data_9LS8
# 
_entry.id   9LS8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9LS8         pdb_00009ls8 10.2210/pdb9ls8/pdb 
WWPDB D_1300055608 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-19 
# 
_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                        9LS8 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              zohibmuhammad@gmail.com 
_pdbx_contact_author.name_first         Muhammad 
_pdbx_contact_author.name_last          Zohib 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2335-4912 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pandey, R.' 1 0000-0002-6913-8345 
'Zohib, M.'  2 0000-0003-2335-4912 
'Arora, A.'  3 0000-0002-0630-2224 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Biol Macromol' 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           1879-0003 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            275 
_citation.language                  ? 
_citation.page_first                133445 
_citation.page_last                 ? 
_citation.title                     
'Characterization of structure of peptidyl-tRNA hydrolase from Enterococcus faecium and its inhibition by a pyrrolinone compound.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.133445 
_citation.pdbx_database_id_PubMed   38945334 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pandey, R.' 1 ? 
primary 'Zohib, M.'  2 ? 
primary 'Arora, A.'  3 ? 
# 
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 'Peptidyl-tRNA hydrolase' 21186.494 1   3.1.1.29 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL            62.068    1   ?        ? ? ? 
3 non-polymer syn BETA-MERCAPTOETHANOL      78.133    1   ?        ? ? ? 
4 non-polymer syn 'SODIUM ION'              22.990    2   ?        ? ? ? 
5 non-polymer syn 'SULFATE ION'             96.063    2   ?        ? ? ? 
6 water       nat water                     18.015    141 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PTH 
# 
_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       
;AMGMKMIVGLGNPGTKYQYTKHNIGFMVVDKIAREHQATFKKNPFEAEVAEFFHNGEKILLVKPQTFMNESGRAVGPLMT
YFGIYPEELVVIYDDLDLAVGKIRLRQKGSAGGHNGIKSIISHLNTNVFDRIKVGIGRPEGKKTVVQHVLSPFSKENQPL
IEESMCQSVKAVEYLIEGHSFVDAMNRFN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AMGMKMIVGLGNPGTKYQYTKHNIGFMVVDKIAREHQATFKKNPFEAEVAEFFHNGEKILLVKPQTFMNESGRAVGPLMT
YFGIYPEELVVIYDDLDLAVGKIRLRQKGSAGGHNGIKSIISHLNTNVFDRIKVGIGRPEGKKTVVQHVLSPFSKENQPL
IEESMCQSVKAVEYLIEGHSFVDAMNRFN
;
_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 1,2-ETHANEDIOL       EDO 
3 BETA-MERCAPTOETHANOL BME 
4 'SODIUM ION'         NA  
5 'SULFATE ION'        SO4 
6 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   MET n 
1 3   GLY n 
1 4   MET n 
1 5   LYS n 
1 6   MET n 
1 7   ILE n 
1 8   VAL n 
1 9   GLY n 
1 10  LEU n 
1 11  GLY n 
1 12  ASN n 
1 13  PRO n 
1 14  GLY n 
1 15  THR n 
1 16  LYS n 
1 17  TYR n 
1 18  GLN n 
1 19  TYR n 
1 20  THR n 
1 21  LYS n 
1 22  HIS n 
1 23  ASN n 
1 24  ILE n 
1 25  GLY n 
1 26  PHE n 
1 27  MET n 
1 28  VAL n 
1 29  VAL n 
1 30  ASP n 
1 31  LYS n 
1 32  ILE n 
1 33  ALA n 
1 34  ARG n 
1 35  GLU n 
1 36  HIS n 
1 37  GLN n 
1 38  ALA n 
1 39  THR n 
1 40  PHE n 
1 41  LYS n 
1 42  LYS n 
1 43  ASN n 
1 44  PRO n 
1 45  PHE n 
1 46  GLU n 
1 47  ALA n 
1 48  GLU n 
1 49  VAL n 
1 50  ALA n 
1 51  GLU n 
1 52  PHE n 
1 53  PHE n 
1 54  HIS n 
1 55  ASN n 
1 56  GLY n 
1 57  GLU n 
1 58  LYS n 
1 59  ILE n 
1 60  LEU n 
1 61  LEU n 
1 62  VAL n 
1 63  LYS n 
1 64  PRO n 
1 65  GLN n 
1 66  THR n 
1 67  PHE n 
1 68  MET n 
1 69  ASN n 
1 70  GLU n 
1 71  SER n 
1 72  GLY n 
1 73  ARG n 
1 74  ALA n 
1 75  VAL n 
1 76  GLY n 
1 77  PRO n 
1 78  LEU n 
1 79  MET n 
1 80  THR n 
1 81  TYR n 
1 82  PHE n 
1 83  GLY n 
1 84  ILE n 
1 85  TYR n 
1 86  PRO n 
1 87  GLU n 
1 88  GLU n 
1 89  LEU n 
1 90  VAL n 
1 91  VAL n 
1 92  ILE n 
1 93  TYR n 
1 94  ASP n 
1 95  ASP n 
1 96  LEU n 
1 97  ASP n 
1 98  LEU n 
1 99  ALA n 
1 100 VAL n 
1 101 GLY n 
1 102 LYS n 
1 103 ILE n 
1 104 ARG n 
1 105 LEU n 
1 106 ARG n 
1 107 GLN n 
1 108 LYS n 
1 109 GLY n 
1 110 SER n 
1 111 ALA n 
1 112 GLY n 
1 113 GLY n 
1 114 HIS n 
1 115 ASN n 
1 116 GLY n 
1 117 ILE n 
1 118 LYS n 
1 119 SER n 
1 120 ILE n 
1 121 ILE n 
1 122 SER n 
1 123 HIS n 
1 124 LEU n 
1 125 ASN n 
1 126 THR n 
1 127 ASN n 
1 128 VAL n 
1 129 PHE n 
1 130 ASP n 
1 131 ARG n 
1 132 ILE n 
1 133 LYS n 
1 134 VAL n 
1 135 GLY n 
1 136 ILE n 
1 137 GLY n 
1 138 ARG n 
1 139 PRO n 
1 140 GLU n 
1 141 GLY n 
1 142 LYS n 
1 143 LYS n 
1 144 THR n 
1 145 VAL n 
1 146 VAL n 
1 147 GLN n 
1 148 HIS n 
1 149 VAL n 
1 150 LEU n 
1 151 SER n 
1 152 PRO n 
1 153 PHE n 
1 154 SER n 
1 155 LYS n 
1 156 GLU n 
1 157 ASN n 
1 158 GLN n 
1 159 PRO n 
1 160 LEU n 
1 161 ILE n 
1 162 GLU n 
1 163 GLU n 
1 164 SER n 
1 165 MET n 
1 166 CYS n 
1 167 GLN n 
1 168 SER n 
1 169 VAL n 
1 170 LYS n 
1 171 ALA n 
1 172 VAL n 
1 173 GLU n 
1 174 TYR n 
1 175 LEU n 
1 176 ILE n 
1 177 GLU n 
1 178 GLY n 
1 179 HIS n 
1 180 SER n 
1 181 PHE n 
1 182 VAL n 
1 183 ASP n 
1 184 ALA n 
1 185 MET n 
1 186 ASN n 
1 187 ARG n 
1 188 PHE n 
1 189 ASN 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                   189 
_entity_src_gen.gene_src_common_name               'Streptococcus faecium' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;pth, AWT83_04625, B1P95_10305, CQR37_02495, CUN04_03690, CUS10_01235, CYQ77_06165, EB12_02316, GBM44_12820, GBM73_11110, KYX88_05820, M3X98_03560, P6Z85_03115
;
_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      'Enterococcus faecium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1352 
_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 
BME non-polymer         . BETA-MERCAPTOETHANOL ?                 'C2 H6 O S'      78.133  
CYS 'L-peptide linking' y CYSTEINE             ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL       'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
NA  non-polymer         . 'SODIUM ION'         ?                 'Na 1'           22.990  
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 
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   ALA 1   -2  -2  ALA ALA A . n 
A 1 2   MET 2   -1  -1  MET MET A . n 
A 1 3   GLY 3   0   0   GLY GLY A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   LYS 5   2   2   LYS LYS A . n 
A 1 6   MET 6   3   3   MET MET A . n 
A 1 7   ILE 7   4   4   ILE ILE A . n 
A 1 8   VAL 8   5   5   VAL VAL A . n 
A 1 9   GLY 9   6   6   GLY GLY A . n 
A 1 10  LEU 10  7   7   LEU LEU A . n 
A 1 11  GLY 11  8   8   GLY GLY A . n 
A 1 12  ASN 12  9   9   ASN ASN A . n 
A 1 13  PRO 13  10  10  PRO PRO A . n 
A 1 14  GLY 14  11  11  GLY GLY A . n 
A 1 15  THR 15  12  12  THR THR A . n 
A 1 16  LYS 16  13  13  LYS LYS A . n 
A 1 17  TYR 17  14  14  TYR TYR A . n 
A 1 18  GLN 18  15  15  GLN GLN A . n 
A 1 19  TYR 19  16  16  TYR TYR A . n 
A 1 20  THR 20  17  17  THR THR A . n 
A 1 21  LYS 21  18  18  LYS LYS A . n 
A 1 22  HIS 22  19  19  HIS HIS A . n 
A 1 23  ASN 23  20  20  ASN ASN A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  GLY 25  22  22  GLY GLY A . n 
A 1 26  PHE 26  23  23  PHE PHE A . n 
A 1 27  MET 27  24  24  MET MET A . n 
A 1 28  VAL 28  25  25  VAL VAL A . n 
A 1 29  VAL 29  26  26  VAL VAL A . n 
A 1 30  ASP 30  27  27  ASP ASP A . n 
A 1 31  LYS 31  28  28  LYS LYS A . n 
A 1 32  ILE 32  29  29  ILE ILE A . n 
A 1 33  ALA 33  30  30  ALA ALA A . n 
A 1 34  ARG 34  31  31  ARG ARG A . n 
A 1 35  GLU 35  32  32  GLU GLU A . n 
A 1 36  HIS 36  33  33  HIS HIS A . n 
A 1 37  GLN 37  34  34  GLN GLN A . n 
A 1 38  ALA 38  35  35  ALA ALA A . n 
A 1 39  THR 39  36  36  THR THR A . n 
A 1 40  PHE 40  37  37  PHE PHE A . n 
A 1 41  LYS 41  38  38  LYS LYS A . n 
A 1 42  LYS 42  39  39  LYS LYS A . n 
A 1 43  ASN 43  40  40  ASN ASN A . n 
A 1 44  PRO 44  41  41  PRO PRO A . n 
A 1 45  PHE 45  42  42  PHE PHE A . n 
A 1 46  GLU 46  43  43  GLU GLU A . n 
A 1 47  ALA 47  44  44  ALA ALA A . n 
A 1 48  GLU 48  45  45  GLU GLU A . n 
A 1 49  VAL 49  46  46  VAL VAL A . n 
A 1 50  ALA 50  47  47  ALA ALA A . n 
A 1 51  GLU 51  48  48  GLU GLU A . n 
A 1 52  PHE 52  49  49  PHE PHE A . n 
A 1 53  PHE 53  50  50  PHE PHE A . n 
A 1 54  HIS 54  51  51  HIS HIS A . n 
A 1 55  ASN 55  52  52  ASN ASN A . n 
A 1 56  GLY 56  53  53  GLY GLY A . n 
A 1 57  GLU 57  54  54  GLU GLU A . n 
A 1 58  LYS 58  55  55  LYS LYS A . n 
A 1 59  ILE 59  56  56  ILE ILE A . n 
A 1 60  LEU 60  57  57  LEU LEU A . n 
A 1 61  LEU 61  58  58  LEU LEU A . n 
A 1 62  VAL 62  59  59  VAL VAL A . n 
A 1 63  LYS 63  60  60  LYS LYS A . n 
A 1 64  PRO 64  61  61  PRO PRO A . n 
A 1 65  GLN 65  62  62  GLN GLN A . n 
A 1 66  THR 66  63  63  THR THR A . n 
A 1 67  PHE 67  64  64  PHE PHE A . n 
A 1 68  MET 68  65  65  MET MET A . n 
A 1 69  ASN 69  66  66  ASN ASN A . n 
A 1 70  GLU 70  67  67  GLU GLU A . n 
A 1 71  SER 71  68  68  SER SER A . n 
A 1 72  GLY 72  69  69  GLY GLY A . n 
A 1 73  ARG 73  70  70  ARG ARG A . n 
A 1 74  ALA 74  71  71  ALA ALA A . n 
A 1 75  VAL 75  72  72  VAL VAL A . n 
A 1 76  GLY 76  73  73  GLY GLY A . n 
A 1 77  PRO 77  74  74  PRO PRO A . n 
A 1 78  LEU 78  75  75  LEU LEU A . n 
A 1 79  MET 79  76  76  MET MET A . n 
A 1 80  THR 80  77  77  THR THR A . n 
A 1 81  TYR 81  78  78  TYR TYR A . n 
A 1 82  PHE 82  79  79  PHE PHE A . n 
A 1 83  GLY 83  80  80  GLY GLY A . n 
A 1 84  ILE 84  81  81  ILE ILE A . n 
A 1 85  TYR 85  82  82  TYR TYR A . n 
A 1 86  PRO 86  83  83  PRO PRO A . n 
A 1 87  GLU 87  84  84  GLU GLU A . n 
A 1 88  GLU 88  85  85  GLU GLU A . n 
A 1 89  LEU 89  86  86  LEU LEU A . n 
A 1 90  VAL 90  87  87  VAL VAL A . n 
A 1 91  VAL 91  88  88  VAL VAL A . n 
A 1 92  ILE 92  89  89  ILE ILE A . n 
A 1 93  TYR 93  90  90  TYR TYR A . n 
A 1 94  ASP 94  91  91  ASP ASP A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  LEU 96  93  93  LEU LEU A . n 
A 1 97  ASP 97  94  94  ASP ASP A . n 
A 1 98  LEU 98  95  95  LEU LEU A . n 
A 1 99  ALA 99  96  96  ALA ALA A . n 
A 1 100 VAL 100 97  97  VAL VAL A . n 
A 1 101 GLY 101 98  98  GLY GLY A . n 
A 1 102 LYS 102 99  99  LYS LYS A . n 
A 1 103 ILE 103 100 100 ILE ILE A . n 
A 1 104 ARG 104 101 101 ARG ARG A . n 
A 1 105 LEU 105 102 102 LEU LEU A . n 
A 1 106 ARG 106 103 103 ARG ARG A . n 
A 1 107 GLN 107 104 104 GLN GLN A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 GLY 109 106 106 GLY GLY A . n 
A 1 110 SER 110 107 107 SER SER A . n 
A 1 111 ALA 111 108 108 ALA ALA A . n 
A 1 112 GLY 112 109 109 GLY GLY A . n 
A 1 113 GLY 113 110 110 GLY GLY A . n 
A 1 114 HIS 114 111 111 HIS HIS A . n 
A 1 115 ASN 115 112 112 ASN ASN A . n 
A 1 116 GLY 116 113 113 GLY GLY A . n 
A 1 117 ILE 117 114 114 ILE ILE A . n 
A 1 118 LYS 118 115 115 LYS LYS A . n 
A 1 119 SER 119 116 116 SER SER A . n 
A 1 120 ILE 120 117 117 ILE ILE A . n 
A 1 121 ILE 121 118 118 ILE ILE A . n 
A 1 122 SER 122 119 119 SER SER A . n 
A 1 123 HIS 123 120 120 HIS HIS A . n 
A 1 124 LEU 124 121 121 LEU LEU A . n 
A 1 125 ASN 125 122 122 ASN ASN A . n 
A 1 126 THR 126 123 123 THR THR A . n 
A 1 127 ASN 127 124 124 ASN ASN A . n 
A 1 128 VAL 128 125 125 VAL VAL A . n 
A 1 129 PHE 129 126 126 PHE PHE A . n 
A 1 130 ASP 130 127 127 ASP ASP A . n 
A 1 131 ARG 131 128 128 ARG ARG A . n 
A 1 132 ILE 132 129 129 ILE ILE A . n 
A 1 133 LYS 133 130 130 LYS LYS A . n 
A 1 134 VAL 134 131 131 VAL VAL A . n 
A 1 135 GLY 135 132 132 GLY GLY A . n 
A 1 136 ILE 136 133 133 ILE ILE A . n 
A 1 137 GLY 137 134 134 GLY GLY A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 PRO 139 136 136 PRO PRO A . n 
A 1 140 GLU 140 137 137 GLU GLU A . n 
A 1 141 GLY 141 138 138 GLY GLY A . n 
A 1 142 LYS 142 139 139 LYS LYS A . n 
A 1 143 LYS 143 140 140 LYS LYS A . n 
A 1 144 THR 144 141 141 THR THR A . n 
A 1 145 VAL 145 142 142 VAL VAL A . n 
A 1 146 VAL 146 143 143 VAL VAL A . n 
A 1 147 GLN 147 144 144 GLN GLN A . n 
A 1 148 HIS 148 145 145 HIS HIS A . n 
A 1 149 VAL 149 146 146 VAL VAL A . n 
A 1 150 LEU 150 147 147 LEU LEU A . n 
A 1 151 SER 151 148 148 SER SER A . n 
A 1 152 PRO 152 149 149 PRO PRO A . n 
A 1 153 PHE 153 150 150 PHE PHE A . n 
A 1 154 SER 154 151 151 SER SER A . n 
A 1 155 LYS 155 152 152 LYS LYS A . n 
A 1 156 GLU 156 153 153 GLU GLU A . n 
A 1 157 ASN 157 154 154 ASN ASN A . n 
A 1 158 GLN 158 155 155 GLN GLN A . n 
A 1 159 PRO 159 156 156 PRO PRO A . n 
A 1 160 LEU 160 157 157 LEU LEU A . n 
A 1 161 ILE 161 158 158 ILE ILE A . n 
A 1 162 GLU 162 159 159 GLU GLU A . n 
A 1 163 GLU 163 160 160 GLU GLU A . n 
A 1 164 SER 164 161 161 SER SER A . n 
A 1 165 MET 165 162 162 MET MET A . n 
A 1 166 CYS 166 163 163 CYS CYS A . n 
A 1 167 GLN 167 164 164 GLN GLN A . n 
A 1 168 SER 168 165 165 SER SER A . n 
A 1 169 VAL 169 166 166 VAL VAL A . n 
A 1 170 LYS 170 167 167 LYS LYS A . n 
A 1 171 ALA 171 168 168 ALA ALA A . n 
A 1 172 VAL 172 169 169 VAL VAL A . n 
A 1 173 GLU 173 170 170 GLU GLU A . n 
A 1 174 TYR 174 171 171 TYR TYR A . n 
A 1 175 LEU 175 172 172 LEU LEU A . n 
A 1 176 ILE 176 173 173 ILE ILE A . n 
A 1 177 GLU 177 174 174 GLU GLU A . n 
A 1 178 GLY 178 175 175 GLY GLY A . n 
A 1 179 HIS 179 176 176 HIS HIS A . n 
A 1 180 SER 180 177 177 SER SER A . n 
A 1 181 PHE 181 178 178 PHE PHE A . n 
A 1 182 VAL 182 179 179 VAL VAL A . n 
A 1 183 ASP 183 180 180 ASP ASP A . n 
A 1 184 ALA 184 181 181 ALA ALA A . n 
A 1 185 MET 185 182 182 MET MET A . n 
A 1 186 ASN 186 183 183 ASN ASN A . n 
A 1 187 ARG 187 184 184 ARG ARG A . n 
A 1 188 PHE 188 185 185 PHE PHE A . n 
A 1 189 ASN 189 186 186 ASN ASN 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 EDO 1   201 201 EDO EDO A . 
C 3 BME 1   202 203 BME BME A . 
D 4 NA  1   203 1   NA  NA  A . 
E 4 NA  1   204 2   NA  NA  A . 
F 5 SO4 1   205 1   SO4 SO4 A . 
G 5 SO4 1   206 2   SO4 SO4 A . 
H 6 HOH 1   301 114 HOH HOH A . 
H 6 HOH 2   302 128 HOH HOH A . 
H 6 HOH 3   303 1   HOH HOH A . 
H 6 HOH 4   304 138 HOH HOH A . 
H 6 HOH 5   305 72  HOH HOH A . 
H 6 HOH 6   306 11  HOH HOH A . 
H 6 HOH 7   307 141 HOH HOH A . 
H 6 HOH 8   308 98  HOH HOH A . 
H 6 HOH 9   309 54  HOH HOH A . 
H 6 HOH 10  310 89  HOH HOH A . 
H 6 HOH 11  311 50  HOH HOH A . 
H 6 HOH 12  312 67  HOH HOH A . 
H 6 HOH 13  313 96  HOH HOH A . 
H 6 HOH 14  314 14  HOH HOH A . 
H 6 HOH 15  315 25  HOH HOH A . 
H 6 HOH 16  316 97  HOH HOH A . 
H 6 HOH 17  317 76  HOH HOH A . 
H 6 HOH 18  318 64  HOH HOH A . 
H 6 HOH 19  319 22  HOH HOH A . 
H 6 HOH 20  320 29  HOH HOH A . 
H 6 HOH 21  321 74  HOH HOH A . 
H 6 HOH 22  322 71  HOH HOH A . 
H 6 HOH 23  323 70  HOH HOH A . 
H 6 HOH 24  324 9   HOH HOH A . 
H 6 HOH 25  325 151 HOH HOH A . 
H 6 HOH 26  326 7   HOH HOH A . 
H 6 HOH 27  327 135 HOH HOH A . 
H 6 HOH 28  328 62  HOH HOH A . 
H 6 HOH 29  329 68  HOH HOH A . 
H 6 HOH 30  330 35  HOH HOH A . 
H 6 HOH 31  331 111 HOH HOH A . 
H 6 HOH 32  332 140 HOH HOH A . 
H 6 HOH 33  333 46  HOH HOH A . 
H 6 HOH 34  334 32  HOH HOH A . 
H 6 HOH 35  335 27  HOH HOH A . 
H 6 HOH 36  336 88  HOH HOH A . 
H 6 HOH 37  337 15  HOH HOH A . 
H 6 HOH 38  338 109 HOH HOH A . 
H 6 HOH 39  339 17  HOH HOH A . 
H 6 HOH 40  340 43  HOH HOH A . 
H 6 HOH 41  341 6   HOH HOH A . 
H 6 HOH 42  342 30  HOH HOH A . 
H 6 HOH 43  343 123 HOH HOH A . 
H 6 HOH 44  344 52  HOH HOH A . 
H 6 HOH 45  345 66  HOH HOH A . 
H 6 HOH 46  346 91  HOH HOH A . 
H 6 HOH 47  347 51  HOH HOH A . 
H 6 HOH 48  348 86  HOH HOH A . 
H 6 HOH 49  349 39  HOH HOH A . 
H 6 HOH 50  350 82  HOH HOH A . 
H 6 HOH 51  351 48  HOH HOH A . 
H 6 HOH 52  352 23  HOH HOH A . 
H 6 HOH 53  353 12  HOH HOH A . 
H 6 HOH 54  354 28  HOH HOH A . 
H 6 HOH 55  355 90  HOH HOH A . 
H 6 HOH 56  356 49  HOH HOH A . 
H 6 HOH 57  357 5   HOH HOH A . 
H 6 HOH 58  358 61  HOH HOH A . 
H 6 HOH 59  359 53  HOH HOH A . 
H 6 HOH 60  360 80  HOH HOH A . 
H 6 HOH 61  361 37  HOH HOH A . 
H 6 HOH 62  362 139 HOH HOH A . 
H 6 HOH 63  363 78  HOH HOH A . 
H 6 HOH 64  364 146 HOH HOH A . 
H 6 HOH 65  365 132 HOH HOH A . 
H 6 HOH 66  366 44  HOH HOH A . 
H 6 HOH 67  367 83  HOH HOH A . 
H 6 HOH 68  368 47  HOH HOH A . 
H 6 HOH 69  369 21  HOH HOH A . 
H 6 HOH 70  370 124 HOH HOH A . 
H 6 HOH 71  371 102 HOH HOH A . 
H 6 HOH 72  372 106 HOH HOH A . 
H 6 HOH 73  373 103 HOH HOH A . 
H 6 HOH 74  374 113 HOH HOH A . 
H 6 HOH 75  375 41  HOH HOH A . 
H 6 HOH 76  376 137 HOH HOH A . 
H 6 HOH 77  377 13  HOH HOH A . 
H 6 HOH 78  378 104 HOH HOH A . 
H 6 HOH 79  379 26  HOH HOH A . 
H 6 HOH 80  380 105 HOH HOH A . 
H 6 HOH 81  381 34  HOH HOH A . 
H 6 HOH 82  382 116 HOH HOH A . 
H 6 HOH 83  383 19  HOH HOH A . 
H 6 HOH 84  384 63  HOH HOH A . 
H 6 HOH 85  385 24  HOH HOH A . 
H 6 HOH 86  386 136 HOH HOH A . 
H 6 HOH 87  387 10  HOH HOH A . 
H 6 HOH 88  388 142 HOH HOH A . 
H 6 HOH 89  389 85  HOH HOH A . 
H 6 HOH 90  390 147 HOH HOH A . 
H 6 HOH 91  391 45  HOH HOH A . 
H 6 HOH 92  392 101 HOH HOH A . 
H 6 HOH 93  393 87  HOH HOH A . 
H 6 HOH 94  394 79  HOH HOH A . 
H 6 HOH 95  395 69  HOH HOH A . 
H 6 HOH 96  396 121 HOH HOH A . 
H 6 HOH 97  397 65  HOH HOH A . 
H 6 HOH 98  398 33  HOH HOH A . 
H 6 HOH 99  399 126 HOH HOH A . 
H 6 HOH 100 400 81  HOH HOH A . 
H 6 HOH 101 401 84  HOH HOH A . 
H 6 HOH 102 402 56  HOH HOH A . 
H 6 HOH 103 403 40  HOH HOH A . 
H 6 HOH 104 404 118 HOH HOH A . 
H 6 HOH 105 405 16  HOH HOH A . 
H 6 HOH 106 406 115 HOH HOH A . 
H 6 HOH 107 407 73  HOH HOH A . 
H 6 HOH 108 408 20  HOH HOH A . 
H 6 HOH 109 409 99  HOH HOH A . 
H 6 HOH 110 410 134 HOH HOH A . 
H 6 HOH 111 411 4   HOH HOH A . 
H 6 HOH 112 412 59  HOH HOH A . 
H 6 HOH 113 413 58  HOH HOH A . 
H 6 HOH 114 414 129 HOH HOH A . 
H 6 HOH 115 415 77  HOH HOH A . 
H 6 HOH 116 416 148 HOH HOH A . 
H 6 HOH 117 417 95  HOH HOH A . 
H 6 HOH 118 418 119 HOH HOH A . 
H 6 HOH 119 419 57  HOH HOH A . 
H 6 HOH 120 420 145 HOH HOH A . 
H 6 HOH 121 421 108 HOH HOH A . 
H 6 HOH 122 422 149 HOH HOH A . 
H 6 HOH 123 423 110 HOH HOH A . 
H 6 HOH 124 424 130 HOH HOH A . 
H 6 HOH 125 425 112 HOH HOH A . 
H 6 HOH 126 426 122 HOH HOH A . 
H 6 HOH 127 427 18  HOH HOH A . 
H 6 HOH 128 428 131 HOH HOH A . 
H 6 HOH 129 429 107 HOH HOH A . 
H 6 HOH 130 430 42  HOH HOH A . 
H 6 HOH 131 431 36  HOH HOH A . 
H 6 HOH 132 432 8   HOH HOH A . 
H 6 HOH 133 433 143 HOH HOH A . 
H 6 HOH 134 434 2   HOH HOH A . 
H 6 HOH 135 435 117 HOH HOH A . 
H 6 HOH 136 436 144 HOH HOH A . 
H 6 HOH 137 437 150 HOH HOH A . 
H 6 HOH 138 438 125 HOH HOH A . 
H 6 HOH 139 439 94  HOH HOH A . 
H 6 HOH 140 440 92  HOH HOH A . 
H 6 HOH 141 441 127 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 2   ? NZ  ? A LYS 5   NZ  
2  1 Y 1 A GLN 34  ? CG  ? A GLN 37  CG  
3  1 Y 1 A GLN 34  ? CD  ? A GLN 37  CD  
4  1 Y 1 A GLN 34  ? OE1 ? A GLN 37  OE1 
5  1 Y 1 A GLN 34  ? NE2 ? A GLN 37  NE2 
6  1 Y 1 A LYS 38  ? CD  ? A LYS 41  CD  
7  1 Y 1 A LYS 38  ? CE  ? A LYS 41  CE  
8  1 Y 1 A LYS 38  ? NZ  ? A LYS 41  NZ  
9  1 Y 1 A LYS 39  ? CD  ? A LYS 42  CD  
10 1 Y 1 A LYS 39  ? CE  ? A LYS 42  CE  
11 1 Y 1 A LYS 39  ? NZ  ? A LYS 42  NZ  
12 1 Y 1 A ASN 52  ? CB  ? A ASN 55  CB  
13 1 Y 1 A ASN 52  ? CG  ? A ASN 55  CG  
14 1 Y 1 A ASN 52  ? OD1 ? A ASN 55  OD1 
15 1 Y 1 A ASN 52  ? ND2 ? A ASN 55  ND2 
16 1 Y 1 A LYS 55  ? CE  ? A LYS 58  CE  
17 1 Y 1 A LYS 55  ? NZ  ? A LYS 58  NZ  
18 1 Y 1 A GLU 67  ? OE2 ? A GLU 70  OE2 
19 1 Y 1 A LYS 139 ? NZ  ? A LYS 142 NZ  
20 1 Y 1 A LYS 140 ? CG  ? A LYS 143 CG  
21 1 Y 1 A LYS 140 ? CD  ? A LYS 143 CD  
22 1 Y 1 A LYS 140 ? CE  ? A LYS 143 CE  
23 1 Y 1 A LYS 140 ? NZ  ? A LYS 143 NZ  
24 1 Y 1 A LYS 152 ? CE  ? A LYS 155 CE  
25 1 Y 1 A LYS 152 ? NZ  ? A LYS 155 NZ  
26 1 Y 1 A GLU 153 ? OE2 ? A GLU 156 OE2 
27 1 Y 1 A GLU 160 ? CD  ? A GLU 163 CD  
28 1 Y 1 A GLU 160 ? OE1 ? A GLU 163 OE1 
29 1 Y 1 A GLU 160 ? OE2 ? A GLU 163 OE2 
30 1 Y 1 A ARG 184 ? CZ  ? A ARG 187 CZ  
31 1 Y 1 A ARG 184 ? NH1 ? A ARG 187 NH1 
32 1 Y 1 A ARG 184 ? NH2 ? A ARG 187 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LS8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.765 
_cell.length_a_esd                 ? 
_cell.length_b                     47.584 
_cell.length_b_esd                 ? 
_cell.length_c                     69.168 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9LS8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9LS8 
_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             1.82 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          32.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Ammonium Sulphate, 0.1M Tris-HCl pH 7.5, 15% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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 EIGER2 X CdTe 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-06 
_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   0.885 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LS8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.22 
_reflns.d_resolution_low                               47.58 
_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                                     40928 
_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                           88.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_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                                    1.22 
_reflns_shell.d_res_low                                     1.24 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2262 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.710 
_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]                            1.51 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.51 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.027 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LS8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.22 
_refine.ls_d_res_low                             30.06 
_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                     38903 
_refine.ls_number_reflns_R_free                  1981 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.20 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16019 
_refine.ls_R_factor_R_free                       0.19805 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15838 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.053 
_refine.pdbx_overall_ESU_R_Free                  0.053 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.948 
_refine.overall_SU_ML                            0.037 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.22 
_refine_hist.d_res_low                        30.06 
_refine_hist.number_atoms_solvent             141 
_refine_hist.number_atoms_total               1617 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1464 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  1513 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1432 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.657  1.657  2040 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.580  1.568  3296 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.082  5.000  192  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.422  5.000  6    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.814 10.000 244  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  225  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  1746 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  338  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.620  1.768  762  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.615  1.767  762  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.393  3.188  953  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.396  3.188  954  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.225  2.132  751  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.014  2.119  744  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.576  3.726  1075 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 12.346 23.11  1712 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 12.015 22.05  1690 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 3.733  3.000  2945 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.223 
_refine_ls_shell.d_res_low                        1.255 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             169 
_refine_ls_shell.number_reflns_R_work             3099 
_refine_ls_shell.percent_reflns_obs               96.57 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.243 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.243 
# 
_struct.entry_id                     9LS8 
_struct.title                        'Crystal structure of peptidyl-tRNA hydrolase from Enterococcus faecium at 1.22 A' 
_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        9LS8 
_struct_keywords.text            'peptidyl-tRNA hydrolase, Enterococcus faecium, 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 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A133CPV0_ENTFC 
_struct_ref.pdbx_db_accession          A0A133CPV0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKMIVGLGNPGTKYQYTKHNIGFMVVDKIAREHQATFKKNPFEAEVAEFFHNGEKILLVKPQTFMNESGRAVGPLMTYFG
IYPEELVVIYDDLDLAVGKIRLRQKGSAGGHNGIKSIISHLNTNVFDRIKVGIGRPEGKKTVVQHVLSPFSKENQPLIEE
SMCQSVKAVEYLIEGHSFVDAMNRFN
;
_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              9LS8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 189 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A133CPV0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  186 
_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       186 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9LS8 ALA A 1 ? UNP A0A133CPV0 ? ? 'expression tag' -2 1 
1 9LS8 MET A 2 ? UNP A0A133CPV0 ? ? 'expression tag' -1 2 
1 9LS8 GLY A 3 ? UNP A0A133CPV0 ? ? 'expression tag' 0  3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 180  ? 
1 MORE         -13  ? 
1 'SSA (A^2)'  8980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 20  ? HIS A 22  ? THR A 17  HIS A 19  5 ? 3  
HELX_P HELX_P2  AA2 ASN A 23  ? HIS A 36  ? ASN A 20  HIS A 33  1 ? 14 
HELX_P HELX_P3  AA3 PHE A 67  ? GLU A 70  ? PHE A 64  GLU A 67  5 ? 4  
HELX_P HELX_P4  AA4 SER A 71  ? GLY A 83  ? SER A 68  GLY A 80  1 ? 13 
HELX_P HELX_P5  AA5 TYR A 85  ? GLU A 87  ? TYR A 82  GLU A 84  5 ? 3  
HELX_P HELX_P6  AA6 SER A 110 ? GLY A 113 ? SER A 107 GLY A 110 5 ? 4  
HELX_P HELX_P7  AA7 HIS A 114 ? ASN A 125 ? HIS A 111 ASN A 122 1 ? 12 
HELX_P HELX_P8  AA8 GLY A 141 ? LYS A 143 ? GLY A 138 LYS A 140 5 ? 3  
HELX_P HELX_P9  AA9 THR A 144 ? LEU A 150 ? THR A 141 LEU A 147 1 ? 7  
HELX_P HELX_P10 AB1 ASN A 157 ? GLU A 177 ? ASN A 154 GLU A 174 1 ? 21 
HELX_P HELX_P11 AB2 SER A 180 ? ASN A 189 ? SER A 177 ASN A 186 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           SER 
_struct_conn.ptnr1_label_seq_id            119 
_struct_conn.ptnr1_label_atom_id           OG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           E 
_struct_conn.ptnr2_label_comp_id           NA 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           NA 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            SER 
_struct_conn.ptnr1_auth_seq_id             116 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            NA 
_struct_conn.ptnr2_auth_seq_id             204 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.723 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   7 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 41  ? ASN A 43  ? LYS A 38  ASN A 40  
AA1 2 ALA A 47  ? HIS A 54  ? ALA A 44  HIS A 51  
AA1 3 GLU A 57  ? PRO A 64  ? GLU A 54  PRO A 61  
AA1 4 MET A 4   ? GLY A 9   ? MET A 1   GLY A 6   
AA1 5 LEU A 89  ? ASP A 95  ? LEU A 86  ASP A 92  
AA1 6 VAL A 128 ? GLY A 135 ? VAL A 125 GLY A 132 
AA1 7 ILE A 103 ? LYS A 108 ? ILE A 100 LYS A 105 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 41  ? N LYS A 38  O VAL A 49  ? O VAL A 46  
AA1 2 3 N PHE A 52  ? N PHE A 49  O ILE A 59  ? O ILE A 56  
AA1 3 4 O LEU A 60  ? O LEU A 57  N ILE A 7   ? N ILE A 4   
AA1 4 5 N VAL A 8   ? N VAL A 5   O ILE A 92  ? O ILE A 89  
AA1 5 6 N TYR A 93  ? N TYR A 90  O VAL A 134 ? O VAL A 131 
AA1 6 7 O LYS A 133 ? O LYS A 130 N ARG A 104 ? N ARG A 101 
# 
_pdbx_entry_details.entry_id                   9LS8 
_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 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              101 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              101 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              101 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                125.81 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            14.01 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 42 ? ? -107.28 46.75  
2 1 ASN A 52 ? ? 38.84   56.55  
3 1 PHE A 64 ? ? 79.27   151.96 
# 
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  
BME C1   C  N N 74  
BME C2   C  N N 75  
BME O1   O  N N 76  
BME S2   S  N N 77  
BME H11  H  N N 78  
BME H12  H  N N 79  
BME H21  H  N N 80  
BME H22  H  N N 81  
BME HO1  H  N N 82  
BME HS2  H  N N 83  
CYS N    N  N N 84  
CYS CA   C  N R 85  
CYS C    C  N N 86  
CYS O    O  N N 87  
CYS CB   C  N N 88  
CYS SG   S  N N 89  
CYS OXT  O  N N 90  
CYS H    H  N N 91  
CYS H2   H  N N 92  
CYS HA   H  N N 93  
CYS HB2  H  N N 94  
CYS HB3  H  N N 95  
CYS HG   H  N N 96  
CYS HXT  H  N N 97  
EDO C1   C  N N 98  
EDO O1   O  N N 99  
EDO C2   C  N N 100 
EDO O2   O  N N 101 
EDO H11  H  N N 102 
EDO H12  H  N N 103 
EDO HO1  H  N N 104 
EDO H21  H  N N 105 
EDO H22  H  N N 106 
EDO HO2  H  N N 107 
GLN N    N  N N 108 
GLN CA   C  N S 109 
GLN C    C  N N 110 
GLN O    O  N N 111 
GLN CB   C  N N 112 
GLN CG   C  N N 113 
GLN CD   C  N N 114 
GLN OE1  O  N N 115 
GLN NE2  N  N N 116 
GLN OXT  O  N N 117 
GLN H    H  N N 118 
GLN H2   H  N N 119 
GLN HA   H  N N 120 
GLN HB2  H  N N 121 
GLN HB3  H  N N 122 
GLN HG2  H  N N 123 
GLN HG3  H  N N 124 
GLN HE21 H  N N 125 
GLN HE22 H  N N 126 
GLN HXT  H  N N 127 
GLU N    N  N N 128 
GLU CA   C  N S 129 
GLU C    C  N N 130 
GLU O    O  N N 131 
GLU CB   C  N N 132 
GLU CG   C  N N 133 
GLU CD   C  N N 134 
GLU OE1  O  N N 135 
GLU OE2  O  N N 136 
GLU OXT  O  N N 137 
GLU H    H  N N 138 
GLU H2   H  N N 139 
GLU HA   H  N N 140 
GLU HB2  H  N N 141 
GLU HB3  H  N N 142 
GLU HG2  H  N N 143 
GLU HG3  H  N N 144 
GLU HE2  H  N N 145 
GLU HXT  H  N N 146 
GLY N    N  N N 147 
GLY CA   C  N N 148 
GLY C    C  N N 149 
GLY O    O  N N 150 
GLY OXT  O  N N 151 
GLY H    H  N N 152 
GLY H2   H  N N 153 
GLY HA2  H  N N 154 
GLY HA3  H  N N 155 
GLY HXT  H  N N 156 
HIS N    N  N N 157 
HIS CA   C  N S 158 
HIS C    C  N N 159 
HIS O    O  N N 160 
HIS CB   C  N N 161 
HIS CG   C  Y N 162 
HIS ND1  N  Y N 163 
HIS CD2  C  Y N 164 
HIS CE1  C  Y N 165 
HIS NE2  N  Y N 166 
HIS OXT  O  N N 167 
HIS H    H  N N 168 
HIS H2   H  N N 169 
HIS HA   H  N N 170 
HIS HB2  H  N N 171 
HIS HB3  H  N N 172 
HIS HD1  H  N N 173 
HIS HD2  H  N N 174 
HIS HE1  H  N N 175 
HIS HE2  H  N N 176 
HIS HXT  H  N N 177 
HOH O    O  N N 178 
HOH H1   H  N N 179 
HOH H2   H  N N 180 
ILE N    N  N N 181 
ILE CA   C  N S 182 
ILE C    C  N N 183 
ILE O    O  N N 184 
ILE CB   C  N S 185 
ILE CG1  C  N N 186 
ILE CG2  C  N N 187 
ILE CD1  C  N N 188 
ILE OXT  O  N N 189 
ILE H    H  N N 190 
ILE H2   H  N N 191 
ILE HA   H  N N 192 
ILE HB   H  N N 193 
ILE HG12 H  N N 194 
ILE HG13 H  N N 195 
ILE HG21 H  N N 196 
ILE HG22 H  N N 197 
ILE HG23 H  N N 198 
ILE HD11 H  N N 199 
ILE HD12 H  N N 200 
ILE HD13 H  N N 201 
ILE HXT  H  N N 202 
LEU N    N  N N 203 
LEU CA   C  N S 204 
LEU C    C  N N 205 
LEU O    O  N N 206 
LEU CB   C  N N 207 
LEU CG   C  N N 208 
LEU CD1  C  N N 209 
LEU CD2  C  N N 210 
LEU OXT  O  N N 211 
LEU H    H  N N 212 
LEU H2   H  N N 213 
LEU HA   H  N N 214 
LEU HB2  H  N N 215 
LEU HB3  H  N N 216 
LEU HG   H  N N 217 
LEU HD11 H  N N 218 
LEU HD12 H  N N 219 
LEU HD13 H  N N 220 
LEU HD21 H  N N 221 
LEU HD22 H  N N 222 
LEU HD23 H  N N 223 
LEU HXT  H  N N 224 
LYS N    N  N N 225 
LYS CA   C  N S 226 
LYS C    C  N N 227 
LYS O    O  N N 228 
LYS CB   C  N N 229 
LYS CG   C  N N 230 
LYS CD   C  N N 231 
LYS CE   C  N N 232 
LYS NZ   N  N N 233 
LYS OXT  O  N N 234 
LYS H    H  N N 235 
LYS H2   H  N N 236 
LYS HA   H  N N 237 
LYS HB2  H  N N 238 
LYS HB3  H  N N 239 
LYS HG2  H  N N 240 
LYS HG3  H  N N 241 
LYS HD2  H  N N 242 
LYS HD3  H  N N 243 
LYS HE2  H  N N 244 
LYS HE3  H  N N 245 
LYS HZ1  H  N N 246 
LYS HZ2  H  N N 247 
LYS HZ3  H  N N 248 
LYS HXT  H  N N 249 
MET N    N  N N 250 
MET CA   C  N S 251 
MET C    C  N N 252 
MET O    O  N N 253 
MET CB   C  N N 254 
MET CG   C  N N 255 
MET SD   S  N N 256 
MET CE   C  N N 257 
MET OXT  O  N N 258 
MET H    H  N N 259 
MET H2   H  N N 260 
MET HA   H  N N 261 
MET HB2  H  N N 262 
MET HB3  H  N N 263 
MET HG2  H  N N 264 
MET HG3  H  N N 265 
MET HE1  H  N N 266 
MET HE2  H  N N 267 
MET HE3  H  N N 268 
MET HXT  H  N N 269 
NA  NA   NA N N 270 
PHE N    N  N N 271 
PHE CA   C  N S 272 
PHE C    C  N N 273 
PHE O    O  N N 274 
PHE CB   C  N N 275 
PHE CG   C  Y N 276 
PHE CD1  C  Y N 277 
PHE CD2  C  Y N 278 
PHE CE1  C  Y N 279 
PHE CE2  C  Y N 280 
PHE CZ   C  Y N 281 
PHE OXT  O  N N 282 
PHE H    H  N N 283 
PHE H2   H  N N 284 
PHE HA   H  N N 285 
PHE HB2  H  N N 286 
PHE HB3  H  N N 287 
PHE HD1  H  N N 288 
PHE HD2  H  N N 289 
PHE HE1  H  N N 290 
PHE HE2  H  N N 291 
PHE HZ   H  N N 292 
PHE HXT  H  N N 293 
PRO N    N  N N 294 
PRO CA   C  N S 295 
PRO C    C  N N 296 
PRO O    O  N N 297 
PRO CB   C  N N 298 
PRO CG   C  N N 299 
PRO CD   C  N N 300 
PRO OXT  O  N N 301 
PRO H    H  N N 302 
PRO HA   H  N N 303 
PRO HB2  H  N N 304 
PRO HB3  H  N N 305 
PRO HG2  H  N N 306 
PRO HG3  H  N N 307 
PRO HD2  H  N N 308 
PRO HD3  H  N N 309 
PRO HXT  H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
SO4 S    S  N N 325 
SO4 O1   O  N N 326 
SO4 O2   O  N N 327 
SO4 O3   O  N N 328 
SO4 O4   O  N N 329 
THR N    N  N N 330 
THR CA   C  N S 331 
THR C    C  N N 332 
THR O    O  N N 333 
THR CB   C  N R 334 
THR OG1  O  N N 335 
THR CG2  C  N N 336 
THR OXT  O  N N 337 
THR H    H  N N 338 
THR H2   H  N N 339 
THR HA   H  N N 340 
THR HB   H  N N 341 
THR HG1  H  N N 342 
THR HG21 H  N N 343 
THR HG22 H  N N 344 
THR HG23 H  N N 345 
THR HXT  H  N N 346 
TYR N    N  N N 347 
TYR CA   C  N S 348 
TYR C    C  N N 349 
TYR O    O  N N 350 
TYR CB   C  N N 351 
TYR CG   C  Y N 352 
TYR CD1  C  Y N 353 
TYR CD2  C  Y N 354 
TYR CE1  C  Y N 355 
TYR CE2  C  Y N 356 
TYR CZ   C  Y N 357 
TYR OH   O  N N 358 
TYR OXT  O  N N 359 
TYR H    H  N N 360 
TYR H2   H  N N 361 
TYR HA   H  N N 362 
TYR HB2  H  N N 363 
TYR HB3  H  N N 364 
TYR HD1  H  N N 365 
TYR HD2  H  N N 366 
TYR HE1  H  N N 367 
TYR HE2  H  N N 368 
TYR HH   H  N N 369 
TYR HXT  H  N N 370 
VAL N    N  N N 371 
VAL CA   C  N S 372 
VAL C    C  N N 373 
VAL O    O  N N 374 
VAL CB   C  N N 375 
VAL CG1  C  N N 376 
VAL CG2  C  N N 377 
VAL OXT  O  N N 378 
VAL H    H  N N 379 
VAL H2   H  N N 380 
VAL HA   H  N N 381 
VAL HB   H  N N 382 
VAL HG11 H  N N 383 
VAL HG12 H  N N 384 
VAL HG13 H  N N 385 
VAL HG21 H  N N 386 
VAL HG22 H  N N 387 
VAL HG23 H  N N 388 
VAL HXT  H  N N 389 
# 
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  
BME C1  C2   sing N N 70  
BME C1  O1   sing N N 71  
BME C1  H11  sing N N 72  
BME C1  H12  sing N N 73  
BME C2  S2   sing N N 74  
BME C2  H21  sing N N 75  
BME C2  H22  sing N N 76  
BME O1  HO1  sing N N 77  
BME S2  HS2  sing N N 78  
CYS N   CA   sing N N 79  
CYS N   H    sing N N 80  
CYS N   H2   sing N N 81  
CYS CA  C    sing N N 82  
CYS CA  CB   sing N N 83  
CYS CA  HA   sing N N 84  
CYS C   O    doub N N 85  
CYS C   OXT  sing N N 86  
CYS CB  SG   sing N N 87  
CYS CB  HB2  sing N N 88  
CYS CB  HB3  sing N N 89  
CYS SG  HG   sing N N 90  
CYS OXT HXT  sing N N 91  
EDO C1  O1   sing N N 92  
EDO C1  C2   sing N N 93  
EDO C1  H11  sing N N 94  
EDO C1  H12  sing N N 95  
EDO O1  HO1  sing N N 96  
EDO C2  O2   sing N N 97  
EDO C2  H21  sing N N 98  
EDO C2  H22  sing N N 99  
EDO O2  HO2  sing N N 100 
GLN N   CA   sing N N 101 
GLN N   H    sing N N 102 
GLN N   H2   sing N N 103 
GLN CA  C    sing N N 104 
GLN CA  CB   sing N N 105 
GLN CA  HA   sing N N 106 
GLN C   O    doub N N 107 
GLN C   OXT  sing N N 108 
GLN CB  CG   sing N N 109 
GLN CB  HB2  sing N N 110 
GLN CB  HB3  sing N N 111 
GLN CG  CD   sing N N 112 
GLN CG  HG2  sing N N 113 
GLN CG  HG3  sing N N 114 
GLN CD  OE1  doub N N 115 
GLN CD  NE2  sing N N 116 
GLN NE2 HE21 sing N N 117 
GLN NE2 HE22 sing N N 118 
GLN OXT HXT  sing N N 119 
GLU N   CA   sing N N 120 
GLU N   H    sing N N 121 
GLU N   H2   sing N N 122 
GLU CA  C    sing N N 123 
GLU CA  CB   sing N N 124 
GLU CA  HA   sing N N 125 
GLU C   O    doub N N 126 
GLU C   OXT  sing N N 127 
GLU CB  CG   sing N N 128 
GLU CB  HB2  sing N N 129 
GLU CB  HB3  sing N N 130 
GLU CG  CD   sing N N 131 
GLU CG  HG2  sing N N 132 
GLU CG  HG3  sing N N 133 
GLU CD  OE1  doub N N 134 
GLU CD  OE2  sing N N 135 
GLU OE2 HE2  sing N N 136 
GLU OXT HXT  sing N N 137 
GLY N   CA   sing N N 138 
GLY N   H    sing N N 139 
GLY N   H2   sing N N 140 
GLY CA  C    sing N N 141 
GLY CA  HA2  sing N N 142 
GLY CA  HA3  sing N N 143 
GLY C   O    doub N N 144 
GLY C   OXT  sing N N 145 
GLY OXT HXT  sing N N 146 
HIS N   CA   sing N N 147 
HIS N   H    sing N N 148 
HIS N   H2   sing N N 149 
HIS CA  C    sing N N 150 
HIS CA  CB   sing N N 151 
HIS CA  HA   sing N N 152 
HIS C   O    doub N N 153 
HIS C   OXT  sing N N 154 
HIS CB  CG   sing N N 155 
HIS CB  HB2  sing N N 156 
HIS CB  HB3  sing N N 157 
HIS CG  ND1  sing Y N 158 
HIS CG  CD2  doub Y N 159 
HIS ND1 CE1  doub Y N 160 
HIS ND1 HD1  sing N N 161 
HIS CD2 NE2  sing Y N 162 
HIS CD2 HD2  sing N N 163 
HIS CE1 NE2  sing Y N 164 
HIS CE1 HE1  sing N N 165 
HIS NE2 HE2  sing N N 166 
HIS OXT HXT  sing N N 167 
HOH O   H1   sing N N 168 
HOH O   H2   sing N N 169 
ILE N   CA   sing N N 170 
ILE N   H    sing N N 171 
ILE N   H2   sing N N 172 
ILE CA  C    sing N N 173 
ILE CA  CB   sing N N 174 
ILE CA  HA   sing N N 175 
ILE C   O    doub N N 176 
ILE C   OXT  sing N N 177 
ILE CB  CG1  sing N N 178 
ILE CB  CG2  sing N N 179 
ILE CB  HB   sing N N 180 
ILE CG1 CD1  sing N N 181 
ILE CG1 HG12 sing N N 182 
ILE CG1 HG13 sing N N 183 
ILE CG2 HG21 sing N N 184 
ILE CG2 HG22 sing N N 185 
ILE CG2 HG23 sing N N 186 
ILE CD1 HD11 sing N N 187 
ILE CD1 HD12 sing N N 188 
ILE CD1 HD13 sing N N 189 
ILE OXT HXT  sing N N 190 
LEU N   CA   sing N N 191 
LEU N   H    sing N N 192 
LEU N   H2   sing N N 193 
LEU CA  C    sing N N 194 
LEU CA  CB   sing N N 195 
LEU CA  HA   sing N N 196 
LEU C   O    doub N N 197 
LEU C   OXT  sing N N 198 
LEU CB  CG   sing N N 199 
LEU CB  HB2  sing N N 200 
LEU CB  HB3  sing N N 201 
LEU CG  CD1  sing N N 202 
LEU CG  CD2  sing N N 203 
LEU CG  HG   sing N N 204 
LEU CD1 HD11 sing N N 205 
LEU CD1 HD12 sing N N 206 
LEU CD1 HD13 sing N N 207 
LEU CD2 HD21 sing N N 208 
LEU CD2 HD22 sing N N 209 
LEU CD2 HD23 sing N N 210 
LEU OXT HXT  sing N N 211 
LYS N   CA   sing N N 212 
LYS N   H    sing N N 213 
LYS N   H2   sing N N 214 
LYS CA  C    sing N N 215 
LYS CA  CB   sing N N 216 
LYS CA  HA   sing N N 217 
LYS C   O    doub N N 218 
LYS C   OXT  sing N N 219 
LYS CB  CG   sing N N 220 
LYS CB  HB2  sing N N 221 
LYS CB  HB3  sing N N 222 
LYS CG  CD   sing N N 223 
LYS CG  HG2  sing N N 224 
LYS CG  HG3  sing N N 225 
LYS CD  CE   sing N N 226 
LYS CD  HD2  sing N N 227 
LYS CD  HD3  sing N N 228 
LYS CE  NZ   sing N N 229 
LYS CE  HE2  sing N N 230 
LYS CE  HE3  sing N N 231 
LYS NZ  HZ1  sing N N 232 
LYS NZ  HZ2  sing N N 233 
LYS NZ  HZ3  sing N N 234 
LYS OXT HXT  sing N N 235 
MET N   CA   sing N N 236 
MET N   H    sing N N 237 
MET N   H2   sing N N 238 
MET CA  C    sing N N 239 
MET CA  CB   sing N N 240 
MET CA  HA   sing N N 241 
MET C   O    doub N N 242 
MET C   OXT  sing N N 243 
MET CB  CG   sing N N 244 
MET CB  HB2  sing N N 245 
MET CB  HB3  sing N N 246 
MET CG  SD   sing N N 247 
MET CG  HG2  sing N N 248 
MET CG  HG3  sing N N 249 
MET SD  CE   sing N N 250 
MET CE  HE1  sing N N 251 
MET CE  HE2  sing N N 252 
MET CE  HE3  sing N N 253 
MET OXT HXT  sing N N 254 
PHE N   CA   sing N N 255 
PHE N   H    sing N N 256 
PHE N   H2   sing N N 257 
PHE CA  C    sing N N 258 
PHE CA  CB   sing N N 259 
PHE CA  HA   sing N N 260 
PHE C   O    doub N N 261 
PHE C   OXT  sing N N 262 
PHE CB  CG   sing N N 263 
PHE CB  HB2  sing N N 264 
PHE CB  HB3  sing N N 265 
PHE CG  CD1  doub Y N 266 
PHE CG  CD2  sing Y N 267 
PHE CD1 CE1  sing Y N 268 
PHE CD1 HD1  sing N N 269 
PHE CD2 CE2  doub Y N 270 
PHE CD2 HD2  sing N N 271 
PHE CE1 CZ   doub Y N 272 
PHE CE1 HE1  sing N N 273 
PHE CE2 CZ   sing Y N 274 
PHE CE2 HE2  sing N N 275 
PHE CZ  HZ   sing N N 276 
PHE OXT HXT  sing N N 277 
PRO N   CA   sing N N 278 
PRO N   CD   sing N N 279 
PRO N   H    sing N N 280 
PRO CA  C    sing N N 281 
PRO CA  CB   sing N N 282 
PRO CA  HA   sing N N 283 
PRO C   O    doub N N 284 
PRO C   OXT  sing N N 285 
PRO CB  CG   sing N N 286 
PRO CB  HB2  sing N N 287 
PRO CB  HB3  sing N N 288 
PRO CG  CD   sing N N 289 
PRO CG  HG2  sing N N 290 
PRO CG  HG3  sing N N 291 
PRO CD  HD2  sing N N 292 
PRO CD  HD3  sing N N 293 
PRO OXT HXT  sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
SO4 S   O1   doub N N 308 
SO4 S   O2   doub N N 309 
SO4 S   O3   sing N N 310 
SO4 S   O4   sing N N 311 
THR N   CA   sing N N 312 
THR N   H    sing N N 313 
THR N   H2   sing N N 314 
THR CA  C    sing N N 315 
THR CA  CB   sing N N 316 
THR CA  HA   sing N N 317 
THR C   O    doub N N 318 
THR C   OXT  sing N N 319 
THR CB  OG1  sing N N 320 
THR CB  CG2  sing N N 321 
THR CB  HB   sing N N 322 
THR OG1 HG1  sing N N 323 
THR CG2 HG21 sing N N 324 
THR CG2 HG22 sing N N 325 
THR CG2 HG23 sing N N 326 
THR OXT HXT  sing N N 327 
TYR N   CA   sing N N 328 
TYR N   H    sing N N 329 
TYR N   H2   sing N N 330 
TYR CA  C    sing N N 331 
TYR CA  CB   sing N N 332 
TYR CA  HA   sing N N 333 
TYR C   O    doub N N 334 
TYR C   OXT  sing N N 335 
TYR CB  CG   sing N N 336 
TYR CB  HB2  sing N N 337 
TYR CB  HB3  sing N N 338 
TYR CG  CD1  doub Y N 339 
TYR CG  CD2  sing Y N 340 
TYR CD1 CE1  sing Y N 341 
TYR CD1 HD1  sing N N 342 
TYR CD2 CE2  doub Y N 343 
TYR CD2 HD2  sing N N 344 
TYR CE1 CZ   doub Y N 345 
TYR CE1 HE1  sing N N 346 
TYR CE2 CZ   sing Y N 347 
TYR CE2 HE2  sing N N 348 
TYR CZ  OH   sing N N 349 
TYR OH  HH   sing N N 350 
TYR OXT HXT  sing N N 351 
VAL N   CA   sing N N 352 
VAL N   H    sing N N 353 
VAL N   H2   sing N N 354 
VAL CA  C    sing N N 355 
VAL CA  CB   sing N N 356 
VAL CA  HA   sing N N 357 
VAL C   O    doub N N 358 
VAL C   OXT  sing N N 359 
VAL CB  CG1  sing N N 360 
VAL CB  CG2  sing N N 361 
VAL CB  HB   sing N N 362 
VAL CG1 HG11 sing N N 363 
VAL CG1 HG12 sing N N 364 
VAL CG1 HG13 sing N N 365 
VAL CG2 HG21 sing N N 366 
VAL CG2 HG22 sing N N 367 
VAL CG2 HG23 sing N N 368 
VAL OXT HXT  sing N N 369 
# 
_pdbx_audit_support.funding_organization   'Department of Science & Technology (DST, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           GAP0438 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7Y52 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LS8 
_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]   0.021384 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021015 
_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]   0.014458 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
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   . ALA A 1 1   ? 5.154   23.482  10.662 1.00 27.74 ? -2  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 4.471   23.595  11.971 1.00 26.52 ? -2  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 3.624   22.358  12.287 1.00 28.46 ? -2  ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 3.123   22.232  13.404 1.00 32.39 ? -2  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 3.626   24.855  11.979 1.00 25.02 ? -2  ALA A CB  1 
ATOM   6    N  N   . MET A 1 2   ? 3.427   21.423  11.349 1.00 32.80 ? -1  MET A N   1 
ATOM   7    C  CA  . MET A 1 2   ? 2.618   20.251  11.693 1.00 35.84 ? -1  MET A CA  1 
ATOM   8    C  C   . MET A 1 2   ? 3.425   19.248  12.534 1.00 38.44 ? -1  MET A C   1 
ATOM   9    O  O   . MET A 1 2   ? 2.839   18.349  13.131 1.00 42.98 ? -1  MET A O   1 
ATOM   10   C  CB  . MET A 1 2   ? 2.014   19.564  10.458 1.00 40.94 ? -1  MET A CB  1 
ATOM   11   C  CG  . MET A 1 2   ? 3.025   19.027  9.476  1.00 44.02 ? -1  MET A CG  1 
ATOM   12   S  SD  . MET A 1 2   ? 4.170   20.283  8.823  1.00 51.52 ? -1  MET A SD  1 
ATOM   13   C  CE  . MET A 1 2   ? 3.139   21.173  7.659  1.00 49.73 ? -1  MET A CE  1 
ATOM   14   N  N   . GLY A 1 3   ? 4.757   19.440  12.627 1.00 36.18 ? 0   GLY A N   1 
ATOM   15   C  CA  . GLY A 1 3   ? 5.654   18.556  13.353 1.00 34.56 ? 0   GLY A CA  1 
ATOM   16   C  C   . GLY A 1 3   ? 6.555   17.802  12.377 1.00 33.68 ? 0   GLY A C   1 
ATOM   17   O  O   . GLY A 1 3   ? 6.890   18.318  11.309 1.00 37.72 ? 0   GLY A O   1 
ATOM   18   N  N   . MET A 1 4   ? 6.959   16.587  12.760 1.00 28.59 ? 1   MET A N   1 
ATOM   19   C  CA  . MET A 1 4   ? 7.713   15.705  11.887 1.00 25.06 ? 1   MET A CA  1 
ATOM   20   C  C   . MET A 1 4   ? 7.149   14.302  12.064 1.00 21.21 ? 1   MET A C   1 
ATOM   21   O  O   . MET A 1 4   ? 6.435   14.063  13.025 1.00 23.95 ? 1   MET A O   1 
ATOM   22   C  CB  . MET A 1 4   ? 9.187   15.677  12.284 1.00 29.50 ? 1   MET A CB  1 
ATOM   23   C  CG  . MET A 1 4   ? 9.875   17.019  12.248 1.00 34.37 ? 1   MET A CG  1 
ATOM   24   S  SD  . MET A 1 4   ? 11.502  16.905  13.012 1.00 41.42 ? 1   MET A SD  1 
ATOM   25   C  CE  . MET A 1 4   ? 12.473  16.541  11.550 1.00 45.07 ? 1   MET A CE  1 
ATOM   26   N  N   . LYS A 1 5   ? 7.491   13.374  11.174 1.00 20.56 ? 2   LYS A N   1 
ATOM   27   C  CA  . LYS A 1 5   ? 7.280   11.955  11.422 1.00 18.80 ? 2   LYS A CA  1 
ATOM   28   C  C   . LYS A 1 5   ? 8.627   11.261  11.287 1.00 17.12 ? 2   LYS A C   1 
ATOM   29   O  O   . LYS A 1 5   ? 9.420   11.644  10.434 1.00 17.94 ? 2   LYS A O   1 
ATOM   30   C  CB  . LYS A 1 5   ? 6.284   11.355  10.437 1.00 22.68 ? 2   LYS A CB  1 
ATOM   31   C  CG  . LYS A 1 5   ? 4.846   11.826  10.605 1.00 28.12 ? 2   LYS A CG  1 
ATOM   32   C  CD  . LYS A 1 5   ? 3.765   10.792  10.390 1.00 33.92 ? 2   LYS A CD  1 
ATOM   33   C  CE  . LYS A 1 5   ? 2.543   11.058  11.246 1.00 32.73 ? 2   LYS A CE  1 
ATOM   34   N  N   . MET A 1 6   ? 8.844   10.227  12.100 1.00 15.55 ? 3   MET A N   1 
ATOM   35   C  CA  . MET A 1 6   ? 10.068  9.459   12.038 1.00 14.94 ? 3   MET A CA  1 
ATOM   36   C  C   . MET A 1 6   ? 9.728   7.989   11.848 1.00 14.07 ? 3   MET A C   1 
ATOM   37   O  O   . MET A 1 6   ? 9.103   7.409   12.719 1.00 14.66 ? 3   MET A O   1 
ATOM   38   C  CB  . MET A 1 6   ? 10.906  9.660   13.296 1.00 15.28 ? 3   MET A CB  1 
ATOM   39   C  CG  . MET A 1 6   ? 12.183  8.838   13.278 1.00 16.55 ? 3   MET A CG  1 
ATOM   40   S  SD  . MET A 1 6   ? 13.196  8.981   14.740 1.00 25.31 ? 3   MET A SD  1 
ATOM   41   C  CE  . MET A 1 6   ? 13.877  10.605  14.467 1.00 28.70 ? 3   MET A CE  1 
ATOM   42   N  N   . ILE A 1 7   ? 10.073  7.463   10.681 1.00 13.56 ? 4   ILE A N   1 
ATOM   43   C  CA  . ILE A 1 7   ? 9.754   6.080   10.328 1.00 12.90 ? 4   ILE A CA  1 
ATOM   44   C  C   . ILE A 1 7   ? 11.027  5.280   10.542 1.00 12.80 ? 4   ILE A C   1 
ATOM   45   O  O   . ILE A 1 7   ? 12.021  5.497   9.842  1.00 14.10 ? 4   ILE A O   1 
ATOM   46   C  CB  . ILE A 1 7   ? 9.312   5.977   8.856  1.00 14.59 ? 4   ILE A CB  1 
ATOM   47   C  CG1 . ILE A 1 7   ? 8.340   7.074   8.430  1.00 16.13 ? 4   ILE A CG1 1 
ATOM   48   C  CG2 . ILE A 1 7   ? 8.763   4.578   8.597  1.00 15.13 ? 4   ILE A CG2 1 
ATOM   49   C  CD1 . ILE A 1 7   ? 7.041   7.063   9.161  1.00 16.06 ? 4   ILE A CD1 1 
ATOM   50   N  N   . VAL A 1 8   ? 10.978  4.370   11.513 1.00 12.45 ? 5   VAL A N   1 
ATOM   51   C  CA  . VAL A 1 8   ? 12.171  3.616   11.876 1.00 12.00 ? 5   VAL A CA  1 
ATOM   52   C  C   . VAL A 1 8   ? 12.003  2.183   11.373 1.00 12.06 ? 5   VAL A C   1 
ATOM   53   O  O   . VAL A 1 8   ? 11.071  1.523   11.797 1.00 13.62 ? 5   VAL A O   1 
ATOM   54   C  CB  . VAL A 1 8   ? 12.386  3.590   13.398 1.00 13.62 ? 5   VAL A CB  1 
ATOM   55   C  CG1 . VAL A 1 8   ? 13.643  2.826   13.733 1.00 14.65 ? 5   VAL A CG1 1 
ATOM   56   C  CG2 . VAL A 1 8   ? 12.426  5.006   13.982 1.00 14.64 ? 5   VAL A CG2 1 
ATOM   57   N  N   . GLY A 1 9   ? 12.916  1.750   10.505 1.00 10.83 ? 6   GLY A N   1 
ATOM   58   C  CA  . GLY A 1 9   ? 12.965  0.384   10.047 1.00 10.94 ? 6   GLY A CA  1 
ATOM   59   C  C   . GLY A 1 9   ? 13.993  -0.396  10.811 1.00 11.12 ? 6   GLY A C   1 
ATOM   60   O  O   . GLY A 1 9   ? 15.130  0.023   10.826 1.00 12.33 ? 6   GLY A O   1 
ATOM   61   N  N   . LEU A 1 10  ? 13.615  -1.517  11.423 1.00 11.75 ? 7   LEU A N   1 
ATOM   62   C  CA  . LEU A 1 10  ? 14.549  -2.264  12.235 1.00 11.76 ? 7   LEU A CA  1 
ATOM   63   C  C   . LEU A 1 10  ? 15.276  -3.320  11.414 1.00 10.99 ? 7   LEU A C   1 
ATOM   64   O  O   . LEU A 1 10  ? 14.796  -3.813  10.384 1.00 11.51 ? 7   LEU A O   1 
ATOM   65   C  CB  . LEU A 1 10  ? 13.837  -2.920  13.409 1.00 11.65 ? 7   LEU A CB  1 
ATOM   66   C  CG  . LEU A 1 10  ? 13.113  -1.965  14.340 1.00 11.75 ? 7   LEU A CG  1 
ATOM   67   C  CD1 . LEU A 1 10  ? 12.586  -2.709  15.555 1.00 12.08 ? 7   LEU A CD1 1 
ATOM   68   C  CD2 . LEU A 1 10  ? 14.016  -0.816  14.753 1.00 12.57 ? 7   LEU A CD2 1 
ATOM   69   N  N   . GLY A 1 11  ? 16.488  -3.649  11.863 1.00 11.18 ? 8   GLY A N   1 
ATOM   70   C  CA  . GLY A 1 11  ? 17.315  -4.635  11.196 1.00 11.28 ? 8   GLY A CA  1 
ATOM   71   C  C   . GLY A 1 11  ? 18.703  -4.641  11.808 1.00 11.72 ? 8   GLY A C   1 
ATOM   72   O  O   . GLY A 1 11  ? 18.970  -3.920  12.774 1.00 12.08 ? 8   GLY A O   1 
ATOM   73   N  N   . ASN A 1 12  ? 19.543  -5.476  11.214 1.00 12.37 ? 9   ASN A N   1 
ATOM   74   C  CA  . ASN A 1 12  ? 20.952  -5.530  11.551 1.00 12.62 ? 9   ASN A CA  1 
ATOM   75   C  C   . ASN A 1 12  ? 21.756  -4.878  10.444 1.00 12.39 ? 9   ASN A C   1 
ATOM   76   O  O   . ASN A 1 12  ? 21.374  -4.963  9.276  1.00 13.63 ? 9   ASN A O   1 
ATOM   77   C  CB  . ASN A 1 12  ? 21.439  -6.972  11.708 1.00 13.27 ? 9   ASN A CB  1 
ATOM   78   C  CG  . ASN A 1 12  ? 20.935  -7.592  12.985 1.00 13.03 ? 9   ASN A CG  1 
ATOM   79   O  OD1 . ASN A 1 12  ? 21.053  -6.984  14.041 1.00 15.47 ? 9   ASN A OD1 1 
ATOM   80   N  ND2 . ASN A 1 12  ? 20.492  -8.834  12.942 1.00 14.28 ? 9   ASN A ND2 1 
ATOM   81   N  N   . PRO A 1 13  ? 22.894  -4.245  10.769 1.00 12.24 ? 10  PRO A N   1 
ATOM   82   C  CA  . PRO A 1 13  ? 23.718  -3.613  9.743  1.00 12.77 ? 10  PRO A CA  1 
ATOM   83   C  C   . PRO A 1 13  ? 24.546  -4.627  8.976  1.00 14.24 ? 10  PRO A C   1 
ATOM   84   O  O   . PRO A 1 13  ? 24.732  -5.716  9.458  1.00 15.20 ? 10  PRO A O   1 
ATOM   85   C  CB  . PRO A 1 13  ? 24.635  -2.738  10.583 1.00 13.86 ? 10  PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 13  ? 24.830  -3.523  11.847 1.00 13.55 ? 10  PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 13  ? 23.503  -4.185  12.112 1.00 13.17 ? 10  PRO A CD  1 
ATOM   88   N  N   . GLY A 1 14  ? 25.059  -4.200  7.841  1.00 15.91 ? 11  GLY A N   1 
ATOM   89   C  CA  . GLY A 1 14  ? 26.063  -4.958  7.118  1.00 16.57 ? 11  GLY A CA  1 
ATOM   90   C  C   . GLY A 1 14  ? 25.434  -5.752  5.977  1.00 15.95 ? 11  GLY A C   1 
ATOM   91   O  O   . GLY A 1 14  ? 24.244  -6.104  5.992  1.00 16.29 ? 11  GLY A O   1 
ATOM   92   N  N   . THR A 1 15  ? 26.279  -6.104  5.022  1.00 16.03 ? 12  THR A N   1 
ATOM   93   C  CA  . THR A 1 15  ? 25.823  -6.876  3.892  1.00 16.61 ? 12  THR A CA  1 
ATOM   94   C  C   . THR A 1 15  ? 25.437  -8.279  4.369  1.00 17.14 ? 12  THR A C   1 
ATOM   95   O  O   . THR A 1 15  ? 24.644  -8.876  3.707  1.00 19.75 ? 12  THR A O   1 
ATOM   96   C  CB  . THR A 1 15  ? 26.857  -6.853  2.772  1.00 16.06 ? 12  THR A CB  1 
ATOM   97   O  OG1 . THR A 1 15  ? 28.001  -7.565  3.244  1.00 16.14 ? 12  THR A OG1 1 
ATOM   98   C  CG2 . THR A 1 15  ? 27.206  -5.446  2.329  1.00 16.80 ? 12  THR A CG2 1 
ATOM   99   N  N   . LYS A 1 16  ? 25.976  -8.756  5.507  1.00 18.26 ? 13  LYS A N   1 
ATOM   100  C  CA  . LYS A 1 16  ? 25.625  -10.047 6.094  1.00 20.24 ? 13  LYS A CA  1 
ATOM   101  C  C   . LYS A 1 16  ? 24.108  -10.187 6.259  1.00 19.62 ? 13  LYS A C   1 
ATOM   102  O  O   . LYS A 1 16  ? 23.572  -11.271 6.085  1.00 22.86 ? 13  LYS A O   1 
ATOM   103  C  CB  . LYS A 1 16  ? 26.310  -10.244 7.457  1.00 21.46 ? 13  LYS A CB  1 
ATOM   104  C  CG  . LYS A 1 16  ? 26.236  -11.658 8.016  1.00 26.82 ? 13  LYS A CG  1 
ATOM   105  C  CD  . LYS A 1 16  ? 27.109  -11.892 9.231  1.00 29.92 ? 13  LYS A CD  1 
ATOM   106  C  CE  . LYS A 1 16  ? 28.581  -12.042 8.917  1.00 33.66 ? 13  LYS A CE  1 
ATOM   107  N  NZ  . LYS A 1 16  ? 29.262  -12.983 9.841  1.00 36.59 ? 13  LYS A NZ  1 
ATOM   108  N  N   . TYR A 1 17  ? 23.390  -9.113  6.552  1.00 16.65 ? 14  TYR A N   1 
ATOM   109  C  CA  . TYR A 1 17  ? 22.014  -9.173  7.023  1.00 14.83 ? 14  TYR A CA  1 
ATOM   110  C  C   . TYR A 1 17  ? 21.013  -8.485  6.111  1.00 14.79 ? 14  TYR A C   1 
ATOM   111  O  O   . TYR A 1 17  ? 19.822  -8.584  6.372  1.00 13.54 ? 14  TYR A O   1 
ATOM   112  C  CB  . TYR A 1 17  ? 21.955  -8.576  8.424  1.00 14.56 ? 14  TYR A CB  1 
ATOM   113  C  CG  . TYR A 1 17  ? 22.744  -9.444  9.378  1.00 15.39 ? 14  TYR A CG  1 
ATOM   114  C  CD1 . TYR A 1 17  ? 22.339  -10.756 9.602  1.00 17.30 ? 14  TYR A CD1 1 
ATOM   115  C  CD2 . TYR A 1 17  ? 23.898  -8.979  10.008 1.00 15.89 ? 14  TYR A CD2 1 
ATOM   116  C  CE1 . TYR A 1 17  ? 23.056  -11.579 10.434 1.00 18.37 ? 14  TYR A CE1 1 
ATOM   117  C  CE2 . TYR A 1 17  ? 24.606  -9.803  10.861 1.00 17.93 ? 14  TYR A CE2 1 
ATOM   118  C  CZ  . TYR A 1 17  ? 24.195  -11.112 11.061 1.00 17.61 ? 14  TYR A CZ  1 
ATOM   119  O  OH  . TYR A 1 17  ? 24.892  -11.962 11.884 1.00 20.69 ? 14  TYR A OH  1 
ATOM   120  N  N   . GLN A 1 18  ? 21.447  -7.825  5.048  1.00 15.98 ? 15  GLN A N   1 
ATOM   121  C  CA  . GLN A 1 18  ? 20.573  -6.934  4.319  1.00 16.71 ? 15  GLN A CA  1 
ATOM   122  C  C   . GLN A 1 18  ? 19.415  -7.646  3.636  1.00 15.88 ? 15  GLN A C   1 
ATOM   123  O  O   . GLN A 1 18  ? 18.426  -6.992  3.385  1.00 16.64 ? 15  GLN A O   1 
ATOM   124  C  CB  . GLN A 1 18  ? 21.386  -6.068  3.361  1.00 20.18 ? 15  GLN A CB  1 
ATOM   125  C  CG  . GLN A 1 18  ? 22.017  -6.772  2.201  1.00 22.71 ? 15  GLN A CG  1 
ATOM   126  C  CD  . GLN A 1 18  ? 22.963  -5.847  1.462  1.00 26.76 ? 15  GLN A CD  1 
ATOM   127  O  OE1 . GLN A 1 18  ? 23.497  -4.859  1.982  1.00 29.39 ? 15  GLN A OE1 1 
ATOM   128  N  NE2 . GLN A 1 18  ? 23.241  -6.212  0.232  1.00 29.17 ? 15  GLN A NE2 1 
ATOM   129  N  N   . TYR A 1 19  ? 19.530  -8.958  3.385  1.00 15.97 ? 16  TYR A N   1 
ATOM   130  C  CA  . TYR A 1 19  ? 18.474  -9.704  2.742  1.00 16.18 ? 16  TYR A CA  1 
ATOM   131  C  C   . TYR A 1 19  ? 17.750  -10.672 3.688  1.00 16.30 ? 16  TYR A C   1 
ATOM   132  O  O   . TYR A 1 19  ? 16.874  -11.425 3.270  1.00 17.80 ? 16  TYR A O   1 
ATOM   133  C  CB  . TYR A 1 19  ? 19.081  -10.497 1.577  1.00 17.85 ? 16  TYR A CB  1 
ATOM   134  C  CG  . TYR A 1 19  ? 19.777  -9.626  0.544  1.00 21.08 ? 16  TYR A CG  1 
ATOM   135  C  CD1 . TYR A 1 19  ? 19.065  -8.694  -0.190 1.00 24.71 ? 16  TYR A CD1 1 
ATOM   136  C  CD2 . TYR A 1 19  ? 21.136  -9.747  0.288  1.00 24.37 ? 16  TYR A CD2 1 
ATOM   137  C  CE1 . TYR A 1 19  ? 19.680  -7.919  -1.166 1.00 28.16 ? 16  TYR A CE1 1 
ATOM   138  C  CE2 . TYR A 1 19  ? 21.763  -8.970  -0.669 1.00 28.76 ? 16  TYR A CE2 1 
ATOM   139  C  CZ  . TYR A 1 19  ? 21.036  -8.040  -1.386 1.00 28.57 ? 16  TYR A CZ  1 
ATOM   140  O  OH  . TYR A 1 19  ? 21.566  -7.227  -2.351 1.00 31.60 ? 16  TYR A OH  1 
ATOM   141  N  N   . THR A 1 20  ? 18.009  -10.602 4.984  1.00 13.55 ? 17  THR A N   1 
ATOM   142  C  CA  . THR A 1 20  ? 17.426  -11.524 5.922  1.00 13.37 ? 17  THR A CA  1 
ATOM   143  C  C   . THR A 1 20  ? 16.050  -11.030 6.356  1.00 12.24 ? 17  THR A C   1 
ATOM   144  O  O   . THR A 1 20  ? 15.756  -9.841  6.319  1.00 12.03 ? 17  THR A O   1 
ATOM   145  C  CB  . THR A 1 20  ? 18.357  -11.741 7.118  1.00 13.29 ? 17  THR A CB  1 
ATOM   146  O  OG1 . THR A 1 20  ? 18.504  -10.538 7.881  1.00 13.07 ? 17  THR A OG1 1 
ATOM   147  C  CG2 . THR A 1 20  ? 19.708  -12.306 6.751  1.00 14.61 ? 17  THR A CG2 1 
ATOM   148  N  N   . LYS A 1 21  ? 15.219  -11.979 6.794  1.00 11.99 ? 18  LYS A N   1 
ATOM   149  C  CA  . LYS A 1 21  ? 13.849  -11.651 7.192  1.00 11.34 ? 18  LYS A CA  1 
ATOM   150  C  C   . LYS A 1 21  ? 13.805  -10.638 8.343  1.00 12.20 ? 18  LYS A C   1 
ATOM   151  O  O   . LYS A 1 21  ? 12.893  -9.802  8.404  1.00 12.00 ? 18  LYS A O   1 
ATOM   152  C  CB  . LYS A 1 21  ? 13.097  -12.904 7.646  1.00 12.59 ? 18  LYS A CB  1 
ATOM   153  C  CG  . LYS A 1 21  ? 13.031  -14.025 6.617  1.00 13.72 ? 18  LYS A CG  1 
ATOM   154  C  CD  . LYS A 1 21  ? 12.154  -15.204 7.130  1.00 13.52 ? 18  LYS A CD  1 
ATOM   155  C  CE  . LYS A 1 21  ? 12.339  -16.491 6.369  1.00 14.41 ? 18  LYS A CE  1 
ATOM   156  N  NZ  . LYS A 1 21  ? 13.723  -16.998 6.491  1.00 14.49 ? 18  LYS A NZ  1 
ATOM   157  N  N   . HIS A 1 22  ? 14.788  -10.708 9.251  1.00 11.83 ? 19  HIS A N   1 
ATOM   158  C  CA  . HIS A 1 22  ? 14.899  -9.816  10.404 1.00 11.90 ? 19  HIS A CA  1 
ATOM   159  C  C   . HIS A 1 22  ? 15.158  -8.376  9.968  1.00 12.43 ? 19  HIS A C   1 
ATOM   160  O  O   . HIS A 1 22  ? 14.991  -7.475  10.780 1.00 13.09 ? 19  HIS A O   1 
ATOM   161  C  CB  . HIS A 1 22  ? 16.034  -10.302 11.303 1.00 11.94 ? 19  HIS A CB  1 
ATOM   162  C  CG  . HIS A 1 22  ? 15.890  -10.099 12.756 1.00 12.52 ? 19  HIS A CG  1 
ATOM   163  N  ND1 . HIS A 1 22  ? 14.727  -10.180 13.477 1.00 13.43 ? 19  HIS A ND1 1 
ATOM   164  C  CD2 . HIS A 1 22  ? 16.883  -9.943  13.664 1.00 14.38 ? 19  HIS A CD2 1 
ATOM   165  C  CE1 . HIS A 1 22  ? 14.995  -10.080 14.767 1.00 14.40 ? 19  HIS A CE1 1 
ATOM   166  N  NE2 . HIS A 1 22  ? 16.301  -9.935  14.897 1.00 16.10 ? 19  HIS A NE2 1 
ATOM   167  N  N   . ASN A 1 23  ? 15.515  -8.171  8.696  1.00 11.27 ? 20  ASN A N   1 
ATOM   168  C  CA  . ASN A 1 23  ? 15.767  -6.866  8.123  1.00 11.87 ? 20  ASN A CA  1 
ATOM   169  C  C   . ASN A 1 23  ? 14.596  -6.339  7.304  1.00 11.92 ? 20  ASN A C   1 
ATOM   170  O  O   . ASN A 1 23  ? 14.739  -5.356  6.594  1.00 12.09 ? 20  ASN A O   1 
ATOM   171  C  CB  . ASN A 1 23  ? 17.025  -6.875  7.283  1.00 12.25 ? 20  ASN A CB  1 
ATOM   172  C  CG  . ASN A 1 23  ? 18.239  -6.513  8.107  1.00 12.22 ? 20  ASN A CG  1 
ATOM   173  O  OD1 . ASN A 1 23  ? 18.444  -7.022  9.207  1.00 12.17 ? 20  ASN A OD1 1 
ATOM   174  N  ND2 . ASN A 1 23  ? 19.018  -5.567  7.630  1.00 13.22 ? 20  ASN A ND2 1 
ATOM   175  N  N   . ILE A 1 24  ? 13.395  -6.897  7.472  1.00 11.59 ? 21  ILE A N   1 
ATOM   176  C  CA  . ILE A 1 24  ? 12.271  -6.448  6.676  1.00 12.34 ? 21  ILE A CA  1 
ATOM   177  C  C   . ILE A 1 24  ? 12.032  -4.955  6.920  1.00 11.17 ? 21  ILE A C   1 
ATOM   178  O  O   . ILE A 1 24  ? 11.633  -4.252  5.992  1.00 11.71 ? 21  ILE A O   1 
ATOM   179  C  CB  . ILE A 1 24  ? 11.040  -7.328  6.932  1.00 12.45 ? 21  ILE A CB  1 
ATOM   180  C  CG1 . ILE A 1 24  ? 9.910   -7.042  5.941  1.00 13.13 ? 21  ILE A CG1 1 
ATOM   181  C  CG2 . ILE A 1 24  ? 10.519  -7.196  8.367  1.00 12.79 ? 21  ILE A CG2 1 
ATOM   182  C  CD1 . ILE A 1 24  ? 10.280  -7.143  4.492  1.00 14.04 ? 21  ILE A CD1 1 
ATOM   183  N  N   . GLY A 1 25  ? 12.227  -4.479  8.162  1.00 11.32 ? 22  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 25  ? 12.043  -3.059  8.423  1.00 11.71 ? 22  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 25  ? 12.968  -2.181  7.584  1.00 11.56 ? 22  GLY A C   1 
ATOM   186  O  O   . GLY A 1 25  ? 12.525  -1.191  7.015  1.00 12.13 ? 22  GLY A O   1 
ATOM   187  N  N   . PHE A 1 26  ? 14.262  -2.520  7.530  1.00 10.94 ? 23  PHE A N   1 
ATOM   188  C  CA  . PHE A 1 26  ? 15.186  -1.826  6.637  1.00 12.09 ? 23  PHE A CA  1 
ATOM   189  C  C   . PHE A 1 26  ? 14.678  -1.856  5.208  1.00 12.20 ? 23  PHE A C   1 
ATOM   190  O  O   . PHE A 1 26  ? 14.711  -0.859  4.488  1.00 13.42 ? 23  PHE A O   1 
ATOM   191  C  CB  . PHE A 1 26  ? 16.575  -2.452  6.613  1.00 12.46 ? 23  PHE A CB  1 
ATOM   192  C  CG  . PHE A 1 26  ? 17.540  -2.129  7.724  1.00 11.62 ? 23  PHE A CG  1 
ATOM   193  C  CD1 . PHE A 1 26  ? 17.134  -1.630  8.946  1.00 12.18 ? 23  PHE A CD1 1 
ATOM   194  C  CD2 . PHE A 1 26  ? 18.906  -2.300  7.500  1.00 12.90 ? 23  PHE A CD2 1 
ATOM   195  C  CE1 . PHE A 1 26  ? 18.099  -1.371  9.922  1.00 12.56 ? 23  PHE A CE1 1 
ATOM   196  C  CE2 . PHE A 1 26  ? 19.853  -2.059  8.470  1.00 14.35 ? 23  PHE A CE2 1 
ATOM   197  C  CZ  . PHE A 1 26  ? 19.451  -1.567  9.683  1.00 13.10 ? 23  PHE A CZ  1 
ATOM   198  N  N   . MET A 1 27  ? 14.202  -3.035  4.775  1.00 11.95 ? 24  MET A N   1 
ATOM   199  C  CA  . MET A 1 27  ? 13.797  -3.179  3.387  1.00 12.98 ? 24  MET A CA  1 
ATOM   200  C  C   . MET A 1 27  ? 12.640  -2.246  3.064  1.00 12.81 ? 24  MET A C   1 
ATOM   201  O  O   . MET A 1 27  ? 12.550  -1.683  1.954  1.00 14.09 ? 24  MET A O   1 
ATOM   202  C  CB  . MET A 1 27  ? 13.369  -4.612  3.121  1.00 13.30 ? 24  MET A CB  1 
ATOM   203  C  CG  . MET A 1 27  ? 14.490  -5.596  3.195  1.00 14.77 ? 24  MET A CG  1 
ATOM   204  S  SD  . MET A 1 27  ? 13.795  -7.297  3.130  1.00 18.17 ? 24  MET A SD  1 
ATOM   205  C  CE  . MET A 1 27  ? 15.265  -8.215  3.559  1.00 20.33 ? 24  MET A CE  1 
ATOM   206  N  N   . VAL A 1 28  ? 11.695  -2.112  3.986  1.00 12.62 ? 25  VAL A N   1 
ATOM   207  C  CA  . VAL A 1 28  ? 10.543  -1.255  3.775  1.00 13.20 ? 25  VAL A CA  1 
ATOM   208  C  C   . VAL A 1 28  ? 10.969  0.214   3.722  1.00 11.65 ? 25  VAL A C   1 
ATOM   209  O  O   . VAL A 1 28  ? 10.564  0.959   2.831  1.00 13.16 ? 25  VAL A O   1 
ATOM   210  C  CB  . VAL A 1 28  ? 9.434   -1.488  4.809  1.00 12.58 ? 25  VAL A CB  1 
ATOM   211  C  CG1 . VAL A 1 28  ? 8.358   -0.424  4.692  1.00 13.51 ? 25  VAL A CG1 1 
ATOM   212  C  CG2 . VAL A 1 28  ? 8.807   -2.881  4.681  1.00 13.05 ? 25  VAL A CG2 1 
ATOM   213  N  N   . VAL A 1 29  ? 11.798  0.667   4.673  1.00 11.99 ? 26  VAL A N   1 
ATOM   214  C  CA  . VAL A 1 29  ? 12.174  2.069   4.629  1.00 12.72 ? 26  VAL A CA  1 
ATOM   215  C  C   . VAL A 1 29  ? 13.063  2.356   3.418  1.00 13.05 ? 26  VAL A C   1 
ATOM   216  O  O   . VAL A 1 29  ? 13.022  3.472   2.907  1.00 13.70 ? 26  VAL A O   1 
ATOM   217  C  CB  . VAL A 1 29  ? 12.747  2.608   5.956  1.00 14.01 ? 26  VAL A CB  1 
ATOM   218  C  CG1 . VAL A 1 29  ? 11.712  2.560   7.068  1.00 14.63 ? 26  VAL A CG1 1 
ATOM   219  C  CG2 . VAL A 1 29  ? 14.057  1.985   6.359  1.00 13.75 ? 26  VAL A CG2 1 
ATOM   220  N  N   . ASP A 1 30  ? 13.827  1.381   2.920  1.00 13.45 ? 27  ASP A N   1 
ATOM   221  C  CA  . ASP A 1 30  ? 14.578  1.572   1.690  1.00 15.17 ? 27  ASP A CA  1 
ATOM   222  C  C   . ASP A 1 30  ? 13.616  1.843   0.536  1.00 14.66 ? 27  ASP A C   1 
ATOM   223  O  O   . ASP A 1 30  ? 13.895  2.651   -0.351 1.00 16.31 ? 27  ASP A O   1 
ATOM   224  C  CB  . ASP A 1 30  ? 15.416  0.343   1.390  1.00 16.73 ? 27  ASP A CB  1 
ATOM   225  C  CG  . ASP A 1 30  ? 16.651  0.167   2.245  1.00 18.88 ? 27  ASP A CG  1 
ATOM   226  O  OD1 . ASP A 1 30  ? 17.073  1.154   2.857  1.00 21.65 ? 27  ASP A OD1 1 
ATOM   227  O  OD2 . ASP A 1 30  ? 17.198  -0.964  2.242  1.00 23.62 ? 27  ASP A OD2 1 
ATOM   228  N  N   . LYS A 1 31  ? 12.485  1.119   0.505  1.00 15.22 ? 28  LYS A N   1 
ATOM   229  C  CA  . LYS A 1 31  ? 11.500  1.278   -0.549 1.00 16.68 ? 28  LYS A CA  1 
ATOM   230  C  C   . LYS A 1 31  ? 10.851  2.664   -0.449 1.00 16.49 ? 28  LYS A C   1 
ATOM   231  O  O   . LYS A 1 31  ? 10.607  3.321   -1.459 1.00 18.25 ? 28  LYS A O   1 
ATOM   232  C  CB  . LYS A 1 31  ? 10.470  0.167   -0.372 1.00 19.04 ? 28  LYS A CB  1 
ATOM   233  C  CG  . LYS A 1 31  ? 9.701   -0.289  -1.566 1.00 23.70 ? 28  LYS A CG  1 
ATOM   234  C  CD  . LYS A 1 31  ? 8.991   -1.581  -1.303 1.00 22.04 ? 28  LYS A CD  1 
ATOM   235  C  CE  . LYS A 1 31  ? 7.791   -1.734  -2.210 1.00 25.40 ? 28  LYS A CE  1 
ATOM   236  N  NZ  . LYS A 1 31  ? 8.209   -1.890  -3.621 1.00 25.10 ? 28  LYS A NZ  1 
ATOM   237  N  N   . ILE A 1 32  ? 10.522  3.095   0.774  1.00 15.96 ? 29  ILE A N   1 
ATOM   238  C  CA  . ILE A 1 32  ? 9.970   4.429   0.975  1.00 16.67 ? 29  ILE A CA  1 
ATOM   239  C  C   . ILE A 1 32  ? 10.971  5.501   0.529  1.00 16.54 ? 29  ILE A C   1 
ATOM   240  O  O   . ILE A 1 32  ? 10.562  6.486   -0.112 1.00 19.73 ? 29  ILE A O   1 
ATOM   241  C  CB  . ILE A 1 32  ? 9.527   4.637   2.431  1.00 16.08 ? 29  ILE A CB  1 
ATOM   242  C  CG1 . ILE A 1 32  ? 8.474   3.633   2.878  1.00 16.31 ? 29  ILE A CG1 1 
ATOM   243  C  CG2 . ILE A 1 32  ? 9.014   6.066   2.644  1.00 17.65 ? 29  ILE A CG2 1 
ATOM   244  C  CD1 . ILE A 1 32  ? 8.262   3.620   4.371  1.00 17.24 ? 29  ILE A CD1 1 
ATOM   245  N  N   . ALA A 1 33  ? 12.275  5.290   0.824  1.00 16.42 ? 30  ALA A N   1 
ATOM   246  C  CA  . ALA A 1 33  ? 13.295  6.235   0.402  1.00 17.89 ? 30  ALA A CA  1 
ATOM   247  C  C   . ALA A 1 33  ? 13.343  6.351   -1.123 1.00 19.01 ? 30  ALA A C   1 
ATOM   248  O  O   . ALA A 1 33  ? 13.367  7.449   -1.661 1.00 20.69 ? 30  ALA A O   1 
ATOM   249  C  CB  . ALA A 1 33  ? 14.623  5.826   0.934  1.00 17.28 ? 30  ALA A CB  1 
ATOM   250  N  N   . ARG A 1 34  ? 13.300  5.204   -1.824 1.00 18.92 ? 31  ARG A N   1 
ATOM   251  C  CA  . ARG A 1 34  ? 13.282  5.223   -3.279 1.00 20.63 ? 31  ARG A CA  1 
ATOM   252  C  C   . ARG A 1 34  ? 12.036  5.957   -3.791 1.00 21.31 ? 31  ARG A C   1 
ATOM   253  O  O   . ARG A 1 34  ? 12.146  6.715   -4.759 1.00 24.44 ? 31  ARG A O   1 
ATOM   254  C  CB  . ARG A 1 34  ? 13.414  3.801   -3.838 1.00 21.58 ? 31  ARG A CB  1 
ATOM   255  C  CG  . ARG A 1 34  ? 14.783  3.172   -3.623 1.00 23.33 ? 31  ARG A CG  1 
ATOM   256  C  CD  . ARG A 1 34  ? 14.965  1.822   -4.310 1.00 25.13 ? 31  ARG A CD  1 
ATOM   257  N  NE  . ARG A 1 34  ? 14.080  0.756   -3.832 1.00 28.28 ? 31  ARG A NE  1 
ATOM   258  C  CZ  . ARG A 1 34  ? 14.406  -0.189  -2.923 1.00 27.93 ? 31  ARG A CZ  1 
ATOM   259  N  NH1 . ARG A 1 34  ? 15.566  -0.175  -2.298 1.00 31.29 ? 31  ARG A NH1 1 
ATOM   260  N  NH2 . ARG A 1 34  ? 13.565  -1.158  -2.628 1.00 28.67 ? 31  ARG A NH2 1 
ATOM   261  N  N   . GLU A 1 35  ? 10.861  5.718   -3.194 1.00 21.10 ? 32  GLU A N   1 
ATOM   262  C  CA  . GLU A 1 35  ? 9.583   6.322   -3.584 1.00 22.30 ? 32  GLU A CA  1 
ATOM   263  C  C   . GLU A 1 35  ? 9.700   7.854   -3.582 1.00 23.80 ? 32  GLU A C   1 
ATOM   264  O  O   . GLU A 1 35  ? 9.054   8.537   -4.374 1.00 24.09 ? 32  GLU A O   1 
ATOM   265  C  CB  . GLU A 1 35  ? 8.494   5.829   -2.616 1.00 24.42 ? 32  GLU A CB  1 
ATOM   266  C  CG  . GLU A 1 35  ? 7.072   6.377   -2.783 1.00 26.97 ? 32  GLU A CG  1 
ATOM   267  C  CD  . GLU A 1 35  ? 6.185   6.089   -1.568 1.00 28.47 ? 32  GLU A CD  1 
ATOM   268  O  OE1 . GLU A 1 35  ? 6.738   5.820   -0.484 1.00 26.98 ? 32  GLU A OE1 1 
ATOM   269  O  OE2 . GLU A 1 35  ? 4.932   6.163   -1.679 1.00 31.93 ? 32  GLU A OE2 1 
ATOM   270  N  N   . HIS A 1 36  ? 10.548  8.384   -2.695 1.00 23.53 ? 33  HIS A N   1 
ATOM   271  C  CA  . HIS A 1 36  ? 10.629  9.818   -2.448 1.00 24.77 ? 33  HIS A CA  1 
ATOM   272  C  C   . HIS A 1 36  ? 11.980  10.395  -2.871 1.00 25.42 ? 33  HIS A C   1 
ATOM   273  O  O   . HIS A 1 36  ? 12.269  11.545  -2.549 1.00 27.63 ? 33  HIS A O   1 
ATOM   274  C  CB  . HIS A 1 36  ? 10.330  10.071  -0.971 1.00 27.59 ? 33  HIS A CB  1 
ATOM   275  C  CG  . HIS A 1 36  ? 8.895   9.871   -0.667 1.00 27.70 ? 33  HIS A CG  1 
ATOM   276  N  ND1 . HIS A 1 36  ? 7.930   10.803  -0.967 1.00 32.00 ? 33  HIS A ND1 1 
ATOM   277  C  CD2 . HIS A 1 36  ? 8.248   8.838   -0.113 1.00 28.25 ? 33  HIS A CD2 1 
ATOM   278  C  CE1 . HIS A 1 36  ? 6.747   10.347  -0.589 1.00 32.23 ? 33  HIS A CE1 1 
ATOM   279  N  NE2 . HIS A 1 36  ? 6.913   9.150   -0.070 1.00 29.15 ? 33  HIS A NE2 1 
ATOM   280  N  N   . GLN A 1 37  ? 12.803  9.608   -3.583 1.00 25.75 ? 34  GLN A N   1 
ATOM   281  C  CA  . GLN A 1 37  ? 14.115  10.049  -4.050 1.00 26.59 ? 34  GLN A CA  1 
ATOM   282  C  C   . GLN A 1 37  ? 14.970  10.564  -2.882 1.00 27.25 ? 34  GLN A C   1 
ATOM   283  O  O   . GLN A 1 37  ? 15.777  11.484  -3.030 1.00 29.67 ? 34  GLN A O   1 
ATOM   284  C  CB  . GLN A 1 37  ? 13.960  11.055  -5.200 1.00 30.01 ? 34  GLN A CB  1 
ATOM   285  N  N   . ALA A 1 38  ? 14.844  9.912   -1.724 1.00 24.82 ? 35  ALA A N   1 
ATOM   286  C  CA  . ALA A 1 38  ? 15.545  10.292  -0.510 1.00 24.52 ? 35  ALA A CA  1 
ATOM   287  C  C   . ALA A 1 38  ? 16.758  9.380   -0.318 1.00 24.75 ? 35  ALA A C   1 
ATOM   288  O  O   . ALA A 1 38  ? 16.681  8.181   -0.553 1.00 27.90 ? 35  ALA A O   1 
ATOM   289  C  CB  . ALA A 1 38  ? 14.590  10.209  0.658  1.00 24.20 ? 35  ALA A CB  1 
ATOM   290  N  N   A THR A 1 39  ? 17.851  9.958   0.178  0.50 25.30 ? 36  THR A N   1 
ATOM   291  N  N   B THR A 1 39  ? 17.852  9.958   0.177  0.50 25.37 ? 36  THR A N   1 
ATOM   292  C  CA  A THR A 1 39  ? 19.116  9.266   0.346  0.50 26.35 ? 36  THR A CA  1 
ATOM   293  C  CA  B THR A 1 39  ? 19.117  9.268   0.346  0.50 26.45 ? 36  THR A CA  1 
ATOM   294  C  C   A THR A 1 39  ? 19.444  9.132   1.831  0.50 23.15 ? 36  THR A C   1 
ATOM   295  C  C   B THR A 1 39  ? 19.445  9.133   1.831  0.50 23.25 ? 36  THR A C   1 
ATOM   296  O  O   A THR A 1 39  ? 19.313  10.095  2.587  0.50 24.83 ? 36  THR A O   1 
ATOM   297  O  O   B THR A 1 39  ? 19.315  10.095  2.587  0.50 25.07 ? 36  THR A O   1 
ATOM   298  C  CB  A THR A 1 39  ? 20.255  10.039  -0.331 0.50 30.22 ? 36  THR A CB  1 
ATOM   299  C  CB  B THR A 1 39  ? 20.256  10.042  -0.329 0.50 30.32 ? 36  THR A CB  1 
ATOM   300  O  OG1 A THR A 1 39  ? 19.781  10.454  -1.612 0.50 33.92 ? 36  THR A OG1 1 
ATOM   301  O  OG1 B THR A 1 39  ? 19.797  10.426  -1.625 0.50 34.09 ? 36  THR A OG1 1 
ATOM   302  C  CG2 A THR A 1 39  ? 21.519  9.217   -0.462 0.50 30.82 ? 36  THR A CG2 1 
ATOM   303  C  CG2 B THR A 1 39  ? 21.533  9.235   -0.427 0.50 30.83 ? 36  THR A CG2 1 
ATOM   304  N  N   . PHE A 1 40  ? 19.895  7.936   2.232  1.00 21.00 ? 37  PHE A N   1 
ATOM   305  C  CA  . PHE A 1 40  ? 20.335  7.693   3.599  1.00 20.57 ? 37  PHE A CA  1 
ATOM   306  C  C   . PHE A 1 40  ? 21.739  8.255   3.768  1.00 20.88 ? 37  PHE A C   1 
ATOM   307  O  O   . PHE A 1 40  ? 22.592  8.038   2.914  1.00 24.16 ? 37  PHE A O   1 
ATOM   308  C  CB  . PHE A 1 40  ? 20.322  6.197   3.930  1.00 19.57 ? 37  PHE A CB  1 
ATOM   309  C  CG  . PHE A 1 40  ? 18.934  5.675   4.142  1.00 17.87 ? 37  PHE A CG  1 
ATOM   310  C  CD1 . PHE A 1 40  ? 18.317  5.836   5.372  1.00 17.17 ? 37  PHE A CD1 1 
ATOM   311  C  CD2 . PHE A 1 40  ? 18.236  5.019   3.137  1.00 18.22 ? 37  PHE A CD2 1 
ATOM   312  C  CE1 . PHE A 1 40  ? 17.028  5.377   5.600  1.00 16.31 ? 37  PHE A CE1 1 
ATOM   313  C  CE2 . PHE A 1 40  ? 16.927  4.611   3.341  1.00 19.55 ? 37  PHE A CE2 1 
ATOM   314  C  CZ  . PHE A 1 40  ? 16.327  4.799   4.560  1.00 19.15 ? 37  PHE A CZ  1 
ATOM   315  N  N   . LYS A 1 41  ? 21.919  9.008   4.860  1.00 20.60 ? 38  LYS A N   1 
ATOM   316  C  CA  . LYS A 1 41  ? 23.188  9.607   5.239  1.00 20.75 ? 38  LYS A CA  1 
ATOM   317  C  C   . LYS A 1 41  ? 23.567  9.120   6.636  1.00 20.89 ? 38  LYS A C   1 
ATOM   318  O  O   . LYS A 1 41  ? 22.685  8.865   7.455  1.00 20.63 ? 38  LYS A O   1 
ATOM   319  C  CB  . LYS A 1 41  ? 23.062  11.140  5.203  1.00 24.91 ? 38  LYS A CB  1 
ATOM   320  C  CG  . LYS A 1 41  ? 22.468  11.699  3.921  1.00 28.67 ? 38  LYS A CG  1 
ATOM   321  N  N   . LYS A 1 42  ? 24.868  8.976   6.899  1.00 22.18 ? 39  LYS A N   1 
ATOM   322  C  CA  . LYS A 1 42  ? 25.348  8.723   8.238  1.00 24.00 ? 39  LYS A CA  1 
ATOM   323  C  C   . LYS A 1 42  ? 24.869  9.811   9.189  1.00 21.09 ? 39  LYS A C   1 
ATOM   324  O  O   . LYS A 1 42  ? 24.995  11.002  8.922  1.00 26.38 ? 39  LYS A O   1 
ATOM   325  C  CB  . LYS A 1 42  ? 26.875  8.718   8.252  1.00 26.77 ? 39  LYS A CB  1 
ATOM   326  C  CG  . LYS A 1 42  ? 27.469  8.048   9.482  1.00 29.38 ? 39  LYS A CG  1 
ATOM   327  N  N   . ASN A 1 43  ? 24.398  9.406   10.350 1.00 21.47 ? 40  ASN A N   1 
ATOM   328  C  CA  . ASN A 1 43  ? 23.968  10.321  11.393 1.00 21.87 ? 40  ASN A CA  1 
ATOM   329  C  C   . ASN A 1 43  ? 24.802  9.975   12.625 1.00 21.59 ? 40  ASN A C   1 
ATOM   330  O  O   . ASN A 1 43  ? 25.213  8.829   12.782 1.00 21.60 ? 40  ASN A O   1 
ATOM   331  C  CB  . ASN A 1 43  ? 22.460  10.166  11.626 1.00 22.97 ? 40  ASN A CB  1 
ATOM   332  C  CG  . ASN A 1 43  ? 21.891  10.882  12.831 1.00 26.40 ? 40  ASN A CG  1 
ATOM   333  O  OD1 . ASN A 1 43  ? 22.116  10.486  13.986 1.00 27.69 ? 40  ASN A OD1 1 
ATOM   334  N  ND2 . ASN A 1 43  ? 21.155  11.950  12.572 1.00 28.25 ? 40  ASN A ND2 1 
ATOM   335  N  N   . PRO A 1 44  ? 25.089  10.937  13.524 1.00 22.29 ? 41  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 44  ? 25.978  10.663  14.653 1.00 23.30 ? 41  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 44  ? 25.475  9.749   15.770 1.00 21.66 ? 41  PRO A C   1 
ATOM   338  O  O   . PRO A 1 44  ? 26.221  9.369   16.683 1.00 23.31 ? 41  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 44  ? 26.238  12.061  15.228 1.00 26.97 ? 41  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 44  ? 25.094  12.922  14.761 1.00 27.04 ? 41  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 44  ? 24.688  12.348  13.419 1.00 24.07 ? 41  PRO A CD  1 
ATOM   342  N  N   . PHE A 1 45  ? 24.208  9.363   15.703 1.00 18.97 ? 42  PHE A N   1 
ATOM   343  C  CA  . PHE A 1 45  ? 23.605  8.536   16.731 1.00 17.98 ? 42  PHE A CA  1 
ATOM   344  C  C   . PHE A 1 45  ? 23.393  7.107   16.210 1.00 17.51 ? 42  PHE A C   1 
ATOM   345  O  O   . PHE A 1 45  ? 22.336  6.511   16.426 1.00 19.24 ? 42  PHE A O   1 
ATOM   346  C  CB  . PHE A 1 45  ? 22.299  9.188   17.191 1.00 18.33 ? 42  PHE A CB  1 
ATOM   347  C  CG  . PHE A 1 45  ? 22.526  10.533  17.846 1.00 20.04 ? 42  PHE A CG  1 
ATOM   348  C  CD1 . PHE A 1 45  ? 23.172  10.624  19.068 1.00 20.58 ? 42  PHE A CD1 1 
ATOM   349  C  CD2 . PHE A 1 45  ? 22.134  11.705  17.222 1.00 21.46 ? 42  PHE A CD2 1 
ATOM   350  C  CE1 . PHE A 1 45  ? 23.439  11.861  19.638 1.00 21.53 ? 42  PHE A CE1 1 
ATOM   351  C  CE2 . PHE A 1 45  ? 22.371  12.937  17.800 1.00 23.15 ? 42  PHE A CE2 1 
ATOM   352  C  CZ  . PHE A 1 45  ? 22.993  13.012  19.020 1.00 22.59 ? 42  PHE A CZ  1 
ATOM   353  N  N   . GLU A 1 46  ? 24.422  6.545   15.572 1.00 17.76 ? 43  GLU A N   1 
ATOM   354  C  CA  . GLU A 1 46  ? 24.470  5.136   15.203 1.00 18.19 ? 43  GLU A CA  1 
ATOM   355  C  C   . GLU A 1 46  ? 23.318  4.781   14.282 1.00 16.54 ? 43  GLU A C   1 
ATOM   356  O  O   . GLU A 1 46  ? 22.642  3.776   14.491 1.00 17.03 ? 43  GLU A O   1 
ATOM   357  C  CB  . GLU A 1 46  ? 24.490  4.231   16.436 1.00 19.58 ? 43  GLU A CB  1 
ATOM   358  C  CG  . GLU A 1 46  ? 25.625  4.573   17.365 1.00 23.55 ? 43  GLU A CG  1 
ATOM   359  C  CD  . GLU A 1 46  ? 25.645  3.694   18.590 1.00 24.75 ? 43  GLU A CD  1 
ATOM   360  O  OE1 . GLU A 1 46  ? 26.111  2.558   18.462 1.00 29.54 ? 43  GLU A OE1 1 
ATOM   361  O  OE2 . GLU A 1 46  ? 25.169  4.140   19.647 1.00 28.32 ? 43  GLU A OE2 1 
ATOM   362  N  N   . ALA A 1 47  ? 23.065  5.626   13.284 1.00 16.45 ? 44  ALA A N   1 
ATOM   363  C  CA  . ALA A 1 47  ? 21.947  5.392   12.385 1.00 16.03 ? 44  ALA A CA  1 
ATOM   364  C  C   . ALA A 1 47  ? 22.265  5.928   10.997 1.00 17.09 ? 44  ALA A C   1 
ATOM   365  O  O   . ALA A 1 47  ? 23.125  6.798   10.847 1.00 19.76 ? 44  ALA A O   1 
ATOM   366  C  CB  . ALA A 1 47  ? 20.706  6.039   12.931 1.00 18.10 ? 44  ALA A CB  1 
ATOM   367  N  N   . GLU A 1 48  ? 21.578  5.358   10.005 1.00 15.94 ? 45  GLU A N   1 
ATOM   368  C  CA  . GLU A 1 48  ? 21.472  5.985   8.703  1.00 17.58 ? 45  GLU A CA  1 
ATOM   369  C  C   . GLU A 1 48  ? 20.112  6.648   8.609  1.00 15.99 ? 45  GLU A C   1 
ATOM   370  O  O   . GLU A 1 48  ? 19.127  6.054   8.999  1.00 16.26 ? 45  GLU A O   1 
ATOM   371  C  CB  . GLU A 1 48  ? 21.643  4.930   7.608  1.00 18.45 ? 45  GLU A CB  1 
ATOM   372  C  CG  . GLU A 1 48  ? 23.084  4.423   7.482  1.00 21.72 ? 45  GLU A CG  1 
ATOM   373  C  CD  . GLU A 1 48  ? 24.031  5.327   6.725  1.00 26.73 ? 45  GLU A CD  1 
ATOM   374  O  OE1 . GLU A 1 48  ? 23.592  5.921   5.724  1.00 32.73 ? 45  GLU A OE1 1 
ATOM   375  O  OE2 . GLU A 1 48  ? 25.180  5.432   7.140  1.00 32.66 ? 45  GLU A OE2 1 
ATOM   376  N  N   . VAL A 1 49  ? 20.059  7.889   8.113  1.00 16.44 ? 46  VAL A N   1 
ATOM   377  C  CA  . VAL A 1 49  ? 18.846  8.689   8.126  1.00 15.97 ? 46  VAL A CA  1 
ATOM   378  C  C   . VAL A 1 49  ? 18.672  9.335   6.763  1.00 16.62 ? 46  VAL A C   1 
ATOM   379  O  O   . VAL A 1 49  ? 19.621  9.881   6.223  1.00 19.31 ? 46  VAL A O   1 
ATOM   380  C  CB  . VAL A 1 49  ? 18.864  9.752   9.227  1.00 17.48 ? 46  VAL A CB  1 
ATOM   381  C  CG1 . VAL A 1 49  ? 17.649  10.641  9.223  1.00 18.12 ? 46  VAL A CG1 1 
ATOM   382  C  CG2 . VAL A 1 49  ? 19.068  9.105   10.581 1.00 17.29 ? 46  VAL A CG2 1 
ATOM   383  N  N   . ALA A 1 50  ? 17.472  9.177   6.202  1.00 16.28 ? 47  ALA A N   1 
ATOM   384  C  CA  . ALA A 1 50  ? 17.085  9.833   4.969  1.00 18.34 ? 47  ALA A CA  1 
ATOM   385  C  C   . ALA A 1 50  ? 15.955  10.777  5.306  1.00 19.04 ? 47  ALA A C   1 
ATOM   386  O  O   . ALA A 1 50  ? 15.182  10.555  6.215  1.00 19.77 ? 47  ALA A O   1 
ATOM   387  C  CB  . ALA A 1 50  ? 16.714  8.815   3.916  1.00 18.24 ? 47  ALA A CB  1 
ATOM   388  N  N   . GLU A 1 51  ? 15.871  11.866  4.558  1.00 22.03 ? 48  GLU A N   1 
ATOM   389  C  CA  . GLU A 1 51  ? 14.876  12.876  4.853  1.00 23.08 ? 48  GLU A CA  1 
ATOM   390  C  C   . GLU A 1 51  ? 14.195  13.317  3.556  1.00 23.01 ? 48  GLU A C   1 
ATOM   391  O  O   . GLU A 1 51  ? 14.832  13.446  2.499  1.00 24.41 ? 48  GLU A O   1 
ATOM   392  C  CB  . GLU A 1 51  ? 15.492  14.077  5.585  1.00 26.72 ? 48  GLU A CB  1 
ATOM   393  C  CG  . GLU A 1 51  ? 16.300  13.759  6.831  1.00 32.31 ? 48  GLU A CG  1 
ATOM   394  C  CD  . GLU A 1 51  ? 16.947  14.967  7.494  1.00 36.57 ? 48  GLU A CD  1 
ATOM   395  O  OE1 . GLU A 1 51  ? 16.496  16.107  7.230  1.00 40.06 ? 48  GLU A OE1 1 
ATOM   396  O  OE2 . GLU A 1 51  ? 17.946  14.765  8.222  1.00 41.99 ? 48  GLU A OE2 1 
ATOM   397  N  N   . PHE A 1 52  ? 12.895  13.589  3.640  1.00 22.29 ? 49  PHE A N   1 
ATOM   398  C  CA  . PHE A 1 52  ? 12.189  14.241  2.554  1.00 23.82 ? 49  PHE A CA  1 
ATOM   399  C  C   . PHE A 1 52  ? 11.027  15.026  3.139  1.00 23.84 ? 49  PHE A C   1 
ATOM   400  O  O   . PHE A 1 52  ? 10.713  14.934  4.320  1.00 24.41 ? 49  PHE A O   1 
ATOM   401  C  CB  . PHE A 1 52  ? 11.709  13.219  1.524  1.00 24.30 ? 49  PHE A CB  1 
ATOM   402  C  CG  . PHE A 1 52  ? 10.691  12.231  2.028  1.00 25.42 ? 49  PHE A CG  1 
ATOM   403  C  CD1 . PHE A 1 52  ? 11.070  11.058  2.655  1.00 24.57 ? 49  PHE A CD1 1 
ATOM   404  C  CD2 . PHE A 1 52  ? 9.342   12.462  1.836  1.00 25.02 ? 49  PHE A CD2 1 
ATOM   405  C  CE1 . PHE A 1 52  ? 10.120  10.168  3.112  1.00 25.49 ? 49  PHE A CE1 1 
ATOM   406  C  CE2 . PHE A 1 52  ? 8.396   11.567  2.294  1.00 26.40 ? 49  PHE A CE2 1 
ATOM   407  C  CZ  . PHE A 1 52  ? 8.790   10.416  2.927  1.00 24.01 ? 49  PHE A CZ  1 
ATOM   408  N  N   . PHE A 1 53  ? 10.452  15.892  2.327  1.00 27.19 ? 50  PHE A N   1 
ATOM   409  C  CA  . PHE A 1 53  ? 9.350   16.713  2.783  1.00 27.64 ? 50  PHE A CA  1 
ATOM   410  C  C   . PHE A 1 53  ? 8.092   16.242  2.086  1.00 28.13 ? 50  PHE A C   1 
ATOM   411  O  O   . PHE A 1 53  ? 8.123   15.846  0.920  1.00 30.14 ? 50  PHE A O   1 
ATOM   412  C  CB  . PHE A 1 53  ? 9.578   18.210  2.548  1.00 31.31 ? 50  PHE A CB  1 
ATOM   413  C  CG  . PHE A 1 53  ? 10.583  18.800  3.497  1.00 32.15 ? 50  PHE A CG  1 
ATOM   414  C  CD1 . PHE A 1 53  ? 11.942  18.612  3.300  1.00 35.48 ? 50  PHE A CD1 1 
ATOM   415  C  CD2 . PHE A 1 53  ? 10.166  19.456  4.644  1.00 33.20 ? 50  PHE A CD2 1 
ATOM   416  C  CE1 . PHE A 1 53  ? 12.864  19.120  4.201  1.00 38.75 ? 50  PHE A CE1 1 
ATOM   417  C  CE2 . PHE A 1 53  ? 11.088  19.959  5.552  1.00 36.41 ? 50  PHE A CE2 1 
ATOM   418  C  CZ  . PHE A 1 53  ? 12.436  19.792  5.326  1.00 37.80 ? 50  PHE A CZ  1 
ATOM   419  N  N   . HIS A 1 54  ? 7.012   16.257  2.859  1.00 25.65 ? 51  HIS A N   1 
ATOM   420  C  CA  . HIS A 1 54  ? 5.680   16.068  2.334  1.00 31.81 ? 51  HIS A CA  1 
ATOM   421  C  C   . HIS A 1 54  ? 4.845   17.297  2.686  1.00 33.36 ? 51  HIS A C   1 
ATOM   422  O  O   . HIS A 1 54  ? 4.540   17.530  3.859  1.00 34.86 ? 51  HIS A O   1 
ATOM   423  C  CB  . HIS A 1 54  ? 5.073   14.789  2.900  1.00 34.87 ? 51  HIS A CB  1 
ATOM   424  C  CG  . HIS A 1 54  ? 3.672   14.625  2.459  1.00 39.08 ? 51  HIS A CG  1 
ATOM   425  N  ND1 . HIS A 1 54  ? 2.598   14.890  3.278  1.00 43.26 ? 51  HIS A ND1 1 
ATOM   426  C  CD2 . HIS A 1 54  ? 3.178   14.315  1.265  1.00 40.97 ? 51  HIS A CD2 1 
ATOM   427  C  CE1 . HIS A 1 54  ? 1.483   14.689  2.597  1.00 42.80 ? 51  HIS A CE1 1 
ATOM   428  N  NE2 . HIS A 1 54  ? 1.814   14.338  1.370  1.00 44.54 ? 51  HIS A NE2 1 
ATOM   429  N  N   . ASN A 1 55  ? 4.551   18.107  1.658  1.00 35.44 ? 52  ASN A N   1 
ATOM   430  C  CA  . ASN A 1 55  ? 3.810   19.350  1.787  1.00 37.59 ? 52  ASN A CA  1 
ATOM   431  C  C   . ASN A 1 55  ? 4.225   20.073  3.065  1.00 38.75 ? 52  ASN A C   1 
ATOM   432  O  O   . ASN A 1 55  ? 3.382   20.324  3.925  1.00 43.55 ? 52  ASN A O   1 
ATOM   433  N  N   . GLY A 1 56  ? 5.535   20.347  3.194  1.00 34.82 ? 53  GLY A N   1 
ATOM   434  C  CA  . GLY A 1 56  ? 6.059   21.192  4.255  1.00 36.07 ? 53  GLY A CA  1 
ATOM   435  C  C   . GLY A 1 56  ? 6.533   20.440  5.503  1.00 35.06 ? 53  GLY A C   1 
ATOM   436  O  O   . GLY A 1 56  ? 7.289   21.004  6.290  1.00 37.05 ? 53  GLY A O   1 
ATOM   437  N  N   . GLU A 1 57  ? 6.104   19.182  5.685  1.00 32.77 ? 54  GLU A N   1 
ATOM   438  C  CA  . GLU A 1 57  ? 6.447   18.383  6.855  1.00 31.12 ? 54  GLU A CA  1 
ATOM   439  C  C   . GLU A 1 57  ? 7.686   17.539  6.590  1.00 27.33 ? 54  GLU A C   1 
ATOM   440  O  O   . GLU A 1 57  ? 7.711   16.829  5.597  1.00 28.26 ? 54  GLU A O   1 
ATOM   441  C  CB  . GLU A 1 57  ? 5.305   17.427  7.207  1.00 32.67 ? 54  GLU A CB  1 
ATOM   442  C  CG  . GLU A 1 57  ? 5.542   16.722  8.530  1.00 35.71 ? 54  GLU A CG  1 
ATOM   443  C  CD  . GLU A 1 57  ? 4.412   15.827  8.987  1.00 37.29 ? 54  GLU A CD  1 
ATOM   444  O  OE1 . GLU A 1 57  ? 4.473   15.374  10.155 1.00 41.81 ? 54  GLU A OE1 1 
ATOM   445  O  OE2 . GLU A 1 57  ? 3.491   15.587  8.178  1.00 44.72 ? 54  GLU A OE2 1 
ATOM   446  N  N   . LYS A 1 58  ? 8.687   17.596  7.490  1.00 26.88 ? 55  LYS A N   1 
ATOM   447  C  CA  . LYS A 1 58  ? 9.881   16.770  7.372  1.00 25.52 ? 55  LYS A CA  1 
ATOM   448  C  C   . LYS A 1 58  ? 9.557   15.342  7.795  1.00 22.47 ? 55  LYS A C   1 
ATOM   449  O  O   . LYS A 1 58  ? 9.034   15.110  8.892  1.00 23.03 ? 55  LYS A O   1 
ATOM   450  C  CB  . LYS A 1 58  ? 11.037  17.296  8.230  1.00 26.22 ? 55  LYS A CB  1 
ATOM   451  C  CG  . LYS A 1 58  ? 12.348  16.569  7.971  1.00 28.69 ? 55  LYS A CG  1 
ATOM   452  C  CD  . LYS A 1 58  ? 13.594  17.204  8.529  1.00 33.37 ? 55  LYS A CD  1 
ATOM   453  N  N   . ILE A 1 59  ? 9.870   14.404  6.892  1.00 20.92 ? 56  ILE A N   1 
ATOM   454  C  CA  . ILE A 1 59  ? 9.750   12.988  7.169  1.00 20.22 ? 56  ILE A CA  1 
ATOM   455  C  C   . ILE A 1 59  ? 11.162  12.435  7.248  1.00 16.93 ? 56  ILE A C   1 
ATOM   456  O  O   . ILE A 1 59  ? 11.966  12.613  6.347  1.00 20.12 ? 56  ILE A O   1 
ATOM   457  C  CB  . ILE A 1 59  ? 8.910   12.242  6.123  1.00 20.56 ? 56  ILE A CB  1 
ATOM   458  C  CG1 . ILE A 1 59  ? 7.578   12.949  5.823  1.00 21.85 ? 56  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A 1 59  ? 8.754   10.801  6.572  1.00 20.78 ? 56  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A 1 59  ? 6.675   13.132  7.007  1.00 23.71 ? 56  ILE A CD1 1 
ATOM   461  N  N   . LEU A 1 60  ? 11.427  11.708  8.336  1.00 15.25 ? 57  LEU A N   1 
ATOM   462  C  CA  . LEU A 1 60  ? 12.697  11.064  8.552  1.00 15.67 ? 57  LEU A CA  1 
ATOM   463  C  C   . LEU A 1 60  ? 12.536  9.559   8.423  1.00 14.68 ? 57  LEU A C   1 
ATOM   464  O  O   . LEU A 1 60  ? 11.585  9.020   8.982  1.00 16.86 ? 57  LEU A O   1 
ATOM   465  C  CB  . LEU A 1 60  ? 13.154  11.407  9.955  1.00 18.38 ? 57  LEU A CB  1 
ATOM   466  C  CG  . LEU A 1 60  ? 13.207  12.895  10.256 1.00 23.21 ? 57  LEU A CG  1 
ATOM   467  C  CD1 . LEU A 1 60  ? 13.183  13.096  11.745 1.00 28.72 ? 57  LEU A CD1 1 
ATOM   468  C  CD2 . LEU A 1 60  ? 14.414  13.509  9.584  1.00 26.97 ? 57  LEU A CD2 1 
ATOM   469  N  N   . LEU A 1 61  ? 13.413  8.932   7.647  1.00 13.75 ? 58  LEU A N   1 
ATOM   470  C  CA  . LEU A 1 61  ? 13.499  7.490   7.572  1.00 13.65 ? 58  LEU A CA  1 
ATOM   471  C  C   . LEU A 1 61  ? 14.789  7.087   8.260  1.00 13.99 ? 58  LEU A C   1 
ATOM   472  O  O   . LEU A 1 61  ? 15.855  7.643   7.954  1.00 17.03 ? 58  LEU A O   1 
ATOM   473  C  CB  . LEU A 1 61  ? 13.548  7.066   6.101  1.00 14.66 ? 58  LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 61  ? 12.434  7.598   5.207  1.00 15.26 ? 58  LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 61  ? 12.597  7.123   3.776  1.00 14.81 ? 58  LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 61  ? 11.059  7.190   5.704  1.00 16.30 ? 58  LEU A CD2 1 
ATOM   477  N  N   . VAL A 1 62  ? 14.698  6.086   9.143  1.00 12.52 ? 59  VAL A N   1 
ATOM   478  C  CA  . VAL A 1 62  ? 15.829  5.760   9.996  1.00 12.63 ? 59  VAL A CA  1 
ATOM   479  C  C   . VAL A 1 62  ? 16.119  4.269   9.938  1.00 11.90 ? 59  VAL A C   1 
ATOM   480  O  O   . VAL A 1 62  ? 15.197  3.469   10.167 1.00 13.60 ? 59  VAL A O   1 
ATOM   481  C  CB  . VAL A 1 62  ? 15.547  6.177   11.449 1.00 13.71 ? 59  VAL A CB  1 
ATOM   482  C  CG1 . VAL A 1 62  ? 16.625  5.738   12.419 1.00 14.47 ? 59  VAL A CG1 1 
ATOM   483  C  CG2 . VAL A 1 62  ? 15.315  7.679   11.580 1.00 14.18 ? 59  VAL A CG2 1 
ATOM   484  N  N   . LYS A 1 63  ? 17.375  3.911   9.721  1.00 13.07 ? 60  LYS A N   1 
ATOM   485  C  CA  . LYS A 1 63  ? 17.846  2.549   9.868  1.00 12.70 ? 60  LYS A CA  1 
ATOM   486  C  C   . LYS A 1 63  ? 18.897  2.571   10.967 1.00 13.12 ? 60  LYS A C   1 
ATOM   487  O  O   . LYS A 1 63  ? 20.047  2.963   10.726 1.00 13.75 ? 60  LYS A O   1 
ATOM   488  C  CB  . LYS A 1 63  ? 18.419  2.038   8.553  1.00 12.68 ? 60  LYS A CB  1 
ATOM   489  C  CG  . LYS A 1 63  ? 17.376  1.891   7.458  1.00 13.50 ? 60  LYS A CG  1 
ATOM   490  C  CD  . LYS A 1 63  ? 17.855  1.229   6.208  1.00 14.73 ? 60  LYS A CD  1 
ATOM   491  C  CE  . LYS A 1 63  ? 18.928  2.050   5.536  1.00 15.68 ? 60  LYS A CE  1 
ATOM   492  N  NZ  . LYS A 1 63  ? 19.474  1.418   4.309  1.00 18.04 ? 60  LYS A NZ  1 
ATOM   493  N  N   . PRO A 1 64  ? 18.588  2.132   12.207 1.00 12.15 ? 61  PRO A N   1 
ATOM   494  C  CA  . PRO A 1 64  ? 19.634  2.029   13.225 1.00 12.63 ? 61  PRO A CA  1 
ATOM   495  C  C   . PRO A 1 64  ? 20.747  1.106   12.749 1.00 13.02 ? 61  PRO A C   1 
ATOM   496  O  O   . PRO A 1 64  ? 20.462  0.083   12.130 1.00 14.02 ? 61  PRO A O   1 
ATOM   497  C  CB  . PRO A 1 64  ? 18.875  1.443   14.416 1.00 13.02 ? 61  PRO A CB  1 
ATOM   498  C  CG  . PRO A 1 64  ? 17.445  1.816   14.190 1.00 13.23 ? 61  PRO A CG  1 
ATOM   499  C  CD  . PRO A 1 64  ? 17.267  1.688   12.691 1.00 12.63 ? 61  PRO A CD  1 
ATOM   500  N  N   . GLN A 1 65  ? 21.982  1.437   13.112 1.00 13.35 ? 62  GLN A N   1 
ATOM   501  C  CA  . GLN A 1 65  ? 23.144  0.622   12.728 1.00 14.03 ? 62  GLN A CA  1 
ATOM   502  C  C   . GLN A 1 65  ? 23.775  -0.051  13.944 1.00 14.51 ? 62  GLN A C   1 
ATOM   503  O  O   . GLN A 1 65  ? 24.950  -0.415  13.940 1.00 16.85 ? 62  GLN A O   1 
ATOM   504  C  CB  . GLN A 1 65  ? 24.141  1.530   12.016 1.00 15.19 ? 62  GLN A CB  1 
ATOM   505  C  CG  . GLN A 1 65  ? 23.555  2.172   10.761 1.00 16.07 ? 62  GLN A CG  1 
ATOM   506  C  CD  . GLN A 1 65  ? 23.263  1.212   9.639  1.00 16.28 ? 62  GLN A CD  1 
ATOM   507  O  OE1 . GLN A 1 65  ? 24.102  0.424   9.214  1.00 18.95 ? 62  GLN A OE1 1 
ATOM   508  N  NE2 . GLN A 1 65  ? 22.027  1.213   9.173  1.00 16.56 ? 62  GLN A NE2 1 
ATOM   509  N  N   . THR A 1 66  ? 22.989  -0.173  15.011 1.00 14.09 ? 63  THR A N   1 
ATOM   510  C  CA  . THR A 1 66  ? 23.391  -0.653  16.324 1.00 14.38 ? 63  THR A CA  1 
ATOM   511  C  C   . THR A 1 66  ? 23.374  -2.178  16.491 1.00 14.49 ? 63  THR A C   1 
ATOM   512  O  O   . THR A 1 66  ? 23.876  -2.654  17.506 1.00 15.57 ? 63  THR A O   1 
ATOM   513  C  CB  . THR A 1 66  ? 22.360  -0.132  17.325 1.00 14.56 ? 63  THR A CB  1 
ATOM   514  O  OG1 . THR A 1 66  ? 21.075  -0.498  16.825 1.00 13.71 ? 63  THR A OG1 1 
ATOM   515  C  CG2 . THR A 1 66  ? 22.383  1.374   17.487 1.00 15.82 ? 63  THR A CG2 1 
ATOM   516  N  N   . PHE A 1 67  ? 22.796  -2.883  15.521 1.00 13.52 ? 64  PHE A N   1 
ATOM   517  C  CA  . PHE A 1 67  ? 22.262  -4.238  15.616 1.00 13.69 ? 64  PHE A CA  1 
ATOM   518  C  C   . PHE A 1 67  ? 20.891  -4.168  16.280 1.00 12.91 ? 64  PHE A C   1 
ATOM   519  O  O   . PHE A 1 67  ? 20.599  -3.262  17.051 1.00 13.28 ? 64  PHE A O   1 
ATOM   520  C  CB  . PHE A 1 67  ? 23.189  -5.256  16.289 1.00 15.24 ? 64  PHE A CB  1 
ATOM   521  C  CG  . PHE A 1 67  ? 24.367  -5.626  15.432 1.00 16.64 ? 64  PHE A CG  1 
ATOM   522  C  CD1 . PHE A 1 67  ? 25.490  -4.819  15.355 1.00 18.96 ? 64  PHE A CD1 1 
ATOM   523  C  CD2 . PHE A 1 67  ? 24.353  -6.776  14.649 1.00 16.82 ? 64  PHE A CD2 1 
ATOM   524  C  CE1 . PHE A 1 67  ? 26.548  -5.162  14.535 1.00 21.74 ? 64  PHE A CE1 1 
ATOM   525  C  CE2 . PHE A 1 67  ? 25.419  -7.123  13.843 1.00 18.87 ? 64  PHE A CE2 1 
ATOM   526  C  CZ  . PHE A 1 67  ? 26.495  -6.303  13.779 1.00 20.68 ? 64  PHE A CZ  1 
ATOM   527  N  N   . MET A 1 68  ? 20.054  -5.144  15.930 1.00 13.29 ? 65  MET A N   1 
ATOM   528  C  CA  . MET A 1 68  ? 18.649  -5.142  16.272 1.00 13.36 ? 65  MET A CA  1 
ATOM   529  C  C   . MET A 1 68  ? 18.465  -4.937  17.770 1.00 13.80 ? 65  MET A C   1 
ATOM   530  O  O   . MET A 1 68  ? 17.651  -4.095  18.164 1.00 13.48 ? 65  MET A O   1 
ATOM   531  C  CB  . MET A 1 68  ? 18.054  -6.492  15.889 1.00 14.50 ? 65  MET A CB  1 
ATOM   532  C  CG  . MET A 1 68  ? 16.569  -6.628  16.173 1.00 13.66 ? 65  MET A CG  1 
ATOM   533  S  SD  . MET A 1 68  ? 15.599  -5.452  15.242 1.00 14.45 ? 65  MET A SD  1 
ATOM   534  C  CE  . MET A 1 68  ? 15.327  -6.431  13.771 1.00 13.67 ? 65  MET A CE  1 
ATOM   535  N  N   . ASN A 1 69  ? 19.221  -5.686  18.578 1.00 15.14 ? 66  ASN A N   1 
ATOM   536  C  CA  . ASN A 1 69  ? 19.008  -5.715  20.020 1.00 16.99 ? 66  ASN A CA  1 
ATOM   537  C  C   . ASN A 1 69  ? 19.439  -4.445  20.735 1.00 15.79 ? 66  ASN A C   1 
ATOM   538  O  O   . ASN A 1 69  ? 19.196  -4.336  21.943 1.00 17.19 ? 66  ASN A O   1 
ATOM   539  C  CB  . ASN A 1 69  ? 19.752  -6.897  20.665 1.00 18.78 ? 66  ASN A CB  1 
ATOM   540  C  CG  . ASN A 1 69  ? 21.284  -6.776  20.648 1.00 24.34 ? 66  ASN A CG  1 
ATOM   541  O  OD1 . ASN A 1 69  ? 21.899  -5.995  19.893 1.00 33.63 ? 66  ASN A OD1 1 
ATOM   542  N  ND2 . ASN A 1 69  ? 21.932  -7.562  21.488 1.00 28.97 ? 66  ASN A ND2 1 
ATOM   543  N  N   . GLU A 1 70  ? 20.045  -3.492  20.000 1.00 14.12 ? 67  GLU A N   1 
ATOM   544  C  CA  . GLU A 1 70  ? 20.487  -2.232  20.544 1.00 14.34 ? 67  GLU A CA  1 
ATOM   545  C  C   . GLU A 1 70  ? 19.804  -1.057  19.847 1.00 13.97 ? 67  GLU A C   1 
ATOM   546  O  O   . GLU A 1 70  ? 20.257  0.062   20.030 1.00 14.47 ? 67  GLU A O   1 
ATOM   547  C  CB  . GLU A 1 70  ? 22.019  -2.163  20.502 1.00 17.21 ? 67  GLU A CB  1 
ATOM   548  C  CG  . GLU A 1 70  ? 22.687  -3.153  21.437 1.00 21.41 ? 67  GLU A CG  1 
ATOM   549  C  CD  . GLU A 1 70  ? 22.386  -2.924  22.905 1.00 29.40 ? 67  GLU A CD  1 
ATOM   550  O  OE1 . GLU A 1 70  ? 21.943  -1.799  23.275 1.00 31.48 ? 67  GLU A OE1 1 
ATOM   551  N  N   . SER A 1 71  ? 18.694  -1.320  19.122 1.00 12.95 ? 68  SER A N   1 
ATOM   552  C  CA  . SER A 1 71  ? 18.077  -0.288  18.296 1.00 12.87 ? 68  SER A CA  1 
ATOM   553  C  C   . SER A 1 71  ? 17.707  0.979   19.062 1.00 12.62 ? 68  SER A C   1 
ATOM   554  O  O   . SER A 1 71  ? 17.723  2.070   18.508 1.00 13.49 ? 68  SER A O   1 
ATOM   555  C  CB  . SER A 1 71  ? 16.809  -0.839  17.690 1.00 12.75 ? 68  SER A CB  1 
ATOM   556  O  OG  . SER A 1 71  ? 17.070  -1.888  16.748 1.00 13.61 ? 68  SER A OG  1 
ATOM   557  N  N   . GLY A 1 72  ? 17.346  0.831   20.332 1.00 13.06 ? 69  GLY A N   1 
ATOM   558  C  CA  . GLY A 1 72  ? 16.970  1.997   21.112 1.00 14.12 ? 69  GLY A CA  1 
ATOM   559  C  C   . GLY A 1 72  ? 18.098  3.001   21.339 1.00 14.55 ? 69  GLY A C   1 
ATOM   560  O  O   . GLY A 1 72  ? 17.805  4.151   21.617 1.00 15.87 ? 69  GLY A O   1 
ATOM   561  N  N   . ARG A 1 73  ? 19.355  2.539   21.232 1.00 14.72 ? 70  ARG A N   1 
ATOM   562  C  CA  . ARG A 1 73  ? 20.502  3.435   21.335 1.00 16.42 ? 70  ARG A CA  1 
ATOM   563  C  C   . ARG A 1 73  ? 20.561  4.432   20.177 1.00 15.60 ? 70  ARG A C   1 
ATOM   564  O  O   . ARG A 1 73  ? 21.246  5.457   20.310 1.00 18.74 ? 70  ARG A O   1 
ATOM   565  C  CB  . ARG A 1 73  ? 21.802  2.651   21.381 1.00 18.74 ? 70  ARG A CB  1 
ATOM   566  C  CG  . ARG A 1 73  ? 21.894  1.678   22.541 1.00 21.52 ? 70  ARG A CG  1 
ATOM   567  C  CD  . ARG A 1 73  ? 23.257  1.032   22.538 1.00 25.44 ? 70  ARG A CD  1 
ATOM   568  N  NE  . ARG A 1 73  ? 23.372  -0.073  23.485 1.00 31.53 ? 70  ARG A NE  1 
ATOM   569  C  CZ  . ARG A 1 73  ? 24.501  -0.749  23.690 1.00 35.63 ? 70  ARG A CZ  1 
ATOM   570  N  NH1 . ARG A 1 73  ? 25.570  -0.496  22.950 1.00 41.59 ? 70  ARG A NH1 1 
ATOM   571  N  NH2 . ARG A 1 73  ? 24.544  -1.712  24.599 1.00 42.88 ? 70  ARG A NH2 1 
ATOM   572  N  N   . ALA A 1 74  ? 19.924  4.132   19.050 1.00 14.44 ? 71  ALA A N   1 
ATOM   573  C  CA  . ALA A 1 74  ? 19.749  5.109   17.993 1.00 14.99 ? 71  ALA A CA  1 
ATOM   574  C  C   . ALA A 1 74  ? 18.435  5.881   18.155 1.00 14.99 ? 71  ALA A C   1 
ATOM   575  O  O   . ALA A 1 74  ? 18.378  7.104   18.036 1.00 17.35 ? 71  ALA A O   1 
ATOM   576  C  CB  . ALA A 1 74  ? 19.812  4.427   16.654 1.00 15.83 ? 71  ALA A CB  1 
ATOM   577  N  N   . VAL A 1 75  ? 17.346  5.183   18.400 1.00 14.91 ? 72  VAL A N   1 
ATOM   578  C  CA  . VAL A 1 75  ? 16.039  5.814   18.358 1.00 14.60 ? 72  VAL A CA  1 
ATOM   579  C  C   . VAL A 1 75  ? 15.885  6.866   19.464 1.00 16.03 ? 72  VAL A C   1 
ATOM   580  O  O   . VAL A 1 75  ? 15.417  7.961   19.198 1.00 16.98 ? 72  VAL A O   1 
ATOM   581  C  CB  . VAL A 1 75  ? 14.924  4.770   18.428 1.00 15.04 ? 72  VAL A CB  1 
ATOM   582  C  CG1 . VAL A 1 75  ? 13.580  5.446   18.594 1.00 17.06 ? 72  VAL A CG1 1 
ATOM   583  C  CG2 . VAL A 1 75  ? 14.943  3.892   17.205 1.00 16.21 ? 72  VAL A CG2 1 
ATOM   584  N  N   . GLY A 1 76  ? 16.280  6.515   20.691 1.00 16.67 ? 73  GLY A N   1 
ATOM   585  C  CA  . GLY A 1 76  ? 16.150  7.426   21.821 1.00 17.28 ? 73  GLY A CA  1 
ATOM   586  C  C   . GLY A 1 76  ? 16.837  8.764   21.564 1.00 18.50 ? 73  GLY A C   1 
ATOM   587  O  O   . GLY A 1 76  ? 16.223  9.821   21.639 1.00 20.42 ? 73  GLY A O   1 
ATOM   588  N  N   . PRO A 1 77  ? 18.145  8.745   21.255 1.00 17.69 ? 74  PRO A N   1 
ATOM   589  C  CA  . PRO A 1 77  ? 18.874  9.974   20.963 1.00 18.01 ? 74  PRO A CA  1 
ATOM   590  C  C   . PRO A 1 77  ? 18.363  10.749  19.748 1.00 18.37 ? 74  PRO A C   1 
ATOM   591  O  O   . PRO A 1 77  ? 18.363  11.988  19.772 1.00 18.25 ? 74  PRO A O   1 
ATOM   592  C  CB  . PRO A 1 77  ? 20.312  9.471   20.791 1.00 19.96 ? 74  PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 77  ? 20.343  8.248   21.650 1.00 21.01 ? 74  PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 77  ? 19.036  7.571   21.385 1.00 20.20 ? 74  PRO A CD  1 
ATOM   595  N  N   . LEU A 1 78  ? 17.867  10.045  18.719 1.00 18.45 ? 75  LEU A N   1 
ATOM   596  C  CA  . LEU A 1 78  ? 17.384  10.741  17.536 1.00 19.07 ? 75  LEU A CA  1 
ATOM   597  C  C   . LEU A 1 78  ? 16.140  11.540  17.903 1.00 19.24 ? 75  LEU A C   1 
ATOM   598  O  O   . LEU A 1 78  ? 15.868  12.603  17.353 1.00 20.38 ? 75  LEU A O   1 
ATOM   599  C  CB  . LEU A 1 78  ? 17.077  9.742   16.410 1.00 20.22 ? 75  LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 78  ? 18.321  9.221   15.709 1.00 23.17 ? 75  LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 78  ? 17.961  8.050   14.835 1.00 23.97 ? 75  LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 78  ? 18.987  10.319  14.899 1.00 25.79 ? 75  LEU A CD2 1 
ATOM   603  N  N   . MET A 1 79  ? 15.321  10.966  18.764 1.00 20.30 ? 76  MET A N   1 
ATOM   604  C  CA  . MET A 1 79  ? 14.103  11.677  19.121 1.00 21.32 ? 76  MET A CA  1 
ATOM   605  C  C   . MET A 1 79  ? 14.463  12.966  19.869 1.00 18.84 ? 76  MET A C   1 
ATOM   606  O  O   . MET A 1 79  ? 13.829  13.984  19.657 1.00 20.46 ? 76  MET A O   1 
ATOM   607  C  CB  . MET A 1 79  ? 13.174  10.799  19.950 1.00 22.07 ? 76  MET A CB  1 
ATOM   608  C  CG  . MET A 1 79  ? 12.513  9.681   19.125 1.00 22.82 ? 76  MET A CG  1 
ATOM   609  S  SD  . MET A 1 79  ? 11.812  8.464   20.128 1.00 28.24 ? 76  MET A SD  1 
ATOM   610  C  CE  . MET A 1 79  ? 10.279  9.321   20.425 1.00 25.13 ? 76  MET A CE  1 
ATOM   611  N  N   . THR A 1 80  ? 15.504  12.902  20.689 1.00 21.36 ? 77  THR A N   1 
ATOM   612  C  CA  . THR A 1 80  ? 16.000  14.066  21.408 1.00 22.15 ? 77  THR A CA  1 
ATOM   613  C  C   . THR A 1 80  ? 16.553  15.121  20.444 1.00 19.73 ? 77  THR A C   1 
ATOM   614  O  O   . THR A 1 80  ? 16.293  16.329  20.522 1.00 22.36 ? 77  THR A O   1 
ATOM   615  C  CB  . THR A 1 80  ? 17.118  13.652  22.376 1.00 24.69 ? 77  THR A CB  1 
ATOM   616  O  OG1 . THR A 1 80  ? 16.529  12.785  23.335 1.00 28.12 ? 77  THR A OG1 1 
ATOM   617  C  CG2 . THR A 1 80  ? 17.756  14.852  23.031 1.00 25.97 ? 77  THR A CG2 1 
ATOM   618  N  N   . TYR A 1 81  ? 17.340  14.635  19.509 1.00 17.95 ? 78  TYR A N   1 
ATOM   619  C  CA  . TYR A 1 81  ? 17.948  15.493  18.517 1.00 19.44 ? 78  TYR A CA  1 
ATOM   620  C  C   . TYR A 1 81  ? 16.892  16.282  17.752 1.00 20.98 ? 78  TYR A C   1 
ATOM   621  O  O   . TYR A 1 81  ? 17.063  17.494  17.591 1.00 24.23 ? 78  TYR A O   1 
ATOM   622  C  CB  . TYR A 1 81  ? 18.849  14.718  17.544 1.00 20.10 ? 78  TYR A CB  1 
ATOM   623  C  CG  . TYR A 1 81  ? 19.506  15.658  16.531 1.00 24.09 ? 78  TYR A CG  1 
ATOM   624  C  CD1 . TYR A 1 81  ? 18.841  16.048  15.364 1.00 26.24 ? 78  TYR A CD1 1 
ATOM   625  C  CD2 . TYR A 1 81  ? 20.780  16.182  16.750 1.00 26.99 ? 78  TYR A CD2 1 
ATOM   626  C  CE1 . TYR A 1 81  ? 19.437  16.907  14.443 1.00 28.94 ? 78  TYR A CE1 1 
ATOM   627  C  CE2 . TYR A 1 81  ? 21.372  17.052  15.847 1.00 29.58 ? 78  TYR A CE2 1 
ATOM   628  C  CZ  . TYR A 1 81  ? 20.689  17.440  14.705 1.00 31.39 ? 78  TYR A CZ  1 
ATOM   629  O  OH  . TYR A 1 81  ? 21.278  18.301  13.798 1.00 37.40 ? 78  TYR A OH  1 
ATOM   630  N  N   . PHE A 1 82  ? 15.894  15.568  17.214 1.00 21.49 ? 79  PHE A N   1 
ATOM   631  C  CA  . PHE A 1 82  ? 14.900  16.159  16.344 1.00 23.81 ? 79  PHE A CA  1 
ATOM   632  C  C   . PHE A 1 82  ? 13.740  16.776  17.132 1.00 25.42 ? 79  PHE A C   1 
ATOM   633  O  O   . PHE A 1 82  ? 12.907  17.481  16.567 1.00 29.26 ? 79  PHE A O   1 
ATOM   634  C  CB  . PHE A 1 82  ? 14.427  15.151  15.291 1.00 28.60 ? 79  PHE A CB  1 
ATOM   635  C  CG  . PHE A 1 82  ? 15.434  14.834  14.212 1.00 27.74 ? 79  PHE A CG  1 
ATOM   636  C  CD1 . PHE A 1 82  ? 15.805  15.788  13.272 1.00 32.15 ? 79  PHE A CD1 1 
ATOM   637  C  CD2 . PHE A 1 82  ? 15.965  13.561  14.097 1.00 30.30 ? 79  PHE A CD2 1 
ATOM   638  C  CE1 . PHE A 1 82  ? 16.705  15.479  12.263 1.00 32.78 ? 79  PHE A CE1 1 
ATOM   639  C  CE2 . PHE A 1 82  ? 16.871  13.252  13.091 1.00 31.71 ? 79  PHE A CE2 1 
ATOM   640  C  CZ  . PHE A 1 82  ? 17.234  14.206  12.172 1.00 32.35 ? 79  PHE A CZ  1 
ATOM   641  N  N   . GLY A 1 83  ? 13.691  16.611  18.455 1.00 23.89 ? 80  GLY A N   1 
ATOM   642  C  CA  . GLY A 1 83  ? 12.557  17.115  19.222 1.00 24.82 ? 80  GLY A CA  1 
ATOM   643  C  C   . GLY A 1 83  ? 11.246  16.416  18.870 1.00 23.18 ? 80  GLY A C   1 
ATOM   644  O  O   . GLY A 1 83  ? 10.209  17.066  18.727 1.00 27.88 ? 80  GLY A O   1 
ATOM   645  N  N   . ILE A 1 84  ? 11.309  15.087  18.776 1.00 23.15 ? 81  ILE A N   1 
ATOM   646  C  CA  . ILE A 1 84  ? 10.226  14.203  18.353 1.00 22.07 ? 81  ILE A CA  1 
ATOM   647  C  C   . ILE A 1 84  ? 9.740   13.436  19.583 1.00 19.79 ? 81  ILE A C   1 
ATOM   648  O  O   . ILE A 1 84  ? 10.498  13.102  20.482 1.00 22.90 ? 81  ILE A O   1 
ATOM   649  C  CB  . ILE A 1 84  ? 10.744  13.242  17.249 1.00 25.62 ? 81  ILE A CB  1 
ATOM   650  C  CG1 . ILE A 1 84  ? 10.965  14.054  15.967 1.00 31.51 ? 81  ILE A CG1 1 
ATOM   651  C  CG2 . ILE A 1 84  ? 9.861   12.024  16.986 1.00 27.87 ? 81  ILE A CG2 1 
ATOM   652  C  CD1 . ILE A 1 84  ? 11.344  13.250  14.775 1.00 34.49 ? 81  ILE A CD1 1 
ATOM   653  N  N   . TYR A 1 85  ? 8.451   13.171  19.639 1.00 18.61 ? 82  TYR A N   1 
ATOM   654  C  CA  . TYR A 1 85  ? 7.851   12.441  20.758 1.00 19.34 ? 82  TYR A CA  1 
ATOM   655  C  C   . TYR A 1 85  ? 7.353   11.109  20.219 1.00 18.96 ? 82  TYR A C   1 
ATOM   656  O  O   . TYR A 1 85  ? 7.226   10.927  19.012 1.00 18.41 ? 82  TYR A O   1 
ATOM   657  C  CB  . TYR A 1 85  ? 6.702   13.211  21.428 1.00 22.47 ? 82  TYR A CB  1 
ATOM   658  C  CG  . TYR A 1 85  ? 7.117   14.646  21.698 1.00 24.28 ? 82  TYR A CG  1 
ATOM   659  C  CD1 . TYR A 1 85  ? 8.084   14.916  22.651 1.00 27.27 ? 82  TYR A CD1 1 
ATOM   660  C  CD2 . TYR A 1 85  ? 6.685   15.689  20.888 1.00 25.27 ? 82  TYR A CD2 1 
ATOM   661  C  CE1 . TYR A 1 85  ? 8.557   16.201  22.858 1.00 29.11 ? 82  TYR A CE1 1 
ATOM   662  C  CE2 . TYR A 1 85  ? 7.178   16.977  21.061 1.00 28.47 ? 82  TYR A CE2 1 
ATOM   663  C  CZ  . TYR A 1 85  ? 8.108   17.224  22.050 1.00 26.45 ? 82  TYR A CZ  1 
ATOM   664  O  OH  . TYR A 1 85  ? 8.576   18.489  22.240 1.00 31.25 ? 82  TYR A OH  1 
ATOM   665  N  N   . PRO A 1 86  ? 7.028   10.139  21.097 1.00 18.81 ? 83  PRO A N   1 
ATOM   666  C  CA  . PRO A 1 86  ? 6.611   8.812   20.629 1.00 18.43 ? 83  PRO A CA  1 
ATOM   667  C  C   . PRO A 1 86  ? 5.466   8.815   19.626 1.00 16.75 ? 83  PRO A C   1 
ATOM   668  O  O   . PRO A 1 86  ? 5.419   7.937   18.782 1.00 17.51 ? 83  PRO A O   1 
ATOM   669  C  CB  . PRO A 1 86  ? 6.219   8.141   21.945 1.00 19.88 ? 83  PRO A CB  1 
ATOM   670  C  CG  . PRO A 1 86  ? 7.194   8.737   22.927 1.00 22.22 ? 83  PRO A CG  1 
ATOM   671  C  CD  . PRO A 1 86  ? 7.190   10.200  22.563 1.00 21.29 ? 83  PRO A CD  1 
ATOM   672  N  N   . GLU A 1 87  ? 4.571   9.800   19.693 1.00 17.05 ? 84  GLU A N   1 
ATOM   673  C  CA  . GLU A 1 87  ? 3.435   9.905   18.803 1.00 17.44 ? 84  GLU A CA  1 
ATOM   674  C  C   . GLU A 1 87  ? 3.810   10.190  17.353 1.00 18.33 ? 84  GLU A C   1 
ATOM   675  O  O   . GLU A 1 87  ? 3.015   9.964   16.440 1.00 19.88 ? 84  GLU A O   1 
ATOM   676  C  CB  . GLU A 1 87  ? 2.544   11.046  19.279 1.00 22.80 ? 84  GLU A CB  1 
ATOM   677  C  CG  . GLU A 1 87  ? 1.811   10.714  20.547 1.00 23.77 ? 84  GLU A CG  1 
ATOM   678  C  CD  . GLU A 1 87  ? 2.682   10.559  21.782 1.00 23.29 ? 84  GLU A CD  1 
ATOM   679  O  OE1 . GLU A 1 87  ? 3.665   11.378  21.875 1.00 25.41 ? 84  GLU A OE1 1 
ATOM   680  O  OE2 . GLU A 1 87  ? 2.386   9.644   22.642 1.00 22.36 ? 84  GLU A OE2 1 
ATOM   681  N  N   . GLU A 1 88  ? 5.046   10.627  17.141 1.00 18.53 ? 85  GLU A N   1 
ATOM   682  C  CA  . GLU A 1 88  ? 5.557   10.913  15.820 1.00 18.31 ? 85  GLU A CA  1 
ATOM   683  C  C   . GLU A 1 88  ? 6.333   9.739   15.236 1.00 15.93 ? 85  GLU A C   1 
ATOM   684  O  O   . GLU A 1 88  ? 6.848   9.882   14.140 1.00 16.52 ? 85  GLU A O   1 
ATOM   685  C  CB  . GLU A 1 88  ? 6.416   12.174  15.910 1.00 19.94 ? 85  GLU A CB  1 
ATOM   686  C  CG  . GLU A 1 88  ? 5.567   13.430  16.025 1.00 23.74 ? 85  GLU A CG  1 
ATOM   687  C  CD  . GLU A 1 88  ? 6.302   14.695  16.412 1.00 25.67 ? 85  GLU A CD  1 
ATOM   688  O  OE1 . GLU A 1 88  ? 6.983   14.673  17.449 1.00 27.39 ? 85  GLU A OE1 1 
ATOM   689  O  OE2 . GLU A 1 88  ? 6.079   15.732  15.744 1.00 31.22 ? 85  GLU A OE2 1 
ATOM   690  N  N   . LEU A 1 89  ? 6.463   8.625   15.972 1.00 15.76 ? 86  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 89  ? 7.214   7.456   15.509 1.00 15.13 ? 86  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 89  ? 6.293   6.516   14.740 1.00 15.18 ? 86  LEU A C   1 
ATOM   693  O  O   . LEU A 1 89  ? 5.139   6.311   15.114 1.00 16.30 ? 86  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 89  ? 7.765   6.617   16.659 1.00 19.32 ? 86  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 89  ? 8.857   7.168   17.542 1.00 21.95 ? 86  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 89  ? 9.228   6.080   18.556 1.00 21.75 ? 86  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 89  ? 10.072  7.587   16.749 1.00 25.07 ? 86  LEU A CD2 1 
ATOM   698  N  N   . VAL A 1 90  ? 6.862   5.831   13.757 1.00 13.99 ? 87  VAL A N   1 
ATOM   699  C  CA  . VAL A 1 90  ? 6.289   4.581   13.259 1.00 13.91 ? 87  VAL A CA  1 
ATOM   700  C  C   . VAL A 1 90  ? 7.459   3.606   13.168 1.00 13.70 ? 87  VAL A C   1 
ATOM   701  O  O   . VAL A 1 90  ? 8.441   3.896   12.495 1.00 15.03 ? 87  VAL A O   1 
ATOM   702  C  CB  . VAL A 1 90  ? 5.627   4.732   11.866 1.00 15.15 ? 87  VAL A CB  1 
ATOM   703  C  CG1 . VAL A 1 90  ? 5.049   3.410   11.392 1.00 17.01 ? 87  VAL A CG1 1 
ATOM   704  C  CG2 . VAL A 1 90  ? 4.607   5.856   11.811 1.00 16.93 ? 87  VAL A CG2 1 
ATOM   705  N  N   . VAL A 1 91  ? 7.342   2.461   13.831 1.00 12.42 ? 88  VAL A N   1 
ATOM   706  C  CA  . VAL A 1 91  ? 8.411   1.468   13.830 1.00 12.18 ? 88  VAL A CA  1 
ATOM   707  C  C   . VAL A 1 91  ? 7.963   0.288   12.980 1.00 12.04 ? 88  VAL A C   1 
ATOM   708  O  O   . VAL A 1 91  ? 6.867   -0.237  13.178 1.00 12.41 ? 88  VAL A O   1 
ATOM   709  C  CB  . VAL A 1 91  ? 8.751   1.012   15.270 1.00 12.42 ? 88  VAL A CB  1 
ATOM   710  C  CG1 . VAL A 1 91  ? 9.826   -0.071  15.269 1.00 13.95 ? 88  VAL A CG1 1 
ATOM   711  C  CG2 . VAL A 1 91  ? 9.197   2.198   16.115 1.00 13.83 ? 88  VAL A CG2 1 
ATOM   712  N  N   . ILE A 1 92  ? 8.814   -0.103  12.039 1.00 11.31 ? 89  ILE A N   1 
ATOM   713  C  CA  . ILE A 1 92  ? 8.502   -1.168  11.092 1.00 11.00 ? 89  ILE A CA  1 
ATOM   714  C  C   . ILE A 1 92  ? 9.475   -2.301  11.360 1.00 10.57 ? 89  ILE A C   1 
ATOM   715  O  O   . ILE A 1 92  ? 10.707  -2.110  11.373 1.00 11.45 ? 89  ILE A O   1 
ATOM   716  C  CB  . ILE A 1 92  ? 8.606   -0.678  9.639  1.00 11.10 ? 89  ILE A CB  1 
ATOM   717  C  CG1 . ILE A 1 92  ? 7.820   0.628   9.453  1.00 12.03 ? 89  ILE A CG1 1 
ATOM   718  C  CG2 . ILE A 1 92  ? 8.163   -1.780  8.689  1.00 11.36 ? 89  ILE A CG2 1 
ATOM   719  C  CD1 . ILE A 1 92  ? 7.776   1.151   8.046  1.00 14.04 ? 89  ILE A CD1 1 
ATOM   720  N  N   . TYR A 1 93  ? 8.933   -3.524  11.564 1.00 11.19 ? 90  TYR A N   1 
ATOM   721  C  CA  . TYR A 1 93  ? 9.798   -4.630  11.959 1.00 11.41 ? 90  TYR A CA  1 
ATOM   722  C  C   . TYR A 1 93  ? 9.134   -5.966  11.599 1.00 11.35 ? 90  TYR A C   1 
ATOM   723  O  O   . TYR A 1 93  ? 7.938   -6.023  11.249 1.00 11.84 ? 90  TYR A O   1 
ATOM   724  C  CB  . TYR A 1 93  ? 10.106  -4.533  13.466 1.00 11.98 ? 90  TYR A CB  1 
ATOM   725  C  CG  . TYR A 1 93  ? 8.920   -4.890  14.343 1.00 13.76 ? 90  TYR A CG  1 
ATOM   726  C  CD1 . TYR A 1 93  ? 7.870   -4.009  14.581 1.00 15.82 ? 90  TYR A CD1 1 
ATOM   727  C  CD2 . TYR A 1 93  ? 8.868   -6.137  14.965 1.00 15.06 ? 90  TYR A CD2 1 
ATOM   728  C  CE1 . TYR A 1 93  ? 6.784   -4.407  15.365 1.00 17.31 ? 90  TYR A CE1 1 
ATOM   729  C  CE2 . TYR A 1 93  ? 7.784   -6.554  15.727 1.00 17.66 ? 90  TYR A CE2 1 
ATOM   730  C  CZ  . TYR A 1 93  ? 6.730   -5.686  15.892 1.00 18.10 ? 90  TYR A CZ  1 
ATOM   731  O  OH  . TYR A 1 93  ? 5.687   -6.089  16.651 1.00 22.31 ? 90  TYR A OH  1 
ATOM   732  N  N   . ASP A 1 94  ? 9.925   -7.027  11.755 1.00 10.70 ? 91  ASP A N   1 
ATOM   733  C  CA  . ASP A 1 94  ? 9.491   -8.381  11.449 1.00 11.26 ? 91  ASP A CA  1 
ATOM   734  C  C   . ASP A 1 94  ? 8.679   -9.021  12.565 1.00 12.28 ? 91  ASP A C   1 
ATOM   735  O  O   . ASP A 1 94  ? 9.112   -9.075  13.713 1.00 13.91 ? 91  ASP A O   1 
ATOM   736  C  CB  . ASP A 1 94  ? 10.691  -9.276  11.236 1.00 11.64 ? 91  ASP A CB  1 
ATOM   737  C  CG  . ASP A 1 94  ? 11.762  -9.243  12.313 1.00 12.90 ? 91  ASP A CG  1 
ATOM   738  O  OD1 . ASP A 1 94  ? 12.172  -8.145  12.735 1.00 13.45 ? 91  ASP A OD1 1 
ATOM   739  O  OD2 . ASP A 1 94  ? 12.278  -10.354 12.638 1.00 13.94 ? 91  ASP A OD2 1 
ATOM   740  N  N   . ASP A 1 95  ? 7.545   -9.618  12.190 1.00 12.51 ? 92  ASP A N   1 
ATOM   741  C  CA  . ASP A 1 95  ? 6.662   -10.304 13.120 1.00 12.60 ? 92  ASP A CA  1 
ATOM   742  C  C   . ASP A 1 95  ? 6.609   -11.797 12.804 1.00 12.28 ? 92  ASP A C   1 
ATOM   743  O  O   . ASP A 1 95  ? 6.065   -12.192 11.784 1.00 12.00 ? 92  ASP A O   1 
ATOM   744  C  CB  . ASP A 1 95  ? 5.283   -9.655  13.012 1.00 14.26 ? 92  ASP A CB  1 
ATOM   745  C  CG  . ASP A 1 95  ? 4.198   -10.187 13.924 1.00 15.22 ? 92  ASP A CG  1 
ATOM   746  O  OD1 . ASP A 1 95  ? 4.410   -11.191 14.596 1.00 15.93 ? 92  ASP A OD1 1 
ATOM   747  O  OD2 . ASP A 1 95  ? 3.113   -9.539  13.920 1.00 16.42 ? 92  ASP A OD2 1 
ATOM   748  N  N   . LEU A 1 96  ? 7.169   -12.592 13.717 1.00 12.74 ? 93  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 96  ? 7.238   -14.037 13.621 1.00 14.89 ? 93  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 96  ? 5.906   -14.696 13.956 1.00 13.90 ? 93  LEU A C   1 
ATOM   751  O  O   . LEU A 1 96  ? 5.814   -15.911 13.933 1.00 15.04 ? 93  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 96  ? 8.220   -14.552 14.688 1.00 22.05 ? 93  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 96  ? 9.683   -14.639 14.369 1.00 25.09 ? 93  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 96  ? 10.450  -14.977 15.630 1.00 23.62 ? 93  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 96  ? 9.945   -15.694 13.336 1.00 25.77 ? 93  LEU A CD2 1 
ATOM   756  N  N   . ASP A 1 97  ? 4.919   -13.901 14.362 1.00 13.70 ? 94  ASP A N   1 
ATOM   757  C  CA  . ASP A 1 97  ? 3.567   -14.376 14.662 1.00 13.92 ? 94  ASP A CA  1 
ATOM   758  C  C   . ASP A 1 97  ? 2.560   -13.839 13.650 1.00 13.36 ? 94  ASP A C   1 
ATOM   759  O  O   . ASP A 1 97  ? 1.417   -13.518 14.012 1.00 16.50 ? 94  ASP A O   1 
ATOM   760  C  CB  . ASP A 1 97  ? 3.140   -13.951 16.083 1.00 16.07 ? 94  ASP A CB  1 
ATOM   761  C  CG  . ASP A 1 97  ? 1.832   -14.544 16.564 1.00 18.39 ? 94  ASP A CG  1 
ATOM   762  O  OD1 . ASP A 1 97  ? 1.616   -15.715 16.245 1.00 19.39 ? 94  ASP A OD1 1 
ATOM   763  O  OD2 . ASP A 1 97  ? 1.051   -13.814 17.311 1.00 23.13 ? 94  ASP A OD2 1 
ATOM   764  N  N   . LEU A 1 98  ? 2.968   -13.758 12.403 1.00 12.64 ? 95  LEU A N   1 
ATOM   765  C  CA  . LEU A 1 98  ? 2.143   -13.263 11.316 1.00 12.65 ? 95  LEU A CA  1 
ATOM   766  C  C   . LEU A 1 98  ? 2.707   -13.808 10.010 1.00 12.59 ? 95  LEU A C   1 
ATOM   767  O  O   . LEU A 1 98  ? 3.938   -13.869 9.858  1.00 12.90 ? 95  LEU A O   1 
ATOM   768  C  CB  . LEU A 1 98  ? 2.171   -11.732 11.367 1.00 13.63 ? 95  LEU A CB  1 
ATOM   769  C  CG  . LEU A 1 98  ? 1.223   -11.003 10.418 1.00 14.86 ? 95  LEU A CG  1 
ATOM   770  C  CD1 . LEU A 1 98  ? -0.236  -11.286 10.721 1.00 16.18 ? 95  LEU A CD1 1 
ATOM   771  C  CD2 . LEU A 1 98  ? 1.458   -9.516  10.482 1.00 15.61 ? 95  LEU A CD2 1 
ATOM   772  N  N   . ALA A 1 99  ? 1.845   -14.192 9.095  1.00 12.68 ? 96  ALA A N   1 
ATOM   773  C  CA  . ALA A 1 99  ? 2.232   -14.856 7.867  1.00 13.59 ? 96  ALA A CA  1 
ATOM   774  C  C   . ALA A 1 99  ? 2.945   -13.884 6.937  1.00 12.90 ? 96  ALA A C   1 
ATOM   775  O  O   . ALA A 1 99  ? 2.616   -12.703 6.859  1.00 13.52 ? 96  ALA A O   1 
ATOM   776  C  CB  . ALA A 1 99  ? 1.033   -15.443 7.145  1.00 15.07 ? 96  ALA A CB  1 
ATOM   777  N  N   . VAL A 1 100 ? 3.875   -14.422 6.153  1.00 13.09 ? 97  VAL A N   1 
ATOM   778  C  CA  . VAL A 1 100 ? 4.414   -13.721 5.009  1.00 14.61 ? 97  VAL A CA  1 
ATOM   779  C  C   . VAL A 1 100 ? 3.250   -13.311 4.115  1.00 14.08 ? 97  VAL A C   1 
ATOM   780  O  O   . VAL A 1 100 ? 2.391   -14.131 3.789  1.00 14.99 ? 97  VAL A O   1 
ATOM   781  C  CB  . VAL A 1 100 ? 5.446   -14.572 4.252  1.00 16.16 ? 97  VAL A CB  1 
ATOM   782  C  CG1 . VAL A 1 100 ? 5.916   -13.843 3.004  1.00 18.79 ? 97  VAL A CG1 1 
ATOM   783  C  CG2 . VAL A 1 100 ? 6.630   -14.953 5.112  1.00 17.55 ? 97  VAL A CG2 1 
ATOM   784  N  N   . GLY A 1 101 ? 3.262   -12.050 3.707  1.00 15.05 ? 98  GLY A N   1 
ATOM   785  C  CA  . GLY A 1 101 ? 2.179   -11.483 2.922  1.00 15.84 ? 98  GLY A CA  1 
ATOM   786  C  C   . GLY A 1 101 ? 1.198   -10.603 3.692  1.00 15.59 ? 98  GLY A C   1 
ATOM   787  O  O   . GLY A 1 101 ? 0.363   -9.949  3.077  1.00 16.54 ? 98  GLY A O   1 
ATOM   788  N  N   . LYS A 1 102 ? 1.266   -10.640 5.018  1.00 14.57 ? 99  LYS A N   1 
ATOM   789  C  CA  . LYS A 1 102 ? 0.378   -9.850  5.844  1.00 14.24 ? 99  LYS A CA  1 
ATOM   790  C  C   . LYS A 1 102 ? 1.136   -8.799  6.641  1.00 13.13 ? 99  LYS A C   1 
ATOM   791  O  O   . LYS A 1 102 ? 2.339   -8.953  6.898  1.00 13.36 ? 99  LYS A O   1 
ATOM   792  C  CB  . LYS A 1 102 ? -0.382  -10.751 6.820  1.00 16.02 ? 99  LYS A CB  1 
ATOM   793  C  CG  . LYS A 1 102 ? -1.294  -11.749 6.125  1.00 19.00 ? 99  LYS A CG  1 
ATOM   794  C  CD  . LYS A 1 102 ? -2.118  -12.572 7.100  1.00 21.26 ? 99  LYS A CD  1 
ATOM   795  C  CE  . LYS A 1 102 ? -3.170  -13.480 6.498  1.00 28.16 ? 99  LYS A CE  1 
ATOM   796  N  NZ  . LYS A 1 102 ? -2.522  -14.421 5.572  1.00 32.47 ? 99  LYS A NZ  1 
ATOM   797  N  N   . ILE A 1 103 ? 0.444   -7.705  6.942  1.00 13.20 ? 100 ILE A N   1 
ATOM   798  C  CA  . ILE A 1 103 ? 0.909   -6.695  7.874  1.00 12.50 ? 100 ILE A CA  1 
ATOM   799  C  C   . ILE A 1 103 ? -0.147  -6.479  8.949  1.00 12.70 ? 100 ILE A C   1 
ATOM   800  O  O   . ILE A 1 103 ? -1.323  -6.783  8.722  1.00 14.25 ? 100 ILE A O   1 
ATOM   801  C  CB  . ILE A 1 103 ? 1.280   -5.390  7.162  1.00 13.59 ? 100 ILE A CB  1 
ATOM   802  C  CG1 . ILE A 1 103 ? 0.065   -4.627  6.640  1.00 14.07 ? 100 ILE A CG1 1 
ATOM   803  C  CG2 . ILE A 1 103 ? 2.307   -5.654  6.082  1.00 14.69 ? 100 ILE A CG2 1 
ATOM   804  C  CD1 . ILE A 1 103 ? 0.454   -3.260  6.105  1.00 15.27 ? 100 ILE A CD1 1 
ATOM   805  N  N   . ARG A 1 104 ? 0.252   -5.875  10.066 1.00 12.35 ? 101 ARG A N   1 
ATOM   806  C  CA  . ARG A 1 104 ? -0.684  -5.499  11.118 1.00 13.02 ? 101 ARG A CA  1 
ATOM   807  C  C   . ARG A 1 104 ? -0.166  -4.236  11.759 1.00 13.54 ? 101 ARG A C   1 
ATOM   808  O  O   . ARG A 1 104 ? 1.011   -4.124  12.061 1.00 15.13 ? 101 ARG A O   1 
ATOM   809  C  CB  . ARG A 1 104 ? -0.834  -6.609  12.166 1.00 16.08 ? 101 ARG A CB  1 
ATOM   810  C  CG  . ARG A 1 104 ? -2.182  -6.624  12.885 1.00 23.06 ? 101 ARG A CG  1 
ATOM   811  C  CD  . ARG A 1 104 ? -3.390  -7.056  12.079 1.00 24.19 ? 101 ARG A CD  1 
ATOM   812  N  NE  . ARG A 1 104 ? -3.482  -8.242  11.271 1.00 27.94 ? 101 ARG A NE  1 
ATOM   813  C  CZ  . ARG A 1 104 ? -3.640  -9.489  11.673 1.00 29.70 ? 101 ARG A CZ  1 
ATOM   814  N  NH1 . ARG A 1 104 ? -3.411  -9.857  12.929 1.00 29.12 ? 101 ARG A NH1 1 
ATOM   815  N  NH2 . ARG A 1 104 ? -3.934  -10.405 10.762 1.00 27.89 ? 101 ARG A NH2 1 
ATOM   816  N  N   . LEU A 1 105 ? -1.072  -3.297  11.962 1.00 13.47 ? 102 LEU A N   1 
ATOM   817  C  CA  . LEU A 1 105 ? -0.776  -2.015  12.575 1.00 12.89 ? 102 LEU A CA  1 
ATOM   818  C  C   . LEU A 1 105 ? -1.308  -2.039  14.002 1.00 12.89 ? 102 LEU A C   1 
ATOM   819  O  O   . LEU A 1 105 ? -2.466  -2.391  14.239 1.00 13.96 ? 102 LEU A O   1 
ATOM   820  C  CB  . LEU A 1 105 ? -1.448  -0.897  11.787 1.00 14.05 ? 102 LEU A CB  1 
ATOM   821  C  CG  . LEU A 1 105 ? -0.651  -0.365  10.598 1.00 15.21 ? 102 LEU A CG  1 
ATOM   822  C  CD1 . LEU A 1 105 ? -0.394  -1.407  9.505  1.00 16.50 ? 102 LEU A CD1 1 
ATOM   823  C  CD2 . LEU A 1 105 ? -1.407  0.856   10.039 1.00 15.14 ? 102 LEU A CD2 1 
ATOM   824  N  N   . ARG A 1 106 ? -0.487  -1.628  14.956 1.00 13.25 ? 103 ARG A N   1 
ATOM   825  C  CA  . ARG A 1 106 ? -0.870  -1.535  16.363 1.00 13.81 ? 103 ARG A CA  1 
ATOM   826  C  C   . ARG A 1 106 ? -0.128  -0.381  17.029 1.00 13.82 ? 103 ARG A C   1 
ATOM   827  O  O   . ARG A 1 106 ? 0.875   0.084   16.538 1.00 14.23 ? 103 ARG A O   1 
ATOM   828  C  CB  . ARG A 1 106 ? -0.470  -2.806  17.122 1.00 15.25 ? 103 ARG A CB  1 
ATOM   829  C  CG  . ARG A 1 106 ? -1.224  -4.042  16.707 1.00 17.17 ? 103 ARG A CG  1 
ATOM   830  C  CD  . ARG A 1 106 ? -2.698  -3.943  17.014 1.00 20.31 ? 103 ARG A CD  1 
ATOM   831  N  NE  . ARG A 1 106 ? -3.291  -5.222  16.698 1.00 25.06 ? 103 ARG A NE  1 
ATOM   832  C  CZ  . ARG A 1 106 ? -4.580  -5.431  16.547 1.00 25.93 ? 103 ARG A CZ  1 
ATOM   833  N  NH1 . ARG A 1 106 ? -5.436  -4.523  16.967 1.00 25.89 ? 103 ARG A NH1 1 
ATOM   834  N  NH2 . ARG A 1 106 ? -4.993  -6.566  16.003 1.00 27.50 ? 103 ARG A NH2 1 
ATOM   835  N  N   . GLN A 1 107 ? -0.681  0.119   18.156 1.00 13.28 ? 104 GLN A N   1 
ATOM   836  C  CA  . GLN A 1 107 ? -0.110  1.251   18.882 1.00 14.72 ? 104 GLN A CA  1 
ATOM   837  C  C   . GLN A 1 107 ? 0.516   0.886   20.229 1.00 15.13 ? 104 GLN A C   1 
ATOM   838  O  O   . GLN A 1 107 ? 1.076   1.762   20.865 1.00 16.70 ? 104 GLN A O   1 
ATOM   839  C  CB  . GLN A 1 107 ? -1.150  2.315   19.151 1.00 15.50 ? 104 GLN A CB  1 
ATOM   840  C  CG  . GLN A 1 107 ? -1.734  2.853   17.871 1.00 16.01 ? 104 GLN A CG  1 
ATOM   841  C  CD  . GLN A 1 107 ? -2.537  4.106   18.118 1.00 16.40 ? 104 GLN A CD  1 
ATOM   842  O  OE1 . GLN A 1 107 ? -3.679  4.041   18.589 1.00 16.99 ? 104 GLN A OE1 1 
ATOM   843  N  NE2 . GLN A 1 107 ? -1.958  5.246   17.774 1.00 17.26 ? 104 GLN A NE2 1 
ATOM   844  N  N   . LYS A 1 108 ? 0.494   -0.391  20.614 1.00 16.24 ? 105 LYS A N   1 
ATOM   845  C  CA  . LYS A 1 108 ? 1.028   -0.780  21.897 1.00 18.60 ? 105 LYS A CA  1 
ATOM   846  C  C   . LYS A 1 108 ? 1.405   -2.236  21.816 1.00 20.81 ? 105 LYS A C   1 
ATOM   847  O  O   . LYS A 1 108 ? 0.809   -3.004  21.062 1.00 23.51 ? 105 LYS A O   1 
ATOM   848  C  CB  . LYS A 1 108 ? -0.011  -0.570  22.997 1.00 21.05 ? 105 LYS A CB  1 
ATOM   849  C  CG  . LYS A 1 108 ? 0.494   -0.698  24.429 1.00 23.69 ? 105 LYS A CG  1 
ATOM   850  C  CD  . LYS A 1 108 ? -0.642  -0.439  25.422 1.00 26.36 ? 105 LYS A CD  1 
ATOM   851  C  CE  . LYS A 1 108 ? -0.322  0.084   26.817 1.00 32.04 ? 105 LYS A CE  1 
ATOM   852  N  NZ  . LYS A 1 108 ? 0.875   -0.512  27.445 1.00 34.04 ? 105 LYS A NZ  1 
ATOM   853  N  N   . GLY A 1 109 ? 2.395   -2.621  22.621 1.00 22.85 ? 106 GLY A N   1 
ATOM   854  C  CA  . GLY A 1 109 ? 2.750   -4.023  22.727 1.00 23.59 ? 106 GLY A CA  1 
ATOM   855  C  C   . GLY A 1 109 ? 4.239   -4.244  22.987 1.00 23.11 ? 106 GLY A C   1 
ATOM   856  O  O   . GLY A 1 109 ? 5.072   -3.372  22.768 1.00 24.57 ? 106 GLY A O   1 
ATOM   857  N  N   . SER A 1 110 ? 4.604   -5.468  23.366 1.00 25.02 ? 107 SER A N   1 
ATOM   858  C  CA  A SER A 1 110 ? 6.009   -5.773  23.591 0.50 23.02 ? 107 SER A CA  1 
ATOM   859  C  CA  B SER A 1 110 ? 5.992   -5.823  23.631 0.50 23.51 ? 107 SER A CA  1 
ATOM   860  C  C   . SER A 1 110 ? 6.541   -6.795  22.587 1.00 22.70 ? 107 SER A C   1 
ATOM   861  O  O   . SER A 1 110 ? 7.683   -7.245  22.725 1.00 23.99 ? 107 SER A O   1 
ATOM   862  C  CB  A SER A 1 110 ? 6.231   -6.161  25.016 0.50 24.85 ? 107 SER A CB  1 
ATOM   863  C  CB  B SER A 1 110 ? 6.125   -6.418  24.991 0.50 26.39 ? 107 SER A CB  1 
ATOM   864  O  OG  A SER A 1 110 ? 5.772   -5.115  25.857 0.50 24.38 ? 107 SER A OG  1 
ATOM   865  O  OG  B SER A 1 110 ? 5.671   -7.753  24.953 0.50 26.94 ? 107 SER A OG  1 
ATOM   866  N  N   . ALA A 1 111 ? 5.752   -7.090  21.537 1.00 21.76 ? 108 ALA A N   1 
ATOM   867  C  CA  . ALA A 1 111 ? 6.193   -7.881  20.389 1.00 22.24 ? 108 ALA A CA  1 
ATOM   868  C  C   . ALA A 1 111 ? 6.779   -9.227  20.797 1.00 22.99 ? 108 ALA A C   1 
ATOM   869  O  O   . ALA A 1 111 ? 7.642   -9.755  20.098 1.00 23.97 ? 108 ALA A O   1 
ATOM   870  C  CB  . ALA A 1 111 ? 7.157   -7.101  19.541 1.00 22.91 ? 108 ALA A CB  1 
ATOM   871  N  N   . GLY A 1 112 ? 6.252   -9.825  21.866 1.00 24.72 ? 109 GLY A N   1 
ATOM   872  C  CA  . GLY A 1 112 ? 6.654   -11.171 22.234 1.00 26.09 ? 109 GLY A CA  1 
ATOM   873  C  C   . GLY A 1 112 ? 8.149   -11.321 22.529 1.00 25.46 ? 109 GLY A C   1 
ATOM   874  O  O   . GLY A 1 112 ? 8.735   -12.384 22.318 1.00 28.84 ? 109 GLY A O   1 
ATOM   875  N  N   . GLY A 1 113 ? 8.773   -10.247 22.989 1.00 22.08 ? 110 GLY A N   1 
ATOM   876  C  CA  . GLY A 1 113 ? 10.189  -10.235 23.304 1.00 24.42 ? 110 GLY A CA  1 
ATOM   877  C  C   . GLY A 1 113 ? 11.100  -9.968  22.103 1.00 22.69 ? 110 GLY A C   1 
ATOM   878  O  O   . GLY A 1 113 ? 12.322  -10.038 22.234 1.00 25.26 ? 110 GLY A O   1 
ATOM   879  N  N   . HIS A 1 114 ? 10.545  -9.656  20.921 1.00 18.40 ? 111 HIS A N   1 
ATOM   880  C  CA  . HIS A 1 114 ? 11.389  -9.176  19.818 1.00 17.65 ? 111 HIS A CA  1 
ATOM   881  C  C   . HIS A 1 114 ? 12.439  -8.201  20.366 1.00 17.56 ? 111 HIS A C   1 
ATOM   882  O  O   . HIS A 1 114 ? 12.048  -7.226  21.002 1.00 18.47 ? 111 HIS A O   1 
ATOM   883  C  CB  . HIS A 1 114 ? 10.528  -8.451  18.754 1.00 17.46 ? 111 HIS A CB  1 
ATOM   884  C  CG  . HIS A 1 114 ? 11.261  -8.027  17.535 1.00 16.60 ? 111 HIS A CG  1 
ATOM   885  N  ND1 . HIS A 1 114 ? 12.034  -6.883  17.464 1.00 17.43 ? 111 HIS A ND1 1 
ATOM   886  C  CD2 . HIS A 1 114 ? 11.274  -8.606  16.314 1.00 17.11 ? 111 HIS A CD2 1 
ATOM   887  C  CE1 . HIS A 1 114 ? 12.526  -6.822  16.228 1.00 17.63 ? 111 HIS A CE1 1 
ATOM   888  N  NE2 . HIS A 1 114 ? 12.097  -7.887  15.513 1.00 16.30 ? 111 HIS A NE2 1 
ATOM   889  N  N   . ASN A 1 115 ? 13.739  -8.454  20.084 1.00 19.74 ? 112 ASN A N   1 
ATOM   890  C  CA  . ASN A 1 115 ? 14.821  -7.773  20.757 1.00 20.75 ? 112 ASN A CA  1 
ATOM   891  C  C   . ASN A 1 115 ? 14.922  -6.325  20.299 1.00 18.06 ? 112 ASN A C   1 
ATOM   892  O  O   . ASN A 1 115 ? 15.396  -5.498  21.057 1.00 18.95 ? 112 ASN A O   1 
ATOM   893  C  CB  . ASN A 1 115 ? 16.157  -8.515  20.636 1.00 26.07 ? 112 ASN A CB  1 
ATOM   894  C  CG  . ASN A 1 115 ? 16.296  -9.660  21.611 1.00 31.22 ? 112 ASN A CG  1 
ATOM   895  O  OD1 . ASN A 1 115 ? 15.664  -9.680  22.676 1.00 37.04 ? 112 ASN A OD1 1 
ATOM   896  N  ND2 . ASN A 1 115 ? 17.162  -10.593 21.268 1.00 38.86 ? 112 ASN A ND2 1 
ATOM   897  N  N   . GLY A 1 116 ? 14.459  -5.995  19.085 1.00 16.37 ? 113 GLY A N   1 
ATOM   898  C  CA  . GLY A 1 116 ? 14.504  -4.613  18.663 1.00 15.59 ? 113 GLY A CA  1 
ATOM   899  C  C   . GLY A 1 116 ? 13.470  -3.736  19.321 1.00 14.82 ? 113 GLY A C   1 
ATOM   900  O  O   . GLY A 1 116 ? 13.775  -2.657  19.839 1.00 14.47 ? 113 GLY A O   1 
ATOM   901  N  N   . ILE A 1 117 ? 12.226  -4.227  19.325 1.00 14.26 ? 114 ILE A N   1 
ATOM   902  C  CA  . ILE A 1 117 ? 11.166  -3.540  20.071 1.00 14.08 ? 114 ILE A CA  1 
ATOM   903  C  C   . ILE A 1 117 ? 11.553  -3.422  21.555 1.00 14.89 ? 114 ILE A C   1 
ATOM   904  O  O   . ILE A 1 117 ? 11.331  -2.390  22.163 1.00 14.57 ? 114 ILE A O   1 
ATOM   905  C  CB  . ILE A 1 117 ? 9.851   -4.303  19.850 1.00 15.87 ? 114 ILE A CB  1 
ATOM   906  C  CG1 . ILE A 1 117 ? 9.391   -4.216  18.396 1.00 15.14 ? 114 ILE A CG1 1 
ATOM   907  C  CG2 . ILE A 1 117 ? 8.757   -3.856  20.825 1.00 16.29 ? 114 ILE A CG2 1 
ATOM   908  C  CD1 . ILE A 1 117 ? 9.017   -2.808  17.909 1.00 15.72 ? 114 ILE A CD1 1 
ATOM   909  N  N   . LYS A 1 118 ? 12.111  -4.484  22.137 1.00 14.65 ? 115 LYS A N   1 
ATOM   910  C  CA  . LYS A 1 118 ? 12.488  -4.451  23.541 1.00 15.29 ? 115 LYS A CA  1 
ATOM   911  C  C   . LYS A 1 118 ? 13.483  -3.323  23.808 1.00 14.43 ? 115 LYS A C   1 
ATOM   912  O  O   . LYS A 1 118 ? 13.398  -2.623  24.804 1.00 14.87 ? 115 LYS A O   1 
ATOM   913  C  CB  . LYS A 1 118 ? 13.079  -5.800  23.947 1.00 16.12 ? 115 LYS A CB  1 
ATOM   914  C  CG  . LYS A 1 118 ? 13.522  -5.927  25.394 1.00 18.57 ? 115 LYS A CG  1 
ATOM   915  C  CD  . LYS A 1 118 ? 14.050  -7.279  25.705 1.00 21.06 ? 115 LYS A CD  1 
ATOM   916  C  CE  . LYS A 1 118 ? 14.368  -7.452  27.167 1.00 25.37 ? 115 LYS A CE  1 
ATOM   917  N  NZ  . LYS A 1 118 ? 14.572  -8.877  27.443 1.00 26.31 ? 115 LYS A NZ  1 
ATOM   918  N  N   . SER A 1 119 ? 14.457  -3.160  22.912 1.00 13.36 ? 116 SER A N   1 
ATOM   919  C  CA  . SER A 1 119 ? 15.475  -2.129  23.078 1.00 13.40 ? 116 SER A CA  1 
ATOM   920  C  C   . SER A 1 119 ? 14.827  -0.748  23.020 1.00 14.70 ? 116 SER A C   1 
ATOM   921  O  O   . SER A 1 119 ? 15.202  0.163   23.750 1.00 15.00 ? 116 SER A O   1 
ATOM   922  C  CB  . SER A 1 119 ? 16.555  -2.295  22.026 1.00 14.51 ? 116 SER A CB  1 
ATOM   923  O  OG  . SER A 1 119 ? 17.535  -1.274  22.139 1.00 14.49 ? 116 SER A OG  1 
ATOM   924  N  N   . ILE A 1 120 ? 13.909  -0.562  22.049 1.00 13.76 ? 117 ILE A N   1 
ATOM   925  C  CA  . ILE A 1 120 ? 13.235  0.707   21.933 1.00 13.80 ? 117 ILE A CA  1 
ATOM   926  C  C   . ILE A 1 120 ? 12.448  0.975   23.218 1.00 14.48 ? 117 ILE A C   1 
ATOM   927  O  O   . ILE A 1 120 ? 12.531  2.076   23.754 1.00 15.95 ? 117 ILE A O   1 
ATOM   928  C  CB  . ILE A 1 120 ? 12.350  0.766   20.689 1.00 15.14 ? 117 ILE A CB  1 
ATOM   929  C  CG1 . ILE A 1 120 ? 13.228  0.779   19.443 1.00 16.72 ? 117 ILE A CG1 1 
ATOM   930  C  CG2 . ILE A 1 120 ? 11.409  1.955   20.748 1.00 16.95 ? 117 ILE A CG2 1 
ATOM   931  C  CD1 . ILE A 1 120 ? 12.503  0.569   18.190 1.00 17.27 ? 117 ILE A CD1 1 
ATOM   932  N  N   . ILE A 1 121 ? 11.683  -0.023  23.689 1.00 15.15 ? 118 ILE A N   1 
ATOM   933  C  CA  . ILE A 1 121 ? 10.948  0.139   24.945 1.00 17.79 ? 118 ILE A CA  1 
ATOM   934  C  C   . ILE A 1 121 ? 11.889  0.534   26.076 1.00 18.69 ? 118 ILE A C   1 
ATOM   935  O  O   . ILE A 1 121 ? 11.574  1.405   26.875 1.00 23.15 ? 118 ILE A O   1 
ATOM   936  C  CB  . ILE A 1 121 ? 10.143  -1.128  25.267 1.00 17.99 ? 118 ILE A CB  1 
ATOM   937  C  CG1 . ILE A 1 121 ? 9.081   -1.361  24.189 1.00 17.95 ? 118 ILE A CG1 1 
ATOM   938  C  CG2 . ILE A 1 121 ? 9.531   -1.062  26.661 1.00 19.64 ? 118 ILE A CG2 1 
ATOM   939  C  CD1 . ILE A 1 121 ? 8.334   -2.662  24.318 1.00 17.88 ? 118 ILE A CD1 1 
ATOM   940  N  N   . SER A 1 122 ? 13.037  -0.141  26.155 1.00 18.65 ? 119 SER A N   1 
ATOM   941  C  CA  . SER A 1 122 ? 14.015  0.134   27.193 1.00 20.42 ? 119 SER A CA  1 
ATOM   942  C  C   . SER A 1 122 ? 14.418  1.606   27.169 1.00 20.85 ? 119 SER A C   1 
ATOM   943  O  O   . SER A 1 122 ? 14.526  2.240   28.220 1.00 24.36 ? 119 SER A O   1 
ATOM   944  C  CB  . SER A 1 122 ? 15.209  -0.751  26.993 1.00 23.00 ? 119 SER A CB  1 
ATOM   945  O  OG  . SER A 1 122 ? 16.179  -0.516  28.006 1.00 27.41 ? 119 SER A OG  1 
ATOM   946  N  N   . HIS A 1 123 ? 14.708  2.120   25.973 1.00 18.26 ? 120 HIS A N   1 
ATOM   947  C  CA  . HIS A 1 123 ? 15.282  3.452   25.864 1.00 19.06 ? 120 HIS A CA  1 
ATOM   948  C  C   . HIS A 1 123 ? 14.225  4.536   26.020 1.00 21.33 ? 120 HIS A C   1 
ATOM   949  O  O   . HIS A 1 123 ? 14.556  5.612   26.510 1.00 25.56 ? 120 HIS A O   1 
ATOM   950  C  CB  . HIS A 1 123 ? 16.103  3.596   24.574 1.00 18.60 ? 120 HIS A CB  1 
ATOM   951  C  CG  . HIS A 1 123 ? 17.448  2.985   24.723 1.00 18.20 ? 120 HIS A CG  1 
ATOM   952  N  ND1 . HIS A 1 123 ? 18.596  3.702   24.935 1.00 18.83 ? 120 HIS A ND1 1 
ATOM   953  C  CD2 . HIS A 1 123 ? 17.834  1.701   24.692 1.00 18.23 ? 120 HIS A CD2 1 
ATOM   954  C  CE1 . HIS A 1 123 ? 19.620  2.877   25.072 1.00 20.63 ? 120 HIS A CE1 1 
ATOM   955  N  NE2 . HIS A 1 123 ? 19.195  1.646   24.887 1.00 20.68 ? 120 HIS A NE2 1 
ATOM   956  N  N   . LEU A 1 124 ? 12.998  4.271   25.541 1.00 21.05 ? 121 LEU A N   1 
ATOM   957  C  CA  . LEU A 1 124 ? 11.918  5.241   25.635 1.00 22.57 ? 121 LEU A CA  1 
ATOM   958  C  C   . LEU A 1 124 ? 11.124  5.098   26.933 1.00 21.98 ? 121 LEU A C   1 
ATOM   959  O  O   . LEU A 1 124 ? 10.373  6.004   27.271 1.00 25.69 ? 121 LEU A O   1 
ATOM   960  C  CB  . LEU A 1 124 ? 10.966  5.053   24.459 1.00 23.04 ? 121 LEU A CB  1 
ATOM   961  C  CG  . LEU A 1 124 ? 11.549  5.232   23.060 1.00 27.15 ? 121 LEU A CG  1 
ATOM   962  C  CD1 . LEU A 1 124 ? 10.424  5.257   22.044 1.00 26.18 ? 121 LEU A CD1 1 
ATOM   963  C  CD2 . LEU A 1 124 ? 12.398  6.481   22.927 1.00 29.53 ? 121 LEU A CD2 1 
ATOM   964  N  N   . ASN A 1 125 ? 11.317  3.994   27.657 1.00 21.81 ? 122 ASN A N   1 
ATOM   965  C  CA  . ASN A 1 125 ? 10.563  3.676   28.864 1.00 23.35 ? 122 ASN A CA  1 
ATOM   966  C  C   . ASN A 1 125 ? 9.060   3.748   28.602 1.00 24.92 ? 122 ASN A C   1 
ATOM   967  O  O   . ASN A 1 125 ? 8.301   4.196   29.444 1.00 28.79 ? 122 ASN A O   1 
ATOM   968  C  CB  . ASN A 1 125 ? 10.969  4.529   30.077 1.00 28.99 ? 122 ASN A CB  1 
ATOM   969  C  CG  . ASN A 1 125 ? 12.289  4.106   30.682 1.00 31.52 ? 122 ASN A CG  1 
ATOM   970  O  OD1 . ASN A 1 125 ? 12.564  2.920   30.912 1.00 32.07 ? 122 ASN A OD1 1 
ATOM   971  N  ND2 . ASN A 1 125 ? 13.138  5.082   30.916 1.00 38.05 ? 122 ASN A ND2 1 
ATOM   972  N  N   . THR A 1 126 ? 8.629   3.271   27.443 1.00 22.57 ? 123 THR A N   1 
ATOM   973  C  CA  . THR A 1 126 ? 7.222   3.137   27.100 1.00 21.98 ? 123 THR A CA  1 
ATOM   974  C  C   . THR A 1 126 ? 7.126   2.054   26.035 1.00 20.33 ? 123 THR A C   1 
ATOM   975  O  O   . THR A 1 126 ? 8.002   1.976   25.180 1.00 19.08 ? 123 THR A O   1 
ATOM   976  C  CB  . THR A 1 126 ? 6.652   4.470   26.597 1.00 23.34 ? 123 THR A CB  1 
ATOM   977  O  OG1 . THR A 1 126 ? 5.261   4.303   26.316 1.00 22.64 ? 123 THR A OG1 1 
ATOM   978  C  CG2 . THR A 1 126 ? 7.338   5.007   25.356 1.00 26.00 ? 123 THR A CG2 1 
ATOM   979  N  N   . ASN A 1 127 ? 6.022   1.293   26.043 1.00 20.50 ? 124 ASN A N   1 
ATOM   980  C  CA  . ASN A 1 127 ? 5.701   0.379   24.947 1.00 19.76 ? 124 ASN A CA  1 
ATOM   981  C  C   . ASN A 1 127 ? 4.575   0.908   24.079 1.00 17.03 ? 124 ASN A C   1 
ATOM   982  O  O   . ASN A 1 127 ? 4.052   0.146   23.264 1.00 18.02 ? 124 ASN A O   1 
ATOM   983  C  CB  . ASN A 1 127 ? 5.411   -1.022  25.477 1.00 23.44 ? 124 ASN A CB  1 
ATOM   984  C  CG  . ASN A 1 127 ? 4.049   -1.164  26.120 1.00 25.48 ? 124 ASN A CG  1 
ATOM   985  O  OD1 . ASN A 1 127 ? 3.389   -0.176  26.414 1.00 24.46 ? 124 ASN A OD1 1 
ATOM   986  N  ND2 . ASN A 1 127 ? 3.653   -2.394  26.383 1.00 30.11 ? 124 ASN A ND2 1 
ATOM   987  N  N   . VAL A 1 128 ? 4.287   2.213   24.170 1.00 17.04 ? 125 VAL A N   1 
ATOM   988  C  CA  . VAL A 1 128 ? 3.207   2.810   23.411 1.00 16.26 ? 125 VAL A CA  1 
ATOM   989  C  C   . VAL A 1 128 ? 3.818   3.648   22.277 1.00 16.28 ? 125 VAL A C   1 
ATOM   990  O  O   . VAL A 1 128 ? 4.421   4.710   22.508 1.00 18.24 ? 125 VAL A O   1 
ATOM   991  C  CB  . VAL A 1 128 ? 2.267   3.648   24.293 1.00 18.79 ? 125 VAL A CB  1 
ATOM   992  C  CG1 . VAL A 1 128 ? 1.221   4.320   23.436 1.00 18.59 ? 125 VAL A CG1 1 
ATOM   993  C  CG2 . VAL A 1 128 ? 1.612   2.798   25.377 1.00 19.54 ? 125 VAL A CG2 1 
ATOM   994  N  N   . PHE A 1 129 ? 3.660   3.156   21.039 1.00 16.10 ? 126 PHE A N   1 
ATOM   995  C  CA  . PHE A 1 129 ? 4.108   3.834   19.844 1.00 14.65 ? 126 PHE A CA  1 
ATOM   996  C  C   . PHE A 1 129 ? 3.591   3.028   18.652 1.00 13.73 ? 126 PHE A C   1 
ATOM   997  O  O   . PHE A 1 129 ? 3.366   1.826   18.736 1.00 14.24 ? 126 PHE A O   1 
ATOM   998  C  CB  . PHE A 1 129 ? 5.625   3.987   19.753 1.00 14.98 ? 126 PHE A CB  1 
ATOM   999  C  CG  . PHE A 1 129 ? 6.444   2.752   19.989 1.00 15.02 ? 126 PHE A CG  1 
ATOM   1000 C  CD1 . PHE A 1 129 ? 6.680   1.847   18.967 1.00 14.85 ? 126 PHE A CD1 1 
ATOM   1001 C  CD2 . PHE A 1 129 ? 6.899   2.431   21.256 1.00 15.96 ? 126 PHE A CD2 1 
ATOM   1002 C  CE1 . PHE A 1 129 ? 7.419   0.700   19.169 1.00 16.52 ? 126 PHE A CE1 1 
ATOM   1003 C  CE2 . PHE A 1 129 ? 7.654   1.297   21.462 1.00 17.42 ? 126 PHE A CE2 1 
ATOM   1004 C  CZ  . PHE A 1 129 ? 7.893   0.425   20.435 1.00 17.03 ? 126 PHE A CZ  1 
ATOM   1005 N  N   . ASP A 1 130 ? 3.385   3.739   17.559 1.00 13.86 ? 127 ASP A N   1 
ATOM   1006 C  CA  . ASP A 1 130 ? 2.816   3.148   16.363 1.00 13.51 ? 127 ASP A CA  1 
ATOM   1007 C  C   . ASP A 1 130 ? 3.807   2.190   15.734 1.00 13.85 ? 127 ASP A C   1 
ATOM   1008 O  O   . ASP A 1 130 ? 5.023   2.458   15.672 1.00 14.12 ? 127 ASP A O   1 
ATOM   1009 C  CB  . ASP A 1 130 ? 2.486   4.227   15.344 1.00 15.44 ? 127 ASP A CB  1 
ATOM   1010 C  CG  . ASP A 1 130 ? 1.356   5.156   15.788 1.00 16.04 ? 127 ASP A CG  1 
ATOM   1011 O  OD1 . ASP A 1 130 ? 0.709   4.869   16.786 1.00 18.38 ? 127 ASP A OD1 1 
ATOM   1012 O  OD2 . ASP A 1 130 ? 1.207   6.206   15.135 1.00 20.67 ? 127 ASP A OD2 1 
ATOM   1013 N  N   . ARG A 1 131 ? 3.279   1.091   15.211 1.00 13.46 ? 128 ARG A N   1 
ATOM   1014 C  CA  . ARG A 1 131 ? 4.142   0.133   14.553 1.00 14.19 ? 128 ARG A CA  1 
ATOM   1015 C  C   . ARG A 1 131 ? 3.420   -0.562  13.417 1.00 12.80 ? 128 ARG A C   1 
ATOM   1016 O  O   . ARG A 1 131 ? 2.194   -0.742  13.445 1.00 14.11 ? 128 ARG A O   1 
ATOM   1017 C  CB  . ARG A 1 131 ? 4.710   -0.882  15.504 1.00 16.33 ? 128 ARG A CB  1 
ATOM   1018 C  CG  . ARG A 1 131 ? 3.606   -1.726  16.064 1.00 16.22 ? 128 ARG A CG  1 
ATOM   1019 C  CD  . ARG A 1 131 ? 3.870   -2.267  17.458 1.00 19.05 ? 128 ARG A CD  1 
ATOM   1020 N  NE  . ARG A 1 131 ? 3.856   -1.166  18.391 1.00 18.94 ? 128 ARG A NE  1 
ATOM   1021 C  CZ  . ARG A 1 131 ? 4.277   -1.277  19.652 1.00 20.16 ? 128 ARG A CZ  1 
ATOM   1022 N  NH1 . ARG A 1 131 ? 4.190   -0.273  20.494 1.00 17.53 ? 128 ARG A NH1 1 
ATOM   1023 N  NH2 . ARG A 1 131 ? 4.785   -2.421  20.027 1.00 20.68 ? 128 ARG A NH2 1 
ATOM   1024 N  N   . ILE A 1 132 ? 4.240   -0.947  12.439 1.00 11.88 ? 129 ILE A N   1 
ATOM   1025 C  CA  . ILE A 1 132 ? 3.800   -1.777  11.335 1.00 11.48 ? 129 ILE A CA  1 
ATOM   1026 C  C   . ILE A 1 132 ? 4.558   -3.084  11.455 1.00 11.53 ? 129 ILE A C   1 
ATOM   1027 O  O   . ILE A 1 132 ? 5.773   -3.112  11.285 1.00 12.27 ? 129 ILE A O   1 
ATOM   1028 C  CB  . ILE A 1 132 ? 4.017   -1.131  9.974  1.00 13.48 ? 129 ILE A CB  1 
ATOM   1029 C  CG1 . ILE A 1 132 ? 3.285   0.210   9.880  1.00 14.51 ? 129 ILE A CG1 1 
ATOM   1030 C  CG2 . ILE A 1 132 ? 3.627   -2.100  8.862  1.00 13.29 ? 129 ILE A CG2 1 
ATOM   1031 C  CD1 . ILE A 1 132 ? 3.617   1.022   8.622  1.00 16.48 ? 129 ILE A CD1 1 
ATOM   1032 N  N   . LYS A 1 133 ? 3.828   -4.125  11.824 1.00 12.61 ? 130 LYS A N   1 
ATOM   1033 C  CA  . LYS A 1 133 ? 4.370   -5.458  11.952 1.00 12.47 ? 130 LYS A CA  1 
ATOM   1034 C  C   . LYS A 1 133 ? 4.266   -6.142  10.608 1.00 12.67 ? 130 LYS A C   1 
ATOM   1035 O  O   . LYS A 1 133 ? 3.166   -6.298  10.078 1.00 13.47 ? 130 LYS A O   1 
ATOM   1036 C  CB  . LYS A 1 133 ? 3.510   -6.243  12.946 1.00 13.88 ? 130 LYS A CB  1 
ATOM   1037 C  CG  . LYS A 1 133 ? 3.293   -5.590  14.301 1.00 16.70 ? 130 LYS A CG  1 
ATOM   1038 C  CD  . LYS A 1 133 ? 2.420   -6.518  15.131 1.00 21.06 ? 130 LYS A CD  1 
ATOM   1039 C  CE  . LYS A 1 133 ? 1.953   -5.950  16.430 1.00 25.78 ? 130 LYS A CE  1 
ATOM   1040 N  NZ  . LYS A 1 133 ? 1.207   -7.034  17.089 1.00 23.61 ? 130 LYS A NZ  1 
ATOM   1041 N  N   . VAL A 1 134 ? 5.391   -6.528  10.047 1.00 12.22 ? 131 VAL A N   1 
ATOM   1042 C  CA  . VAL A 1 134 ? 5.420   -7.151  8.729  1.00 11.73 ? 131 VAL A CA  1 
ATOM   1043 C  C   . VAL A 1 134 ? 5.633   -8.639  8.952  1.00 11.81 ? 131 VAL A C   1 
ATOM   1044 O  O   . VAL A 1 134 ? 6.639   -9.047  9.493  1.00 12.50 ? 131 VAL A O   1 
ATOM   1045 C  CB  . VAL A 1 134 ? 6.496   -6.556  7.815  1.00 12.51 ? 131 VAL A CB  1 
ATOM   1046 C  CG1 . VAL A 1 134 ? 6.363   -7.156  6.427  1.00 13.17 ? 131 VAL A CG1 1 
ATOM   1047 C  CG2 . VAL A 1 134 ? 6.425   -5.033  7.749  1.00 13.42 ? 131 VAL A CG2 1 
ATOM   1048 N  N   . GLY A 1 135 ? 4.666   -9.455  8.556  1.00 12.35 ? 132 GLY A N   1 
ATOM   1049 C  CA  . GLY A 1 135 ? 4.781   -10.868 8.815  1.00 12.62 ? 132 GLY A CA  1 
ATOM   1050 C  C   . GLY A 1 135 ? 5.957   -11.514 8.099  1.00 11.75 ? 132 GLY A C   1 
ATOM   1051 O  O   . GLY A 1 135 ? 6.192   -11.284 6.916  1.00 12.34 ? 132 GLY A O   1 
ATOM   1052 N  N   . ILE A 1 136 ? 6.670   -12.366 8.842  1.00 11.07 ? 133 ILE A N   1 
ATOM   1053 C  CA  . ILE A 1 136 ? 7.774   -13.103 8.246  1.00 11.64 ? 133 ILE A CA  1 
ATOM   1054 C  C   . ILE A 1 136 ? 7.581   -14.602 8.386  1.00 12.72 ? 133 ILE A C   1 
ATOM   1055 O  O   . ILE A 1 136 ? 8.493   -15.356 8.075  1.00 12.56 ? 133 ILE A O   1 
ATOM   1056 C  CB  . ILE A 1 136 ? 9.126   -12.652 8.815  1.00 12.19 ? 133 ILE A CB  1 
ATOM   1057 C  CG1 . ILE A 1 136 ? 9.291   -12.923 10.312 1.00 11.95 ? 133 ILE A CG1 1 
ATOM   1058 C  CG2 . ILE A 1 136 ? 9.353   -11.170 8.482  1.00 13.04 ? 133 ILE A CG2 1 
ATOM   1059 C  CD1 . ILE A 1 136 ? 10.703  -13.036 10.735 1.00 12.41 ? 133 ILE A CD1 1 
ATOM   1060 N  N   . GLY A 1 137 ? 6.406   -15.030 8.830  1.00 13.05 ? 134 GLY A N   1 
ATOM   1061 C  CA  . GLY A 1 137 ? 6.089   -16.428 8.931  1.00 13.66 ? 134 GLY A CA  1 
ATOM   1062 C  C   . GLY A 1 137 ? 6.466   -16.985 10.287 1.00 13.58 ? 134 GLY A C   1 
ATOM   1063 O  O   . GLY A 1 137 ? 7.463   -16.609 10.894 1.00 14.88 ? 134 GLY A O   1 
ATOM   1064 N  N   . ARG A 1 138 ? 5.616   -17.874 10.774 1.00 14.21 ? 135 ARG A N   1 
ATOM   1065 C  CA  . ARG A 1 138 ? 5.815   -18.481 12.065 1.00 15.50 ? 135 ARG A CA  1 
ATOM   1066 C  C   . ARG A 1 138 ? 6.883   -19.545 11.926 1.00 15.90 ? 135 ARG A C   1 
ATOM   1067 O  O   . ARG A 1 138 ? 6.899   -20.303 10.955 1.00 18.78 ? 135 ARG A O   1 
ATOM   1068 C  CB  . ARG A 1 138 ? 4.492   -19.102 12.508 1.00 15.77 ? 135 ARG A CB  1 
ATOM   1069 C  CG  . ARG A 1 138 ? 3.442   -18.053 12.870 1.00 16.57 ? 135 ARG A CG  1 
ATOM   1070 C  CD  . ARG A 1 138 ? 2.072   -18.674 12.882 1.00 16.50 ? 135 ARG A CD  1 
ATOM   1071 N  NE  . ARG A 1 138 ? 1.005   -17.789 13.321 1.00 17.68 ? 135 ARG A NE  1 
ATOM   1072 C  CZ  . ARG A 1 138 ? 0.385   -16.905 12.558 1.00 18.22 ? 135 ARG A CZ  1 
ATOM   1073 N  NH1 . ARG A 1 138 ? 0.797   -16.670 11.326 1.00 17.39 ? 135 ARG A NH1 1 
ATOM   1074 N  NH2 . ARG A 1 138 ? -0.683  -16.282 13.026 1.00 19.97 ? 135 ARG A NH2 1 
ATOM   1075 N  N   . PRO A 1 139 ? 7.744   -19.715 12.951 1.00 16.82 ? 136 PRO A N   1 
ATOM   1076 C  CA  . PRO A 1 139 ? 8.765   -20.740 12.931 1.00 18.53 ? 136 PRO A CA  1 
ATOM   1077 C  C   . PRO A 1 139 ? 8.205   -22.044 13.465 1.00 16.73 ? 136 PRO A C   1 
ATOM   1078 O  O   . PRO A 1 139 ? 7.143   -22.064 14.090 1.00 18.78 ? 136 PRO A O   1 
ATOM   1079 C  CB  . PRO A 1 139 ? 9.784   -20.156 13.905 1.00 19.65 ? 136 PRO A CB  1 
ATOM   1080 C  CG  . PRO A 1 139 ? 8.936   -19.494 14.953 1.00 21.53 ? 136 PRO A CG  1 
ATOM   1081 C  CD  . PRO A 1 139 ? 7.750   -18.922 14.185 1.00 18.51 ? 136 PRO A CD  1 
ATOM   1082 N  N   . GLU A 1 140 ? 8.950   -23.135 13.264 1.00 18.63 ? 137 GLU A N   1 
ATOM   1083 C  CA  . GLU A 1 140 ? 8.538   -24.416 13.814 1.00 18.56 ? 137 GLU A CA  1 
ATOM   1084 C  C   . GLU A 1 140 ? 8.554   -24.435 15.348 1.00 17.42 ? 137 GLU A C   1 
ATOM   1085 O  O   . GLU A 1 140 ? 7.703   -25.074 15.988 1.00 19.66 ? 137 GLU A O   1 
ATOM   1086 C  CB  . GLU A 1 140 ? 9.425   -25.507 13.237 1.00 22.57 ? 137 GLU A CB  1 
ATOM   1087 C  CG  . GLU A 1 140 ? 8.897   -26.911 13.462 1.00 27.18 ? 137 GLU A CG  1 
ATOM   1088 C  CD  . GLU A 1 140 ? 9.272   -27.542 14.789 1.00 27.84 ? 137 GLU A CD  1 
ATOM   1089 O  OE1 . GLU A 1 140 ? 8.625   -28.558 15.183 1.00 32.65 ? 137 GLU A OE1 1 
ATOM   1090 O  OE2 . GLU A 1 140 ? 10.212  -27.045 15.403 1.00 30.17 ? 137 GLU A OE2 1 
ATOM   1091 N  N   . GLY A 1 141 ? 9.488   -23.722 15.967 1.00 19.05 ? 138 GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 141 ? 9.603   -23.693 17.399 1.00 19.47 ? 138 GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 141 ? 10.771  -22.803 17.785 1.00 19.42 ? 138 GLY A C   1 
ATOM   1094 O  O   . GLY A 1 141 ? 11.447  -22.266 16.917 1.00 19.24 ? 138 GLY A O   1 
ATOM   1095 N  N   . LYS A 1 142 ? 11.012  -22.675 19.084 1.00 22.11 ? 139 LYS A N   1 
ATOM   1096 C  CA  . LYS A 1 142 ? 12.006  -21.729 19.558 1.00 22.75 ? 139 LYS A CA  1 
ATOM   1097 C  C   . LYS A 1 142 ? 13.377  -22.122 19.007 1.00 24.71 ? 139 LYS A C   1 
ATOM   1098 O  O   . LYS A 1 142 ? 14.184  -21.249 18.728 1.00 23.63 ? 139 LYS A O   1 
ATOM   1099 C  CB  . LYS A 1 142 ? 11.982  -21.675 21.090 1.00 26.33 ? 139 LYS A CB  1 
ATOM   1100 C  CG  . LYS A 1 142 ? 12.865  -20.592 21.698 1.00 28.58 ? 139 LYS A CG  1 
ATOM   1101 C  CD  . LYS A 1 142 ? 12.474  -20.147 23.096 1.00 30.66 ? 139 LYS A CD  1 
ATOM   1102 C  CE  . LYS A 1 142 ? 13.442  -19.138 23.686 1.00 33.22 ? 139 LYS A CE  1 
ATOM   1103 N  N   . LYS A 1 143 ? 13.590  -23.421 18.753 1.00 22.81 ? 140 LYS A N   1 
ATOM   1104 C  CA  . LYS A 1 143 ? 14.876  -23.948 18.297 1.00 22.76 ? 140 LYS A CA  1 
ATOM   1105 C  C   . LYS A 1 143 ? 15.299  -23.352 16.957 1.00 21.92 ? 140 LYS A C   1 
ATOM   1106 O  O   . LYS A 1 143 ? 16.482  -23.284 16.663 1.00 23.34 ? 140 LYS A O   1 
ATOM   1107 C  CB  . LYS A 1 143 ? 14.788  -25.471 18.121 1.00 23.05 ? 140 LYS A CB  1 
ATOM   1108 N  N   . THR A 1 144 ? 14.318  -22.970 16.119 1.00 19.35 ? 141 THR A N   1 
ATOM   1109 C  CA  . THR A 1 144 ? 14.582  -22.543 14.747 1.00 19.42 ? 141 THR A CA  1 
ATOM   1110 C  C   . THR A 1 144 ? 14.391  -21.040 14.571 1.00 17.43 ? 141 THR A C   1 
ATOM   1111 O  O   . THR A 1 144 ? 14.589  -20.556 13.465 1.00 18.15 ? 141 THR A O   1 
ATOM   1112 C  CB  . THR A 1 144 ? 13.734  -23.302 13.708 1.00 21.50 ? 141 THR A CB  1 
ATOM   1113 O  OG1 . THR A 1 144 ? 12.326  -23.177 13.958 1.00 22.96 ? 141 THR A OG1 1 
ATOM   1114 C  CG2 . THR A 1 144 ? 14.070  -24.773 13.687 1.00 27.17 ? 141 THR A CG2 1 
ATOM   1115 N  N   . VAL A 1 145 ? 14.056  -20.318 15.647 1.00 16.63 ? 142 VAL A N   1 
ATOM   1116 C  CA  . VAL A 1 145 ? 13.768  -18.900 15.492 1.00 17.82 ? 142 VAL A CA  1 
ATOM   1117 C  C   . VAL A 1 145 ? 14.938  -18.152 14.851 1.00 16.54 ? 142 VAL A C   1 
ATOM   1118 O  O   . VAL A 1 145 ? 14.759  -17.362 13.915 1.00 17.13 ? 142 VAL A O   1 
ATOM   1119 C  CB  . VAL A 1 145 ? 13.377  -18.250 16.827 1.00 19.95 ? 142 VAL A CB  1 
ATOM   1120 C  CG1 . VAL A 1 145 ? 13.586  -16.735 16.800 1.00 20.90 ? 142 VAL A CG1 1 
ATOM   1121 C  CG2 . VAL A 1 145 ? 11.954  -18.584 17.228 1.00 21.13 ? 142 VAL A CG2 1 
ATOM   1122 N  N   . VAL A 1 146 ? 16.134  -18.293 15.430 1.00 16.65 ? 143 VAL A N   1 
ATOM   1123 C  CA  . VAL A 1 146 ? 17.220  -17.431 15.000 1.00 16.06 ? 143 VAL A CA  1 
ATOM   1124 C  C   . VAL A 1 146 ? 17.562  -17.719 13.546 1.00 16.78 ? 143 VAL A C   1 
ATOM   1125 O  O   . VAL A 1 146 ? 17.743  -16.800 12.751 1.00 17.50 ? 143 VAL A O   1 
ATOM   1126 C  CB  . VAL A 1 146 ? 18.443  -17.578 15.902 1.00 17.45 ? 143 VAL A CB  1 
ATOM   1127 C  CG1 . VAL A 1 146 ? 19.648  -16.849 15.310 1.00 19.29 ? 143 VAL A CG1 1 
ATOM   1128 C  CG2 . VAL A 1 146 ? 18.099  -17.082 17.288 1.00 19.71 ? 143 VAL A CG2 1 
ATOM   1129 N  N   . GLN A 1 147 ? 17.639  -18.998 13.170 1.00 17.61 ? 144 GLN A N   1 
ATOM   1130 C  CA  . GLN A 1 147 ? 17.917  -19.309 11.778 1.00 19.22 ? 144 GLN A CA  1 
ATOM   1131 C  C   . GLN A 1 147 ? 16.804  -18.794 10.873 1.00 17.31 ? 144 GLN A C   1 
ATOM   1132 O  O   . GLN A 1 147 ? 17.073  -18.386 9.749  1.00 17.74 ? 144 GLN A O   1 
ATOM   1133 C  CB  . GLN A 1 147 ? 18.139  -20.805 11.575 1.00 20.66 ? 144 GLN A CB  1 
ATOM   1134 C  CG  . GLN A 1 147 ? 19.535  -21.239 11.970 1.00 26.12 ? 144 GLN A CG  1 
ATOM   1135 C  CD  . GLN A 1 147 ? 20.637  -20.307 11.495 1.00 29.01 ? 144 GLN A CD  1 
ATOM   1136 O  OE1 . GLN A 1 147 ? 21.387  -19.724 12.287 1.00 31.93 ? 144 GLN A OE1 1 
ATOM   1137 N  NE2 . GLN A 1 147 ? 20.752  -20.146 10.189 1.00 31.01 ? 144 GLN A NE2 1 
ATOM   1138 N  N   . HIS A 1 148 ? 15.555  -18.826 11.361 1.00 15.82 ? 145 HIS A N   1 
ATOM   1139 C  CA  . HIS A 1 148 ? 14.430  -18.339 10.587 1.00 14.75 ? 145 HIS A CA  1 
ATOM   1140 C  C   . HIS A 1 148 ? 14.615  -16.863 10.259 1.00 14.02 ? 145 HIS A C   1 
ATOM   1141 O  O   . HIS A 1 148 ? 14.382  -16.432 9.135  1.00 15.51 ? 145 HIS A O   1 
ATOM   1142 C  CB  . HIS A 1 148 ? 13.143  -18.602 11.340 1.00 15.73 ? 145 HIS A CB  1 
ATOM   1143 C  CG  . HIS A 1 148 ? 11.919  -18.223 10.594 1.00 17.14 ? 145 HIS A CG  1 
ATOM   1144 N  ND1 . HIS A 1 148 ? 11.387  -18.995 9.595  1.00 21.10 ? 145 HIS A ND1 1 
ATOM   1145 C  CD2 . HIS A 1 148 ? 11.122  -17.201 10.735 1.00 18.16 ? 145 HIS A CD2 1 
ATOM   1146 C  CE1 . HIS A 1 148 ? 10.290  -18.409 9.144  1.00 19.66 ? 145 HIS A CE1 1 
ATOM   1147 N  NE2 . HIS A 1 148 ? 10.129  -17.301 9.803  1.00 18.13 ? 145 HIS A NE2 1 
ATOM   1148 N  N   . VAL A 1 149 ? 14.971  -16.066 11.270 1.00 13.24 ? 146 VAL A N   1 
ATOM   1149 C  CA  . VAL A 1 149 ? 15.014  -14.622 11.064 1.00 13.35 ? 146 VAL A CA  1 
ATOM   1150 C  C   . VAL A 1 149 ? 16.318  -14.198 10.403 1.00 12.91 ? 146 VAL A C   1 
ATOM   1151 O  O   . VAL A 1 149 ? 16.336  -13.196 9.693  1.00 13.46 ? 146 VAL A O   1 
ATOM   1152 C  CB  . VAL A 1 149 ? 14.734  -13.802 12.332 1.00 13.75 ? 146 VAL A CB  1 
ATOM   1153 C  CG1 . VAL A 1 149 ? 13.468  -14.282 12.993 1.00 14.94 ? 146 VAL A CG1 1 
ATOM   1154 C  CG2 . VAL A 1 149 ? 15.924  -13.796 13.284 1.00 14.86 ? 146 VAL A CG2 1 
ATOM   1155 N  N   . LEU A 1 150 ? 17.386  -14.974 10.555 1.00 14.01 ? 147 LEU A N   1 
ATOM   1156 C  CA  . LEU A 1 150 ? 18.680  -14.593 10.015 1.00 14.25 ? 147 LEU A CA  1 
ATOM   1157 C  C   . LEU A 1 150 ? 18.971  -15.329 8.713  1.00 15.58 ? 147 LEU A C   1 
ATOM   1158 O  O   . LEU A 1 150 ? 20.126  -15.572 8.367  1.00 21.55 ? 147 LEU A O   1 
ATOM   1159 C  CB  . LEU A 1 150 ? 19.792  -14.833 11.047 1.00 15.07 ? 147 LEU A CB  1 
ATOM   1160 C  CG  . LEU A 1 150 ? 19.710  -14.018 12.328 1.00 15.24 ? 147 LEU A CG  1 
ATOM   1161 C  CD1 . LEU A 1 150 ? 20.952  -14.207 13.153 1.00 16.18 ? 147 LEU A CD1 1 
ATOM   1162 C  CD2 . LEU A 1 150 ? 19.463  -12.539 12.019 1.00 15.41 ? 147 LEU A CD2 1 
ATOM   1163 N  N   . SER A 1 151 ? 17.931  -15.638 7.965  1.00 16.11 ? 148 SER A N   1 
ATOM   1164 C  CA  . SER A 1 151 ? 18.014  -16.219 6.633  1.00 16.52 ? 148 SER A CA  1 
ATOM   1165 C  C   . SER A 1 151 ? 17.123  -15.402 5.708  1.00 14.50 ? 148 SER A C   1 
ATOM   1166 O  O   . SER A 1 151 ? 16.241  -14.700 6.174  1.00 13.99 ? 148 SER A O   1 
ATOM   1167 C  CB  . SER A 1 151 ? 17.628  -17.672 6.625  1.00 17.83 ? 148 SER A CB  1 
ATOM   1168 O  OG  . SER A 1 151 ? 16.317  -17.880 7.120  1.00 18.16 ? 148 SER A OG  1 
ATOM   1169 N  N   . PRO A 1 152 ? 17.357  -15.441 4.374  1.00 14.97 ? 149 PRO A N   1 
ATOM   1170 C  CA  . PRO A 1 152 ? 16.483  -14.761 3.433  1.00 15.59 ? 149 PRO A CA  1 
ATOM   1171 C  C   . PRO A 1 152 ? 15.090  -15.350 3.352  1.00 14.87 ? 149 PRO A C   1 
ATOM   1172 O  O   . PRO A 1 152 ? 14.813  -16.406 3.880  1.00 15.64 ? 149 PRO A O   1 
ATOM   1173 C  CB  . PRO A 1 152 ? 17.209  -14.872 2.089  1.00 17.17 ? 149 PRO A CB  1 
ATOM   1174 C  CG  . PRO A 1 152 ? 18.038  -16.097 2.247  1.00 20.63 ? 149 PRO A CG  1 
ATOM   1175 C  CD  . PRO A 1 152 ? 18.443  -16.145 3.700  1.00 18.04 ? 149 PRO A CD  1 
ATOM   1176 N  N   . PHE A 1 153 ? 14.207  -14.578 2.741  1.00 14.64 ? 150 PHE A N   1 
ATOM   1177 C  CA  . PHE A 1 153 ? 12.916  -15.127 2.360  1.00 15.56 ? 150 PHE A CA  1 
ATOM   1178 C  C   . PHE A 1 153 ? 13.172  -16.181 1.293  1.00 16.77 ? 150 PHE A C   1 
ATOM   1179 O  O   . PHE A 1 153 ? 14.085  -16.076 0.499  1.00 16.95 ? 150 PHE A O   1 
ATOM   1180 C  CB  . PHE A 1 153 ? 11.950  -14.043 1.856  1.00 16.13 ? 150 PHE A CB  1 
ATOM   1181 C  CG  . PHE A 1 153 ? 11.585  -13.057 2.939  1.00 14.88 ? 150 PHE A CG  1 
ATOM   1182 C  CD1 . PHE A 1 153 ? 10.579  -13.348 3.859  1.00 16.06 ? 150 PHE A CD1 1 
ATOM   1183 C  CD2 . PHE A 1 153 ? 12.286  -11.870 3.074  1.00 14.97 ? 150 PHE A CD2 1 
ATOM   1184 C  CE1 . PHE A 1 153 ? 10.292  -12.466 4.885  1.00 14.94 ? 150 PHE A CE1 1 
ATOM   1185 C  CE2 . PHE A 1 153 ? 11.970  -10.981 4.085  1.00 14.17 ? 150 PHE A CE2 1 
ATOM   1186 C  CZ  . PHE A 1 153 ? 10.978  -11.281 4.990  1.00 14.42 ? 150 PHE A CZ  1 
ATOM   1187 N  N   . SER A 1 154 ? 12.340  -17.219 1.289  1.00 16.44 ? 151 SER A N   1 
ATOM   1188 C  CA  . SER A 1 154 ? 12.440  -18.232 0.253  1.00 16.92 ? 151 SER A CA  1 
ATOM   1189 C  C   . SER A 1 154 ? 12.141  -17.644 -1.118 1.00 17.44 ? 151 SER A C   1 
ATOM   1190 O  O   . SER A 1 154 ? 11.437  -16.661 -1.245 1.00 16.47 ? 151 SER A O   1 
ATOM   1191 C  CB  . SER A 1 154 ? 11.521  -19.373 0.532  1.00 16.92 ? 151 SER A CB  1 
ATOM   1192 O  OG  . SER A 1 154 ? 10.168  -19.016 0.317  1.00 17.01 ? 151 SER A OG  1 
ATOM   1193 N  N   . LYS A 1 155 ? 12.674  -18.291 -2.153 1.00 18.42 ? 152 LYS A N   1 
ATOM   1194 C  CA  . LYS A 1 155 ? 12.386  -17.884 -3.511 1.00 19.14 ? 152 LYS A CA  1 
ATOM   1195 C  C   . LYS A 1 155 ? 10.879  -17.889 -3.739 1.00 17.81 ? 152 LYS A C   1 
ATOM   1196 O  O   . LYS A 1 155 ? 10.307  -16.998 -4.352 1.00 19.04 ? 152 LYS A O   1 
ATOM   1197 C  CB  . LYS A 1 155 ? 13.085  -18.820 -4.513 1.00 21.58 ? 152 LYS A CB  1 
ATOM   1198 C  CG  . LYS A 1 155 ? 14.607  -18.873 -4.440 1.00 25.24 ? 152 LYS A CG  1 
ATOM   1199 C  CD  . LYS A 1 155 ? 15.253  -17.514 -4.538 1.00 29.46 ? 152 LYS A CD  1 
ATOM   1200 N  N   . GLU A 1 156 ? 10.236  -18.931 -3.240 1.00 16.31 ? 153 GLU A N   1 
ATOM   1201 C  CA  . GLU A 1 156 ? 8.808   -19.102 -3.441 1.00 17.53 ? 153 GLU A CA  1 
ATOM   1202 C  C   . GLU A 1 156 ? 8.012   -17.949 -2.814 1.00 17.31 ? 153 GLU A C   1 
ATOM   1203 O  O   . GLU A 1 156 ? 6.970   -17.573 -3.341 1.00 17.28 ? 153 GLU A O   1 
ATOM   1204 C  CB  . GLU A 1 156 ? 8.360   -20.440 -2.869 1.00 21.30 ? 153 GLU A CB  1 
ATOM   1205 C  CG  . GLU A 1 156 ? 8.747   -21.624 -3.750 1.00 27.35 ? 153 GLU A CG  1 
ATOM   1206 C  CD  . GLU A 1 156 ? 7.871   -22.852 -3.573 1.00 34.60 ? 153 GLU A CD  1 
ATOM   1207 O  OE1 . GLU A 1 156 ? 6.888   -22.764 -2.803 1.00 43.80 ? 153 GLU A OE1 1 
ATOM   1208 N  N   . ASN A 1 157 ? 8.491   -17.441 -1.662 1.00 16.70 ? 154 ASN A N   1 
ATOM   1209 C  CA  . ASN A 1 157 ? 7.789   -16.436 -0.882 1.00 17.00 ? 154 ASN A CA  1 
ATOM   1210 C  C   . ASN A 1 157 ? 8.161   -15.023 -1.298 1.00 16.49 ? 154 ASN A C   1 
ATOM   1211 O  O   . ASN A 1 157 ? 7.540   -14.078 -0.817 1.00 16.84 ? 154 ASN A O   1 
ATOM   1212 C  CB  . ASN A 1 157 ? 7.979   -16.634 0.616  1.00 16.99 ? 154 ASN A CB  1 
ATOM   1213 C  CG  . ASN A 1 157 ? 7.082   -17.734 1.149  1.00 18.34 ? 154 ASN A CG  1 
ATOM   1214 O  OD1 . ASN A 1 157 ? 6.065   -18.086 0.545  1.00 21.64 ? 154 ASN A OD1 1 
ATOM   1215 N  ND2 . ASN A 1 157 ? 7.423   -18.285 2.291  1.00 19.32 ? 154 ASN A ND2 1 
ATOM   1216 N  N   . GLN A 1 158 ? 9.187   -14.869 -2.125 1.00 17.19 ? 155 GLN A N   1 
ATOM   1217 C  CA  . GLN A 1 158 ? 9.643   -13.524 -2.427 1.00 18.06 ? 155 GLN A CA  1 
ATOM   1218 C  C   . GLN A 1 158 ? 8.532   -12.649 -3.010 1.00 18.95 ? 155 GLN A C   1 
ATOM   1219 O  O   . GLN A 1 158 ? 8.400   -11.472 -2.618 1.00 17.17 ? 155 GLN A O   1 
ATOM   1220 C  CB  . GLN A 1 158 ? 10.878  -13.539 -3.317 1.00 20.74 ? 155 GLN A CB  1 
ATOM   1221 C  CG  . GLN A 1 158 ? 11.399  -12.160 -3.639 1.00 24.38 ? 155 GLN A CG  1 
ATOM   1222 C  CD  . GLN A 1 158 ? 11.813  -11.406 -2.404 1.00 27.83 ? 155 GLN A CD  1 
ATOM   1223 O  OE1 . GLN A 1 158 ? 11.611  -10.192 -2.265 1.00 35.83 ? 155 GLN A OE1 1 
ATOM   1224 N  NE2 . GLN A 1 158 ? 12.431  -12.135 -1.500 1.00 24.63 ? 155 GLN A NE2 1 
ATOM   1225 N  N   . PRO A 1 159 ? 7.643   -13.134 -3.917 1.00 18.52 ? 156 PRO A N   1 
ATOM   1226 C  CA  . PRO A 1 159 ? 6.603   -12.246 -4.442 1.00 19.37 ? 156 PRO A CA  1 
ATOM   1227 C  C   . PRO A 1 159 ? 5.638   -11.797 -3.360 1.00 17.57 ? 156 PRO A C   1 
ATOM   1228 O  O   . PRO A 1 159 ? 5.089   -10.700 -3.426 1.00 19.80 ? 156 PRO A O   1 
ATOM   1229 C  CB  . PRO A 1 159 ? 5.871   -13.062 -5.515 1.00 21.11 ? 156 PRO A CB  1 
ATOM   1230 C  CG  . PRO A 1 159 ? 6.909   -14.042 -5.923 1.00 21.20 ? 156 PRO A CG  1 
ATOM   1231 C  CD  . PRO A 1 159 ? 7.662   -14.410 -4.653 1.00 20.48 ? 156 PRO A CD  1 
ATOM   1232 N  N   . LEU A 1 160 ? 5.396   -12.667 -2.397 1.00 17.21 ? 157 LEU A N   1 
ATOM   1233 C  CA  . LEU A 1 160 ? 4.429   -12.367 -1.367 1.00 18.60 ? 157 LEU A CA  1 
ATOM   1234 C  C   . LEU A 1 160 ? 4.997   -11.353 -0.368 1.00 16.36 ? 157 LEU A C   1 
ATOM   1235 O  O   . LEU A 1 160 ? 4.276   -10.448 0.028  1.00 17.53 ? 157 LEU A O   1 
ATOM   1236 C  CB  . LEU A 1 160 ? 4.029   -13.692 -0.722 1.00 21.20 ? 157 LEU A CB  1 
ATOM   1237 C  CG  . LEU A 1 160 ? 2.823   -13.648 0.203  1.00 23.38 ? 157 LEU A CG  1 
ATOM   1238 C  CD1 . LEU A 1 160 ? 1.649   -12.952 -0.463 1.00 25.41 ? 157 LEU A CD1 1 
ATOM   1239 C  CD2 . LEU A 1 160 ? 2.464   -15.049 0.669  1.00 26.20 ? 157 LEU A CD2 1 
ATOM   1240 N  N   . ILE A 1 161 ? 6.299   -11.415 -0.041 1.00 14.89 ? 158 ILE A N   1 
ATOM   1241 C  CA  . ILE A 1 161 ? 6.877   -10.414 0.832  1.00 14.83 ? 158 ILE A CA  1 
ATOM   1242 C  C   . ILE A 1 161 ? 6.945   -9.090  0.067  1.00 14.12 ? 158 ILE A C   1 
ATOM   1243 O  O   . ILE A 1 161 ? 6.787   -8.030  0.675  1.00 15.04 ? 158 ILE A O   1 
ATOM   1244 C  CB  . ILE A 1 161 ? 8.234   -10.843 1.422  1.00 16.11 ? 158 ILE A CB  1 
ATOM   1245 C  CG1 . ILE A 1 161 ? 8.596   -9.960  2.614  1.00 17.50 ? 158 ILE A CG1 1 
ATOM   1246 C  CG2 . ILE A 1 161 ? 9.373   -10.863 0.402  1.00 17.17 ? 158 ILE A CG2 1 
ATOM   1247 C  CD1 . ILE A 1 161 ? 7.717   -10.179 3.810  1.00 18.93 ? 158 ILE A CD1 1 
ATOM   1248 N  N   . GLU A 1 162 ? 7.147   -9.117  -1.248 1.00 14.26 ? 159 GLU A N   1 
ATOM   1249 C  CA  . GLU A 1 162 ? 7.117   -7.883  -2.007 1.00 16.06 ? 159 GLU A CA  1 
ATOM   1250 C  C   . GLU A 1 162 ? 5.744   -7.221  -1.892 1.00 15.44 ? 159 GLU A C   1 
ATOM   1251 O  O   . GLU A 1 162 ? 5.652   -5.987  -1.768 1.00 16.92 ? 159 GLU A O   1 
ATOM   1252 C  CB  . GLU A 1 162 ? 7.502   -8.184  -3.454 1.00 19.25 ? 159 GLU A CB  1 
ATOM   1253 C  CG  . GLU A 1 162 ? 8.990   -8.475  -3.628 1.00 24.42 ? 159 GLU A CG  1 
ATOM   1254 C  CD  . GLU A 1 162 ? 9.448   -9.017  -4.980 1.00 31.40 ? 159 GLU A CD  1 
ATOM   1255 O  OE1 . GLU A 1 162 ? 8.586   -9.204  -5.880 1.00 38.23 ? 159 GLU A OE1 1 
ATOM   1256 O  OE2 . GLU A 1 162 ? 10.677  -9.277  -5.133 1.00 34.81 ? 159 GLU A OE2 1 
ATOM   1257 N  N   . GLU A 1 163 ? 4.673   -8.022  -1.898 1.00 15.35 ? 160 GLU A N   1 
ATOM   1258 C  CA  . GLU A 1 163 ? 3.323   -7.495  -1.718 1.00 17.04 ? 160 GLU A CA  1 
ATOM   1259 C  C   . GLU A 1 163 ? 3.147   -6.820  -0.359 1.00 15.38 ? 160 GLU A C   1 
ATOM   1260 O  O   . GLU A 1 163 ? 2.546   -5.736  -0.266 1.00 15.82 ? 160 GLU A O   1 
ATOM   1261 C  CB  . GLU A 1 163 ? 2.282   -8.602  -1.910 1.00 18.60 ? 160 GLU A CB  1 
ATOM   1262 C  CG  . GLU A 1 163 ? 0.846   -8.194  -1.621 1.00 23.67 ? 160 GLU A CG  1 
ATOM   1263 N  N   . SER A 1 164 ? 3.552   -7.474  0.724  1.00 14.71 ? 161 SER A N   1 
ATOM   1264 C  CA  . SER A 1 164 ? 3.392   -6.858  2.031  1.00 14.23 ? 161 SER A CA  1 
ATOM   1265 C  C   . SER A 1 164 ? 4.315   -5.643  2.176  1.00 13.26 ? 161 SER A C   1 
ATOM   1266 O  O   . SER A 1 164 ? 3.952   -4.719  2.888  1.00 13.97 ? 161 SER A O   1 
ATOM   1267 C  CB  . SER A 1 164 ? 3.547   -7.830  3.151  1.00 15.71 ? 161 SER A CB  1 
ATOM   1268 O  OG  . SER A 1 164 ? 4.797   -8.454  3.082  1.00 18.46 ? 161 SER A OG  1 
ATOM   1269 N  N   . MET A 1 165 ? 5.501   -5.627  1.559  1.00 14.09 ? 162 MET A N   1 
ATOM   1270 C  CA  . MET A 1 165 ? 6.301   -4.408  1.563  1.00 14.28 ? 162 MET A CA  1 
ATOM   1271 C  C   . MET A 1 165 ? 5.541   -3.269  0.884  1.00 15.14 ? 162 MET A C   1 
ATOM   1272 O  O   . MET A 1 165 ? 5.569   -2.136  1.355  1.00 14.85 ? 162 MET A O   1 
ATOM   1273 C  CB  . MET A 1 165 ? 7.641   -4.610  0.840  1.00 15.84 ? 162 MET A CB  1 
ATOM   1274 C  CG  . MET A 1 165 ? 8.602   -5.469  1.630  1.00 16.78 ? 162 MET A CG  1 
ATOM   1275 S  SD  . MET A 1 165 ? 10.231  -5.540  0.895  1.00 26.52 ? 162 MET A SD  1 
ATOM   1276 C  CE  . MET A 1 165 ? 9.919   -6.640  -0.463 1.00 28.68 ? 162 MET A CE  1 
ATOM   1277 N  N   . CYS A 1 166 ? 4.907   -3.564  -0.245 1.00 15.23 ? 163 CYS A N   1 
ATOM   1278 C  CA  . CYS A 1 166 ? 4.111   -2.549  -0.904 1.00 15.93 ? 163 CYS A CA  1 
ATOM   1279 C  C   . CYS A 1 166 ? 2.960   -2.046  -0.035 1.00 14.82 ? 163 CYS A C   1 
ATOM   1280 O  O   . CYS A 1 166 ? 2.728   -0.855  0.049  1.00 15.47 ? 163 CYS A O   1 
ATOM   1281 C  CB  . CYS A 1 166 ? 3.525   -3.130  -2.175 1.00 16.68 ? 163 CYS A CB  1 
ATOM   1282 S  SG  . CYS A 1 166 ? 4.752   -3.492  -3.434 1.00 32.23 ? 163 CYS A SG  1 
ATOM   1283 N  N   . GLN A 1 167 ? 2.256   -2.937  0.658  1.00 14.14 ? 164 GLN A N   1 
ATOM   1284 C  CA  . GLN A 1 167 ? 1.187   -2.487  1.542  1.00 14.72 ? 164 GLN A CA  1 
ATOM   1285 C  C   . GLN A 1 167 ? 1.741   -1.637  2.680  1.00 13.90 ? 164 GLN A C   1 
ATOM   1286 O  O   . GLN A 1 167 ? 1.090   -0.684  3.105  1.00 15.01 ? 164 GLN A O   1 
ATOM   1287 C  CB  . GLN A 1 167 ? 0.424   -3.692  2.065  1.00 17.55 ? 164 GLN A CB  1 
ATOM   1288 C  CG  . GLN A 1 167 ? -0.387  -4.336  0.948  1.00 21.23 ? 164 GLN A CG  1 
ATOM   1289 C  CD  . GLN A 1 167 ? -1.189  -3.314  0.146  1.00 25.67 ? 164 GLN A CD  1 
ATOM   1290 O  OE1 . GLN A 1 167 ? -2.016  -2.576  0.687  1.00 29.67 ? 164 GLN A OE1 1 
ATOM   1291 N  NE2 . GLN A 1 167 ? -0.947  -3.235  -1.162 1.00 28.68 ? 164 GLN A NE2 1 
ATOM   1292 N  N   . SER A 1 168 ? 2.919   -1.995  3.172  1.00 13.86 ? 165 SER A N   1 
ATOM   1293 C  CA  . SER A 1 168 ? 3.572   -1.249  4.232  1.00 13.75 ? 165 SER A CA  1 
ATOM   1294 C  C   . SER A 1 168 ? 3.884   0.173   3.778  1.00 14.12 ? 165 SER A C   1 
ATOM   1295 O  O   . SER A 1 168 ? 3.676   1.136   4.505  1.00 14.64 ? 165 SER A O   1 
ATOM   1296 C  CB  . SER A 1 168 ? 4.832   -1.912  4.706  1.00 13.69 ? 165 SER A CB  1 
ATOM   1297 O  OG  . SER A 1 168 ? 4.582   -3.175  5.266  1.00 14.49 ? 165 SER A OG  1 
ATOM   1298 N  N   . VAL A 1 169 ? 4.383   0.312   2.536  1.00 14.11 ? 166 VAL A N   1 
ATOM   1299 C  CA  . VAL A 1 169 ? 4.677   1.625   2.000  1.00 15.08 ? 166 VAL A CA  1 
ATOM   1300 C  C   . VAL A 1 169 ? 3.380   2.419   1.869  1.00 16.24 ? 166 VAL A C   1 
ATOM   1301 O  O   . VAL A 1 169 ? 3.345   3.602   2.196  1.00 15.83 ? 166 VAL A O   1 
ATOM   1302 C  CB  . VAL A 1 169 ? 5.388   1.473   0.645  1.00 16.33 ? 166 VAL A CB  1 
ATOM   1303 C  CG1 . VAL A 1 169 ? 5.440   2.792   -0.131 1.00 18.67 ? 166 VAL A CG1 1 
ATOM   1304 C  CG2 . VAL A 1 169 ? 6.772   0.856   0.818  1.00 17.32 ? 166 VAL A CG2 1 
ATOM   1305 N  N   . LYS A 1 170 ? 2.317   1.754   1.428  1.00 15.41 ? 167 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 170 ? 1.040   2.446   1.302  1.00 16.85 ? 167 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 170 ? 0.514   2.912   2.665  1.00 15.49 ? 167 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 170 ? -0.066  3.990   2.822  1.00 16.82 ? 167 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 170 ? 0.039   1.560   0.576  1.00 17.59 ? 167 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 170 ? 0.387   1.368   -0.893 1.00 22.12 ? 167 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 170 ? -0.591  0.558   -1.675 1.00 26.58 ? 167 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 170 ? -0.254  0.613   -3.152 1.00 30.48 ? 167 LYS A CE  1 
ATOM   1313 N  NZ  . LYS A 1 170 ? -0.730  -0.585  -3.879 1.00 36.98 ? 167 LYS A NZ  1 
ATOM   1314 N  N   . ALA A 1 171 ? 0.715   2.080   3.676  1.00 15.46 ? 168 ALA A N   1 
ATOM   1315 C  CA  . ALA A 1 171 ? 0.277   2.422   5.020  1.00 14.22 ? 168 ALA A CA  1 
ATOM   1316 C  C   . ALA A 1 171 ? 1.021   3.641   5.547  1.00 14.94 ? 168 ALA A C   1 
ATOM   1317 O  O   . ALA A 1 171 ? 0.414   4.549   6.141  1.00 16.30 ? 168 ALA A O   1 
ATOM   1318 C  CB  . ALA A 1 171 ? 0.437   1.260   5.953  1.00 14.87 ? 168 ALA A CB  1 
ATOM   1319 N  N   . VAL A 1 172 ? 2.333   3.674   5.311  1.00 15.16 ? 169 VAL A N   1 
ATOM   1320 C  CA  . VAL A 1 172 ? 3.119   4.831   5.716  1.00 15.78 ? 169 VAL A CA  1 
ATOM   1321 C  C   . VAL A 1 172 ? 2.653   6.077   4.997  1.00 17.27 ? 169 VAL A C   1 
ATOM   1322 O  O   . VAL A 1 172 ? 2.508   7.118   5.618  1.00 17.24 ? 169 VAL A O   1 
ATOM   1323 C  CB  . VAL A 1 172 ? 4.633   4.612   5.564  1.00 15.34 ? 169 VAL A CB  1 
ATOM   1324 C  CG1 . VAL A 1 172 ? 5.439   5.898   5.746  1.00 17.28 ? 169 VAL A CG1 1 
ATOM   1325 C  CG2 . VAL A 1 172 ? 5.070   3.534   6.532  1.00 16.84 ? 169 VAL A CG2 1 
ATOM   1326 N  N   . GLU A 1 173 ? 2.388   5.939   3.703  1.00 16.60 ? 170 GLU A N   1 
ATOM   1327 C  CA  . GLU A 1 173 ? 1.925   7.095   2.945  1.00 18.40 ? 170 GLU A CA  1 
ATOM   1328 C  C   . GLU A 1 173 ? 0.611   7.617   3.536  1.00 18.59 ? 170 GLU A C   1 
ATOM   1329 O  O   . GLU A 1 173 ? 0.444   8.837   3.646  1.00 19.77 ? 170 GLU A O   1 
ATOM   1330 C  CB  . GLU A 1 173 ? 1.845   6.791   1.435  1.00 20.49 ? 170 GLU A CB  1 
ATOM   1331 C  CG  . GLU A 1 173 ? 1.972   8.061   0.587  1.00 25.72 ? 170 GLU A CG  1 
ATOM   1332 C  CD  . GLU A 1 173 ? 3.338   8.758   0.619  1.00 28.05 ? 170 GLU A CD  1 
ATOM   1333 O  OE1 . GLU A 1 173 ? 4.354   8.104   1.038  1.00 28.51 ? 170 GLU A OE1 1 
ATOM   1334 O  OE2 . GLU A 1 173 ? 3.408   9.942   0.217  1.00 36.28 ? 170 GLU A OE2 1 
ATOM   1335 N  N   . TYR A 1 174 ? -0.326  6.710   3.851  1.00 18.33 ? 171 TYR A N   1 
ATOM   1336 C  CA  . TYR A 1 174 ? -1.626  7.050   4.406  1.00 19.11 ? 171 TYR A CA  1 
ATOM   1337 C  C   . TYR A 1 174 ? -1.474  7.824   5.719  1.00 19.29 ? 171 TYR A C   1 
ATOM   1338 O  O   . TYR A 1 174 ? -2.188  8.810   5.960  1.00 21.38 ? 171 TYR A O   1 
ATOM   1339 C  CB  . TYR A 1 174 ? -2.353  5.729   4.589  1.00 19.59 ? 171 TYR A CB  1 
ATOM   1340 C  CG  . TYR A 1 174 ? -3.817  5.844   4.946  1.00 18.77 ? 171 TYR A CG  1 
ATOM   1341 C  CD1 . TYR A 1 174 ? -4.739  6.215   3.994  1.00 20.36 ? 171 TYR A CD1 1 
ATOM   1342 C  CD2 . TYR A 1 174 ? -4.269  5.576   6.232  1.00 20.58 ? 171 TYR A CD2 1 
ATOM   1343 C  CE1 . TYR A 1 174 ? -6.080  6.280   4.292  1.00 22.40 ? 171 TYR A CE1 1 
ATOM   1344 C  CE2 . TYR A 1 174 ? -5.613  5.646   6.550  1.00 22.04 ? 171 TYR A CE2 1 
ATOM   1345 C  CZ  . TYR A 1 174 ? -6.519  5.998   5.570  1.00 23.32 ? 171 TYR A CZ  1 
ATOM   1346 O  OH  . TYR A 1 174 ? -7.851  6.061   5.798  1.00 27.86 ? 171 TYR A OH  1 
ATOM   1347 N  N   . LEU A 1 175 ? -0.459  7.465   6.520  1.00 18.80 ? 172 LEU A N   1 
ATOM   1348 C  CA  . LEU A 1 175 ? -0.177  8.179   7.772  1.00 18.90 ? 172 LEU A CA  1 
ATOM   1349 C  C   . LEU A 1 175 ? 0.465   9.538   7.515  1.00 22.04 ? 172 LEU A C   1 
ATOM   1350 O  O   . LEU A 1 175 ? 0.089   10.506  8.171  1.00 23.96 ? 172 LEU A O   1 
ATOM   1351 C  CB  . LEU A 1 175 ? 0.787   7.333   8.594  1.00 19.25 ? 172 LEU A CB  1 
ATOM   1352 C  CG  . LEU A 1 175 ? 0.168   6.051   9.128  1.00 18.41 ? 172 LEU A CG  1 
ATOM   1353 C  CD1 . LEU A 1 175 ? 1.206   5.169   9.794  1.00 18.52 ? 172 LEU A CD1 1 
ATOM   1354 C  CD2 . LEU A 1 175 ? -0.944  6.378   10.108 1.00 18.87 ? 172 LEU A CD2 1 
ATOM   1355 N  N   . ILE A 1 176 ? 1.449   9.600   6.612  1.00 21.79 ? 173 ILE A N   1 
ATOM   1356 C  CA  . ILE A 1 176 ? 2.133   10.841  6.277  1.00 25.60 ? 173 ILE A CA  1 
ATOM   1357 C  C   . ILE A 1 176 ? 1.092   11.874  5.838  1.00 27.08 ? 173 ILE A C   1 
ATOM   1358 O  O   . ILE A 1 176 ? 1.242   13.064  6.118  1.00 31.19 ? 173 ILE A O   1 
ATOM   1359 C  CB  . ILE A 1 176 ? 3.205   10.584  5.192  1.00 27.25 ? 173 ILE A CB  1 
ATOM   1360 C  CG1 . ILE A 1 176 ? 4.415   9.844   5.772  1.00 28.58 ? 173 ILE A CG1 1 
ATOM   1361 C  CG2 . ILE A 1 176 ? 3.619   11.862  4.466  1.00 31.24 ? 173 ILE A CG2 1 
ATOM   1362 C  CD1 . ILE A 1 176 ? 5.426   9.369   4.729  1.00 27.52 ? 173 ILE A CD1 1 
ATOM   1363 N  N   . GLU A 1 177 ? 0.041   11.401  5.158  1.00 25.30 ? 174 GLU A N   1 
ATOM   1364 C  CA  . GLU A 1 177 ? -1.013  12.236  4.613  1.00 27.01 ? 174 GLU A CA  1 
ATOM   1365 C  C   . GLU A 1 177 ? -2.042  12.678  5.643  1.00 29.18 ? 174 GLU A C   1 
ATOM   1366 O  O   . GLU A 1 177 ? -2.974  13.407  5.298  1.00 33.57 ? 174 GLU A O   1 
ATOM   1367 C  CB  . GLU A 1 177 ? -1.779  11.470  3.543  1.00 27.68 ? 174 GLU A CB  1 
ATOM   1368 C  CG  . GLU A 1 177 ? -0.988  11.308  2.271  1.00 28.88 ? 174 GLU A CG  1 
ATOM   1369 C  CD  . GLU A 1 177 ? -1.574  10.242  1.383  1.00 31.60 ? 174 GLU A CD  1 
ATOM   1370 O  OE1 . GLU A 1 177 ? -1.032  10.038  0.278  1.00 35.05 ? 174 GLU A OE1 1 
ATOM   1371 O  OE2 . GLU A 1 177 ? -2.565  9.609   1.825  1.00 32.68 ? 174 GLU A OE2 1 
ATOM   1372 N  N   . GLY A 1 178 ? -1.861  12.282  6.898  1.00 27.87 ? 175 GLY A N   1 
ATOM   1373 C  CA  . GLY A 1 178 ? -2.570  12.910  7.997  1.00 28.08 ? 175 GLY A CA  1 
ATOM   1374 C  C   . GLY A 1 178 ? -3.742  12.080  8.506  1.00 24.17 ? 175 GLY A C   1 
ATOM   1375 O  O   . GLY A 1 178 ? -4.431  12.501  9.446  1.00 26.20 ? 175 GLY A O   1 
ATOM   1376 N  N   . HIS A 1 179 ? -3.926  10.865  7.965  1.00 23.14 ? 176 HIS A N   1 
ATOM   1377 C  CA  . HIS A 1 179 ? -5.003  10.014  8.448  1.00 21.78 ? 176 HIS A CA  1 
ATOM   1378 C  C   . HIS A 1 179 ? -4.606  9.509   9.826  1.00 20.78 ? 176 HIS A C   1 
ATOM   1379 O  O   . HIS A 1 179 ? -3.441  9.242   10.084 1.00 22.67 ? 176 HIS A O   1 
ATOM   1380 C  CB  . HIS A 1 179 ? -5.316  8.815   7.554  1.00 21.83 ? 176 HIS A CB  1 
ATOM   1381 C  CG  . HIS A 1 179 ? -5.776  9.213   6.208  1.00 23.45 ? 176 HIS A CG  1 
ATOM   1382 N  ND1 . HIS A 1 179 ? -4.919  9.470   5.158  1.00 24.78 ? 176 HIS A ND1 1 
ATOM   1383 C  CD2 . HIS A 1 179 ? -7.015  9.418   5.745  1.00 24.88 ? 176 HIS A CD2 1 
ATOM   1384 C  CE1 . HIS A 1 179 ? -5.650  9.819   4.098  1.00 26.07 ? 176 HIS A CE1 1 
ATOM   1385 N  NE2 . HIS A 1 179 ? -6.918  9.752   4.433  1.00 26.27 ? 176 HIS A NE2 1 
ATOM   1386 N  N   . SER A 1 180 ? -5.592  9.299   10.676 1.00 20.69 ? 177 SER A N   1 
ATOM   1387 C  CA  . SER A 1 180 ? -5.296  8.800   11.998 1.00 20.26 ? 177 SER A CA  1 
ATOM   1388 C  C   . SER A 1 180 ? -4.739  7.380   11.909 1.00 19.84 ? 177 SER A C   1 
ATOM   1389 O  O   . SER A 1 180 ? -5.012  6.615   10.976 1.00 18.90 ? 177 SER A O   1 
ATOM   1390 C  CB  . SER A 1 180 ? -6.514  8.843   12.854 1.00 22.14 ? 177 SER A CB  1 
ATOM   1391 O  OG  . SER A 1 180 ? -7.443  7.836   12.511 1.00 22.54 ? 177 SER A OG  1 
ATOM   1392 N  N   . PHE A 1 181 ? -3.941  7.019   12.910 1.00 18.24 ? 178 PHE A N   1 
ATOM   1393 C  CA  . PHE A 1 181 ? -3.427  5.666   12.960 1.00 16.31 ? 178 PHE A CA  1 
ATOM   1394 C  C   . PHE A 1 181 ? -4.571  4.665   13.144 1.00 16.90 ? 178 PHE A C   1 
ATOM   1395 O  O   . PHE A 1 181 ? -4.545  3.585   12.539 1.00 16.74 ? 178 PHE A O   1 
ATOM   1396 C  CB  . PHE A 1 181 ? -2.293  5.559   13.987 1.00 17.36 ? 178 PHE A CB  1 
ATOM   1397 C  CG  . PHE A 1 181 ? -1.522  4.267   13.873 1.00 16.06 ? 178 PHE A CG  1 
ATOM   1398 C  CD1 . PHE A 1 181 ? -1.945  3.132   14.526 1.00 16.26 ? 178 PHE A CD1 1 
ATOM   1399 C  CD2 . PHE A 1 181 ? -0.399  4.182   13.078 1.00 17.11 ? 178 PHE A CD2 1 
ATOM   1400 C  CE1 . PHE A 1 181 ? -1.259  1.940   14.400 1.00 15.75 ? 178 PHE A CE1 1 
ATOM   1401 C  CE2 . PHE A 1 181 ? 0.304   2.997   12.956 1.00 15.62 ? 178 PHE A CE2 1 
ATOM   1402 C  CZ  . PHE A 1 181 ? -0.116  1.881   13.645 1.00 15.34 ? 178 PHE A CZ  1 
ATOM   1403 N  N   . VAL A 1 182 ? -5.605  4.993   13.938 1.00 16.90 ? 179 VAL A N   1 
ATOM   1404 C  CA  . VAL A 1 182 ? -6.754  4.105   14.046 1.00 19.64 ? 179 VAL A CA  1 
ATOM   1405 C  C   . VAL A 1 182 ? -7.441  3.938   12.686 1.00 17.95 ? 179 VAL A C   1 
ATOM   1406 O  O   . VAL A 1 182 ? -7.878  2.849   12.343 1.00 18.79 ? 179 VAL A O   1 
ATOM   1407 C  CB  . VAL A 1 182 ? -7.723  4.569   15.148 1.00 22.74 ? 179 VAL A CB  1 
ATOM   1408 C  CG1 . VAL A 1 182 ? -9.035  3.794   15.135 1.00 24.42 ? 179 VAL A CG1 1 
ATOM   1409 C  CG2 . VAL A 1 182 ? -7.077  4.452   16.506 1.00 25.17 ? 179 VAL A CG2 1 
ATOM   1410 N  N   . ASP A 1 183 ? -7.499  4.991   11.866 1.00 18.34 ? 180 ASP A N   1 
ATOM   1411 C  CA  . ASP A 1 183 ? -8.054  4.817   10.533 1.00 18.77 ? 180 ASP A CA  1 
ATOM   1412 C  C   . ASP A 1 183 ? -7.165  3.918   9.668  1.00 17.82 ? 180 ASP A C   1 
ATOM   1413 O  O   . ASP A 1 183 ? -7.642  3.119   8.870  1.00 20.09 ? 180 ASP A O   1 
ATOM   1414 C  CB  . ASP A 1 183 ? -8.335  6.166   9.856  1.00 21.45 ? 180 ASP A CB  1 
ATOM   1415 C  CG  . ASP A 1 183 ? -9.624  6.850   10.292 1.00 24.95 ? 180 ASP A CG  1 
ATOM   1416 O  OD1 . ASP A 1 183 ? -10.374 6.261   11.088 1.00 29.46 ? 180 ASP A OD1 1 
ATOM   1417 O  OD2 . ASP A 1 183 ? -9.831  7.985   9.884  1.00 33.04 ? 180 ASP A OD2 1 
ATOM   1418 N  N   . ALA A 1 184 ? -5.852  4.062   9.822  1.00 16.12 ? 181 ALA A N   1 
ATOM   1419 C  CA  . ALA A 1 184 ? -4.915  3.215   9.121  1.00 16.10 ? 181 ALA A CA  1 
ATOM   1420 C  C   . ALA A 1 184 ? -5.064  1.752   9.544  1.00 16.09 ? 181 ALA A C   1 
ATOM   1421 O  O   . ALA A 1 184 ? -5.003  0.853   8.704  1.00 16.53 ? 181 ALA A O   1 
ATOM   1422 C  CB  . ALA A 1 184 ? -3.499  3.703   9.313  1.00 16.11 ? 181 ALA A CB  1 
ATOM   1423 N  N   . MET A 1 185 ? -5.268  1.520   10.840 1.00 15.30 ? 182 MET A N   1 
ATOM   1424 C  CA  . MET A 1 185 ? -5.528  0.180   11.330 1.00 16.50 ? 182 MET A CA  1 
ATOM   1425 C  C   . MET A 1 185 ? -6.770  -0.382  10.645 1.00 16.33 ? 182 MET A C   1 
ATOM   1426 O  O   . MET A 1 185 ? -6.776  -1.523  10.205 1.00 18.66 ? 182 MET A O   1 
ATOM   1427 C  CB  . MET A 1 185 ? -5.726  0.169   12.848 1.00 16.13 ? 182 MET A CB  1 
ATOM   1428 C  CG  . MET A 1 185 ? -4.398  0.419   13.603 1.00 15.20 ? 182 MET A CG  1 
ATOM   1429 S  SD  . MET A 1 185 ? -4.653  0.901   15.354 1.00 18.74 ? 182 MET A SD  1 
ATOM   1430 C  CE  . MET A 1 185 ? -5.392  -0.626  15.884 1.00 19.36 ? 182 MET A CE  1 
ATOM   1431 N  N   . ASN A 1 186 ? -7.847  0.413   10.558 1.00 16.90 ? 183 ASN A N   1 
ATOM   1432 C  CA  . ASN A 1 186 ? -9.088  -0.053  9.980  1.00 19.34 ? 183 ASN A CA  1 
ATOM   1433 C  C   . ASN A 1 186 ? -8.902  -0.376  8.506  1.00 19.77 ? 183 ASN A C   1 
ATOM   1434 O  O   . ASN A 1 186 ? -9.445  -1.359  8.012  1.00 20.47 ? 183 ASN A O   1 
ATOM   1435 C  CB  . ASN A 1 186 ? -10.162 1.002   10.200 1.00 20.91 ? 183 ASN A CB  1 
ATOM   1436 C  CG  . ASN A 1 186 ? -11.461 0.617   9.536  1.00 24.36 ? 183 ASN A CG  1 
ATOM   1437 O  OD1 . ASN A 1 186 ? -12.119 -0.325  9.960  1.00 30.15 ? 183 ASN A OD1 1 
ATOM   1438 N  ND2 . ASN A 1 186 ? -11.763 1.275   8.437  1.00 26.29 ? 183 ASN A ND2 1 
ATOM   1439 N  N   . ARG A 1 187 ? -8.101  0.444   7.813  1.00 18.19 ? 184 ARG A N   1 
ATOM   1440 C  CA  . ARG A 1 187 ? -7.868  0.249   6.384  1.00 18.61 ? 184 ARG A CA  1 
ATOM   1441 C  C   . ARG A 1 187 ? -6.977  -0.963  6.089  1.00 18.25 ? 184 ARG A C   1 
ATOM   1442 O  O   . ARG A 1 187 ? -7.199  -1.656  5.086  1.00 20.64 ? 184 ARG A O   1 
ATOM   1443 C  CB  . ARG A 1 187 ? -7.218  1.494   5.765  1.00 19.05 ? 184 ARG A CB  1 
ATOM   1444 C  CG  . ARG A 1 187 ? -6.876  1.339   4.293  1.00 21.13 ? 184 ARG A CG  1 
ATOM   1445 C  CD  . ARG A 1 187 ? -6.421  2.633   3.656  1.00 25.34 ? 184 ARG A CD  1 
ATOM   1446 N  NE  . ARG A 1 187 ? -6.040  2.429   2.268  1.00 31.54 ? 184 ARG A NE  1 
ATOM   1447 N  N   . PHE A 1 188 ? -5.911  -1.188  6.873  1.00 16.72 ? 185 PHE A N   1 
ATOM   1448 C  CA  . PHE A 1 188 ? -4.866  -2.125  6.482  1.00 16.77 ? 185 PHE A CA  1 
ATOM   1449 C  C   . PHE A 1 188 ? -4.887  -3.436  7.270  1.00 17.09 ? 185 PHE A C   1 
ATOM   1450 O  O   . PHE A 1 188 ? -4.252  -4.380  6.819  1.00 18.71 ? 185 PHE A O   1 
ATOM   1451 C  CB  . PHE A 1 188 ? -3.491  -1.464  6.630  1.00 16.66 ? 185 PHE A CB  1 
ATOM   1452 C  CG  . PHE A 1 188 ? -3.227  -0.425  5.571  1.00 17.78 ? 185 PHE A CG  1 
ATOM   1453 C  CD1 . PHE A 1 188 ? -2.838  -0.790  4.292  1.00 18.46 ? 185 PHE A CD1 1 
ATOM   1454 C  CD2 . PHE A 1 188 ? -3.407  0.922   5.821  1.00 18.72 ? 185 PHE A CD2 1 
ATOM   1455 C  CE1 . PHE A 1 188 ? -2.672  0.173   3.308  1.00 19.01 ? 185 PHE A CE1 1 
ATOM   1456 C  CE2 . PHE A 1 188 ? -3.225  1.879   4.838  1.00 19.85 ? 185 PHE A CE2 1 
ATOM   1457 C  CZ  . PHE A 1 188 ? -2.888  1.488   3.569  1.00 20.14 ? 185 PHE A CZ  1 
ATOM   1458 N  N   . ASN A 1 189 ? -5.537  -3.500  8.442  1.00 16.73 ? 186 ASN A N   1 
ATOM   1459 C  CA  . ASN A 1 189 ? -5.514  -4.707  9.250  1.00 18.82 ? 186 ASN A CA  1 
ATOM   1460 C  C   . ASN A 1 189 ? -6.457  -5.772  8.674  1.00 22.75 ? 186 ASN A C   1 
ATOM   1461 O  O   . ASN A 1 189 ? -7.367  -5.385  7.911  1.00 26.03 ? 186 ASN A O   1 
ATOM   1462 C  CB  . ASN A 1 189 ? -5.844  -4.395  10.711 1.00 16.99 ? 186 ASN A CB  1 
ATOM   1463 C  CG  . ASN A 1 189 ? -4.655  -3.801  11.420 1.00 15.41 ? 186 ASN A CG  1 
ATOM   1464 O  OD1 . ASN A 1 189 ? -3.547  -3.802  10.890 1.00 16.59 ? 186 ASN A OD1 1 
ATOM   1465 N  ND2 . ASN A 1 189 ? -4.862  -3.324  12.619 1.00 15.89 ? 186 ASN A ND2 1 
ATOM   1466 O  OXT . ASN A 1 189 ? -6.239  -6.969  9.010  1.00 28.78 ? 186 ASN A OXT 1 
HETATM 1467 C  C1  . EDO B 2 .   ? 5.303   -1.422  -5.644 1.00 40.12 ? 201 EDO A C1  1 
HETATM 1468 O  O1  . EDO B 2 .   ? 4.137   -2.132  -5.922 1.00 43.75 ? 201 EDO A O1  1 
HETATM 1469 C  C2  . EDO B 2 .   ? 5.312   -0.757  -4.314 1.00 38.58 ? 201 EDO A C2  1 
HETATM 1470 O  O2  . EDO B 2 .   ? 4.065   -0.550  -3.705 1.00 27.83 ? 201 EDO A O2  1 
HETATM 1471 C  C1  . BME C 3 .   ? 8.589   2.207   -3.979 1.00 34.92 ? 202 BME A C1  1 
HETATM 1472 C  C2  . BME C 3 .   ? 10.109  2.101   -3.929 1.00 28.36 ? 202 BME A C2  1 
HETATM 1473 O  O1  . BME C 3 .   ? 7.858   0.996   -4.105 1.00 33.36 ? 202 BME A O1  1 
HETATM 1474 S  S2  . BME C 3 .   ? 11.167  1.038   -4.973 1.00 45.02 ? 202 BME A S2  1 
HETATM 1475 NA NA  . NA  D 4 .   ? 27.000  9.926   4.057  1.00 51.95 ? 203 NA  A NA  1 
HETATM 1476 NA NA  . NA  E 4 .   ? 18.907  -1.652  24.460 1.00 35.12 ? 204 NA  A NA  1 
HETATM 1477 S  S   . SO4 F 5 .   ? -1.866  -8.710  16.064 1.00 39.69 ? 205 SO4 A S   1 
HETATM 1478 O  O1  . SO4 F 5 .   ? -1.173  -9.348  14.945 1.00 45.60 ? 205 SO4 A O1  1 
HETATM 1479 O  O2  . SO4 F 5 .   ? -3.298  -8.667  15.817 1.00 33.74 ? 205 SO4 A O2  1 
HETATM 1480 O  O3  . SO4 F 5 .   ? -1.619  -9.501  17.249 1.00 49.77 ? 205 SO4 A O3  1 
HETATM 1481 O  O4  . SO4 F 5 .   ? -1.320  -7.398  16.237 1.00 38.26 ? 205 SO4 A O4  1 
HETATM 1482 S  S   . SO4 G 5 .   ? 11.472  -22.699 10.528 1.00 29.74 ? 206 SO4 A S   1 
HETATM 1483 O  O1  . SO4 G 5 .   ? 11.669  -21.780 9.411  1.00 35.70 ? 206 SO4 A O1  1 
HETATM 1484 O  O2  . SO4 G 5 .   ? 10.210  -23.409 10.375 1.00 39.34 ? 206 SO4 A O2  1 
HETATM 1485 O  O3  . SO4 G 5 .   ? 12.568  -23.661 10.576 1.00 33.60 ? 206 SO4 A O3  1 
HETATM 1486 O  O4  . SO4 G 5 .   ? 11.400  -21.912 11.747 1.00 29.79 ? 206 SO4 A O4  1 
HETATM 1487 O  O   . HOH H 6 .   ? 9.800   -6.926  23.488 1.00 54.09 ? 301 HOH A O   1 
HETATM 1488 O  O   . HOH H 6 .   ? 16.519  -2.917  0.975  1.00 28.03 ? 302 HOH A O   1 
HETATM 1489 O  O   . HOH H 6 .   ? 3.326   23.181  15.651 1.00 20.73 ? 303 HOH A O   1 
HETATM 1490 O  O   . HOH H 6 .   ? 1.063   -11.284 17.804 1.00 36.41 ? 304 HOH A O   1 
HETATM 1491 O  O   . HOH H 6 .   ? -3.903  -3.548  2.178  1.00 31.35 ? 305 HOH A O   1 
HETATM 1492 O  O   . HOH H 6 .   ? 19.103  -2.036  3.639  1.00 32.20 ? 306 HOH A O   1 
HETATM 1493 O  O   . HOH H 6 .   ? -1.131  10.250  10.747 1.00 38.31 ? 307 HOH A O   1 
HETATM 1494 O  O   . HOH H 6 .   ? 19.475  12.462  5.782  1.00 44.48 ? 308 HOH A O   1 
HETATM 1495 O  O   . HOH H 6 .   ? 18.097  12.408  2.829  1.00 36.21 ? 309 HOH A O   1 
HETATM 1496 O  O   . HOH H 6 .   ? 26.704  0.361   9.610  1.00 31.45 ? 310 HOH A O   1 
HETATM 1497 O  O   . HOH H 6 .   ? 5.377   5.577   1.779  1.00 24.97 ? 311 HOH A O   1 
HETATM 1498 O  O   . HOH H 6 .   ? 1.129   -10.828 15.118 1.00 21.33 ? 312 HOH A O   1 
HETATM 1499 O  O   . HOH H 6 .   ? 26.819  7.211   14.140 1.00 30.54 ? 313 HOH A O   1 
HETATM 1500 O  O   . HOH H 6 .   ? 15.323  -12.197 1.258  1.00 20.36 ? 314 HOH A O   1 
HETATM 1501 O  O   . HOH H 6 .   ? 8.800   -21.258 0.856  1.00 26.52 ? 315 HOH A O   1 
HETATM 1502 O  O   . HOH H 6 .   ? 23.670  6.453   19.734 1.00 26.91 ? 316 HOH A O   1 
HETATM 1503 O  O   . HOH H 6 .   ? -0.287  -14.104 3.613  1.00 28.22 ? 317 HOH A O   1 
HETATM 1504 O  O   . HOH H 6 .   ? 3.595   6.549   17.383 1.00 17.08 ? 318 HOH A O   1 
HETATM 1505 O  O   . HOH H 6 .   ? 4.441   -10.011 5.326  1.00 14.39 ? 319 HOH A O   1 
HETATM 1506 O  O   . HOH H 6 .   ? 20.993  -2.231  13.408 1.00 14.86 ? 320 HOH A O   1 
HETATM 1507 O  O   . HOH H 6 .   ? 15.756  4.619   31.402 1.00 32.35 ? 321 HOH A O   1 
HETATM 1508 O  O   . HOH H 6 .   ? -2.980  -4.659  4.445  1.00 25.56 ? 322 HOH A O   1 
HETATM 1509 O  O   . HOH H 6 .   ? -3.680  -6.982  7.322  1.00 27.64 ? 323 HOH A O   1 
HETATM 1510 O  O   . HOH H 6 .   ? 24.501  -1.364  7.196  1.00 21.27 ? 324 HOH A O   1 
HETATM 1511 O  O   . HOH H 6 .   ? 8.771   19.650  9.850  1.00 31.31 ? 325 HOH A O   1 
HETATM 1512 O  O   . HOH H 6 .   ? 21.951  -4.706  6.619  1.00 14.95 ? 326 HOH A O   1 
HETATM 1513 O  O   . HOH H 6 .   ? 1.609   -5.176  19.052 1.00 35.85 ? 327 HOH A O   1 
HETATM 1514 O  O   . HOH H 6 .   ? 3.631   4.066   28.497 1.00 40.04 ? 328 HOH A O   1 
HETATM 1515 O  O   . HOH H 6 .   ? -0.110  -7.416  2.162  1.00 26.03 ? 329 HOH A O   1 
HETATM 1516 O  O   . HOH H 6 .   ? 21.946  -10.691 3.959  1.00 31.32 ? 330 HOH A O   1 
HETATM 1517 O  O   . HOH H 6 .   ? 24.400  -3.208  3.972  1.00 36.53 ? 331 HOH A O   1 
HETATM 1518 O  O   . HOH H 6 .   ? -6.253  -2.347  2.610  1.00 30.58 ? 332 HOH A O   1 
HETATM 1519 O  O   . HOH H 6 .   ? 11.227  -11.815 14.703 1.00 23.98 ? 333 HOH A O   1 
HETATM 1520 O  O   . HOH H 6 .   ? 27.126  -6.885  10.096 1.00 22.54 ? 334 HOH A O   1 
HETATM 1521 O  O   . HOH H 6 .   ? 5.412   -20.216 8.655  1.00 31.81 ? 335 HOH A O   1 
HETATM 1522 O  O   . HOH H 6 .   ? 7.968   17.439  17.190 1.00 27.34 ? 336 HOH A O   1 
HETATM 1523 O  O   . HOH H 6 .   ? 14.236  -14.571 -1.790 1.00 31.80 ? 337 HOH A O   1 
HETATM 1524 O  O   . HOH H 6 .   ? 21.636  2.875   3.449  1.00 35.21 ? 338 HOH A O   1 
HETATM 1525 O  O   . HOH H 6 .   ? 8.820   -17.509 6.393  1.00 17.64 ? 339 HOH A O   1 
HETATM 1526 O  O   . HOH H 6 .   ? 13.861  -2.715  -0.238 1.00 20.50 ? 340 HOH A O   1 
HETATM 1527 O  O   . HOH H 6 .   ? 19.131  -9.424  10.379 1.00 14.10 ? 341 HOH A O   1 
HETATM 1528 O  O   . HOH H 6 .   ? 25.852  0.313   20.325 1.00 35.53 ? 342 HOH A O   1 
HETATM 1529 O  O   . HOH H 6 .   ? 4.232   9.366   24.687 1.00 28.71 ? 343 HOH A O   1 
HETATM 1530 O  O   . HOH H 6 .   ? 11.326  16.289  -0.272 1.00 36.36 ? 344 HOH A O   1 
HETATM 1531 O  O   . HOH H 6 .   ? 4.956   -17.308 16.179 1.00 18.58 ? 345 HOH A O   1 
HETATM 1532 O  O   . HOH H 6 .   ? 13.875  -10.321 0.036  1.00 32.79 ? 346 HOH A O   1 
HETATM 1533 O  O   . HOH H 6 .   ? 8.261   13.336  -2.074 1.00 49.74 ? 347 HOH A O   1 
HETATM 1534 O  O   . HOH H 6 .   ? -10.040 3.469   7.495  1.00 33.43 ? 348 HOH A O   1 
HETATM 1535 O  O   . HOH H 6 .   ? 16.979  -5.957  23.304 1.00 24.90 ? 349 HOH A O   1 
HETATM 1536 O  O   . HOH H 6 .   ? -1.532  5.071   0.710  1.00 24.24 ? 350 HOH A O   1 
HETATM 1537 O  O   . HOH H 6 .   ? 5.397   -8.849  16.959 1.00 29.48 ? 351 HOH A O   1 
HETATM 1538 O  O   . HOH H 6 .   ? 2.419   -16.917 3.986  1.00 22.03 ? 352 HOH A O   1 
HETATM 1539 O  O   . HOH H 6 .   ? 18.161  -4.662  4.908  1.00 15.38 ? 353 HOH A O   1 
HETATM 1540 O  O   . HOH H 6 .   ? 17.449  -1.735  13.976 1.00 12.54 ? 354 HOH A O   1 
HETATM 1541 O  O   . HOH H 6 .   ? 26.659  -10.414 13.412 1.00 30.14 ? 355 HOH A O   1 
HETATM 1542 O  O   . HOH H 6 .   ? 4.416   -5.037  19.079 1.00 27.28 ? 356 HOH A O   1 
HETATM 1543 O  O   . HOH H 6 .   ? 12.757  -5.704  10.804 1.00 11.56 ? 357 HOH A O   1 
HETATM 1544 O  O   . HOH H 6 .   ? 4.301   6.607   24.593 1.00 23.57 ? 358 HOH A O   1 
HETATM 1545 O  O   . HOH H 6 .   ? 18.396  12.921  -1.413 1.00 57.50 ? 359 HOH A O   1 
HETATM 1546 O  O   . HOH H 6 .   ? 16.614  -20.071 17.852 1.00 26.07 ? 360 HOH A O   1 
HETATM 1547 O  O   . HOH H 6 .   ? 17.534  -9.951  17.459 1.00 27.69 ? 361 HOH A O   1 
HETATM 1548 O  O   . HOH H 6 .   ? -5.925  -0.113  0.973  1.00 39.68 ? 362 HOH A O   1 
HETATM 1549 O  O   . HOH H 6 .   ? 7.988   -26.877 18.185 1.00 21.32 ? 363 HOH A O   1 
HETATM 1550 O  O   . HOH H 6 .   ? -9.818  -1.352  3.970  1.00 35.94 ? 364 HOH A O   1 
HETATM 1551 O  O   . HOH H 6 .   ? 14.367  -10.566 18.246 1.00 29.37 ? 365 HOH A O   1 
HETATM 1552 O  O   . HOH H 6 .   ? 16.676  3.305   -0.630 1.00 30.06 ? 366 HOH A O   1 
HETATM 1553 O  O   . HOH H 6 .   ? -3.094  8.921   14.888 1.00 24.60 ? 367 HOH A O   1 
HETATM 1554 O  O   . HOH H 6 .   ? 8.756   -11.192 15.659 1.00 24.18 ? 368 HOH A O   1 
HETATM 1555 O  O   . HOH H 6 .   ? -0.889  -14.781 9.806  1.00 16.27 ? 369 HOH A O   1 
HETATM 1556 O  O   . HOH H 6 .   ? 3.010   -7.060  20.631 1.00 37.93 ? 370 HOH A O   1 
HETATM 1557 O  O   . HOH H 6 .   ? 20.740  -7.988  17.710 1.00 25.01 ? 371 HOH A O   1 
HETATM 1558 O  O   . HOH H 6 .   ? 5.183   -9.383  -6.009 1.00 28.71 ? 372 HOH A O   1 
HETATM 1559 O  O   . HOH H 6 .   ? 20.524  -5.139  24.403 1.00 38.11 ? 373 HOH A O   1 
HETATM 1560 O  O   . HOH H 6 .   ? 7.488   -4.211  28.037 1.00 70.57 ? 374 HOH A O   1 
HETATM 1561 O  O   . HOH H 6 .   ? 12.097  -3.234  27.349 1.00 22.88 ? 375 HOH A O   1 
HETATM 1562 O  O   . HOH H 6 .   ? 3.405   8.592   13.887 1.00 29.90 ? 376 HOH A O   1 
HETATM 1563 O  O   . HOH H 6 .   ? 17.656  -5.457  1.016  1.00 26.13 ? 377 HOH A O   1 
HETATM 1564 O  O   . HOH H 6 .   ? 0.970   4.498   19.823 1.00 25.34 ? 378 HOH A O   1 
HETATM 1565 O  O   . HOH H 6 .   ? 11.610  -21.373 -2.381 1.00 27.47 ? 379 HOH A O   1 
HETATM 1566 O  O   . HOH H 6 .   ? 14.691  -20.274 -1.385 1.00 28.51 ? 380 HOH A O   1 
HETATM 1567 O  O   . HOH H 6 .   ? 29.062  -5.387  5.611  1.00 20.33 ? 381 HOH A O   1 
HETATM 1568 O  O   . HOH H 6 .   ? 17.886  -21.225 15.101 1.00 19.79 ? 382 HOH A O   1 
HETATM 1569 O  O   . HOH H 6 .   ? 4.028   -17.375 6.242  1.00 17.72 ? 383 HOH A O   1 
HETATM 1570 O  O   . HOH H 6 .   ? 4.913   1.678   28.771 1.00 36.61 ? 384 HOH A O   1 
HETATM 1571 O  O   . HOH H 6 .   ? 6.103   -20.376 3.936  1.00 29.69 ? 385 HOH A O   1 
HETATM 1572 O  O   . HOH H 6 .   ? 8.164   -13.854 24.846 1.00 32.88 ? 386 HOH A O   1 
HETATM 1573 O  O   . HOH H 6 .   ? 21.548  0.247   6.391  1.00 20.52 ? 387 HOH A O   1 
HETATM 1574 O  O   . HOH H 6 .   ? 11.658  -26.488 10.865 1.00 42.61 ? 388 HOH A O   1 
HETATM 1575 O  O   . HOH H 6 .   ? -7.601  -2.913  13.741 1.00 25.35 ? 389 HOH A O   1 
HETATM 1576 O  O   . HOH H 6 .   ? 23.947  -14.677 11.047 1.00 32.93 ? 390 HOH A O   1 
HETATM 1577 O  O   . HOH H 6 .   ? 20.080  5.850   0.091  1.00 32.59 ? 391 HOH A O   1 
HETATM 1578 O  O   . HOH H 6 .   ? 19.667  -9.974  15.589 1.00 23.66 ? 392 HOH A O   1 
HETATM 1579 O  O   . HOH H 6 .   ? -10.159 6.389   3.912  1.00 45.03 ? 393 HOH A O   1 
HETATM 1580 O  O   . HOH H 6 .   ? 9.292   -24.253 20.984 1.00 30.69 ? 394 HOH A O   1 
HETATM 1581 O  O   . HOH H 6 .   ? -1.850  -7.541  4.996  1.00 25.84 ? 395 HOH A O   1 
HETATM 1582 O  O   . HOH H 6 .   ? 11.795  -25.733 19.517 1.00 27.28 ? 396 HOH A O   1 
HETATM 1583 O  O   . HOH H 6 .   ? 0.961   7.230   18.733 1.00 20.68 ? 397 HOH A O   1 
HETATM 1584 O  O   . HOH H 6 .   ? 28.051  -7.498  7.410  1.00 27.79 ? 398 HOH A O   1 
HETATM 1585 O  O   . HOH H 6 .   ? 15.684  19.331  20.148 1.00 45.62 ? 399 HOH A O   1 
HETATM 1586 O  O   . HOH H 6 .   ? 13.412  -20.029 7.036  1.00 41.24 ? 400 HOH A O   1 
HETATM 1587 O  O   . HOH H 6 .   ? -5.174  7.405   15.905 1.00 22.99 ? 401 HOH A O   1 
HETATM 1588 O  O   . HOH H 6 .   ? 27.130  11.925  11.039 1.00 34.88 ? 402 HOH A O   1 
HETATM 1589 O  O   . HOH H 6 .   ? 17.810  -8.093  24.363 1.00 38.76 ? 403 HOH A O   1 
HETATM 1590 O  O   . HOH H 6 .   ? 18.061  -23.729 13.962 1.00 29.21 ? 404 HOH A O   1 
HETATM 1591 O  O   . HOH H 6 .   ? 10.055  -17.098 3.613  1.00 10.99 ? 405 HOH A O   1 
HETATM 1592 O  O   . HOH H 6 .   ? 18.397  6.902   24.867 1.00 44.45 ? 406 HOH A O   1 
HETATM 1593 O  O   . HOH H 6 .   ? 17.093  4.988   28.425 1.00 40.19 ? 407 HOH A O   1 
HETATM 1594 O  O   . HOH H 6 .   ? 2.778   -18.219 9.244  1.00 14.23 ? 408 HOH A O   1 
HETATM 1595 O  O   . HOH H 6 .   ? 29.037  9.353   15.016 1.00 40.87 ? 409 HOH A O   1 
HETATM 1596 O  O   . HOH H 6 .   ? 10.879  20.146  17.724 1.00 36.31 ? 410 HOH A O   1 
HETATM 1597 O  O   . HOH H 6 .   ? 5.360   21.210  15.657 1.00 25.68 ? 411 HOH A O   1 
HETATM 1598 O  O   . HOH H 6 .   ? 23.448  6.715   22.547 1.00 31.85 ? 412 HOH A O   1 
HETATM 1599 O  O   . HOH H 6 .   ? 21.369  5.570   24.005 1.00 29.52 ? 413 HOH A O   1 
HETATM 1600 O  O   . HOH H 6 .   ? 21.721  -15.192 5.221  1.00 36.54 ? 414 HOH A O   1 
HETATM 1601 O  O   . HOH H 6 .   ? -2.051  -16.676 8.421  1.00 27.35 ? 415 HOH A O   1 
HETATM 1602 O  O   . HOH H 6 .   ? 8.842   -11.588 26.401 1.00 39.10 ? 416 HOH A O   1 
HETATM 1603 O  O   . HOH H 6 .   ? 13.391  4.886   -7.707 1.00 33.29 ? 417 HOH A O   1 
HETATM 1604 O  O   . HOH H 6 .   ? 20.994  21.603  15.419 1.00 51.05 ? 418 HOH A O   1 
HETATM 1605 O  O   . HOH H 6 .   ? 22.716  2.580   26.010 1.00 49.30 ? 419 HOH A O   1 
HETATM 1606 O  O   . HOH H 6 .   ? -10.026 3.168   4.746  1.00 38.70 ? 420 HOH A O   1 
HETATM 1607 O  O   . HOH H 6 .   ? 17.020  -4.064  25.569 1.00 30.67 ? 421 HOH A O   1 
HETATM 1608 O  O   . HOH H 6 .   ? 18.785  18.009  10.874 1.00 50.33 ? 422 HOH A O   1 
HETATM 1609 O  O   . HOH H 6 .   ? 26.822  -2.297  4.498  1.00 39.76 ? 423 HOH A O   1 
HETATM 1610 O  O   . HOH H 6 .   ? 16.157  -13.069 17.199 1.00 35.05 ? 424 HOH A O   1 
HETATM 1611 O  O   . HOH H 6 .   ? -4.243  -5.762  0.405  1.00 38.14 ? 425 HOH A O   1 
HETATM 1612 O  O   . HOH H 6 .   ? -5.994  -11.763 7.580  1.00 45.71 ? 426 HOH A O   1 
HETATM 1613 O  O   . HOH H 6 .   ? 6.348   -18.830 6.234  1.00 21.23 ? 427 HOH A O   1 
HETATM 1614 O  O   . HOH H 6 .   ? 19.023  -12.781 16.148 1.00 32.30 ? 428 HOH A O   1 
HETATM 1615 O  O   . HOH H 6 .   ? -1.744  -7.252  -0.468 1.00 37.29 ? 429 HOH A O   1 
HETATM 1616 O  O   . HOH H 6 .   ? 14.065  -4.124  28.632 1.00 26.92 ? 430 HOH A O   1 
HETATM 1617 O  O   . HOH H 6 .   ? 20.831  -13.253 3.378  1.00 32.66 ? 431 HOH A O   1 
HETATM 1618 O  O   . HOH H 6 .   ? 22.114  -2.401  5.424  1.00 23.75 ? 432 HOH A O   1 
HETATM 1619 O  O   . HOH H 6 .   ? 23.994  1.063   5.025  1.00 50.52 ? 433 HOH A O   1 
HETATM 1620 O  O   . HOH H 6 .   ? 4.883   25.401  15.623 1.00 21.07 ? 434 HOH A O   1 
HETATM 1621 O  O   . HOH H 6 .   ? 16.805  -23.981 11.331 1.00 42.69 ? 435 HOH A O   1 
HETATM 1622 O  O   . HOH H 6 .   ? 13.316  -12.638 16.819 1.00 36.72 ? 436 HOH A O   1 
HETATM 1623 O  O   . HOH H 6 .   ? 17.931  -16.066 -1.765 1.00 38.71 ? 437 HOH A O   1 
HETATM 1624 O  O   . HOH H 6 .   ? 28.815  -5.013  11.154 1.00 44.36 ? 438 HOH A O   1 
HETATM 1625 O  O   . HOH H 6 .   ? 20.423  -11.540 -2.928 1.00 38.92 ? 439 HOH A O   1 
HETATM 1626 O  O   . HOH H 6 .   ? 17.067  -12.964 -0.967 1.00 35.53 ? 440 HOH A O   1 
HETATM 1627 O  O   . HOH H 6 .   ? 16.364  -6.406  -0.924 1.00 35.08 ? 441 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ALA A 1   ? 0.3447 0.3677 0.3414 0.0239  -0.0176 0.0327  -2  ALA A N   
2    C  CA  . ALA A 1   ? 0.3631 0.3068 0.3378 0.0296  0.0062  0.0305  -2  ALA A CA  
3    C  C   . ALA A 1   ? 0.4214 0.2801 0.3796 0.0269  -0.0109 0.0076  -2  ALA A C   
4    O  O   . ALA A 1   ? 0.4763 0.3906 0.3635 -0.0124 -0.0070 0.0277  -2  ALA A O   
5    C  CB  . ALA A 1   ? 0.3770 0.2332 0.3403 -0.0076 0.0426  0.0184  -2  ALA A CB  
6    N  N   . MET A 2   ? 0.4840 0.3327 0.4296 0.0469  -0.0409 0.0058  -1  MET A N   
7    C  CA  . MET A 2   ? 0.5679 0.2924 0.5015 0.0247  -0.0305 0.0243  -1  MET A CA  
8    C  C   . MET A 2   ? 0.5352 0.3188 0.6065 0.0249  -0.0313 0.0317  -1  MET A C   
9    O  O   . MET A 2   ? 0.6186 0.3565 0.6578 0.0046  -0.0511 0.1397  -1  MET A O   
10   C  CB  . MET A 2   ? 0.6240 0.4229 0.5085 0.0468  -0.0344 0.0188  -1  MET A CB  
11   C  CG  . MET A 2   ? 0.6747 0.4545 0.5432 0.1050  -0.0145 -0.0298 -1  MET A CG  
12   S  SD  . MET A 2   ? 0.7588 0.5639 0.6344 0.1074  0.0316  -0.0801 -1  MET A SD  
13   C  CE  . MET A 2   ? 0.7683 0.5478 0.5732 0.1739  0.0639  -0.0389 -1  MET A CE  
14   N  N   . GLY A 3   ? 0.5244 0.2248 0.6251 0.0303  -0.0296 0.0097  0   GLY A N   
15   C  CA  . GLY A 3   ? 0.4980 0.2778 0.5373 0.0437  0.0145  0.0207  0   GLY A CA  
16   C  C   . GLY A 3   ? 0.4923 0.2867 0.5007 0.0619  0.0124  0.0514  0   GLY A C   
17   O  O   . GLY A 3   ? 0.5505 0.3368 0.5458 -0.0051 0.0667  0.1102  0   GLY A O   
18   N  N   . MET A 4   ? 0.4199 0.2563 0.4098 0.0591  0.0253  0.0143  1   MET A N   
19   C  CA  . MET A 4   ? 0.3653 0.2315 0.3551 0.0480  -0.0044 -0.0005 1   MET A CA  
20   C  C   . MET A 4   ? 0.3128 0.2290 0.2640 0.0380  -0.0010 0.0150  1   MET A C   
21   O  O   . MET A 4   ? 0.3354 0.2539 0.3204 0.0721  0.0298  0.0289  1   MET A O   
22   C  CB  . MET A 4   ? 0.3896 0.2977 0.4335 0.0188  -0.0120 0.0041  1   MET A CB  
23   C  CG  . MET A 4   ? 0.4395 0.3710 0.4951 -0.0008 -0.0178 0.0263  1   MET A CG  
24   S  SD  . MET A 4   ? 0.5213 0.5664 0.4861 -0.0714 -0.0830 0.0071  1   MET A SD  
25   C  CE  . MET A 4   ? 0.5118 0.6486 0.5518 -0.0447 -0.0616 -0.0173 1   MET A CE  
26   N  N   . LYS A 5   ? 0.2854 0.2272 0.2686 0.0476  -0.0070 0.0233  2   LYS A N   
27   C  CA  . LYS A 5   ? 0.2710 0.2116 0.2314 0.0447  0.0086  0.0168  2   LYS A CA  
28   C  C   . LYS A 5   ? 0.2361 0.1877 0.2267 0.0215  0.0117  0.0099  2   LYS A C   
29   O  O   . LYS A 5   ? 0.2384 0.2100 0.2330 0.0338  0.0210  0.0273  2   LYS A O   
30   C  CB  . LYS A 5   ? 0.2781 0.2708 0.3128 0.0357  -0.0083 0.0127  2   LYS A CB  
31   C  CG  . LYS A 5   ? 0.3162 0.3539 0.3984 0.0391  -0.0257 0.0021  2   LYS A CG  
32   C  CD  . LYS A 5   ? 0.3789 0.4317 0.4779 -0.0016 -0.0218 -0.0103 2   LYS A CD  
33   C  CE  . LYS A 5   ? 0.3102 0.4345 0.4988 -0.0262 -0.0440 -0.0601 2   LYS A CE  
34   N  N   . MET A 6   ? 0.1921 0.1884 0.2100 -0.0014 0.0130  0.0106  3   MET A N   
35   C  CA  . MET A 6   ? 0.1932 0.1628 0.2113 -0.0050 0.0126  0.0013  3   MET A CA  
36   C  C   . MET A 6   ? 0.1789 0.1595 0.1959 0.0043  0.0015  0.0082  3   MET A C   
37   O  O   . MET A 6   ? 0.2036 0.1642 0.1889 -0.0180 0.0136  -0.0033 3   MET A O   
38   C  CB  . MET A 6   ? 0.1851 0.1720 0.2235 0.0040  0.0004  0.0036  3   MET A CB  
39   C  CG  . MET A 6   ? 0.1901 0.1955 0.2430 0.0013  -0.0034 -0.0244 3   MET A CG  
40   S  SD  . MET A 6   ? 0.2630 0.3989 0.2996 0.0740  -0.0663 -0.0639 3   MET A SD  
41   C  CE  . MET A 6   ? 0.2893 0.4343 0.3667 0.0472  -0.0574 -0.0368 3   MET A CE  
42   N  N   . ILE A 7   ? 0.1764 0.1583 0.1803 -0.0134 0.0110  0.0038  4   ILE A N   
43   C  CA  . ILE A 7   ? 0.1607 0.1540 0.1754 -0.0089 0.0107  0.0045  4   ILE A CA  
44   C  C   . ILE A 7   ? 0.1392 0.1700 0.1769 0.0017  0.0154  -0.0066 4   ILE A C   
45   O  O   . ILE A 7   ? 0.1785 0.1878 0.1693 -0.0078 0.0236  0.0145  4   ILE A O   
46   C  CB  . ILE A 7   ? 0.1856 0.1788 0.1900 -0.0052 -0.0133 0.0010  4   ILE A CB  
47   C  CG1 . ILE A 7   ? 0.2126 0.1958 0.2045 -0.0048 -0.0275 -0.0072 4   ILE A CG1 
48   C  CG2 . ILE A 7   ? 0.1719 0.1888 0.2140 -0.0070 -0.0133 -0.0137 4   ILE A CG2 
49   C  CD1 . ILE A 7   ? 0.2138 0.1727 0.2235 0.0011  -0.0215 0.0111  4   ILE A CD1 
50   N  N   . VAL A 8   ? 0.1500 0.1611 0.1617 -0.0018 0.0121  -0.0011 5   VAL A N   
51   C  CA  . VAL A 8   ? 0.1412 0.1556 0.1591 -0.0021 0.0180  -0.0109 5   VAL A CA  
52   C  C   . VAL A 8   ? 0.1456 0.1530 0.1596 -0.0155 0.0214  -0.0123 5   VAL A C   
53   O  O   . VAL A 8   ? 0.1576 0.1612 0.1988 -0.0200 0.0416  -0.0108 5   VAL A O   
54   C  CB  . VAL A 8   ? 0.1849 0.1728 0.1595 0.0041  0.0101  -0.0085 5   VAL A CB  
55   C  CG1 . VAL A 8   ? 0.1947 0.1919 0.1697 0.0125  -0.0187 -0.0062 5   VAL A CG1 
56   C  CG2 . VAL A 8   ? 0.2227 0.1673 0.1662 -0.0116 -0.0021 -0.0042 5   VAL A CG2 
57   N  N   . GLY A 9   ? 0.1247 0.1448 0.1417 -0.0090 0.0103  -0.0054 6   GLY A N   
58   C  CA  . GLY A 9   ? 0.1243 0.1524 0.1387 -0.0227 0.0154  -0.0113 6   GLY A CA  
59   C  C   . GLY A 9   ? 0.1328 0.1454 0.1443 -0.0181 0.0055  -0.0046 6   GLY A C   
60   O  O   . GLY A 9   ? 0.1443 0.1539 0.1701 -0.0219 -0.0030 0.0073  6   GLY A O   
61   N  N   . LEU A 10  ? 0.1460 0.1426 0.1577 -0.0126 0.0037  -0.0030 7   LEU A N   
62   C  CA  . LEU A 10  ? 0.1486 0.1452 0.1529 -0.0079 0.0006  -0.0026 7   LEU A CA  
63   C  C   . LEU A 10  ? 0.1186 0.1484 0.1503 -0.0038 0.0063  0.0035  7   LEU A C   
64   O  O   . LEU A 10  ? 0.1199 0.1581 0.1591 -0.0139 0.0014  -0.0037 7   LEU A O   
65   C  CB  . LEU A 10  ? 0.1304 0.1557 0.1565 -0.0047 -0.0030 -0.0006 7   LEU A CB  
66   C  CG  . LEU A 10  ? 0.1289 0.1651 0.1521 -0.0027 0.0050  -0.0019 7   LEU A CG  
67   C  CD1 . LEU A 10  ? 0.1442 0.1739 0.1408 0.0010  0.0031  -0.0030 7   LEU A CD1 
68   C  CD2 . LEU A 10  ? 0.1461 0.1723 0.1592 -0.0029 -0.0005 -0.0123 7   LEU A CD2 
69   N  N   . GLY A 11  ? 0.1167 0.1600 0.1479 -0.0044 -0.0018 -0.0034 8   GLY A N   
70   C  CA  . GLY A 11  ? 0.1185 0.1598 0.1501 -0.0141 0.0155  0.0044  8   GLY A CA  
71   C  C   . GLY A 11  ? 0.1270 0.1646 0.1534 -0.0216 0.0062  -0.0007 8   GLY A C   
72   O  O   . GLY A 11  ? 0.1099 0.1833 0.1658 -0.0103 0.0006  -0.0054 8   GLY A O   
73   N  N   . ASN A 12  ? 0.1320 0.1765 0.1612 -0.0161 0.0052  -0.0132 9   ASN A N   
74   C  CA  . ASN A 12  ? 0.1345 0.1834 0.1613 -0.0211 -0.0046 -0.0068 9   ASN A CA  
75   C  C   . ASN A 12  ? 0.1324 0.1701 0.1683 -0.0210 0.0074  -0.0108 9   ASN A C   
76   O  O   . ASN A 12  ? 0.1586 0.1984 0.1607 -0.0219 0.0253  -0.0026 9   ASN A O   
77   C  CB  . ASN A 12  ? 0.1390 0.1882 0.1771 -0.0095 0.0017  -0.0070 9   ASN A CB  
78   C  CG  . ASN A 12  ? 0.1339 0.1846 0.1765 -0.0010 0.0192  -0.0114 9   ASN A CG  
79   O  OD1 . ASN A 12  ? 0.1799 0.2036 0.2043 -0.0130 0.0279  -0.0130 9   ASN A OD1 
80   N  ND2 . ASN A 12  ? 0.1690 0.2052 0.1682 -0.0230 -0.0002 -0.0031 9   ASN A ND2 
81   N  N   . PRO A 13  ? 0.1246 0.1837 0.1567 -0.0188 0.0128  -0.0180 10  PRO A N   
82   C  CA  . PRO A 13  ? 0.1175 0.1906 0.1770 -0.0124 0.0175  -0.0008 10  PRO A CA  
83   C  C   . PRO A 13  ? 0.1284 0.2110 0.2015 -0.0070 0.0110  -0.0044 10  PRO A C   
84   O  O   . PRO A 13  ? 0.1398 0.2020 0.2354 -0.0010 0.0210  -0.0150 10  PRO A O   
85   C  CB  . PRO A 13  ? 0.1288 0.2059 0.1917 -0.0254 0.0215  -0.0066 10  PRO A CB  
86   C  CG  . PRO A 13  ? 0.1306 0.2011 0.1829 -0.0266 0.0038  -0.0079 10  PRO A CG  
87   C  CD  . PRO A 13  ? 0.1191 0.2097 0.1715 -0.0172 -0.0003 -0.0044 10  PRO A CD  
88   N  N   . GLY A 14  ? 0.1599 0.2258 0.2185 -0.0052 0.0293  -0.0152 11  GLY A N   
89   C  CA  . GLY A 14  ? 0.1365 0.2636 0.2295 0.0115  0.0321  -0.0186 11  GLY A CA  
90   C  C   . GLY A 14  ? 0.1523 0.2254 0.2283 0.0098  0.0467  -0.0242 11  GLY A C   
91   O  O   . GLY A 14  ? 0.1640 0.2028 0.2519 -0.0232 0.0269  -0.0316 11  GLY A O   
92   N  N   . THR A 15  ? 0.1520 0.2477 0.2093 0.0057  0.0372  -0.0244 12  THR A N   
93   C  CA  . THR A 15  ? 0.1595 0.2433 0.2282 -0.0103 0.0418  -0.0331 12  THR A CA  
94   C  C   . THR A 15  ? 0.1519 0.2629 0.2361 0.0036  0.0452  -0.0267 12  THR A C   
95   O  O   . THR A 15  ? 0.1699 0.2877 0.2926 -0.0211 0.0641  -0.0782 12  THR A O   
96   C  CB  . THR A 15  ? 0.1622 0.2432 0.2046 -0.0049 0.0232  -0.0287 12  THR A CB  
97   O  OG1 . THR A 15  ? 0.1523 0.2276 0.2333 -0.0046 0.0321  -0.0298 12  THR A OG1 
98   C  CG2 . THR A 15  ? 0.1966 0.2612 0.1803 0.0166  0.0460  -0.0076 12  THR A CG2 
99   N  N   . LYS A 16  ? 0.1741 0.2578 0.2617 -0.0051 0.0301  -0.0076 13  LYS A N   
100  C  CA  . LYS A 16  ? 0.1826 0.2987 0.2875 0.0172  0.0262  0.0298  13  LYS A CA  
101  C  C   . LYS A 16  ? 0.1755 0.2457 0.3241 0.0121  0.0512  0.0017  13  LYS A C   
102  O  O   . LYS A 16  ? 0.2395 0.2317 0.3971 0.0059  0.0463  -0.0148 13  LYS A O   
103  C  CB  . LYS A 16  ? 0.2160 0.3362 0.2630 0.0244  0.0289  0.0023  13  LYS A CB  
104  C  CG  . LYS A 16  ? 0.3319 0.3820 0.3049 0.0080  0.0386  -0.0077 13  LYS A CG  
105  C  CD  . LYS A 16  ? 0.3684 0.4421 0.3263 0.0276  0.0486  0.0074  13  LYS A CD  
106  C  CE  . LYS A 16  ? 0.3890 0.5177 0.3720 0.0615  0.0493  0.0334  13  LYS A CE  
107  N  NZ  . LYS A 16  ? 0.5024 0.5384 0.3491 0.0315  0.0713  0.0594  13  LYS A NZ  
108  N  N   . TYR A 17  ? 0.1363 0.2077 0.2884 0.0066  0.0509  0.0198  14  TYR A N   
109  C  CA  . TYR A 17  ? 0.1246 0.1983 0.2404 -0.0213 0.0283  0.0022  14  TYR A CA  
110  C  C   . TYR A 17  ? 0.1436 0.2078 0.2106 -0.0173 0.0155  -0.0136 14  TYR A C   
111  O  O   . TYR A 17  ? 0.1215 0.1965 0.1964 -0.0182 0.0297  -0.0122 14  TYR A O   
112  C  CB  . TYR A 17  ? 0.1372 0.1866 0.2294 -0.0115 0.0046  0.0006  14  TYR A CB  
113  C  CG  . TYR A 17  ? 0.1625 0.1873 0.2349 -0.0084 0.0088  0.0231  14  TYR A CG  
114  C  CD1 . TYR A 17  ? 0.1984 0.2094 0.2495 -0.0132 0.0103  0.0298  14  TYR A CD1 
115  C  CD2 . TYR A 17  ? 0.1803 0.2013 0.2220 -0.0023 0.0111  0.0049  14  TYR A CD2 
116  C  CE1 . TYR A 17  ? 0.2134 0.2137 0.2708 0.0077  0.0018  0.0258  14  TYR A CE1 
117  C  CE2 . TYR A 17  ? 0.1925 0.2273 0.2611 0.0201  0.0005  0.0042  14  TYR A CE2 
118  C  CZ  . TYR A 17  ? 0.1934 0.2202 0.2553 0.0153  -0.0171 0.0259  14  TYR A CZ  
119  O  OH  . TYR A 17  ? 0.2485 0.2669 0.2705 0.0450  -0.0084 0.0537  14  TYR A OH  
120  N  N   . GLN A 18  ? 0.1476 0.2348 0.2245 -0.0342 0.0036  -0.0036 15  GLN A N   
121  C  CA  . GLN A 18  ? 0.2018 0.2348 0.1981 -0.0273 0.0065  -0.0094 15  GLN A CA  
122  C  C   . GLN A 18  ? 0.1901 0.2148 0.1983 -0.0118 0.0122  0.0000  15  GLN A C   
123  O  O   . GLN A 18  ? 0.1709 0.2424 0.2187 -0.0026 0.0018  -0.0184 15  GLN A O   
124  C  CB  . GLN A 18  ? 0.2516 0.2640 0.2509 -0.0411 0.0085  0.0034  15  GLN A CB  
125  C  CG  . GLN A 18  ? 0.2781 0.3157 0.2689 -0.0419 -0.0032 -0.0141 15  GLN A CG  
126  C  CD  . GLN A 18  ? 0.3539 0.3154 0.3472 -0.0681 0.0155  0.0120  15  GLN A CD  
127  O  OE1 . GLN A 18  ? 0.3741 0.3343 0.4083 -0.1062 0.0742  0.0408  15  GLN A OE1 
128  N  NE2 . GLN A 18  ? 0.3633 0.3542 0.3907 -0.0277 0.0436  0.0059  15  GLN A NE2 
129  N  N   . TYR A 19  ? 0.1978 0.2224 0.1864 -0.0282 0.0294  -0.0207 16  TYR A N   
130  C  CA  . TYR A 19  ? 0.1986 0.2209 0.1953 -0.0073 -0.0095 -0.0351 16  TYR A CA  
131  C  C   . TYR A 19  ? 0.1903 0.2248 0.2043 -0.0116 -0.0149 -0.0334 16  TYR A C   
132  O  O   . TYR A 19  ? 0.2239 0.2318 0.2204 -0.0356 -0.0390 -0.0298 16  TYR A O   
133  C  CB  . TYR A 19  ? 0.2269 0.2717 0.1796 0.0000  -0.0035 -0.0346 16  TYR A CB  
134  C  CG  . TYR A 19  ? 0.2366 0.3198 0.2444 -0.0282 0.0216  -0.0188 16  TYR A CG  
135  C  CD1 . TYR A 19  ? 0.2804 0.3900 0.2684 -0.0360 0.0270  0.0454  16  TYR A CD1 
136  C  CD2 . TYR A 19  ? 0.2515 0.3973 0.2769 -0.0038 0.0416  0.0081  16  TYR A CD2 
137  C  CE1 . TYR A 19  ? 0.3171 0.4521 0.3006 -0.0356 0.0517  0.0748  16  TYR A CE1 
138  C  CE2 . TYR A 19  ? 0.3130 0.4578 0.3218 -0.0367 0.0509  0.0383  16  TYR A CE2 
139  C  CZ  . TYR A 19  ? 0.3382 0.4553 0.2918 -0.0184 0.0697  0.0506  16  TYR A CZ  
140  O  OH  . TYR A 19  ? 0.3787 0.5011 0.3208 -0.0476 0.0922  0.0650  16  TYR A OH  
141  N  N   . THR A 20  ? 0.1310 0.1940 0.1898 -0.0069 0.0097  -0.0227 17  THR A N   
142  C  CA  . THR A 20  ? 0.1464 0.1686 0.1930 -0.0003 0.0113  -0.0223 17  THR A CA  
143  C  C   . THR A 20  ? 0.1266 0.1668 0.1713 -0.0093 -0.0126 -0.0139 17  THR A C   
144  O  O   . THR A 20  ? 0.1277 0.1613 0.1678 -0.0065 0.0004  -0.0139 17  THR A O   
145  C  CB  . THR A 20  ? 0.1122 0.1821 0.2107 -0.0059 0.0123  -0.0065 17  THR A CB  
146  O  OG1 . THR A 20  ? 0.1233 0.1881 0.1853 -0.0039 0.0042  -0.0166 17  THR A OG1 
147  C  CG2 . THR A 20  ? 0.1045 0.1979 0.2525 0.0008  -0.0058 -0.0176 17  THR A CG2 
148  N  N   . LYS A 21  ? 0.1040 0.1694 0.1821 0.0003  0.0103  -0.0129 18  LYS A N   
149  C  CA  . LYS A 21  ? 0.0889 0.1684 0.1735 0.0023  -0.0114 -0.0088 18  LYS A CA  
150  C  C   . LYS A 21  ? 0.1247 0.1674 0.1711 0.0055  0.0052  0.0058  18  LYS A C   
151  O  O   . LYS A 21  ? 0.1152 0.1581 0.1824 -0.0009 -0.0026 0.0017  18  LYS A O   
152  C  CB  . LYS A 21  ? 0.1177 0.1729 0.1876 0.0025  -0.0124 -0.0047 18  LYS A CB  
153  C  CG  . LYS A 21  ? 0.1314 0.1849 0.2047 0.0000  -0.0159 -0.0114 18  LYS A CG  
154  C  CD  . LYS A 21  ? 0.1349 0.1807 0.1980 -0.0080 -0.0240 -0.0187 18  LYS A CD  
155  C  CE  . LYS A 21  ? 0.1409 0.1812 0.2253 -0.0079 -0.0122 -0.0201 18  LYS A CE  
156  N  NZ  . LYS A 21  ? 0.1466 0.1766 0.2272 0.0113  -0.0083 -0.0206 18  LYS A NZ  
157  N  N   . HIS A 22  ? 0.1174 0.1608 0.1711 -0.0005 -0.0081 0.0020  19  HIS A N   
158  C  CA  . HIS A 22  ? 0.1301 0.1614 0.1603 0.0033  -0.0084 0.0079  19  HIS A CA  
159  C  C   . HIS A 22  ? 0.1339 0.1645 0.1736 -0.0065 0.0050  -0.0049 19  HIS A C   
160  O  O   . HIS A 22  ? 0.1774 0.1521 0.1679 0.0059  0.0118  -0.0030 19  HIS A O   
161  C  CB  . HIS A 22  ? 0.1013 0.1730 0.1793 -0.0060 -0.0186 -0.0055 19  HIS A CB  
162  C  CG  . HIS A 22  ? 0.1261 0.1587 0.1907 0.0000  -0.0095 -0.0027 19  HIS A CG  
163  N  ND1 . HIS A 22  ? 0.1841 0.1581 0.1680 0.0078  0.0178  0.0017  19  HIS A ND1 
164  C  CD2 . HIS A 22  ? 0.1502 0.1833 0.2128 0.0092  -0.0240 0.0005  19  HIS A CD2 
165  C  CE1 . HIS A 22  ? 0.1896 0.1710 0.1862 0.0123  -0.0164 0.0122  19  HIS A CE1 
166  N  NE2 . HIS A 22  ? 0.2097 0.1799 0.2218 0.0057  -0.0288 -0.0122 19  HIS A NE2 
167  N  N   . ASN A 23  ? 0.1245 0.1456 0.1580 -0.0058 0.0023  -0.0065 20  ASN A N   
168  C  CA  . ASN A 23  ? 0.1553 0.1491 0.1466 -0.0106 0.0151  -0.0118 20  ASN A CA  
169  C  C   . ASN A 23  ? 0.1519 0.1545 0.1464 -0.0127 0.0156  -0.0098 20  ASN A C   
170  O  O   . ASN A 23  ? 0.1538 0.1545 0.1508 -0.0148 0.0057  0.0015  20  ASN A O   
171  C  CB  . ASN A 23  ? 0.1348 0.1762 0.1544 -0.0272 0.0109  -0.0145 20  ASN A CB  
172  C  CG  . ASN A 23  ? 0.1342 0.1638 0.1663 -0.0044 0.0029  -0.0085 20  ASN A CG  
173  O  OD1 . ASN A 23  ? 0.1402 0.1632 0.1587 -0.0203 0.0030  -0.0051 20  ASN A OD1 
174  N  ND2 . ASN A 23  ? 0.1507 0.1805 0.1709 -0.0167 -0.0049 0.0103  20  ASN A ND2 
175  N  N   . ILE A 24  ? 0.1399 0.1496 0.1505 -0.0106 0.0056  0.0049  21  ILE A N   
176  C  CA  . ILE A 24  ? 0.1521 0.1502 0.1664 0.0025  0.0064  0.0030  21  ILE A CA  
177  C  C   . ILE A 24  ? 0.1356 0.1451 0.1436 -0.0039 0.0062  0.0000  21  ILE A C   
178  O  O   . ILE A 24  ? 0.1422 0.1536 0.1492 -0.0061 -0.0035 0.0085  21  ILE A O   
179  C  CB  . ILE A 24  ? 0.1349 0.1585 0.1795 0.0001  -0.0077 0.0042  21  ILE A CB  
180  C  CG1 . ILE A 24  ? 0.1283 0.1710 0.1994 0.0076  -0.0221 -0.0058 21  ILE A CG1 
181  C  CG2 . ILE A 24  ? 0.1373 0.1675 0.1811 -0.0158 -0.0017 0.0140  21  ILE A CG2 
182  C  CD1 . ILE A 24  ? 0.1345 0.1955 0.2034 -0.0145 -0.0471 -0.0135 21  ILE A CD1 
183  N  N   . GLY A 25  ? 0.1393 0.1474 0.1431 -0.0107 0.0093  0.0008  22  GLY A N   
184  C  CA  . GLY A 25  ? 0.1378 0.1596 0.1475 0.0085  -0.0069 0.0072  22  GLY A CA  
185  C  C   . GLY A 25  ? 0.1513 0.1460 0.1417 -0.0047 -0.0052 -0.0061 22  GLY A C   
186  O  O   . GLY A 25  ? 0.1674 0.1502 0.1433 0.0010  -0.0015 -0.0035 22  GLY A O   
187  N  N   . PHE A 26  ? 0.1360 0.1609 0.1185 -0.0069 0.0076  0.0055  23  PHE A N   
188  C  CA  . PHE A 26  ? 0.1549 0.1632 0.1410 -0.0176 0.0055  -0.0009 23  PHE A CA  
189  C  C   . PHE A 26  ? 0.1500 0.1662 0.1474 -0.0072 0.0091  0.0049  23  PHE A C   
190  O  O   . PHE A 26  ? 0.1753 0.1768 0.1575 -0.0202 -0.0058 0.0099  23  PHE A O   
191  C  CB  . PHE A 26  ? 0.1535 0.1691 0.1509 -0.0250 0.0067  -0.0039 23  PHE A CB  
192  C  CG  . PHE A 26  ? 0.1274 0.1572 0.1569 -0.0181 -0.0044 0.0024  23  PHE A CG  
193  C  CD1 . PHE A 26  ? 0.1498 0.1572 0.1558 -0.0173 -0.0160 0.0086  23  PHE A CD1 
194  C  CD2 . PHE A 26  ? 0.1398 0.1818 0.1686 -0.0090 0.0023  -0.0037 23  PHE A CD2 
195  C  CE1 . PHE A 26  ? 0.1481 0.1684 0.1605 -0.0154 -0.0150 0.0118  23  PHE A CE1 
196  C  CE2 . PHE A 26  ? 0.1506 0.1987 0.1956 -0.0062 -0.0159 0.0036  23  PHE A CE2 
197  C  CZ  . PHE A 26  ? 0.1579 0.1696 0.1702 -0.0117 -0.0147 0.0038  23  PHE A CZ  
198  N  N   . MET A 27  ? 0.1481 0.1739 0.1317 -0.0119 0.0102  0.0010  24  MET A N   
199  C  CA  . MET A 27  ? 0.1683 0.1894 0.1353 -0.0083 -0.0014 -0.0004 24  MET A CA  
200  C  C   . MET A 27  ? 0.1883 0.1615 0.1368 -0.0119 0.0020  -0.0168 24  MET A C   
201  O  O   . MET A 27  ? 0.2003 0.1953 0.1395 -0.0163 0.0039  0.0062  24  MET A O   
202  C  CB  . MET A 27  ? 0.1892 0.1788 0.1370 0.0035  0.0000  -0.0064 24  MET A CB  
203  C  CG  . MET A 27  ? 0.2030 0.1927 0.1653 0.0092  -0.0183 -0.0234 24  MET A CG  
204  S  SD  . MET A 27  ? 0.2143 0.2206 0.2555 -0.0015 -0.0138 -0.0268 24  MET A SD  
205  C  CE  . MET A 27  ? 0.2373 0.2306 0.3045 0.0028  -0.0457 -0.0012 24  MET A CE  
206  N  N   . VAL A 28  ? 0.1769 0.1706 0.1318 -0.0145 0.0027  -0.0004 25  VAL A N   
207  C  CA  . VAL A 28  ? 0.1728 0.1860 0.1426 -0.0068 -0.0030 0.0027  25  VAL A CA  
208  C  C   . VAL A 28  ? 0.1386 0.1757 0.1283 -0.0075 0.0015  0.0056  25  VAL A C   
209  O  O   . VAL A 28  ? 0.1721 0.1822 0.1457 -0.0098 -0.0003 0.0158  25  VAL A O   
210  C  CB  . VAL A 28  ? 0.1526 0.1710 0.1541 -0.0124 -0.0098 0.0051  25  VAL A CB  
211  C  CG1 . VAL A 28  ? 0.1629 0.1864 0.1638 -0.0035 0.0070  0.0142  25  VAL A CG1 
212  C  CG2 . VAL A 28  ? 0.1547 0.1747 0.1661 -0.0166 -0.0179 0.0139  25  VAL A CG2 
213  N  N   . VAL A 29  ? 0.1486 0.1655 0.1413 -0.0115 -0.0069 0.0049  26  VAL A N   
214  C  CA  . VAL A 29  ? 0.1725 0.1678 0.1428 -0.0171 -0.0076 0.0065  26  VAL A CA  
215  C  C   . VAL A 29  ? 0.1580 0.1852 0.1527 -0.0117 -0.0061 0.0006  26  VAL A C   
216  O  O   . VAL A 29  ? 0.1973 0.1722 0.1508 -0.0150 -0.0058 0.0132  26  VAL A O   
217  C  CB  . VAL A 29  ? 0.2011 0.1711 0.1601 -0.0166 -0.0072 -0.0072 26  VAL A CB  
218  C  CG1 . VAL A 29  ? 0.2157 0.1766 0.1634 0.0025  -0.0183 -0.0133 26  VAL A CG1 
219  C  CG2 . VAL A 29  ? 0.2051 0.1739 0.1431 -0.0229 0.0109  -0.0081 26  VAL A CG2 
220  N  N   . ASP A 30  ? 0.2032 0.1707 0.1368 -0.0149 0.0134  0.0080  27  ASP A N   
221  C  CA  . ASP A 30  ? 0.2239 0.1965 0.1558 -0.0263 0.0290  0.0030  27  ASP A CA  
222  C  C   . ASP A 30  ? 0.2397 0.1860 0.1311 -0.0226 0.0171  0.0016  27  ASP A C   
223  O  O   . ASP A 30  ? 0.2550 0.2199 0.1445 -0.0254 0.0173  0.0154  27  ASP A O   
224  C  CB  . ASP A 30  ? 0.2327 0.2209 0.1819 -0.0182 0.0512  0.0121  27  ASP A CB  
225  C  CG  . ASP A 30  ? 0.2512 0.2467 0.2192 0.0063  0.0540  0.0157  27  ASP A CG  
226  O  OD1 . ASP A 30  ? 0.2734 0.3170 0.2321 -0.0104 0.0133  -0.0031 27  ASP A OD1 
227  O  OD2 . ASP A 30  ? 0.3003 0.3108 0.2861 0.0594  0.0190  -0.0114 27  ASP A OD2 
228  N  N   . LYS A 31  ? 0.2413 0.2025 0.1342 -0.0199 0.0014  0.0048  28  LYS A N   
229  C  CA  . LYS A 31  ? 0.2580 0.2363 0.1393 -0.0330 -0.0020 0.0115  28  LYS A CA  
230  C  C   . LYS A 31  ? 0.2439 0.2153 0.1671 -0.0480 -0.0176 0.0167  28  LYS A C   
231  O  O   . LYS A 31  ? 0.2773 0.2424 0.1736 -0.0400 -0.0327 0.0352  28  LYS A O   
232  C  CB  . LYS A 31  ? 0.2550 0.2886 0.1796 -0.0524 0.0212  0.0256  28  LYS A CB  
233  C  CG  . LYS A 31  ? 0.3044 0.3557 0.2403 -0.0648 0.0064  0.0316  28  LYS A CG  
234  C  CD  . LYS A 31  ? 0.3205 0.3188 0.1980 -0.0687 0.0060  0.0057  28  LYS A CD  
235  C  CE  . LYS A 31  ? 0.3403 0.3770 0.2476 -0.0595 0.0071  0.0079  28  LYS A CE  
236  N  NZ  . LYS A 31  ? 0.3431 0.3757 0.2348 -0.0674 0.0030  0.0111  28  LYS A NZ  
237  N  N   . ILE A 32  ? 0.2290 0.2068 0.1704 -0.0280 -0.0103 0.0010  29  ILE A N   
238  C  CA  . ILE A 32  ? 0.2423 0.2169 0.1743 -0.0172 -0.0300 0.0206  29  ILE A CA  
239  C  C   . ILE A 32  ? 0.2383 0.2148 0.1752 -0.0183 -0.0339 0.0280  29  ILE A C   
240  O  O   . ILE A 32  ? 0.2956 0.2366 0.2172 -0.0344 -0.0531 0.0530  29  ILE A O   
241  C  CB  . ILE A 32  ? 0.2191 0.2080 0.1839 -0.0010 -0.0332 0.0158  29  ILE A CB  
242  C  CG1 . ILE A 32  ? 0.2194 0.2010 0.1990 -0.0007 -0.0380 0.0144  29  ILE A CG1 
243  C  CG2 . ILE A 32  ? 0.2619 0.2037 0.2047 0.0055  -0.0383 0.0225  29  ILE A CG2 
244  C  CD1 . ILE A 32  ? 0.2171 0.2269 0.2111 0.0013  -0.0096 0.0012  29  ILE A CD1 
245  N  N   . ALA A 33  ? 0.2408 0.2249 0.1580 -0.0263 -0.0242 0.0349  30  ALA A N   
246  C  CA  . ALA A 33  ? 0.2793 0.2339 0.1664 -0.0280 -0.0126 0.0308  30  ALA A CA  
247  C  C   . ALA A 33  ? 0.3288 0.2273 0.1659 -0.0503 0.0038  0.0330  30  ALA A C   
248  O  O   . ALA A 33  ? 0.3648 0.2439 0.1773 -0.0531 -0.0286 0.0478  30  ALA A O   
249  C  CB  . ALA A 33  ? 0.2707 0.2263 0.1594 -0.0308 -0.0010 0.0432  30  ALA A CB  
250  N  N   . ARG A 34  ? 0.3287 0.2286 0.1613 -0.0558 -0.0150 0.0294  31  ARG A N   
251  C  CA  . ARG A 34  ? 0.3418 0.2698 0.1723 -0.0542 -0.0065 0.0238  31  ARG A CA  
252  C  C   . ARG A 34  ? 0.3768 0.2631 0.1697 -0.0450 -0.0351 0.0292  31  ARG A C   
253  O  O   . ARG A 34  ? 0.4344 0.3127 0.1816 -0.0449 -0.0483 0.0605  31  ARG A O   
254  C  CB  . ARG A 34  ? 0.3643 0.2961 0.1593 -0.0267 -0.0141 0.0213  31  ARG A CB  
255  C  CG  . ARG A 34  ? 0.3797 0.3218 0.1847 -0.0358 -0.0091 0.0079  31  ARG A CG  
256  C  CD  . ARG A 34  ? 0.4286 0.3429 0.1832 -0.0006 0.0154  0.0054  31  ARG A CD  
257  N  NE  . ARG A 34  ? 0.4539 0.3682 0.2522 -0.0096 0.0000  0.0274  31  ARG A NE  
258  C  CZ  . ARG A 34  ? 0.4407 0.3607 0.2598 0.0119  -0.0079 0.0238  31  ARG A CZ  
259  N  NH1 . ARG A 34  ? 0.5131 0.4193 0.2563 0.0633  -0.0430 -0.0026 31  ARG A NH1 
260  N  NH2 . ARG A 34  ? 0.4725 0.3678 0.2491 0.0409  0.0447  0.0262  31  ARG A NH2 
261  N  N   . GLU A 35  ? 0.3396 0.2553 0.2066 -0.0209 -0.0630 0.0208  32  GLU A N   
262  C  CA  . GLU A 35  ? 0.3485 0.2920 0.2068 -0.0111 -0.0587 0.0332  32  GLU A CA  
263  C  C   . GLU A 35  ? 0.3707 0.2823 0.2513 -0.0082 -0.0802 0.0273  32  GLU A C   
264  O  O   . GLU A 35  ? 0.3616 0.2805 0.2731 0.0163  -0.0392 0.0454  32  GLU A O   
265  C  CB  . GLU A 35  ? 0.3406 0.3228 0.2645 -0.0250 -0.0566 0.0214  32  GLU A CB  
266  C  CG  . GLU A 35  ? 0.3799 0.3477 0.2970 0.0057  -0.0376 0.0175  32  GLU A CG  
267  C  CD  . GLU A 35  ? 0.3893 0.3794 0.3127 -0.0131 -0.0475 0.0435  32  GLU A CD  
268  O  OE1 . GLU A 35  ? 0.3551 0.3722 0.2976 -0.0256 -0.0547 0.0487  32  GLU A OE1 
269  O  OE2 . GLU A 35  ? 0.4003 0.4196 0.3932 0.0214  -0.0384 0.0823  32  GLU A OE2 
270  N  N   . HIS A 36  ? 0.3965 0.2446 0.2528 -0.0477 -0.0953 0.0566  33  HIS A N   
271  C  CA  . HIS A 36  ? 0.4209 0.2516 0.2684 -0.0354 -0.0920 0.0400  33  HIS A CA  
272  C  C   . HIS A 36  ? 0.4435 0.2727 0.2493 -0.0495 -0.0663 0.0571  33  HIS A C   
273  O  O   . HIS A 36  ? 0.5013 0.2527 0.2958 -0.0653 -0.0518 0.0621  33  HIS A O   
274  C  CB  . HIS A 36  ? 0.4753 0.2548 0.3180 -0.0144 -0.0656 0.0328  33  HIS A CB  
275  C  CG  . HIS A 36  ? 0.4623 0.2808 0.3093 -0.0165 -0.0743 0.0454  33  HIS A CG  
276  N  ND1 . HIS A 36  ? 0.5022 0.2749 0.4386 -0.0087 -0.0536 0.0852  33  HIS A ND1 
277  C  CD2 . HIS A 36  ? 0.4639 0.2429 0.3664 -0.0127 -0.0633 0.0392  33  HIS A CD2 
278  C  CE1 . HIS A 36  ? 0.4864 0.3100 0.4280 -0.0249 -0.0631 0.0810  33  HIS A CE1 
279  N  NE2 . HIS A 36  ? 0.4696 0.2746 0.3631 0.0053  -0.0469 0.0432  33  HIS A NE2 
280  N  N   . GLN A 37  ? 0.4515 0.2553 0.2715 -0.0652 -0.0531 0.0645  34  GLN A N   
281  C  CA  . GLN A 37  ? 0.4726 0.2868 0.2509 -0.0788 -0.0077 0.0690  34  GLN A CA  
282  C  C   . GLN A 37  ? 0.4802 0.2577 0.2971 -0.1020 -0.0007 0.0811  34  GLN A C   
283  O  O   . GLN A 37  ? 0.4806 0.3476 0.2991 -0.1519 -0.0118 0.0656  34  GLN A O   
284  C  CB  . GLN A 37  ? 0.5178 0.3071 0.3153 -0.0658 -0.0063 0.1036  34  GLN A CB  
285  N  N   . ALA A 38  ? 0.4081 0.2782 0.2567 -0.0961 0.0066  0.0616  35  ALA A N   
286  C  CA  . ALA A 38  ? 0.3718 0.2744 0.2852 -0.0753 -0.0115 0.0596  35  ALA A CA  
287  C  C   . ALA A 38  ? 0.3759 0.2731 0.2911 -0.0559 0.0161  0.0552  35  ALA A C   
288  O  O   . ALA A 38  ? 0.3987 0.2824 0.3788 -0.0548 0.0295  0.0269  35  ALA A O   
289  C  CB  . ALA A 38  ? 0.3571 0.2657 0.2965 -0.0698 -0.0403 0.0201  35  ALA A CB  
290  N  N   A THR A 39  ? 0.3545 0.3215 0.2851 -0.0684 0.0355  0.0782  36  THR A N   
291  N  N   B THR A 39  ? 0.3557 0.3225 0.2855 -0.0685 0.0351  0.0779  36  THR A N   
292  C  CA  A THR A 39  ? 0.3540 0.3509 0.2962 -0.0600 0.0384  0.0617  36  THR A CA  
293  C  CA  B THR A 39  ? 0.3559 0.3524 0.2964 -0.0600 0.0380  0.0615  36  THR A CA  
294  C  C   A THR A 39  ? 0.2926 0.3048 0.2821 -0.0736 0.0442  0.0621  36  THR A C   
295  C  C   B THR A 39  ? 0.2942 0.3061 0.2828 -0.0733 0.0437  0.0620  36  THR A C   
296  O  O   A THR A 39  ? 0.3237 0.2958 0.3238 -0.0773 0.0535  0.0593  36  THR A O   
297  O  O   B THR A 39  ? 0.3271 0.2988 0.3263 -0.0769 0.0527  0.0580  36  THR A O   
298  C  CB  A THR A 39  ? 0.3792 0.4505 0.3185 -0.0589 0.0517  0.0923  36  THR A CB  
299  C  CB  B THR A 39  ? 0.3822 0.4524 0.3171 -0.0594 0.0512  0.0923  36  THR A CB  
300  O  OG1 A THR A 39  ? 0.4189 0.5244 0.3453 -0.0662 0.0408  0.1185  36  THR A OG1 
301  O  OG1 B THR A 39  ? 0.4229 0.5293 0.3431 -0.0668 0.0408  0.1179  36  THR A OG1 
302  C  CG2 A THR A 39  ? 0.3651 0.4800 0.3257 -0.0464 0.0441  0.0873  36  THR A CG2 
303  C  CG2 B THR A 39  ? 0.3692 0.4813 0.3209 -0.0470 0.0432  0.0876  36  THR A CG2 
304  N  N   . PHE A 40  ? 0.2699 0.2797 0.2483 -0.0637 0.0311  0.0370  37  PHE A N   
305  C  CA  . PHE A 40  ? 0.2692 0.2539 0.2583 -0.0448 0.0222  0.0357  37  PHE A CA  
306  C  C   . PHE A 40  ? 0.2653 0.2579 0.2701 -0.0406 0.0097  0.0241  37  PHE A C   
307  O  O   . PHE A 40  ? 0.2969 0.3028 0.3182 -0.0593 0.0236  -0.0209 37  PHE A O   
308  C  CB  . PHE A 40  ? 0.2582 0.2423 0.2427 -0.0304 -0.0021 0.0404  37  PHE A CB  
309  C  CG  . PHE A 40  ? 0.2370 0.2129 0.2289 -0.0342 -0.0195 0.0282  37  PHE A CG  
310  C  CD1 . PHE A 40  ? 0.2280 0.1997 0.2245 -0.0603 -0.0247 0.0102  37  PHE A CD1 
311  C  CD2 . PHE A 40  ? 0.2764 0.2300 0.1859 -0.0385 -0.0049 0.0457  37  PHE A CD2 
312  C  CE1 . PHE A 40  ? 0.2175 0.1839 0.2181 -0.0415 -0.0009 0.0342  37  PHE A CE1 
313  C  CE2 . PHE A 40  ? 0.2504 0.2093 0.2831 -0.0375 -0.0306 0.0193  37  PHE A CE2 
314  C  CZ  . PHE A 40  ? 0.2491 0.2063 0.2720 -0.0474 -0.0210 0.0380  37  PHE A CZ  
315  N  N   . LYS A 41  ? 0.2535 0.2774 0.2519 -0.0919 -0.0038 0.0549  38  LYS A N   
316  C  CA  . LYS A 41  ? 0.2478 0.2789 0.2615 -0.0923 0.0073  0.0523  38  LYS A CA  
317  C  C   . LYS A 41  ? 0.2345 0.2920 0.2669 -0.0582 0.0002  0.0721  38  LYS A C   
318  O  O   . LYS A 41  ? 0.2367 0.2875 0.2597 -0.0865 -0.0126 0.0826  38  LYS A O   
319  C  CB  . LYS A 41  ? 0.3554 0.3007 0.2901 -0.1136 0.0038  0.0732  38  LYS A CB  
320  C  CG  . LYS A 41  ? 0.3944 0.3703 0.3244 -0.1067 -0.0255 0.0563  38  LYS A CG  
321  N  N   . LYS A 42  ? 0.2406 0.3037 0.2984 -0.0558 0.0290  0.0395  39  LYS A N   
322  C  CA  . LYS A 42  ? 0.2677 0.3247 0.3193 -0.0610 0.0092  0.0300  39  LYS A CA  
323  C  C   . LYS A 42  ? 0.2371 0.2893 0.2749 -0.0732 0.0044  0.0414  39  LYS A C   
324  O  O   . LYS A 42  ? 0.3851 0.3001 0.3171 -0.0931 0.0354  0.0806  39  LYS A O   
325  C  CB  . LYS A 42  ? 0.2874 0.3817 0.3479 -0.0542 0.0239  0.0225  39  LYS A CB  
326  C  CG  . LYS A 42  ? 0.3790 0.3991 0.3379 -0.0317 0.0217  0.0162  39  LYS A CG  
327  N  N   . ASN A 43  ? 0.2877 0.2587 0.2692 -0.0895 -0.0087 0.0536  40  ASN A N   
328  C  CA  . ASN A 43  ? 0.2875 0.2446 0.2987 -0.1053 -0.0288 0.0617  40  ASN A CA  
329  C  C   . ASN A 43  ? 0.2654 0.2676 0.2873 -0.0848 -0.0389 0.0265  40  ASN A C   
330  O  O   . ASN A 43  ? 0.2525 0.2670 0.3009 -0.0551 -0.0238 0.0112  40  ASN A O   
331  C  CB  . ASN A 43  ? 0.2612 0.2993 0.3123 -0.0968 -0.0615 0.0593  40  ASN A CB  
332  C  CG  . ASN A 43  ? 0.3041 0.3288 0.3699 -0.1085 -0.0658 0.0594  40  ASN A CG  
333  O  OD1 . ASN A 43  ? 0.3302 0.3572 0.3647 -0.0697 -0.0648 0.0819  40  ASN A OD1 
334  N  ND2 . ASN A 43  ? 0.3467 0.3448 0.3818 -0.0949 -0.0896 0.0754  40  ASN A ND2 
335  N  N   . PRO A 44  ? 0.2948 0.2446 0.3075 -0.1044 -0.0353 0.0258  41  PRO A N   
336  C  CA  . PRO A 44  ? 0.2671 0.2838 0.3342 -0.0529 -0.0456 0.0189  41  PRO A CA  
337  C  C   . PRO A 44  ? 0.2363 0.2739 0.3125 -0.0591 -0.0470 -0.0066 41  PRO A C   
338  O  O   . PRO A 44  ? 0.2098 0.3616 0.3141 -0.0249 -0.0372 0.0211  41  PRO A O   
339  C  CB  . PRO A 44  ? 0.3453 0.3134 0.3658 -0.0996 -0.0716 0.0111  41  PRO A CB  
340  C  CG  . PRO A 44  ? 0.3655 0.2721 0.3896 -0.0858 -0.0659 -0.0325 41  PRO A CG  
341  C  CD  . PRO A 44  ? 0.3141 0.2623 0.3379 -0.1158 -0.0640 0.0165  41  PRO A CD  
342  N  N   . PHE A 45  ? 0.2054 0.2500 0.2653 -0.0498 -0.0345 -0.0215 42  PHE A N   
343  C  CA  . PHE A 45  ? 0.2141 0.2193 0.2495 -0.0159 -0.0334 -0.0172 42  PHE A CA  
344  C  C   . PHE A 45  ? 0.2025 0.2228 0.2400 -0.0364 -0.0279 -0.0172 42  PHE A C   
345  O  O   . PHE A 45  ? 0.2192 0.2624 0.2494 -0.0595 0.0017  -0.0068 42  PHE A O   
346  C  CB  . PHE A 45  ? 0.1919 0.2337 0.2706 -0.0205 -0.0480 -0.0019 42  PHE A CB  
347  C  CG  . PHE A 45  ? 0.2143 0.2561 0.2908 -0.0094 -0.0394 -0.0174 42  PHE A CG  
348  C  CD1 . PHE A 45  ? 0.2164 0.2423 0.3232 0.0079  -0.0530 -0.0502 42  PHE A CD1 
349  C  CD2 . PHE A 45  ? 0.2223 0.2718 0.3210 -0.0162 -0.0460 -0.0052 42  PHE A CD2 
350  C  CE1 . PHE A 45  ? 0.2360 0.2546 0.3274 0.0250  -0.0321 -0.0661 42  PHE A CE1 
351  C  CE2 . PHE A 45  ? 0.2362 0.2893 0.3538 0.0349  -0.0118 -0.0198 42  PHE A CE2 
352  C  CZ  . PHE A 45  ? 0.2561 0.2560 0.3461 0.0179  -0.0341 -0.0445 42  PHE A CZ  
353  N  N   . GLU A 46  ? 0.1845 0.2218 0.2685 -0.0546 -0.0297 -0.0145 43  GLU A N   
354  C  CA  . GLU A 46  ? 0.1887 0.2232 0.2791 -0.0392 -0.0440 -0.0095 43  GLU A CA  
355  C  C   . GLU A 46  ? 0.1803 0.2062 0.2419 -0.0453 -0.0381 0.0025  43  GLU A C   
356  O  O   . GLU A 46  ? 0.2185 0.1861 0.2421 -0.0282 -0.0192 0.0172  43  GLU A O   
357  C  CB  . GLU A 46  ? 0.1957 0.2436 0.3043 -0.0432 -0.0339 -0.0056 43  GLU A CB  
358  C  CG  . GLU A 46  ? 0.2159 0.2980 0.3806 -0.0428 -0.0491 -0.0072 43  GLU A CG  
359  C  CD  . GLU A 46  ? 0.2229 0.3186 0.3987 -0.0234 -0.0561 -0.0049 43  GLU A CD  
360  O  OE1 . GLU A 46  ? 0.3272 0.3153 0.4799 0.0469  -0.0657 0.0006  43  GLU A OE1 
361  O  OE2 . GLU A 46  ? 0.2850 0.3801 0.4108 0.0239  -0.0019 -0.0069 43  GLU A OE2 
362  N  N   . ALA A 47  ? 0.2023 0.1960 0.2265 -0.0548 -0.0173 0.0053  44  ALA A N   
363  C  CA  . ALA A 47  ? 0.2013 0.1886 0.2190 -0.0506 -0.0013 0.0058  44  ALA A CA  
364  C  C   . ALA A 47  ? 0.2182 0.1916 0.2393 -0.0509 0.0133  0.0088  44  ALA A C   
365  O  O   . ALA A 47  ? 0.2756 0.2209 0.2541 -0.0880 -0.0143 0.0338  44  ALA A O   
366  C  CB  . ALA A 47  ? 0.2512 0.2187 0.2178 -0.0233 0.0295  0.0167  44  ALA A CB  
367  N  N   . GLU A 48  ? 0.2013 0.2067 0.1976 -0.0585 0.0120  0.0343  45  GLU A N   
368  C  CA  . GLU A 48  ? 0.2268 0.2208 0.2200 -0.0459 -0.0054 0.0411  45  GLU A CA  
369  C  C   . GLU A 48  ? 0.1940 0.1981 0.2153 -0.0567 0.0092  0.0399  45  GLU A C   
370  O  O   . GLU A 48  ? 0.1747 0.1998 0.2434 -0.0519 -0.0008 0.0538  45  GLU A O   
371  C  CB  . GLU A 48  ? 0.2340 0.2470 0.2200 -0.0466 0.0052  0.0313  45  GLU A CB  
372  C  CG  . GLU A 48  ? 0.2628 0.3145 0.2478 -0.0218 0.0170  0.0622  45  GLU A CG  
373  C  CD  . GLU A 48  ? 0.3151 0.3816 0.3186 -0.0293 0.0108  0.0834  45  GLU A CD  
374  O  OE1 . GLU A 48  ? 0.4253 0.4740 0.3440 -0.0013 0.0132  0.1133  45  GLU A OE1 
375  O  OE2 . GLU A 48  ? 0.3356 0.4490 0.4561 -0.0102 -0.0048 0.0721  45  GLU A OE2 
376  N  N   . VAL A 49  ? 0.1974 0.2085 0.2188 -0.0512 0.0202  0.0548  46  VAL A N   
377  C  CA  . VAL A 49  ? 0.1865 0.2127 0.2073 -0.0589 0.0005  0.0397  46  VAL A CA  
378  C  C   . VAL A 49  ? 0.2000 0.2203 0.2110 -0.0466 0.0062  0.0318  46  VAL A C   
379  O  O   . VAL A 49  ? 0.2239 0.2573 0.2522 -0.0581 0.0236  0.0749  46  VAL A O   
380  C  CB  . VAL A 49  ? 0.2112 0.2134 0.2393 -0.0449 -0.0001 0.0216  46  VAL A CB  
381  C  CG1 . VAL A 49  ? 0.2475 0.2273 0.2135 -0.0294 -0.0143 0.0096  46  VAL A CG1 
382  C  CG2 . VAL A 49  ? 0.1998 0.2304 0.2268 -0.0447 0.0059  0.0143  46  VAL A CG2 
383  N  N   . ALA A 50  ? 0.2080 0.1820 0.2285 -0.0356 0.0000  0.0498  47  ALA A N   
384  C  CA  . ALA A 50  ? 0.2449 0.2218 0.2301 -0.0365 0.0182  0.0592  47  ALA A CA  
385  C  C   . ALA A 50  ? 0.2732 0.2050 0.2450 -0.0209 0.0124  0.0588  47  ALA A C   
386  O  O   . ALA A 50  ? 0.2605 0.2090 0.2816 0.0006  0.0385  0.0865  47  ALA A O   
387  C  CB  . ALA A 50  ? 0.2235 0.2561 0.2131 -0.0250 0.0221  0.0609  47  ALA A CB  
388  N  N   . GLU A 51  ? 0.3464 0.2193 0.2711 0.0237  0.0319  0.0749  48  GLU A N   
389  C  CA  . GLU A 51  ? 0.3457 0.2395 0.2916 0.0330  0.0284  0.0798  48  GLU A CA  
390  C  C   . GLU A 51  ? 0.3414 0.2488 0.2840 0.0333  0.0402  0.1038  48  GLU A C   
391  O  O   . GLU A 51  ? 0.3635 0.2792 0.2848 0.0514  0.0443  0.0920  48  GLU A O   
392  C  CB  . GLU A 51  ? 0.4003 0.2712 0.3437 0.0281  0.0356  0.0433  48  GLU A CB  
393  C  CG  . GLU A 51  ? 0.4879 0.3337 0.4057 0.0072  0.0247  0.0275  48  GLU A CG  
394  C  CD  . GLU A 51  ? 0.5440 0.3757 0.4696 -0.0238 -0.0112 0.0073  48  GLU A CD  
395  O  OE1 . GLU A 51  ? 0.6347 0.3637 0.5235 -0.0396 -0.0254 -0.0271 48  GLU A OE1 
396  O  OE2 . GLU A 51  ? 0.5934 0.4720 0.5298 -0.0356 -0.0415 0.0173  48  GLU A OE2 
397  N  N   . PHE A 52  ? 0.3432 0.2319 0.2717 0.0300  0.0178  0.0939  49  PHE A N   
398  C  CA  . PHE A 52  ? 0.3609 0.2615 0.2824 0.0407  0.0127  0.0783  49  PHE A CA  
399  C  C   . PHE A 52  ? 0.3732 0.2435 0.2889 0.0613  0.0202  0.0789  49  PHE A C   
400  O  O   . PHE A 52  ? 0.3831 0.2402 0.3040 0.0407  0.0544  0.0781  49  PHE A O   
401  C  CB  . PHE A 52  ? 0.3672 0.2767 0.2793 0.0505  0.0093  0.0565  49  PHE A CB  
402  C  CG  . PHE A 52  ? 0.3793 0.2748 0.3115 0.0430  -0.0055 0.0404  49  PHE A CG  
403  C  CD1 . PHE A 52  ? 0.3832 0.2642 0.2862 0.0318  -0.0377 0.0230  49  PHE A CD1 
404  C  CD2 . PHE A 52  ? 0.3625 0.3064 0.2816 0.0558  -0.0219 0.0424  49  PHE A CD2 
405  C  CE1 . PHE A 52  ? 0.3903 0.2663 0.3118 0.0332  -0.0164 0.0194  49  PHE A CE1 
406  C  CE2 . PHE A 52  ? 0.4039 0.2813 0.3178 0.0233  -0.0315 0.0036  49  PHE A CE2 
407  C  CZ  . PHE A 52  ? 0.3628 0.2441 0.3053 0.0157  -0.0181 0.0029  49  PHE A CZ  
408  N  N   . PHE A 53  ? 0.4384 0.2869 0.3078 0.0621  0.0328  0.1191  50  PHE A N   
409  C  CA  . PHE A 53  ? 0.4308 0.2632 0.3559 0.0702  0.0321  0.0954  50  PHE A CA  
410  C  C   . PHE A 53  ? 0.4099 0.3122 0.3466 0.0665  0.0339  0.0956  50  PHE A C   
411  O  O   . PHE A 53  ? 0.3660 0.3967 0.3823 0.0810  0.0251  0.0623  50  PHE A O   
412  C  CB  . PHE A 53  ? 0.5006 0.2724 0.4167 0.0483  0.0180  0.0888  50  PHE A CB  
413  C  CG  . PHE A 53  ? 0.5073 0.3150 0.3991 0.0375  0.0200  0.0673  50  PHE A CG  
414  C  CD1 . PHE A 53  ? 0.5326 0.3712 0.4442 0.0121  0.0423  0.0387  50  PHE A CD1 
415  C  CD2 . PHE A 53  ? 0.5048 0.2877 0.4687 0.0584  0.0385  0.0398  50  PHE A CD2 
416  C  CE1 . PHE A 53  ? 0.5317 0.4495 0.4912 0.0090  0.0417  0.0222  50  PHE A CE1 
417  C  CE2 . PHE A 53  ? 0.5115 0.3768 0.4950 0.0319  0.0400  0.0662  50  PHE A CE2 
418  C  CZ  . PHE A 53  ? 0.5215 0.4104 0.5040 0.0393  0.0372  0.0284  50  PHE A CZ  
419  N  N   . HIS A 54  ? 0.3497 0.2948 0.3299 0.0843  0.0384  0.1084  51  HIS A N   
420  C  CA  . HIS A 54  ? 0.4025 0.3761 0.4300 0.0764  0.0061  0.1138  51  HIS A CA  
421  C  C   . HIS A 54  ? 0.4718 0.3830 0.4125 0.1018  0.0400  0.1174  51  HIS A C   
422  O  O   . HIS A 54  ? 0.4362 0.4544 0.4337 0.1168  0.0340  0.1291  51  HIS A O   
423  C  CB  . HIS A 54  ? 0.4249 0.4080 0.4921 0.0435  -0.0048 0.1198  51  HIS A CB  
424  C  CG  . HIS A 54  ? 0.4553 0.4668 0.5625 0.0380  -0.0462 0.1348  51  HIS A CG  
425  N  ND1 . HIS A 54  ? 0.5607 0.5203 0.5625 -0.0012 -0.0215 0.1481  51  HIS A ND1 
426  C  CD2 . HIS A 54  ? 0.5047 0.4671 0.5846 -0.0027 -0.0564 0.1042  51  HIS A CD2 
427  C  CE1 . HIS A 54  ? 0.5150 0.5243 0.5866 -0.0203 -0.0391 0.1305  51  HIS A CE1 
428  N  NE2 . HIS A 54  ? 0.5100 0.5482 0.6340 -0.0134 -0.0019 0.0942  51  HIS A NE2 
429  N  N   . ASN A 55  ? 0.5640 0.3952 0.3870 0.1252  0.0138  0.0929  52  ASN A N   
430  C  CA  . ASN A 55  ? 0.5522 0.4457 0.4303 0.1536  -0.0092 0.0755  52  ASN A CA  
431  C  C   . ASN A 55  ? 0.5789 0.4124 0.4809 0.1444  0.0228  0.0235  52  ASN A C   
432  O  O   . ASN A 55  ? 0.5474 0.5309 0.5764 0.1807  0.0453  0.0600  52  ASN A O   
433  N  N   . GLY A 56  ? 0.5569 0.3246 0.4412 0.1344  0.0072  0.0716  53  GLY A N   
434  C  CA  . GLY A 56  ? 0.5710 0.3295 0.4697 0.0976  0.0155  0.0652  53  GLY A CA  
435  C  C   . GLY A 56  ? 0.5435 0.3600 0.4285 0.0817  0.0030  0.0553  53  GLY A C   
436  O  O   . GLY A 56  ? 0.6340 0.3740 0.3995 0.0330  0.0351  0.0370  53  GLY A O   
437  N  N   . GLU A 57  ? 0.4770 0.3588 0.4093 0.1069  0.0043  0.0398  54  GLU A N   
438  C  CA  . GLU A 57  ? 0.4534 0.3540 0.3746 0.1225  0.0261  0.0298  54  GLU A CA  
439  C  C   . GLU A 57  ? 0.4268 0.2878 0.3235 0.1098  -0.0021 0.0209  54  GLU A C   
440  O  O   . GLU A 57  ? 0.4588 0.2866 0.3282 0.0984  0.0093  0.0270  54  GLU A O   
441  C  CB  . GLU A 57  ? 0.4493 0.3732 0.4185 0.1324  0.0109  0.0856  54  GLU A CB  
442  C  CG  . GLU A 57  ? 0.4906 0.4410 0.4249 0.1346  0.0315  0.0925  54  GLU A CG  
443  C  CD  . GLU A 57  ? 0.4836 0.4604 0.4727 0.1419  0.0200  0.1042  54  GLU A CD  
444  O  OE1 . GLU A 57  ? 0.5271 0.5447 0.5166 0.1839  0.0150  0.1709  54  GLU A OE1 
445  O  OE2 . GLU A 57  ? 0.5271 0.5712 0.6008 0.0941  -0.0072 0.1121  54  GLU A OE2 
446  N  N   . LYS A 58  ? 0.4013 0.2924 0.3275 0.1007  0.0312  0.0166  55  LYS A N   
447  C  CA  . LYS A 58  ? 0.3716 0.2571 0.3407 0.0675  0.0052  0.0364  55  LYS A CA  
448  C  C   . LYS A 58  ? 0.3028 0.2652 0.2857 0.0581  0.0141  0.0353  55  LYS A C   
449  O  O   . LYS A 58  ? 0.3032 0.2990 0.2727 0.0502  0.0004  0.0286  55  LYS A O   
450  C  CB  . LYS A 58  ? 0.4005 0.2103 0.3853 0.0174  0.0116  0.0394  55  LYS A CB  
451  C  CG  . LYS A 58  ? 0.3965 0.2377 0.4556 0.0134  -0.0016 -0.0008 55  LYS A CG  
452  C  CD  . LYS A 58  ? 0.3986 0.3484 0.5206 -0.0364 -0.0272 0.0128  55  LYS A CD  
453  N  N   . ILE A 59  ? 0.2953 0.2151 0.2843 0.0416  0.0075  0.0373  56  ILE A N   
454  C  CA  . ILE A 59  ? 0.2818 0.2321 0.2542 0.0259  -0.0043 0.0411  56  ILE A CA  
455  C  C   . ILE A 59  ? 0.2562 0.1637 0.2231 0.0107  -0.0001 0.0289  56  ILE A C   
456  O  O   . ILE A 59  ? 0.3154 0.1971 0.2518 0.0158  0.0075  0.0397  56  ILE A O   
457  C  CB  . ILE A 59  ? 0.2827 0.2361 0.2620 0.0351  0.0000  0.0370  56  ILE A CB  
458  C  CG1 . ILE A 59  ? 0.2819 0.2732 0.2750 0.0444  -0.0393 0.0421  56  ILE A CG1 
459  C  CG2 . ILE A 59  ? 0.3026 0.2192 0.2677 0.0361  0.0040  0.0255  56  ILE A CG2 
460  C  CD1 . ILE A 59  ? 0.3113 0.2914 0.2979 0.0506  -0.0513 0.0560  56  ILE A CD1 
461  N  N   . LEU A 60  ? 0.2129 0.1606 0.2058 -0.0053 -0.0077 0.0147  57  LEU A N   
462  C  CA  . LEU A 60  ? 0.2078 0.1656 0.2219 -0.0033 0.0105  0.0257  57  LEU A CA  
463  C  C   . LEU A 60  ? 0.2065 0.1576 0.1935 -0.0069 0.0125  0.0212  57  LEU A C   
464  O  O   . LEU A 60  ? 0.2201 0.1641 0.2564 -0.0091 0.0443  0.0122  57  LEU A O   
465  C  CB  . LEU A 60  ? 0.2416 0.2069 0.2497 -0.0187 -0.0136 -0.0029 57  LEU A CB  
466  C  CG  . LEU A 60  ? 0.3295 0.2498 0.3023 -0.0488 -0.0102 -0.0308 57  LEU A CG  
467  C  CD1 . LEU A 60  ? 0.4221 0.3291 0.3399 -0.0713 -0.0424 -0.0589 57  LEU A CD1 
468  C  CD2 . LEU A 60  ? 0.3742 0.3095 0.3408 -0.0612 -0.0190 -0.0317 57  LEU A CD2 
469  N  N   . LEU A 61  ? 0.1812 0.1665 0.1745 -0.0156 -0.0004 0.0250  58  LEU A N   
470  C  CA  . LEU A 61  ? 0.1849 0.1628 0.1706 -0.0143 -0.0005 0.0078  58  LEU A CA  
471  C  C   . LEU A 61  ? 0.1858 0.1657 0.1798 -0.0228 -0.0103 0.0195  58  LEU A C   
472  O  O   . LEU A 61  ? 0.2346 0.1995 0.2127 -0.0423 -0.0012 0.0570  58  LEU A O   
473  C  CB  . LEU A 61  ? 0.2088 0.1677 0.1803 -0.0170 0.0092  0.0129  58  LEU A CB  
474  C  CG  . LEU A 61  ? 0.1882 0.1871 0.2042 -0.0154 0.0000  0.0035  58  LEU A CG  
475  C  CD1 . LEU A 61  ? 0.1679 0.2056 0.1891 -0.0149 -0.0038 0.0210  58  LEU A CD1 
476  C  CD2 . LEU A 61  ? 0.2001 0.2259 0.1933 -0.0220 -0.0058 0.0083  58  LEU A CD2 
477  N  N   . VAL A 62  ? 0.1420 0.1496 0.1838 -0.0267 -0.0097 0.0248  59  VAL A N   
478  C  CA  . VAL A 62  ? 0.1369 0.1691 0.1738 -0.0175 -0.0038 0.0105  59  VAL A CA  
479  C  C   . VAL A 62  ? 0.1385 0.1589 0.1546 -0.0189 -0.0051 0.0040  59  VAL A C   
480  O  O   . VAL A 62  ? 0.1399 0.1807 0.1961 -0.0238 -0.0075 0.0100  59  VAL A O   
481  C  CB  . VAL A 62  ? 0.1673 0.1730 0.1804 -0.0215 0.0046  0.0060  59  VAL A CB  
482  C  CG1 . VAL A 62  ? 0.1910 0.1803 0.1783 -0.0251 -0.0062 0.0100  59  VAL A CG1 
483  C  CG2 . VAL A 62  ? 0.1753 0.1886 0.1747 -0.0019 0.0065  0.0180  59  VAL A CG2 
484  N  N   . LYS A 63  ? 0.1540 0.1671 0.1752 -0.0156 -0.0063 0.0124  60  LYS A N   
485  C  CA  . LYS A 63  ? 0.1665 0.1559 0.1600 -0.0155 0.0044  0.0164  60  LYS A CA  
486  C  C   . LYS A 63  ? 0.1622 0.1737 0.1624 -0.0218 0.0006  0.0011  60  LYS A C   
487  O  O   . LYS A 63  ? 0.1634 0.1781 0.1810 -0.0141 0.0102  0.0204  60  LYS A O   
488  C  CB  . LYS A 63  ? 0.1626 0.1409 0.1783 -0.0153 0.0052  0.0030  60  LYS A CB  
489  C  CG  . LYS A 63  ? 0.1723 0.1660 0.1744 -0.0169 0.0088  0.0131  60  LYS A CG  
490  C  CD  . LYS A 63  ? 0.1928 0.1822 0.1846 -0.0204 0.0093  0.0091  60  LYS A CD  
491  C  CE  . LYS A 63  ? 0.2017 0.2024 0.1914 -0.0201 0.0112  -0.0043 60  LYS A CE  
492  N  NZ  . LYS A 63  ? 0.2540 0.2506 0.1807 -0.0108 0.0096  -0.0136 60  LYS A NZ  
493  N  N   . PRO A 64  ? 0.1303 0.1731 0.1580 -0.0204 0.0007  0.0006  61  PRO A N   
494  C  CA  . PRO A 64  ? 0.1484 0.1652 0.1661 -0.0118 -0.0110 -0.0018 61  PRO A CA  
495  C  C   . PRO A 64  ? 0.1554 0.1695 0.1695 -0.0208 0.0075  0.0174  61  PRO A C   
496  O  O   . PRO A 64  ? 0.1769 0.1788 0.1767 -0.0173 0.0018  -0.0040 61  PRO A O   
497  C  CB  . PRO A 64  ? 0.1535 0.1749 0.1661 -0.0076 -0.0072 0.0047  61  PRO A CB  
498  C  CG  . PRO A 64  ? 0.1525 0.1799 0.1701 -0.0132 0.0116  -0.0011 61  PRO A CG  
499  C  CD  . PRO A 64  ? 0.1427 0.1633 0.1736 -0.0164 0.0075  0.0022  61  PRO A CD  
500  N  N   . GLN A 65  ? 0.1567 0.1845 0.1658 -0.0187 -0.0098 0.0064  62  GLN A N   
501  C  CA  . GLN A 65  ? 0.1662 0.1935 0.1731 -0.0071 0.0074  0.0123  62  GLN A CA  
502  C  C   . GLN A 65  ? 0.1629 0.2075 0.1808 -0.0103 -0.0139 0.0034  62  GLN A C   
503  O  O   . GLN A 65  ? 0.1484 0.2887 0.2031 -0.0088 0.0039  0.0275  62  GLN A O   
504  C  CB  . GLN A 65  ? 0.1667 0.2171 0.1932 -0.0158 0.0242  0.0063  62  GLN A CB  
505  C  CG  . GLN A 65  ? 0.1817 0.2108 0.2179 -0.0165 0.0396  0.0315  62  GLN A CG  
506  C  CD  . GLN A 65  ? 0.1812 0.2159 0.2213 -0.0136 0.0496  0.0147  62  GLN A CD  
507  O  OE1 . GLN A 65  ? 0.2251 0.2513 0.2434 0.0016  0.0394  0.0003  62  GLN A OE1 
508  N  NE2 . GLN A 65  ? 0.2197 0.1896 0.2197 -0.0318 0.0246  -0.0028 62  GLN A NE2 
509  N  N   . THR A 66  ? 0.1582 0.1909 0.1862 -0.0077 -0.0109 0.0158  63  THR A N   
510  C  CA  . THR A 66  ? 0.1739 0.1896 0.1829 -0.0102 -0.0130 -0.0013 63  THR A CA  
511  C  C   . THR A 66  ? 0.1544 0.1981 0.1980 -0.0038 -0.0164 0.0092  63  THR A C   
512  O  O   . THR A 66  ? 0.1898 0.2077 0.1939 -0.0030 -0.0296 0.0133  63  THR A O   
513  C  CB  . THR A 66  ? 0.1710 0.1998 0.1824 -0.0148 -0.0136 -0.0027 63  THR A CB  
514  O  OG1 . THR A 66  ? 0.1479 0.1833 0.1897 0.0000  0.0026  0.0043  63  THR A OG1 
515  C  CG2 . THR A 66  ? 0.1992 0.1967 0.2049 -0.0122 -0.0092 -0.0091 63  THR A CG2 
516  N  N   . PHE A 67  ? 0.1640 0.1823 0.1674 -0.0165 0.0098  0.0137  64  PHE A N   
517  C  CA  . PHE A 67  ? 0.1686 0.1752 0.1764 0.0028  0.0004  -0.0006 64  PHE A CA  
518  C  C   . PHE A 67  ? 0.1604 0.1722 0.1577 0.0026  0.0075  -0.0010 64  PHE A C   
519  O  O   . PHE A 67  ? 0.1701 0.1737 0.1608 -0.0046 0.0063  0.0001  64  PHE A O   
520  C  CB  . PHE A 67  ? 0.2006 0.1861 0.1923 0.0042  -0.0143 0.0094  64  PHE A CB  
521  C  CG  . PHE A 67  ? 0.2157 0.2128 0.2036 0.0194  0.0005  0.0056  64  PHE A CG  
522  C  CD1 . PHE A 67  ? 0.2227 0.2255 0.2720 0.0356  0.0282  0.0020  64  PHE A CD1 
523  C  CD2 . PHE A 67  ? 0.1760 0.2372 0.2256 0.0416  0.0096  -0.0005 64  PHE A CD2 
524  C  CE1 . PHE A 67  ? 0.2273 0.2871 0.3116 0.0528  0.0226  -0.0140 64  PHE A CE1 
525  C  CE2 . PHE A 67  ? 0.2157 0.2759 0.2253 0.0670  0.0073  -0.0268 64  PHE A CE2 
526  C  CZ  . PHE A 67  ? 0.2097 0.3006 0.2754 0.0638  0.0172  -0.0139 64  PHE A CZ  
527  N  N   . MET A 68  ? 0.1678 0.1826 0.1545 -0.0020 0.0055  -0.0148 65  MET A N   
528  C  CA  . MET A 68  ? 0.1580 0.1783 0.1711 0.0215  -0.0046 -0.0065 65  MET A CA  
529  C  C   . MET A 68  ? 0.1763 0.1705 0.1774 0.0120  0.0029  -0.0005 65  MET A C   
530  O  O   . MET A 68  ? 0.1654 0.1765 0.1700 0.0067  0.0148  0.0009  65  MET A O   
531  C  CB  . MET A 68  ? 0.1715 0.1889 0.1905 0.0016  -0.0110 -0.0044 65  MET A CB  
532  C  CG  . MET A 68  ? 0.1715 0.1751 0.1724 0.0080  -0.0007 0.0013  65  MET A CG  
533  S  SD  . MET A 68  ? 0.2034 0.1859 0.1595 0.0155  -0.0181 -0.0047 65  MET A SD  
534  C  CE  . MET A 68  ? 0.2058 0.1566 0.1567 -0.0189 -0.0046 0.0085  65  MET A CE  
535  N  N   . ASN A 69  ? 0.1974 0.1917 0.1860 0.0125  0.0024  0.0027  66  ASN A N   
536  C  CA  . ASN A 69  ? 0.2292 0.2213 0.1950 0.0164  -0.0078 0.0142  66  ASN A CA  
537  C  C   . ASN A 69  ? 0.1933 0.2205 0.1862 0.0259  0.0038  0.0163  66  ASN A C   
538  O  O   . ASN A 69  ? 0.2479 0.2255 0.1797 0.0206  0.0081  0.0197  66  ASN A O   
539  C  CB  . ASN A 69  ? 0.2787 0.2062 0.2286 0.0150  -0.0159 0.0196  66  ASN A CB  
540  C  CG  . ASN A 69  ? 0.2908 0.3281 0.3059 0.0147  -0.0138 0.0012  66  ASN A CG  
541  O  OD1 . ASN A 69  ? 0.3341 0.4983 0.4453 0.0529  0.0131  0.0109  66  ASN A OD1 
542  N  ND2 . ASN A 69  ? 0.3308 0.3861 0.3836 0.0388  -0.0364 -0.0156 66  ASN A ND2 
543  N  N   . GLU A 70  ? 0.1673 0.2062 0.1629 0.0191  -0.0112 0.0135  67  GLU A N   
544  C  CA  . GLU A 70  ? 0.1642 0.2134 0.1672 0.0045  -0.0073 -0.0020 67  GLU A CA  
545  C  C   . GLU A 70  ? 0.1585 0.1987 0.1733 0.0038  -0.0057 -0.0146 67  GLU A C   
546  O  O   . GLU A 70  ? 0.1637 0.2065 0.1795 0.0082  0.0016  -0.0101 67  GLU A O   
547  C  CB  . GLU A 70  ? 0.1902 0.2453 0.2182 0.0054  -0.0208 0.0120  67  GLU A CB  
548  C  CG  . GLU A 70  ? 0.2627 0.2766 0.2740 0.0002  -0.0376 0.0263  67  GLU A CG  
549  C  CD  . GLU A 70  ? 0.3600 0.4048 0.3521 -0.0040 -0.0139 -0.0365 67  GLU A CD  
550  O  OE1 . GLU A 70  ? 0.3437 0.4913 0.3611 0.0216  -0.0232 -0.0345 67  GLU A OE1 
551  N  N   . SER A 71  ? 0.1561 0.1749 0.1609 -0.0061 -0.0042 0.0042  68  SER A N   
552  C  CA  . SER A 71  ? 0.1376 0.1803 0.1711 -0.0006 -0.0049 -0.0065 68  SER A CA  
553  C  C   . SER A 71  ? 0.1301 0.1872 0.1621 -0.0001 -0.0086 -0.0114 68  SER A C   
554  O  O   . SER A 71  ? 0.1596 0.1791 0.1736 0.0053  -0.0059 -0.0112 68  SER A O   
555  C  CB  . SER A 71  ? 0.1309 0.1938 0.1598 -0.0016 -0.0041 -0.0119 68  SER A CB  
556  O  OG  . SER A 71  ? 0.1745 0.2020 0.1405 -0.0063 -0.0071 -0.0091 68  SER A OG  
557  N  N   . GLY A 72  ? 0.1400 0.1858 0.1702 -0.0070 0.0020  -0.0108 69  GLY A N   
558  C  CA  . GLY A 72  ? 0.1684 0.1792 0.1886 -0.0210 0.0019  -0.0174 69  GLY A CA  
559  C  C   . GLY A 72  ? 0.1741 0.1876 0.1910 -0.0137 -0.0028 -0.0120 69  GLY A C   
560  O  O   . GLY A 72  ? 0.2080 0.1973 0.1976 -0.0322 0.0003  -0.0315 69  GLY A O   
561  N  N   . ARG A 73  ? 0.1662 0.2036 0.1894 -0.0027 -0.0208 -0.0223 70  ARG A N   
562  C  CA  . ARG A 73  ? 0.1992 0.2198 0.2046 -0.0235 -0.0159 -0.0258 70  ARG A CA  
563  C  C   . ARG A 73  ? 0.1771 0.1909 0.2245 0.0019  -0.0079 -0.0267 70  ARG A C   
564  O  O   . ARG A 73  ? 0.2051 0.2022 0.3046 -0.0274 -0.0229 -0.0227 70  ARG A O   
565  C  CB  . ARG A 73  ? 0.2213 0.2635 0.2272 -0.0043 -0.0513 -0.0494 70  ARG A CB  
566  C  CG  . ARG A 73  ? 0.2151 0.3516 0.2508 0.0279  -0.0791 -0.0189 70  ARG A CG  
567  C  CD  . ARG A 73  ? 0.2217 0.4398 0.3051 0.0624  -0.0954 -0.0043 70  ARG A CD  
568  N  NE  . ARG A 73  ? 0.3321 0.4855 0.3803 0.1173  -0.0866 0.0251  70  ARG A NE  
569  C  CZ  . ARG A 73  ? 0.3705 0.5646 0.4186 0.1677  -0.0725 0.0897  70  ARG A CZ  
570  N  NH1 . ARG A 73  ? 0.4427 0.6549 0.4826 0.1395  -0.0280 0.1045  70  ARG A NH1 
571  N  NH2 . ARG A 73  ? 0.5463 0.6393 0.4436 0.1226  -0.0035 0.1245  70  ARG A NH2 
572  N  N   . ALA A 74  ? 0.1721 0.1834 0.1929 -0.0015 0.0202  -0.0234 71  ALA A N   
573  C  CA  . ALA A 74  ? 0.1762 0.1720 0.2212 -0.0103 0.0153  -0.0107 71  ALA A CA  
574  C  C   . ALA A 74  ? 0.1843 0.1843 0.2010 -0.0012 -0.0026 -0.0119 71  ALA A C   
575  O  O   . ALA A 74  ? 0.2116 0.1766 0.2708 -0.0007 -0.0013 -0.0179 71  ALA A O   
576  C  CB  . ALA A 74  ? 0.1873 0.1878 0.2262 -0.0082 0.0285  -0.0088 71  ALA A CB  
577  N  N   . VAL A 75  ? 0.1968 0.1847 0.1848 0.0037  -0.0096 -0.0279 72  VAL A N   
578  C  CA  . VAL A 75  ? 0.1904 0.1863 0.1779 0.0046  -0.0087 -0.0155 72  VAL A CA  
579  C  C   . VAL A 75  ? 0.1976 0.1991 0.2122 -0.0019 -0.0071 -0.0284 72  VAL A C   
580  O  O   . VAL A 75  ? 0.2090 0.2111 0.2250 0.0264  -0.0227 -0.0360 72  VAL A O   
581  C  CB  . VAL A 75  ? 0.1803 0.1950 0.1961 0.0107  -0.0091 -0.0125 72  VAL A CB  
582  C  CG1 . VAL A 75  ? 0.1840 0.2222 0.2419 0.0150  -0.0178 -0.0270 72  VAL A CG1 
583  C  CG2 . VAL A 75  ? 0.2083 0.2035 0.2040 0.0001  -0.0051 -0.0093 72  VAL A CG2 
584  N  N   . GLY A 76  ? 0.2138 0.2070 0.2125 -0.0036 -0.0061 -0.0432 73  GLY A N   
585  C  CA  . GLY A 76  ? 0.2246 0.2328 0.1990 -0.0028 -0.0088 -0.0411 73  GLY A CA  
586  C  C   . GLY A 76  ? 0.2338 0.2250 0.2441 0.0035  -0.0287 -0.0479 73  GLY A C   
587  O  O   . GLY A 76  ? 0.2730 0.2193 0.2835 0.0030  -0.0143 -0.0664 73  GLY A O   
588  N  N   . PRO A 77  ? 0.2188 0.2099 0.2432 -0.0039 -0.0204 -0.0272 74  PRO A N   
589  C  CA  . PRO A 77  ? 0.2059 0.2097 0.2687 -0.0086 -0.0471 -0.0368 74  PRO A CA  
590  C  C   . PRO A 77  ? 0.2052 0.2398 0.2530 -0.0253 -0.0463 -0.0345 74  PRO A C   
591  O  O   . PRO A 77  ? 0.2068 0.2217 0.2648 0.0051  -0.0687 -0.0441 74  PRO A O   
592  C  CB  . PRO A 77  ? 0.2018 0.2626 0.2938 0.0082  -0.0665 -0.0333 74  PRO A CB  
593  C  CG  . PRO A 77  ? 0.2350 0.2519 0.3112 0.0080  -0.0625 -0.0396 74  PRO A CG  
594  C  CD  . PRO A 77  ? 0.2432 0.2269 0.2971 0.0111  -0.0493 -0.0303 74  PRO A CD  
595  N  N   . LEU A 78  ? 0.2220 0.2302 0.2487 -0.0179 -0.0415 -0.0341 75  LEU A N   
596  C  CA  . LEU A 78  ? 0.2302 0.2407 0.2537 -0.0068 -0.0502 -0.0473 75  LEU A CA  
597  C  C   . LEU A 78  ? 0.2613 0.2261 0.2436 -0.0028 -0.0382 -0.0534 75  LEU A C   
598  O  O   . LEU A 78  ? 0.2623 0.2415 0.2703 0.0394  -0.0522 -0.0227 75  LEU A O   
599  C  CB  . LEU A 78  ? 0.2410 0.2694 0.2576 -0.0136 -0.0526 -0.0496 75  LEU A CB  
600  C  CG  . LEU A 78  ? 0.2653 0.3262 0.2887 0.0075  -0.0433 -0.0494 75  LEU A CG  
601  C  CD1 . LEU A 78  ? 0.2695 0.3528 0.2881 0.0062  -0.0395 -0.0664 75  LEU A CD1 
602  C  CD2 . LEU A 78  ? 0.2874 0.3838 0.3085 0.0121  -0.0503 -0.0228 75  LEU A CD2 
603  N  N   . MET A 79  ? 0.2253 0.2173 0.3284 -0.0052 -0.0383 -0.0229 76  MET A N   
604  C  CA  . MET A 79  ? 0.2398 0.2219 0.3484 0.0065  -0.0080 -0.0213 76  MET A CA  
605  C  C   . MET A 79  ? 0.2199 0.2022 0.2937 0.0067  -0.0105 -0.0087 76  MET A C   
606  O  O   . MET A 79  ? 0.2340 0.2157 0.3276 0.0322  0.0363  0.0396  76  MET A O   
607  C  CB  . MET A 79  ? 0.2501 0.2399 0.3485 0.0230  -0.0099 -0.0069 76  MET A CB  
608  C  CG  . MET A 79  ? 0.2800 0.2221 0.3648 0.0407  -0.0093 -0.0285 76  MET A CG  
609  S  SD  . MET A 79  ? 0.2883 0.3204 0.4644 0.0143  0.0492  -0.0462 76  MET A SD  
610  C  CE  . MET A 79  ? 0.2527 0.2994 0.4027 0.0192  0.0883  -0.0307 76  MET A CE  
611  N  N   . THR A 80  ? 0.2847 0.2450 0.2817 -0.0169 -0.0251 0.0105  77  THR A N   
612  C  CA  . THR A 80  ? 0.3030 0.2521 0.2864 0.0009  -0.0115 -0.0041 77  THR A CA  
613  C  C   . THR A 80  ? 0.2338 0.2187 0.2968 -0.0068 -0.0236 -0.0136 77  THR A C   
614  O  O   . THR A 80  ? 0.2890 0.2150 0.3453 0.0127  0.0104  -0.0152 77  THR A O   
615  C  CB  . THR A 80  ? 0.3512 0.2967 0.2900 -0.0203 -0.0180 -0.0059 77  THR A CB  
616  O  OG1 . THR A 80  ? 0.4433 0.3358 0.2892 -0.0175 -0.0551 0.0052  77  THR A OG1 
617  C  CG2 . THR A 80  ? 0.4200 0.2856 0.2810 -0.0123 0.0008  -0.0196 77  THR A CG2 
618  N  N   . TYR A 81  ? 0.1935 0.2029 0.2856 -0.0089 -0.0221 -0.0037 78  TYR A N   
619  C  CA  . TYR A 81  ? 0.1963 0.2572 0.2850 -0.0354 -0.0208 0.0112  78  TYR A CA  
620  C  C   . TYR A 81  ? 0.2122 0.2717 0.3130 -0.0388 -0.0031 0.0575  78  TYR A C   
621  O  O   . TYR A 81  ? 0.2075 0.2900 0.4231 -0.0424 -0.0179 0.0756  78  TYR A O   
622  C  CB  . TYR A 81  ? 0.1647 0.3338 0.2653 -0.0285 -0.0520 0.0083  78  TYR A CB  
623  C  CG  . TYR A 81  ? 0.2031 0.4259 0.2863 -0.0618 -0.0419 0.0265  78  TYR A CG  
624  C  CD1 . TYR A 81  ? 0.1915 0.4736 0.3316 -0.0910 -0.0577 0.0344  78  TYR A CD1 
625  C  CD2 . TYR A 81  ? 0.2550 0.4504 0.3201 -0.1007 -0.0637 0.0288  78  TYR A CD2 
626  C  CE1 . TYR A 81  ? 0.2868 0.5331 0.2794 -0.1143 -0.0656 0.0372  78  TYR A CE1 
627  C  CE2 . TYR A 81  ? 0.2701 0.5317 0.3218 -0.1179 -0.0691 0.0631  78  TYR A CE2 
628  C  CZ  . TYR A 81  ? 0.3303 0.5560 0.3065 -0.1441 -0.0739 0.0567  78  TYR A CZ  
629  O  OH  . TYR A 81  ? 0.3831 0.6861 0.3518 -0.1750 0.0250  0.0815  78  TYR A OH  
630  N  N   . PHE A 82  ? 0.2048 0.2940 0.3175 -0.0289 0.0041  0.0621  79  PHE A N   
631  C  CA  . PHE A 82  ? 0.2282 0.3173 0.3591 -0.0225 -0.0176 0.0933  79  PHE A CA  
632  C  C   . PHE A 82  ? 0.2703 0.3032 0.3923 0.0017  -0.0007 0.1045  79  PHE A C   
633  O  O   . PHE A 82  ? 0.2534 0.3680 0.4903 0.0269  -0.0065 0.1609  79  PHE A O   
634  C  CB  . PHE A 82  ? 0.3007 0.3794 0.4064 -0.0167 -0.0511 0.0810  79  PHE A CB  
635  C  CG  . PHE A 82  ? 0.2568 0.4437 0.3534 -0.0317 -0.0931 0.0662  79  PHE A CG  
636  C  CD1 . PHE A 82  ? 0.3026 0.4933 0.4256 -0.0370 -0.0850 0.0630  79  PHE A CD1 
637  C  CD2 . PHE A 82  ? 0.2780 0.4978 0.3755 -0.0061 -0.0985 0.0716  79  PHE A CD2 
638  C  CE1 . PHE A 82  ? 0.3422 0.5151 0.3882 -0.0027 -0.0915 0.0760  79  PHE A CE1 
639  C  CE2 . PHE A 82  ? 0.3191 0.5033 0.3824 -0.0015 -0.1034 0.0562  79  PHE A CE2 
640  C  CZ  . PHE A 82  ? 0.3075 0.5218 0.3998 0.0001  -0.1143 0.0701  79  PHE A CZ  
641  N  N   . GLY A 83  ? 0.2017 0.2915 0.4143 -0.0036 -0.0191 0.0840  80  GLY A N   
642  C  CA  . GLY A 83  ? 0.2513 0.2499 0.4417 0.0154  0.0106  0.0700  80  GLY A CA  
643  C  C   . GLY A 83  ? 0.1818 0.2712 0.4274 0.0331  0.0247  0.0637  80  GLY A C   
644  O  O   . GLY A 83  ? 0.2410 0.3638 0.4543 0.0931  0.0291  0.0874  80  GLY A O   
645  N  N   . ILE A 84  ? 0.2229 0.2633 0.3932 0.0022  0.0147  0.0761  81  ILE A N   
646  C  CA  . ILE A 84  ? 0.1911 0.2823 0.3652 -0.0066 0.0388  0.0784  81  ILE A CA  
647  C  C   . ILE A 84  ? 0.2069 0.2358 0.3091 -0.0117 0.0260  0.0342  81  ILE A C   
648  O  O   . ILE A 84  ? 0.2105 0.3206 0.3388 -0.0027 0.0052  0.0796  81  ILE A O   
649  C  CB  . ILE A 84  ? 0.2789 0.3438 0.3504 -0.0912 0.0410  0.0249  81  ILE A CB  
650  C  CG1 . ILE A 84  ? 0.3744 0.4500 0.3725 -0.0918 0.0288  0.0306  81  ILE A CG1 
651  C  CG2 . ILE A 84  ? 0.3367 0.3366 0.3855 -0.0533 0.0311  0.0131  81  ILE A CG2 
652  C  CD1 . ILE A 84  ? 0.4251 0.4658 0.4194 -0.0658 0.0382  -0.0029 81  ILE A CD1 
653  N  N   . TYR A 85  ? 0.2037 0.2172 0.2861 -0.0195 0.0562  -0.0335 82  TYR A N   
654  C  CA  . TYR A 85  ? 0.2195 0.2400 0.2750 -0.0558 0.0633  -0.0566 82  TYR A CA  
655  C  C   . TYR A 85  ? 0.2346 0.2350 0.2507 -0.0406 0.0367  -0.0543 82  TYR A C   
656  O  O   . TYR A 85  ? 0.2515 0.2199 0.2280 -0.0446 0.0490  -0.0376 82  TYR A O   
657  C  CB  . TYR A 85  ? 0.2338 0.2810 0.3388 -0.0476 0.0644  -0.0867 82  TYR A CB  
658  C  CG  . TYR A 85  ? 0.2702 0.2887 0.3633 -0.0466 0.0660  -0.0859 82  TYR A CG  
659  C  CD1 . TYR A 85  ? 0.3242 0.3154 0.3962 -0.0341 0.0301  -0.0847 82  TYR A CD1 
660  C  CD2 . TYR A 85  ? 0.3055 0.2770 0.3774 -0.0354 0.0659  -0.0930 82  TYR A CD2 
661  C  CE1 . TYR A 85  ? 0.3788 0.2856 0.4416 -0.0393 0.0160  -0.1126 82  TYR A CE1 
662  C  CE2 . TYR A 85  ? 0.3748 0.2894 0.4175 -0.0321 0.0453  -0.1131 82  TYR A CE2 
663  C  CZ  . TYR A 85  ? 0.3254 0.2596 0.4197 -0.0142 0.0488  -0.1283 82  TYR A CZ  
664  O  OH  . TYR A 85  ? 0.3587 0.2838 0.5447 -0.0600 0.0230  -0.1246 82  TYR A OH  
665  N  N   . PRO A 86  ? 0.2367 0.2447 0.2332 -0.0454 0.0154  -0.0391 83  PRO A N   
666  C  CA  . PRO A 86  ? 0.2365 0.2311 0.2326 -0.0517 0.0072  -0.0232 83  PRO A CA  
667  C  C   . PRO A 86  ? 0.2102 0.1905 0.2356 -0.0110 0.0087  -0.0076 83  PRO A C   
668  O  O   . PRO A 86  ? 0.2278 0.1963 0.2412 -0.0193 0.0005  -0.0291 83  PRO A O   
669  C  CB  . PRO A 86  ? 0.2731 0.2490 0.2330 -0.0410 -0.0137 -0.0073 83  PRO A CB  
670  C  CG  . PRO A 86  ? 0.2890 0.3103 0.2447 -0.0431 -0.0073 -0.0253 83  PRO A CG  
671  C  CD  . PRO A 86  ? 0.2605 0.2936 0.2547 -0.0649 -0.0061 -0.0552 83  PRO A CD  
672  N  N   . GLU A 87  ? 0.2440 0.1852 0.2184 -0.0057 0.0084  -0.0320 84  GLU A N   
673  C  CA  . GLU A 87  ? 0.2164 0.2114 0.2344 0.0150  0.0134  -0.0248 84  GLU A CA  
674  C  C   . GLU A 87  ? 0.2449 0.2103 0.2411 0.0298  0.0127  -0.0368 84  GLU A C   
675  O  O   . GLU A 87  ? 0.2808 0.2272 0.2471 0.0154  -0.0017 -0.0384 84  GLU A O   
676  C  CB  . GLU A 87  ? 0.3014 0.2870 0.2777 0.0301  0.0317  -0.0384 84  GLU A CB  
677  C  CG  . GLU A 87  ? 0.2570 0.3292 0.3170 -0.0107 0.0545  -0.0313 84  GLU A CG  
678  C  CD  . GLU A 87  ? 0.2466 0.3150 0.3233 -0.0431 0.0629  -0.0182 84  GLU A CD  
679  O  OE1 . GLU A 87  ? 0.2627 0.3461 0.3565 -0.0797 0.1265  -0.1338 84  GLU A OE1 
680  O  OE2 . GLU A 87  ? 0.2751 0.3063 0.2679 -0.0374 0.0683  -0.0212 84  GLU A OE2 
681  N  N   . GLU A 88  ? 0.2756 0.2072 0.2211 0.0229  0.0210  -0.0240 85  GLU A N   
682  C  CA  . GLU A 88  ? 0.2800 0.2027 0.2129 0.0251  0.0340  -0.0209 85  GLU A CA  
683  C  C   . GLU A 88  ? 0.1969 0.2134 0.1948 0.0196  0.0152  -0.0199 85  GLU A C   
684  O  O   . GLU A 88  ? 0.2153 0.2011 0.2112 0.0539  0.0306  0.0145  85  GLU A O   
685  C  CB  . GLU A 88  ? 0.3238 0.2211 0.2125 0.0079  0.0254  -0.0312 85  GLU A CB  
686  C  CG  . GLU A 88  ? 0.3728 0.2474 0.2815 0.0308  0.0194  -0.0029 85  GLU A CG  
687  C  CD  . GLU A 88  ? 0.4209 0.2533 0.3010 0.0361  0.0027  -0.0245 85  GLU A CD  
688  O  OE1 . GLU A 88  ? 0.3210 0.2995 0.4200 0.0496  -0.0611 0.0034  85  GLU A OE1 
689  O  OE2 . GLU A 88  ? 0.5778 0.2992 0.3092 0.0211  0.0190  -0.0135 85  GLU A OE2 
690  N  N   . LEU A 89  ? 0.2126 0.1976 0.1885 0.0124  0.0203  -0.0315 86  LEU A N   
691  C  CA  . LEU A 89  ? 0.1670 0.1917 0.2159 0.0072  0.0254  -0.0080 86  LEU A CA  
692  C  C   . LEU A 89  ? 0.1819 0.1663 0.2282 0.0014  0.0275  -0.0097 86  LEU A C   
693  O  O   . LEU A 89  ? 0.1806 0.1715 0.2671 0.0063  0.0391  -0.0292 86  LEU A O   
694  C  CB  . LEU A 89  ? 0.2110 0.2665 0.2565 0.0107  0.0415  0.0220  86  LEU A CB  
695  C  CG  . LEU A 89  ? 0.2775 0.2864 0.2699 -0.0050 0.0243  0.0164  86  LEU A CG  
696  C  CD1 . LEU A 89  ? 0.2294 0.3300 0.2670 -0.0096 0.0384  0.0610  86  LEU A CD1 
697  C  CD2 . LEU A 89  ? 0.2955 0.3326 0.3242 -0.0117 0.0466  -0.0015 86  LEU A CD2 
698  N  N   . VAL A 90  ? 0.1682 0.1472 0.2160 -0.0033 0.0250  -0.0089 87  VAL A N   
699  C  CA  . VAL A 90  ? 0.1526 0.1657 0.2101 0.0066  0.0105  -0.0023 87  VAL A CA  
700  C  C   . VAL A 90  ? 0.1650 0.1675 0.1878 0.0180  0.0101  0.0036  87  VAL A C   
701  O  O   . VAL A 90  ? 0.1855 0.1696 0.2157 0.0177  0.0297  0.0235  87  VAL A O   
702  C  CB  . VAL A 90  ? 0.1513 0.1904 0.2339 0.0120  -0.0136 -0.0030 87  VAL A CB  
703  C  CG1 . VAL A 90  ? 0.1996 0.2060 0.2403 0.0000  -0.0245 -0.0116 87  VAL A CG1 
704  C  CG2 . VAL A 90  ? 0.1765 0.2067 0.2601 0.0321  -0.0210 -0.0034 87  VAL A CG2 
705  N  N   . VAL A 91  ? 0.1351 0.1584 0.1780 -0.0028 0.0143  0.0060  88  VAL A N   
706  C  CA  . VAL A 91  ? 0.1364 0.1546 0.1715 0.0024  0.0103  -0.0090 88  VAL A CA  
707  C  C   . VAL A 91  ? 0.1371 0.1564 0.1640 0.0006  0.0094  -0.0078 88  VAL A C   
708  O  O   . VAL A 91  ? 0.1412 0.1724 0.1577 -0.0154 0.0147  -0.0186 88  VAL A O   
709  C  CB  . VAL A 91  ? 0.1358 0.1713 0.1646 -0.0055 0.0198  -0.0104 88  VAL A CB  
710  C  CG1 . VAL A 91  ? 0.1549 0.1927 0.1821 0.0085  -0.0020 0.0025  88  VAL A CG1 
711  C  CG2 . VAL A 91  ? 0.1522 0.2041 0.1690 0.0009  0.0063  -0.0160 88  VAL A CG2 
712  N  N   . ILE A 92  ? 0.1301 0.1402 0.1591 -0.0023 -0.0002 -0.0100 89  ILE A N   
713  C  CA  . ILE A 92  ? 0.1185 0.1427 0.1566 -0.0135 0.0072  -0.0096 89  ILE A CA  
714  C  C   . ILE A 92  ? 0.1225 0.1360 0.1430 -0.0032 -0.0021 -0.0054 89  ILE A C   
715  O  O   . ILE A 92  ? 0.1334 0.1522 0.1495 -0.0098 0.0028  -0.0144 89  ILE A O   
716  C  CB  . ILE A 92  ? 0.1115 0.1596 0.1504 -0.0036 0.0013  0.0004  89  ILE A CB  
717  C  CG1 . ILE A 92  ? 0.1360 0.1612 0.1596 -0.0062 -0.0087 -0.0002 89  ILE A CG1 
718  C  CG2 . ILE A 92  ? 0.1037 0.1685 0.1594 0.0030  0.0092  -0.0075 89  ILE A CG2 
719  C  CD1 . ILE A 92  ? 0.1910 0.1711 0.1713 -0.0033 -0.0244 0.0018  89  ILE A CD1 
720  N  N   . TYR A 93  ? 0.1154 0.1467 0.1628 0.0049  -0.0048 0.0041  90  TYR A N   
721  C  CA  . TYR A 93  ? 0.1182 0.1420 0.1733 0.0122  0.0008  -0.0020 90  TYR A CA  
722  C  C   . TYR A 93  ? 0.1072 0.1518 0.1722 0.0051  0.0035  -0.0038 90  TYR A C   
723  O  O   . TYR A 93  ? 0.1210 0.1564 0.1724 -0.0071 -0.0079 -0.0045 90  TYR A O   
724  C  CB  . TYR A 93  ? 0.1335 0.1521 0.1692 0.0193  -0.0094 -0.0087 90  TYR A CB  
725  C  CG  . TYR A 93  ? 0.1515 0.2060 0.1652 0.0137  -0.0149 -0.0252 90  TYR A CG  
726  C  CD1 . TYR A 93  ? 0.1763 0.2569 0.1679 0.0326  -0.0026 -0.0019 90  TYR A CD1 
727  C  CD2 . TYR A 93  ? 0.1679 0.2280 0.1760 -0.0012 0.0120  -0.0029 90  TYR A CD2 
728  C  CE1 . TYR A 93  ? 0.1915 0.2711 0.1951 0.0409  0.0118  0.0200  90  TYR A CE1 
729  C  CE2 . TYR A 93  ? 0.1882 0.2700 0.2125 -0.0053 -0.0015 0.0175  90  TYR A CE2 
730  C  CZ  . TYR A 93  ? 0.2201 0.2995 0.1681 0.0172  0.0407  0.0188  90  TYR A CZ  
731  O  OH  . TYR A 93  ? 0.2214 0.3915 0.2346 0.0086  0.0311  0.0687  90  TYR A OH  
732  N  N   . ASP A 94  ? 0.1201 0.1363 0.1499 -0.0045 0.0021  -0.0011 91  ASP A N   
733  C  CA  . ASP A 94  ? 0.1304 0.1428 0.1543 -0.0008 0.0064  -0.0027 91  ASP A CA  
734  C  C   . ASP A 94  ? 0.1440 0.1650 0.1574 -0.0137 0.0040  -0.0041 91  ASP A C   
735  O  O   . ASP A 94  ? 0.1662 0.2023 0.1598 -0.0389 0.0023  0.0019  91  ASP A O   
736  C  CB  . ASP A 94  ? 0.1378 0.1337 0.1706 0.0013  0.0139  0.0013  91  ASP A CB  
737  C  CG  . ASP A 94  ? 0.1403 0.1553 0.1946 0.0007  0.0093  -0.0034 91  ASP A CG  
738  O  OD1 . ASP A 94  ? 0.1463 0.1609 0.2037 0.0093  -0.0127 -0.0032 91  ASP A OD1 
739  O  OD2 . ASP A 94  ? 0.1574 0.1538 0.2183 -0.0078 0.0094  0.0010  91  ASP A OD2 
740  N  N   . ASP A 95  ? 0.1395 0.1700 0.1656 -0.0179 -0.0018 -0.0054 92  ASP A N   
741  C  CA  . ASP A 95  ? 0.1449 0.1609 0.1727 -0.0139 0.0042  -0.0058 92  ASP A CA  
742  C  C   . ASP A 95  ? 0.1160 0.1779 0.1726 -0.0081 0.0086  0.0115  92  ASP A C   
743  O  O   . ASP A 95  ? 0.1239 0.1690 0.1628 -0.0066 0.0088  0.0000  92  ASP A O   
744  C  CB  . ASP A 95  ? 0.1743 0.1649 0.2023 0.0015  0.0221  0.0066  92  ASP A CB  
745  C  CG  . ASP A 95  ? 0.1770 0.1858 0.2154 0.0053  0.0314  -0.0031 92  ASP A CG  
746  O  OD1 . ASP A 95  ? 0.1672 0.2053 0.2327 0.0086  0.0340  0.0046  92  ASP A OD1 
747  O  OD2 . ASP A 95  ? 0.1648 0.1932 0.2658 0.0140  0.0212  -0.0042 92  ASP A OD2 
748  N  N   . LEU A 96  ? 0.1260 0.1868 0.1711 -0.0143 -0.0118 0.0216  93  LEU A N   
749  C  CA  . LEU A 96  ? 0.1557 0.1886 0.2214 -0.0067 0.0049  0.0211  93  LEU A CA  
750  C  C   . LEU A 96  ? 0.1633 0.1582 0.2064 -0.0182 0.0060  0.0171  93  LEU A C   
751  O  O   . LEU A 96  ? 0.1417 0.1686 0.2610 -0.0062 0.0140  0.0140  93  LEU A O   
752  C  CB  . LEU A 96  ? 0.2554 0.2332 0.3488 0.0087  -0.0250 0.0427  93  LEU A CB  
753  C  CG  . LEU A 96  ? 0.2693 0.2812 0.4028 0.0171  -0.0568 0.0106  93  LEU A CG  
754  C  CD1 . LEU A 96  ? 0.2432 0.2553 0.3990 0.0631  -0.0521 0.0642  93  LEU A CD1 
755  C  CD2 . LEU A 96  ? 0.2619 0.2502 0.4670 0.0460  -0.0350 0.0004  93  LEU A CD2 
756  N  N   . ASP A 97  ? 0.1437 0.1605 0.2161 -0.0146 0.0115  0.0170  94  ASP A N   
757  C  CA  . ASP A 97  ? 0.1454 0.1735 0.2097 -0.0086 0.0033  0.0270  94  ASP A CA  
758  C  C   . ASP A 97  ? 0.1396 0.1752 0.1925 -0.0045 0.0104  0.0146  94  ASP A C   
759  O  O   . ASP A 97  ? 0.1536 0.2289 0.2442 0.0071  0.0260  0.0297  94  ASP A O   
760  C  CB  . ASP A 97  ? 0.1813 0.2155 0.2138 0.0060  0.0039  0.0328  94  ASP A CB  
761  C  CG  . ASP A 97  ? 0.2008 0.2393 0.2586 0.0076  0.0225  0.0255  94  ASP A CG  
762  O  OD1 . ASP A 97  ? 0.2149 0.2388 0.2830 0.0059  0.0184  0.0485  94  ASP A OD1 
763  O  OD2 . ASP A 97  ? 0.2579 0.3192 0.3014 0.0136  0.0492  -0.0090 94  ASP A OD2 
764  N  N   . LEU A 98  ? 0.1292 0.1627 0.1882 0.0005  0.0075  0.0122  95  LEU A N   
765  C  CA  . LEU A 98  ? 0.1237 0.1671 0.1898 0.0080  0.0057  0.0121  95  LEU A CA  
766  C  C   . LEU A 98  ? 0.1207 0.1683 0.1893 -0.0110 -0.0004 0.0149  95  LEU A C   
767  O  O   . LEU A 98  ? 0.1074 0.1846 0.1980 -0.0065 0.0085  0.0052  95  LEU A O   
768  C  CB  . LEU A 98  ? 0.1326 0.1782 0.2069 0.0088  0.0119  0.0078  95  LEU A CB  
769  C  CG  . LEU A 98  ? 0.1417 0.1949 0.2278 0.0223  0.0120  0.0106  95  LEU A CG  
770  C  CD1 . LEU A 98  ? 0.1501 0.2150 0.2496 0.0174  0.0053  0.0209  95  LEU A CD1 
771  C  CD2 . LEU A 98  ? 0.1493 0.1828 0.2607 0.0203  0.0117  -0.0053 95  LEU A CD2 
772  N  N   . ALA A 99  ? 0.1360 0.1673 0.1782 0.0014  -0.0036 0.0124  96  ALA A N   
773  C  CA  . ALA A 99  ? 0.1592 0.1730 0.1840 -0.0038 -0.0090 -0.0010 96  ALA A CA  
774  C  C   . ALA A 99  ? 0.1458 0.1745 0.1699 -0.0023 -0.0106 -0.0111 96  ALA A C   
775  O  O   . ALA A 99  ? 0.1503 0.1841 0.1792 -0.0015 -0.0027 -0.0127 96  ALA A O   
776  C  CB  . ALA A 99  ? 0.1897 0.1994 0.1833 -0.0152 -0.0143 -0.0019 96  ALA A CB  
777  N  N   . VAL A 100 ? 0.1530 0.1599 0.1843 0.0138  -0.0011 -0.0010 97  VAL A N   
778  C  CA  . VAL A 100 ? 0.1978 0.1710 0.1863 0.0048  0.0000  -0.0094 97  VAL A CA  
779  C  C   . VAL A 100 ? 0.1919 0.1688 0.1740 0.0084  -0.0039 -0.0218 97  VAL A C   
780  O  O   . VAL A 100 ? 0.1881 0.1858 0.1953 -0.0076 -0.0155 -0.0132 97  VAL A O   
781  C  CB  . VAL A 100 ? 0.2130 0.2034 0.1975 0.0054  0.0123  -0.0151 97  VAL A CB  
782  C  CG1 . VAL A 100 ? 0.2631 0.2386 0.2121 0.0094  0.0508  -0.0173 97  VAL A CG1 
783  C  CG2 . VAL A 100 ? 0.2081 0.2333 0.2252 0.0058  0.0029  -0.0131 97  VAL A CG2 
784  N  N   . GLY A 101 ? 0.2041 0.1668 0.2009 0.0039  -0.0048 -0.0071 98  GLY A N   
785  C  CA  . GLY A 101 ? 0.2085 0.2061 0.1869 0.0011  -0.0149 -0.0092 98  GLY A CA  
786  C  C   . GLY A 101 ? 0.2031 0.1889 0.2003 -0.0044 -0.0187 -0.0018 98  GLY A C   
787  O  O   . GLY A 101 ? 0.2050 0.2378 0.1853 0.0239  -0.0219 -0.0045 98  GLY A O   
788  N  N   . LYS A 102 ? 0.1750 0.1807 0.1980 -0.0058 -0.0035 -0.0084 99  LYS A N   
789  C  CA  . LYS A 102 ? 0.1715 0.1882 0.1813 0.0057  -0.0236 -0.0149 99  LYS A CA  
790  C  C   . LYS A 102 ? 0.1373 0.1779 0.1836 0.0046  -0.0205 -0.0043 99  LYS A C   
791  O  O   . LYS A 102 ? 0.1241 0.1822 0.2013 0.0123  -0.0121 -0.0123 99  LYS A O   
792  C  CB  . LYS A 102 ? 0.2069 0.1892 0.2124 0.0049  -0.0120 -0.0104 99  LYS A CB  
793  C  CG  . LYS A 102 ? 0.2365 0.2427 0.2427 -0.0319 -0.0091 -0.0020 99  LYS A CG  
794  C  CD  . LYS A 102 ? 0.2421 0.2884 0.2771 -0.0291 0.0133  0.0039  99  LYS A CD  
795  C  CE  . LYS A 102 ? 0.3347 0.3772 0.3580 -0.0193 -0.0287 -0.0176 99  LYS A CE  
796  N  NZ  . LYS A 102 ? 0.3782 0.4621 0.3933 0.0258  -0.0182 -0.0252 99  LYS A NZ  
797  N  N   . ILE A 103 ? 0.1194 0.1976 0.1843 0.0099  -0.0119 -0.0084 100 ILE A N   
798  C  CA  . ILE A 103 ? 0.1110 0.1782 0.1854 0.0176  -0.0139 -0.0075 100 ILE A CA  
799  C  C   . ILE A 103 ? 0.1288 0.1750 0.1788 0.0031  -0.0028 -0.0054 100 ILE A C   
800  O  O   . ILE A 103 ? 0.1351 0.2210 0.1852 0.0210  -0.0108 -0.0181 100 ILE A O   
801  C  CB  . ILE A 103 ? 0.1422 0.1863 0.1877 0.0251  -0.0058 -0.0026 100 ILE A CB  
802  C  CG1 . ILE A 103 ? 0.1533 0.1880 0.1933 0.0413  0.0177  0.0007  100 ILE A CG1 
803  C  CG2 . ILE A 103 ? 0.1675 0.2038 0.1868 0.0343  0.0074  0.0084  100 ILE A CG2 
804  C  CD1 . ILE A 103 ? 0.1677 0.2091 0.2034 0.0340  0.0128  0.0210  100 ILE A CD1 
805  N  N   . ARG A 104 ? 0.1216 0.1695 0.1778 0.0226  0.0078  -0.0172 101 ARG A N   
806  C  CA  . ARG A 104 ? 0.1215 0.1789 0.1942 0.0216  0.0129  -0.0097 101 ARG A CA  
807  C  C   . ARG A 104 ? 0.1275 0.1862 0.2006 0.0064  0.0162  -0.0214 101 ARG A C   
808  O  O   . ARG A 104 ? 0.1270 0.2037 0.2441 0.0104  0.0037  -0.0315 101 ARG A O   
809  C  CB  . ARG A 104 ? 0.1885 0.2135 0.2089 0.0120  0.0191  0.0016  101 ARG A CB  
810  C  CG  . ARG A 104 ? 0.2707 0.2798 0.3254 0.0308  0.0543  0.0094  101 ARG A CG  
811  C  CD  . ARG A 104 ? 0.2101 0.3213 0.3877 0.0393  0.0554  0.0435  101 ARG A CD  
812  N  NE  . ARG A 104 ? 0.1888 0.4606 0.4120 0.0537  0.1103  0.0282  101 ARG A NE  
813  C  CZ  . ARG A 104 ? 0.2572 0.4581 0.4131 0.0153  0.1109  0.0280  101 ARG A CZ  
814  N  NH1 . ARG A 104 ? 0.2730 0.3709 0.4624 0.0022  0.1239  0.0737  101 ARG A NH1 
815  N  NH2 . ARG A 104 ? 0.2091 0.5477 0.3028 0.0303  0.0889  0.0167  101 ARG A NH2 
816  N  N   . LEU A 105 ? 0.1198 0.1856 0.2064 0.0076  0.0039  -0.0255 102 LEU A N   
817  C  CA  . LEU A 105 ? 0.1249 0.1776 0.1871 0.0094  0.0043  -0.0146 102 LEU A CA  
818  C  C   . LEU A 105 ? 0.1376 0.1744 0.1775 0.0018  0.0062  -0.0135 102 LEU A C   
819  O  O   . LEU A 105 ? 0.1377 0.2069 0.1856 -0.0042 0.0173  -0.0181 102 LEU A O   
820  C  CB  . LEU A 105 ? 0.1539 0.1910 0.1887 0.0235  0.0117  -0.0174 102 LEU A CB  
821  C  CG  . LEU A 105 ? 0.1734 0.2076 0.1968 0.0163  0.0023  -0.0056 102 LEU A CG  
822  C  CD1 . LEU A 105 ? 0.1715 0.2465 0.2090 0.0218  0.0056  -0.0092 102 LEU A CD1 
823  C  CD2 . LEU A 105 ? 0.1863 0.1965 0.1923 0.0038  -0.0015 0.0025  102 LEU A CD2 
824  N  N   . ARG A 106 ? 0.1418 0.1775 0.1838 0.0044  -0.0028 -0.0169 103 ARG A N   
825  C  CA  . ARG A 106 ? 0.1433 0.1819 0.1994 -0.0006 0.0077  -0.0054 103 ARG A CA  
826  C  C   . ARG A 106 ? 0.1477 0.1829 0.1942 -0.0090 0.0037  0.0014  103 ARG A C   
827  O  O   . ARG A 106 ? 0.1484 0.1961 0.1959 -0.0073 0.0113  -0.0188 103 ARG A O   
828  C  CB  . ARG A 106 ? 0.1522 0.1961 0.2308 -0.0087 -0.0093 0.0025  103 ARG A CB  
829  C  CG  . ARG A 106 ? 0.1799 0.1954 0.2769 -0.0068 -0.0128 0.0105  103 ARG A CG  
830  C  CD  . ARG A 106 ? 0.2011 0.2156 0.3547 0.0007  0.0051  0.0006  103 ARG A CD  
831  N  NE  . ARG A 106 ? 0.2553 0.2511 0.4455 -0.0251 -0.0111 -0.0061 103 ARG A NE  
832  C  CZ  . ARG A 106 ? 0.2328 0.2616 0.4906 -0.0126 -0.0109 -0.0212 103 ARG A CZ  
833  N  NH1 . ARG A 106 ? 0.1601 0.3138 0.5097 -0.0060 -0.0238 -0.0309 103 ARG A NH1 
834  N  NH2 . ARG A 106 ? 0.2332 0.3032 0.5084 0.0021  0.0269  -0.0723 103 ARG A NH2 
835  N  N   . GLN A 107 ? 0.1100 0.1966 0.1980 -0.0107 0.0165  -0.0068 104 GLN A N   
836  C  CA  . GLN A 107 ? 0.1578 0.2103 0.1911 0.0036  0.0172  -0.0345 104 GLN A CA  
837  C  C   . GLN A 107 ? 0.1601 0.2239 0.1907 0.0069  0.0265  -0.0215 104 GLN A C   
838  O  O   . GLN A 107 ? 0.1811 0.2542 0.1992 -0.0060 -0.0001 -0.0218 104 GLN A O   
839  C  CB  . GLN A 107 ? 0.1824 0.2042 0.2023 0.0097  0.0088  -0.0226 104 GLN A CB  
840  C  CG  . GLN A 107 ? 0.1921 0.2215 0.1945 0.0234  -0.0026 -0.0169 104 GLN A CG  
841  C  CD  . GLN A 107 ? 0.1935 0.2220 0.2074 0.0128  0.0158  -0.0217 104 GLN A CD  
842  O  OE1 . GLN A 107 ? 0.1936 0.2030 0.2490 0.0037  0.0275  -0.0300 104 GLN A OE1 
843  N  NE2 . GLN A 107 ? 0.1881 0.2258 0.2418 0.0262  -0.0081 -0.0144 104 GLN A NE2 
844  N  N   . LYS A 108 ? 0.1567 0.2632 0.1968 -0.0098 0.0081  -0.0064 105 LYS A N   
845  C  CA  . LYS A 108 ? 0.1809 0.3139 0.2120 -0.0101 0.0276  0.0156  105 LYS A CA  
846  C  C   . LYS A 108 ? 0.2170 0.3149 0.2588 -0.0090 -0.0090 0.0302  105 LYS A C   
847  O  O   . LYS A 108 ? 0.2584 0.2890 0.3458 -0.0122 -0.0600 0.0392  105 LYS A O   
848  C  CB  . LYS A 108 ? 0.2142 0.3467 0.2389 0.0025  0.0472  0.0145  105 LYS A CB  
849  C  CG  . LYS A 108 ? 0.2761 0.3743 0.2497 -0.0077 0.0359  0.0180  105 LYS A CG  
850  C  CD  . LYS A 108 ? 0.3098 0.4278 0.2640 0.0286  0.0665  0.0188  105 LYS A CD  
851  C  CE  . LYS A 108 ? 0.3759 0.5082 0.3330 0.0350  0.0659  -0.0002 105 LYS A CE  
852  N  NZ  . LYS A 108 ? 0.4316 0.5210 0.3407 0.0677  0.0978  0.0543  105 LYS A NZ  
853  N  N   . GLY A 109 ? 0.2738 0.3251 0.2693 -0.0058 -0.0472 0.0512  106 GLY A N   
854  C  CA  . GLY A 109 ? 0.2898 0.2956 0.3106 -0.0180 -0.0245 0.0478  106 GLY A CA  
855  C  C   . GLY A 109 ? 0.2709 0.2997 0.3075 -0.0341 -0.0110 0.0420  106 GLY A C   
856  O  O   . GLY A 109 ? 0.2950 0.3343 0.3042 -0.0914 -0.0692 0.0330  106 GLY A O   
857  N  N   . SER A 110 ? 0.3021 0.3119 0.3365 -0.0225 -0.0100 0.0623  107 SER A N   
858  C  CA  A SER A 110 ? 0.2863 0.2838 0.3044 0.0066  0.0186  0.0533  107 SER A CA  
859  C  CA  B SER A 110 ? 0.2873 0.2919 0.3138 0.0133  0.0076  0.0625  107 SER A CA  
860  C  C   . SER A 110 ? 0.2961 0.2765 0.2895 0.0049  0.0031  0.0621  107 SER A C   
861  O  O   . SER A 110 ? 0.2593 0.3392 0.3130 0.0312  0.0383  0.0589  107 SER A O   
862  C  CB  A SER A 110 ? 0.3247 0.3135 0.3059 0.0257  0.0227  0.0263  107 SER A CB  
863  C  CB  B SER A 110 ? 0.3209 0.3526 0.3291 0.0403  -0.0101 0.0561  107 SER A CB  
864  O  OG  A SER A 110 ? 0.3395 0.2982 0.2884 0.0188  0.0456  0.0056  107 SER A OG  
865  O  OG  B SER A 110 ? 0.3420 0.3431 0.3383 0.0601  0.0006  0.0407  107 SER A OG  
866  N  N   . ALA A 111 ? 0.2617 0.3045 0.2606 0.0088  0.0247  0.0210  108 ALA A N   
867  C  CA  . ALA A 111 ? 0.2405 0.3123 0.2922 -0.0011 0.0497  0.0299  108 ALA A CA  
868  C  C   . ALA A 111 ? 0.2496 0.3082 0.3157 -0.0258 0.0234  0.0265  108 ALA A C   
869  O  O   . ALA A 111 ? 0.2848 0.2883 0.3374 0.0005  0.0041  0.0003  108 ALA A O   
870  C  CB  . ALA A 111 ? 0.2645 0.3304 0.2754 -0.0124 0.0477  0.0637  108 ALA A CB  
871  N  N   . GLY A 112 ? 0.2944 0.2933 0.3515 -0.0160 0.0312  0.0419  109 GLY A N   
872  C  CA  . GLY A 112 ? 0.3164 0.2948 0.3799 0.0140  0.0305  0.0722  109 GLY A CA  
873  C  C   . GLY A 112 ? 0.3072 0.3010 0.3592 -0.0073 0.0201  0.0503  109 GLY A C   
874  O  O   . GLY A 112 ? 0.3732 0.2899 0.4327 -0.0042 0.0378  0.0059  109 GLY A O   
875  N  N   . GLY A 113 ? 0.2993 0.2779 0.2615 0.0416  0.0047  0.0357  110 GLY A N   
876  C  CA  . GLY A 113 ? 0.3024 0.3495 0.2760 0.0254  0.0014  0.0246  110 GLY A CA  
877  C  C   . GLY A 113 ? 0.2883 0.2974 0.2764 0.0056  0.0059  0.0227  110 GLY A C   
878  O  O   . GLY A 113 ? 0.3017 0.3383 0.3195 0.0260  -0.0083 0.0340  110 GLY A O   
879  N  N   . HIS A 114 ? 0.2407 0.2148 0.2436 -0.0303 -0.0026 0.0140  111 HIS A N   
880  C  CA  . HIS A 114 ? 0.2334 0.2056 0.2313 -0.0243 -0.0019 0.0159  111 HIS A CA  
881  C  C   . HIS A 114 ? 0.2398 0.1754 0.2518 -0.0155 -0.0002 0.0252  111 HIS A C   
882  O  O   . HIS A 114 ? 0.2307 0.2289 0.2419 -0.0123 0.0181  -0.0283 111 HIS A O   
883  C  CB  . HIS A 114 ? 0.2145 0.2068 0.2422 -0.0253 0.0029  0.0159  111 HIS A CB  
884  C  CG  . HIS A 114 ? 0.2077 0.2045 0.2186 -0.0147 -0.0113 0.0067  111 HIS A CG  
885  N  ND1 . HIS A 114 ? 0.2061 0.2464 0.2095 -0.0228 -0.0245 -0.0138 111 HIS A ND1 
886  C  CD2 . HIS A 114 ? 0.2124 0.2080 0.2295 -0.0062 -0.0128 0.0099  111 HIS A CD2 
887  C  CE1 . HIS A 114 ? 0.2383 0.2292 0.2022 -0.0205 -0.0110 -0.0036 111 HIS A CE1 
888  N  NE2 . HIS A 114 ? 0.2053 0.1995 0.2144 -0.0194 -0.0123 0.0052  111 HIS A NE2 
889  N  N   . ASN A 115 ? 0.2548 0.2057 0.2893 0.0215  -0.0396 0.0143  112 ASN A N   
890  C  CA  . ASN A 115 ? 0.2778 0.2071 0.3035 0.0281  -0.0246 0.0016  112 ASN A CA  
891  C  C   . ASN A 115 ? 0.2448 0.2161 0.2252 -0.0017 -0.0054 0.0249  112 ASN A C   
892  O  O   . ASN A 115 ? 0.2953 0.2149 0.2097 0.0087  -0.0296 0.0086  112 ASN A O   
893  C  CB  . ASN A 115 ? 0.3215 0.2793 0.3897 0.0555  -0.0101 0.0000  112 ASN A CB  
894  C  CG  . ASN A 115 ? 0.3883 0.3449 0.4528 0.0794  0.0049  0.0051  112 ASN A CG  
895  O  OD1 . ASN A 115 ? 0.5541 0.3902 0.4629 0.0202  0.0339  0.0993  112 ASN A OD1 
896  N  ND2 . ASN A 115 ? 0.4351 0.4765 0.5649 0.1584  0.0065  -0.0026 112 ASN A ND2 
897  N  N   . GLY A 116 ? 0.1840 0.2221 0.2157 0.0041  -0.0132 -0.0141 113 GLY A N   
898  C  CA  . GLY A 116 ? 0.1623 0.2360 0.1940 -0.0089 -0.0122 -0.0023 113 GLY A CA  
899  C  C   . GLY A 116 ? 0.1715 0.2115 0.1800 -0.0095 -0.0118 0.0123  113 GLY A C   
900  O  O   . GLY A 116 ? 0.1609 0.2090 0.1798 -0.0140 -0.0020 -0.0010 113 GLY A O   
901  N  N   . ILE A 117 ? 0.1576 0.2034 0.1807 -0.0173 0.0000  -0.0120 114 ILE A N   
902  C  CA  . ILE A 117 ? 0.1524 0.2179 0.1644 0.0011  -0.0119 0.0040  114 ILE A CA  
903  C  C   . ILE A 117 ? 0.1722 0.2208 0.1726 -0.0154 -0.0146 -0.0021 114 ILE A C   
904  O  O   . ILE A 117 ? 0.1675 0.2141 0.1720 -0.0219 -0.0030 -0.0046 114 ILE A O   
905  C  CB  . ILE A 117 ? 0.1780 0.2350 0.1899 -0.0202 -0.0062 -0.0164 114 ILE A CB  
906  C  CG1 . ILE A 117 ? 0.1572 0.2405 0.1774 -0.0066 0.0029  -0.0148 114 ILE A CG1 
907  C  CG2 . ILE A 117 ? 0.1891 0.2489 0.1809 -0.0334 0.0028  -0.0039 114 ILE A CG2 
908  C  CD1 . ILE A 117 ? 0.1634 0.2630 0.1706 -0.0130 -0.0075 -0.0071 114 ILE A CD1 
909  N  N   . LYS A 118 ? 0.1845 0.2046 0.1674 -0.0285 -0.0114 -0.0010 115 LYS A N   
910  C  CA  . LYS A 118 ? 0.1873 0.2259 0.1674 -0.0341 0.0026  0.0096  115 LYS A CA  
911  C  C   . LYS A 118 ? 0.1744 0.2093 0.1642 -0.0236 0.0082  0.0181  115 LYS A C   
912  O  O   . LYS A 118 ? 0.1775 0.2239 0.1633 -0.0342 0.0059  0.0015  115 LYS A O   
913  C  CB  . LYS A 118 ? 0.2069 0.2245 0.1809 -0.0320 -0.0034 0.0098  115 LYS A CB  
914  C  CG  . LYS A 118 ? 0.2600 0.2503 0.1952 -0.0110 -0.0001 0.0177  115 LYS A CG  
915  C  CD  . LYS A 118 ? 0.3485 0.2520 0.1997 -0.0104 0.0077  0.0233  115 LYS A CD  
916  C  CE  . LYS A 118 ? 0.4089 0.3030 0.2519 0.0260  -0.0153 0.0273  115 LYS A CE  
917  N  NZ  . LYS A 118 ? 0.4154 0.3203 0.2637 0.0381  0.0010  0.0682  115 LYS A NZ  
918  N  N   . SER A 119 ? 0.1424 0.2096 0.1554 -0.0221 -0.0087 0.0094  116 SER A N   
919  C  CA  . SER A 119 ? 0.1577 0.1866 0.1648 -0.0189 -0.0086 0.0083  116 SER A CA  
920  C  C   . SER A 119 ? 0.1689 0.2034 0.1862 -0.0105 -0.0040 -0.0055 116 SER A C   
921  O  O   . SER A 119 ? 0.1729 0.2071 0.1898 -0.0223 -0.0029 -0.0067 116 SER A O   
922  C  CB  . SER A 119 ? 0.1715 0.2118 0.1677 -0.0052 -0.0112 -0.0033 116 SER A CB  
923  O  OG  . SER A 119 ? 0.1694 0.2070 0.1739 -0.0150 0.0046  0.0098  116 SER A OG  
924  N  N   . ILE A 120 ? 0.1645 0.1883 0.1699 -0.0078 -0.0012 -0.0049 117 ILE A N   
925  C  CA  . ILE A 120 ? 0.1508 0.2053 0.1681 0.0086  0.0033  -0.0098 117 ILE A CA  
926  C  C   . ILE A 120 ? 0.1533 0.2133 0.1836 -0.0028 0.0223  -0.0101 117 ILE A C   
927  O  O   . ILE A 120 ? 0.1886 0.2215 0.1958 -0.0048 0.0266  -0.0321 117 ILE A O   
928  C  CB  . ILE A 120 ? 0.1675 0.2202 0.1874 0.0009  -0.0013 -0.0082 117 ILE A CB  
929  C  CG1 . ILE A 120 ? 0.2035 0.2392 0.1924 0.0145  0.0002  -0.0244 117 ILE A CG1 
930  C  CG2 . ILE A 120 ? 0.2112 0.2286 0.2042 0.0157  0.0004  -0.0082 117 ILE A CG2 
931  C  CD1 . ILE A 120 ? 0.2191 0.2311 0.2060 0.0061  -0.0064 -0.0234 117 ILE A CD1 
932  N  N   . ILE A 121 ? 0.1744 0.2321 0.1690 -0.0248 0.0318  -0.0239 118 ILE A N   
933  C  CA  . ILE A 121 ? 0.2180 0.2870 0.1706 -0.0256 0.0284  -0.0254 118 ILE A CA  
934  C  C   . ILE A 121 ? 0.2364 0.2824 0.1912 -0.0429 0.0280  -0.0409 118 ILE A C   
935  O  O   . ILE A 121 ? 0.2612 0.3874 0.2308 -0.0668 0.0548  -0.0941 118 ILE A O   
936  C  CB  . ILE A 121 ? 0.2047 0.3186 0.1602 -0.0421 0.0176  -0.0148 118 ILE A CB  
937  C  CG1 . ILE A 121 ? 0.1755 0.3142 0.1922 -0.0414 0.0099  -0.0053 118 ILE A CG1 
938  C  CG2 . ILE A 121 ? 0.2270 0.3485 0.1706 -0.0500 0.0244  -0.0301 118 ILE A CG2 
939  C  CD1 . ILE A 121 ? 0.1816 0.3218 0.1758 -0.0354 -0.0165 0.0138  118 ILE A CD1 
940  N  N   . SER A 122 ? 0.2326 0.3075 0.1682 -0.0625 0.0164  -0.0316 119 SER A N   
941  C  CA  . SER A 122 ? 0.2741 0.3309 0.1707 -0.0982 -0.0007 0.0041  119 SER A CA  
942  C  C   . SER A 122 ? 0.2640 0.3466 0.1815 -0.0817 0.0015  -0.0411 119 SER A C   
943  O  O   . SER A 122 ? 0.3490 0.3908 0.1854 -0.1071 0.0251  -0.0741 119 SER A O   
944  C  CB  . SER A 122 ? 0.3003 0.3509 0.2225 -0.1057 -0.0278 0.0224  119 SER A CB  
945  O  OG  . SER A 122 ? 0.3249 0.4226 0.2938 -0.0916 -0.0605 0.0170  119 SER A OG  
946  N  N   . HIS A 123 ? 0.2083 0.2929 0.1925 -0.0802 0.0177  -0.0313 120 HIS A N   
947  C  CA  . HIS A 123 ? 0.2292 0.2867 0.2080 -0.0606 0.0019  -0.0492 120 HIS A CA  
948  C  C   . HIS A 123 ? 0.2552 0.2928 0.2623 -0.0444 0.0096  -0.0701 120 HIS A C   
949  O  O   . HIS A 123 ? 0.2863 0.3115 0.3732 -0.0683 -0.0179 -0.1015 120 HIS A O   
950  C  CB  . HIS A 123 ? 0.2342 0.2600 0.2125 -0.0672 0.0211  -0.0231 120 HIS A CB  
951  C  CG  . HIS A 123 ? 0.2247 0.2949 0.1719 -0.0523 0.0068  -0.0097 120 HIS A CG  
952  N  ND1 . HIS A 123 ? 0.2160 0.2773 0.2219 -0.0320 0.0087  -0.0439 120 HIS A ND1 
953  C  CD2 . HIS A 123 ? 0.1858 0.2966 0.2101 -0.0473 -0.0193 -0.0303 120 HIS A CD2 
954  C  CE1 . HIS A 123 ? 0.2318 0.2967 0.2551 -0.0106 -0.0004 -0.0420 120 HIS A CE1 
955  N  NE2 . HIS A 123 ? 0.1991 0.3359 0.2505 -0.0364 -0.0085 -0.0111 120 HIS A NE2 
956  N  N   . LEU A 124 ? 0.2459 0.2800 0.2736 -0.0018 -0.0159 -0.1050 121 LEU A N   
957  C  CA  . LEU A 124 ? 0.2568 0.3185 0.2821 0.0210  -0.0081 -0.0894 121 LEU A CA  
958  C  C   . LEU A 124 ? 0.2229 0.3415 0.2708 0.0246  -0.0247 -0.0905 121 LEU A C   
959  O  O   . LEU A 124 ? 0.2662 0.3715 0.3385 0.0630  -0.0290 -0.1168 121 LEU A O   
960  C  CB  . LEU A 124 ? 0.2454 0.3292 0.3007 0.0709  -0.0222 -0.0645 121 LEU A CB  
961  C  CG  . LEU A 124 ? 0.3604 0.3520 0.3192 0.0403  -0.0207 -0.0433 121 LEU A CG  
962  C  CD1 . LEU A 124 ? 0.3827 0.3386 0.2732 0.0684  -0.0151 -0.0226 121 LEU A CD1 
963  C  CD2 . LEU A 124 ? 0.3824 0.3567 0.3829 0.0291  -0.0155 -0.0501 121 LEU A CD2 
964  N  N   . ASN A 125 ? 0.2136 0.3564 0.2583 0.0326  -0.0470 -0.0971 122 ASN A N   
965  C  CA  . ASN A 125 ? 0.2437 0.3959 0.2475 0.0421  -0.0507 -0.0899 122 ASN A CA  
966  C  C   . ASN A 125 ? 0.2250 0.4731 0.2485 0.0356  -0.0418 -0.1093 122 ASN A C   
967  O  O   . ASN A 125 ? 0.2519 0.5948 0.2472 0.0292  -0.0284 -0.1227 122 ASN A O   
968  C  CB  . ASN A 125 ? 0.3704 0.4180 0.3129 0.0187  -0.0682 -0.1154 122 ASN A CB  
969  C  CG  . ASN A 125 ? 0.4349 0.4177 0.3447 0.0013  -0.0768 -0.0723 122 ASN A CG  
970  O  OD1 . ASN A 125 ? 0.5326 0.3949 0.2910 -0.1011 -0.1121 0.0316  122 ASN A OD1 
971  N  ND2 . ASN A 125 ? 0.5172 0.4559 0.4726 -0.0520 -0.0382 -0.0730 122 ASN A ND2 
972  N  N   . THR A 126 ? 0.1895 0.4770 0.1909 0.0371  -0.0040 -0.0815 123 THR A N   
973  C  CA  . THR A 126 ? 0.1785 0.4469 0.2097 -0.0055 0.0169  -0.0737 123 THR A CA  
974  C  C   . THR A 126 ? 0.1760 0.4034 0.1928 -0.0024 -0.0064 -0.0284 123 THR A C   
975  O  O   . THR A 126 ? 0.1439 0.3720 0.2090 0.0081  -0.0052 -0.0437 123 THR A O   
976  C  CB  . THR A 126 ? 0.2203 0.4284 0.2379 -0.0001 0.0201  -0.0712 123 THR A CB  
977  O  OG1 . THR A 126 ? 0.2327 0.4024 0.2248 0.0312  0.0180  -0.0724 123 THR A OG1 
978  C  CG2 . THR A 126 ? 0.2507 0.4404 0.2965 0.0048  0.0061  -0.0507 123 THR A CG2 
979  N  N   . ASN A 127 ? 0.2001 0.3738 0.2048 -0.0255 0.0132  -0.0183 124 ASN A N   
980  C  CA  . ASN A 127 ? 0.1783 0.3433 0.2290 0.0072  -0.0175 -0.0117 124 ASN A CA  
981  C  C   . ASN A 127 ? 0.1718 0.2843 0.1909 0.0011  0.0046  -0.0258 124 ASN A C   
982  O  O   . ASN A 127 ? 0.1548 0.2966 0.2332 0.0040  0.0203  -0.0399 124 ASN A O   
983  C  CB  . ASN A 127 ? 0.2356 0.3743 0.2806 -0.0123 -0.0256 0.0094  124 ASN A CB  
984  C  CG  . ASN A 127 ? 0.2802 0.3947 0.2930 -0.0549 -0.0025 0.0437  124 ASN A CG  
985  O  OD1 . ASN A 127 ? 0.2338 0.4401 0.2552 -0.0465 0.0100  0.0346  124 ASN A OD1 
986  N  ND2 . ASN A 127 ? 0.3441 0.4320 0.3680 -0.0835 -0.0203 0.0586  124 ASN A ND2 
987  N  N   . VAL A 128 ? 0.1725 0.2798 0.1951 -0.0008 0.0066  -0.0311 125 VAL A N   
988  C  CA  . VAL A 128 ? 0.1821 0.2325 0.2031 0.0025  0.0097  -0.0295 125 VAL A CA  
989  C  C   . VAL A 128 ? 0.1552 0.2462 0.2169 -0.0071 0.0246  -0.0304 125 VAL A C   
990  O  O   . VAL A 128 ? 0.2161 0.2607 0.2161 -0.0354 -0.0005 -0.0440 125 VAL A O   
991  C  CB  . VAL A 128 ? 0.2030 0.2769 0.2337 -0.0016 0.0161  -0.0365 125 VAL A CB  
992  C  CG1 . VAL A 128 ? 0.2068 0.2855 0.2138 0.0190  0.0143  -0.0311 125 VAL A CG1 
993  C  CG2 . VAL A 128 ? 0.2084 0.2794 0.2545 0.0097  0.0155  -0.0233 125 VAL A CG2 
994  N  N   . PHE A 129 ? 0.1732 0.2241 0.2143 -0.0037 0.0150  -0.0318 126 PHE A N   
995  C  CA  . PHE A 129 ? 0.1492 0.2030 0.2043 -0.0017 -0.0004 -0.0263 126 PHE A CA  
996  C  C   . PHE A 129 ? 0.1367 0.1912 0.1937 0.0078  0.0089  -0.0372 126 PHE A C   
997  O  O   . PHE A 129 ? 0.1673 0.1983 0.1754 0.0098  0.0003  -0.0347 126 PHE A O   
998  C  CB  . PHE A 129 ? 0.1502 0.2152 0.2036 -0.0052 0.0135  -0.0160 126 PHE A CB  
999  C  CG  . PHE A 129 ? 0.1468 0.2342 0.1893 0.0012  0.0169  -0.0085 126 PHE A CG  
1000 C  CD1 . PHE A 129 ? 0.1426 0.2418 0.1797 0.0040  -0.0030 -0.0130 126 PHE A CD1 
1001 C  CD2 . PHE A 129 ? 0.1715 0.2636 0.1710 -0.0023 0.0194  -0.0161 126 PHE A CD2 
1002 C  CE1 . PHE A 129 ? 0.1838 0.2425 0.2014 0.0125  0.0068  0.0066  126 PHE A CE1 
1003 C  CE2 . PHE A 129 ? 0.1829 0.2911 0.1878 -0.0074 -0.0032 0.0126  126 PHE A CE2 
1004 C  CZ  . PHE A 129 ? 0.1851 0.2651 0.1965 0.0048  0.0198  0.0155  126 PHE A CZ  
1005 N  N   . ASP A 130 ? 0.1499 0.1737 0.2029 -0.0022 0.0101  -0.0340 127 ASP A N   
1006 C  CA  . ASP A 130 ? 0.1430 0.1872 0.1830 -0.0013 0.0211  -0.0391 127 ASP A CA  
1007 C  C   . ASP A 130 ? 0.1464 0.1782 0.2013 0.0071  0.0117  -0.0367 127 ASP A C   
1008 O  O   . ASP A 130 ? 0.1563 0.1887 0.1912 0.0061  0.0008  -0.0103 127 ASP A O   
1009 C  CB  . ASP A 130 ? 0.1699 0.2002 0.2164 0.0127  -0.0190 -0.0390 127 ASP A CB  
1010 C  CG  . ASP A 130 ? 0.1998 0.1894 0.2202 0.0081  -0.0288 -0.0382 127 ASP A CG  
1011 O  OD1 . ASP A 130 ? 0.1700 0.2320 0.2963 0.0423  -0.0106 -0.0480 127 ASP A OD1 
1012 O  OD2 . ASP A 130 ? 0.2613 0.2053 0.3186 0.0110  -0.0744 0.0021  127 ASP A OD2 
1013 N  N   . ARG A 131 ? 0.1240 0.1807 0.2065 0.0136  -0.0088 -0.0314 128 ARG A N   
1014 C  CA  . ARG A 131 ? 0.1551 0.1962 0.1875 0.0239  0.0114  -0.0383 128 ARG A CA  
1015 C  C   . ARG A 131 ? 0.1336 0.1636 0.1889 0.0160  0.0084  -0.0202 128 ARG A C   
1016 O  O   . ARG A 131 ? 0.1481 0.1845 0.2034 -0.0030 0.0029  -0.0202 128 ARG A O   
1017 C  CB  . ARG A 131 ? 0.1981 0.2167 0.2055 0.0204  0.0129  -0.0339 128 ARG A CB  
1018 C  CG  . ARG A 131 ? 0.1866 0.2087 0.2207 0.0131  0.0216  -0.0185 128 ARG A CG  
1019 C  CD  . ARG A 131 ? 0.2183 0.2641 0.2414 0.0052  0.0317  0.0005  128 ARG A CD  
1020 N  NE  . ARG A 131 ? 0.2267 0.2714 0.2212 0.0291  0.0189  0.0037  128 ARG A NE  
1021 C  CZ  . ARG A 131 ? 0.2059 0.2955 0.2646 -0.0106 0.0012  0.0137  128 ARG A CZ  
1022 N  NH1 . ARG A 131 ? 0.1901 0.2661 0.2096 -0.0187 0.0211  0.0196  128 ARG A NH1 
1023 N  NH2 . ARG A 131 ? 0.1833 0.3012 0.3011 -0.0038 -0.0040 0.0169  128 ARG A NH2 
1024 N  N   . ILE A 132 ? 0.1257 0.1506 0.1749 0.0006  0.0039  -0.0167 129 ILE A N   
1025 C  CA  . ILE A 132 ? 0.1047 0.1616 0.1696 -0.0056 -0.0045 -0.0025 129 ILE A CA  
1026 C  C   . ILE A 132 ? 0.1210 0.1541 0.1627 0.0058  0.0024  -0.0130 129 ILE A C   
1027 O  O   . ILE A 132 ? 0.1177 0.1604 0.1878 0.0123  0.0071  -0.0110 129 ILE A O   
1028 C  CB  . ILE A 132 ? 0.1466 0.1837 0.1816 0.0097  -0.0055 0.0000  129 ILE A CB  
1029 C  CG1 . ILE A 132 ? 0.1653 0.1991 0.1867 0.0183  0.0082  0.0005  129 ILE A CG1 
1030 C  CG2 . ILE A 132 ? 0.1568 0.1916 0.1562 0.0242  -0.0118 0.0058  129 ILE A CG2 
1031 C  CD1 . ILE A 132 ? 0.1955 0.2205 0.2101 0.0111  0.0011  0.0180  129 ILE A CD1 
1032 N  N   . LYS A 133 ? 0.1315 0.1633 0.1843 0.0023  -0.0003 -0.0148 130 LYS A N   
1033 C  CA  . LYS A 133 ? 0.1266 0.1656 0.1814 0.0059  -0.0003 -0.0178 130 LYS A CA  
1034 C  C   . LYS A 133 ? 0.1422 0.1756 0.1635 0.0006  -0.0070 -0.0071 130 LYS A C   
1035 O  O   . LYS A 133 ? 0.1196 0.2000 0.1921 -0.0034 0.0048  -0.0189 130 LYS A O   
1036 C  CB  . LYS A 133 ? 0.1740 0.1601 0.1930 0.0251  0.0001  -0.0006 130 LYS A CB  
1037 C  CG  . LYS A 133 ? 0.2166 0.2004 0.2174 0.0478  0.0133  0.0151  130 LYS A CG  
1038 C  CD  . LYS A 133 ? 0.2867 0.2611 0.2523 0.0440  0.0185  0.0524  130 LYS A CD  
1039 C  CE  . LYS A 133 ? 0.3120 0.3298 0.3376 0.0511  0.0361  0.0481  130 LYS A CE  
1040 N  NZ  . LYS A 133 ? 0.2915 0.2984 0.3072 0.0398  0.0622  0.0455  130 LYS A NZ  
1041 N  N   . VAL A 134 ? 0.1421 0.1639 0.1580 0.0120  -0.0054 -0.0107 131 VAL A N   
1042 C  CA  . VAL A 134 ? 0.1245 0.1648 0.1564 0.0034  -0.0093 -0.0034 131 VAL A CA  
1043 C  C   . VAL A 134 ? 0.1428 0.1573 0.1483 0.0014  -0.0079 -0.0059 131 VAL A C   
1044 O  O   . VAL A 134 ? 0.1460 0.1653 0.1633 0.0156  -0.0152 0.0033  131 VAL A O   
1045 C  CB  . VAL A 134 ? 0.1353 0.1669 0.1731 0.0096  -0.0031 -0.0017 131 VAL A CB  
1046 C  CG1 . VAL A 134 ? 0.1326 0.1890 0.1787 0.0054  -0.0099 0.0032  131 VAL A CG1 
1047 C  CG2 . VAL A 134 ? 0.1686 0.1625 0.1785 -0.0092 -0.0172 0.0077  131 VAL A CG2 
1048 N  N   . GLY A 135 ? 0.1376 0.1566 0.1749 -0.0015 -0.0011 -0.0032 132 GLY A N   
1049 C  CA  . GLY A 135 ? 0.1375 0.1682 0.1738 -0.0034 0.0024  -0.0016 132 GLY A CA  
1050 C  C   . GLY A 135 ? 0.1281 0.1608 0.1576 -0.0067 0.0037  0.0043  132 GLY A C   
1051 O  O   . GLY A 135 ? 0.1410 0.1713 0.1566 0.0109  0.0086  0.0008  132 GLY A O   
1052 N  N   . ILE A 136 ? 0.1143 0.1563 0.1497 -0.0004 0.0194  0.0002  133 ILE A N   
1053 C  CA  . ILE A 136 ? 0.1234 0.1554 0.1632 0.0081  0.0117  -0.0055 133 ILE A CA  
1054 C  C   . ILE A 136 ? 0.1424 0.1634 0.1774 0.0004  0.0008  -0.0049 133 ILE A C   
1055 O  O   . ILE A 136 ? 0.1272 0.1547 0.1950 0.0083  0.0005  -0.0122 133 ILE A O   
1056 C  CB  . ILE A 136 ? 0.1136 0.1622 0.1872 0.0031  0.0095  0.0047  133 ILE A CB  
1057 C  CG1 . ILE A 136 ? 0.1063 0.1601 0.1875 0.0037  0.0188  0.0024  133 ILE A CG1 
1058 C  CG2 . ILE A 136 ? 0.1436 0.1635 0.1883 -0.0013 0.0034  0.0106  133 ILE A CG2 
1059 C  CD1 . ILE A 136 ? 0.1166 0.1595 0.1952 0.0152  0.0141  -0.0172 133 ILE A CD1 
1060 N  N   . GLY A 137 ? 0.1369 0.1509 0.2078 -0.0032 -0.0073 -0.0075 134 GLY A N   
1061 C  CA  . GLY A 137 ? 0.1475 0.1600 0.2115 0.0106  -0.0019 0.0001  134 GLY A CA  
1062 C  C   . GLY A 137 ? 0.1623 0.1394 0.2142 0.0003  -0.0070 0.0076  134 GLY A C   
1063 O  O   . GLY A 137 ? 0.1547 0.1922 0.2182 -0.0196 -0.0188 0.0169  134 GLY A O   
1064 N  N   . ARG A 138 ? 0.1581 0.1797 0.2018 -0.0151 -0.0214 0.0181  135 ARG A N   
1065 C  CA  . ARG A 138 ? 0.1896 0.1692 0.2298 -0.0095 -0.0250 0.0162  135 ARG A CA  
1066 C  C   . ARG A 138 ? 0.1812 0.1744 0.2486 -0.0080 -0.0310 0.0026  135 ARG A C   
1067 O  O   . ARG A 138 ? 0.2468 0.2290 0.2375 -0.0004 -0.0227 0.0087  135 ARG A O   
1068 C  CB  . ARG A 138 ? 0.1897 0.1853 0.2241 -0.0326 -0.0296 0.0189  135 ARG A CB  
1069 C  CG  . ARG A 138 ? 0.1905 0.1940 0.2447 -0.0371 -0.0155 0.0256  135 ARG A CG  
1070 C  CD  . ARG A 138 ? 0.1753 0.1908 0.2606 -0.0209 -0.0109 0.0298  135 ARG A CD  
1071 N  NE  . ARG A 138 ? 0.1665 0.2389 0.2662 -0.0120 0.0088  0.0288  135 ARG A NE  
1072 C  CZ  . ARG A 138 ? 0.1880 0.2343 0.2700 -0.0265 0.0086  0.0531  135 ARG A CZ  
1073 N  NH1 . ARG A 138 ? 0.1552 0.2505 0.2550 -0.0331 -0.0071 0.0598  135 ARG A NH1 
1074 N  NH2 . ARG A 138 ? 0.1976 0.2686 0.2924 -0.0178 0.0209  0.0524  135 ARG A NH2 
1075 N  N   . PRO A 139 ? 0.1916 0.1671 0.2803 -0.0079 -0.0449 0.0198  136 PRO A N   
1076 C  CA  . PRO A 139 ? 0.2118 0.2050 0.2870 0.0112  -0.0426 0.0319  136 PRO A CA  
1077 C  C   . PRO A 139 ? 0.1679 0.2115 0.2560 0.0168  -0.0040 0.0327  136 PRO A C   
1078 O  O   . PRO A 139 ? 0.2083 0.2085 0.2966 -0.0020 0.0349  0.0233  136 PRO A O   
1079 C  CB  . PRO A 139 ? 0.2156 0.2147 0.3162 -0.0227 -0.0357 0.0498  136 PRO A CB  
1080 C  CG  . PRO A 139 ? 0.2561 0.2480 0.3137 -0.0065 -0.0584 0.0402  136 PRO A CG  
1081 C  CD  . PRO A 139 ? 0.2242 0.1973 0.2817 0.0000  -0.0443 0.0265  136 PRO A CD  
1082 N  N   . GLU A 140 ? 0.2177 0.2061 0.2840 0.0126  0.0002  0.0244  137 GLU A N   
1083 C  CA  . GLU A 140 ? 0.2111 0.2016 0.2926 0.0169  -0.0056 0.0308  137 GLU A CA  
1084 C  C   . GLU A 140 ? 0.1761 0.2060 0.2795 0.0165  0.0024  0.0354  137 GLU A C   
1085 O  O   . GLU A 140 ? 0.2052 0.2551 0.2866 0.0191  0.0193  0.0630  137 GLU A O   
1086 C  CB  . GLU A 140 ? 0.2670 0.2426 0.3477 0.0453  0.0062  0.0195  137 GLU A CB  
1087 C  CG  . GLU A 140 ? 0.3290 0.2975 0.4063 0.0062  -0.0054 0.0201  137 GLU A CG  
1088 C  CD  . GLU A 140 ? 0.3658 0.3055 0.3861 -0.0185 0.0033  0.0153  137 GLU A CD  
1089 O  OE1 . GLU A 140 ? 0.4451 0.3851 0.4102 -0.0433 0.0342  0.0630  137 GLU A OE1 
1090 O  OE2 . GLU A 140 ? 0.3559 0.3784 0.4119 -0.0004 0.0060  -0.0257 137 GLU A OE2 
1091 N  N   . GLY A 141 ? 0.2235 0.2260 0.2742 0.0214  0.0023  0.0255  138 GLY A N   
1092 C  CA  . GLY A 141 ? 0.2042 0.2722 0.2635 0.0187  -0.0179 0.0270  138 GLY A CA  
1093 C  C   . GLY A 141 ? 0.2227 0.2691 0.2460 0.0051  0.0070  0.0384  138 GLY A C   
1094 O  O   . GLY A 141 ? 0.2264 0.2628 0.2418 -0.0040 0.0034  0.0552  138 GLY A O   
1095 N  N   . LYS A 142 ? 0.2877 0.2941 0.2580 -0.0283 0.0063  0.0453  139 LYS A N   
1096 C  CA  . LYS A 142 ? 0.3026 0.2795 0.2822 -0.0225 -0.0314 0.0304  139 LYS A CA  
1097 C  C   . LYS A 142 ? 0.2909 0.3242 0.3236 -0.0362 -0.0120 0.0417  139 LYS A C   
1098 O  O   . LYS A 142 ? 0.2914 0.3247 0.2816 -0.0632 -0.0288 0.0521  139 LYS A O   
1099 C  CB  . LYS A 142 ? 0.3490 0.3489 0.3025 -0.0473 -0.0306 0.0243  139 LYS A CB  
1100 C  CG  . LYS A 142 ? 0.3487 0.4124 0.3246 -0.0736 -0.0735 0.0059  139 LYS A CG  
1101 C  CD  . LYS A 142 ? 0.2925 0.4658 0.4066 -0.0752 -0.0427 -0.0023 139 LYS A CD  
1102 C  CE  . LYS A 142 ? 0.3243 0.4963 0.4416 -0.0830 -0.0732 -0.0175 139 LYS A CE  
1103 N  N   . LYS A 143 ? 0.2221 0.3253 0.3194 -0.0014 -0.0257 0.0725  140 LYS A N   
1104 C  CA  . LYS A 143 ? 0.2019 0.3218 0.3411 0.0089  -0.0303 0.0900  140 LYS A CA  
1105 C  C   . LYS A 143 ? 0.1826 0.3124 0.3378 -0.0099 -0.0174 0.0848  140 LYS A C   
1106 O  O   . LYS A 143 ? 0.2005 0.3505 0.3356 -0.0013 -0.0088 0.1082  140 LYS A O   
1107 C  CB  . LYS A 143 ? 0.2012 0.3153 0.3593 0.0353  -0.0109 0.0586  140 LYS A CB  
1108 N  N   . THR A 144 ? 0.1488 0.2547 0.3317 -0.0144 -0.0310 0.0553  141 THR A N   
1109 C  CA  . THR A 144 ? 0.1881 0.2313 0.3183 0.0081  -0.0477 0.0523  141 THR A CA  
1110 C  C   . THR A 144 ? 0.1549 0.2179 0.2892 0.0022  -0.0499 0.0249  141 THR A C   
1111 O  O   . THR A 144 ? 0.1989 0.2078 0.2829 -0.0120 -0.0188 0.0030  141 THR A O   
1112 C  CB  . THR A 144 ? 0.1967 0.2650 0.3551 -0.0093 -0.0453 0.0290  141 THR A CB  
1113 O  OG1 . THR A 144 ? 0.1968 0.3325 0.3431 -0.0187 -0.0254 0.0266  141 THR A OG1 
1114 C  CG2 . THR A 144 ? 0.3097 0.2996 0.4229 -0.0014 -0.0598 0.0332  141 THR A CG2 
1115 N  N   . VAL A 145 ? 0.1520 0.2292 0.2507 -0.0025 -0.0347 0.0453  142 VAL A N   
1116 C  CA  . VAL A 145 ? 0.1893 0.2282 0.2596 0.0108  -0.0235 0.0346  142 VAL A CA  
1117 C  C   . VAL A 145 ? 0.1764 0.2011 0.2507 -0.0005 -0.0485 0.0251  142 VAL A C   
1118 O  O   . VAL A 145 ? 0.1900 0.2030 0.2577 0.0010  -0.0299 0.0287  142 VAL A O   
1119 C  CB  . VAL A 145 ? 0.2271 0.2560 0.2747 -0.0029 -0.0027 0.0272  142 VAL A CB  
1120 C  CG1 . VAL A 145 ? 0.2525 0.2543 0.2870 -0.0030 0.0052  0.0221  142 VAL A CG1 
1121 C  CG2 . VAL A 145 ? 0.2351 0.2883 0.2792 -0.0208 -0.0044 0.0252  142 VAL A CG2 
1122 N  N   . VAL A 146 ? 0.1741 0.2249 0.2337 0.0053  -0.0414 0.0372  143 VAL A N   
1123 C  CA  . VAL A 146 ? 0.1549 0.1977 0.2575 0.0051  -0.0425 0.0302  143 VAL A CA  
1124 C  C   . VAL A 146 ? 0.1484 0.2227 0.2662 -0.0011 -0.0461 0.0241  143 VAL A C   
1125 O  O   . VAL A 146 ? 0.1806 0.2217 0.2623 -0.0101 -0.0522 0.0382  143 VAL A O   
1126 C  CB  . VAL A 146 ? 0.1756 0.2378 0.2496 -0.0109 -0.0443 0.0252  143 VAL A CB  
1127 C  CG1 . VAL A 146 ? 0.2064 0.2640 0.2624 -0.0278 -0.0279 0.0318  143 VAL A CG1 
1128 C  CG2 . VAL A 146 ? 0.2314 0.2701 0.2472 -0.0075 -0.0541 0.0275  143 VAL A CG2 
1129 N  N   . GLN A 147 ? 0.1536 0.2382 0.2771 0.0084  -0.0385 0.0271  144 GLN A N   
1130 C  CA  . GLN A 147 ? 0.1870 0.2573 0.2859 0.0343  -0.0371 0.0209  144 GLN A CA  
1131 C  C   . GLN A 147 ? 0.1789 0.2324 0.2461 0.0338  -0.0156 0.0054  144 GLN A C   
1132 O  O   . GLN A 147 ? 0.1524 0.2655 0.2559 0.0467  -0.0031 0.0058  144 GLN A O   
1133 C  CB  . GLN A 147 ? 0.2290 0.2696 0.2863 0.0367  -0.0468 0.0280  144 GLN A CB  
1134 C  CG  . GLN A 147 ? 0.2496 0.3876 0.3553 0.0289  -0.0430 0.0224  144 GLN A CG  
1135 C  CD  . GLN A 147 ? 0.2881 0.4567 0.3573 -0.0032 -0.0217 0.0462  144 GLN A CD  
1136 O  OE1 . GLN A 147 ? 0.2139 0.5611 0.4381 0.0291  -0.0679 0.0870  144 GLN A OE1 
1137 N  NE2 . GLN A 147 ? 0.2828 0.5209 0.3743 0.0415  -0.0279 0.0694  144 GLN A NE2 
1138 N  N   . HIS A 148 ? 0.1804 0.1712 0.2494 0.0162  -0.0231 0.0098  145 HIS A N   
1139 C  CA  . HIS A 148 ? 0.1727 0.1740 0.2135 0.0057  -0.0209 0.0082  145 HIS A CA  
1140 C  C   . HIS A 148 ? 0.1558 0.1823 0.1944 0.0027  -0.0092 0.0026  145 HIS A C   
1141 O  O   . HIS A 148 ? 0.2046 0.1798 0.2048 0.0212  -0.0223 -0.0078 145 HIS A O   
1142 C  CB  . HIS A 148 ? 0.1751 0.1777 0.2445 -0.0081 -0.0148 0.0091  145 HIS A CB  
1143 C  CG  . HIS A 148 ? 0.1551 0.2042 0.2919 -0.0047 -0.0295 0.0038  145 HIS A CG  
1144 N  ND1 . HIS A 148 ? 0.1951 0.2820 0.3243 0.0351  -0.0716 -0.0261 145 HIS A ND1 
1145 C  CD2 . HIS A 148 ? 0.1597 0.2113 0.3191 -0.0151 -0.0578 -0.0288 145 HIS A CD2 
1146 C  CE1 . HIS A 148 ? 0.1474 0.2838 0.3156 0.0094  -0.0762 -0.0357 145 HIS A CE1 
1147 N  NE2 . HIS A 148 ? 0.1411 0.2297 0.3180 0.0060  -0.0607 -0.0003 145 HIS A NE2 
1148 N  N   . VAL A 149 ? 0.1473 0.1731 0.1825 0.0175  -0.0234 0.0062  146 VAL A N   
1149 C  CA  . VAL A 149 ? 0.1528 0.1746 0.1795 0.0037  -0.0180 0.0138  146 VAL A CA  
1150 C  C   . VAL A 149 ? 0.1419 0.1709 0.1777 0.0138  -0.0033 0.0012  146 VAL A C   
1151 O  O   . VAL A 149 ? 0.1423 0.1751 0.1937 0.0026  0.0023  0.0039  146 VAL A O   
1152 C  CB  . VAL A 149 ? 0.1717 0.1683 0.1823 0.0118  -0.0074 0.0105  146 VAL A CB  
1153 C  CG1 . VAL A 149 ? 0.1798 0.1903 0.1973 0.0096  0.0051  0.0013  146 VAL A CG1 
1154 C  CG2 . VAL A 149 ? 0.1833 0.1883 0.1928 0.0105  -0.0027 0.0154  146 VAL A CG2 
1155 N  N   . LEU A 150 ? 0.1411 0.1783 0.2126 0.0114  -0.0125 0.0142  147 LEU A N   
1156 C  CA  . LEU A 150 ? 0.1258 0.1992 0.2163 0.0010  -0.0193 0.0023  147 LEU A CA  
1157 C  C   . LEU A 150 ? 0.1269 0.2223 0.2426 0.0133  -0.0098 -0.0130 147 LEU A C   
1158 O  O   . LEU A 150 ? 0.1457 0.3402 0.3327 0.0300  0.0219  -0.0761 147 LEU A O   
1159 C  CB  . LEU A 150 ? 0.1259 0.2087 0.2380 0.0080  -0.0172 0.0075  147 LEU A CB  
1160 C  CG  . LEU A 150 ? 0.1441 0.2111 0.2238 0.0001  -0.0307 0.0134  147 LEU A CG  
1161 C  CD1 . LEU A 150 ? 0.1439 0.2413 0.2293 -0.0149 -0.0361 0.0102  147 LEU A CD1 
1162 C  CD2 . LEU A 150 ? 0.1614 0.2053 0.2187 0.0042  -0.0149 -0.0031 147 LEU A CD2 
1163 N  N   . SER A 151 ? 0.1688 0.2312 0.2119 0.0111  -0.0226 -0.0212 148 SER A N   
1164 C  CA  . SER A 151 ? 0.1671 0.2255 0.2350 0.0357  -0.0047 -0.0188 148 SER A CA  
1165 C  C   . SER A 151 ? 0.1599 0.1930 0.1978 0.0159  0.0003  -0.0293 148 SER A C   
1166 O  O   . SER A 151 ? 0.1394 0.2017 0.1901 0.0057  -0.0108 -0.0249 148 SER A O   
1167 C  CB  . SER A 151 ? 0.1983 0.2240 0.2551 0.0491  -0.0051 -0.0439 148 SER A CB  
1168 O  OG  . SER A 151 ? 0.1980 0.2171 0.2747 0.0118  -0.0031 -0.0227 148 SER A OG  
1169 N  N   . PRO A 152 ? 0.1647 0.2117 0.1921 0.0184  0.0112  -0.0268 149 PRO A N   
1170 C  CA  . PRO A 152 ? 0.1711 0.2188 0.2022 0.0036  0.0028  -0.0400 149 PRO A CA  
1171 C  C   . PRO A 152 ? 0.1650 0.2018 0.1981 0.0074  0.0122  -0.0222 149 PRO A C   
1172 O  O   . PRO A 152 ? 0.1561 0.2140 0.2239 0.0057  -0.0127 -0.0282 149 PRO A O   
1173 C  CB  . PRO A 152 ? 0.1739 0.2618 0.2168 -0.0041 0.0104  -0.0286 149 PRO A CB  
1174 C  CG  . PRO A 152 ? 0.2201 0.3038 0.2598 0.0376  0.0319  -0.0388 149 PRO A CG  
1175 C  CD  . PRO A 152 ? 0.1839 0.2483 0.2533 0.0403  0.0224  -0.0309 149 PRO A CD  
1176 N  N   . PHE A 153 ? 0.1722 0.2025 0.1814 0.0073  0.0057  -0.0235 150 PHE A N   
1177 C  CA  . PHE A 153 ? 0.1755 0.2168 0.1986 0.0044  -0.0160 -0.0278 150 PHE A CA  
1178 C  C   . PHE A 153 ? 0.1862 0.2361 0.2145 0.0066  -0.0129 -0.0369 150 PHE A C   
1179 O  O   . PHE A 153 ? 0.2008 0.2464 0.1969 -0.0164 -0.0059 -0.0571 150 PHE A O   
1180 C  CB  . PHE A 153 ? 0.1726 0.2530 0.1871 0.0200  -0.0098 -0.0219 150 PHE A CB  
1181 C  CG  . PHE A 153 ? 0.1710 0.2220 0.1721 0.0165  -0.0076 -0.0164 150 PHE A CG  
1182 C  CD1 . PHE A 153 ? 0.1681 0.2290 0.2128 0.0062  -0.0064 -0.0127 150 PHE A CD1 
1183 C  CD2 . PHE A 153 ? 0.1561 0.2354 0.1772 0.0090  -0.0064 -0.0069 150 PHE A CD2 
1184 C  CE1 . PHE A 153 ? 0.1690 0.2186 0.1796 -0.0054 -0.0217 -0.0101 150 PHE A CE1 
1185 C  CE2 . PHE A 153 ? 0.1543 0.2045 0.1794 0.0125  0.0054  -0.0090 150 PHE A CE2 
1186 C  CZ  . PHE A 153 ? 0.1387 0.2140 0.1951 0.0002  -0.0072 -0.0065 150 PHE A CZ  
1187 N  N   . SER A 154 ? 0.1766 0.2349 0.2127 0.0000  -0.0014 -0.0445 151 SER A N   
1188 C  CA  . SER A 154 ? 0.1922 0.2279 0.2225 0.0344  -0.0040 -0.0543 151 SER A CA  
1189 C  C   . SER A 154 ? 0.1875 0.2342 0.2409 0.0199  -0.0209 -0.0687 151 SER A C   
1190 O  O   . SER A 154 ? 0.1780 0.2441 0.2035 0.0164  -0.0152 -0.0558 151 SER A O   
1191 C  CB  . SER A 154 ? 0.1754 0.2291 0.2380 0.0301  -0.0169 -0.0471 151 SER A CB  
1192 O  OG  . SER A 154 ? 0.1827 0.2154 0.2481 0.0155  -0.0125 -0.0382 151 SER A OG  
1193 N  N   . LYS A 155 ? 0.2320 0.2273 0.2402 0.0312  -0.0220 -0.0765 152 LYS A N   
1194 C  CA  . LYS A 155 ? 0.2136 0.2859 0.2276 0.0348  -0.0040 -0.0660 152 LYS A CA  
1195 C  C   . LYS A 155 ? 0.2125 0.2558 0.2082 0.0243  -0.0049 -0.0503 152 LYS A C   
1196 O  O   . LYS A 155 ? 0.2281 0.2669 0.2284 0.0164  -0.0358 -0.0293 152 LYS A O   
1197 C  CB  . LYS A 155 ? 0.2394 0.3313 0.2490 0.0305  0.0130  -0.0785 152 LYS A CB  
1198 C  CG  . LYS A 155 ? 0.2637 0.4037 0.2914 0.0327  0.0249  -0.0582 152 LYS A CG  
1199 C  CD  . LYS A 155 ? 0.3056 0.4664 0.3474 -0.0083 0.0155  -0.0642 152 LYS A CD  
1200 N  N   . GLU A 156 ? 0.1703 0.2474 0.2020 0.0179  -0.0201 -0.0604 153 GLU A N   
1201 C  CA  . GLU A 156 ? 0.1601 0.2573 0.2487 0.0119  -0.0195 -0.0736 153 GLU A CA  
1202 C  C   . GLU A 156 ? 0.1711 0.2493 0.2372 0.0070  -0.0316 -0.0650 153 GLU A C   
1203 O  O   . GLU A 156 ? 0.1966 0.2348 0.2249 0.0272  -0.0402 -0.0422 153 GLU A O   
1204 C  CB  . GLU A 156 ? 0.2256 0.2792 0.3045 0.0084  -0.0040 -0.0636 153 GLU A CB  
1205 C  CG  . GLU A 156 ? 0.3204 0.3414 0.3773 0.0005  0.0380  -0.0719 153 GLU A CG  
1206 C  CD  . GLU A 156 ? 0.3960 0.4161 0.5023 -0.0499 0.0112  -0.0498 153 GLU A CD  
1207 O  OE1 . GLU A 156 ? 0.5297 0.5573 0.5770 -0.0239 0.0811  -0.0337 153 GLU A OE1 
1208 N  N   . ASN A 157 ? 0.1706 0.2419 0.2219 -0.0024 -0.0333 -0.0614 154 ASN A N   
1209 C  CA  . ASN A 157 ? 0.1780 0.2377 0.2302 0.0119  -0.0189 -0.0366 154 ASN A CA  
1210 C  C   . ASN A 157 ? 0.1918 0.2202 0.2145 0.0180  -0.0192 -0.0495 154 ASN A C   
1211 O  O   . ASN A 157 ? 0.1875 0.2277 0.2244 0.0390  -0.0324 -0.0475 154 ASN A O   
1212 C  CB  . ASN A 157 ? 0.1809 0.2280 0.2365 0.0099  -0.0089 -0.0304 154 ASN A CB  
1213 C  CG  . ASN A 157 ? 0.2045 0.2614 0.2308 -0.0208 -0.0051 -0.0299 154 ASN A CG  
1214 O  OD1 . ASN A 157 ? 0.2422 0.2955 0.2845 -0.0459 -0.0446 -0.0209 154 ASN A OD1 
1215 N  ND2 . ASN A 157 ? 0.2275 0.2780 0.2283 -0.0357 -0.0203 -0.0250 154 ASN A ND2 
1216 N  N   . GLN A 158 ? 0.1901 0.2144 0.2484 0.0350  -0.0152 -0.0473 155 GLN A N   
1217 C  CA  . GLN A 158 ? 0.2054 0.2096 0.2711 0.0236  0.0207  -0.0433 155 GLN A CA  
1218 C  C   . GLN A 158 ? 0.2383 0.2295 0.2519 0.0071  -0.0248 -0.0415 155 GLN A C   
1219 O  O   . GLN A 158 ? 0.2053 0.2161 0.2308 0.0069  -0.0231 -0.0450 155 GLN A O   
1220 C  CB  . GLN A 158 ? 0.2519 0.2375 0.2986 0.0020  0.0487  -0.0618 155 GLN A CB  
1221 C  CG  . GLN A 158 ? 0.2977 0.2743 0.3543 -0.0087 0.0467  -0.0150 155 GLN A CG  
1222 C  CD  . GLN A 158 ? 0.3451 0.3218 0.3903 -0.0175 0.0292  -0.0141 155 GLN A CD  
1223 O  OE1 . GLN A 158 ? 0.4636 0.3462 0.5513 -0.0493 0.0471  -0.0330 155 GLN A OE1 
1224 N  NE2 . GLN A 158 ? 0.2520 0.3360 0.3475 -0.0021 0.0154  -0.0505 155 GLN A NE2 
1225 N  N   . PRO A 159 ? 0.2214 0.2439 0.2383 -0.0071 -0.0204 -0.0584 156 PRO A N   
1226 C  CA  . PRO A 159 ? 0.2340 0.2686 0.2333 -0.0152 -0.0583 -0.0422 156 PRO A CA  
1227 C  C   . PRO A 159 ? 0.2021 0.2202 0.2453 -0.0257 -0.0626 -0.0462 156 PRO A C   
1228 O  O   . PRO A 159 ? 0.2302 0.2346 0.2874 -0.0062 -0.0755 -0.0463 156 PRO A O   
1229 C  CB  . PRO A 159 ? 0.2641 0.2941 0.2438 -0.0078 -0.0803 -0.0425 156 PRO A CB  
1230 C  CG  . PRO A 159 ? 0.2593 0.2884 0.2576 -0.0241 -0.0214 -0.0442 156 PRO A CG  
1231 C  CD  . PRO A 159 ? 0.2585 0.2588 0.2608 -0.0166 -0.0297 -0.0626 156 PRO A CD  
1232 N  N   . LEU A 160 ? 0.1972 0.1967 0.2599 -0.0226 -0.0337 -0.0476 157 LEU A N   
1233 C  CA  . LEU A 160 ? 0.2081 0.2402 0.2583 -0.0048 -0.0238 -0.0375 157 LEU A CA  
1234 C  C   . LEU A 160 ? 0.1439 0.2193 0.2583 -0.0036 -0.0185 -0.0410 157 LEU A C   
1235 O  O   . LEU A 160 ? 0.1774 0.2315 0.2572 0.0094  0.0000  -0.0318 157 LEU A O   
1236 C  CB  . LEU A 160 ? 0.2263 0.2860 0.2929 -0.0260 0.0082  -0.0476 157 LEU A CB  
1237 C  CG  . LEU A 160 ? 0.2921 0.3418 0.2544 -0.0298 0.0237  -0.0473 157 LEU A CG  
1238 C  CD1 . LEU A 160 ? 0.3052 0.3865 0.2736 -0.0514 -0.0247 -0.0673 157 LEU A CD1 
1239 C  CD2 . LEU A 160 ? 0.3281 0.3711 0.2959 -0.0682 0.0332  -0.0506 157 LEU A CD2 
1240 N  N   . ILE A 161 ? 0.1537 0.2001 0.2118 0.0005  -0.0151 -0.0283 158 ILE A N   
1241 C  CA  . ILE A 161 ? 0.1616 0.2104 0.1912 0.0072  -0.0119 -0.0228 158 ILE A CA  
1242 C  C   . ILE A 161 ? 0.1537 0.2059 0.1766 0.0015  -0.0239 -0.0216 158 ILE A C   
1243 O  O   . ILE A 161 ? 0.1613 0.2079 0.2022 0.0135  -0.0229 -0.0269 158 ILE A O   
1244 C  CB  . ILE A 161 ? 0.1650 0.2271 0.2199 0.0178  -0.0253 -0.0433 158 ILE A CB  
1245 C  CG1 . ILE A 161 ? 0.2073 0.2556 0.2017 0.0265  -0.0368 -0.0285 158 ILE A CG1 
1246 C  CG2 . ILE A 161 ? 0.1893 0.2355 0.2273 0.0100  -0.0379 -0.0498 158 ILE A CG2 
1247 C  CD1 . ILE A 161 ? 0.2054 0.2964 0.2173 0.0085  -0.0380 -0.0270 158 ILE A CD1 
1248 N  N   . GLU A 162 ? 0.1682 0.1968 0.1767 -0.0012 -0.0269 -0.0221 159 GLU A N   
1249 C  CA  . GLU A 162 ? 0.2071 0.2145 0.1884 0.0101  -0.0176 -0.0187 159 GLU A CA  
1250 C  C   . GLU A 162 ? 0.2019 0.2071 0.1775 0.0010  -0.0175 -0.0152 159 GLU A C   
1251 O  O   . GLU A 162 ? 0.2197 0.2104 0.2125 0.0011  -0.0177 -0.0285 159 GLU A O   
1252 C  CB  . GLU A 162 ? 0.2616 0.2586 0.2108 0.0150  -0.0040 -0.0082 159 GLU A CB  
1253 C  CG  . GLU A 162 ? 0.2915 0.3300 0.3061 0.0259  -0.0033 -0.0127 159 GLU A CG  
1254 C  CD  . GLU A 162 ? 0.3776 0.4487 0.3667 0.0482  0.0131  -0.0255 159 GLU A CD  
1255 O  OE1 . GLU A 162 ? 0.4729 0.5640 0.4156 0.0849  -0.0164 -0.0443 159 GLU A OE1 
1256 O  OE2 . GLU A 162 ? 0.3837 0.4740 0.4647 0.0596  0.0419  0.0473  159 GLU A OE2 
1257 N  N   . GLU A 163 ? 0.2177 0.1883 0.1770 0.0089  -0.0296 -0.0187 160 GLU A N   
1258 C  CA  . GLU A 163 ? 0.2076 0.2175 0.2224 0.0054  -0.0219 -0.0222 160 GLU A CA  
1259 C  C   . GLU A 163 ? 0.1833 0.1975 0.2035 0.0086  -0.0348 -0.0125 160 GLU A C   
1260 O  O   . GLU A 163 ? 0.1689 0.2085 0.2235 0.0326  -0.0343 -0.0200 160 GLU A O   
1261 C  CB  . GLU A 163 ? 0.1953 0.2450 0.2661 0.0077  -0.0197 -0.0359 160 GLU A CB  
1262 C  CG  . GLU A 163 ? 0.2255 0.3363 0.3374 0.0007  0.0055  -0.0281 160 GLU A CG  
1263 N  N   . SER A 164 ? 0.1740 0.1766 0.2082 0.0073  -0.0367 -0.0024 161 SER A N   
1264 C  CA  . SER A 164 ? 0.1702 0.1802 0.1902 0.0174  -0.0240 -0.0034 161 SER A CA  
1265 C  C   . SER A 164 ? 0.1430 0.1902 0.1705 0.0114  -0.0240 -0.0114 161 SER A C   
1266 O  O   . SER A 164 ? 0.1716 0.1820 0.1772 0.0102  -0.0126 -0.0107 161 SER A O   
1267 C  CB  . SER A 164 ? 0.2007 0.2092 0.1870 0.0112  -0.0091 0.0091  161 SER A CB  
1268 O  OG  . SER A 164 ? 0.2654 0.2293 0.2065 0.0333  0.0028  0.0019  161 SER A OG  
1269 N  N   . MET A 165 ? 0.1705 0.1853 0.1793 0.0221  -0.0094 -0.0135 162 MET A N   
1270 C  CA  . MET A 165 ? 0.1599 0.1964 0.1862 0.0208  -0.0249 -0.0164 162 MET A CA  
1271 C  C   . MET A 165 ? 0.1885 0.2033 0.1834 0.0170  -0.0263 -0.0119 162 MET A C   
1272 O  O   . MET A 165 ? 0.1760 0.1881 0.1998 0.0119  -0.0181 0.0054  162 MET A O   
1273 C  CB  . MET A 165 ? 0.1615 0.2103 0.2298 0.0162  -0.0262 -0.0200 162 MET A CB  
1274 C  CG  . MET A 165 ? 0.1639 0.2371 0.2363 0.0361  -0.0309 -0.0269 162 MET A CG  
1275 S  SD  . MET A 165 ? 0.1854 0.4695 0.3525 0.0659  0.0008  0.0646  162 MET A SD  
1276 C  CE  . MET A 165 ? 0.2320 0.4366 0.4211 0.0366  0.0019  0.0557  162 MET A CE  
1277 N  N   . CYS A 166 ? 0.2053 0.2054 0.1677 0.0181  -0.0185 -0.0081 163 CYS A N   
1278 C  CA  . CYS A 166 ? 0.2272 0.2056 0.1725 0.0222  -0.0242 -0.0042 163 CYS A CA  
1279 C  C   . CYS A 166 ? 0.1982 0.1895 0.1754 0.0070  -0.0343 -0.0083 163 CYS A C   
1280 O  O   . CYS A 166 ? 0.2143 0.1935 0.1800 0.0268  -0.0199 -0.0011 163 CYS A O   
1281 C  CB  . CYS A 166 ? 0.2770 0.1959 0.1608 0.0633  -0.0544 0.0312  163 CYS A CB  
1282 S  SG  . CYS A 166 ? 0.4886 0.4256 0.3103 0.0246  0.0076  0.0169  163 CYS A SG  
1283 N  N   . GLN A 167 ? 0.1692 0.1742 0.1937 0.0145  -0.0121 -0.0097 164 GLN A N   
1284 C  CA  . GLN A 167 ? 0.1621 0.1917 0.2052 0.0285  -0.0262 -0.0126 164 GLN A CA  
1285 C  C   . GLN A 167 ? 0.1665 0.1727 0.1888 0.0201  -0.0151 0.0023  164 GLN A C   
1286 O  O   . GLN A 167 ? 0.1841 0.1819 0.2041 0.0265  -0.0089 -0.0092 164 GLN A O   
1287 C  CB  . GLN A 167 ? 0.1763 0.2311 0.2595 0.0238  0.0000  -0.0115 164 GLN A CB  
1288 C  CG  . GLN A 167 ? 0.2168 0.2612 0.3287 -0.0076 -0.0191 -0.0487 164 GLN A CG  
1289 C  CD  . GLN A 167 ? 0.2984 0.3311 0.3457 0.0119  -0.0183 -0.0373 164 GLN A CD  
1290 O  OE1 . GLN A 167 ? 0.3021 0.3955 0.4294 0.0182  -0.0574 -0.1076 164 GLN A OE1 
1291 N  NE2 . GLN A 167 ? 0.3428 0.3589 0.3878 0.0038  -0.0092 -0.0591 164 GLN A NE2 
1292 N  N   . SER A 168 ? 0.1682 0.1865 0.1717 0.0290  -0.0138 -0.0030 165 SER A N   
1293 C  CA  . SER A 168 ? 0.1813 0.1782 0.1628 0.0251  -0.0155 0.0020  165 SER A CA  
1294 C  C   . SER A 168 ? 0.1880 0.1812 0.1670 0.0203  -0.0103 0.0104  165 SER A C   
1295 O  O   . SER A 168 ? 0.1953 0.1824 0.1784 0.0219  -0.0156 0.0021  165 SER A O   
1296 C  CB  . SER A 168 ? 0.1757 0.1716 0.1726 0.0215  -0.0084 0.0018  165 SER A CB  
1297 O  OG  . SER A 168 ? 0.1906 0.1855 0.1743 0.0149  0.0028  0.0132  165 SER A OG  
1298 N  N   . VAL A 169 ? 0.1962 0.1715 0.1682 0.0191  0.0043  0.0202  166 VAL A N   
1299 C  CA  . VAL A 169 ? 0.2112 0.1805 0.1810 0.0126  0.0046  0.0226  166 VAL A CA  
1300 C  C   . VAL A 169 ? 0.2374 0.1927 0.1869 0.0266  -0.0014 0.0336  166 VAL A C   
1301 O  O   . VAL A 169 ? 0.2283 0.1887 0.1843 0.0188  -0.0188 0.0229  166 VAL A O   
1302 C  CB  . VAL A 169 ? 0.2187 0.1919 0.2098 0.0044  0.0259  0.0138  166 VAL A CB  
1303 C  CG1 . VAL A 169 ? 0.2588 0.2257 0.2248 -0.0052 0.0466  0.0281  166 VAL A CG1 
1304 C  CG2 . VAL A 169 ? 0.2216 0.2112 0.2250 -0.0073 0.0305  0.0014  166 VAL A CG2 
1305 N  N   . LYS A 170 ? 0.2204 0.1813 0.1835 0.0393  0.0033  0.0089  167 LYS A N   
1306 C  CA  . LYS A 170 ? 0.2176 0.2213 0.2012 0.0420  -0.0050 0.0234  167 LYS A CA  
1307 C  C   . LYS A 170 ? 0.2137 0.1883 0.1862 0.0310  -0.0003 0.0080  167 LYS A C   
1308 O  O   . LYS A 170 ? 0.2116 0.2154 0.2121 0.0541  -0.0363 0.0103  167 LYS A O   
1309 C  CB  . LYS A 170 ? 0.2323 0.2297 0.2063 0.0562  -0.0368 0.0296  167 LYS A CB  
1310 C  CG  . LYS A 170 ? 0.3177 0.2768 0.2458 0.0492  -0.0527 0.0095  167 LYS A CG  
1311 C  CD  . LYS A 170 ? 0.3733 0.3316 0.3048 0.0307  -0.0682 -0.0043 167 LYS A CD  
1312 C  CE  . LYS A 170 ? 0.4268 0.3973 0.3340 0.0198  -0.0654 -0.0292 167 LYS A CE  
1313 N  NZ  . LYS A 170 ? 0.4970 0.4314 0.4764 0.0279  -0.0657 -0.0419 167 LYS A NZ  
1314 N  N   . ALA A 171 ? 0.2197 0.1935 0.1741 0.0395  -0.0086 0.0032  168 ALA A N   
1315 C  CA  . ALA A 171 ? 0.1716 0.2053 0.1633 0.0377  -0.0154 0.0088  168 ALA A CA  
1316 C  C   . ALA A 171 ? 0.1960 0.1850 0.1864 0.0372  -0.0190 0.0062  168 ALA A C   
1317 O  O   . ALA A 171 ? 0.2135 0.2079 0.1978 0.0482  -0.0241 -0.0008 168 ALA A O   
1318 C  CB  . ALA A 171 ? 0.1868 0.2027 0.1755 0.0469  -0.0029 -0.0054 168 ALA A CB  
1319 N  N   . VAL A 172 ? 0.2108 0.1734 0.1919 0.0232  -0.0044 0.0105  169 VAL A N   
1320 C  CA  . VAL A 172 ? 0.2078 0.1984 0.1931 0.0140  -0.0203 0.0012  169 VAL A CA  
1321 C  C   . VAL A 172 ? 0.2174 0.2092 0.2294 0.0062  -0.0205 0.0012  169 VAL A C   
1322 O  O   . VAL A 172 ? 0.2183 0.2097 0.2267 0.0105  -0.0152 -0.0105 169 VAL A O   
1323 C  CB  . VAL A 172 ? 0.2010 0.1949 0.1869 0.0030  -0.0242 0.0077  169 VAL A CB  
1324 C  CG1 . VAL A 172 ? 0.2219 0.2002 0.2343 0.0068  -0.0185 0.0026  169 VAL A CG1 
1325 C  CG2 . VAL A 172 ? 0.2473 0.1964 0.1959 0.0139  -0.0146 0.0066  169 VAL A CG2 
1326 N  N   . GLU A 173 ? 0.2430 0.1869 0.2005 0.0310  0.0052  0.0062  170 GLU A N   
1327 C  CA  . GLU A 173 ? 0.2660 0.1991 0.2337 0.0416  -0.0242 0.0249  170 GLU A CA  
1328 C  C   . GLU A 173 ? 0.2762 0.1913 0.2387 0.0442  -0.0244 0.0274  170 GLU A C   
1329 O  O   . GLU A 173 ? 0.2943 0.1970 0.2598 0.0530  -0.0271 0.0159  170 GLU A O   
1330 C  CB  . GLU A 173 ? 0.2973 0.2379 0.2433 0.0640  -0.0592 0.0398  170 GLU A CB  
1331 C  CG  . GLU A 173 ? 0.3946 0.2839 0.2985 0.0254  -0.0530 0.0408  170 GLU A CG  
1332 C  CD  . GLU A 173 ? 0.4072 0.3350 0.3232 0.0108  -0.0823 0.0523  170 GLU A CD  
1333 O  OE1 . GLU A 173 ? 0.4376 0.3183 0.3273 0.0119  -0.0503 0.0458  170 GLU A OE1 
1334 O  OE2 . GLU A 173 ? 0.5070 0.4042 0.4673 -0.0266 -0.0643 0.0382  170 GLU A OE2 
1335 N  N   . TYR A 174 ? 0.2810 0.1880 0.2272 0.0546  -0.0141 0.0100  171 TYR A N   
1336 C  CA  . TYR A 174 ? 0.2749 0.2190 0.2321 0.0490  -0.0166 0.0119  171 TYR A CA  
1337 C  C   . TYR A 174 ? 0.2852 0.2192 0.2284 0.0735  -0.0373 -0.0075 171 TYR A C   
1338 O  O   . TYR A 174 ? 0.3139 0.2152 0.2831 0.0882  -0.0322 0.0000  171 TYR A O   
1339 C  CB  . TYR A 174 ? 0.2521 0.2414 0.2507 0.0536  -0.0163 -0.0110 171 TYR A CB  
1340 C  CG  . TYR A 174 ? 0.2407 0.2361 0.2364 0.0554  -0.0208 0.0037  171 TYR A CG  
1341 C  CD1 . TYR A 174 ? 0.2589 0.2357 0.2789 0.0554  -0.0387 0.0049  171 TYR A CD1 
1342 C  CD2 . TYR A 174 ? 0.2593 0.2522 0.2705 0.0541  0.0037  0.0252  171 TYR A CD2 
1343 C  CE1 . TYR A 174 ? 0.2603 0.2789 0.3117 0.0466  -0.0269 -0.0035 171 TYR A CE1 
1344 C  CE2 . TYR A 174 ? 0.2558 0.2668 0.3148 0.0526  0.0000  0.0239  171 TYR A CE2 
1345 C  CZ  . TYR A 174 ? 0.2190 0.3053 0.3618 0.0676  -0.0013 0.0096  171 TYR A CZ  
1346 O  OH  . TYR A 174 ? 0.2075 0.3210 0.5299 0.0793  0.0177  0.0395  171 TYR A OH  
1347 N  N   . LEU A 175 ? 0.2715 0.2142 0.2285 0.0636  -0.0261 -0.0081 172 LEU A N   
1348 C  CA  . LEU A 175 ? 0.2522 0.2178 0.2479 0.0327  -0.0203 -0.0082 172 LEU A CA  
1349 C  C   . LEU A 175 ? 0.3043 0.2274 0.3057 0.0413  -0.0055 -0.0044 172 LEU A C   
1350 O  O   . LEU A 175 ? 0.3756 0.2242 0.3106 0.0169  0.0283  -0.0249 172 LEU A O   
1351 C  CB  . LEU A 175 ? 0.2450 0.2410 0.2451 0.0342  -0.0219 -0.0194 172 LEU A CB  
1352 C  CG  . LEU A 175 ? 0.2056 0.2396 0.2541 0.0303  -0.0459 -0.0110 172 LEU A CG  
1353 C  CD1 . LEU A 175 ? 0.1812 0.2487 0.2736 0.0351  -0.0439 -0.0196 172 LEU A CD1 
1354 C  CD2 . LEU A 175 ? 0.2092 0.2384 0.2692 0.0376  -0.0454 0.0039  172 LEU A CD2 
1355 N  N   . ILE A 176 ? 0.3413 0.1910 0.2953 0.0441  0.0110  -0.0027 173 ILE A N   
1356 C  CA  . ILE A 176 ? 0.3961 0.2024 0.3739 0.0286  -0.0157 -0.0002 173 ILE A CA  
1357 C  C   . ILE A 176 ? 0.3835 0.2325 0.4129 0.0563  -0.0070 0.0104  173 ILE A C   
1358 O  O   . ILE A 176 ? 0.4711 0.2596 0.4544 0.0647  0.0155  -0.0249 173 ILE A O   
1359 C  CB  . ILE A 176 ? 0.3776 0.2265 0.4312 0.0226  0.0032  0.0039  173 ILE A CB  
1360 C  CG1 . ILE A 176 ? 0.3629 0.2817 0.4410 -0.0161 -0.0090 0.0114  173 ILE A CG1 
1361 C  CG2 . ILE A 176 ? 0.4221 0.3095 0.4552 -0.0151 0.0115  0.0050  173 ILE A CG2 
1362 C  CD1 . ILE A 176 ? 0.3620 0.2692 0.4141 -0.0516 -0.0051 0.0124  173 ILE A CD1 
1363 N  N   . GLU A 177 ? 0.3923 0.1916 0.3773 0.0738  0.0003  0.0134  174 GLU A N   
1364 C  CA  . GLU A 177 ? 0.4038 0.2312 0.3911 0.1022  0.0014  0.0145  174 GLU A CA  
1365 C  C   . GLU A 177 ? 0.4185 0.2758 0.4142 0.1022  -0.0149 -0.0173 174 GLU A C   
1366 O  O   . GLU A 177 ? 0.4366 0.3547 0.4842 0.1151  -0.0485 0.0316  174 GLU A O   
1367 C  CB  . GLU A 177 ? 0.3910 0.2493 0.4112 0.1281  -0.0400 0.0335  174 GLU A CB  
1368 C  CG  . GLU A 177 ? 0.3897 0.2798 0.4276 0.1444  -0.0313 0.0638  174 GLU A CG  
1369 C  CD  . GLU A 177 ? 0.4243 0.3272 0.4491 0.1053  -0.0251 0.0634  174 GLU A CD  
1370 O  OE1 . GLU A 177 ? 0.4849 0.3719 0.4749 0.0216  0.0172  0.1078  174 GLU A OE1 
1371 O  OE2 . GLU A 177 ? 0.4635 0.3909 0.3872 0.0905  0.0275  0.0011  174 GLU A OE2 
1372 N  N   . GLY A 178 ? 0.4383 0.2407 0.3800 0.0847  0.0006  -0.0107 175 GLY A N   
1373 C  CA  . GLY A 178 ? 0.4246 0.2471 0.3950 0.0673  0.0087  -0.0299 175 GLY A CA  
1374 C  C   . GLY A 178 ? 0.3668 0.2291 0.3221 0.0616  0.0133  -0.0344 175 GLY A C   
1375 O  O   . GLY A 178 ? 0.3655 0.2670 0.3630 0.0731  0.0488  -0.0285 175 GLY A O   
1376 N  N   . HIS A 179 ? 0.3352 0.2229 0.3210 0.0764  -0.0135 -0.0129 176 HIS A N   
1377 C  CA  . HIS A 179 ? 0.3203 0.2342 0.2729 0.0704  -0.0187 -0.0059 176 HIS A CA  
1378 C  C   . HIS A 179 ? 0.3037 0.2072 0.2783 0.0619  -0.0267 -0.0082 176 HIS A C   
1379 O  O   . HIS A 179 ? 0.2981 0.2445 0.3188 0.0824  -0.0462 0.0087  176 HIS A O   
1380 C  CB  . HIS A 179 ? 0.2901 0.2464 0.2926 0.0714  -0.0168 -0.0120 176 HIS A CB  
1381 C  CG  . HIS A 179 ? 0.2907 0.2951 0.3050 0.0833  -0.0246 -0.0197 176 HIS A CG  
1382 N  ND1 . HIS A 179 ? 0.3337 0.3017 0.3061 0.0922  -0.0232 0.0143  176 HIS A ND1 
1383 C  CD2 . HIS A 179 ? 0.3065 0.3142 0.3245 0.0899  -0.0447 -0.0115 176 HIS A CD2 
1384 C  CE1 . HIS A 179 ? 0.3352 0.3482 0.3071 0.0857  -0.0129 -0.0160 176 HIS A CE1 
1385 N  NE2 . HIS A 179 ? 0.3234 0.3180 0.3566 0.0914  -0.0236 0.0084  176 HIS A NE2 
1386 N  N   . SER A 180 ? 0.3106 0.1929 0.2827 0.0625  -0.0348 0.0097  177 SER A N   
1387 C  CA  . SER A 180 ? 0.3027 0.1968 0.2701 0.0577  -0.0415 0.0041  177 SER A CA  
1388 C  C   . SER A 180 ? 0.2865 0.2130 0.2544 0.0602  -0.0459 -0.0052 177 SER A C   
1389 O  O   . SER A 180 ? 0.2426 0.2212 0.2540 0.0459  -0.0351 -0.0090 177 SER A O   
1390 C  CB  . SER A 180 ? 0.3094 0.2158 0.3157 0.0810  -0.0324 -0.0143 177 SER A CB  
1391 O  OG  . SER A 180 ? 0.2808 0.2465 0.3290 0.0604  -0.0099 -0.0438 177 SER A OG  
1392 N  N   . PHE A 181 ? 0.2721 0.1963 0.2244 0.0513  -0.0499 -0.0132 178 PHE A N   
1393 C  CA  . PHE A 181 ? 0.2198 0.1984 0.2013 0.0430  -0.0276 -0.0086 178 PHE A CA  
1394 C  C   . PHE A 181 ? 0.2229 0.2070 0.2120 0.0290  -0.0242 -0.0251 178 PHE A C   
1395 O  O   . PHE A 181 ? 0.1983 0.2220 0.2155 0.0231  -0.0168 -0.0378 178 PHE A O   
1396 C  CB  . PHE A 181 ? 0.2202 0.2012 0.2381 0.0231  -0.0342 0.0043  178 PHE A CB  
1397 C  CG  . PHE A 181 ? 0.2097 0.1950 0.2053 0.0163  -0.0390 0.0009  178 PHE A CG  
1398 C  CD1 . PHE A 181 ? 0.1935 0.2116 0.2127 -0.0050 -0.0294 -0.0063 178 PHE A CD1 
1399 C  CD2 . PHE A 181 ? 0.2093 0.2098 0.2310 0.0084  -0.0441 -0.0079 178 PHE A CD2 
1400 C  CE1 . PHE A 181 ? 0.1980 0.1914 0.2088 0.0014  -0.0297 -0.0095 178 PHE A CE1 
1401 C  CE2 . PHE A 181 ? 0.1685 0.2091 0.2158 0.0085  -0.0356 -0.0129 178 PHE A CE2 
1402 C  CZ  . PHE A 181 ? 0.1913 0.1877 0.2036 0.0047  -0.0349 -0.0173 178 PHE A CZ  
1403 N  N   . VAL A 182 ? 0.2155 0.2073 0.2191 0.0322  -0.0227 -0.0304 179 VAL A N   
1404 C  CA  . VAL A 182 ? 0.2425 0.2567 0.2470 0.0260  -0.0182 -0.0267 179 VAL A CA  
1405 C  C   . VAL A 182 ? 0.1877 0.2353 0.2587 0.0240  -0.0282 -0.0302 179 VAL A C   
1406 O  O   . VAL A 182 ? 0.1980 0.2524 0.2633 0.0334  -0.0115 -0.0470 179 VAL A O   
1407 C  CB  . VAL A 182 ? 0.2645 0.3022 0.2970 0.0010  -0.0046 -0.0375 179 VAL A CB  
1408 C  CG1 . VAL A 182 ? 0.2943 0.3250 0.3083 -0.0289 0.0111  -0.0338 179 VAL A CG1 
1409 C  CG2 . VAL A 182 ? 0.3404 0.3242 0.2917 0.0054  0.0090  -0.0297 179 VAL A CG2 
1410 N  N   . ASP A 183 ? 0.1981 0.2391 0.2595 0.0166  -0.0224 -0.0387 180 ASP A N   
1411 C  CA  . ASP A 183 ? 0.1772 0.2533 0.2823 0.0369  -0.0335 -0.0470 180 ASP A CA  
1412 C  C   . ASP A 183 ? 0.1799 0.2275 0.2695 0.0313  -0.0552 -0.0583 180 ASP A C   
1413 O  O   . ASP A 183 ? 0.2199 0.2644 0.2788 0.0317  -0.0572 -0.0594 180 ASP A O   
1414 C  CB  . ASP A 183 ? 0.2248 0.2694 0.3207 0.0563  -0.0472 -0.0538 180 ASP A CB  
1415 C  CG  . ASP A 183 ? 0.2396 0.2987 0.4094 0.0689  -0.0466 -0.0323 180 ASP A CG  
1416 O  OD1 . ASP A 183 ? 0.2781 0.3845 0.4564 0.1131  -0.0004 -0.0223 180 ASP A OD1 
1417 O  OD2 . ASP A 183 ? 0.4080 0.3150 0.5321 0.0821  -0.1422 -0.0483 180 ASP A OD2 
1418 N  N   . ALA A 184 ? 0.1704 0.2296 0.2124 0.0121  -0.0462 -0.0403 181 ALA A N   
1419 C  CA  . ALA A 184 ? 0.2141 0.2110 0.1865 0.0252  -0.0226 -0.0225 181 ALA A CA  
1420 C  C   . ALA A 184 ? 0.1944 0.2132 0.2035 0.0309  -0.0386 -0.0209 181 ALA A C   
1421 O  O   . ALA A 184 ? 0.1868 0.2226 0.2184 0.0104  -0.0242 -0.0344 181 ALA A O   
1422 C  CB  . ALA A 184 ? 0.2298 0.1894 0.1927 0.0242  -0.0272 -0.0347 181 ALA A CB  
1423 N  N   . MET A 185 ? 0.1713 0.2067 0.2033 0.0267  0.0017  -0.0345 182 MET A N   
1424 C  CA  . MET A 185 ? 0.1795 0.2262 0.2212 0.0202  -0.0050 -0.0279 182 MET A CA  
1425 C  C   . MET A 185 ? 0.1663 0.2205 0.2337 0.0272  -0.0032 -0.0301 182 MET A C   
1426 O  O   . MET A 185 ? 0.1929 0.2454 0.2705 0.0163  -0.0161 -0.0537 182 MET A O   
1427 C  CB  . MET A 185 ? 0.1622 0.2324 0.2182 0.0170  0.0073  -0.0214 182 MET A CB  
1428 C  CG  . MET A 185 ? 0.1573 0.2174 0.2027 0.0216  0.0069  -0.0199 182 MET A CG  
1429 S  SD  . MET A 185 ? 0.2064 0.2735 0.2320 0.0039  -0.0104 -0.0177 182 MET A SD  
1430 C  CE  . MET A 185 ? 0.2513 0.2136 0.2704 0.0260  -0.0539 -0.0257 182 MET A CE  
1431 N  N   . ASN A 186 ? 0.1606 0.2518 0.2296 0.0195  -0.0207 -0.0505 183 ASN A N   
1432 C  CA  . ASN A 186 ? 0.1725 0.2940 0.2683 0.0122  -0.0335 -0.0505 183 ASN A CA  
1433 C  C   . ASN A 186 ? 0.2045 0.2683 0.2780 -0.0123 -0.0442 -0.0518 183 ASN A C   
1434 O  O   . ASN A 186 ? 0.1862 0.2991 0.2922 -0.0364 -0.0475 -0.0764 183 ASN A O   
1435 C  CB  . ASN A 186 ? 0.1793 0.3144 0.3006 0.0310  -0.0231 -0.0683 183 ASN A CB  
1436 C  CG  . ASN A 186 ? 0.2138 0.3625 0.3492 0.0113  -0.0420 -0.0599 183 ASN A CG  
1437 O  OD1 . ASN A 186 ? 0.2666 0.4127 0.4661 -0.0091 0.0104  -0.0722 183 ASN A OD1 
1438 N  ND2 . ASN A 186 ? 0.2435 0.4282 0.3270 -0.0143 -0.0688 -0.0690 183 ASN A ND2 
1439 N  N   . ARG A 187 ? 0.1856 0.2714 0.2339 -0.0172 -0.0534 -0.0395 184 ARG A N   
1440 C  CA  . ARG A 187 ? 0.1964 0.2822 0.2284 0.0038  -0.0495 -0.0286 184 ARG A CA  
1441 C  C   . ARG A 187 ? 0.2163 0.2451 0.2320 0.0003  -0.0685 -0.0496 184 ARG A C   
1442 O  O   . ARG A 187 ? 0.2772 0.2773 0.2298 0.0260  -0.0922 -0.0519 184 ARG A O   
1443 C  CB  . ARG A 187 ? 0.2181 0.2796 0.2258 0.0189  -0.0665 -0.0174 184 ARG A CB  
1444 C  CG  . ARG A 187 ? 0.2600 0.3022 0.2406 0.0280  -0.0811 -0.0117 184 ARG A CG  
1445 C  CD  . ARG A 187 ? 0.3000 0.3584 0.3044 0.0207  -0.0544 0.0068  184 ARG A CD  
1446 N  NE  . ARG A 187 ? 0.4039 0.4524 0.3418 0.0018  -0.0479 0.0294  184 ARG A NE  
1447 N  N   . PHE A 188 ? 0.2078 0.2321 0.1953 0.0137  -0.0445 -0.0499 185 PHE A N   
1448 C  CA  . PHE A 188 ? 0.2140 0.2360 0.1871 0.0014  -0.0257 -0.0377 185 PHE A CA  
1449 C  C   . PHE A 188 ? 0.1898 0.2316 0.2279 -0.0016 -0.0231 -0.0265 185 PHE A C   
1450 O  O   . PHE A 188 ? 0.2478 0.2357 0.2272 0.0131  -0.0095 -0.0366 185 PHE A O   
1451 C  CB  . PHE A 188 ? 0.1955 0.2265 0.2107 0.0054  -0.0126 -0.0365 185 PHE A CB  
1452 C  CG  . PHE A 188 ? 0.2182 0.2523 0.2050 0.0065  -0.0231 -0.0221 185 PHE A CG  
1453 C  CD1 . PHE A 188 ? 0.2299 0.2558 0.2157 -0.0162 -0.0032 -0.0118 185 PHE A CD1 
1454 C  CD2 . PHE A 188 ? 0.2314 0.2666 0.2133 -0.0043 -0.0127 -0.0227 185 PHE A CD2 
1455 C  CE1 . PHE A 188 ? 0.2329 0.2677 0.2215 -0.0339 -0.0003 -0.0215 185 PHE A CE1 
1456 C  CE2 . PHE A 188 ? 0.2461 0.2775 0.2305 -0.0117 -0.0224 -0.0170 185 PHE A CE2 
1457 C  CZ  . PHE A 188 ? 0.2657 0.2722 0.2270 -0.0040 -0.0187 -0.0007 185 PHE A CZ  
1458 N  N   . ASN A 189 ? 0.1865 0.2257 0.2233 -0.0097 -0.0252 -0.0204 186 ASN A N   
1459 C  CA  . ASN A 189 ? 0.2170 0.2595 0.2386 -0.0217 -0.0346 -0.0155 186 ASN A CA  
1460 C  C   . ASN A 189 ? 0.2753 0.2736 0.3152 -0.0353 -0.0647 -0.0265 186 ASN A C   
1461 O  O   . ASN A 189 ? 0.3067 0.3198 0.3623 -0.0366 -0.0800 -0.0113 186 ASN A O   
1462 C  CB  . ASN A 189 ? 0.1675 0.2377 0.2404 -0.0069 -0.0140 -0.0137 186 ASN A CB  
1463 C  CG  . ASN A 189 ? 0.1488 0.2093 0.2272 0.0037  -0.0182 0.0020  186 ASN A CG  
1464 O  OD1 . ASN A 189 ? 0.1582 0.2526 0.2193 0.0240  0.0065  -0.0241 186 ASN A OD1 
1465 N  ND2 . ASN A 189 ? 0.1359 0.2404 0.2272 -0.0133 -0.0213 0.0075  186 ASN A ND2 
1466 O  OXT . ASN A 189 ? 0.4057 0.2972 0.3906 -0.0499 -0.0685 0.0174  186 ASN A OXT 
1467 C  C1  . EDO B .   ? 0.4231 0.5593 0.5419 -0.0472 -0.0502 -0.0313 201 EDO A C1  
1468 O  O1  . EDO B .   ? 0.4548 0.6178 0.5895 -0.0357 -0.1030 -0.0813 201 EDO A O1  
1469 C  C2  . EDO B .   ? 0.3972 0.5763 0.4922 -0.0243 -0.0276 0.0093  201 EDO A C2  
1470 O  O2  . EDO B .   ? 0.3707 0.3900 0.2965 -0.0573 -0.0568 0.0515  201 EDO A O2  
1471 C  C1  . BME C .   ? 0.5596 0.5221 0.2450 -0.1346 -0.0187 -0.0088 202 BME A C1  
1472 C  C2  . BME C .   ? 0.4566 0.4137 0.2072 -0.1796 -0.0974 -0.0279 202 BME A C2  
1473 O  O1  . BME C .   ? 0.4609 0.5405 0.2661 -0.1294 0.0027  -0.0565 202 BME A O1  
1474 S  S2  . BME C .   ? 0.5579 0.6892 0.4635 -0.1376 -0.0626 -0.0806 202 BME A S2  
1475 NA NA  . NA  D .   ? 0.6054 0.7539 0.6145 0.0175  -0.0267 -0.0621 203 NA  A NA  
1476 NA NA  . NA  E .   ? 0.5097 0.4521 0.3726 0.0664  -0.0562 0.0011  204 NA  A NA  
1477 S  S   . SO4 F .   ? 0.2832 0.3727 0.8518 -0.0200 -0.0356 -0.0418 205 SO4 A S   
1478 O  O1  . SO4 F .   ? 0.4409 0.4287 0.8629 0.0970  0.0547  -0.0245 205 SO4 A O1  
1479 O  O2  . SO4 F .   ? 0.2333 0.3787 0.6697 -0.0681 -0.0097 -0.0192 205 SO4 A O2  
1480 O  O3  . SO4 F .   ? 0.4997 0.5816 0.8096 -0.0644 -0.0548 0.0103  205 SO4 A O3  
1481 O  O4  . SO4 F .   ? 0.3117 0.2951 0.8468 -0.0017 0.0244  -0.0528 205 SO4 A O4  
1482 S  S   . SO4 G .   ? 0.2975 0.3808 0.4516 0.0713  -0.0175 0.0386  206 SO4 A S   
1483 O  O1  . SO4 G .   ? 0.5257 0.3346 0.4960 0.0496  -0.0234 0.0838  206 SO4 A O1  
1484 O  O2  . SO4 G .   ? 0.4317 0.4307 0.6323 -0.0473 -0.0365 -0.0260 206 SO4 A O2  
1485 O  O3  . SO4 G .   ? 0.3717 0.4493 0.4556 0.1493  -0.0691 0.0201  206 SO4 A O3  
1486 O  O4  . SO4 G .   ? 0.3267 0.4129 0.3922 0.0452  0.0561  0.0110  206 SO4 A O4  
1487 O  O   . HOH H .   ? 0.6969 0.6865 0.6715 0.0677  0.0562  0.1483  301 HOH A O   
1488 O  O   . HOH H .   ? 0.2953 0.3900 0.3795 0.0108  0.0047  0.0564  302 HOH A O   
1489 O  O   . HOH H .   ? 0.1797 0.3082 0.2996 0.0630  0.0329  0.0540  303 HOH A O   
1490 O  O   . HOH H .   ? 0.5773 0.4390 0.3671 -0.0050 0.0492  -0.0006 304 HOH A O   
1491 O  O   . HOH H .   ? 0.5658 0.3185 0.3069 -0.0155 -0.0564 -0.0767 305 HOH A O   
1492 O  O   . HOH H .   ? 0.5895 0.3691 0.2647 0.1361  0.0660  0.0553  306 HOH A O   
1493 O  O   . HOH H .   ? 0.6180 0.4409 0.3966 0.0715  0.0507  -0.0462 307 HOH A O   
1494 O  O   . HOH H .   ? 0.5214 0.3757 0.7929 -0.0502 0.1371  0.1230  308 HOH A O   
1495 O  O   . HOH H .   ? 0.5680 0.3605 0.4472 -0.0135 0.1842  0.0870  309 HOH A O   
1496 O  O   . HOH H .   ? 0.2625 0.5066 0.4256 -0.0409 0.0177  -0.0404 310 HOH A O   
1497 O  O   . HOH H .   ? 0.3083 0.3112 0.3292 0.0172  -0.0540 0.0048  311 HOH A O   
1498 O  O   . HOH H .   ? 0.1724 0.3236 0.3143 -0.0150 0.0603  -0.0240 312 HOH A O   
1499 O  O   . HOH H .   ? 0.2889 0.4894 0.3819 -0.0960 0.0108  0.0240  313 HOH A O   
1500 O  O   . HOH H .   ? 0.2156 0.2958 0.2622 -0.0317 -0.0159 -0.0376 314 HOH A O   
1501 O  O   . HOH H .   ? 0.3165 0.2757 0.4152 -0.0314 0.0257  -0.0256 315 HOH A O   
1502 O  O   . HOH H .   ? 0.2400 0.3882 0.3943 -0.0598 0.0025  0.0498  316 HOH A O   
1503 O  O   . HOH H .   ? 0.2653 0.4074 0.3992 0.0548  -0.0872 -0.1140 317 HOH A O   
1504 O  O   . HOH H .   ? 0.1835 0.1977 0.2676 -0.0192 0.0227  -0.0405 318 HOH A O   
1505 O  O   . HOH H .   ? 0.1544 0.2009 0.1911 -0.0003 0.0001  -0.0138 319 HOH A O   
1506 O  O   . HOH H .   ? 0.1860 0.1753 0.2034 -0.0192 -0.0332 0.0043  320 HOH A O   
1507 O  O   . HOH H .   ? 0.3733 0.4911 0.3647 -0.1323 -0.0814 -0.0128 321 HOH A O   
1508 O  O   . HOH H .   ? 0.2287 0.4209 0.3213 0.0573  0.0185  -0.0670 322 HOH A O   
1509 O  O   . HOH H .   ? 0.3725 0.3481 0.3294 0.0300  -0.0168 0.0340  323 HOH A O   
1510 O  O   . HOH H .   ? 0.2903 0.2865 0.2312 0.0017  0.0347  0.0152  324 HOH A O   
1511 O  O   . HOH H .   ? 0.4977 0.3335 0.3583 0.0639  0.0409  -0.0046 325 HOH A O   
1512 O  O   . HOH H .   ? 0.1586 0.2236 0.1858 -0.0161 0.0109  -0.0020 326 HOH A O   
1513 O  O   . HOH H .   ? 0.5091 0.4207 0.4321 0.0616  -0.1736 0.0459  327 HOH A O   
1514 O  O   . HOH H .   ? 0.4417 0.6740 0.4055 0.1494  0.0202  -0.0433 328 HOH A O   
1515 O  O   . HOH H .   ? 0.3126 0.3033 0.3732 -0.0183 -0.0340 -0.0210 329 HOH A O   
1516 O  O   . HOH H .   ? 0.3203 0.3051 0.5643 0.0931  0.0651  -0.0914 330 HOH A O   
1517 O  O   . HOH H .   ? 0.4572 0.3750 0.5558 0.0487  0.2046  -0.0227 331 HOH A O   
1518 O  O   . HOH H .   ? 0.3311 0.5127 0.3179 0.0186  -0.0269 -0.1010 332 HOH A O   
1519 O  O   . HOH H .   ? 0.3720 0.2203 0.3189 0.0043  0.0606  -0.0159 333 HOH A O   
1520 O  O   . HOH H .   ? 0.2115 0.3532 0.2915 0.0513  0.0227  0.0134  334 HOH A O   
1521 O  O   . HOH H .   ? 0.4730 0.3810 0.3543 -0.0242 -0.0987 0.0272  335 HOH A O   
1522 O  O   . HOH H .   ? 0.2219 0.3386 0.4783 0.0095  -0.0193 0.0308  336 HOH A O   
1523 O  O   . HOH H .   ? 0.4497 0.4357 0.3227 -0.1423 0.0214  0.0159  337 HOH A O   
1524 O  O   . HOH H .   ? 0.3717 0.4483 0.5175 0.0163  0.0336  0.0430  338 HOH A O   
1525 O  O   . HOH H .   ? 0.2015 0.1932 0.2754 0.0199  -0.0238 -0.0512 339 HOH A O   
1526 O  O   . HOH H .   ? 0.2842 0.3055 0.1893 0.0240  0.0148  -0.0290 340 HOH A O   
1527 O  O   . HOH H .   ? 0.1571 0.1775 0.2011 -0.0243 -0.0133 0.0040  341 HOH A O   
1528 O  O   . HOH H .   ? 0.5124 0.3412 0.4963 -0.0030 0.1601  0.0335  342 HOH A O   
1529 O  O   . HOH H .   ? 0.2948 0.4298 0.3660 0.0036  0.0651  -0.0191 343 HOH A O   
1530 O  O   . HOH H .   ? 0.5876 0.4660 0.3277 0.0362  0.0865  0.1448  344 HOH A O   
1531 O  O   . HOH H .   ? 0.2015 0.2270 0.2772 -0.0322 -0.0237 0.0468  345 HOH A O   
1532 O  O   . HOH H .   ? 0.4350 0.4096 0.4011 0.0114  -0.0742 0.0586  346 HOH A O   
1533 O  O   . HOH H .   ? 0.7372 0.6388 0.5137 -0.0337 -0.2134 0.0427  347 HOH A O   
1534 O  O   . HOH H .   ? 0.2092 0.5102 0.5507 0.0888  -0.1114 -0.0800 348 HOH A O   
1535 O  O   . HOH H .   ? 0.2872 0.3961 0.2627 0.0715  -0.0025 0.0574  349 HOH A O   
1536 O  O   . HOH H .   ? 0.3150 0.3155 0.2905 0.0754  -0.0512 0.0408  350 HOH A O   
1537 O  O   . HOH H .   ? 0.3554 0.3713 0.3931 -0.0887 -0.0375 -0.0284 351 HOH A O   
1538 O  O   . HOH H .   ? 0.3249 0.2439 0.2680 -0.0419 0.0059  -0.0340 352 HOH A O   
1539 O  O   . HOH H .   ? 0.1520 0.2358 0.1965 0.0003  0.0116  -0.0137 353 HOH A O   
1540 O  O   . HOH H .   ? 0.1346 0.1778 0.1638 -0.0126 -0.0090 -0.0045 354 HOH A O   
1541 O  O   . HOH H .   ? 0.3269 0.3073 0.5109 0.0530  -0.1507 -0.0103 355 HOH A O   
1542 O  O   . HOH H .   ? 0.3178 0.3035 0.4150 0.0212  0.0089  0.0382  356 HOH A O   
1543 O  O   . HOH H .   ? 0.1255 0.1696 0.1441 0.0045  0.0029  0.0022  357 HOH A O   
1544 O  O   . HOH H .   ? 0.2465 0.3275 0.3214 -0.0208 0.0479  -0.0525 358 HOH A O   
1545 O  O   . HOH H .   ? 1.0664 0.4483 0.6697 0.2816  0.0081  -0.1758 359 HOH A O   
1546 O  O   . HOH H .   ? 0.2484 0.3475 0.3943 -0.0696 -0.0596 0.0913  360 HOH A O   
1547 O  O   . HOH H .   ? 0.5156 0.2738 0.2625 0.0403  -0.0418 -0.0082 361 HOH A O   
1548 O  O   . HOH H .   ? 0.5061 0.4620 0.5392 0.0348  -0.0173 0.0784  362 HOH A O   
1549 O  O   . HOH H .   ? 0.2554 0.2526 0.3017 0.0129  0.0224  0.0278  363 HOH A O   
1550 O  O   . HOH H .   ? 0.4926 0.3548 0.5182 -0.0453 -0.2482 0.0187  364 HOH A O   
1551 O  O   . HOH H .   ? 0.3273 0.3937 0.3948 0.0797  -0.0221 -0.0972 365 HOH A O   
1552 O  O   . HOH H .   ? 0.4003 0.4196 0.3222 -0.0953 0.0157  0.0261  366 HOH A O   
1553 O  O   . HOH H .   ? 0.3453 0.2932 0.2962 0.0096  -0.0716 -0.0464 367 HOH A O   
1554 O  O   . HOH H .   ? 0.3607 0.2889 0.2688 -0.0307 -0.1171 0.0304  368 HOH A O   
1555 O  O   . HOH H .   ? 0.1411 0.2558 0.2213 -0.0076 0.0061  0.0210  369 HOH A O   
1556 O  O   . HOH H .   ? 0.4122 0.5989 0.4300 0.1121  -0.1198 0.0596  370 HOH A O   
1557 O  O   . HOH H .   ? 0.3877 0.2603 0.3020 -0.0148 0.0618  0.0225  371 HOH A O   
1558 O  O   . HOH H .   ? 0.4142 0.3603 0.3160 0.0301  -0.1425 -0.0251 372 HOH A O   
1559 O  O   . HOH H .   ? 0.7364 0.4428 0.2685 -0.0198 -0.0058 0.0003  373 HOH A O   
1560 O  O   . HOH H .   ? 1.0558 0.8836 0.7416 -0.1949 0.5159  0.3133  374 HOH A O   
1561 O  O   . HOH H .   ? 0.2981 0.2945 0.2765 -0.0401 0.0743  -0.0274 375 HOH A O   
1562 O  O   . HOH H .   ? 0.2998 0.4057 0.4305 0.0648  0.0313  -0.0701 376 HOH A O   
1563 O  O   . HOH H .   ? 0.3240 0.3978 0.2709 0.0450  0.0218  0.0145  377 HOH A O   
1564 O  O   . HOH H .   ? 0.2308 0.3546 0.3772 0.0904  -0.0111 -0.0529 378 HOH A O   
1565 O  O   . HOH H .   ? 0.3998 0.2840 0.3596 0.0547  -0.0778 -0.0587 379 HOH A O   
1566 O  O   . HOH H .   ? 0.3006 0.3997 0.3827 0.1343  0.0280  -0.0096 380 HOH A O   
1567 O  O   . HOH H .   ? 0.1615 0.3560 0.2549 0.0123  0.0314  -0.0714 381 HOH A O   
1568 O  O   . HOH H .   ? 0.1421 0.2320 0.3777 -0.0130 -0.0240 0.0626  382 HOH A O   
1569 O  O   . HOH H .   ? 0.2137 0.1913 0.2680 0.0000  -0.0073 -0.0150 383 HOH A O   
1570 O  O   . HOH H .   ? 0.3521 0.7512 0.2876 -0.1322 -0.0140 -0.0120 384 HOH A O   
1571 O  O   . HOH H .   ? 0.4767 0.3324 0.3189 -0.1011 0.0144  -0.0169 385 HOH A O   
1572 O  O   . HOH H .   ? 0.3180 0.4134 0.5176 -0.1414 -0.0959 0.1013  386 HOH A O   
1573 O  O   . HOH H .   ? 0.2349 0.2699 0.2749 -0.0253 -0.0186 -0.0063 387 HOH A O   
1574 O  O   . HOH H .   ? 0.4428 0.5510 0.6250 0.1006  0.0589  0.0996  388 HOH A O   
1575 O  O   . HOH H .   ? 0.2016 0.4653 0.2963 -0.0066 0.0349  0.0087  389 HOH A O   
1576 O  O   . HOH H .   ? 0.3055 0.4187 0.5268 0.0875  -0.0627 0.0556  390 HOH A O   
1577 O  O   . HOH H .   ? 0.5161 0.4071 0.3150 -0.1226 0.0320  0.0165  391 HOH A O   
1578 O  O   . HOH H .   ? 0.2448 0.3701 0.2841 -0.0239 -0.0309 0.1027  392 HOH A O   
1579 O  O   . HOH H .   ? 0.4757 0.7388 0.4965 0.1937  0.1344  0.1579  393 HOH A O   
1580 O  O   . HOH H .   ? 0.2598 0.5338 0.3724 -0.1565 0.0239  -0.0471 394 HOH A O   
1581 O  O   . HOH H .   ? 0.2741 0.3812 0.3264 0.0802  -0.0916 -0.1025 395 HOH A O   
1582 O  O   . HOH H .   ? 0.2525 0.3375 0.4465 -0.0037 0.0482  0.0350  396 HOH A O   
1583 O  O   . HOH H .   ? 0.1997 0.3160 0.2697 0.0297  -0.0205 -0.0537 397 HOH A O   
1584 O  O   . HOH H .   ? 0.2709 0.3983 0.3867 0.0643  0.0311  0.0039  398 HOH A O   
1585 O  O   . HOH H .   ? 0.6148 0.7226 0.3960 0.0024  -0.1581 -0.3773 399 HOH A O   
1586 O  O   . HOH H .   ? 0.3773 0.4181 0.7715 0.0609  -0.0539 -0.2032 400 HOH A O   
1587 O  O   . HOH H .   ? 0.3144 0.2933 0.2657 0.0406  0.0028  -0.0555 401 HOH A O   
1588 O  O   . HOH H .   ? 0.4056 0.3658 0.5539 -0.1081 -0.0234 -0.0361 402 HOH A O   
1589 O  O   . HOH H .   ? 0.5319 0.4638 0.4769 -0.0485 0.0913  0.0798  403 HOH A O   
1590 O  O   . HOH H .   ? 0.2685 0.3247 0.5164 0.0584  -0.0261 0.0026  404 HOH A O   
1591 O  O   . HOH H .   ? 0.0982 0.1846 0.1347 -0.0367 -0.0092 -0.0378 405 HOH A O   
1592 O  O   . HOH H .   ? 0.6552 0.6624 0.3711 0.0348  0.0505  0.0340  406 HOH A O   
1593 O  O   . HOH H .   ? 0.6335 0.3055 0.5879 -0.0928 -0.1857 -0.0249 407 HOH A O   
1594 O  O   . HOH H .   ? 0.0943 0.2099 0.2363 -0.0118 0.0012  0.0621  408 HOH A O   
1595 O  O   . HOH H .   ? 0.5379 0.5552 0.4598 0.0901  0.0679  0.0518  409 HOH A O   
1596 O  O   . HOH H .   ? 0.4079 0.5146 0.4571 0.1867  -0.0629 -0.0084 410 HOH A O   
1597 O  O   . HOH H .   ? 0.2678 0.2989 0.4088 0.0345  -0.0421 0.0077  411 HOH A O   
1598 O  O   . HOH H .   ? 0.3126 0.4552 0.4423 0.0308  -0.0188 -0.0035 412 HOH A O   
1599 O  O   . HOH H .   ? 0.3609 0.3521 0.4084 -0.0279 -0.0405 -0.0517 413 HOH A O   
1600 O  O   . HOH H .   ? 0.4575 0.3118 0.6188 -0.0737 -0.0663 0.0192  414 HOH A O   
1601 O  O   . HOH H .   ? 0.3359 0.3832 0.3197 -0.0897 0.0079  -0.0587 415 HOH A O   
1602 O  O   . HOH H .   ? 0.6548 0.4214 0.4094 -0.1353 0.0748  -0.1200 416 HOH A O   
1603 O  O   . HOH H .   ? 0.4626 0.3796 0.4224 -0.1164 0.0351  -0.0528 417 HOH A O   
1604 O  O   . HOH H .   ? 0.7313 0.4972 0.7110 -0.2580 0.1306  -0.2011 418 HOH A O   
1605 O  O   . HOH H .   ? 0.5427 0.9039 0.4263 -0.0738 -0.0157 -0.1032 419 HOH A O   
1606 O  O   . HOH H .   ? 0.2568 0.5953 0.6182 0.0955  -0.0494 0.0439  420 HOH A O   
1607 O  O   . HOH H .   ? 0.3710 0.4116 0.3825 0.0239  -0.0779 -0.0001 421 HOH A O   
1608 O  O   . HOH H .   ? 0.6637 0.4699 0.7787 -0.0298 -0.0110 -0.0541 422 HOH A O   
1609 O  O   . HOH H .   ? 0.6784 0.3640 0.4682 -0.0412 -0.0022 -0.0078 423 HOH A O   
1610 O  O   . HOH H .   ? 0.4788 0.4831 0.3697 0.0267  -0.0370 0.0391  424 HOH A O   
1611 O  O   . HOH H .   ? 0.5913 0.4575 0.4000 0.0996  -0.1646 -0.1611 425 HOH A O   
1612 O  O   . HOH H .   ? 0.4122 0.4421 0.8823 0.0004  0.0589  -0.1966 426 HOH A O   
1613 O  O   . HOH H .   ? 0.2602 0.2258 0.3205 0.0156  0.0044  -0.0178 427 HOH A O   
1614 O  O   . HOH H .   ? 0.5241 0.4029 0.3003 -0.0223 -0.0297 0.0702  428 HOH A O   
1615 O  O   . HOH H .   ? 0.4672 0.3719 0.5777 0.0094  -0.1587 -0.1273 429 HOH A O   
1616 O  O   . HOH H .   ? 0.4223 0.3087 0.2918 -0.0002 -0.0120 0.0260  430 HOH A O   
1617 O  O   . HOH H .   ? 0.6033 0.3242 0.3133 0.0437  -0.0993 -0.0280 431 HOH A O   
1618 O  O   . HOH H .   ? 0.3798 0.2463 0.2760 0.0041  0.0645  -0.0133 432 HOH A O   
1619 O  O   . HOH H .   ? 0.8076 0.7499 0.3617 -0.2509 0.0805  0.0471  433 HOH A O   
1620 O  O   . HOH H .   ? 0.2224 0.2576 0.3204 -0.0211 0.0476  0.0281  434 HOH A O   
1621 O  O   . HOH H .   ? 0.5616 0.4358 0.6246 0.0069  0.0768  -0.0300 435 HOH A O   
1622 O  O   . HOH H .   ? 0.7425 0.3643 0.2883 -0.1569 0.0326  0.0368  436 HOH A O   
1623 O  O   . HOH H .   ? 0.4765 0.5696 0.4244 -0.0959 0.0494  -0.1286 437 HOH A O   
1624 O  O   . HOH H .   ? 0.3328 0.6328 0.7198 -0.0689 0.0822  -0.0798 438 HOH A O   
1625 O  O   . HOH H .   ? 0.5393 0.6121 0.3272 0.2006  0.0147  -0.1137 439 HOH A O   
1626 O  O   . HOH H .   ? 0.7698 0.3685 0.2114 -0.0535 0.0497  -0.0516 440 HOH A O   
1627 O  O   . HOH H .   ? 0.4047 0.4700 0.4582 -0.0868 -0.1032 0.0834  441 HOH A O   
# 
