.1836 0.7187 0.8541 0.2416  0.1183  0.0063  38  ILE A O   
297  C CB  . ILE A 38  ? 1.2879 0.7476 0.9404 0.2091  0.1132  0.0252  38  ILE A CB  
298  C CG1 . ILE A 38  ? 1.2758 0.7498 0.9512 0.1755  0.1084  0.0345  38  ILE A CG1 
299  C CG2 . ILE A 38  ? 1.1688 0.6889 0.8668 0.2486  0.1199  0.0362  38  ILE A CG2 
300  C CD1 . ILE A 38  ? 1.2601 0.7141 0.9339 0.1950  0.1120  0.0479  38  ILE A CD1 
301  N N   . ALA A 39  ? 1.3191 0.7071 0.8848 0.2311  0.1145  -0.0094 39  ALA A N   
302  C CA  . ALA A 39  ? 1.3252 0.6992 0.8653 0.2672  0.1205  -0.0180 39  ALA A CA  
303  C C   . ALA A 39  ? 1.2598 0.6769 0.8137 0.2569  0.1182  -0.0277 39  ALA A C   
304  O O   . ALA A 39  ? 1.2289 0.6894 0.8024 0.2856  0.1251  -0.0262 39  ALA A O   
305  C CB  . ALA A 39  ? 1.4574 0.7321 0.9239 0.2764  0.1193  -0.0298 39  ALA A CB  
306  N N   . ALA A 40  ? 1.2835 0.6878 0.8264 0.2161  0.1084  -0.0378 40  ALA A N   
307  C CA  . ALA A 40  ? 1.2993 0.7426 0.8541 0.2037  0.1044  -0.0478 40  ALA A CA  
308  C C   . ALA A 40  ? 1.1914 0.7334 0.8176 0.2027  0.1062  -0.0359 40  ALA A C   
309  O O   . ALA A 40  ? 1.1247 0.7106 0.7676 0.2190  0.1096  -0.0378 40  ALA A O   
310  C CB  . ALA A 40  ? 1.3461 0.7552 0.8778 0.1585  0.0923  -0.0609 40  ALA A CB  
311  N N   . PHE A 41  ? 1.1424 0.7201 0.8111 0.1834  0.1036  -0.0234 41  PHE A N   
312  C CA  . PHE A 41  ? 1.0002 0.6712 0.7389 0.1830  0.1040  -0.0116 41  PHE A CA  
313  C C   . PHE A 41  ? 1.0289 0.7357 0.7885 0.2284  0.1146  -0.0030 41  PHE A C   
314  O O   . PHE A 41  ? 0.9316 0.6939 0.7198 0.2368  0.1162  -0.0028 41  PHE A O   
315  C CB  . PHE A 41  ? 1.0274 0.7224 0.8026 0.1643  0.1009  0.0014  41  PHE A CB  
316  C CG  . PHE A 41  ? 0.9773 0.7655 0.8250 0.1685  0.1007  0.0144  41  PHE A CG  
317  C CD1 . PHE A 41  ? 0.8063 0.6541 0.6908 0.1446  0.0935  0.0109  41  PHE A CD1 
318  C CD2 . PHE A 41  ? 0.9533 0.7682 0.8325 0.1961  0.1064  0.0297  41  PHE A CD2 
319  C CE1 . PHE A 41  ? 0.7998 0.7318 0.7511 0.1481  0.0920  0.0226  41  PHE A CE1 
320  C CE2 . PHE A 41  ? 0.7963 0.6954 0.7429 0.1996  0.1047  0.0412  41  PHE A CE2 
321  C CZ  . PHE A 41  ? 0.6916 0.6491 0.6742 0.1752  0.0975  0.0378  41  PHE A CZ  
322  N N   . ILE A 42  ? 0.9999 0.6726 0.7433 0.2583  0.1219  0.0040  42  ILE A N   
323  C CA  . ILE A 42  ? 0.9742 0.6796 0.7396 0.3024  0.1324  0.0128  42  ILE A CA  
324  C C   . ILE A 42  ? 1.0326 0.7324 0.7718 0.3221  0.1378  0.0022  42  ILE A C   
325  O O   . ILE A 42  ? 0.9604 0.7211 0.7371 0.3425  0.1438  0.0085  42  ILE A O   
326  C CB  . ILE A 42  ? 1.0125 0.6699 0.7560 0.3298  0.1381  0.0193  42  ILE A CB  
327  C CG1 . ILE A 42  ? 1.0235 0.7038 0.8043 0.3155  0.1338  0.0327  42  ILE A CG1 
328  C CG2 . ILE A 42  ? 1.0098 0.6841 0.7615 0.3781  0.1496  0.0241  42  ILE A CG2 
329  C CD1 . ILE A 42  ? 0.9599 0.7340 0.8169 0.3226  0.1342  0.0468  42  ILE A CD1 
330  N N   . ALA A 43  ? 1.0837 0.7116 0.7590 0.3156  0.1354  -0.0140 43  ALA A N   
331  C CA  . ALA A 43  ? 1.1447 0.7621 0.7891 0.3351  0.1400  -0.0254 43  ALA A CA  
332  C C   . ALA A 43  ? 1.0721 0.7571 0.7528 0.3189  0.1367  -0.0266 43  ALA A C   
333  O O   . ALA A 43  ? 1.0653 0.7911 0.7618 0.3445  0.1448  -0.0239 43  ALA A O   
334  C CB  . ALA A 43  ? 1.2140 0.7418 0.7846 0.3259  0.1348  -0.0438 43  ALA A CB  
335  N N   . GLN A 44  ? 1.0420 0.7376 0.7345 0.2760  0.1248  -0.0312 44  GLN A N   
336  C CA  . GLN A 44  ? 1.0595 0.8204 0.7894 0.2574  0.1196  -0.0323 44  GLN A CA  
337  C C   . GLN A 44  ? 0.9316 0.7790 0.7310 0.2734  0.1251  -0.0144 44  GLN A C   
338  O O   . GLN A 44  ? 0.9112 0.8085 0.7330 0.2848  0.1284  -0.0127 44  GLN A O   
339  C CB  . GLN A 44  ? 0.9760 0.7341 0.7118 0.2084  0.1056  -0.0389 44  GLN A CB  
340  C CG  . GLN A 44  ? 1.0339 0.8674 0.8199 0.1862  0.0985  -0.0374 44  GLN A CG  
341  C CD  . GLN A 44  ? 1.0733 0.9040 0.8334 0.1848  0.0956  -0.0519 44  GLN A CD  
342  O OE1 . GLN A 44  ? 1.0663 0.9048 0.8156 0.2176  0.1048  -0.0514 44  GLN A OE1 
343  N NE2 . GLN A 44  ? 1.1014 0.9215 0.8516 0.1469  0.0828  -0.0649 44  GLN A NE2 
344  N N   . LEU A 45  ? 0.8754 0.7398 0.7085 0.2758  0.1261  -0.0007 45  LEU A N   
345  C CA  . LEU A 45  ? 0.8112 0.7536 0.7109 0.2936  0.1305  0.0165  45  LEU A CA  
346  C C   . LEU A 45  ? 0.8504 0.8046 0.7487 0.3385  0.1441  0.0211  45  LEU A C   
347  O O   . LEU A 45  ? 0.7582 0.7818 0.7048 0.3506  0.1476  0.0306  45  LEU A O   
348  C CB  . LEU A 45  ? 0.8257 0.7683 0.7497 0.2931  0.1293  0.0285  45  LEU A CB  
349  C CG  . LEU A 45  ? 0.7511 0.7689 0.7479 0.2991  0.1284  0.0461  45  LEU A CG  
350  C CD1 . LEU A 45  ? 0.7627 0.8207 0.7885 0.3406  0.1392  0.0562  45  LEU A CD1 
351  C CD2 . LEU A 45  ? 0.7371 0.8192 0.7826 0.2640  0.1169  0.0475  45  LEU A CD2 
352  N N   . MET A 46  ? 0.8583 0.7457 0.7024 0.3636  0.1518  0.0146  46  MET A N   
353  C CA  . MET A 46  ? 0.9205 0.8173 0.7642 0.4087  0.1657  0.0198  46  MET A CA  
354  C C   . MET A 46  ? 0.9437 0.8575 0.7735 0.4168  0.1703  0.0123  46  MET A C   
355  O O   . MET A 46  ? 0.9038 0.8640 0.7618 0.4459  0.1809  0.0213  46  MET A O   
356  C CB  . MET A 46  ? 1.0655 0.8844 0.8548 0.4336  0.1717  0.0143  46  MET A CB  
357  C CG  . MET A 46  ? 1.0985 0.9113 0.9087 0.4435  0.1722  0.0261  46  MET A CG  
358  S SD  . MET A 46  ? 1.0268 0.9269 0.9120 0.4520  0.1720  0.0454  46  MET A SD  
359  C CE  . MET A 46  ? 0.9725 0.9429 0.9247 0.4226  0.1626  0.0555  46  MET A CE  
360  N N   . VAL A 47  ? 0.9279 0.8043 0.7141 0.3922  0.1626  -0.0039 47  VAL A N   
361  C CA  . VAL A 47  ? 1.0197 0.9092 0.7885 0.4008  0.1664  -0.0118 47  VAL A CA  
362  C C   . VAL A 47  ? 0.9009 0.8706 0.7262 0.3807  0.1610  -0.0045 47  VAL A C   
363  O O   . VAL A 47  ? 0.9634 0.9770 0.8053 0.3992  0.1686  0.0000  47  VAL A O   
364  C CB  . VAL A 47  ? 1.1472 0.9612 0.8437 0.3867  0.1597  -0.0333 47  VAL A CB  
365  C CG1 . VAL A 47  ? 1.0334 0.8289 0.7278 0.3396  0.1436  -0.0407 47  VAL A CG1 
366  C CG2 . VAL A 47  ? 1.1728 1.0007 0.8496 0.3970  0.1632  -0.0418 47  VAL A CG2 
367  N N   . GLU A 48  ? 0.9022 0.8947 0.7600 0.3438  0.1481  -0.0024 48  GLU A N   
368  C CA  . GLU A 48  ? 0.8492 0.9163 0.7597 0.3237  0.1413  0.0032  48  GLU A CA  
369  C C   . GLU A 48  ? 0.8377 0.9807 0.8156 0.3461  0.1487  0.0235  48  GLU A C   
370  O O   . GLU A 48  ? 0.8114 1.0150 0.8252 0.3453  0.1483  0.0290  48  GLU A O   
371  C CB  . GLU A 48  ? 0.7956 0.8676 0.7229 0.2781  0.1252  -0.0011 48  GLU A CB  
372  C CG  . GLU A 48  ? 0.7038 0.8362 0.6667 0.2529  0.1153  -0.0027 48  GLU A CG  
373  C CD  . GLU A 48  ? 0.7997 0.9308 0.7716 0.2064  0.0990  -0.0105 48  GLU A CD  
374  O OE1 . GLU A 48  ? 0.8028 0.8694 0.7322 0.1900  0.0950  -0.0211 48  GLU A OE1 
375  O OE2 . GLU A 48  ? 0.7760 0.9710 0.7986 0.1860  0.0901  -0.0061 48  GLU A OE2 
376  N N   . SER A 49  ? 0.9788 0.7092 0.7673 0.2047  0.1189  -0.0347 49  SER A N   
377  C CA  . SER A 49  ? 0.8941 0.7488 0.7628 0.2109  0.1193  -0.0078 49  SER A CA  
378  C C   . SER A 49  ? 0.8807 0.7844 0.7138 0.2759  0.1298  0.0239  49  SER A C   
379  O O   . SER A 49  ? 0.8115 0.8170 0.7025 0.2875  0.1319  0.0491  49  SER A O   
380  C CB  . SER A 49  ? 0.8322 0.7022 0.7302 0.1932  0.1292  -0.0052 49  SER A CB  
381  O OG  . SER A 49  ? 0.9071 0.7297 0.7219 0.2398  0.1502  0.0070  49  SER A OG  
382  N N   . GLY A 50  ? 0.9715 0.8068 0.7119 0.3181  0.1362  0.0234  50  GLY A N   
383  C CA  . GLY A 50  ? 1.0308 0.9092 0.7329 0.3818  0.1473  0.0536  50  GLY A CA  
384  C C   . GLY A 50  ? 0.9975 0.9004 0.6846 0.4122  0.1665  0.0757  50  GLY A C   
385  O O   . GLY A 50  ? 0.9470 0.9461 0.6707 0.4392  0.1708  0.1052  50  GLY A O   
386  N N   . GLU A 51  ? 1.0560 0.8723 0.6913 0.4057  0.1776  0.0613  51  GLU A N   
387  C CA  . GLU A 51  ? 1.0707 0.8993 0.6918 0.4270  0.1957  0.0784  51  GLU A CA  
388  C C   . GLU A 51  ? 0.9493 0.8919 0.6776 0.3978  0.1905  0.0923  51  GLU A C   
389  O O   . GLU A 51  ? 0.9191 0.9377 0.6636 0.4302  0.2002  0.1216  51  GLU A O   
390  C CB  . GLU A 51  ? 1.1251 0.9531 0.6697 0.4995  0.2134  0.1053  51  GLU A CB  
391  C CG  . GLU A 51  ? 1.3263 1.0506 0.7703 0.5293  0.2165  0.0919  51  GLU A CG  
392  C CD  . GLU A 51  ? 1.5387 1.2419 0.8941 0.6013  0.2367  0.1151  51  GLU A CD  
393  O OE1 . GLU A 51  ? 1.5332 1.3276 0.9138 0.6354  0.2436  0.1466  51  GLU A OE1 
394  O OE2 . GLU A 51  ? 1.5301 1.1245 0.7903 0.6236  0.2456  0.1018  51  GLU A OE2 
395  N N   . LEU A 52  ? 0.8863 0.8414 0.6892 0.3356  0.1746  0.0709  52  LEU A N   
396  C CA  . LEU A 52  ? 0.7917 0.8378 0.6976 0.2962  0.1683  0.0762  52  LEU A CA  
397  C C   . LEU A 52  ? 0.7248 0.8947 0.7109 0.3008  0.1581  0.0987  52  LEU A C   
398  O O   . LEU A 52  ? 0.6821 0.9361 0.7521 0.2750  0.1544  0.1074  52  LEU A O   
399  C CB  . LEU A 52  ? 0.9070 0.9604 0.8008 0.3095  0.1859  0.0895  52  LEU A CB  
400  C CG  . LEU A 52  ? 0.9266 0.8647 0.7600 0.2918  0.1934  0.0645  52  LEU A CG  
401  C CD1 . LEU A 52  ? 1.0205 0.9640 0.8480 0.2975  0.2096  0.0750  52  LEU A CD1 
402  C CD2 . LEU A 52  ? 0.9152 0.8284 0.8028 0.2257  0.1754  0.0328  52  LEU A CD2 
403  N N   . ASN A 53  ? 0.8154 0.9999 0.7801 0.3313  0.1530  0.1081  53  ASN A N   
404  C CA  . ASN A 53  ? 0.7025 1.0037 0.7449 0.3337  0.1419  0.1291  53  ASN A CA  
405  C C   . ASN A 53  ? 0.6401 0.9657 0.7585 0.2809  0.1191  0.1100  53  ASN A C   
406  O O   . ASN A 53  ? 0.6133 1.0422 0.8177 0.2677  0.1084  0.1243  53  ASN A O   
407  C CB  . ASN A 53  ? 0.7268 1.0436 0.7123 0.3962  0.1483  0.1527  53  ASN A CB  
408  C CG  . ASN A 53  ? 0.8537 1.1808 0.7852 0.4510  0.1700  0.1797  53  ASN A CG  
409  O OD1 . ASN A 53  ? 0.7490 1.1564 0.7280 0.4466  0.1704  0.2011  53  ASN A OD1 
410  N ND2 . ASN A 53  ? 0.8746 1.1100 0.6995 0.4927  0.1840  0.1772  53  ASN A ND2 
411  N N   . ARG A 54  ? 0.6617 0.8973 0.7530 0.2495  0.1113  0.0787  54  ARG A N   
412  C CA  . ARG A 54  ? 0.5804 0.8330 0.7383 0.2006  0.0899  0.0601  54  ARG A CA  
413  C C   . ARG A 54  ? 0.5164 0.7417 0.7227 0.1391  0.0836  0.0342  54  ARG A C   
414  O O   . ARG A 54  ? 0.6285 0.7569 0.7763 0.1302  0.0911  0.0143  54  ARG A O   
415  C CB  . ARG A 54  ? 0.6856 0.8606 0.7795 0.2098  0.0834  0.0439  54  ARG A CB  
416  C CG  . ARG A 54  ? 0.7069 0.8736 0.8608 0.1501  0.0624  0.0176  54  ARG A CG  
417  C CD  . ARG A 54  ? 0.6876 0.7886 0.7871 0.1564  0.0538  0.0026  54  ARG A CD  
418  N NE  . ARG A 54  ? 0.8992 0.9843 0.9165 0.2203  0.0650  0.0206  54  ARG A NE  
419  C CZ  . ARG A 54  ? 0.9505 1.1078 0.9844 0.2506  0.0605  0.0425  54  ARG A CZ  
420  N NH1 . ARG A 54  ? 0.8443 1.0966 0.9750 0.2233  0.0445  0.0499  54  ARG A NH1 
421  N NH2 . ARG A 54  ? 0.9465 1.0804 0.8978 0.3101  0.0725  0.0576  54  ARG A NH2 
422  N N   . VAL A 55  ? 0.4160 0.7247 0.7285 0.0965  0.0697  0.0339  55  VAL A N   
423  C CA  . VAL A 55  ? 0.4789 0.7652 0.8439 0.0348  0.0615  0.0078  55  VAL A CA  
424  C C   . VAL A 55  ? 0.4100 0.7268 0.8495 -0.0108 0.0396  -0.0068 55  VAL A C   
425  O O   . VAL A 55  ? 0.3947 0.7086 0.8927 -0.0648 0.0306  -0.0269 55  VAL A O   
426  C CB  . VAL A 55  ? 0.4447 0.7966 0.8699 0.0204  0.0682  0.0186  55  VAL A CB  
427  C CG1 . VAL A 55  ? 0.5462 0.8369 0.8915 0.0510  0.0889  0.0225  55  VAL A CG1 
428  C CG2 . VAL A 55  ? 0.3377 0.8149 0.8276 0.0416  0.0659  0.0502  55  VAL A CG2 
429  N N   . VAL A 56  ? 0.4077 0.7531 0.8452 0.0102  0.0309  0.0031  56  VAL A N   
430  C CA  . VAL A 56  ? 0.3153 0.6861 0.8161 -0.0286 0.0100  -0.0094 56  VAL A CA  
431  C C   . VAL A 56  ? 0.4028 0.7132 0.8316 -0.0036 0.0063  -0.0151 56  VAL A C   
432  O O   . VAL A 56  ? 0.4178 0.7261 0.7830 0.0512  0.0163  0.0037  56  VAL A O   
433  C CB  . VAL A 56  ? 0.3485 0.8253 0.9020 -0.0321 -0.0001 0.0100  56  VAL A CB  
434  C CG1 . VAL A 56  ? 0.2917 0.7329 0.7970 -0.0752 -0.0158 -0.0029 56  VAL A CG1 
435  C CG2 . VAL A 56  ? 0.4226 0.9187 0.9430 -0.0281 0.0081  0.0094  56  VAL A CG2 
436  N N   . GLU A 57  ? 0.4488 0.7151 0.8908 -0.0438 -0.0084 -0.0403 57  GLU A N   
437  C CA  . GLU A 57  ? 0.4903 0.6870 0.8598 -0.0256 -0.0121 -0.0501 57  GLU A CA  
438  C C   . GLU A 57  ? 0.4664 0.7273 0.8321 0.0182  -0.0146 -0.0248 57  GLU A C   
439  O O   . GLU A 57  ? 0.3232 0.6892 0.7721 0.0123  -0.0234 -0.0068 57  GLU A O   
440  C CB  . GLU A 57  ? 0.4653 0.6256 0.8695 -0.0810 -0.0301 -0.0785 57  GLU A CB  
441  C CG  . GLU A 57  ? 0.5250 0.6039 0.8504 -0.0665 -0.0345 -0.0920 57  GLU A CG  
442  C CD  . GLU A 57  ? 0.5697 0.6094 0.9281 -0.1233 -0.0520 -0.1206 57  GLU A CD  
443  O OE1 . GLU A 57  ? 0.5247 0.5869 0.9566 -0.1724 -0.0586 -0.1319 57  GLU A OE1 
444  O OE2 . GLU A 57  ? 0.5931 0.5804 0.9039 -0.1186 -0.0591 -0.1316 57  GLU A OE2 
445  N N   . ASN A 58  ? 0.5210 0.7181 0.7880 0.0636  -0.0062 -0.0228 58  ASN A N   
446  C CA  . ASN A 58  ? 0.5943 0.8393 0.8487 0.1038  -0.0095 -0.0024 58  ASN A CA  
447  C C   . ASN A 58  ? 0.5080 0.7508 0.7947 0.0708  -0.0296 -0.0180 58  ASN A C   
448  O O   . ASN A 58  ? 0.5423 0.6924 0.7817 0.0512  -0.0337 -0.0444 58  ASN A O   
449  C CB  . ASN A 58  ? 0.7449 0.9199 0.8812 0.1637  0.0070  0.0039  58  ASN A CB  
450  C CG  . ASN A 58  ? 0.7554 0.9975 0.8808 0.2148  0.0082  0.0325  58  ASN A CG  
451  O OD1 . ASN A 58  ? 0.6645 0.9622 0.8385 0.2045  -0.0070 0.0370  58  ASN A OD1 
452  N ND2 . ASN A 58  ? 0.8107 1.0478 0.8712 0.2710  0.0266  0.0526  58  ASN A ND2 
453  N N   . LEU A 59  ? 0.4029 0.7474 0.7700 0.0641  -0.0425 -0.0016 59  LEU A N   
454  C CA  . LEU A 59  ? 0.5112 0.8626 0.9151 0.0330  -0.0620 -0.0140 59  LEU A CA  
455  C C   . LEU A 59  ? 0.5622 0.9749 0.9639 0.0712  -0.0670 0.0087  59  LEU A C   
456  O O   . LEU A 59  ? 0.4670 0.9299 0.9313 0.0461  -0.0844 0.0084  59  LEU A O   
457  C CB  . LEU A 59  ? 0.2940 0.7048 0.8133 -0.0282 -0.0771 -0.0222 59  LEU A CB  
458  C CG  . LEU A 59  ? 0.3893 0.7176 0.9075 -0.0798 -0.0810 -0.0556 59  LEU A CG  
459  C CD1 . LEU A 59  ? 0.4183 0.7669 0.9494 -0.1148 -0.0751 -0.0472 59  LEU A CD1 
460  C CD2 . LEU A 59  ? 0.4586 0.7410 0.9695 -0.1070 -0.0966 -0.0765 59  LEU A CD2 
461  N N   . SER A 60  ? 0.5834 0.9915 0.9127 0.1316  -0.0520 0.0283  60  SER A N   
462  C CA  . SER A 60  ? 0.6451 1.0947 0.9526 0.1735  -0.0547 0.0480  60  SER A CA  
463  C C   . SER A 60  ? 0.7217 1.0657 0.9210 0.1974  -0.0510 0.0312  60  SER A C   
464  O O   . SER A 60  ? 0.8229 1.0937 0.9309 0.2329  -0.0339 0.0290  60  SER A O   
465  C CB  . SER A 60  ? 0.5596 1.0789 0.8589 0.2268  -0.0407 0.0823  60  SER A CB  
466  O OG  . SER A 60  ? 0.7020 1.2544 0.9715 0.2701  -0.0422 0.1008  60  SER A OG  
467  N N   . TYR A 61  ? 0.7679 1.1053 0.9772 0.1789  -0.0668 0.0201  61  TYR A N   
468  C CA  . TYR A 61  ? 0.9243 1.1625 1.0378 0.1946  -0.0659 0.0015  61  TYR A CA  
469  C C   . TYR A 61  ? 0.9723 1.2567 1.0802 0.2225  -0.0743 0.0160  61  TYR A C   
470  O O   . TYR A 61  ? 0.8654 1.2433 1.0609 0.2033  -0.0889 0.0284  61  TYR A O   
471  C CB  . TYR A 61  ? 0.8873 1.0512 1.0090 0.1371  -0.0782 -0.0332 61  TYR A CB  
472  C CG  . TYR A 61  ? 0.9153 1.0012 1.0115 0.1144  -0.0686 -0.0530 61  TYR A CG  
473  C CD1 . TYR A 61  ? 0.7876 0.9219 0.9630 0.0811  -0.0688 -0.0506 61  TYR A CD1 
474  C CD2 . TYR A 61  ? 1.0354 0.9987 1.0281 0.1257  -0.0596 -0.0743 61  TYR A CD2 
475  C CE1 . TYR A 61  ? 0.7523 0.8166 0.9047 0.0600  -0.0599 -0.0684 61  TYR A CE1 
476  C CE2 . TYR A 61  ? 1.0288 0.9199 0.9980 0.1043  -0.0510 -0.0921 61  TYR A CE2 
477  C CZ  . TYR A 61  ? 0.9143 0.8577 0.9642 0.0715  -0.0512 -0.0888 61  TYR A CZ  
478  O OH  . TYR A 61  ? 0.7753 0.6504 0.8037 0.0500  -0.0427 -0.1059 61  TYR A OH  
479  N N   . SER A 62  ? 1.0140 1.2308 1.0181 0.2671  -0.0652 0.0136  62  SER A N   
480  C CA  . SER A 62  ? 1.0748 1.3185 1.0633 0.2899  -0.0739 0.0219  62  SER A CA  
481  C C   . SER A 62  ? 1.0591 1.2852 1.0865 0.2374  -0.0947 -0.0012 62  SER A C   
482  O O   . SER A 62  ? 1.0567 1.2271 1.0997 0.1891  -0.1001 -0.0268 62  SER A O   
483  C CB  . SER A 62  ? 1.0956 1.2578 0.9593 0.3454  -0.0596 0.0198  62  SER A CB  
484  O OG  . SER A 62  ? 1.1625 1.3093 1.0006 0.3480  -0.0712 0.0120  62  SER A OG  
485  N N   . THR A 63  ? 1.2563 1.2473 1.0368 0.0546  -0.0166 -0.0234 63  THR A N   
486  C CA  . THR A 63  ? 1.2139 1.1661 0.9837 0.0146  -0.0712 -0.0603 63  THR A CA  
487  C C   . THR A 63  ? 1.3004 1.1786 1.0789 0.0095  -0.0462 -0.1000 63  THR A C   
488  O O   . THR A 63  ? 1.2863 1.1340 1.1014 -0.0129 -0.0774 -0.1250 63  THR A O   
489  C CB  . THR A 63  ? 1.2072 1.1627 0.8926 -0.0112 -0.1094 -0.0695 63  THR A CB  
490  O OG1 . THR A 63  ? 1.2352 1.2600 0.9131 -0.0073 -0.1341 -0.0324 63  THR A OG1 
491  C CG2 . THR A 63  ? 1.2692 1.1859 0.9457 -0.0531 -0.1670 -0.1066 63  THR A CG2 
492  N N   . LYS A 64  ? 1.4232 1.2720 1.1689 0.0305  0.0108  -0.1057 64  LYS A N   
493  C CA  . LYS A 64  ? 1.4506 1.2301 1.2076 0.0299  0.0421  -0.1408 64  LYS A CA  
494  C C   . LYS A 64  ? 1.3755 1.1548 1.2222 0.0511  0.0691  -0.1315 64  LYS A C   
495  O O   . LYS A 64  ? 1.4171 1.1479 1.2976 0.0382  0.0650  -0.1614 64  LYS A O   
496  C CB  . LYS A 64  ? 1.5500 1.3009 1.2472 0.0481  0.0975  -0.1472 64  LYS A CB  
497  C CG  . LYS A 64  ? 1.6166 1.3487 1.2219 0.0225  0.0733  -0.1679 64  LYS A CG  
498  C CD  . LYS A 64  ? 1.6779 1.4244 1.2251 0.0475  0.1202  -0.1501 64  LYS A CD  
499  C CE  . LYS A 64  ? 1.6376 1.3419 1.1938 0.0761  0.1918  -0.1586 64  LYS A CE  
500  N NZ  . LYS A 64  ? 1.6074 1.3434 1.2353 0.1142  0.2347  -0.1255 64  LYS A NZ  
501  N N   . ARG A 65  ? 1.3467 1.1804 1.2327 0.0829  0.0962  -0.0901 65  ARG A N   
502  C CA  . ARG A 65  ? 1.3146 1.1503 1.2844 0.1059  0.1273  -0.0785 65  ARG A CA  
503  C C   . ARG A 65  ? 1.2437 1.0762 1.2742 0.0822  0.0784  -0.0909 65  ARG A C   
504  O O   . ARG A 65  ? 1.2097 1.0016 1.2890 0.0820  0.0919  -0.1113 65  ARG A O   
505  C CB  . ARG A 65  ? 1.2771 1.1790 1.2735 0.1409  0.1577  -0.0293 65  ARG A CB  
506  C CG  . ARG A 65  ? 1.3046 1.2024 1.3692 0.1736  0.2120  -0.0159 65  ARG A CG  
507  C CD  . ARG A 65  ? 1.4796 1.3465 1.5103 0.2001  0.2782  -0.0187 65  ARG A CD  
508  N NE  . ARG A 65  ? 1.5740 1.4310 1.6692 0.2304  0.3310  -0.0088 65  ARG A NE  
509  C CZ  . ARG A 65  ? 1.5538 1.4623 1.6906 0.2624  0.3621  0.0325  65  ARG A CZ  
510  N NH1 . ARG A 65  ? 1.5041 1.4792 1.6272 0.2688  0.3463  0.0685  65  ARG A NH1 
511  N NH2 . ARG A 65  ? 1.4508 1.3442 1.6444 0.2881  0.4100  0.0382  65  ARG A NH2 
512  N N   . LEU A 66  ? 1.2091 1.0847 1.2378 0.0621  0.0213  -0.0785 66  LEU A N   
513  C CA  . LEU A 66  ? 1.1240 0.9998 1.2074 0.0378  -0.0296 -0.0895 66  LEU A CA  
514  C C   . LEU A 66  ? 1.1993 1.0043 1.2766 0.0098  -0.0465 -0.1375 66  LEU A C   
515  O O   . LEU A 66  ? 1.1592 0.9434 1.2994 0.0034  -0.0550 -0.1512 66  LEU A O   
516  C CB  . LEU A 66  ? 1.0421 0.9672 1.1049 0.0163  -0.0904 -0.0742 66  LEU A CB  
517  C CG  . LEU A 66  ? 0.9834 0.9839 1.0708 0.0385  -0.0869 -0.0263 66  LEU A CG  
518  C CD1 . LEU A 66  ? 0.9170 0.9582 0.9674 0.0152  -0.1452 -0.0155 66  LEU A CD1 
519  C CD2 . LEU A 66  ? 0.7934 0.8124 0.9733 0.0501  -0.0831 -0.0121 66  LEU A CD2 
520  N N   . ARG A 67  ? 1.2133 0.9812 1.2145 -0.0079 -0.0521 -0.1637 67  ARG A N   
521  C CA  . ARG A 67  ? 1.2879 0.9882 1.2761 -0.0365 -0.0690 -0.2099 67  ARG A CA  
522  C C   . ARG A 67  ? 1.2477 0.9020 1.2863 -0.0201 -0.0219 -0.2258 67  ARG A C   
523  O O   . ARG A 67  ? 1.2285 0.8424 1.2994 -0.0406 -0.0423 -0.2551 67  ARG A O   
524  C CB  . ARG A 67  ? 1.3313 0.9995 1.2262 -0.0518 -0.0689 -0.2322 67  ARG A CB  
525  C CG  . ARG A 67  ? 1.4063 1.0662 1.2636 -0.0943 -0.1371 -0.2545 67  ARG A CG  
526  C CD  . ARG A 67  ? 1.4605 1.1534 1.2415 -0.1022 -0.1584 -0.2408 67  ARG A CD  
527  N NE  . ARG A 67  ? 1.6091 1.2550 1.3083 -0.1200 -0.1548 -0.2715 67  ARG A NE  
528  C CZ  . ARG A 67  ? 1.6541 1.2448 1.3319 -0.1527 -0.1816 -0.3126 67  ARG A CZ  
529  N NH1 . ARG A 67  ? 1.5978 1.1650 1.3327 -0.1692 -0.2067 -0.3316 67  ARG A NH1 
530  N NH2 . ARG A 67  ? 1.6513 1.2094 1.2482 -0.1697 -0.1826 -0.3356 67  ARG A NH2 
531  N N   . GLU A 68  ? 1.2549 0.9161 1.3027 0.0171  0.0410  -0.2056 68  GLU A N   
532  C CA  . GLU A 68  ? 1.2235 0.8428 1.3190 0.0356  0.0899  -0.2179 68  GLU A CA  
533  C C   . GLU A 68  ? 1.2362 0.8823 1.4247 0.0459  0.0850  -0.2002 68  GLU A C   
534  O O   . GLU A 68  ? 1.2286 0.8353 1.4631 0.0357  0.0813  -0.2246 68  GLU A O   
535  C CB  . GLU A 68  ? 1.3298 0.9480 1.4012 0.0721  0.1592  -0.2014 68  GLU A CB  
536  C CG  . GLU A 68  ? 1.4100 1.0199 1.3889 0.0671  0.1650  -0.2077 68  GLU A CG  
537  C CD  . GLU A 68  ? 1.4503 1.0592 1.4086 0.1044  0.2353  -0.1909 68  GLU A CD  
538  O OE1 . GLU A 68  ? 1.3951 1.0400 1.4046 0.1370  0.2702  -0.1578 68  GLU A OE1 
539  O OE2 . GLU A 68  ? 1.4685 1.0402 1.3598 0.1010  0.2561  -0.2108 68  GLU A OE2 
540  N N   . VAL A 69  ? 1.1658 0.8791 1.3828 0.0658  0.0855  -0.1580 69  VAL A N   
541  C CA  . VAL A 69  ? 1.0744 0.8159 1.3795 0.0808  0.0905  -0.1373 69  VAL A CA  
542  C C   . VAL A 69  ? 1.0832 0.8174 1.4296 0.0487  0.0315  -0.1564 69  VAL A C   
543  O O   . VAL A 69  ? 1.0562 0.7698 1.4682 0.0500  0.0378  -0.1663 69  VAL A O   
544  C CB  . VAL A 69  ? 1.0572 0.8745 1.3767 0.1058  0.0991  -0.0881 69  VAL A CB  
545  C CG1 . VAL A 69  ? 1.0111 0.8508 1.4169 0.1307  0.1268  -0.0653 69  VAL A CG1 
546  C CG2 . VAL A 69  ? 1.1019 0.9303 1.3595 0.1290  0.1423  -0.0714 69  VAL A CG2 
547  N N   . TRP A 70  ? 1.1175 0.8685 1.4267 0.0195  -0.0266 -0.1614 70  TRP A N   
548  C CA  . TRP A 70  ? 1.0684 0.8154 1.4112 -0.0130 -0.0874 -0.1788 70  TRP A CA  
549  C C   . TRP A 70  ? 1.1056 0.8126 1.3816 -0.0490 -0.1271 -0.2144 70  TRP A C   
550  O O   . TRP A 70  ? 1.1058 0.8417 1.3434 -0.0687 -0.1737 -0.2084 70  TRP A O   
551  C CB  . TRP A 70  ? 1.0012 0.8181 1.3758 -0.0135 -0.1252 -0.1444 70  TRP A CB  
552  C CG  . TRP A 70  ? 0.9663 0.8242 1.4111 0.0186  -0.0916 -0.1098 70  TRP A CG  
553  C CD1 . TRP A 70  ? 0.9262 0.7760 1.4511 0.0238  -0.0847 -0.1122 70  TRP A CD1 
554  C CD2 . TRP A 70  ? 0.8986 0.8133 1.3397 0.0488  -0.0616 -0.0672 70  TRP A CD2 
555  N NE1 . TRP A 70  ? 0.8002 0.6974 1.3709 0.0553  -0.0517 -0.0741 70  TRP A NE1 
556  C CE2 . TRP A 70  ? 0.8177 0.7557 1.3386 0.0710  -0.0372 -0.0457 70  TRP A CE2 
557  C CE3 . TRP A 70  ? 0.8620 0.8102 1.2401 0.0589  -0.0530 -0.0452 70  TRP A CE3 
558  C CZ2 . TRP A 70  ? 0.7141 0.7079 1.2530 0.1023  -0.0050 -0.0029 70  TRP A CZ2 
559  C CZ3 . TRP A 70  ? 0.7785 0.7822 1.1752 0.0904  -0.0207 -0.0026 70  TRP A CZ3 
560  C CH2 . TRP A 70  ? 0.6807 0.7067 1.1571 0.1116  0.0028  0.0181  70  TRP A CH2 
561  N N   . PRO A 71  ? 1.2025 0.8426 1.4624 -0.0592 -0.1101 -0.2520 71  PRO A N   
562  C CA  . PRO A 71  ? 1.2048 0.8052 1.3980 -0.0940 -0.1459 -0.2866 71  PRO A CA  
563  C C   . PRO A 71  ? 1.2439 0.8426 1.4601 -0.1310 -0.2146 -0.3041 71  PRO A C   
564  O O   . PRO A 71  ? 1.2455 0.8369 1.4050 -0.1601 -0.2573 -0.3197 71  PRO A O   
565  C CB  . PRO A 71  ? 1.2879 0.8179 1.4669 -0.0906 -0.1013 -0.3198 71  PRO A CB  
566  C CG  . PRO A 71  ? 1.2881 0.8146 1.5501 -0.0677 -0.0671 -0.3120 71  PRO A CG  
567  C CD  . PRO A 71  ? 1.1905 0.7876 1.4923 -0.0403 -0.0582 -0.2651 71  PRO A CD  
568  N N   . LYS A 72  ? 1.2532 0.8587 1.5504 -0.1310 -0.2267 -0.3017 72  LYS A N   
569  C CA  . LYS A 72  ? 1.2455 0.8536 1.5693 -0.1650 -0.2926 -0.3157 72  LYS A CA  
570  C C   . LYS A 72  ? 1.1816 0.8524 1.4920 -0.1730 -0.3390 -0.2875 72  LYS A C   
571  O O   . LYS A 72  ? 1.1833 0.8768 1.4434 -0.1925 -0.3649 -0.2802 72  LYS A O   
572  C CB  . LYS A 72  ? 1.2981 0.9144 1.6994 -0.1551 -0.2802 -0.3068 72  LYS A CB  
573  C CG  . LYS A 72  ? 1.2588 0.8174 1.6730 -0.1503 -0.2391 -0.3322 72  LYS A CG  
574  C CD  . LYS A 72  ? 1.2533 0.7957 1.6254 -0.1763 -0.2558 -0.3449 72  LYS A CD  
575  C CE  . LYS A 72  ? 1.2951 0.7990 1.6951 -0.1684 -0.2200 -0.3580 72  LYS A CE  
576  N NZ  . LYS A 72  ? 1.2920 0.7422 1.6333 -0.1921 -0.2181 -0.3870 72  LYS A NZ  
577  N N   . ARG A 73  ? 1.1425 0.8691 1.4712 -0.1439 -0.3164 -0.2471 73  ARG A N   
578  C CA  . ARG A 73  ? 1.1023 0.8899 1.4193 -0.1499 -0.3577 -0.2186 73  ARG A CA  
579  C C   . ARG A 73  ? 1.0863 0.8848 1.3135 -0.1530 -0.3599 -0.2131 73  ARG A C   
580  O O   . ARG A 73  ? 0.9997 0.8354 1.2019 -0.1691 -0.4061 -0.2004 73  ARG A O   
581  C CB  . ARG A 73  ? 0.9521 0.7972 1.3273 -0.1189 -0.3346 -0.1770 73  ARG A CB  
582  C CG  . ARG A 73  ? 0.9768 0.8204 1.4441 -0.1162 -0.3371 -0.1780 73  ARG A CG  
583  C CD  . ARG A 73  ? 0.9687 0.8500 1.4854 -0.0774 -0.2873 -0.1425 73  ARG A CD  
584  N NE  . ARG A 73  ? 0.9019 0.7663 1.5002 -0.0699 -0.2716 -0.1491 73  ARG A NE  
585  C CZ  . ARG A 73  ? 1.0192 0.8261 1.6302 -0.0677 -0.2406 -0.1772 73  ARG A CZ  
586  N NH1 . ARG A 73  ? 1.0033 0.7614 1.5517 -0.0741 -0.2235 -0.2036 73  ARG A NH1 
587  N NH2 . ARG A 73  ? 1.0456 0.8433 1.7336 -0.0594 -0.2263 -0.1793 73  ARG A NH2 
588  N N   . PHE A 74  ? 1.1572 0.9235 1.3354 -0.1384 -0.3112 -0.2226 74  PHE A N   
589  C CA  . PHE A 74  ? 1.1407 0.9135 1.2321 -0.1395 -0.3067 -0.2187 74  PHE A CA  
590  C C   . PHE A 74  ? 1.2179 0.9224 1.2535 -0.1582 -0.2993 -0.2605 74  PHE A C   
591  O O   . PHE A 74  ? 1.2368 0.9099 1.2506 -0.1384 -0.2440 -0.2678 74  PHE A O   
592  C CB  . PHE A 74  ? 1.0500 0.8558 1.1314 -0.1000 -0.2495 -0.1851 74  PHE A CB  
593  C CG  . PHE A 74  ? 1.0181 0.8905 1.1525 -0.0805 -0.2524 -0.1435 74  PHE A CG  
594  C CD1 . PHE A 74  ? 0.9583 0.8835 1.0723 -0.0911 -0.2959 -0.1209 74  PHE A CD1 
595  C CD2 . PHE A 74  ? 1.0318 0.9144 1.2355 -0.0514 -0.2107 -0.1264 74  PHE A CD2 
596  C CE1 . PHE A 74  ? 0.8333 0.8198 0.9949 -0.0735 -0.2975 -0.0825 74  PHE A CE1 
597  C CE2 . PHE A 74  ? 0.9058 0.8505 1.1572 -0.0338 -0.2125 -0.0877 74  PHE A CE2 
598  C CZ  . PHE A 74  ? 0.7807 0.7770 1.0106 -0.0452 -0.2559 -0.0660 74  PHE A CZ  
599  N N   . PRO A 75  ? 1.2823 0.9624 1.2940 -0.1963 -0.3531 -0.2883 75  PRO A N   
600  C CA  . PRO A 75  ? 1.3567 0.9731 1.3091 -0.2163 -0.3479 -0.3281 75  PRO A CA  
601  C C   . PRO A 75  ? 1.4825 1.1024 1.3491 -0.2087 -0.3249 -0.3223 75  PRO A C   
602  O O   . PRO A 75  ? 1.4989 1.0859 1.3407 -0.1900 -0.2699 -0.3310 75  PRO A O   
603  C CB  . PRO A 75  ? 1.2855 0.9027 1.2339 -0.2543 -0.4042 -0.3436 75  PRO A CB  
604  C CG  . PRO A 75  ? 1.3003 0.9809 1.3214 -0.2436 -0.4106 -0.3077 75  PRO A CG  
605  C CD  . PRO A 75  ? 1.1862 0.8960 1.2269 -0.2218 -0.4164 -0.2839 75  PRO A CD  
606  N N   . ASP A 76  ? 1.5328 1.1933 1.3552 -0.2216 -0.3644 -0.3064 76  ASP A N   
607  C CA  . ASP A 76  ? 1.6527 1.3124 1.3862 -0.2231 -0.3544 -0.3066 76  ASP A CA  
608  C C   . ASP A 76  ? 1.5773 1.3038 1.3000 -0.1978 -0.3426 -0.2624 76  ASP A C   
609  O O   . ASP A 76  ? 1.4571 1.2307 1.2400 -0.1801 -0.3434 -0.2318 76  ASP A O   
610  C CB  . ASP A 76  ? 1.6858 1.3267 1.3624 -0.2660 -0.4138 -0.3325 76  ASP A CB  
611  C CG  . ASP A 76  ? 1.6554 1.3792 1.3619 -0.2685 -0.4452 -0.2984 76  ASP A CG  
612  O OD1 . ASP A 76  ? 1.5781 1.3414 1.3568 -0.2561 -0.4481 -0.2744 76  ASP A OD1 
613  O OD2 . ASP A 76  ? 1.6290 1.3875 1.2976 -0.2743 -0.4497 -0.2918 76  ASP A OD2 
614  N N   . ASP A 77  ? 1.3982 2.0046 1.2245 -0.1460 -0.0983 -0.4971 77  ASP A N   
615  C CA  . ASP A 77  ? 1.3233 1.9584 1.1490 -0.1594 -0.0662 -0.4809 77  ASP A CA  
616  C C   . ASP A 77  ? 1.2170 1.8271 0.9998 -0.1884 -0.0601 -0.4057 77  ASP A C   
617  O O   . ASP A 77  ? 1.1976 1.7865 1.0022 -0.1947 -0.0434 -0.3753 77  ASP A O   
618  C CB  . ASP A 77  ? 1.3967 2.1290 1.1885 -0.1659 -0.0419 -0.5254 77  ASP A CB  
619  C CG  . ASP A 77  ? 1.3913 2.1519 1.2294 -0.1368 -0.0440 -0.6013 77  ASP A CG  
620  O OD1 . ASP A 77  ? 1.3993 2.2340 1.2203 -0.1377 -0.0245 -0.6373 77  ASP A OD1 
621  O OD2 . ASP A 77  ? 1.4356 2.1397 1.3310 -0.1119 -0.0649 -0.6195 77  ASP A OD2 
622  N N   . ARG A 78  ? 1.2136 1.8262 0.9348 -0.2064 -0.0733 -0.3750 78  ARG A N   
623  C CA  . ARG A 78  ? 1.1486 1.7348 0.8271 -0.2338 -0.0693 -0.3026 78  ARG A CA  
624  C C   . ARG A 78  ? 1.1419 1.6399 0.8717 -0.2269 -0.0796 -0.2603 78  ARG A C   
625  O O   . ARG A 78  ? 1.0576 1.5367 0.7756 -0.2452 -0.0659 -0.2083 78  ARG A O   
626  C CB  . ARG A 78  ? 1.0732 1.6632 0.6853 -0.2494 -0.0884 -0.2788 78  ARG A CB  
627  N N   . THR A 79  ? 1.0646 1.5083 0.8514 -0.2007 -0.1034 -0.2822 79  THR A N   
628  C CA  . THR A 79  ? 1.0940 1.4532 0.9358 -0.1913 -0.1143 -0.2482 79  THR A CA  
629  C C   . THR A 79  ? 0.9894 1.3455 0.8936 -0.1773 -0.0944 -0.2699 79  THR A C   
630  O O   . THR A 79  ? 0.9936 1.3200 0.9114 -0.1871 -0.0812 -0.2274 79  THR A O   
631  C CB  . THR A 79  ? 1.0718 1.3741 0.9464 -0.1700 -0.1489 -0.2625 79  THR A CB  
632  O OG1 . THR A 79  ? 1.1089 1.4176 0.9237 -0.1832 -0.1669 -0.2438 79  THR A OG1 
633  C CG2 . THR A 79  ? 0.9503 1.1642 0.8762 -0.1628 -0.1613 -0.2227 79  THR A CG2 
634  N N   . ALA A 80  ? 0.9974 1.3847 0.9393 -0.1544 -0.0919 -0.3360 80  ALA A N   
635  C CA  . ALA A 80  ? 0.8500 1.2279 0.8570 -0.1377 -0.0766 -0.3601 80  ALA A CA  
636  C C   . ALA A 80  ? 0.9008 1.3281 0.8889 -0.1556 -0.0414 -0.3470 80  ALA A C   
637  O O   . ALA A 80  ? 0.9118 1.3218 0.9502 -0.1465 -0.0274 -0.3500 80  ALA A O   
638  C CB  . ALA A 80  ? 0.8992 1.3033 0.9462 -0.1095 -0.0823 -0.4358 80  ALA A CB  
639  N N   . MET A 81  ? 0.8454 1.3330 0.7623 -0.1811 -0.0270 -0.3317 81  MET A N   
640  C CA  . MET A 81  ? 0.9142 1.4521 0.8112 -0.1989 0.0071  -0.3208 81  MET A CA  
641  C C   . MET A 81  ? 0.7908 1.2790 0.6875 -0.2165 0.0151  -0.2515 81  MET A C   
642  O O   . MET A 81  ? 0.7685 1.2695 0.6844 -0.2208 0.0400  -0.2453 81  MET A O   
643  C CB  . MET A 81  ? 0.9329 1.5518 0.7523 -0.2215 0.0201  -0.3268 81  MET A CB  
644  C CG  . MET A 81  ? 1.0139 1.6141 0.7682 -0.2467 0.0080  -0.2685 81  MET A CG  
645  S SD  . MET A 81  ? 1.0878 1.7289 0.7791 -0.2844 0.0394  -0.2157 81  MET A SD  
646  C CE  . MET A 81  ? 1.0190 1.7695 0.6491 -0.2948 0.0549  -0.2654 81  MET A CE  
647  N N   . ARG A 82  ? 0.8098 1.2430 0.6832 -0.2273 -0.0055 -0.1991 82  ARG A N   
648  C CA  . ARG A 82  ? 0.8272 1.2156 0.6931 -0.2461 0.0014  -0.1307 82  ARG A CA  
649  C C   . ARG A 82  ? 0.7509 1.0782 0.6939 -0.2282 0.0021  -0.1253 82  ARG A C   
650  O O   . ARG A 82  ? 0.6852 0.9926 0.6336 -0.2409 0.0182  -0.0829 82  ARG A O   
651  C CB  . ARG A 82  ? 0.7812 1.1230 0.6074 -0.2591 -0.0235 -0.0798 82  ARG A CB  
652  C CG  . ARG A 82  ? 1.0155 1.4123 0.7676 -0.2744 -0.0282 -0.0872 82  ARG A CG  
653  C CD  . ARG A 82  ? 1.0658 1.4153 0.7762 -0.2891 -0.0516 -0.0318 82  ARG A CD  
654  N NE  . ARG A 82  ? 1.0599 1.3710 0.7891 -0.2701 -0.0844 -0.0509 82  ARG A NE  
655  C CZ  . ARG A 82  ? 1.0522 1.2832 0.8155 -0.2608 -0.1080 -0.0212 82  ARG A CZ  
656  N NH1 . ARG A 82  ? 1.0484 1.2255 0.8347 -0.2672 -0.1033 0.0289  82  ARG A NH1 
657  N NH2 . ARG A 82  ? 1.0866 1.2915 0.8602 -0.2451 -0.1369 -0.0416 82  ARG A NH2 
658  N N   . TYR A 83  ? 0.7302 1.0279 0.7324 -0.1990 -0.0149 -0.1683 83  TYR A N   
659  C CA  . TYR A 83  ? 0.7167 0.9488 0.7929 -0.1806 -0.0189 -0.1632 83  TYR A CA  
660  C C   . TYR A 83  ? 0.6999 0.9646 0.8265 -0.1623 0.0008  -0.2163 83  TYR A C   
661  O O   . TYR A 83  ? 0.6961 0.9182 0.8779 -0.1524 0.0066  -0.2070 83  TYR A O   
662  C CB  . TYR A 83  ? 0.6914 0.8568 0.8016 -0.1609 -0.0540 -0.1687 83  TYR A CB  
663  C CG  . TYR A 83  ? 0.7136 0.8360 0.7817 -0.1782 -0.0739 -0.1101 83  TYR A CG  
664  C CD1 . TYR A 83  ? 0.6890 0.7542 0.7638 -0.1904 -0.0733 -0.0471 83  TYR A CD1 
665  C CD2 . TYR A 83  ? 0.8082 0.9476 0.8299 -0.1821 -0.0933 -0.1178 83  TYR A CD2 
666  C CE1 . TYR A 83  ? 0.7210 0.7462 0.7583 -0.2057 -0.0916 0.0065  83  TYR A CE1 
667  C CE2 . TYR A 83  ? 0.7764 0.8759 0.7596 -0.1976 -0.1119 -0.0640 83  TYR A CE2 
668  C CZ  . TYR A 83  ? 0.7930 0.8349 0.7847 -0.2091 -0.1111 -0.0020 83  TYR A CZ  
669  O OH  . TYR A 83  ? 0.8193 0.8200 0.7743 -0.2241 -0.1295 0.0523  83  TYR A OH  
670  N N   . ALA A 84  ? 0.7121 1.0510 0.8207 -0.1577 0.0108  -0.2714 84  ALA A N   
671  C CA  . ALA A 84  ? 0.6852 1.0669 0.8308 -0.1447 0.0337  -0.3189 84  ALA A CA  
672  C C   . ALA A 84  ? 0.6703 1.0758 0.7992 -0.1660 0.0648  -0.2834 84  ALA A C   
673  O O   . ALA A 84  ? 0.7690 1.2032 0.8342 -0.1940 0.0753  -0.2445 84  ALA A O   
674  C CB  . ALA A 84  ? 0.8200 1.2824 0.9396 -0.1389 0.0387  -0.3813 84  ALA A CB  
675  N N   . ASN A 85  ? 0.6805 1.0736 0.8666 -0.1529 0.0795  -0.2973 85  ASN A N   
676  C CA  . ASN A 85  ? 0.6639 1.0747 0.8438 -0.1704 0.1093  -0.2659 85  ASN A CA  
677  C C   . ASN A 85  ? 0.6270 0.9825 0.7841 -0.1924 0.1057  -0.1876 85  ASN A C   
678  O O   . ASN A 85  ? 0.6728 1.0553 0.7909 -0.2174 0.1279  -0.1506 85  ASN A O   
679  C CB  . ASN A 85  ? 0.6046 1.1117 0.7305 -0.1880 0.1363  -0.2873 85  ASN A CB  
680  C CG  . ASN A 85  ? 0.6815 1.2444 0.8399 -0.1664 0.1474  -0.3623 85  ASN A CG  
681  O OD1 . ASN A 85  ? 0.7532 1.3143 0.9618 -0.1540 0.1626  -0.3804 85  ASN A OD1 
682  N ND2 . ASN A 85  ? 0.6328 1.2461 0.7623 -0.1619 0.1398  -0.4059 85  ASN A ND2 
683  N N   . ASN A 86  ? 0.6233 0.9020 0.8028 -0.1839 0.0776  -0.1617 86  ASN A N   
684  C CA  . ASN A 86  ? 0.6182 0.8340 0.7894 -0.2003 0.0723  -0.0891 86  ASN A CA  
685  C C   . ASN A 86  ? 0.5205 0.6508 0.7598 -0.1773 0.0490  -0.0855 86  ASN A C   
686  O O   . ASN A 86  ? 0.5032 0.5881 0.7416 -0.1715 0.0204  -0.0749 86  ASN A O   
687  C CB  . ASN A 86  ? 0.6609 0.8808 0.7593 -0.2234 0.0596  -0.0493 86  ASN A CB  
688  C CG  . ASN A 86  ? 0.6786 0.8549 0.7534 -0.2468 0.0627  0.0269  86  ASN A CG  
689  O OD1 . ASN A 86  ? 0.6497 0.7574 0.7715 -0.2397 0.0563  0.0567  86  ASN A OD1 
690  N ND2 . ASN A 86  ? 0.6823 0.8971 0.6839 -0.2749 0.0720  0.0589  86  ASN A ND2 
691  N N   . PRO A 87  ? 0.6930 0.6434 0.7255 0.0454  -0.0445 0.0066  87  PRO A N   
692  C CA  . PRO A 87  ? 0.6467 0.6114 0.6926 0.0343  -0.0542 0.0059  87  PRO A CA  
693  C C   . PRO A 87  ? 0.5580 0.5297 0.6160 0.0302  -0.0515 0.0060  87  PRO A C   
694  O O   . PRO A 87  ? 0.5655 0.5425 0.6314 0.0276  -0.0626 0.0060  87  PRO A O   
695  C CB  . PRO A 87  ? 0.6570 0.6345 0.7079 0.0243  -0.0481 0.0034  87  PRO A CB  
696  C CG  . PRO A 87  ? 0.6763 0.6464 0.7161 0.0302  -0.0412 0.0017  87  PRO A CG  
697  C CD  . PRO A 87  ? 0.6834 0.6368 0.7160 0.0402  -0.0324 0.0033  87  PRO A CD  
698  N N   . GLN A 88  ? 0.5021 0.4724 0.5620 0.0301  -0.0356 0.0056  88  GLN A N   
699  C CA  . GLN A 88  ? 0.5881 0.5650 0.6587 0.0266  -0.0315 0.0062  88  GLN A CA  
700  C C   . GLN A 88  ? 0.5629 0.5352 0.6280 0.0398  -0.0401 0.0086  88  GLN A C   
701  O O   . GLN A 88  ? 0.5252 0.5083 0.6015 0.0362  -0.0485 0.0079  88  GLN A O   
702  C CB  . GLN A 88  ? 0.6052 0.5791 0.6783 0.0234  -0.0096 0.0045  88  GLN A CB  
703  C CG  . GLN A 88  ? 0.5162 0.4954 0.5990 0.0202  -0.0032 0.0058  88  GLN A CG  
704  C CD  . GLN A 88  ? 0.6204 0.5977 0.7091 0.0128  0.0203  0.0018  88  GLN A CD  
705  O OE1 . GLN A 88  ? 0.7171 0.6864 0.8023 0.0124  0.0343  -0.0025 88  GLN A OE1 
706  N NE2 . GLN A 88  ? 0.5773 0.5622 0.6765 0.0065  0.0257  0.0019  88  GLN A NE2 
707  N N   . ALA A 89  ? 0.6257 0.5838 0.6737 0.0565  -0.0370 0.0106  89  ALA A N   
708  C CA  . ALA A 89  ? 0.6354 0.5943 0.6762 0.0728  -0.0469 0.0110  89  ALA A CA  
709  C C   . ALA A 89  ? 0.5782 0.5488 0.6274 0.0689  -0.0687 0.0056  89  ALA A C   
710  O O   . ALA A 89  ? 0.5703 0.5542 0.6291 0.0703  -0.0781 0.0018  89  ALA A O   
711  C CB  . ALA A 89  ? 0.6304 0.5719 0.6480 0.0943  -0.0402 0.0144  89  ALA A CB  
712  N N   . LEU A 90  ? 0.5931 0.5595 0.6407 0.0625  -0.0751 0.0043  90  LEU A N   
713  C CA  . LEU A 90  ? 0.6072 0.5797 0.6623 0.0581  -0.0922 -0.0013 90  LEU A CA  
714  C C   . LEU A 90  ? 0.6562 0.6425 0.7334 0.0429  -0.0952 -0.0039 90  LEU A C   
715  O O   . LEU A 90  ? 0.6114 0.6080 0.6995 0.0436  -0.1058 -0.0107 90  LEU A O   
716  C CB  . LEU A 90  ? 0.5625 0.5251 0.6102 0.0537  -0.0939 0.0000  90  LEU A CB  
717  C CG  . LEU A 90  ? 0.6810 0.6444 0.7355 0.0471  -0.1067 -0.0048 90  LEU A CG  
718  C CD1 . LEU A 90  ? 0.7203 0.6887 0.7767 0.0564  -0.1199 -0.0136 90  LEU A CD1 
719  C CD2 . LEU A 90  ? 0.7366 0.6877 0.7776 0.0483  -0.1070 -0.0020 90  LEU A CD2 
720  N N   . ALA A 91  ? 0.5133 0.5019 0.5981 0.0299  -0.0854 0.0004  91  ALA A N   
721  C CA  . ALA A 91  ? 0.5821 0.5817 0.6861 0.0166  -0.0859 -0.0002 91  ALA A CA  
722  C C   . ALA A 91  ? 0.5968 0.6072 0.7107 0.0193  -0.0860 -0.0022 91  ALA A C   
723  O O   . ALA A 91  ? 0.5798 0.6002 0.7101 0.0134  -0.0930 -0.0069 91  ALA A O   
724  C CB  . ALA A 91  ? 0.5217 0.5242 0.6284 0.0062  -0.0747 0.0044  91  ALA A CB  
725  N N   . ASN A 92  ? 0.5428 0.5509 0.6471 0.0287  -0.0767 0.0010  92  ASN A N   
726  C CA  . ASN A 92  ? 0.5625 0.5806 0.6730 0.0340  -0.0754 0.0004  92  ASN A CA  
727  C C   . ASN A 92  ? 0.6115 0.6396 0.7232 0.0459  -0.0901 -0.0072 92  ASN A C   
728  O O   . ASN A 92  ? 0.5967 0.6409 0.7212 0.0465  -0.0943 -0.0112 92  ASN A O   
729  C CB  . ASN A 92  ? 0.5246 0.5333 0.6211 0.0441  -0.0590 0.0061  92  ASN A CB  
730  C CG  . ASN A 92  ? 0.5598 0.5668 0.6628 0.0301  -0.0439 0.0094  92  ASN A CG  
731  O OD1 . ASN A 92  ? 0.4672 0.4848 0.5859 0.0160  -0.0462 0.0087  92  ASN A OD1 
732  N ND2 . ASN A 92  ? 0.5539 0.5480 0.6456 0.0342  -0.0273 0.0118  92  ASN A ND2 
733  N N   . TYR A 93  ? 0.5507 0.5723 0.6499 0.0558  -0.0984 -0.0107 93  TYR A N   
734  C CA  . TYR A 93  ? 0.6263 0.6623 0.7274 0.0682  -0.1132 -0.0210 93  TYR A CA  
735  C C   . TYR A 93  ? 0.6409 0.6868 0.7640 0.0533  -0.1255 -0.0320 93  TYR A C   
736  O O   . TYR A 93  ? 0.6281 0.6944 0.7697 0.0514  -0.1329 -0.0419 93  TYR A O   
737  C CB  . TYR A 93  ? 0.5806 0.6066 0.6573 0.0888  -0.1162 -0.0208 93  TYR A CB  
738  C CG  . TYR A 93  ? 0.6614 0.7049 0.7399 0.1016  -0.1339 -0.0346 93  TYR A CG  
739  C CD1 . TYR A 93  ? 0.6431 0.7109 0.7278 0.1139  -0.1400 -0.0421 93  TYR A CD1 
740  C CD2 . TYR A 93  ? 0.7114 0.7498 0.7860 0.1022  -0.1445 -0.0417 93  TYR A CD2 
741  C CE1 . TYR A 93  ? 0.6869 0.7772 0.7752 0.1263  -0.1571 -0.0583 93  TYR A CE1 
742  C CE2 . TYR A 93  ? 0.6893 0.7467 0.7673 0.1134  -0.1609 -0.0574 93  TYR A CE2 
743  C CZ  . TYR A 93  ? 0.7150 0.8001 0.8008 0.1252  -0.1676 -0.0668 93  TYR A CZ  
744  O OH  . TYR A 93  ? 0.7842 0.8942 0.8755 0.1369  -0.1847 -0.0858 93  TYR A OH  
745  N N   . VAL A 94  ? 0.6718 0.7035 0.7944 0.0424  -0.1255 -0.0306 94  VAL A N   
746  C CA  . VAL A 94  ? 0.6197 0.6557 0.7608 0.0303  -0.1341 -0.0415 94  VAL A CA  
747  C C   . VAL A 94  ? 0.6533 0.6968 0.8191 0.0126  -0.1287 -0.0418 94  VAL A C   
748  O O   . VAL A 94  ? 0.6425 0.6957 0.8301 0.0038  -0.1341 -0.0539 94  VAL A O   
749  C CB  . VAL A 94  ? 0.6525 0.6685 0.7826 0.0265  -0.1338 -0.0385 94  VAL A CB  
750  C CG1 . VAL A 94  ? 0.7015 0.7102 0.8075 0.0445  -0.1381 -0.0375 94  VAL A CG1 
751  C CG2 . VAL A 94  ? 0.6526 0.6560 0.7783 0.0164  -0.1212 -0.0254 94  VAL A CG2 
752  N N   . TYR A 95  ? 0.5458 0.5854 0.7100 0.0071  -0.1170 -0.0299 95  TYR A N   
753  C CA  . TYR A 95  ? 0.5252 0.5716 0.7107 -0.0075 -0.1111 -0.0289 95  TYR A CA  
754  C C   . TYR A 95  ? 0.5754 0.6407 0.7714 -0.0039 -0.1113 -0.0313 95  TYR A C   
755  O O   . TYR A 95  ? 0.4753 0.5466 0.6880 -0.0149 -0.1054 -0.0292 95  TYR A O   
756  C CB  . TYR A 95  ? 0.5208 0.5552 0.6994 -0.0152 -0.0988 -0.0162 95  TYR A CB  
757  C CG  . TYR A 95  ? 0.6139 0.6323 0.7840 -0.0182 -0.0983 -0.0142 95  TYR A CG  
758  C CD1 . TYR A 95  ? 0.6277 0.6413 0.8085 -0.0233 -0.1033 -0.0227 95  TYR A CD1 
759  C CD2 . TYR A 95  ? 0.5915 0.6006 0.7435 -0.0155 -0.0921 -0.0054 95  TYR A CD2 
760  C CE1 . TYR A 95  ? 0.6382 0.6347 0.8094 -0.0246 -0.1011 -0.0200 95  TYR A CE1 
761  C CE2 . TYR A 95  ? 0.6392 0.6351 0.7816 -0.0159 -0.0916 -0.0030 95  TYR A CE2 
762  C CZ  . TYR A 95  ? 0.6165 0.6044 0.7671 -0.0198 -0.0956 -0.0092 95  TYR A CZ  
763  O OH  . TYR A 95  ? 0.6059 0.5781 0.7452 -0.0190 -0.0932 -0.0058 95  TYR A OH  
764  N N   . ALA A 96  ? 0.5658 0.6404 0.7510 0.0131  -0.1174 -0.0350 96  ALA A N   
765  C CA  . ALA A 96  ? 0.5458 0.6382 0.7372 0.0197  -0.1162 -0.0357 96  ALA A CA  
766  C C   . ALA A 96  ? 0.5301 0.6443 0.7510 0.0105  -0.1239 -0.0493 96  ALA A C   
767  O O   . ALA A 96  ? 0.5356 0.6556 0.7687 0.0066  -0.1333 -0.0629 96  ALA A O   
768  C CB  . ALA A 96  ? 0.6342 0.7316 0.8046 0.0441  -0.1197 -0.0364 96  ALA A CB  
769  N N   . ASN A 97  ? 0.5275 0.6530 0.7619 0.0053  -0.1181 -0.0464 97  ASN A N   
770  C CA  . ASN A 97  ? 0.5371 0.6868 0.8011 -0.0022 -0.1237 -0.0598 97  ASN A CA  
771  C C   . ASN A 97  ? 0.5423 0.6868 0.8297 -0.0215 -0.1240 -0.0691 97  ASN A C   
772  O O   . ASN A 97  ? 0.5459 0.7110 0.8598 -0.0274 -0.1304 -0.0865 97  ASN A O   
773  C CB  . ASN A 97  ? 0.5345 0.7123 0.7984 0.0167  -0.1371 -0.0743 97  ASN A CB  
774  C CG  . ASN A 97  ? 0.5109 0.6862 0.7444 0.0403  -0.1337 -0.0630 97  ASN A CG  
775  O OD1 . ASN A 97  ? 0.5313 0.7066 0.7612 0.0426  -0.1239 -0.0525 97  ASN A OD1 
776  N ND2 . ASN A 97  ? 0.5374 0.7085 0.7484 0.0585  -0.1398 -0.0648 97  ASN A ND2 
777  N N   . ARG A 98  ? 0.4926 0.6104 0.7705 -0.0305 -0.1159 -0.0586 98  ARG A N   
778  C CA  . ARG A 98  ? 0.5659 0.6714 0.8606 -0.0468 -0.1112 -0.0632 98  ARG A CA  
779  C C   . ARG A 98  ? 0.5252 0.6141 0.8189 -0.0570 -0.0960 -0.0471 98  ARG A C   
780  O O   . ARG A 98  ? 0.4902 0.5749 0.7664 -0.0516 -0.0910 -0.0335 98  ARG A O   
781  C CB  . ARG A 98  ? 0.6023 0.6905 0.8822 -0.0439 -0.1154 -0.0656 98  ARG A CB  
782  C CG  . ARG A 98  ? 0.6895 0.7945 0.9733 -0.0350 -0.1305 -0.0847 98  ARG A CG  
783  C CD  . ARG A 98  ? 0.7357 0.8228 1.0141 -0.0378 -0.1327 -0.0906 98  ARG A CD  
784  N NE  . ARG A 98  ? 0.9890 1.0970 1.2835 -0.0352 -0.1457 -0.1148 98  ARG A NE  
785  C CZ  . ARG A 98  ? 0.9575 1.0764 1.2856 -0.0503 -0.1444 -0.1339 98  ARG A CZ  
786  N NH1 . ARG A 98  ? 0.9125 1.0189 1.2604 -0.0684 -0.1291 -0.1297 98  ARG A NH1 
787  N NH2 . ARG A 98  ? 0.9051 1.0487 1.2480 -0.0465 -0.1577 -0.1591 98  ARG A NH2 
788  N N   . ILE A 99  ? 0.5655 0.6449 0.8782 -0.0710 -0.0873 -0.0497 99  ILE A N   
789  C CA  . ILE A 99  ? 0.5409 0.6042 0.8530 -0.0788 -0.0715 -0.0352 99  ILE A CA  
790  C C   . ILE A 99  ? 0.5092 0.5816 0.8148 -0.0752 -0.0677 -0.0236 99  ILE A C   
791  O O   . ILE A 99  ? 0.4773 0.5394 0.7641 -0.0721 -0.0607 -0.0099 99  ILE A O   
792  C CB  . ILE A 99  ? 0.5591 0.5977 0.8480 -0.0759 -0.0657 -0.0246 99  ILE A CB  
793  C CG1 . ILE A 99  ? 0.4692 0.5076 0.7325 -0.0634 -0.0764 -0.0233 99  ILE A CG1 
794  C CG2 . ILE A 99  ? 0.6518 0.6737 0.9535 -0.0846 -0.0590 -0.0319 99  ILE A CG2 
795  C CD1 . ILE A 99  ? 0.5291 0.5475 0.7704 -0.0596 -0.0721 -0.0145 99  ILE A CD1 
796  N N   . GLY A 100 ? 0.5228 0.6166 0.8434 -0.0746 -0.0725 -0.0303 100 GLY A N   
797  C CA  . GLY A 100 ? 0.4539 0.5557 0.7703 -0.0718 -0.0676 -0.0204 100 GLY A CA  
798  C C   . GLY A 100 ? 0.4591 0.5641 0.7516 -0.0584 -0.0720 -0.0153 100 GLY A C   
799  O O   . GLY A 100 ? 0.5091 0.6222 0.7996 -0.0554 -0.0678 -0.0096 100 GLY A O   
800  N N   . ASN A 101 ? 0.4719 0.5690 0.7460 -0.0500 -0.0784 -0.0170 101 ASN A N   
801  C CA  . ASN A 101 ? 0.4458 0.5407 0.6963 -0.0376 -0.0780 -0.0111 101 ASN A CA  
802  C C   . ASN A 101 ? 0.4658 0.5776 0.7169 -0.0256 -0.0832 -0.0160 101 ASN A C   
803  O O   . ASN A 101 ? 0.4249 0.5536 0.6913 -0.0237 -0.0927 -0.0279 101 ASN A O   
804  C CB  . ASN A 101 ? 0.4549 0.5367 0.6863 -0.0308 -0.0826 -0.0118 101 ASN A CB  
805  C CG  . ASN A 101 ? 0.5100 0.5762 0.7337 -0.0378 -0.0759 -0.0046 101 ASN A CG  
806  O OD1 . ASN A 101 ? 0.4780 0.5434 0.7044 -0.0445 -0.0663 0.0028  101 ASN A OD1 
807  N ND2 . ASN A 101 ? 0.4460 0.5013 0.6585 -0.0345 -0.0808 -0.0068 101 ASN A ND2 
808  N N   . GLY A 102 ? 0.4692 0.5776 0.7036 -0.0168 -0.0756 -0.0078 102 GLY A N   
809  C CA  . GLY A 102 ? 0.5401 0.6587 0.7651 0.0006  -0.0780 -0.0097 102 GLY A CA  
810  C C   . GLY A 102 ? 0.5208 0.6362 0.7291 0.0157  -0.0865 -0.0149 102 GLY A C   
811  O O   . GLY A 102 ? 0.4827 0.5902 0.6905 0.0110  -0.0929 -0.0191 102 GLY A O   
812  N N   . ASN A 103 ? 0.4868 0.6069 0.6789 0.0362  -0.0853 -0.0136 103 ASN A N   
813  C CA  . ASN A 103 ? 0.5143 0.6331 0.6885 0.0548  -0.0931 -0.0182 103 ASN A CA  
814  C C   . ASN A 103 ? 0.5411 0.6321 0.6927 0.0568  -0.0829 -0.0090 103 ASN A C   
815  O O   . ASN A 103 ? 0.5338 0.6101 0.6862 0.0425  -0.0717 -0.0018 103 ASN A O   
816  C CB  . ASN A 103 ? 0.5715 0.7070 0.7342 0.0802  -0.0949 -0.0200 103 ASN A CB  
817  C CG  . ASN A 103 ? 0.6091 0.7298 0.7527 0.0908  -0.0754 -0.0058 103 ASN A CG  
818  O OD1 . ASN A 103 ? 0.6485 0.7457 0.7857 0.0802  -0.0607 0.0036  103 ASN A OD1 
819  N ND2 . ASN A 103 ? 0.5621 0.6979 0.6966 0.1129  -0.0744 -0.0054 103 ASN A ND2 
820  N N   . GLU A 104 ? 0.5706 0.6565 0.7025 0.0755  -0.0871 -0.0107 104 GLU A N   
821  C CA  . GLU A 104 ? 0.5696 0.6299 0.6813 0.0781  -0.0774 -0.0034 104 GLU A CA  
822  C C   . GLU A 104 ? 0.5181 0.5620 0.6189 0.0791  -0.0553 0.0076  104 GLU A C   
823  O O   . GLU A 104 ? 0.5312 0.5593 0.6302 0.0671  -0.0445 0.0116  104 GLU A O   
824  C CB  . GLU A 104 ? 0.5233 0.5809 0.6138 0.1018  -0.0841 -0.0062 104 GLU A CB  
825  C CG  . GLU A 104 ? 0.5123 0.5430 0.5831 0.1043  -0.0740 0.0006  104 GLU A CG  
826  C CD  . GLU A 104 ? 0.6604 0.6877 0.7090 0.1293  -0.0808 -0.0015 104 GLU A CD  
827  O OE1 . GLU A 104 ? 0.5944 0.6369 0.6351 0.1511  -0.0867 -0.0050 104 GLU A OE1 
828  O OE2 . GLU A 104 ? 0.6825 0.6933 0.7203 0.1290  -0.0805 -0.0001 104 GLU A OE2 
829  N N   . ALA A 105 ? 0.4988 0.5482 0.5940 0.0928  -0.0476 0.0113  105 ALA A N   
830  C CA  . ALA A 105 ? 0.6132 0.6439 0.6972 0.0951  -0.0235 0.0210  105 ALA A CA  
831  C C   . ALA A 105 ? 0.5824 0.6130 0.6851 0.0695  -0.0163 0.0218  105 ALA A C   
832  O O   . ALA A 105 ? 0.5413 0.5551 0.6391 0.0633  0.0028  0.0258  105 ALA A O   
833  C CB  . ALA A 105 ? 0.5257 0.5623 0.5983 0.1172  -0.0164 0.0255  105 ALA A CB  
834  N N   . SER A 106 ? 0.5492 0.5992 0.6743 0.0548  -0.0306 0.0168  106 SER A N   
835  C CA  . SER A 106 ? 0.5184 0.5708 0.6599 0.0341  -0.0241 0.0183  106 SER A CA  
836  C C   . SER A 106 ? 0.4658 0.5073 0.6072 0.0201  -0.0191 0.0178  106 SER A C   
837  O O   . SER A 106 ? 0.5234 0.5642 0.6714 0.0075  -0.0081 0.0189  106 SER A O   
838  C CB  . SER A 106 ? 0.5050 0.5782 0.6697 0.0232  -0.0389 0.0136  106 SER A CB  
839  O OG  . SER A 106 ? 0.4837 0.5578 0.6563 0.0135  -0.0512 0.0084  106 SER A OG  
840  N N   . GLY A 107 ? 0.4662 0.5015 0.5999 0.0230  -0.0270 0.0151  107 GLY A N   
841  C CA  . GLY A 107 ? 0.4444 0.4735 0.5782 0.0112  -0.0236 0.0139  107 GLY A CA  
842  C C   . GLY A 107 ? 0.5484 0.5885 0.6976 -0.0034 -0.0340 0.0120  107 GLY A C   
843  O O   . GLY A 107 ? 0.4980 0.5363 0.6459 -0.0109 -0.0321 0.0112  107 GLY A O   
844  N N   . ASP A 108 ? 0.4509 0.5024 0.6141 -0.0062 -0.0437 0.0109  108 ASP A N   
845  C CA  . ASP A 108 ? 0.5144 0.5722 0.6920 -0.0191 -0.0492 0.0104  108 ASP A CA  
846  C C   . ASP A 108 ? 0.4900 0.5407 0.6625 -0.0200 -0.0571 0.0083  108 ASP A C   
847  O O   . ASP A 108 ? 0.4655 0.5157 0.6410 -0.0280 -0.0553 0.0104  108 ASP A O   
848  C CB  . ASP A 108 ? 0.4449 0.5147 0.6406 -0.0220 -0.0562 0.0079  108 ASP A CB  
849  C CG  . ASP A 108 ? 0.4438 0.5215 0.6485 -0.0266 -0.0473 0.0118  108 ASP A CG  
850  O OD1 . ASP A 108 ? 0.4949 0.5685 0.6918 -0.0280 -0.0354 0.0156  108 ASP A OD1 
851  O OD2 . ASP A 108 ? 0.4566 0.5456 0.6773 -0.0291 -0.0515 0.0098  108 ASP A OD2 
852  N N   . GLY A 109 ? 0.4678 0.5131 0.6314 -0.0101 -0.0654 0.0046  109 GLY A N   
853  C CA  . GLY A 109 ? 0.4890 0.5266 0.6480 -0.0109 -0.0731 0.0023  109 GLY A CA  
854  C C   . GLY A 109 ? 0.4895 0.5198 0.6370 -0.0135 -0.0660 0.0064  109 GLY A C   
855  O O   . GLY A 109 ? 0.4241 0.4521 0.5726 -0.0190 -0.0672 0.0078  109 GLY A O   
856  N N   . TRP A 110 ? 0.5021 0.5296 0.6389 -0.0090 -0.0567 0.0077  110 TRP A N   
857  C CA  . TRP A 110 ? 0.4809 0.5072 0.6099 -0.0119 -0.0490 0.0082  110 TRP A CA  
858  C C   . TRP A 110 ? 0.5037 0.5428 0.6425 -0.0218 -0.0418 0.0090  110 TRP A C   
859  O O   . TRP A 110 ? 0.5116 0.5560 0.6480 -0.0245 -0.0415 0.0092  110 TRP A O   
860  C CB  . TRP A 110 ? 0.4680 0.4867 0.5863 -0.0048 -0.0385 0.0070  110 TRP A CB  
861  C CG  . TRP A 110 ? 0.4575 0.4788 0.5723 -0.0091 -0.0276 0.0038  110 TRP A CG  
862  C CD1 . TRP A 110 ? 0.5562 0.5834 0.6765 -0.0149 -0.0122 -0.0001 110 TRP A CD1 
863  C CD2 . TRP A 110 ? 0.4684 0.4891 0.5752 -0.0080 -0.0308 0.0020  110 TRP A CD2 
864  N NE1 . TRP A 110 ? 0.5637 0.5970 0.6820 -0.0182 -0.0062 -0.0062 110 TRP A NE1 
865  C CE2 . TRP A 110 ? 0.5212 0.5509 0.6304 -0.0132 -0.0177 -0.0042 110 TRP A CE2 
866  C CE3 . TRP A 110 ? 0.5244 0.5385 0.6227 -0.0030 -0.0428 0.0040  110 TRP A CE3 
867  C CZ2 . TRP A 110 ? 0.5083 0.5438 0.6120 -0.0129 -0.0173 -0.0085 110 TRP A CZ2 
868  C CZ3 . TRP A 110 ? 0.4870 0.5030 0.5772 -0.0020 -0.0418 0.0020  110 TRP A CZ3 
869  C CH2 . TRP A 110 ? 0.4714 0.4995 0.5645 -0.0065 -0.0296 -0.0042 110 TRP A CH2 
870  N N   . ARG A 111 ? 0.4599 0.5051 0.6082 -0.0253 -0.0359 0.0096  111 ARG A N   
871  C CA  . ARG A 111 ? 0.4900 0.5483 0.6473 -0.0335 -0.0289 0.0100  111 ARG A CA  
872  C C   . ARG A 111 ? 0.4722 0.5345 0.6337 -0.0366 -0.0349 0.0136  111 ARG A C   
873  O O   . ARG A 111 ? 0.4740 0.5466 0.6338 -0.0383 -0.0306 0.0137  111 ARG A O   
874  C CB  . ARG A 111 ? 0.4459 0.5075 0.6128 -0.0357 -0.0235 0.0113  111 ARG A CB  
875  C CG  . ARG A 111 ? 0.5307 0.6058 0.7078 -0.0436 -0.0171 0.0122  111 ARG A CG  
876  C CD  . ARG A 111 ? 0.5315 0.6079 0.7165 -0.0448 -0.0108 0.0138  111 ARG A CD  
877  N NE  . ARG A 111 ? 0.6150 0.6846 0.7930 -0.0417 0.0010  0.0106  111 ARG A NE  
878  C CZ  . ARG A 111 ? 0.6840 0.7424 0.8556 -0.0327 0.0029  0.0126  111 ARG A CZ  
879  N NH1 . ARG A 111 ? 0.5855 0.6440 0.7595 -0.0265 -0.0083 0.0159  111 ARG A NH1 
880  N NH2 . ARG A 111 ? 0.6661 0.7137 0.8289 -0.0289 0.0177  0.0104  111 ARG A NH2 
881  N N   . PHE A 112 ? 0.4518 0.5063 0.6183 -0.0361 -0.0435 0.0156  112 PHE A N   
882  C CA  . PHE A 112 ? 0.4382 0.4912 0.6102 -0.0392 -0.0449 0.0194  112 PHE A CA  
883  C C   . PHE A 112 ? 0.4075 0.4480 0.5711 -0.0355 -0.0512 0.0192  112 PHE A C   
884  O O   . PHE A 112 ? 0.4819 0.5142 0.6531 -0.0382 -0.0534 0.0199  112 PHE A O   
885  C CB  . PHE A 112 ? 0.4578 0.5122 0.6476 -0.0446 -0.0459 0.0199  112 PHE A CB  
886  C CG  . PHE A 112 ? 0.4121 0.4778 0.6095 -0.0481 -0.0387 0.0217  112 PHE A CG  
887  C CD1 . PHE A 112 ? 0.4725 0.5459 0.6685 -0.0498 -0.0306 0.0257  112 PHE A CD1 
888  C CD2 . PHE A 112 ? 0.4005 0.4702 0.6047 -0.0476 -0.0397 0.0193  112 PHE A CD2 
889  C CE1 . PHE A 112 ? 0.4967 0.5807 0.6997 -0.0531 -0.0239 0.0265  112 PHE A CE1 
890  C CE2 . PHE A 112 ? 0.5090 0.5874 0.7194 -0.0506 -0.0320 0.0214  112 PHE A CE2 
891  C CZ  . PHE A 112 ? 0.4983 0.5835 0.7089 -0.0544 -0.0242 0.0246  112 PHE A CZ  
892  N N   . ARG A 113 ? 0.4686 0.5063 0.6175 -0.0298 -0.0529 0.0173  113 ARG A N   
893  C CA  . ARG A 113 ? 0.4709 0.4968 0.6090 -0.0253 -0.0580 0.0178  113 ARG A CA  
894  C C   . ARG A 113 ? 0.4919 0.5174 0.6253 -0.0243 -0.0524 0.0238  113 ARG A C   
895  O O   . ARG A 113 ? 0.4423 0.4798 0.5780 -0.0253 -0.0453 0.0268  113 ARG A O   
896  C CB  . ARG A 113 ? 0.4842 0.5088 0.6076 -0.0188 -0.0593 0.0150  113 ARG A CB  
897  C CG  . ARG A 113 ? 0.4445 0.4836 0.5620 -0.0183 -0.0510 0.0139  113 ARG A CG  
898  C CD  . ARG A 113 ? 0.4744 0.5104 0.5815 -0.0135 -0.0504 0.0095  113 ARG A CD  
899  N NE  . ARG A 113 ? 0.4063 0.4586 0.5111 -0.0142 -0.0421 0.0044  113 ARG A NE  
900  C CZ  . ARG A 113 ? 0.5316 0.5965 0.6455 -0.0198 -0.0327 -0.0010 113 ARG A CZ  
901  N NH1 . ARG A 113 ? 0.4916 0.5532 0.6153 -0.0240 -0.0302 0.0005  113 ARG A NH1 
902  N NH2 . ARG A 113 ? 0.5434 0.6262 0.6577 -0.0211 -0.0252 -0.0094 113 ARG A NH2 
903  N N   . GLY A 114 ? 0.5079 0.5189 0.6334 -0.0208 -0.0548 0.0258  114 GLY A N   
904  C CA  . GLY A 114 ? 0.5893 0.5953 0.7065 -0.0165 -0.0472 0.0332  114 GLY A CA  
905  C C   . GLY A 114 ? 0.5437 0.5677 0.6478 -0.0089 -0.0420 0.0358  114 GLY A C   
906  O O   . GLY A 114 ? 0.5066 0.5401 0.6019 -0.0053 -0.0454 0.0312  114 GLY A O   
907  N N   . ARG A 115 ? 0.5515 0.5825 0.6550 -0.0057 -0.0332 0.0420  115 ARG A N   
908  C CA  . ARG A 115 ? 0.5396 0.5936 0.6309 0.0039  -0.0287 0.0426  115 ARG A CA  
909  C C   . ARG A 115 ? 0.6033 0.6532 0.6834 0.0152  -0.0185 0.0534  115 ARG A C   
910  O O   . ARG A 115 ? 0.5169 0.5520 0.6059 0.0117  -0.0114 0.0598  115 ARG A O   
911  C CB  . ARG A 115 ? 0.5483 0.6258 0.6513 -0.0019 -0.0275 0.0360  115 ARG A CB  
912  C CG  . ARG A 115 ? 0.4990 0.5873 0.6066 -0.0078 -0.0320 0.0249  115 ARG A CG  
913  C CD  . ARG A 115 ? 0.6018 0.7115 0.7206 -0.0133 -0.0269 0.0187  115 ARG A CD  
914  N NE  . ARG A 115 ? 0.6062 0.7190 0.7328 -0.0210 -0.0265 0.0091  115 ARG A NE  
915  C CZ  . ARG A 115 ? 0.6236 0.7207 0.7588 -0.0275 -0.0281 0.0097  115 ARG A CZ  
916  N NH1 . ARG A 115 ? 0.4498 0.5307 0.5903 -0.0293 -0.0323 0.0169  115 ARG A NH1 
917  N NH2 . ARG A 115 ? 0.6159 0.7144 0.7548 -0.0315 -0.0239 0.0021  115 ARG A NH2 
918  N N   . GLY A 116 ? 0.6786 0.7431 0.7390 0.0302  -0.0162 0.0551  116 GLY A N   
919  C CA  . GLY A 116 ? 0.5309 0.5909 0.5741 0.0466  -0.0049 0.0669  116 GLY A CA  
920  C C   . GLY A 116 ? 0.6799 0.7186 0.7046 0.0563  -0.0031 0.0732  116 GLY A C   
921  O O   . GLY A 116 ? 0.5991 0.6197 0.6288 0.0470  -0.0101 0.0694  116 GLY A O   
922  N N   . PRO A 117 ? 0.6463 0.6871 0.6474 0.0772  0.0070  0.0831  117 PRO A N   
923  C CA  . PRO A 117 ? 0.6253 0.6429 0.6063 0.0881  0.0111  0.0906  117 PRO A CA  
924  C C   . PRO A 117 ? 0.7289 0.7027 0.7195 0.0766  0.0177  0.0957  117 PRO A C   
925  O O   . PRO A 117 ? 0.7789 0.7346 0.7662 0.0731  0.0130  0.0935  117 PRO A O   
926  C CB  . PRO A 117 ? 0.6990 0.7272 0.6524 0.1153  0.0242  0.1022  117 PRO A CB  
927  C CG  . PRO A 117 ? 0.6834 0.7243 0.6466 0.1153  0.0310  0.1044  117 PRO A CG  
928  C CD  . PRO A 117 ? 0.6191 0.6820 0.6089 0.0938  0.0162  0.0887  117 PRO A CD  
929  N N   . ILE A 118 ? 0.6757 0.6331 0.6794 0.0703  0.0291  0.1010  118 ILE A N   
930  C CA  . ILE A 118 ? 0.7052 0.6317 0.7314 0.0515  0.0316  0.0979  118 ILE A CA  
931  C C   . ILE A 118 ? 0.7139 0.6580 0.7679 0.0332  0.0202  0.0872  118 ILE A C   
932  O O   . ILE A 118 ? 0.6755 0.6354 0.7347 0.0345  0.0245  0.0898  118 ILE A O   
933  C CB  . ILE A 118 ? 0.6885 0.5825 0.7127 0.0562  0.0553  0.1099  118 ILE A CB  
934  C CG1 . ILE A 118 ? 0.7638 0.6350 0.7583 0.0755  0.0690  0.1214  118 ILE A CG1 
935  C CG2 . ILE A 118 ? 0.6441 0.5139 0.6989 0.0337  0.0578  0.1019  118 ILE A CG2 
936  C CD1 . ILE A 118 ? 0.8288 0.6659 0.8162 0.0847  0.0977  0.1358  118 ILE A CD1 
937  N N   . GLN A 119 ? 0.5665 0.5079 0.6368 0.0180  0.0065  0.0756  119 GLN A N   
938  C CA  . GLN A 119 ? 0.6644 0.6282 0.7527 0.0063  -0.0065 0.0655  119 GLN A CA  
939  C C   . GLN A 119 ? 0.5763 0.5358 0.6904 -0.0072 -0.0028 0.0631  119 GLN A C   
940  O O   . GLN A 119 ? 0.5666 0.5037 0.6932 -0.0144 0.0044  0.0625  119 GLN A O   
941  C CB  . GLN A 119 ? 0.6088 0.5735 0.6991 0.0007  -0.0218 0.0553  119 GLN A CB  
942  C CG  . GLN A 119 ? 0.6393 0.6128 0.7066 0.0129  -0.0260 0.0563  119 GLN A CG  
943  C CD  . GLN A 119 ? 0.6863 0.6559 0.7539 0.0088  -0.0387 0.0479  119 GLN A CD  
944  O OE1 . GLN A 119 ? 0.6915 0.6591 0.7756 -0.0014 -0.0461 0.0404  119 GLN A OE1 
945  N NE2 . GLN A 119 ? 0.5898 0.5593 0.6381 0.0188  -0.0411 0.0492  119 GLN A NE2 
946  N N   . THR A 120 ? 0.5536 0.5355 0.6766 -0.0106 -0.0063 0.0609  120 THR A N   
947  C CA  . THR A 120 ? 0.6210 0.6049 0.7691 -0.0237 -0.0067 0.0565  120 THR A CA  
948  C C   . THR A 120 ? 0.5510 0.5468 0.7080 -0.0310 -0.0221 0.0454  120 THR A C   
949  O O   . THR A 120 ? 0.5435 0.5536 0.6890 -0.0263 -0.0284 0.0430  120 THR A O   
950  C CB  . THR A 120 ? 0.5446 0.5440 0.6952 -0.0213 0.0009  0.0623  120 THR A CB  
951  O OG1 . THR A 120 ? 0.6228 0.6112 0.7600 -0.0096 0.0165  0.0742  120 THR A OG1 
952  C CG2 . THR A 120 ? 0.5857 0.5856 0.7628 -0.0346 0.0016  0.0585  120 THR A CG2 
953  N N   . THR A 121 ? 0.5053 0.4958 0.6828 -0.0415 -0.0266 0.0378  121 THR A N   
954  C CA  . THR A 121 ? 0.5570 0.5563 0.7393 -0.0442 -0.0404 0.0279  121 THR A CA  
955  C C   . THR A 121 ? 0.5032 0.5119 0.7090 -0.0528 -0.0432 0.0215  121 THR A C   
956  O O   . THR A 121 ? 0.5161 0.5182 0.7402 -0.0603 -0.0385 0.0185  121 THR A O   
957  C CB  . THR A 121 ? 0.5464 0.5319 0.7240 -0.0428 -0.0474 0.0219  121 THR A CB  
958  O OG1 . THR A 121 ? 0.5926 0.5675 0.7487 -0.0343 -0.0423 0.0294  121 THR A OG1 
959  C CG2 . THR A 121 ? 0.4540 0.4489 0.6285 -0.0400 -0.0608 0.0139  121 THR A CG2 
960  N N   . GLY A 122 ? 0.5038 0.5274 0.7092 -0.0514 -0.0493 0.0188  122 GLY A N   
961  C CA  . GLY A 122 ? 0.4541 0.4888 0.6783 -0.0561 -0.0536 0.0123  122 GLY A CA  
962  C C   . GLY A 122 ? 0.4663 0.5107 0.7003 -0.0603 -0.0454 0.0177  122 GLY A C   
963  O O   . GLY A 122 ? 0.4473 0.4870 0.6814 -0.0620 -0.0353 0.0252  122 GLY A O   
964  N N   . ARG A 123 ? 0.4772 0.4766 0.6001 -0.0279 -0.0192 0.0505  123 ARG A N   
965  C CA  . ARG A 123 ? 0.4838 0.4838 0.5999 -0.0205 -0.0135 0.0495  123 ARG A CA  
966  C C   . ARG A 123 ? 0.5233 0.5464 0.6494 -0.0221 -0.0124 0.0531  123 ARG A C   
967  O O   . ARG A 123 ? 0.4994 0.5216 0.6189 -0.0202 -0.0083 0.0521  123 ARG A O   
968  C CB  . ARG A 123 ? 0.5360 0.5337 0.6460 -0.0065 -0.0096 0.0503  123 ARG A CB  
969  C CG  . ARG A 123 ? 0.4959 0.4924 0.5955 0.0044  -0.0023 0.0497  123 ARG A CG  
970  C CD  . ARG A 123 ? 0.5477 0.5389 0.6386 0.0208  0.0030  0.0514  123 ARG A CD  
971  N NE  . ARG A 123 ? 0.5535 0.5129 0.6291 0.0226  0.0043  0.0473  123 ARG A NE  
972  C CZ  . ARG A 123 ? 0.6968 0.6278 0.7525 0.0252  0.0086  0.0420  123 ARG A CZ  
973  N NH1 . ARG A 123 ? 0.5935 0.5229 0.6400 0.0272  0.0119  0.0390  123 ARG A NH1 
974  N NH2 . ARG A 123 ? 0.6275 0.5299 0.6711 0.0256  0.0095  0.0398  123 ARG A NH2 
975  N N   . ALA A 124 ? 0.4931 0.5368 0.6344 -0.0258 -0.0164 0.0578  124 ALA A N   
976  C CA  . ALA A 124 ? 0.5267 0.5949 0.6801 -0.0277 -0.0151 0.0634  124 ALA A CA  
977  C C   . ALA A 124 ? 0.5163 0.5821 0.6711 -0.0379 -0.0152 0.0635  124 ALA A C   
978  O O   . ALA A 124 ? 0.5720 0.6505 0.7293 -0.0365 -0.0108 0.0670  124 ALA A O   
979  C CB  . ALA A 124 ? 0.5092 0.5994 0.6790 -0.0322 -0.0210 0.0687  124 ALA A CB  
980  N N   . ASN A 125 ? 0.4908 0.5411 0.6430 -0.0464 -0.0193 0.0606  125 ASN A N   
981  C CA  . ASN A 125 ? 0.5385 0.5871 0.6915 -0.0546 -0.0189 0.0619  125 ASN A CA  
982  C C   . ASN A 125 ? 0.5785 0.6164 0.7182 -0.0515 -0.0150 0.0583  125 ASN A C   
983  O O   . ASN A 125 ? 0.5360 0.5815 0.6758 -0.0533 -0.0124 0.0606  125 ASN A O   
984  C CB  . ASN A 125 ? 0.4842 0.5209 0.6380 -0.0626 -0.0238 0.0614  125 ASN A CB  
985  C CG  . ASN A 125 ? 0.6004 0.6453 0.7644 -0.0678 -0.0288 0.0640  125 ASN A CG  
986  O OD1 . ASN A 125 ? 0.5810 0.6438 0.7562 -0.0711 -0.0289 0.0688  125 ASN A OD1 
987  N ND2 . ASN A 125 ? 0.6403 0.6725 0.7999 -0.0687 -0.0334 0.0613  125 ASN A ND2 
988  N N   . TYR A 126 ? 0.5036 0.5237 0.6313 -0.0477 -0.0150 0.0530  126 TYR A N   
989  C CA  . TYR A 126 ? 0.5625 0.5707 0.6754 -0.0459 -0.0126 0.0487  126 TYR A CA  
990  C C   . TYR A 126 ? 0.4796 0.4964 0.5867 -0.0367 -0.0071 0.0487  126 TYR A C   
991  O O   . TYR A 126 ? 0.5318 0.5481 0.6300 -0.0369 -0.0052 0.0473  126 TYR A O   
992  C CB  . TYR A 126 ? 0.4912 0.4774 0.5926 -0.0439 -0.0136 0.0437  126 TYR A CB  
993  C CG  . TYR A 126 ? 0.4914 0.4694 0.5953 -0.0528 -0.0178 0.0445  126 TYR A CG  
994  C CD1 . TYR A 126 ? 0.5006 0.4799 0.6132 -0.0538 -0.0200 0.0475  126 TYR A CD1 
995  C CD2 . TYR A 126 ? 0.5525 0.5231 0.6495 -0.0597 -0.0196 0.0430  126 TYR A CD2 
996  C CE1 . TYR A 126 ? 0.5275 0.5006 0.6415 -0.0596 -0.0224 0.0497  126 TYR A CE1 
997  C CE2 . TYR A 126 ? 0.5870 0.5548 0.6881 -0.0669 -0.0227 0.0460  126 TYR A CE2 
998  C CZ  . TYR A 126 ? 0.5074 0.4762 0.6168 -0.0658 -0.0233 0.0497  126 TYR A CZ  
999  O OH  . TYR A 126 ? 0.4634 0.4304 0.5758 -0.0708 -0.0249 0.0539  126 TYR A OH  
1000 N N   . LEU A 127 ? 0.5849 0.6108 0.6960 -0.0274 -0.0042 0.0510  127 LEU A N   
1001 C CA  . LEU A 127 ? 0.6018 0.6394 0.7083 -0.0162 0.0025  0.0533  127 LEU A CA  
1002 C C   . LEU A 127 ? 0.6248 0.6847 0.7426 -0.0208 0.0039  0.0598  127 LEU A C   
1003 O O   . LEU A 127 ? 0.5757 0.6380 0.6833 -0.0152 0.0089  0.0598  127 LEU A O   
1004 C CB  . LEU A 127 ? 0.5752 0.6257 0.6888 -0.0056 0.0051  0.0576  127 LEU A CB  
1005 C CG  . LEU A 127 ? 0.6786 0.7433 0.7872 0.0094  0.0137  0.0618  127 LEU A CG  
1006 C CD1 . LEU A 127 ? 0.7884 0.8233 0.8682 0.0204  0.0187  0.0536  127 LEU A CD1 
1007 C CD2 . LEU A 127 ? 0.6555 0.7459 0.7789 0.0184  0.0158  0.0703  127 LEU A CD2 
1008 N N   . GLN A 128 ? 0.5636 0.6377 0.7007 -0.0309 -0.0003 0.0653  128 GLN A N   
1009 C CA  . GLN A 128 ? 0.6155 0.7088 0.7641 -0.0362 0.0015  0.0727  128 GLN A CA  
1010 C C   . GLN A 128 ? 0.5717 0.6542 0.7103 -0.0413 0.0013  0.0701  128 GLN A C   
1011 O O   . GLN A 128 ? 0.5756 0.6682 0.7109 -0.0381 0.0060  0.0736  128 GLN A O   
1012 C CB  . GLN A 128 ? 0.6591 0.7637 0.8274 -0.0473 -0.0038 0.0784  128 GLN A CB  
1013 C CG  . GLN A 128 ? 0.7725 0.9059 0.9576 -0.0473 -0.0009 0.0886  128 GLN A CG  
1014 C CD  . GLN A 128 ? 0.8438 0.9851 1.0465 -0.0603 -0.0078 0.0931  128 GLN A CD  
1015 O OE1 . GLN A 128 ? 0.9523 1.0889 1.1569 -0.0620 -0.0138 0.0898  128 GLN A OE1 
1016 N NE2 . GLN A 128 ? 0.8374 0.9888 1.0513 -0.0696 -0.0073 0.1006  128 GLN A NE2 
1017 N N   . LEU A 129 ? 0.5680 0.6319 0.7013 -0.0481 -0.0038 0.0649  129 LEU A N   
1018 C CA  . LEU A 129 ? 0.5365 0.5921 0.6594 -0.0520 -0.0045 0.0627  129 LEU A CA  
1019 C C   . LEU A 129 ? 0.6350 0.6850 0.7387 -0.0437 -0.0011 0.0576  129 LEU A C   
1020 O O   . LEU A 129 ? 0.6205 0.6767 0.7179 -0.0434 0.0009  0.0592  129 LEU A O   
1021 C CB  . LEU A 129 ? 0.4993 0.5377 0.6191 -0.0587 -0.0100 0.0587  129 LEU A CB  
1022 C CG  . LEU A 129 ? 0.6087 0.6460 0.7258 -0.0653 -0.0120 0.0604  129 LEU A CG  
1023 C CD1 . LEU A 129 ? 0.6472 0.6996 0.7758 -0.0681 -0.0095 0.0688  129 LEU A CD1 
1024 C CD2 . LEU A 129 ? 0.6255 0.6511 0.7444 -0.0704 -0.0162 0.0595  129 LEU A CD2 
1025 N N   . GLU A 130 ? 0.5390 0.5756 0.6309 -0.0359 0.0001  0.0515  130 GLU A N   
1026 C CA  . GLU A 130 ? 0.6074 0.6325 0.6761 -0.0270 0.0035  0.0454  130 GLU A CA  
1027 C C   . GLU A 130 ? 0.6673 0.7126 0.7358 -0.0175 0.0109  0.0513  130 GLU A C   
1028 O O   . GLU A 130 ? 0.6238 0.6664 0.6757 -0.0142 0.0127  0.0488  130 GLU A O   
1029 C CB  . GLU A 130 ? 0.6120 0.6172 0.6678 -0.0182 0.0051  0.0393  130 GLU A CB  
1030 C CG  . GLU A 130 ? 0.6099 0.6044 0.6410 -0.0043 0.0114  0.0346  130 GLU A CG  
1031 C CD  . GLU A 130 ? 0.7772 0.7376 0.7851 0.0003  0.0109  0.0251  130 GLU A CD  
1032 O OE1 . GLU A 130 ? 0.6822 0.6344 0.6972 -0.0008 0.0093  0.0251  130 GLU A OE1 
1033 O OE2 . GLU A 130 ? 0.9093 0.8493 0.8899 0.0052  0.0122  0.0175  130 GLU A OE2 
1034 N N   . ARG A 131 ? 0.6423 0.7096 0.7292 -0.0131 0.0149  0.0600  131 ARG A N   
1035 C CA  . ARG A 131 ? 0.6941 0.7840 0.7831 -0.0033 0.0229  0.0679  131 ARG A CA  
1036 C C   . ARG A 131 ? 0.6596 0.7617 0.7536 -0.0105 0.0230  0.0733  131 ARG A C   
1037 O O   . ARG A 131 ? 0.7059 0.8142 0.7874 -0.0020 0.0287  0.0750  131 ARG A O   
1038 C CB  . ARG A 131 ? 0.6909 0.8068 0.8034 -0.0005 0.0258  0.0783  131 ARG A CB  
1039 C CG  . ARG A 131 ? 0.7373 0.8457 0.8475 0.0074  0.0258  0.0751  131 ARG A CG  
1040 C CD  . ARG A 131 ? 0.9240 1.0641 1.0503 0.0172  0.0320  0.0869  131 ARG A CD  
1041 N NE  . ARG A 131 ? 1.0258 1.1625 1.1484 0.0287  0.0337  0.0856  131 ARG A NE  
1042 C CZ  . ARG A 131 ? 1.1003 1.2171 1.1977 0.0453  0.0399  0.0797  131 ARG A CZ  
1043 N NH1 . ARG A 131 ? 1.1382 1.2337 1.2093 0.0512  0.0436  0.0724  131 ARG A NH1 
1044 N NH2 . ARG A 131 ? 1.0216 1.1380 1.1181 0.0565  0.0421  0.0809  131 ARG A NH2 
1045 N N   . ALA A 132 ? 0.5895 0.6940 0.6999 -0.0246 0.0174  0.0764  132 ALA A N   
1046 C CA  . ALA A 132 ? 0.6165 0.7328 0.7336 -0.0309 0.0183  0.0835  132 ALA A CA  
1047 C C   . ALA A 132 ? 0.6812 0.7844 0.7783 -0.0321 0.0157  0.0772  132 ALA A C   
1048 O O   . ALA A 132 ? 0.6202 0.7350 0.7138 -0.0300 0.0193  0.0825  132 ALA A O   
1049 C CB  . ALA A 132 ? 0.5787 0.6975 0.7166 -0.0442 0.0136  0.0887  132 ALA A CB  
1050 N N   . LEU A 133 ? 0.5984 0.6797 0.6836 -0.0362 0.0092  0.0671  133 LEU A N   
1051 C CA  . LEU A 133 ? 0.6205 0.6925 0.6897 -0.0405 0.0047  0.0621  133 LEU A CA  
1052 C C   . LEU A 133 ? 0.5962 0.6528 0.6367 -0.0326 0.0047  0.0520  133 LEU A C   
1053 O O   . LEU A 133 ? 0.5872 0.6394 0.6121 -0.0357 0.0006  0.0480  133 LEU A O   
1054 C CB  . LEU A 133 ? 0.6378 0.6975 0.7124 -0.0519 -0.0031 0.0591  133 LEU A CB  
1055 C CG  . LEU A 133 ? 0.6476 0.7155 0.7449 -0.0588 -0.0035 0.0675  133 LEU A CG  
1056 C CD1 . LEU A 133 ? 0.5747 0.6336 0.6736 -0.0673 -0.0096 0.0664  133 LEU A CD1 
1057 C CD2 . LEU A 133 ? 0.6946 0.7810 0.8008 -0.0584 0.0012  0.0778  133 LEU A CD2 
1058 N N   . GLY A 134 ? 0.6334 0.6811 0.6650 -0.0222 0.0090  0.0478  134 GLY A N   
1059 C CA  . GLY A 134 ? 0.5733 0.6000 0.5730 -0.0133 0.0097  0.0373  134 GLY A CA  
1060 C C   . GLY A 134 ? 0.6405 0.6388 0.6237 -0.0231 0.0004  0.0259  134 GLY A C   
1061 O O   . GLY A 134 ? 0.6229 0.6056 0.5792 -0.0231 -0.0031 0.0174  134 GLY A O   
1062 N N   . ILE A 135 ? 0.6296 0.6211 0.6278 -0.0321 -0.0040 0.0258  135 ILE A N   
1063 C CA  . ILE A 135 ? 0.6803 0.6481 0.6685 -0.0432 -0.0126 0.0178  135 ILE A CA  
1064 C C   . ILE A 135 ? 0.6929 0.6448 0.6849 -0.0400 -0.0109 0.0158  135 ILE A C   
1065 O O   . ILE A 135 ? 0.6703 0.6370 0.6837 -0.0368 -0.0071 0.0229  135 ILE A O   
1066 C CB  . ILE A 135 ? 0.6989 0.6799 0.7044 -0.0581 -0.0197 0.0232  135 ILE A CB  
1067 C CG1 . ILE A 135 ? 0.7908 0.7846 0.8243 -0.0601 -0.0177 0.0317  135 ILE A CG1 
1068 C CG2 . ILE A 135 ? 0.6341 0.6364 0.6400 -0.0585 -0.0194 0.0284  135 ILE A CG2 
1069 C CD1 . ILE A 135 ? 0.7420 0.7546 0.7937 -0.0691 -0.0206 0.0405  135 ILE A CD1 
1070 N N   . PRO A 136 ? 0.7156 0.6370 0.6866 -0.0406 -0.0134 0.0065  136 PRO A N   
1071 C CA  . PRO A 136 ? 0.6896 0.5954 0.6612 -0.0336 -0.0096 0.0055  136 PRO A CA  
1072 C C   . PRO A 136 ? 0.6607 0.5679 0.6530 -0.0448 -0.0144 0.0096  136 PRO A C   
1073 O O   . PRO A 136 ? 0.6598 0.5431 0.6438 -0.0510 -0.0181 0.0052  136 PRO A O   
1074 C CB  . PRO A 136 ? 0.7400 0.6079 0.6768 -0.0300 -0.0102 -0.0061 136 PRO A CB  
1075 C CG  . PRO A 136 ? 0.7727 0.6345 0.6998 -0.0464 -0.0203 -0.0111 136 PRO A CG  
1076 C CD  . PRO A 136 ? 0.7765 0.6745 0.7216 -0.0490 -0.0208 -0.0032 136 PRO A CD  
1077 N N   . VAL A 137 ? 0.5341 0.4685 0.5525 -0.0476 -0.0141 0.0185  137 VAL A N   
1078 C CA  . VAL A 137 ? 0.5842 0.5215 0.6205 -0.0564 -0.0180 0.0230  137 VAL A CA  
1079 C C   . VAL A 137 ? 0.6356 0.5666 0.6774 -0.0485 -0.0145 0.0242  137 VAL A C   
1080 O O   . VAL A 137 ? 0.6452 0.5751 0.6981 -0.0536 -0.0170 0.0274  137 VAL A O   
1081 C CB  . VAL A 137 ? 0.6123 0.5755 0.6701 -0.0617 -0.0191 0.0314  137 VAL A CB  
1082 C CG1 . VAL A 137 ? 0.5720 0.5417 0.6263 -0.0702 -0.0232 0.0319  137 VAL A CG1 
1083 C CG2 . VAL A 137 ? 0.6047 0.5877 0.6730 -0.0531 -0.0135 0.0363  137 VAL A CG2 
1084 N N   . THR A 138 ? 0.6432 0.5721 0.6770 -0.0348 -0.0083 0.0228  138 THR A N   
1085 C CA  . THR A 138 ? 0.5702 0.4914 0.6055 -0.0261 -0.0051 0.0238  138 THR A CA  
1086 C C   . THR A 138 ? 0.6904 0.5787 0.7086 -0.0286 -0.0066 0.0180  138 THR A C   
1087 O O   . THR A 138 ? 0.6394 0.5211 0.6646 -0.0305 -0.0077 0.0205  138 THR A O   
1088 C CB  . THR A 138 ? 0.6256 0.5549 0.6561 -0.0093 0.0027  0.0253  138 THR A CB  
1089 O OG1 . THR A 138 ? 0.7576 0.7188 0.8055 -0.0090 0.0038  0.0320  138 THR A OG1 
1090 C CG2 . THR A 138 ? 0.7297 0.6564 0.7643 0.0005  0.0057  0.0282  138 THR A CG2 
1091 N N   . ARG A 139 ? 0.6092 0.4753 0.6038 -0.0290 -0.0068 0.0104  139 ARG A N   
1092 C CA  . ARG A 139 ? 0.6867 0.5172 0.6625 -0.0340 -0.0091 0.0044  139 ARG A CA  
1093 C C   . ARG A 139 ? 0.6911 0.5205 0.6744 -0.0539 -0.0180 0.0050  139 ARG A C   
1094 O O   . ARG A 139 ? 0.6782 0.4880 0.6594 -0.0610 -0.0204 0.0051  139 ARG A O   
1095 C CB  . ARG A 139 ? 0.6508 0.4541 0.5941 -0.0266 -0.0063 -0.0050 139 ARG A CB  
1096 C CG  . ARG A 139 ? 0.7873 0.5543 0.7085 -0.0397 -0.0128 -0.0133 139 ARG A CG  
1097 C CD  . ARG A 139 ? 1.0629 0.7889 0.9595 -0.0297 -0.0074 -0.0183 139 ARG A CD  
1098 N NE  . ARG A 139 ? 1.1969 0.8892 1.0796 -0.0471 -0.0150 -0.0237 139 ARG A NE  
1099 C CZ  . ARG A 139 ? 1.2446 0.9048 1.0967 -0.0538 -0.0197 -0.0345 139 ARG A CZ  
1100 N NH1 . ARG A 139 ? 1.2164 0.8695 1.0442 -0.0414 -0.0161 -0.0418 139 ARG A NH1 
1101 N NH2 . ARG A 139 ? 1.2624 0.8973 1.1075 -0.0738 -0.0285 -0.0377 139 ARG A NH2 
1102 N N   . LYS A 140 ? 0.6177 0.4695 0.6107 -0.0626 -0.0225 0.0070  140 LYS A N   
1103 C CA  . LYS A 140 ? 0.7316 0.5876 0.7326 -0.0802 -0.0307 0.0094  140 LYS A CA  
1104 C C   . LYS A 140 ? 0.6548 0.5436 0.6821 -0.0824 -0.0310 0.0189  140 LYS A C   
1105 O O   . LYS A 140 ? 0.6448 0.5521 0.6768 -0.0871 -0.0337 0.0210  140 LYS A O   
1106 C CB  . LYS A 140 ? 0.7346 0.5834 0.7175 -0.0892 -0.0369 0.0026  140 LYS A CB  
1107 C CG  . LYS A 140 ? 0.7504 0.5677 0.7006 -0.0817 -0.0349 -0.0087 140 LYS A CG  
1108 C CD  . LYS A 140 ? 0.8596 0.6551 0.7894 -0.0979 -0.0448 -0.0164 140 LYS A CD  
1109 C CE  . LYS A 140 ? 0.8960 0.6772 0.8341 -0.1127 -0.0501 -0.0132 140 LYS A CE  
1110 N NZ  . LYS A 140 ? 1.0539 0.8167 0.9769 -0.1329 -0.0616 -0.0187 140 LYS A NZ  
1111 N N   . PRO A 141 ? 0.5802 0.4750 0.6229 -0.0783 -0.0282 0.0248  141 PRO A N   
1112 C CA  . PRO A 141 ? 0.5551 0.4759 0.6182 -0.0788 -0.0281 0.0327  141 PRO A CA  
1113 C C   . PRO A 141 ? 0.6294 0.5603 0.7016 -0.0907 -0.0331 0.0384  141 PRO A C   
1114 O O   . PRO A 141 ? 0.5859 0.5366 0.6697 -0.0912 -0.0329 0.0441  141 PRO A O   
1115 C CB  . PRO A 141 ? 0.5934 0.5128 0.6651 -0.0710 -0.0247 0.0360  141 PRO A CB  
1116 C CG  . PRO A 141 ? 0.6174 0.5117 0.6776 -0.0709 -0.0243 0.0330  141 PRO A CG  
1117 C CD  . PRO A 141 ? 0.5955 0.4720 0.6353 -0.0725 -0.0251 0.0247  141 PRO A CD  
1118 N N   . GLU A 142 ? 0.5869 0.5053 0.6542 -0.1005 -0.0373 0.0380  142 GLU A N   
1119 C CA  . GLU A 142 ? 0.6344 0.5676 0.7122 -0.1117 -0.0421 0.0456  142 GLU A CA  
1120 C C   . GLU A 142 ? 0.6108 0.5588 0.6856 -0.1172 -0.0461 0.0448  142 GLU A C   
1121 O O   . GLU A 142 ? 0.5857 0.5508 0.6700 -0.1253 -0.0499 0.0524  142 GLU A O   
1122 C CB  . GLU A 142 ? 0.6157 0.5342 0.6909 -0.1228 -0.0463 0.0467  142 GLU A CB  
1123 C CG  . GLU A 142 ? 0.6215 0.5212 0.6774 -0.1328 -0.0525 0.0377  142 GLU A CG  
1124 C CD  . GLU A 142 ? 0.7053 0.5761 0.7402 -0.1235 -0.0487 0.0266  142 GLU A CD  
1125 O OE1 . GLU A 142 ? 0.6275 0.4957 0.6655 -0.1099 -0.0414 0.0271  142 GLU A OE1 
1126 O OE2 . GLU A 142 ? 0.7537 0.6041 0.7677 -0.1295 -0.0531 0.0177  142 GLU A OE2 
1127 N N   . LEU A 143 ? 0.6454 0.5896 0.7070 -0.1117 -0.0448 0.0373  143 LEU A N   
1128 C CA  . LEU A 143 ? 0.6145 0.5755 0.6734 -0.1149 -0.0477 0.0380  143 LEU A CA  
1129 C C   . LEU A 143 ? 0.6488 0.6348 0.7252 -0.1104 -0.0440 0.0476  143 LEU A C   
1130 O O   . LEU A 143 ? 0.5739 0.5769 0.6512 -0.1129 -0.0459 0.0514  143 LEU A O   
1131 C CB  . LEU A 143 ? 0.5915 0.5429 0.6309 -0.1079 -0.0458 0.0286  143 LEU A CB  
1132 C CG  . LEU A 143 ? 0.6730 0.5949 0.6873 -0.1105 -0.0491 0.0173  143 LEU A CG  
1133 C CD1 . LEU A 143 ? 0.6792 0.5936 0.6746 -0.0979 -0.0440 0.0099  143 LEU A CD1 
1134 C CD2 . LEU A 143 ? 0.7365 0.6559 0.7423 -0.1269 -0.0597 0.0152  143 LEU A CD2 
1135 N N   . LEU A 144 ? 0.5502 0.5370 0.6383 -0.1034 -0.0389 0.0517  144 LEU A N   
1136 C CA  . LEU A 144 ? 0.6057 0.6099 0.7071 -0.1000 -0.0357 0.0603  144 LEU A CA  
1137 C C   . LEU A 144 ? 0.6008 0.6157 0.7125 -0.1050 -0.0376 0.0700  144 LEU A C   
1138 O O   . LEU A 144 ? 0.6022 0.6291 0.7223 -0.1011 -0.0345 0.0780  144 LEU A O   
1139 C CB  . LEU A 144 ? 0.6155 0.6151 0.7229 -0.0915 -0.0307 0.0602  144 LEU A CB  
1140 C CG  . LEU A 144 ? 0.6080 0.6057 0.7103 -0.0851 -0.0276 0.0546  144 LEU A CG  
1141 C CD1 . LEU A 144 ? 0.6356 0.6374 0.7482 -0.0800 -0.0243 0.0578  144 LEU A CD1 
1142 C CD2 . LEU A 144 ? 0.6103 0.6189 0.7074 -0.0856 -0.0272 0.0547  144 LEU A CD2 
1143 N N   . GLU A 145 ? 0.5490 0.5594 0.6597 -0.1130 -0.0422 0.0704  145 GLU A N   
1144 C CA  . GLU A 145 ? 0.6249 0.6512 0.7467 -0.1181 -0.0440 0.0817  145 GLU A CA  
1145 C C   . GLU A 145 ? 0.6689 0.7149 0.7903 -0.1250 -0.0489 0.0856  145 GLU A C   
1146 O O   . GLU A 145 ? 0.6707 0.7359 0.8026 -0.1282 -0.0502 0.0970  145 GLU A O   
1147 C CB  . GLU A 145 ? 0.5201 0.5372 0.6440 -0.1254 -0.0470 0.0830  145 GLU A CB  
1148 C CG  . GLU A 145 ? 0.5753 0.5750 0.6993 -0.1172 -0.0418 0.0807  145 GLU A CG  
1149 C CD  . GLU A 145 ? 0.6998 0.6924 0.8278 -0.1230 -0.0431 0.0853  145 GLU A CD  
1150 O OE1 . GLU A 145 ? 0.7013 0.6754 0.8251 -0.1178 -0.0401 0.0812  145 GLU A OE1 
1151 O OE2 . GLU A 145 ? 0.5850 0.5922 0.7214 -0.1326 -0.0468 0.0942  145 GLU A OE2 
1152 N N   . THR A 146 ? 0.6491 0.6925 0.7583 -0.1263 -0.0514 0.0774  146 THR A N   
1153 C CA  . THR A 146 ? 0.6855 0.7486 0.7923 -0.1319 -0.0565 0.0809  146 THR A CA  
1154 C C   . THR A 146 ? 0.6706 0.7523 0.7853 -0.1225 -0.0504 0.0902  146 THR A C   
1155 O O   . THR A 146 ? 0.5869 0.6614 0.7040 -0.1127 -0.0430 0.0901  146 THR A O   
1156 C CB  . THR A 146 ? 0.6720 0.7240 0.7592 -0.1352 -0.0612 0.0686  146 THR A CB  
1157 O OG1 . THR A 146 ? 0.6432 0.6879 0.7247 -0.1235 -0.0539 0.0636  146 THR A OG1 
1158 C CG2 . THR A 146 ? 0.6977 0.7248 0.7738 -0.1436 -0.0663 0.0590  146 THR A CG2 
1159 N N   . GLN A 147 ? 0.4598 0.8837 0.6772 0.1459  0.1004  0.0930  147 GLN A N   
1160 C CA  . GLN A 147 ? 0.4975 0.8872 0.6962 0.1610  0.0882  0.0972  147 GLN A CA  
1161 C C   . GLN A 147 ? 0.4826 0.8297 0.6455 0.1439  0.0813  0.0999  147 GLN A C   
1162 O O   . GLN A 147 ? 0.5074 0.8130 0.6457 0.1505  0.0800  0.0988  147 GLN A O   
1163 C CB  . GLN A 147 ? 0.4828 0.8983 0.7023 0.1750  0.0738  0.1063  147 GLN A CB  
1164 C CG  . GLN A 147 ? 0.4734 0.9330 0.7306 0.1936  0.0799  0.1061  147 GLN A CG  
1165 C CD  . GLN A 147 ? 0.6175 1.0851 0.8854 0.2177  0.0675  0.1155  147 GLN A CD  
1166 O OE1 . GLN A 147 ? 0.7170 1.1868 0.9810 0.2128  0.0511  0.1239  147 GLN A OE1 
1167 N NE2 . GLN A 147 ? 0.5339 1.0034 0.8120 0.2448  0.0752  0.1147  147 GLN A NE2 
1168 N N   . ALA A 148 ? 0.5456 0.9010 0.7042 0.1215  0.0778  0.1036  148 ALA A N   
1169 C CA  . ALA A 148 ? 0.5212 0.8394 0.6473 0.1067  0.0701  0.1089  148 ALA A CA  
1170 C C   . ALA A 148 ? 0.5215 0.8075 0.6236 0.0964  0.0816  0.1040  148 ALA A C   
1171 O O   . ALA A 148 ? 0.5019 0.7474 0.5784 0.0968  0.0768  0.1065  148 ALA A O   
1172 C CB  . ALA A 148 ? 0.6444 0.9804 0.7709 0.0863  0.0649  0.1137  148 ALA A CB  
1173 N N   . LEU A 149 ? 0.5820 0.8860 0.6921 0.0869  0.0972  0.0975  149 LEU A N   
1174 C CA  . LEU A 149 ? 0.5523 0.8299 0.6402 0.0768  0.1073  0.0939  149 LEU A CA  
1175 C C   . LEU A 149 ? 0.4749 0.7421 0.5633 0.0926  0.1141  0.0851  149 LEU A C   
1176 O O   . LEU A 149 ? 0.5991 0.8355 0.6651 0.0871  0.1169  0.0826  149 LEU A O   
1177 C CB  . LEU A 149 ? 0.5311 0.8289 0.6216 0.0582  0.1216  0.0927  149 LEU A CB  
1178 C CG  . LEU A 149 ? 0.6471 0.9468 0.7293 0.0406  0.1160  0.1010  149 LEU A CG  
1179 C CD1 . LEU A 149 ? 0.7113 1.0267 0.7928 0.0234  0.1329  0.1001  149 LEU A CD1 
1180 C CD2 . LEU A 149 ? 0.6410 0.9006 0.6926 0.0331  0.1059  0.1090  149 LEU A CD2 
1181 N N   . GLY A 150 ? 0.4709 0.7625 0.5834 0.1120  0.1168  0.0806  150 GLY A N   
1182 C CA  . GLY A 150 ? 0.5686 0.8437 0.6769 0.1302  0.1216  0.0726  150 GLY A CA  
1183 C C   . GLY A 150 ? 0.5709 0.8009 0.6557 0.1386  0.1098  0.0749  150 GLY A C   
1184 O O   . GLY A 150 ? 0.5580 0.7545 0.6213 0.1385  0.1127  0.0690  150 GLY A O   
1185 N N   . ALA A 151 ? 0.5707 0.7989 0.6586 0.1453  0.0963  0.0839  151 ALA A N   
1186 C CA  . ALA A 151 ? 0.6146 0.7980 0.6789 0.1531  0.0858  0.0880  151 ALA A CA  
1187 C C   . ALA A 151 ? 0.5770 0.7234 0.6118 0.1317  0.0843  0.0898  151 ALA A C   
1188 O O   . ALA A 151 ? 0.6062 0.7111 0.6185 0.1338  0.0837  0.0868  151 ALA A O   
1189 C CB  . ALA A 151 ? 0.5829 0.7758 0.6558 0.1628  0.0718  0.0991  151 ALA A CB  
1190 N N   . LEU A 152 ? 0.5529 0.7126 0.5866 0.1107  0.0841  0.0952  152 LEU A N   
1191 C CA  . LEU A 152 ? 0.6268 0.7541 0.6339 0.0910  0.0834  0.0993  152 LEU A CA  
1192 C C   . LEU A 152 ? 0.6136 0.7296 0.6110 0.0831  0.0948  0.0902  152 LEU A C   
1193 O O   . LEU A 152 ? 0.6017 0.6803 0.5763 0.0754  0.0929  0.0907  152 LEU A O   
1194 C CB  . LEU A 152 ? 0.6081 0.7535 0.6155 0.0721  0.0827  0.1074  152 LEU A CB  
1195 C CG  . LEU A 152 ? 0.7050 0.8197 0.6866 0.0564  0.0767  0.1181  152 LEU A CG  
1196 C CD1 . LEU A 152 ? 0.6725 0.7616 0.6439 0.0681  0.0620  0.1260  152 LEU A CD1 
1197 C CD2 . LEU A 152 ? 0.6355 0.7717 0.6175 0.0392  0.0795  0.1242  152 LEU A CD2 
1198 N N   . ALA A 153 ? 0.5275 0.6762 0.5424 0.0852  0.1066  0.0820  153 ALA A N   
1199 C CA  . ALA A 153 ? 0.6494 0.7930 0.6561 0.0792  0.1176  0.0730  153 ALA A CA  
1200 C C   . ALA A 153 ? 0.6481 0.7639 0.6453 0.0953  0.1162  0.0637  153 ALA A C   
1201 O O   . ALA A 153 ? 0.5921 0.6807 0.5694 0.0869  0.1177  0.0587  153 ALA A O   
1202 C CB  . ALA A 153 ? 0.5014 0.6888 0.5292 0.0789  0.1316  0.0679  153 ALA A CB  
1203 N N   . ALA A 154 ? 0.5808 0.7042 0.5918 0.1186  0.1141  0.0612  154 ALA A N   
1204 C CA  . ALA A 154 ? 0.6216 0.7113 0.6194 0.1365  0.1122  0.0539  154 ALA A CA  
1205 C C   . ALA A 154 ? 0.6670 0.7053 0.6367 0.1292  0.1022  0.0582  154 ALA A C   
1206 O O   . ALA A 154 ? 0.6720 0.6748 0.6203 0.1270  0.1033  0.0503  154 ALA A O   
1207 C CB  . ALA A 154 ? 0.6163 0.7222 0.6334 0.1633  0.1104  0.0554  154 ALA A CB  
1208 N N   . ALA A 155 ? 0.6477 0.6805 0.6163 0.1249  0.0924  0.0705  155 ALA A N   
1209 C CA  . ALA A 155 ? 0.7045 0.6878 0.6469 0.1190  0.0840  0.0758  155 ALA A CA  
1210 C C   . ALA A 155 ? 0.7181 0.6853 0.6435 0.0925  0.0865  0.0757  155 ALA A C   
1211 O O   . ALA A 155 ? 0.7329 0.6574 0.6360 0.0870  0.0842  0.0730  155 ALA A O   
1212 C CB  . ALA A 155 ? 0.6904 0.6729 0.6347 0.1221  0.0733  0.0900  155 ALA A CB  
1213 N N   . LYS A 156 ? 0.6528 0.6531 0.5881 0.0757  0.0917  0.0791  156 LYS A N   
1214 C CA  . LYS A 156 ? 0.7681 0.7575 0.6889 0.0519  0.0952  0.0804  156 LYS A CA  
1215 C C   . LYS A 156 ? 0.7455 0.7266 0.6589 0.0506  0.1017  0.0667  156 LYS A C   
1216 O O   . LYS A 156 ? 0.8031 0.7572 0.6983 0.0351  0.1003  0.0660  156 LYS A O   
1217 C CB  . LYS A 156 ? 0.8098 0.8363 0.7412 0.0364  0.1019  0.0873  156 LYS A CB  
1218 C CG  . LYS A 156 ? 0.8173 0.8427 0.7382 0.0162  0.1093  0.0862  156 LYS A CG  
1219 C CD  . LYS A 156 ? 0.7549 0.8049 0.6781 -0.0013 0.1164  0.0964  156 LYS A CD  
1220 C CE  . LYS A 156 ? 0.8167 0.8723 0.7330 -0.0163 0.1251  0.0933  156 LYS A CE  
1221 N NZ  . LYS A 156 ? 0.6433 0.6628 0.5395 -0.0317 0.1189  0.0992  156 LYS A NZ  
1222 N N   . PHE A 157 ? 0.7119 0.7161 0.6388 0.0664  0.1085  0.0559  157 PHE A N   
1223 C CA  . PHE A 157 ? 0.7132 0.7091 0.6305 0.0667  0.1143  0.0421  157 PHE A CA  
1224 C C   . PHE A 157 ? 0.7266 0.6686 0.6198 0.0714  0.1070  0.0361  157 PHE A C   
1225 O O   . PHE A 157 ? 0.8148 0.7349 0.6901 0.0587  0.1072  0.0287  157 PHE A O   
1226 C CB  . PHE A 157 ? 0.7923 0.8219 0.7284 0.0860  0.1236  0.0328  157 PHE A CB  
1227 C CG  . PHE A 157 ? 0.7676 0.7900 0.6925 0.0896  0.1300  0.0179  157 PHE A CG  
1228 C CD1 . PHE A 157 ? 0.7456 0.7273 0.6519 0.1029  0.1262  0.0081  157 PHE A CD1 
1229 C CD2 . PHE A 157 ? 0.7369 0.7933 0.6689 0.0812  0.1405  0.0136  157 PHE A CD2 
1230 C CE1 . PHE A 157 ? 0.7918 0.7654 0.6850 0.1061  0.1315  -0.0064 157 PHE A CE1 
1231 C CE2 . PHE A 157 ? 0.7521 0.8037 0.6728 0.0852  0.1458  -0.0001 157 PHE A CE2 
1232 C CZ  . PHE A 157 ? 0.7790 0.7888 0.6796 0.0973  0.1408  -0.0107 157 PHE A CZ  
1233 N N   . TRP A 158 ? 0.7234 0.6436 0.6151 0.0896  0.1009  0.0394  158 TRP A N   
1234 C CA  . TRP A 158 ? 0.8185 0.6829 0.6853 0.0956  0.0954  0.0347  158 TRP A CA  
1235 C C   . TRP A 158 ? 0.8808 0.7111 0.7291 0.0725  0.0885  0.0429  158 TRP A C   
1236 O O   . TRP A 158 ? 0.8709 0.6604 0.6967 0.0633  0.0865  0.0359  158 TRP A O   
1237 C CB  . TRP A 158 ? 0.8020 0.6554 0.6732 0.1232  0.0921  0.0387  158 TRP A CB  
1238 C CG  . TRP A 158 ? 0.9533 0.7464 0.7978 0.1333  0.0882  0.0354  158 TRP A CG  
1239 C CD1 . TRP A 158 ? 1.0004 0.7523 0.8280 0.1272  0.0808  0.0447  158 TRP A CD1 
1240 C CD2 . TRP A 158 ? 0.9283 0.6930 0.7582 0.1526  0.0930  0.0221  158 TRP A CD2 
1241 N NE1 . TRP A 158 ? 1.1000 0.7990 0.9037 0.1407  0.0810  0.0379  158 TRP A NE1 
1242 C CE2 . TRP A 158 ? 1.0913 0.7962 0.8949 0.1564  0.0883  0.0238  158 TRP A CE2 
1243 C CE3 . TRP A 158 ? 0.9747 0.7570 0.8096 0.1676  0.1016  0.0093  158 TRP A CE3 
1244 C CZ2 . TRP A 158 ? 1.1311 0.7915 0.9117 0.1741  0.0923  0.0125  158 TRP A CZ2 
1245 C CZ3 . TRP A 158 ? 1.0879 0.8268 0.8998 0.1860  0.1050  -0.0018 158 TRP A CZ3 
1246 C CH2 . TRP A 158 ? 1.0982 0.7762 0.8826 0.1888  0.1004  -0.0004 158 TRP A CH2 
1247 N N   . TYR A 159 ? 0.8134 0.6599 0.6706 0.0625  0.0851  0.0577  159 TYR A N   
1248 C CA  . TYR A 159 ? 0.8806 0.7014 0.7232 0.0403  0.0802  0.0680  159 TYR A CA  
1249 C C   . TYR A 159 ? 0.8673 0.6915 0.7030 0.0163  0.0840  0.0628  159 TYR A C   
1250 O O   . TYR A 159 ? 0.8262 0.6141 0.6437 0.0006  0.0801  0.0639  159 TYR A O   
1251 C CB  . TYR A 159 ? 0.8571 0.7034 0.7117 0.0353  0.0780  0.0839  159 TYR A CB  
1252 C CG  . TYR A 159 ? 0.8423 0.6722 0.6850 0.0125  0.0754  0.0965  159 TYR A CG  
1253 C CD1 . TYR A 159 ? 0.9376 0.7206 0.7623 0.0110  0.0686  0.1042  159 TYR A CD1 
1254 C CD2 . TYR A 159 ? 0.8592 0.7209 0.7089 -0.0061 0.0810  0.1026  159 TYR A CD2 
1255 C CE1 . TYR A 159 ? 0.9586 0.7280 0.7739 -0.0091 0.0671  0.1174  159 TYR A CE1 
1256 C CE2 . TYR A 159 ? 0.8691 0.7173 0.7085 -0.0253 0.0798  0.1162  159 TYR A CE2 
1257 C CZ  . TYR A 159 ? 0.9053 0.7084 0.7283 -0.0270 0.0727  0.1235  159 TYR A CZ  
1258 O OH  . TYR A 159 ? 1.0041 0.7946 0.8178 -0.0457 0.0724  0.1381  159 TYR A OH  
1259 N N   . ASP A 160 ? 0.8120 0.6813 0.6626 0.0126  0.0919  0.0585  160 ASP A N   
1260 C CA  . ASP A 160 ? 0.9139 0.7917 0.7588 -0.0080 0.0959  0.0538  160 ASP A CA  
1261 C C   . ASP A 160 ? 0.9295 0.7715 0.7553 -0.0080 0.0933  0.0384  160 ASP A C   
1262 O O   . ASP A 160 ? 0.9220 0.7467 0.7344 -0.0291 0.0906  0.0374  160 ASP A O   
1263 C CB  . ASP A 160 ? 0.9023 0.8341 0.7658 -0.0068 0.1065  0.0508  160 ASP A CB  
1264 C CG  . ASP A 160 ? 0.8772 0.8415 0.7551 -0.0133 0.1102  0.0659  160 ASP A CG  
1265 O OD1 . ASP A 160 ? 0.7365 0.6827 0.6075 -0.0231 0.1047  0.0790  160 ASP A OD1 
1266 O OD2 . ASP A 160 ? 0.8715 0.8776 0.7661 -0.0086 0.1194  0.0647  160 ASP A OD2 
1267 N N   . ASN A 161 ? 0.9044 0.7348 0.7281 0.0155  0.0943  0.0266  161 ASN A N   
1268 C CA  . ASN A 161 ? 0.9869 0.7804 0.7890 0.0173  0.0927  0.0104  161 ASN A CA  
1269 C C   . ASN A 161 ? 0.9725 0.7069 0.7514 0.0082  0.0843  0.0130  161 ASN A C   
1270 O O   . ASN A 161 ? 0.9777 0.6807 0.7363 -0.0055 0.0814  0.0029  161 ASN A O   
1271 C CB  . ASN A 161 ? 0.8439 0.6380 0.6483 0.0473  0.0974  -0.0011 161 ASN A CB  
1272 C CG  . ASN A 161 ? 1.0306 0.8648 0.8444 0.0518  0.1063  -0.0123 161 ASN A CG  
1273 O OD1 . ASN A 161 ? 1.0372 0.9007 0.8561 0.0330  0.1092  -0.0114 161 ASN A OD1 
1274 N ND2 . ASN A 161 ? 1.0998 0.9358 0.9157 0.0782  0.1117  -0.0217 161 ASN A ND2 
1275 N N   . LYS A 162 ? 0.9955 0.7136 0.7765 0.0150  0.0803  0.0264  162 LYS A N   
1276 C CA  . LYS A 162 ? 1.0791 0.7406 0.8385 0.0060  0.0737  0.0307  162 LYS A CA  
1277 C C   . LYS A 162 ? 0.9796 0.6404 0.7360 -0.0262 0.0707  0.0398  162 LYS A C   
1278 O O   . LYS A 162 ? 1.0469 0.6635 0.7836 -0.0414 0.0664  0.0373  162 LYS A O   
1279 C CB  . LYS A 162 ? 1.0810 0.7260 0.8425 0.0246  0.0708  0.0435  162 LYS A CB  
1280 C CG  . LYS A 162 ? 1.2351 0.8387 0.9818 0.0512  0.0711  0.0357  162 LYS A CG  
1281 C CD  . LYS A 162 ? 1.2865 0.8300 1.0025 0.0427  0.0700  0.0228  162 LYS A CD  
1282 C CE  . LYS A 162 ? 1.3418 0.8538 1.0444 0.0122  0.0649  0.0297  162 LYS A CE  
1283 N NZ  . LYS A 162 ? 1.4360 0.9106 1.1303 0.0162  0.0617  0.0452  162 LYS A NZ  
1284 N N   . LEU A 163 ? 0.9170 0.6254 0.6923 -0.0368 0.0736  0.0510  163 LEU A N   
1285 C CA  . LEU A 163 ? 0.9706 0.6856 0.7448 -0.0661 0.0726  0.0601  163 LEU A CA  
1286 C C   . LEU A 163 ? 1.0005 0.7109 0.7643 -0.0830 0.0721  0.0460  163 LEU A C   
1287 O O   . LEU A 163 ? 0.9580 0.6398 0.7091 -0.1050 0.0672  0.0481  163 LEU A O   
1288 C CB  . LEU A 163 ? 0.8656 0.6350 0.6603 -0.0710 0.0784  0.0725  163 LEU A CB  
1289 C CG  . LEU A 163 ? 1.0390 0.8150 0.8426 -0.0574 0.0779  0.0865  163 LEU A CG  
1290 C CD1 . LEU A 163 ? 0.9628 0.7850 0.7813 -0.0668 0.0840  0.0994  163 LEU A CD1 
1291 C CD2 . LEU A 163 ? 0.9937 0.7209 0.7825 -0.0595 0.0709  0.0973  163 LEU A CD2 
1292 N N   . THR A 164 ? 0.9690 0.7086 0.7383 -0.0734 0.0769  0.0318  164 THR A N   
1293 C CA  . THR A 164 ? 1.0020 0.7381 0.7592 -0.0874 0.0757  0.0168  164 THR A CA  
1294 C C   . THR A 164 ? 0.9945 0.6667 0.7249 -0.0899 0.0686  0.0053  164 THR A C   
1295 O O   . THR A 164 ? 1.0150 0.6654 0.7325 -0.1150 0.0629  0.0033  164 THR A O   
1296 C CB  . THR A 164 ? 1.0261 0.7978 0.7903 -0.0709 0.0827  0.0026  164 THR A CB  
1297 O OG1 . THR A 164 ? 1.0282 0.8564 0.8169 -0.0667 0.0908  0.0129  164 THR A OG1 
1298 C CG2 . THR A 164 ? 0.9924 0.7664 0.7440 -0.0875 0.0808  -0.0111 164 THR A CG2 
1299 N N   . SER A 165 ? 1.0096 0.6505 0.7312 -0.0641 0.0692  -0.0017 165 SER A N   
1300 C CA  . SER A 165 ? 1.0755 0.6502 0.7688 -0.0627 0.0646  -0.0124 165 SER A CA  
1301 C C   . SER A 165 ? 1.1475 0.6845 0.8316 -0.0853 0.0584  -0.0002 165 SER A C   
1302 O O   . SER A 165 ? 1.1418 0.6401 0.8057 -0.1051 0.0534  -0.0086 165 SER A O   
1303 C CB  . SER A 165 ? 1.1496 0.7014 0.8386 -0.0284 0.0680  -0.0155 165 SER A CB  
1304 O OG  . SER A 165 ? 1.2197 0.7046 0.8843 -0.0268 0.0645  -0.0162 165 SER A OG  
1305 N N   . LEU A 166 ? 1.1237 0.6713 0.8221 -0.0828 0.0588  0.0196  166 LEU A N   
1306 C CA  . LEU A 166 ? 1.1537 0.6705 0.8458 -0.1035 0.0544  0.0340  166 LEU A CA  
1307 C C   . LEU A 166 ? 1.1712 0.7073 0.8668 -0.1376 0.0517  0.0366  166 LEU A C   
1308 O O   . LEU A 166 ? 1.1432 0.6404 0.8246 -0.1595 0.0468  0.0373  166 LEU A O   
1309 C CB  . LEU A 166 ? 1.0453 0.5790 0.7528 -0.0932 0.0560  0.0551  166 LEU A CB  
1310 C CG  . LEU A 166 ? 1.1171 0.6293 0.8220 -0.1128 0.0532  0.0739  166 LEU A CG  
1311 C CD1 . LEU A 166 ? 1.1735 0.6166 0.8535 -0.1213 0.0494  0.0696  166 LEU A CD1 
1312 C CD2 . LEU A 166 ? 1.1461 0.6704 0.8614 -0.0959 0.0546  0.0919  166 LEU A CD2 
1313 N N   . ALA A 167 ? 1.0927 0.6894 0.8075 -0.1428 0.0554  0.0390  167 ALA A N   
1314 C CA  . ALA A 167 ? 1.1572 0.7794 0.8783 -0.1736 0.0537  0.0456  167 ALA A CA  
1315 C C   . ALA A 167 ? 1.2233 0.8253 0.9274 -0.1922 0.0479  0.0275  167 ALA A C   
1316 O O   . ALA A 167 ? 1.2142 0.8212 0.9192 -0.2213 0.0438  0.0334  167 ALA A O   
1317 C CB  . ALA A 167 ? 1.1174 0.8085 0.8612 -0.1719 0.0608  0.0525  167 ALA A CB  
1318 N N   . LEU A 168 ? 1.1945 0.7739 0.8827 -0.1763 0.0473  0.0062  168 LEU A N   
1319 C CA  . LEU A 168 ? 1.2398 0.7933 0.9070 -0.1940 0.0409  -0.0124 168 LEU A CA  
1320 C C   . LEU A 168 ? 1.3338 0.8148 0.9773 -0.2058 0.0348  -0.0150 168 LEU A C   
1321 O O   . LEU A 168 ? 1.4324 0.8962 1.0657 -0.2356 0.0277  -0.0190 168 LEU A O   
1322 C CB  . LEU A 168 ? 1.2183 0.7762 0.8751 -0.1721 0.0439  -0.0344 168 LEU A CB  
1323 C CG  . LEU A 168 ? 1.1859 0.8131 0.8654 -0.1583 0.0516  -0.0329 168 LEU A CG  
1324 C CD1 . LEU A 168 ? 1.1204 0.7522 0.7866 -0.1452 0.0534  -0.0556 168 LEU A CD1 
1325 C CD2 . LEU A 168 ? 1.2294 0.9109 0.9295 -0.1823 0.0520  -0.0179 168 LEU A CD2 
1326 N N   . ASP A 169 ? 1.3269 0.7657 0.9617 -0.1835 0.0376  -0.0118 169 ASP A N   
1327 C CA  . ASP A 169 ? 1.4147 0.7812 1.0257 -0.1925 0.0338  -0.0131 169 ASP A CA  
1328 C C   . ASP A 169 ? 1.4865 0.8505 1.1050 -0.2258 0.0293  0.0037  169 ASP A C   
1329 O O   . ASP A 169 ? 1.5891 0.9058 1.1892 -0.2487 0.0239  -0.0020 169 ASP A O   
1330 C CB  . ASP A 169 ? 1.4093 0.7408 1.0149 -0.1617 0.0388  -0.0062 169 ASP A CB  
1331 C CG  . ASP A 169 ? 1.5003 0.8260 1.0964 -0.1279 0.0437  -0.0221 169 ASP A CG  
1332 O OD1 . ASP A 169 ? 1.5533 0.8349 1.1220 -0.1261 0.0429  -0.0416 169 ASP A OD1 
1333 O OD2 . ASP A 169 ? 1.4431 0.8082 1.0587 -0.1029 0.0487  -0.0146 169 ASP A OD2 
1334 N N   . ILE A 170 ? 1.4292 0.8427 1.0743 -0.2286 0.0322  0.0250  170 ILE A N   
1335 C CA  . ILE A 170 ? 1.4884 0.9071 1.1435 -0.2586 0.0296  0.0437  170 ILE A CA  
1336 C C   . ILE A 170 ? 1.5112 0.9432 1.1641 -0.2917 0.0228  0.0343  170 ILE A C   
1337 O O   . ILE A 170 ? 1.5338 0.9340 1.1794 -0.3194 0.0174  0.0379  170 ILE A O   
1338 C CB  . ILE A 170 ? 1.3531 0.8277 1.0352 -0.2529 0.0353  0.0668  170 ILE A CB  
1339 C CG1 . ILE A 170 ? 1.3622 0.8112 1.0434 -0.2296 0.0393  0.0805  170 ILE A CG1 
1340 C CG2 . ILE A 170 ? 1.2603 0.7608 0.9560 -0.2851 0.0337  0.0838  170 ILE A CG2 
1341 C CD1 . ILE A 170 ? 1.2451 0.7456 0.9483 -0.2187 0.0450  0.0996  170 ILE A CD1 
1342 N N   . ALA A 171 ? 1.4380 0.9166 1.0969 -0.2892 0.0227  0.0220  171 ALA A N   
1343 C CA  . ALA A 171 ? 1.4886 0.9880 1.1459 -0.3186 0.0157  0.0125  171 ALA A CA  
1344 C C   . ALA A 171 ? 1.5716 1.0313 1.2000 -0.3181 0.0098  -0.0165 171 ALA A C   
1345 O O   . ALA A 171 ? 1.6255 1.1188 1.2526 -0.3227 0.0071  -0.0303 171 ALA A O   
1346 C CB  . ALA A 171 ? 1.3923 0.9713 1.0738 -0.3177 0.0199  0.0196  171 ALA A CB  
1347 N N   . GLY A 172 ? 1.5224 1.2750 1.1924 -0.2977 -0.0588 -0.0662 172 GLY A N   
1348 C CA  . GLY A 172 ? 1.5982 1.2661 1.2133 -0.3251 -0.0325 -0.0489 172 GLY A CA  
1349 C C   . GLY A 172 ? 1.6586 1.2837 1.2633 -0.3815 -0.0366 -0.0480 172 GLY A C   
1350 O O   . GLY A 172 ? 1.5635 1.1817 1.1942 -0.4039 -0.0660 -0.0562 172 GLY A O   
1351 N N   . GLY A 192 ? 1.5721 0.9082 1.2522 -0.0725 -0.1703 -0.1396 192 GLY A N   
1352 C CA  . GLY A 192 ? 1.6783 1.0327 1.3715 -0.0967 -0.1863 -0.1364 192 GLY A CA  
1353 C C   . GLY A 192 ? 1.7500 1.1185 1.4287 -0.0729 -0.1630 -0.1239 192 GLY A C   
1354 O O   . GLY A 192 ? 1.6911 1.1100 1.3910 -0.0241 -0.1642 -0.1269 192 GLY A O   
1355 N N   . LEU A 193 ? 1.7782 1.1022 1.4204 -0.1082 -0.1421 -0.1100 193 LEU A N   
1356 C CA  . LEU A 193 ? 1.7393 1.0690 1.3614 -0.0902 -0.1167 -0.0970 193 LEU A CA  
1357 C C   . LEU A 193 ? 1.7788 1.0758 1.3585 -0.0587 -0.0738 -0.0853 193 LEU A C   
1358 O O   . LEU A 193 ? 1.7843 1.0985 1.3539 -0.0289 -0.0552 -0.0769 193 LEU A O   
1359 C CB  . LEU A 193 ? 1.6967 0.9873 1.2922 -0.1392 -0.1075 -0.0860 193 LEU A CB  
1360 C CG  . LEU A 193 ? 1.6748 1.0150 1.3131 -0.1548 -0.1440 -0.0943 193 LEU A CG  
1361 C CD1 . LEU A 193 ? 1.7011 0.9949 1.3222 -0.2161 -0.1486 -0.0902 193 LEU A CD1 
1362 C CD2 . LEU A 193 ? 1.4867 0.8654 1.1286 -0.1258 -0.1334 -0.0882 193 LEU A CD2 
1363 N N   . ALA A 194 ? 1.8893 1.1383 1.4432 -0.0656 -0.0577 -0.0849 194 ALA A N   
1364 C CA  . ALA A 194 ? 1.9097 1.1336 1.4300 -0.0304 -0.0211 -0.0767 194 ALA A CA  
1365 C C   . ALA A 194 ? 1.8653 1.1516 1.4220 0.0279  -0.0343 -0.0872 194 ALA A C   
1366 O O   . ALA A 194 ? 1.8620 1.1486 1.3994 0.0669  -0.0080 -0.0797 194 ALA A O   
1367 C CB  . ALA A 194 ? 1.9546 1.1130 1.4412 -0.0543 -0.0024 -0.0754 194 ALA A CB  
1368 N N   . ARG A 195 ? 1.7640 1.1030 1.3731 0.0342  -0.0751 -0.1045 195 ARG A N   
1369 C CA  . ARG A 195 ? 1.6636 1.0674 1.3122 0.0884  -0.0915 -0.1155 195 ARG A CA  
1370 C C   . ARG A 195 ? 1.6040 1.0523 1.2615 0.1209  -0.0872 -0.1096 195 ARG A C   
1371 O O   . ARG A 195 ? 1.5806 1.0454 1.2322 0.1673  -0.0700 -0.1065 195 ARG A O   
1372 C CB  . ARG A 195 ? 1.6444 1.0964 1.3483 0.0826  -0.1385 -0.1347 195 ARG A CB  
1373 C CG  . ARG A 195 ? 1.6922 1.1450 1.4080 0.1007  -0.1453 -0.1467 195 ARG A CG  
1374 C CD  . ARG A 195 ? 1.6064 1.1191 1.3524 0.1621  -0.1514 -0.1543 195 ARG A CD  
1375 N NE  . ARG A 195 ? 1.6839 1.1973 1.4423 0.1774  -0.1589 -0.1667 195 ARG A NE  
1376 C CZ  . ARG A 195 ? 1.6765 1.1585 1.4061 0.2007  -0.1293 -0.1634 195 ARG A CZ  
1377 N NH1 . ARG A 195 ? 1.6393 1.0927 1.3288 0.2185  -0.0915 -0.1483 195 ARG A NH1 
1378 N NH2 . ARG A 195 ? 1.7236 1.2020 1.4644 0.2059  -0.1381 -0.1759 195 ARG A NH2 
1379 N N   . ARG A 196 ? 1.5909 1.0586 1.2625 0.0962  -0.1030 -0.1082 196 ARG A N   
1380 C CA  . ARG A 196 ? 1.5888 1.0941 1.2653 0.1202  -0.0972 -0.1020 196 ARG A CA  
1381 C C   . ARG A 196 ? 1.6511 1.1126 1.2728 0.1356  -0.0503 -0.0838 196 ARG A C   
1382 O O   . ARG A 196 ? 1.6109 1.1047 1.2339 0.1740  -0.0402 -0.0796 196 ARG A O   
1383 C CB  . ARG A 196 ? 1.5930 1.1078 1.2823 0.0802  -0.1155 -0.1017 196 ARG A CB  
1384 C CG  . ARG A 196 ? 1.4686 1.0482 1.1895 0.1049  -0.1296 -0.1045 196 ARG A CG  
1385 C CD  . ARG A 196 ? 1.5451 1.1115 1.2555 0.0645  -0.1288 -0.0975 196 ARG A CD  
1386 N NE  . ARG A 196 ? 1.6547 1.2701 1.3785 0.0926  -0.1274 -0.0956 196 ARG A NE  
1387 C CZ  . ARG A 196 ? 1.6747 1.2723 1.3601 0.1126  -0.0913 -0.0812 196 ARG A CZ  
1388 N NH1 . ARG A 196 ? 1.6878 1.2166 1.3171 0.1043  -0.0528 -0.0665 196 ARG A NH1 
1389 N NH2 . ARG A 196 ? 1.5022 1.1522 1.2057 0.1417  -0.0941 -0.0818 196 ARG A NH2 
1390 N N   . ARG A 197 ? 1.6581 1.0453 1.2309 0.1060  -0.0212 -0.0731 197 ARG A N   
1391 C CA  . ARG A 197 ? 1.7112 1.0519 1.2297 0.1175  0.0237  -0.0554 197 ARG A CA  
1392 C C   . ARG A 197 ? 1.7040 1.0500 1.2160 0.1684  0.0398  -0.0562 197 ARG A C   
1393 O O   . ARG A 197 ? 1.6364 0.9862 1.1279 0.2013  0.0634  -0.0463 197 ARG A O   
1394 C CB  . ARG A 197 ? 1.8119 1.0712 1.2806 0.0692  0.0496  -0.0439 197 ARG A CB  
1395 C CG  . ARG A 197 ? 1.7993 1.0443 1.2620 0.0209  0.0438  -0.0385 197 ARG A CG  
1396 C CD  . ARG A 197 ? 1.8503 1.1288 1.3142 0.0364  0.0492  -0.0312 197 ARG A CD  
1397 N NE  . ARG A 197 ? 1.9022 1.1428 1.3154 0.0547  0.0923  -0.0142 197 ARG A NE  
1398 C CZ  . ARG A 197 ? 1.8772 1.1482 1.2909 0.1046  0.1034  -0.0117 197 ARG A CZ  
1399 N NH1 . ARG A 197 ? 1.7993 1.1402 1.2617 0.1429  0.0757  -0.0250 197 ARG A NH1 
1400 N NH2 . ARG A 197 ? 1.9371 1.1674 1.3010 0.1161  0.1430  0.0047  197 ARG A NH2 
1401 N N   . GLN A 198 ? 1.6866 1.0304 1.2138 0.1748  0.0285  -0.0677 198 GLN A N   
1402 C CA  . GLN A 198 ? 1.6236 0.9761 1.1493 0.2239  0.0407  -0.0706 198 GLN A CA  
1403 C C   . GLN A 198 ? 1.5460 0.9660 1.1009 0.2747  0.0309  -0.0734 198 GLN A C   
1404 O O   . GLN A 198 ? 1.5347 0.9466 1.0622 0.3065  0.0586  -0.0626 198 GLN A O   
1405 C CB  . GLN A 198 ? 1.5839 0.9459 1.1383 0.2259  0.0185  -0.0871 198 GLN A CB  
1406 C CG  . GLN A 198 ? 1.7448 1.0379 1.2666 0.1874  0.0339  -0.0852 198 GLN A CG  
1407 C CD  . GLN A 198 ? 1.7518 1.0633 1.3103 0.1782  0.0023  -0.1034 198 GLN A CD  
1408 O OE1 . GLN A 198 ? 1.7225 1.0132 1.2736 0.1897  0.0111  -0.1093 198 GLN A OE1 
1409 N NE2 . GLN A 198 ? 1.7136 1.0658 1.3130 0.1580  -0.0353 -0.1131 198 GLN A NE2 
1410 N N   . TYR A 199 ? 1.4976 0.9838 1.1080 0.2821  -0.0089 -0.0881 199 TYR A N   
1411 C CA  . TYR A 199 ? 1.4638 1.0202 1.1080 0.3284  -0.0227 -0.0928 199 TYR A CA  
1412 C C   . TYR A 199 ? 1.4299 0.9814 1.0445 0.3371  0.0026  -0.0771 199 TYR A C   
1413 O O   . TYR A 199 ? 1.4395 1.0045 1.0434 0.3809  0.0199  -0.0719 199 TYR A O   
1414 C CB  . TYR A 199 ? 1.3370 0.9572 1.0405 0.3198  -0.0685 -0.1085 199 TYR A CB  
1415 C CG  . TYR A 199 ? 1.3012 0.9343 1.0378 0.3168  -0.0960 -0.1251 199 TYR A CG  
1416 C CD1 . TYR A 199 ? 1.2901 0.9452 1.0415 0.3602  -0.0977 -0.1336 199 TYR A CD1 
1417 C CD2 . TYR A 199 ? 1.2966 0.9200 1.0493 0.2705  -0.1207 -0.1325 199 TYR A CD2 
1418 C CE1 . TYR A 199 ? 1.2919 0.9595 1.0736 0.3571  -0.1228 -0.1492 199 TYR A CE1 
1419 C CE2 . TYR A 199 ? 1.3071 0.9421 1.0894 0.2668  -0.1465 -0.1478 199 TYR A CE2 
1420 C CZ  . TYR A 199 ? 1.2593 0.9165 1.0559 0.3100  -0.1472 -0.1562 199 TYR A CZ  
1421 O OH  . TYR A 199 ? 1.2047 0.8728 1.0299 0.3052  -0.1725 -0.1717 199 TYR A OH  
1422 N N   . ARG A 200 ? 1.4460 0.9762 1.0459 0.2946  0.0051  -0.0695 200 ARG A N   
1423 C CA  . ARG A 200 ? 1.5236 1.0546 1.1000 0.2979  0.0248  -0.0561 200 ARG A CA  
1424 C C   . ARG A 200 ? 1.5674 1.0529 1.0905 0.3220  0.0681  -0.0403 200 ARG A C   
1425 O O   . ARG A 200 ? 1.5520 1.0656 1.0723 0.3611  0.0782  -0.0356 200 ARG A O   
1426 C CB  . ARG A 200 ? 1.5082 1.0086 1.0697 0.2423  0.0250  -0.0499 200 ARG A CB  
1427 C CG  . ARG A 200 ? 1.5098 1.0184 1.0541 0.2406  0.0398  -0.0385 200 ARG A CG  
1428 C CD  . ARG A 200 ? 1.5884 1.0716 1.1243 0.1845  0.0353  -0.0349 200 ARG A CD  
1429 N NE  . ARG A 200 ? 1.6200 1.1162 1.1443 0.1813  0.0462  -0.0261 200 ARG A NE  
1430 C CZ  . ARG A 200 ? 1.7006 1.1683 1.2064 0.1366  0.0521  -0.0192 200 ARG A CZ  
1431 N NH1 . ARG A 200 ? 1.7757 1.1969 1.2697 0.0902  0.0495  -0.0189 200 ARG A NH1 
1432 N NH2 . ARG A 200 ? 1.6485 1.1345 1.1471 0.1380  0.0610  -0.0128 200 ARG A NH2 
1433 N N   . ASP A 201 ? 1.6432 1.0573 1.1232 0.2989  0.0937  -0.0321 201 ASP A N   
1434 C CA  . ASP A 201 ? 1.6957 1.0637 1.1251 0.3215  0.1343  -0.0176 201 ASP A CA  
1435 C C   . ASP A 201 ? 1.6222 1.0208 1.0678 0.3773  0.1328  -0.0247 201 ASP A C   
1436 O O   . ASP A 201 ? 1.6507 1.0499 1.0744 0.4135  0.1547  -0.0156 201 ASP A O   
1437 C CB  . ASP A 201 ? 1.7228 1.0091 1.1057 0.2839  0.1604  -0.0089 201 ASP A CB  
1438 C CG  . ASP A 201 ? 1.8163 1.0675 1.1790 0.2280  0.1647  -0.0006 201 ASP A CG  
1439 O OD1 . ASP A 201 ? 1.7369 1.0167 1.1077 0.2223  0.1585  0.0029  201 ASP A OD1 
1440 O OD2 . ASP A 201 ? 1.8845 1.0796 1.2234 0.1899  0.1743  0.0018  201 ASP A OD2 
1441 N N   . LYS A 202 ? 1.6148 1.0389 1.0985 0.3849  0.1068  -0.0411 202 LYS A N   
1442 C CA  . LYS A 202 ? 1.5762 1.0385 1.0826 0.4388  0.1007  -0.0499 202 LYS A CA  
1443 C C   . LYS A 202 ? 1.5853 1.1160 1.1205 0.4772  0.0875  -0.0517 202 LYS A C   
1444 O O   . LYS A 202 ? 1.5893 1.1349 1.1183 0.5240  0.1000  -0.0491 202 LYS A O   
1445 C CB  . LYS A 202 ? 1.5702 1.0560 1.1185 0.4370  0.0702  -0.0687 202 LYS A CB  
1446 C CG  . LYS A 202 ? 1.6078 1.0360 1.1299 0.4278  0.0877  -0.0698 202 LYS A CG  
1447 C CD  . LYS A 202 ? 1.5666 1.0252 1.1337 0.4278  0.0549  -0.0897 202 LYS A CD  
1448 C CE  . LYS A 202 ? 1.5102 0.9114 1.0523 0.4138  0.0712  -0.0920 202 LYS A CE  
1449 N NZ  . LYS A 202 ? 1.5676 0.9164 1.0894 0.3535  0.0734  -0.0890 202 LYS A NZ  
1450 N N   . ALA A 203 ? 1.5401 1.1123 1.1065 0.4577  0.0622  -0.0564 203 ALA A N   
1451 C CA  . ALA A 203 ? 1.5293 1.1638 1.1201 0.4889  0.0515  -0.0573 203 ALA A CA  
1452 C C   . ALA A 203 ? 1.6230 1.2270 1.1655 0.4913  0.0861  -0.0384 203 ALA A C   
1453 O O   . ALA A 203 ? 1.5087 1.1389 1.0475 0.5334  0.0958  -0.0343 203 ALA A O   
1454 C CB  . ALA A 203 ? 1.4054 1.0919 1.0446 0.4651  0.0140  -0.0688 203 ALA A CB  
1455 N N   . ARG A 204 ? 1.6116 1.1602 1.1163 0.4456  0.1047  -0.0267 204 ARG A N   
1456 C CA  . ARG A 204 ? 1.6492 1.1651 1.1057 0.4437  0.1381  -0.0084 204 ARG A CA  
1457 C C   . ARG A 204 ? 1.7543 1.2343 1.1696 0.4799  0.1714  0.0022  204 ARG A C   
1458 O O   . ARG A 204 ? 1.7617 1.2383 1.1489 0.5002  0.1933  0.0144  204 ARG A O   
1459 C CB  . ARG A 204 ? 1.6742 1.1322 1.0974 0.3861  0.1519  0.0012  204 ARG A CB  
1460 C CG  . ARG A 204 ? 1.7264 1.1518 1.1025 0.3748  0.1831  0.0193  204 ARG A CG  
1461 C CD  . ARG A 204 ? 1.7483 1.2355 1.1468 0.3984  0.1726  0.0181  204 ARG A CD  
1462 N NE  . ARG A 204 ? 1.7941 1.2744 1.1602 0.4395  0.2003  0.0297  204 ARG A NE  
1463 C CZ  . ARG A 204 ? 1.7949 1.2991 1.1522 0.4533  0.2088  0.0367  204 ARG A CZ  
1464 N NH1 . ARG A 204 ? 1.7438 1.2821 1.1228 0.4300  0.1926  0.0331  204 ARG A NH1 
1465 N NH2 . ARG A 204 ? 1.7332 1.2265 1.0588 0.4910  0.2340  0.0472  204 ARG A NH2 
1466 N N   . LYS A 205 ? 1.8573 1.3122 1.2700 0.4895  0.1744  -0.0029 205 LYS A N   
1467 C CA  . LYS A 205 ? 1.9095 1.3344 1.2886 0.5272  0.2027  0.0048  205 LYS A CA  
1468 C C   . LYS A 205 ? 1.8723 1.3550 1.2716 0.5821  0.1966  0.0025  205 LYS A C   
1469 O O   . LYS A 205 ? 1.9312 1.3928 1.2941 0.6100  0.2240  0.0147  205 LYS A O   
1470 C CB  . LYS A 205 ? 1.8945 1.2958 1.2793 0.5302  0.2001  -0.0047 205 LYS A CB  
1471 C CG  . LYS A 205 ? 2.0560 1.3750 1.3835 0.5169  0.2377  0.0080  205 LYS A CG  
1472 C CD  . LYS A 205 ? 2.0895 1.3854 1.4258 0.5111  0.2326  -0.0033 205 LYS A CD  
1473 C CE  . LYS A 205 ? 1.9606 1.2558 1.3213 0.4618  0.2083  -0.0130 205 LYS A CE  
1474 N NZ  . LYS A 205 ? 1.9183 1.1845 1.2818 0.4517  0.2062  -0.0231 205 LYS A NZ  
1475 N N   . HIS A 206 ? 1.6709 1.2263 1.1277 0.5981  0.1604  -0.0132 206 HIS A N   
1476 C CA  . HIS A 206 ? 1.6519 1.2688 1.1322 0.6460  0.1514  -0.0161 206 HIS A CA  
1477 C C   . HIS A 206 ? 1.6714 1.2921 1.1292 0.6394  0.1652  -0.0032 206 HIS A C   
1478 O O   . HIS A 206 ? 1.6424 1.2937 1.1241 0.6132  0.1465  -0.0073 206 HIS A O   
1479 C CB  . HIS A 206 ? 1.5839 1.2774 1.1323 0.6582  0.1081  -0.0362 206 HIS A CB  
1480 C CG  . HIS A 206 ? 1.5379 1.2552 1.1117 0.6991  0.0971  -0.0481 206 HIS A CG  
1481 N ND1 . HIS A 206 ? 1.4827 1.2760 1.1105 0.7335  0.0664  -0.0628 206 HIS A ND1 
1482 C CD2 . HIS A 206 ? 1.5905 1.2664 1.1438 0.7110  0.1127  -0.0480 206 HIS A CD2 
1483 C CE1 . HIS A 206 ? 1.4031 1.2017 1.0426 0.7607  0.0633  -0.0703 206 HIS A CE1 
1484 N NE2 . HIS A 206 ? 1.4809 1.2081 1.0756 0.7521  0.0914  -0.0626 206 HIS A NE2 
# 
