data_8WKD
# 
_entry.id   8WKD 
# 
_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   8WKD         pdb_00008wkd 10.2210/pdb8wkd/pdb 
WWPDB D_1300041442 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-01-22 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8WKD 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-27 
_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              wubin@ntu.edu.sg 
_pdbx_contact_author.name_first         Bin 
_pdbx_contact_author.name_last          Wu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0883-8006 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chong, H.C.' 1 0000-0002-8137-2556 
'Wu, B.'      2 0000-0002-0883-8006 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                1604 
_citation.page_last                 1611 
_citation.title                     'Structural Basis of High-Precision Protein Ligation and Its Application.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c10689 
_citation.pdbx_database_id_PubMed   39745918 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chong, K.H.C.' 1  ?                   
primary 'Liu, L.'       2  ?                   
primary 'Chua, R.'      3  ?                   
primary 'Chai, Y.T.'    4  ?                   
primary 'Lu, Z.'        5  0009-0006-1671-8844 
primary 'Liu, R.'       6  ?                   
primary 'Tan, E.Y.J.'   7  ?                   
primary 'Dong, J.'      8  ?                   
primary 'Khoh, Y.H.'    9  ?                   
primary 'Lin, J.'       10 0000-0003-4336-9003 
primary 'Zhong, F.L.'   11 ?                   
primary 'Lescar, J.'    12 ?                   
primary 'Zheng, P.'     13 0000-0003-4792-6364 
primary 'Wu, B.'        14 0000-0002-0883-8006 
# 
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 'DUF2121 domain-containing protein'                     21084.197 1  ?        C192S     ? ? 
2 polymer syn 'Tetrahydromethanopterin S-methyltransferase subunit A' 2110.430  1  2.1.1.86 F11V,D14K ? ? 
3 water   nat water                                                   18.015    73 ?        ?         ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        'N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;ALVIAFIGKNGAVMAGDMREITFEGEKPDREKLEKELYSGSIVTDEEMQKKAEEFGVKITVADCKEKVSERNGVLVGEVS
SAEGGVVKKRRLYASAGNFAIAELINTEMTLTSQGKGSNFIAFGNEFTKQVANKCFKDNWTKKSNLQDAVKILILCMETV
ARKTASVSKQFMIVQTASNADVLKVVEKDRNS
;
;ALVIAFIGKNGAVMAGDMREITFEGEKPDREKLEKELYSGSIVTDEEMQKKAEEFGVKITVADCKEKVSERNGVLVGEVS
SAEGGVVKKRRLYASAGNFAIAELINTEMTLTSQGKGSNFIAFGNEFTKQVANKCFKDNWTKKSNLQDAVKILILCMETV
ARKTASVSKQFMIVQTASNADVLKVVEKDRNS
;
A ? 
2 'polypeptide(L)' no no RELASKDPGAVDAKPLVVEI RELASKDPGAVDAKPLVVEI C ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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   LEU n 
1 3   VAL n 
1 4   ILE n 
1 5   ALA n 
1 6   PHE n 
1 7   ILE n 
1 8   GLY n 
1 9   LYS n 
1 10  ASN n 
1 11  GLY n 
1 12  ALA n 
1 13  VAL n 
1 14  MET n 
1 15  ALA n 
1 16  GLY n 
1 17  ASP n 
1 18  MET n 
1 19  ARG n 
1 20  GLU n 
1 21  ILE n 
1 22  THR n 
1 23  PHE n 
1 24  GLU n 
1 25  GLY n 
1 26  GLU n 
1 27  LYS n 
1 28  PRO n 
1 29  ASP n 
1 30  ARG n 
1 31  GLU n 
1 32  LYS n 
1 33  LEU n 
1 34  GLU n 
1 35  LYS n 
1 36  GLU n 
1 37  LEU n 
1 38  TYR n 
1 39  SER n 
1 40  GLY n 
1 41  SER n 
1 42  ILE n 
1 43  VAL n 
1 44  THR n 
1 45  ASP n 
1 46  GLU n 
1 47  GLU n 
1 48  MET n 
1 49  GLN n 
1 50  LYS n 
1 51  LYS n 
1 52  ALA n 
1 53  GLU n 
1 54  GLU n 
1 55  PHE n 
1 56  GLY n 
1 57  VAL n 
1 58  LYS n 
1 59  ILE n 
1 60  THR n 
1 61  VAL n 
1 62  ALA n 
1 63  ASP n 
1 64  CYS n 
1 65  LYS n 
1 66  GLU n 
1 67  LYS n 
1 68  VAL n 
1 69  SER n 
1 70  GLU n 
1 71  ARG n 
1 72  ASN n 
1 73  GLY n 
1 74  VAL n 
1 75  LEU n 
1 76  VAL n 
1 77  GLY n 
1 78  GLU n 
1 79  VAL n 
1 80  SER n 
1 81  SER n 
1 82  ALA n 
1 83  GLU n 
1 84  GLY n 
1 85  GLY n 
1 86  VAL n 
1 87  VAL n 
1 88  LYS n 
1 89  LYS n 
1 90  ARG n 
1 91  ARG n 
1 92  LEU n 
1 93  TYR n 
1 94  ALA n 
1 95  SER n 
1 96  ALA n 
1 97  GLY n 
1 98  ASN n 
1 99  PHE n 
1 100 ALA n 
1 101 ILE n 
1 102 ALA n 
1 103 GLU n 
1 104 LEU n 
1 105 ILE n 
1 106 ASN n 
1 107 THR n 
1 108 GLU n 
1 109 MET n 
1 110 THR n 
1 111 LEU n 
1 112 THR n 
1 113 SER n 
1 114 GLN n 
1 115 GLY n 
1 116 LYS n 
1 117 GLY n 
1 118 SER n 
1 119 ASN n 
1 120 PHE n 
1 121 ILE n 
1 122 ALA n 
1 123 PHE n 
1 124 GLY n 
1 125 ASN n 
1 126 GLU n 
1 127 PHE n 
1 128 THR n 
1 129 LYS n 
1 130 GLN n 
1 131 VAL n 
1 132 ALA n 
1 133 ASN n 
1 134 LYS n 
1 135 CYS n 
1 136 PHE n 
1 137 LYS n 
1 138 ASP n 
1 139 ASN n 
1 140 TRP n 
1 141 THR n 
1 142 LYS n 
1 143 LYS n 
1 144 SER n 
1 145 ASN n 
1 146 LEU n 
1 147 GLN n 
1 148 ASP n 
1 149 ALA n 
1 150 VAL n 
1 151 LYS n 
1 152 ILE n 
1 153 LEU n 
1 154 ILE n 
1 155 LEU n 
1 156 CYS n 
1 157 MET n 
1 158 GLU n 
1 159 THR n 
1 160 VAL n 
1 161 ALA n 
1 162 ARG n 
1 163 LYS n 
1 164 THR n 
1 165 ALA n 
1 166 SER n 
1 167 VAL n 
1 168 SER n 
1 169 LYS n 
1 170 GLN n 
1 171 PHE n 
1 172 MET n 
1 173 ILE n 
1 174 VAL n 
1 175 GLN n 
1 176 THR n 
1 177 ALA n 
1 178 SER n 
1 179 ASN n 
1 180 ALA n 
1 181 ASP n 
1 182 VAL n 
1 183 LEU n 
1 184 LYS n 
1 185 VAL n 
1 186 VAL n 
1 187 GLU n 
1 188 LYS n 
1 189 ASP n 
1 190 ARG n 
1 191 ASN n 
1 192 SER n 
2 1   ARG n 
2 2   GLU n 
2 3   LEU n 
2 4   ALA n 
2 5   SER n 
2 6   LYS n 
2 7   ASP n 
2 8   PRO n 
2 9   GLY n 
2 10  ALA n 
2 11  VAL n 
2 12  ASP n 
2 13  ALA n 
2 14  LYS n 
2 15  PRO n 
2 16  LEU n 
2 17  VAL n 
2 18  VAL n 
2 19  GLU n 
2 20  ILE 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                   192 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DU44_16730, DU48_12575, DU65_18300, DU71_01400, DU72_16840, FQU78_09620' 
_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      'Methanosarcina mazei' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2209 
_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                       pET47b-CntT1AC192S 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       20 
_pdbx_entity_src_syn.organism_scientific    'Methanosarcina mazei' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       2209 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  PHE 23  23  23  PHE PHE A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  CYS 64  64  64  CYS CYS A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 CYS 135 135 135 CYS CYS A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 TRP 140 140 140 TRP TRP A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ILE 154 154 154 ILE ILE A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ASN 179 179 179 ASN ASN A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 SER 192 192 192 SER SER A . n 
B 2 1   ARG 1   1   ?   ?   ?   C . n 
B 2 2   GLU 2   2   ?   ?   ?   C . n 
B 2 3   LEU 3   3   ?   ?   ?   C . n 
B 2 4   ALA 4   4   4   ALA ALA C . n 
B 2 5   SER 5   5   5   SER SER C . n 
B 2 6   LYS 6   6   6   LYS LYS C . n 
B 2 7   ASP 7   7   7   ASP ASP C . n 
B 2 8   PRO 8   8   8   PRO PRO C . n 
B 2 9   GLY 9   9   9   GLY GLY C . n 
B 2 10  ALA 10  10  10  ALA ALA C . n 
B 2 11  VAL 11  11  11  VAL VAL C . n 
B 2 12  ASP 12  12  12  ASP ASP C . n 
B 2 13  ALA 13  13  13  ALA ALA C . n 
B 2 14  LYS 14  14  14  LYS LYS C . n 
B 2 15  PRO 15  15  15  PRO PRO C . n 
B 2 16  LEU 16  16  16  LEU LEU C . n 
B 2 17  VAL 17  17  17  VAL VAL C . n 
B 2 18  VAL 18  18  18  VAL VAL C . n 
B 2 19  GLU 19  19  19  GLU GLU C . n 
B 2 20  ILE 20  20  20  ILE ILE C . 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 
C 3 HOH 1  201 53 HOH HOH A . 
C 3 HOH 2  202 47 HOH HOH A . 
C 3 HOH 3  203 50 HOH HOH A . 
C 3 HOH 4  204 65 HOH HOH A . 
C 3 HOH 5  205 39 HOH HOH A . 
C 3 HOH 6  206 66 HOH HOH A . 
C 3 HOH 7  207 78 HOH HOH A . 
C 3 HOH 8  208 76 HOH HOH A . 
C 3 HOH 9  209 2  HOH HOH A . 
C 3 HOH 10 210 29 HOH HOH A . 
C 3 HOH 11 211 70 HOH HOH A . 
C 3 HOH 12 212 2  HOH HOH A . 
C 3 HOH 13 213 21 HOH HOH A . 
C 3 HOH 14 214 74 HOH HOH A . 
C 3 HOH 15 215 35 HOH HOH A . 
C 3 HOH 16 216 38 HOH HOH A . 
C 3 HOH 17 217 77 HOH HOH A . 
C 3 HOH 18 218 14 HOH HOH A . 
C 3 HOH 19 219 19 HOH HOH A . 
C 3 HOH 20 220 32 HOH HOH A . 
C 3 HOH 21 221 26 HOH HOH A . 
C 3 HOH 22 222 20 HOH HOH A . 
C 3 HOH 23 223 25 HOH HOH A . 
C 3 HOH 24 224 5  HOH HOH A . 
C 3 HOH 25 225 52 HOH HOH A . 
C 3 HOH 26 226 33 HOH HOH A . 
C 3 HOH 27 227 30 HOH HOH A . 
C 3 HOH 28 228 12 HOH HOH A . 
C 3 HOH 29 229 22 HOH HOH A . 
C 3 HOH 30 230 7  HOH HOH A . 
C 3 HOH 31 231 8  HOH HOH A . 
C 3 HOH 32 232 1  HOH HOH A . 
C 3 HOH 33 233 57 HOH HOH A . 
C 3 HOH 34 234 46 HOH HOH A . 
C 3 HOH 35 235 36 HOH HOH A . 
C 3 HOH 36 236 11 HOH HOH A . 
C 3 HOH 37 237 10 HOH HOH A . 
C 3 HOH 38 238 64 HOH HOH A . 
C 3 HOH 39 239 40 HOH HOH A . 
C 3 HOH 40 240 9  HOH HOH A . 
C 3 HOH 41 241 1  HOH HOH A . 
C 3 HOH 42 242 16 HOH HOH A . 
C 3 HOH 43 243 15 HOH HOH A . 
C 3 HOH 44 244 13 HOH HOH A . 
C 3 HOH 45 245 48 HOH HOH A . 
C 3 HOH 46 246 6  HOH HOH A . 
C 3 HOH 47 247 55 HOH HOH A . 
C 3 HOH 48 248 41 HOH HOH A . 
C 3 HOH 49 249 18 HOH HOH A . 
C 3 HOH 50 250 34 HOH HOH A . 
C 3 HOH 51 251 69 HOH HOH A . 
C 3 HOH 52 252 62 HOH HOH A . 
C 3 HOH 53 253 58 HOH HOH A . 
C 3 HOH 54 254 75 HOH HOH A . 
C 3 HOH 55 255 31 HOH HOH A . 
C 3 HOH 56 256 49 HOH HOH A . 
C 3 HOH 57 257 42 HOH HOH A . 
C 3 HOH 58 258 23 HOH HOH A . 
C 3 HOH 59 259 71 HOH HOH A . 
C 3 HOH 60 260 60 HOH HOH A . 
C 3 HOH 61 261 45 HOH HOH A . 
C 3 HOH 62 262 59 HOH HOH A . 
C 3 HOH 63 263 67 HOH HOH A . 
C 3 HOH 64 264 61 HOH HOH A . 
C 3 HOH 65 265 43 HOH HOH A . 
D 3 HOH 1  101 51 HOH HOH C . 
D 3 HOH 2  102 3  HOH HOH C . 
D 3 HOH 3  103 54 HOH HOH C . 
D 3 HOH 4  104 37 HOH HOH C . 
D 3 HOH 5  105 68 HOH HOH C . 
D 3 HOH 6  106 24 HOH HOH C . 
D 3 HOH 7  107 56 HOH HOH C . 
D 3 HOH 8  108 27 HOH HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.21rc1_5015: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WKD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.100 
_cell.length_a_esd                 ? 
_cell.length_b                     100.970 
_cell.length_b_esd                 ? 
_cell.length_c                     32.600 
_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                         8WKD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WKD 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.92 
_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              8.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'constant temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 8.2, 0.05 M NaCl, 24% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   7.5-9.0 
_exptl_crystal_grow.temp            291.15 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-27 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WKD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.98 
_reflns.d_resolution_low                               47.69 
_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                                     61160 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.17 
_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                                   0.999 
_reflns.pdbx_CC_star                                   1 
_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                                    1.98 
_reflns_shell.d_res_low                                     2.07 
_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                             6196 
_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                                  0.739 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8WKD 
_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                            1.98 
_refine.ls_d_res_low                             47.69 
_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                     23726 
_refine.ls_number_reflns_R_free                  1182 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.26 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2209 
_refine.ls_R_factor_R_free                       0.2693 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2182 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.69 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1591 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             73 
_refine_hist.number_atoms_total               1664 
_refine_hist.d_res_high                       1.98 
_refine_hist.d_res_low                        47.69 
# 
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' ? 0.021  ? 1605 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 2.380  ? 2150 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 22.838 ? 609  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.114  ? 251  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.014  ? 276  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.98 2.07  . . 136 2696 95.00  . . . . 0.3236 . . . . . . . . . . . 0.3769 
'X-RAY DIFFRACTION' 2.07 2.18  . . 151 2851 100.00 . . . . 0.2894 . . . . . . . . . . . 0.3201 
'X-RAY DIFFRACTION' 2.18 2.32  . . 148 2830 100.00 . . . . 0.2812 . . . . . . . . . . . 0.3378 
'X-RAY DIFFRACTION' 2.32 2.50  . . 149 2837 100.00 . . . . 0.2577 . . . . . . . . . . . 0.2729 
'X-RAY DIFFRACTION' 2.50 2.75  . . 154 2836 100.00 . . . . 0.2473 . . . . . . . . . . . 0.3086 
'X-RAY DIFFRACTION' 2.75 3.15  . . 138 2836 100.00 . . . . 0.2295 . . . . . . . . . . . 0.2875 
'X-RAY DIFFRACTION' 3.15 3.97  . . 155 2832 100.00 . . . . 0.1922 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 3.97 47.69 . . 151 2826 100.00 . . . . 0.1774 . . . . . . . . . . . 0.2288 
# 
_struct.entry_id                     8WKD 
_struct.title                        'Connectase T1A C192S mutant from Methanocaldococcus mazei with peptide substrate' 
_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        8WKD 
_struct_keywords.text            'methanogenic archea, proteasome, protein ligation, transpeptidase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A0F8NKN3_METMZ A0A0F8NKN3 ? 1 
;LVIAFIGKNGAVMAGDMREITFEGEKPDREKLEKELYSGSIVTDEEMQKKAEEFGVKITVADCKEKVSERNGVLVGEVSS
AEGGVVKKRRLYASAGNFAIAELINTEMTLTSQGKGSNFIAFGNEFTKQVANKCFKDNWTKKSNLQDAVKILILCMETVA
RKTASVSKQFMIVQTASNADVLKVVEKDRNC
;
3   
2 UNP MTRA_METMA       O59640     ? 2 RELASKDPGAFDADPLVVEI 148 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8WKD A 2 ? 192 ? A0A0F8NKN3 3   ? 193 ? 2 192 
2 2 8WKD C 1 ? 20  ? O59640     148 ? 167 ? 1 20  
# 
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 8WKD ALA A 1   ? UNP A0A0F8NKN3 ?   ?   'expression tag'      1   1 
1 8WKD SER A 192 ? UNP A0A0F8NKN3 CYS 193 'engineered mutation' 192 2 
2 8WKD VAL C 11  ? UNP O59640     PHE 158 'engineered mutation' 11  3 
2 8WKD LYS C 14  ? UNP O59640     ASP 161 'engineered mutation' 14  4 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2360  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  10120 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 26  ? SER A 39  ? GLU A 26  SER A 39  1 ? 14 
HELX_P HELX_P2 AA2 THR A 44  ? GLY A 56  ? THR A 44  GLY A 56  1 ? 13 
HELX_P HELX_P3 AA3 ASN A 125 ? TRP A 140 ? ASN A 125 TRP A 140 1 ? 16 
HELX_P HELX_P4 AA4 ASN A 145 ? THR A 164 ? ASN A 145 THR A 164 1 ? 20 
HELX_P HELX_P5 AA5 ASP A 181 ? ASN A 191 ? ASP A 181 ASN A 191 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? 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 PHE A 171 ? THR A 176 ? PHE A 171 THR A 176 
AA1 2 GLY A 11  ? ASP A 17  ? GLY A 11  ASP A 17  
AA1 3 LEU A 2   ? GLY A 8   ? LEU A 2   GLY A 8   
AA1 4 ASN A 119 ? GLY A 124 ? ASN A 119 GLY A 124 
AA1 5 LEU B 16  ? GLU B 19  ? LEU C 16  GLU C 19  
AA2 1 GLU A 20  ? GLU A 24  ? GLU A 20  GLU A 24  
AA2 2 LYS A 58  ? ALA A 62  ? LYS A 58  ALA A 62  
AA3 1 VAL A 68  ? ARG A 71  ? VAL A 68  ARG A 71  
AA3 2 VAL A 74  ? GLU A 83  ? VAL A 74  GLU A 83  
AA3 3 VAL A 86  ? SER A 95  ? VAL A 86  SER A 95  
AA3 4 ASN A 98  ? ILE A 105 ? ASN A 98  ILE A 105 
AA3 5 GLU A 108 ? LYS A 116 ? GLU A 108 LYS A 116 
# 
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 O MET A 172 ? O MET A 172 N GLY A 16  ? N GLY A 16  
AA1 2 3 O GLY A 11  ? O GLY A 11  N GLY A 8   ? N GLY A 8   
AA1 3 4 N VAL A 3   ? N VAL A 3   O PHE A 123 ? O PHE A 123 
AA1 4 5 N PHE A 120 ? N PHE A 120 O VAL B 18  ? O VAL C 18  
AA2 1 2 N GLU A 20  ? N GLU A 20  O ALA A 62  ? O ALA A 62  
AA3 1 2 N SER A 69  ? N SER A 69  O VAL A 76  ? O VAL A 76  
AA3 2 3 N LEU A 75  ? N LEU A 75  O ALA A 94  ? O ALA A 94  
AA3 3 4 N ARG A 91  ? N ARG A 91  O ALA A 102 ? O ALA A 102 
AA3 4 5 N GLU A 103 ? N GLU A 103 O THR A 110 ? O THR A 110 
# 
_pdbx_entry_details.entry_id                   8WKD 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    SG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    CYS 
_pdbx_validate_symm_contact.auth_seq_id_1     64 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    SG 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    CYS 
_pdbx_validate_symm_contact.auth_seq_id_2     64 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_455 
_pdbx_validate_symm_contact.dist              1.10 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 106 ? ? 57.03 -123.58 
2 1 LYS C 6   ? ? 91.01 152.38  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -15.5054 -0.1440 -7.5529  0.2859 ? -0.0083 ? -0.0413 ? 0.2717 ? -0.0064 ? 0.3250 ? 1.7578 ? 0.0454 
? -0.4768 ? 2.9519 ? -0.8441 ? 0.9274 ? 0.0384  ? 0.0292  ? -0.4171 ? 0.0959  ? -0.1093 ? 0.0259  ? 0.1280  ? 0.0391 ? 0.1028  ? 
2 'X-RAY DIFFRACTION' ? refined -19.2884 14.6217 1.9107   0.2787 ? -0.0073 ? -0.0088 ? 0.2362 ? 0.0010  ? 0.1737 ? 3.3071 ? 0.3140 
? -0.6834 ? 2.4754 ? -0.4153 ? 3.2423 ? 0.1025  ? -0.4546 ? -0.1433 ? 0.1419  ? -0.0798 ? -0.0406 ? 0.3891  ? 0.0710 ? 0.0673  ? 
3 'X-RAY DIFFRACTION' ? refined -12.5223 15.5064 -11.2299 0.2200 ? -0.0160 ? 0.0183  ? 0.2466 ? 0.0432  ? 0.2041 ? 3.1634 ? 0.2426 
? -0.5269 ? 2.8387 ? 0.0593  ? 2.5431 ? 0.0245  ? -0.0222 ? 0.0481  ? -0.1399 ? -0.0019 ? -0.1927 ? -0.2075 ? 0.0674 ? 0.0200  ? 
4 'X-RAY DIFFRACTION' ? refined -17.0305 1.1696  -1.6193  1.6911 ? -0.3695 ? -0.0409 ? 0.8335 ? -0.2271 ? 0.5883 ? 0.3467 ? 
-0.1089 ? -0.0632 ? 0.0659 ? 0.0042  ? 0.0188 ? -0.0088 ? 0.1955  ? 0.0137  ? -0.0199 ? 0.1304  ? -0.0275 ? -0.0990 ? 0.2050 ? 
-0.0365 ? 
5 'X-RAY DIFFRACTION' ? refined -7.3227  15.5587 -1.6742  0.4447 ? -0.1550 ? -0.0118 ? 0.4334 ? -0.0405 ? 0.3650 ? 0.1798 ? 
-0.0263 ? -0.1557 ? 0.2683 ? -0.1649 ? 0.2715 ? -0.1668 ? -0.5384 ? -0.0434 ? 0.3832  ? -0.1614 ? -0.1226 ? -0.1257 ? 0.0065 ? 
-0.0082 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 73 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 74 through 116 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 117 through 192 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 4 through 11 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 12 through 20 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 C ARG 1 ? B ARG 1 
2 1 Y 1 C GLU 2 ? B GLU 2 
3 1 Y 1 C LEU 3 ? B LEU 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HOH O    O N N 137 
HOH H1   H N N 138 
HOH H2   H N N 139 
ILE N    N N N 140 
ILE CA   C N S 141 
ILE C    C N N 142 
ILE O    O N N 143 
ILE CB   C N S 144 
ILE CG1  C N N 145 
ILE CG2  C N N 146 
ILE CD1  C N N 147 
ILE OXT  O N N 148 
ILE H    H N N 149 
ILE H2   H N N 150 
ILE HA   H N N 151 
ILE HB   H N N 152 
ILE HG12 H N N 153 
ILE HG13 H N N 154 
ILE HG21 H N N 155 
ILE HG22 H N N 156 
ILE HG23 H N N 157 
ILE HD11 H N N 158 
ILE HD12 H N N 159 
ILE HD13 H N N 160 
ILE HXT  H N N 161 
LEU N    N N N 162 
LEU CA   C N S 163 
LEU C    C N N 164 
LEU O    O N N 165 
LEU CB   C N N 166 
LEU CG   C N N 167 
LEU CD1  C N N 168 
LEU CD2  C N N 169 
LEU OXT  O N N 170 
LEU H    H N N 171 
LEU H2   H N N 172 
LEU HA   H N N 173 
LEU HB2  H N N 174 
LEU HB3  H N N 175 
LEU HG   H N N 176 
LEU HD11 H N N 177 
LEU HD12 H N N 178 
LEU HD13 H N N 179 
LEU HD21 H N N 180 
LEU HD22 H N N 181 
LEU HD23 H N N 182 
LEU HXT  H N N 183 
LYS N    N N N 184 
LYS CA   C N S 185 
LYS C    C N N 186 
LYS O    O N N 187 
LYS CB   C N N 188 
LYS CG   C N N 189 
LYS CD   C N N 190 
LYS CE   C N N 191 
LYS NZ   N N N 192 
LYS OXT  O N N 193 
LYS H    H N N 194 
LYS H2   H N N 195 
LYS HA   H N N 196 
LYS HB2  H N N 197 
LYS HB3  H N N 198 
LYS HG2  H N N 199 
LYS HG3  H N N 200 
LYS HD2  H N N 201 
LYS HD3  H N N 202 
LYS HE2  H N N 203 
LYS HE3  H N N 204 
LYS HZ1  H N N 205 
LYS HZ2  H N N 206 
LYS HZ3  H N N 207 
LYS HXT  H N N 208 
MET N    N N N 209 
MET CA   C N S 210 
MET C    C N N 211 
MET O    O N N 212 
MET CB   C N N 213 
MET CG   C N N 214 
MET SD   S N N 215 
MET CE   C N N 216 
MET OXT  O N N 217 
MET H    H N N 218 
MET H2   H N N 219 
MET HA   H N N 220 
MET HB2  H N N 221 
MET HB3  H N N 222 
MET HG2  H N N 223 
MET HG3  H N N 224 
MET HE1  H N N 225 
MET HE2  H N N 226 
MET HE3  H N N 227 
MET HXT  H N N 228 
PHE N    N N N 229 
PHE CA   C N S 230 
PHE C    C N N 231 
PHE O    O N N 232 
PHE CB   C N N 233 
PHE CG   C Y N 234 
PHE CD1  C Y N 235 
PHE CD2  C Y N 236 
PHE CE1  C Y N 237 
PHE CE2  C Y N 238 
PHE CZ   C Y N 239 
PHE OXT  O N N 240 
PHE H    H N N 241 
PHE H2   H N N 242 
PHE HA   H N N 243 
PHE HB2  H N N 244 
PHE HB3  H N N 245 
PHE HD1  H N N 246 
PHE HD2  H N N 247 
PHE HE1  H N N 248 
PHE HE2  H N N 249 
PHE HZ   H N N 250 
PHE HXT  H N N 251 
PRO N    N N N 252 
PRO CA   C N S 253 
PRO C    C N N 254 
PRO O    O N N 255 
PRO CB   C N N 256 
PRO CG   C N N 257 
PRO CD   C N N 258 
PRO OXT  O N N 259 
PRO H    H N N 260 
PRO HA   H N N 261 
PRO HB2  H N N 262 
PRO HB3  H N N 263 
PRO HG2  H N N 264 
PRO HG3  H N N 265 
PRO HD2  H N N 266 
PRO HD3  H N N 267 
PRO HXT  H N N 268 
SER N    N N N 269 
SER CA   C N S 270 
SER C    C N N 271 
SER O    O N N 272 
SER CB   C N N 273 
SER OG   O N N 274 
SER OXT  O N N 275 
SER H    H N N 276 
SER H2   H N N 277 
SER HA   H N N 278 
SER HB2  H N N 279 
SER HB3  H N N 280 
SER HG   H N N 281 
SER HXT  H N N 282 
THR N    N N N 283 
THR CA   C N S 284 
THR C    C N N 285 
THR O    O N N 286 
THR CB   C N R 287 
THR OG1  O N N 288 
THR CG2  C N N 289 
THR OXT  O N N 290 
THR H    H N N 291 
THR H2   H N N 292 
THR HA   H N N 293 
THR HB   H N N 294 
THR HG1  H N N 295 
THR HG21 H N N 296 
THR HG22 H N N 297 
THR HG23 H N N 298 
THR HXT  H N N 299 
TRP N    N N N 300 
TRP CA   C N S 301 
TRP C    C N N 302 
TRP O    O N N 303 
TRP CB   C N N 304 
TRP CG   C Y N 305 
TRP CD1  C Y N 306 
TRP CD2  C Y N 307 
TRP NE1  N Y N 308 
TRP CE2  C Y N 309 
TRP CE3  C Y N 310 
TRP CZ2  C Y N 311 
TRP CZ3  C Y N 312 
TRP CH2  C Y N 313 
TRP OXT  O N N 314 
TRP H    H N N 315 
TRP H2   H N N 316 
TRP HA   H N N 317 
TRP HB2  H N N 318 
TRP HB3  H N N 319 
TRP HD1  H N N 320 
TRP HE1  H N N 321 
TRP HE3  H N N 322 
TRP HZ2  H N N 323 
TRP HZ3  H N N 324 
TRP HH2  H N N 325 
TRP HXT  H N N 326 
TYR N    N N N 327 
TYR CA   C N S 328 
TYR C    C N N 329 
TYR O    O N N 330 
TYR CB   C N N 331 
TYR CG   C Y N 332 
TYR CD1  C Y N 333 
TYR CD2  C Y N 334 
TYR CE1  C Y N 335 
TYR CE2  C Y N 336 
TYR CZ   C Y N 337 
TYR OH   O N N 338 
TYR OXT  O N N 339 
TYR H    H N N 340 
TYR H2   H N N 341 
TYR HA   H N N 342 
TYR HB2  H N N 343 
TYR HB3  H N N 344 
TYR HD1  H N N 345 
TYR HD2  H N N 346 
TYR HE1  H N N 347 
TYR HE2  H N N 348 
TYR HH   H N N 349 
TYR HXT  H N N 350 
VAL N    N N N 351 
VAL CA   C N S 352 
VAL C    C N N 353 
VAL O    O N N 354 
VAL CB   C N N 355 
VAL CG1  C N N 356 
VAL CG2  C N N 357 
VAL OXT  O N N 358 
VAL H    H N N 359 
VAL H2   H N N 360 
VAL HA   H N N 361 
VAL HB   H N N 362 
VAL HG11 H N N 363 
VAL HG12 H N N 364 
VAL HG13 H N N 365 
VAL HG21 H N N 366 
VAL HG22 H N N 367 
VAL HG23 H N N 368 
VAL HXT  H N N 369 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HOH O   H1   sing N N 129 
HOH O   H2   sing N N 130 
ILE N   CA   sing N N 131 
ILE N   H    sing N N 132 
ILE N   H2   sing N N 133 
ILE CA  C    sing N N 134 
ILE CA  CB   sing N N 135 
ILE CA  HA   sing N N 136 
ILE C   O    doub N N 137 
ILE C   OXT  sing N N 138 
ILE CB  CG1  sing N N 139 
ILE CB  CG2  sing N N 140 
ILE CB  HB   sing N N 141 
ILE CG1 CD1  sing N N 142 
ILE CG1 HG12 sing N N 143 
ILE CG1 HG13 sing N N 144 
ILE CG2 HG21 sing N N 145 
ILE CG2 HG22 sing N N 146 
ILE CG2 HG23 sing N N 147 
ILE CD1 HD11 sing N N 148 
ILE CD1 HD12 sing N N 149 
ILE CD1 HD13 sing N N 150 
ILE OXT HXT  sing N N 151 
LEU N   CA   sing N N 152 
LEU N   H    sing N N 153 
LEU N   H2   sing N N 154 
LEU CA  C    sing N N 155 
LEU CA  CB   sing N N 156 
LEU CA  HA   sing N N 157 
LEU C   O    doub N N 158 
LEU C   OXT  sing N N 159 
LEU CB  CG   sing N N 160 
LEU CB  HB2  sing N N 161 
LEU CB  HB3  sing N N 162 
LEU CG  CD1  sing N N 163 
LEU CG  CD2  sing N N 164 
LEU CG  HG   sing N N 165 
LEU CD1 HD11 sing N N 166 
LEU CD1 HD12 sing N N 167 
LEU CD1 HD13 sing N N 168 
LEU CD2 HD21 sing N N 169 
LEU CD2 HD22 sing N N 170 
LEU CD2 HD23 sing N N 171 
LEU OXT HXT  sing N N 172 
LYS N   CA   sing N N 173 
LYS N   H    sing N N 174 
LYS N   H2   sing N N 175 
LYS CA  C    sing N N 176 
LYS CA  CB   sing N N 177 
LYS CA  HA   sing N N 178 
LYS C   O    doub N N 179 
LYS C   OXT  sing N N 180 
LYS CB  CG   sing N N 181 
LYS CB  HB2  sing N N 182 
LYS CB  HB3  sing N N 183 
LYS CG  CD   sing N N 184 
LYS CG  HG2  sing N N 185 
LYS CG  HG3  sing N N 186 
LYS CD  CE   sing N N 187 
LYS CD  HD2  sing N N 188 
LYS CD  HD3  sing N N 189 
LYS CE  NZ   sing N N 190 
LYS CE  HE2  sing N N 191 
LYS CE  HE3  sing N N 192 
LYS NZ  HZ1  sing N N 193 
LYS NZ  HZ2  sing N N 194 
LYS NZ  HZ3  sing N N 195 
LYS OXT HXT  sing N N 196 
MET N   CA   sing N N 197 
MET N   H    sing N N 198 
MET N   H2   sing N N 199 
MET CA  C    sing N N 200 
MET CA  CB   sing N N 201 
MET CA  HA   sing N N 202 
MET C   O    doub N N 203 
MET C   OXT  sing N N 204 
MET CB  CG   sing N N 205 
MET CB  HB2  sing N N 206 
MET CB  HB3  sing N N 207 
MET CG  SD   sing N N 208 
MET CG  HG2  sing N N 209 
MET CG  HG3  sing N N 210 
MET SD  CE   sing N N 211 
MET CE  HE1  sing N N 212 
MET CE  HE2  sing N N 213 
MET CE  HE3  sing N N 214 
MET OXT HXT  sing N N 215 
PHE N   CA   sing N N 216 
PHE N   H    sing N N 217 
PHE N   H2   sing N N 218 
PHE CA  C    sing N N 219 
PHE CA  CB   sing N N 220 
PHE CA  HA   sing N N 221 
PHE C   O    doub N N 222 
PHE C   OXT  sing N N 223 
PHE CB  CG   sing N N 224 
PHE CB  HB2  sing N N 225 
PHE CB  HB3  sing N N 226 
PHE CG  CD1  doub Y N 227 
PHE CG  CD2  sing Y N 228 
PHE CD1 CE1  sing Y N 229 
PHE CD1 HD1  sing N N 230 
PHE CD2 CE2  doub Y N 231 
PHE CD2 HD2  sing N N 232 
PHE CE1 CZ   doub Y N 233 
PHE CE1 HE1  sing N N 234 
PHE CE2 CZ   sing Y N 235 
PHE CE2 HE2  sing N N 236 
PHE CZ  HZ   sing N N 237 
PHE OXT HXT  sing N N 238 
PRO N   CA   sing N N 239 
PRO N   CD   sing N N 240 
PRO N   H    sing N N 241 
PRO CA  C    sing N N 242 
PRO CA  CB   sing N N 243 
PRO CA  HA   sing N N 244 
PRO C   O    doub N N 245 
PRO C   OXT  sing N N 246 
PRO CB  CG   sing N N 247 
PRO CB  HB2  sing N N 248 
PRO CB  HB3  sing N N 249 
PRO CG  CD   sing N N 250 
PRO CG  HG2  sing N N 251 
PRO CG  HG3  sing N N 252 
PRO CD  HD2  sing N N 253 
PRO CD  HD3  sing N N 254 
PRO OXT HXT  sing N N 255 
SER N   CA   sing N N 256 
SER N   H    sing N N 257 
SER N   H2   sing N N 258 
SER CA  C    sing N N 259 
SER CA  CB   sing N N 260 
SER CA  HA   sing N N 261 
SER C   O    doub N N 262 
SER C   OXT  sing N N 263 
SER CB  OG   sing N N 264 
SER CB  HB2  sing N N 265 
SER CB  HB3  sing N N 266 
SER OG  HG   sing N N 267 
SER OXT HXT  sing N N 268 
THR N   CA   sing N N 269 
THR N   H    sing N N 270 
THR N   H2   sing N N 271 
THR CA  C    sing N N 272 
THR CA  CB   sing N N 273 
THR CA  HA   sing N N 274 
THR C   O    doub N N 275 
THR C   OXT  sing N N 276 
THR CB  OG1  sing N N 277 
THR CB  CG2  sing N N 278 
THR CB  HB   sing N N 279 
THR OG1 HG1  sing N N 280 
THR CG2 HG21 sing N N 281 
THR CG2 HG22 sing N N 282 
THR CG2 HG23 sing N N 283 
THR OXT HXT  sing N N 284 
TRP N   CA   sing N N 285 
TRP N   H    sing N N 286 
TRP N   H2   sing N N 287 
TRP CA  C    sing N N 288 
TRP CA  CB   sing N N 289 
TRP CA  HA   sing N N 290 
TRP C   O    doub N N 291 
TRP C   OXT  sing N N 292 
TRP CB  CG   sing N N 293 
TRP CB  HB2  sing N N 294 
TRP CB  HB3  sing N N 295 
TRP CG  CD1  doub Y N 296 
TRP CG  CD2  sing Y N 297 
TRP CD1 NE1  sing Y N 298 
TRP CD1 HD1  sing N N 299 
TRP CD2 CE2  doub Y N 300 
TRP CD2 CE3  sing Y N 301 
TRP NE1 CE2  sing Y N 302 
TRP NE1 HE1  sing N N 303 
TRP CE2 CZ2  sing Y N 304 
TRP CE3 CZ3  doub Y N 305 
TRP CE3 HE3  sing N N 306 
TRP CZ2 CH2  doub Y N 307 
TRP CZ2 HZ2  sing N N 308 
TRP CZ3 CH2  sing Y N 309 
TRP CZ3 HZ3  sing N N 310 
TRP CH2 HH2  sing N N 311 
TRP OXT HXT  sing N N 312 
TYR N   CA   sing N N 313 
TYR N   H    sing N N 314 
TYR N   H2   sing N N 315 
TYR CA  C    sing N N 316 
TYR CA  CB   sing N N 317 
TYR CA  HA   sing N N 318 
TYR C   O    doub N N 319 
TYR C   OXT  sing N N 320 
TYR CB  CG   sing N N 321 
TYR CB  HB2  sing N N 322 
TYR CB  HB3  sing N N 323 
TYR CG  CD1  doub Y N 324 
TYR CG  CD2  sing Y N 325 
TYR CD1 CE1  sing Y N 326 
TYR CD1 HD1  sing N N 327 
TYR CD2 CE2  doub Y N 328 
TYR CD2 HD2  sing N N 329 
TYR CE1 CZ   doub Y N 330 
TYR CE1 HE1  sing N N 331 
TYR CE2 CZ   sing Y N 332 
TYR CE2 HE2  sing N N 333 
TYR CZ  OH   sing N N 334 
TYR OH  HH   sing N N 335 
TYR OXT HXT  sing N N 336 
VAL N   CA   sing N N 337 
VAL N   H    sing N N 338 
VAL N   H2   sing N N 339 
VAL CA  C    sing N N 340 
VAL CA  CB   sing N N 341 
VAL CA  HA   sing N N 342 
VAL C   O    doub N N 343 
VAL C   OXT  sing N N 344 
VAL CB  CG1  sing N N 345 
VAL CB  CG2  sing N N 346 
VAL CB  HB   sing N N 347 
VAL CG1 HG11 sing N N 348 
VAL CG1 HG12 sing N N 349 
VAL CG1 HG13 sing N N 350 
VAL CG2 HG21 sing N N 351 
VAL CG2 HG22 sing N N 352 
VAL CG2 HG23 sing N N 353 
VAL OXT HXT  sing N N 354 
# 
_pdbx_audit_support.funding_organization   'Ministry of Education (MoE, Singapore)' 
_pdbx_audit_support.country                Singapore 
_pdbx_audit_support.grant_number           MOE2018-T1-002-010 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8WKD 
_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]   0.018484 
_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]   0.009904 
_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]   0.030675 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? -13.690 2.945   -7.156  1.00 65.32  ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? -14.563 4.114   -7.404  1.00 62.99  ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? -13.733 5.387   -7.600  1.00 44.93  ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? -12.588 5.466   -7.134  1.00 40.42  ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? -15.538 4.310   -6.249  1.00 84.06  ? 1   ALA A CB  1 
ATOM   6    N N   . LEU A 1 2   ? -14.307 6.375   -8.302  1.00 39.02  ? 2   LEU A N   1 
ATOM   7    C CA  . LEU A 1 2   ? -13.598 7.600   -8.580  1.00 33.95  ? 2   LEU A CA  1 
ATOM   8    C C   . LEU A 1 2   ? -14.514 8.756   -8.926  1.00 31.28  ? 2   LEU A C   1 
ATOM   9    O O   . LEU A 1 2   ? -15.333 8.660   -9.844  1.00 23.15  ? 2   LEU A O   1 
ATOM   10   C CB  . LEU A 1 2   ? -12.626 7.375   -9.734  1.00 33.65  ? 2   LEU A CB  1 
ATOM   11   C CG  . LEU A 1 2   ? -11.807 8.603   -10.137 1.00 31.94  ? 2   LEU A CG  1 
ATOM   12   C CD1 . LEU A 1 2   ? -10.662 8.821   -9.191  1.00 31.39  ? 2   LEU A CD1 1 
ATOM   13   C CD2 . LEU A 1 2   ? -11.248 8.421   -11.514 1.00 31.84  ? 2   LEU A CD2 1 
ATOM   14   N N   . VAL A 1 3   ? -14.402 9.840   -8.152  1.00 26.63  ? 3   VAL A N   1 
ATOM   15   C CA  . VAL A 1 3   ? -15.059 11.100  -8.439  1.00 26.12  ? 3   VAL A CA  1 
ATOM   16   C C   . VAL A 1 3   ? -13.936 12.110  -8.512  1.00 28.49  ? 3   VAL A C   1 
ATOM   17   O O   . VAL A 1 3   ? -13.097 12.160  -7.614  1.00 20.50  ? 3   VAL A O   1 
ATOM   18   C CB  . VAL A 1 3   ? -16.155 11.570  -7.456  1.00 24.55  ? 3   VAL A CB  1 
ATOM   19   C CG1 . VAL A 1 3   ? -16.642 12.989  -7.835  1.00 25.11  ? 3   VAL A CG1 1 
ATOM   20   C CG2 . VAL A 1 3   ? -17.330 10.601  -7.449  1.00 24.49  ? 3   VAL A CG2 1 
ATOM   21   N N   . ILE A 1 4   ? -13.876 12.885  -9.594  1.00 22.80  ? 4   ILE A N   1 
ATOM   22   C CA  . ILE A 1 4   ? -12.883 13.935  -9.738  1.00 23.36  ? 4   ILE A CA  1 
ATOM   23   C C   . ILE A 1 4   ? -13.557 15.245  -10.165 1.00 27.13  ? 4   ILE A C   1 
ATOM   24   O O   . ILE A 1 4   ? -14.637 15.241  -10.784 1.00 22.21  ? 4   ILE A O   1 
ATOM   25   C CB  . ILE A 1 4   ? -11.729 13.524  -10.682 1.00 28.25  ? 4   ILE A CB  1 
ATOM   26   C CG1 . ILE A 1 4   ? -12.218 13.452  -12.135 1.00 27.15  ? 4   ILE A CG1 1 
ATOM   27   C CG2 . ILE A 1 4   ? -11.117 12.173  -10.233 1.00 24.32  ? 4   ILE A CG2 1 
ATOM   28   C CD1 . ILE A 1 4   ? -11.134 12.864  -13.105 1.00 27.49  ? 4   ILE A CD1 1 
ATOM   29   N N   . ALA A 1 5   ? -12.955 16.359  -9.781  1.00 24.63  ? 5   ALA A N   1 
ATOM   30   C CA  . ALA A 1 5   ? -13.493 17.667  -10.096 1.00 26.60  ? 5   ALA A CA  1 
ATOM   31   C C   . ALA A 1 5   ? -12.420 18.680  -10.314 1.00 26.53  ? 5   ALA A C   1 
ATOM   32   O O   . ALA A 1 5   ? -11.340 18.599  -9.732  1.00 26.06  ? 5   ALA A O   1 
ATOM   33   C CB  . ALA A 1 5   ? -14.444 18.156  -9.011  1.00 22.80  ? 5   ALA A CB  1 
ATOM   34   N N   . PHE A 1 6   ? -12.718 19.641  -11.165 1.00 25.31  ? 6   PHE A N   1 
ATOM   35   C CA  . PHE A 1 6   ? -11.849 20.773  -11.374 1.00 27.70  ? 6   PHE A CA  1 
ATOM   36   C C   . PHE A 1 6   ? -12.671 22.006  -11.006 1.00 28.04  ? 6   PHE A C   1 
ATOM   37   O O   . PHE A 1 6   ? -13.790 22.190  -11.490 1.00 24.84  ? 6   PHE A O   1 
ATOM   38   C CB  . PHE A 1 6   ? -11.333 20.874  -12.818 1.00 26.95  ? 6   PHE A CB  1 
ATOM   39   C CG  . PHE A 1 6   ? -10.740 22.240  -13.095 1.00 31.17  ? 6   PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 6   ? -9.521  22.607  -12.548 1.00 29.42  ? 6   PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 6   ? -11.476 23.212  -13.765 1.00 30.97  ? 6   PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 6   ? -9.010  23.881  -12.749 1.00 36.38  ? 6   PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 6   ? -10.956 24.485  -13.976 1.00 33.16  ? 6   PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 6   ? -9.731  24.818  -13.457 1.00 34.74  ? 6   PHE A CZ  1 
ATOM   45   N N   . ILE A 1 7   ? -12.117 22.847  -10.160 1.00 26.22  ? 7   ILE A N   1 
ATOM   46   C CA  . ILE A 1 7   ? -12.766 24.087  -9.782  1.00 28.77  ? 7   ILE A CA  1 
ATOM   47   C C   . ILE A 1 7   ? -11.930 25.201  -10.327 1.00 33.82  ? 7   ILE A C   1 
ATOM   48   O O   . ILE A 1 7   ? -10.724 25.254  -10.103 1.00 30.57  ? 7   ILE A O   1 
ATOM   49   C CB  . ILE A 1 7   ? -13.007 24.175  -8.261  1.00 32.64  ? 7   ILE A CB  1 
ATOM   50   C CG1 . ILE A 1 7   ? -13.961 23.041  -7.797  1.00 28.61  ? 7   ILE A CG1 1 
ATOM   51   C CG2 . ILE A 1 7   ? -13.570 25.526  -7.888  1.00 31.22  ? 7   ILE A CG2 1 
ATOM   52   C CD1 . ILE A 1 7   ? -13.278 21.847  -7.233  1.00 27.57  ? 7   ILE A CD1 1 
ATOM   53   N N   . GLY A 1 8   ? -12.553 26.035  -11.123 1.00 31.90  ? 8   GLY A N   1 
ATOM   54   C CA  . GLY A 1 8   ? -11.876 27.190  -11.691 1.00 36.86  ? 8   GLY A CA  1 
ATOM   55   C C   . GLY A 1 8   ? -12.547 28.478  -11.293 1.00 37.51  ? 8   GLY A C   1 
ATOM   56   O O   . GLY A 1 8   ? -13.611 28.468  -10.667 1.00 35.19  ? 8   GLY A O   1 
ATOM   57   N N   . LYS A 1 9   ? -11.994 29.590  -11.751 1.00 39.48  ? 9   LYS A N   1 
ATOM   58   C CA  . LYS A 1 9   ? -12.553 30.919  -11.486 1.00 41.92  ? 9   LYS A CA  1 
ATOM   59   C C   . LYS A 1 9   ? -13.919 31.108  -12.169 1.00 37.86  ? 9   LYS A C   1 
ATOM   60   O O   . LYS A 1 9   ? -14.756 31.844  -11.655 1.00 35.62  ? 9   LYS A O   1 
ATOM   61   C CB  . LYS A 1 9   ? -11.588 32.013  -11.982 1.00 44.20  ? 9   LYS A CB  1 
ATOM   62   C CG  . LYS A 1 9   ? -10.260 32.103  -11.213 1.00 53.41  ? 9   LYS A CG  1 
ATOM   63   C CD  . LYS A 1 9   ? -9.318  33.183  -11.749 1.00 58.34  ? 9   LYS A CD  1 
ATOM   64   C CE  . LYS A 1 9   ? -8.039  33.246  -10.945 1.00 64.99  ? 9   LYS A CE  1 
ATOM   65   N NZ  . LYS A 1 9   ? -7.112  34.284  -11.483 1.00 63.87  ? 9   LYS A NZ  1 
ATOM   66   N N   . ASN A 1 10  ? -14.147 30.456  -13.328 1.00 38.00  ? 10  ASN A N   1 
ATOM   67   C CA  . ASN A 1 10  ? -15.407 30.643  -14.057 1.00 38.45  ? 10  ASN A CA  1 
ATOM   68   C C   . ASN A 1 10  ? -16.393 29.491  -14.008 1.00 36.96  ? 10  ASN A C   1 
ATOM   69   O O   . ASN A 1 10  ? -17.415 29.544  -14.695 1.00 37.25  ? 10  ASN A O   1 
ATOM   70   C CB  . ASN A 1 10  ? -15.140 31.015  -15.504 1.00 41.30  ? 10  ASN A CB  1 
ATOM   71   C CG  . ASN A 1 10  ? -14.302 32.270  -15.646 1.00 45.13  ? 10  ASN A CG  1 
ATOM   72   O OD1 . ASN A 1 10  ? -13.414 32.355  -16.510 1.00 46.34  ? 10  ASN A OD1 1 
ATOM   73   N ND2 . ASN A 1 10  ? -14.537 33.250  -14.785 1.00 44.95  ? 10  ASN A ND2 1 
ATOM   74   N N   . GLY A 1 11  ? -16.080 28.450  -13.256 1.00 35.05  ? 11  GLY A N   1 
ATOM   75   C CA  . GLY A 1 11  ? -16.967 27.310  -13.154 1.00 33.86  ? 11  GLY A CA  1 
ATOM   76   C C   . GLY A 1 11  ? -16.307 26.083  -12.588 1.00 32.56  ? 11  GLY A C   1 
ATOM   77   O O   . GLY A 1 11  ? -15.186 26.147  -12.086 1.00 34.77  ? 11  GLY A O   1 
ATOM   78   N N   . ALA A 1 12  ? -17.009 24.974  -12.640 1.00 26.72  ? 12  ALA A N   1 
ATOM   79   C CA  . ALA A 1 12  ? -16.497 23.727  -12.105 1.00 26.94  ? 12  ALA A CA  1 
ATOM   80   C C   . ALA A 1 12  ? -16.976 22.553  -12.952 1.00 30.73  ? 12  ALA A C   1 
ATOM   81   O O   . ALA A 1 12  ? -18.107 22.551  -13.449 1.00 24.91  ? 12  ALA A O   1 
ATOM   82   C CB  . ALA A 1 12  ? -16.936 23.554  -10.646 1.00 26.99  ? 12  ALA A CB  1 
ATOM   83   N N   . VAL A 1 13  ? -16.121 21.534  -13.063 1.00 25.83  ? 13  VAL A N   1 
ATOM   84   C CA  . VAL A 1 13  ? -16.466 20.347  -13.796 1.00 26.79  ? 13  VAL A CA  1 
ATOM   85   C C   . VAL A 1 13  ? -16.266 19.135  -12.882 1.00 23.25  ? 13  VAL A C   1 
ATOM   86   O O   . VAL A 1 13  ? -15.391 19.142  -12.017 1.00 27.35  ? 13  VAL A O   1 
ATOM   87   C CB  . VAL A 1 13  ? -15.733 20.271  -15.165 1.00 23.88  ? 13  VAL A CB  1 
ATOM   88   C CG1 . VAL A 1 13  ? -14.227 20.382  -14.988 1.00 31.04  ? 13  VAL A CG1 1 
ATOM   89   C CG2 . VAL A 1 13  ? -16.098 18.986  -15.908 1.00 28.65  ? 13  VAL A CG2 1 
ATOM   90   N N   . MET A 1 14  ? -17.145 18.160  -12.990 1.00 20.87  ? 14  MET A N   1 
ATOM   91   C CA  . MET A 1 14  ? -17.083 16.997  -12.123 1.00 25.81  ? 14  MET A CA  1 
ATOM   92   C C   . MET A 1 14  ? -17.421 15.701  -12.899 1.00 24.47  ? 14  MET A C   1 
ATOM   93   O O   . MET A 1 14  ? -18.410 15.658  -13.626 1.00 20.81  ? 14  MET A O   1 
ATOM   94   C CB  . MET A 1 14  ? -18.006 17.225  -10.926 1.00 21.47  ? 14  MET A CB  1 
ATOM   95   C CG  . MET A 1 14  ? -17.930 16.141  -9.893  1.00 26.82  ? 14  MET A CG  1 
ATOM   96   S SD  . MET A 1 14  ? -19.173 16.363  -8.587  1.00 26.36  ? 14  MET A SD  1 
ATOM   97   C CE  . MET A 1 14  ? -18.483 17.670  -7.657  1.00 26.83  ? 14  MET A CE  1 
ATOM   98   N N   . ALA A 1 15  ? -16.596 14.674  -12.742 1.00 24.09  ? 15  ALA A N   1 
ATOM   99   C CA  . ALA A 1 15  ? -16.795 13.401  -13.390 1.00 26.37  ? 15  ALA A CA  1 
ATOM   100  C C   . ALA A 1 15  ? -16.807 12.263  -12.373 1.00 28.84  ? 15  ALA A C   1 
ATOM   101  O O   . ALA A 1 15  ? -16.133 12.344  -11.345 1.00 21.68  ? 15  ALA A O   1 
ATOM   102  C CB  . ALA A 1 15  ? -15.716 13.166  -14.427 1.00 23.98  ? 15  ALA A CB  1 
ATOM   103  N N   . GLY A 1 16  ? -17.633 11.258  -12.618 1.00 23.05  ? 16  GLY A N   1 
ATOM   104  C CA  . GLY A 1 16  ? -17.723 10.116  -11.726 1.00 22.30  ? 16  GLY A CA  1 
ATOM   105  C C   . GLY A 1 16  ? -17.944 8.843   -12.494 1.00 27.48  ? 16  GLY A C   1 
ATOM   106  O O   . GLY A 1 16  ? -18.617 8.864   -13.532 1.00 21.15  ? 16  GLY A O   1 
ATOM   107  N N   . ASP A 1 17  ? -17.358 7.726   -12.031 1.00 27.48  ? 17  ASP A N   1 
ATOM   108  C CA  . ASP A 1 17  ? -17.606 6.439   -12.691 1.00 28.94  ? 17  ASP A CA  1 
ATOM   109  C C   . ASP A 1 17  ? -19.004 5.913   -12.228 1.00 27.96  ? 17  ASP A C   1 
ATOM   110  O O   . ASP A 1 17  ? -19.666 6.541   -11.395 1.00 25.78  ? 17  ASP A O   1 
ATOM   111  C CB  . ASP A 1 17  ? -16.475 5.419   -12.443 1.00 30.65  ? 17  ASP A CB  1 
ATOM   112  C CG  . ASP A 1 17  ? -16.639 4.627   -11.154 1.00 36.16  ? 17  ASP A CG  1 
ATOM   113  O OD1 . ASP A 1 17  ? -16.690 5.256   -10.074 1.00 34.88  ? 17  ASP A OD1 1 
ATOM   114  O OD2 . ASP A 1 17  ? -16.676 3.389   -11.224 1.00 33.22  ? 17  ASP A OD2 1 
ATOM   115  N N   . MET A 1 18  ? -19.444 4.789   -12.771 1.00 27.01  ? 18  MET A N   1 
ATOM   116  C CA  . MET A 1 18  ? -20.770 4.278   -12.446 1.00 31.81  ? 18  MET A CA  1 
ATOM   117  C C   . MET A 1 18  ? -20.779 2.895   -11.789 1.00 35.72  ? 18  MET A C   1 
ATOM   118  O O   . MET A 1 18  ? -21.851 2.344   -11.564 1.00 32.73  ? 18  MET A O   1 
ATOM   119  C CB  . MET A 1 18  ? -21.607 4.325   -13.710 1.00 30.83  ? 18  MET A CB  1 
ATOM   120  C CG  . MET A 1 18  ? -21.615 5.729   -14.304 1.00 34.34  ? 18  MET A CG  1 
ATOM   121  S SD  . MET A 1 18  ? -22.506 5.893   -15.835 1.00 41.37  ? 18  MET A SD  1 
ATOM   122  C CE  . MET A 1 18  ? -24.163 6.100   -15.179 1.00 40.97  ? 18  MET A CE  1 
ATOM   123  N N   . ARG A 1 19  ? -19.594 2.370   -11.422 1.00 35.93  ? 19  ARG A N   1 
ATOM   124  C CA  . ARG A 1 19  ? -19.462 1.046   -10.845 1.00 43.87  ? 19  ARG A CA  1 
ATOM   125  C C   . ARG A 1 19  ? -19.817 0.946   -9.350  1.00 45.42  ? 19  ARG A C   1 
ATOM   126  O O   . ARG A 1 19  ? -19.392 1.751   -8.533  1.00 45.61  ? 19  ARG A O   1 
ATOM   127  C CB  . ARG A 1 19  ? -18.058 0.490   -11.097 1.00 39.25  ? 19  ARG A CB  1 
ATOM   128  C CG  . ARG A 1 19  ? -17.909 -0.962  -10.682 1.00 40.69  ? 19  ARG A CG  1 
ATOM   129  C CD  . ARG A 1 19  ? -16.768 -1.586  -11.450 1.00 39.66  ? 19  ARG A CD  1 
ATOM   130  N NE  . ARG A 1 19  ? -17.231 -2.017  -12.764 1.00 38.47  ? 19  ARG A NE  1 
ATOM   131  C CZ  . ARG A 1 19  ? -16.600 -2.899  -13.531 1.00 41.79  ? 19  ARG A CZ  1 
ATOM   132  N NH1 . ARG A 1 19  ? -15.438 -3.420  -13.145 1.00 38.65  ? 19  ARG A NH1 1 
ATOM   133  N NH2 . ARG A 1 19  ? -17.127 -3.274  -14.686 1.00 40.52  ? 19  ARG A NH2 1 
ATOM   134  N N   . GLU A 1 20  ? -20.611 -0.047  -9.026  1.00 40.46  ? 20  GLU A N   1 
ATOM   135  C CA  . GLU A 1 20  ? -21.015 -0.387  -7.689  1.00 46.65  ? 20  GLU A CA  1 
ATOM   136  C C   . GLU A 1 20  ? -20.731 -1.882  -7.534  1.00 48.83  ? 20  GLU A C   1 
ATOM   137  O O   . GLU A 1 20  ? -21.132 -2.686  -8.383  1.00 40.03  ? 20  GLU A O   1 
ATOM   138  C CB  . GLU A 1 20  ? -22.493 -0.078  -7.488  1.00 43.84  ? 20  GLU A CB  1 
ATOM   139  C CG  . GLU A 1 20  ? -23.056 -0.839  -6.309  1.00 54.02  ? 20  GLU A CG  1 
ATOM   140  C CD  . GLU A 1 20  ? -24.567 -0.788  -6.192  1.00 56.49  ? 20  GLU A CD  1 
ATOM   141  O OE1 . GLU A 1 20  ? -25.100 0.315   -5.920  1.00 59.39  ? 20  GLU A OE1 1 
ATOM   142  O OE2 . GLU A 1 20  ? -25.216 -1.847  -6.367  1.00 52.83  ? 20  GLU A OE2 1 
ATOM   143  N N   . ILE A 1 21  ? -19.946 -2.252  -6.515  1.00 57.99  ? 21  ILE A N   1 
ATOM   144  C CA  . ILE A 1 21  ? -19.565 -3.641  -6.307  1.00 53.22  ? 21  ILE A CA  1 
ATOM   145  C C   . ILE A 1 21  ? -20.069 -4.139  -4.997  1.00 52.83  ? 21  ILE A C   1 
ATOM   146  O O   . ILE A 1 21  ? -19.846 -3.484  -3.982  1.00 63.07  ? 21  ILE A O   1 
ATOM   147  C CB  . ILE A 1 21  ? -18.030 -3.836  -6.381  1.00 55.16  ? 21  ILE A CB  1 
ATOM   148  C CG1 . ILE A 1 21  ? -17.454 -3.278  -7.697  1.00 57.99  ? 21  ILE A CG1 1 
ATOM   149  C CG2 . ILE A 1 21  ? -17.678 -5.322  -6.204  1.00 51.76  ? 21  ILE A CG2 1 
ATOM   150  C CD1 . ILE A 1 21  ? -16.147 -3.918  -8.149  1.00 54.08  ? 21  ILE A CD1 1 
ATOM   151  N N   . THR A 1 22  ? -20.751 -5.277  -5.000  1.00 44.21  ? 22  THR A N   1 
ATOM   152  C CA  . THR A 1 22  ? -21.170 -5.893  -3.749  1.00 50.01  ? 22  THR A CA  1 
ATOM   153  C C   . THR A 1 22  ? -20.400 -7.191  -3.572  1.00 47.46  ? 22  THR A C   1 
ATOM   154  O O   . THR A 1 22  ? -20.166 -7.922  -4.539  1.00 41.93  ? 22  THR A O   1 
ATOM   155  C CB  . THR A 1 22  ? -22.689 -6.090  -3.611  1.00 48.36  ? 22  THR A CB  1 
ATOM   156  O OG1 . THR A 1 22  ? -23.200 -6.908  -4.660  1.00 48.81  ? 22  THR A OG1 1 
ATOM   157  C CG2 . THR A 1 22  ? -23.458 -4.795  -3.499  1.00 46.66  ? 22  THR A CG2 1 
ATOM   158  N N   . PHE A 1 23  ? -20.022 -7.478  -2.330  1.00 50.04  ? 23  PHE A N   1 
ATOM   159  C CA  . PHE A 1 23  ? -19.289 -8.690  -2.006  1.00 44.66  ? 23  PHE A CA  1 
ATOM   160  C C   . PHE A 1 23  ? -20.117 -9.517  -1.042  1.00 48.50  ? 23  PHE A C   1 
ATOM   161  O O   . PHE A 1 23  ? -20.871 -8.972  -0.225  1.00 48.47  ? 23  PHE A O   1 
ATOM   162  C CB  . PHE A 1 23  ? -17.916 -8.373  -1.387  1.00 43.53  ? 23  PHE A CB  1 
ATOM   163  C CG  . PHE A 1 23  ? -17.032 -7.381  -2.115  1.00 47.39  ? 23  PHE A CG  1 
ATOM   164  C CD1 . PHE A 1 23  ? -17.222 -6.014  -1.966  1.00 52.78  ? 23  PHE A CD1 1 
ATOM   165  C CD2 . PHE A 1 23  ? -15.940 -7.811  -2.851  1.00 48.00  ? 23  PHE A CD2 1 
ATOM   166  C CE1 . PHE A 1 23  ? -16.385 -5.100  -2.612  1.00 52.75  ? 23  PHE A CE1 1 
ATOM   167  C CE2 . PHE A 1 23  ? -15.085 -6.895  -3.470  1.00 45.43  ? 23  PHE A CE2 1 
ATOM   168  C CZ  . PHE A 1 23  ? -15.308 -5.547  -3.336  1.00 49.87  ? 23  PHE A CZ  1 
ATOM   169  N N   . GLU A 1 24  ? -20.008 -10.844 -1.159  1.00 43.44  ? 24  GLU A N   1 
ATOM   170  C CA  . GLU A 1 24  ? -20.714 -11.738 -0.253  1.00 45.69  ? 24  GLU A CA  1 
ATOM   171  C C   . GLU A 1 24  ? -19.791 -12.924 0.021   1.00 45.99  ? 24  GLU A C   1 
ATOM   172  O O   . GLU A 1 24  ? -19.227 -13.494 -0.909  1.00 43.02  ? 24  GLU A O   1 
ATOM   173  C CB  . GLU A 1 24  ? -22.051 -12.193 -0.854  1.00 50.61  ? 24  GLU A CB  1 
ATOM   174  C CG  . GLU A 1 24  ? -22.812 -11.090 -1.580  1.00 56.34  ? 24  GLU A CG  1 
ATOM   175  C CD  . GLU A 1 24  ? -24.325 -11.240 -1.592  1.00 60.60  ? 24  GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 24  ? -25.030 -10.227 -1.373  1.00 62.92  ? 24  GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 24  ? -24.801 -12.379 -1.812  1.00 63.80  ? 24  GLU A OE2 1 
ATOM   178  N N   . GLY A 1 25  ? -19.618 -13.249 1.290   1.00 46.52  ? 25  GLY A N   1 
ATOM   179  C CA  . GLY A 1 25  ? -18.755 -14.339 1.729   1.00 50.28  ? 25  GLY A CA  1 
ATOM   180  C C   . GLY A 1 25  ? -18.058 -14.033 3.038   1.00 51.24  ? 25  GLY A C   1 
ATOM   181  O O   . GLY A 1 25  ? -18.266 -12.969 3.620   1.00 52.68  ? 25  GLY A O   1 
ATOM   182  N N   . GLU A 1 26  ? -17.225 -14.962 3.519   1.00 47.19  ? 26  GLU A N   1 
ATOM   183  C CA  . GLU A 1 26  ? -16.504 -14.770 4.767   1.00 49.96  ? 26  GLU A CA  1 
ATOM   184  C C   . GLU A 1 26  ? -15.663 -13.494 4.755   1.00 48.18  ? 26  GLU A C   1 
ATOM   185  O O   . GLU A 1 26  ? -15.099 -13.140 3.731   1.00 43.56  ? 26  GLU A O   1 
ATOM   186  C CB  . GLU A 1 26  ? -15.648 -16.004 5.089   1.00 50.66  ? 26  GLU A CB  1 
ATOM   187  C CG  . GLU A 1 26  ? -16.403 -17.323 4.998   1.00 48.00  ? 26  GLU A CG  1 
ATOM   188  C CD  . GLU A 1 26  ? -17.841 -17.299 5.481   1.00 57.68  ? 26  GLU A CD  1 
ATOM   189  O OE1 . GLU A 1 26  ? -18.047 -17.292 6.716   1.00 62.32  ? 26  GLU A OE1 1 
ATOM   190  O OE2 . GLU A 1 26  ? -18.759 -17.303 4.631   1.00 65.81  ? 26  GLU A OE2 1 
ATOM   191  N N   . LYS A 1 27  ? -15.593 -12.804 5.906   1.00 51.32  ? 27  LYS A N   1 
ATOM   192  C CA  . LYS A 1 27  ? -14.856 -11.551 6.086   1.00 49.28  ? 27  LYS A CA  1 
ATOM   193  C C   . LYS A 1 27  ? -13.348 -11.625 5.719   1.00 45.99  ? 27  LYS A C   1 
ATOM   194  O O   . LYS A 1 27  ? -12.892 -10.725 5.010   1.00 45.99  ? 27  LYS A O   1 
ATOM   195  C CB  . LYS A 1 27  ? -15.055 -10.988 7.509   1.00 53.00  ? 27  LYS A CB  1 
ATOM   196  C CG  . LYS A 1 27  ? -14.525 -9.568  7.693   1.00 59.26  ? 27  LYS A CG  1 
ATOM   197  C CD  . LYS A 1 27  ? -15.302 -8.778  8.750   1.00 59.55  ? 27  LYS A CD  1 
ATOM   198  C CE  . LYS A 1 27  ? -14.444 -7.686  9.366   1.00 70.26  ? 27  LYS A CE  1 
ATOM   199  N NZ  . LYS A 1 27  ? -13.029 -8.122  9.537   1.00 69.69  ? 27  LYS A NZ  1 
ATOM   200  N N   . PRO A 1 28  ? -12.556 -12.643 6.143   1.00 48.08  ? 28  PRO A N   1 
ATOM   201  C CA  . PRO A 1 28  ? -11.137 -12.672 5.733   1.00 49.26  ? 28  PRO A CA  1 
ATOM   202  C C   . PRO A 1 28  ? -10.972 -12.783 4.223   1.00 49.13  ? 28  PRO A C   1 
ATOM   203  O O   . PRO A 1 28  ? -10.017 -12.244 3.675   1.00 45.91  ? 28  PRO A O   1 
ATOM   204  C CB  . PRO A 1 28  ? -10.583 -13.932 6.416   1.00 51.63  ? 28  PRO A CB  1 
ATOM   205  C CG  . PRO A 1 28  ? -11.568 -14.292 7.458   1.00 52.51  ? 28  PRO A CG  1 
ATOM   206  C CD  . PRO A 1 28  ? -12.899 -13.830 6.950   1.00 52.15  ? 28  PRO A CD  1 
ATOM   207  N N   . ASP A 1 29  ? -11.898 -13.489 3.556   1.00 46.90  ? 29  ASP A N   1 
ATOM   208  C CA  . ASP A 1 29  ? -11.891 -13.705 2.119   1.00 49.27  ? 29  ASP A CA  1 
ATOM   209  C C   . ASP A 1 29  ? -12.238 -12.411 1.365   1.00 44.91  ? 29  ASP A C   1 
ATOM   210  O O   . ASP A 1 29  ? -11.515 -12.029 0.442   1.00 44.68  ? 29  ASP A O   1 
ATOM   211  C CB  . ASP A 1 29  ? -12.871 -14.830 1.771   1.00 46.53  ? 29  ASP A CB  1 
ATOM   212  C CG  . ASP A 1 29  ? -12.494 -16.138 2.435   1.00 49.99  ? 29  ASP A CG  1 
ATOM   213  O OD1 . ASP A 1 29  ? -11.306 -16.517 2.360   1.00 49.97  ? 29  ASP A OD1 1 
ATOM   214  O OD2 . ASP A 1 29  ? -13.385 -16.785 3.013   1.00 47.65  ? 29  ASP A OD2 1 
ATOM   215  N N   . ARG A 1 30  ? -13.308 -11.718 1.800   1.00 44.49  ? 30  ARG A N   1 
ATOM   216  C CA  . ARG A 1 30  ? -13.719 -10.451 1.205   1.00 43.40  ? 30  ARG A CA  1 
ATOM   217  C C   . ARG A 1 30  ? -12.604 -9.420  1.349   1.00 46.62  ? 30  ARG A C   1 
ATOM   218  O O   . ARG A 1 30  ? -12.255 -8.774  0.366   1.00 44.59  ? 30  ARG A O   1 
ATOM   219  C CB  . ARG A 1 30  ? -15.023 -9.938  1.821   1.00 45.04  ? 30  ARG A CB  1 
ATOM   220  C CG  . ARG A 1 30  ? -16.259 -10.727 1.414   1.00 43.76  ? 30  ARG A CG  1 
ATOM   221  C CD  . ARG A 1 30  ? -17.573 -10.171 1.959   1.00 50.91  ? 30  ARG A CD  1 
ATOM   222  N NE  . ARG A 1 30  ? -17.888 -10.652 3.309   1.00 51.80  ? 30  ARG A NE  1 
ATOM   223  C CZ  . ARG A 1 30  ? -17.767 -9.928  4.412   1.00 53.60  ? 30  ARG A CZ  1 
ATOM   224  N NH1 . ARG A 1 30  ? -17.283 -8.694  4.356   1.00 48.19  ? 30  ARG A NH1 1 
ATOM   225  N NH2 . ARG A 1 30  ? -18.103 -10.439 5.587   1.00 54.81  ? 30  ARG A NH2 1 
ATOM   226  N N   . GLU A 1 31  ? -11.985 -9.340  2.543   1.00 46.74  ? 31  GLU A N   1 
ATOM   227  C CA  . GLU A 1 31  ? -10.857 -8.449  2.819   1.00 47.94  ? 31  GLU A CA  1 
ATOM   228  C C   . GLU A 1 31  ? -9.645  -8.715  1.915   1.00 48.52  ? 31  GLU A C   1 
ATOM   229  O O   . GLU A 1 31  ? -8.961  -7.767  1.528   1.00 47.92  ? 31  GLU A O   1 
ATOM   230  C CB  . GLU A 1 31  ? -10.441 -8.524  4.298   1.00 46.41  ? 31  GLU A CB  1 
ATOM   231  C CG  . GLU A 1 31  ? -11.484 -7.955  5.235   1.00 52.84  ? 31  GLU A CG  1 
ATOM   232  C CD  . GLU A 1 31  ? -10.976 -7.643  6.631   1.00 61.95  ? 31  GLU A CD  1 
ATOM   233  O OE1 . GLU A 1 31  ? -10.339 -8.530  7.246   1.00 56.87  ? 31  GLU A OE1 1 
ATOM   234  O OE2 . GLU A 1 31  ? -11.227 -6.513  7.112   1.00 64.83  ? 31  GLU A OE2 1 
ATOM   235  N N   . LYS A 1 32  ? -9.369  -9.988  1.594   1.00 46.82  ? 32  LYS A N   1 
ATOM   236  C CA  . LYS A 1 32  ? -8.259  -10.343 0.717   1.00 48.40  ? 32  LYS A CA  1 
ATOM   237  C C   . LYS A 1 32  ? -8.545  -9.888  -0.730  1.00 50.23  ? 32  LYS A C   1 
ATOM   238  O O   . LYS A 1 32  ? -7.652  -9.369  -1.409  1.00 53.66  ? 32  LYS A O   1 
ATOM   239  C CB  . LYS A 1 32  ? -8.006  -11.860 0.754   1.00 52.38  ? 32  LYS A CB  1 
ATOM   240  C CG  . LYS A 1 32  ? -6.949  -12.314 -0.245  1.00 57.15  ? 32  LYS A CG  1 
ATOM   241  C CD  . LYS A 1 32  ? -6.485  -13.745 0.001   1.00 64.91  ? 32  LYS A CD  1 
ATOM   242  C CE  . LYS A 1 32  ? -7.435  -14.547 0.863   1.00 66.62  ? 32  LYS A CE  1 
ATOM   243  N NZ  . LYS A 1 32  ? -7.042  -15.986 0.916   1.00 73.39  ? 32  LYS A NZ  1 
ATOM   244  N N   . LEU A 1 33  ? -9.784  -10.091 -1.203  1.00 50.35  ? 33  LEU A N   1 
ATOM   245  C CA  . LEU A 1 33  ? -10.157 -9.671  -2.549  1.00 48.26  ? 33  LEU A CA  1 
ATOM   246  C C   . LEU A 1 33  ? -10.124 -8.141  -2.654  1.00 48.94  ? 33  LEU A C   1 
ATOM   247  O O   . LEU A 1 33  ? -9.517  -7.615  -3.578  1.00 50.90  ? 33  LEU A O   1 
ATOM   248  C CB  . LEU A 1 33  ? -11.537 -10.212 -2.938  1.00 42.57  ? 33  LEU A CB  1 
ATOM   249  C CG  . LEU A 1 33  ? -12.032 -9.797  -4.309  1.00 42.96  ? 33  LEU A CG  1 
ATOM   250  C CD1 . LEU A 1 33  ? -11.112 -10.317 -5.409  1.00 45.84  ? 33  LEU A CD1 1 
ATOM   251  C CD2 . LEU A 1 33  ? -13.440 -10.283 -4.535  1.00 42.68  ? 33  LEU A CD2 1 
ATOM   252  N N   . GLU A 1 34  ? -10.714 -7.439  -1.682  1.00 46.53  ? 34  GLU A N   1 
ATOM   253  C CA  . GLU A 1 34  ? -10.727 -5.977  -1.633  1.00 50.94  ? 34  GLU A CA  1 
ATOM   254  C C   . GLU A 1 34  ? -9.324  -5.401  -1.779  1.00 53.58  ? 34  GLU A C   1 
ATOM   255  O O   . GLU A 1 34  ? -9.110  -4.549  -2.630  1.00 55.89  ? 34  GLU A O   1 
ATOM   256  C CB  . GLU A 1 34  ? -11.315 -5.480  -0.312  1.00 55.30  ? 34  GLU A CB  1 
ATOM   257  C CG  . GLU A 1 34  ? -12.782 -5.140  -0.373  1.00 59.22  ? 34  GLU A CG  1 
ATOM   258  C CD  . GLU A 1 34  ? -13.230 -4.463  0.905   1.00 66.38  ? 34  GLU A CD  1 
ATOM   259  O OE1 . GLU A 1 34  ? -13.085 -3.222  1.004   1.00 68.68  ? 34  GLU A OE1 1 
ATOM   260  O OE2 . GLU A 1 34  ? -13.734 -5.175  1.805   1.00 65.74  ? 34  GLU A OE2 1 
ATOM   261  N N   . LYS A 1 35  ? -8.370  -5.887  -0.973  1.00 53.31  ? 35  LYS A N   1 
ATOM   262  C CA  . LYS A 1 35  ? -6.989  -5.438  -1.035  1.00 52.57  ? 35  LYS A CA  1 
ATOM   263  C C   . LYS A 1 35  ? -6.439  -5.577  -2.462  1.00 54.45  ? 35  LYS A C   1 
ATOM   264  O O   . LYS A 1 35  ? -5.859  -4.628  -2.974  1.00 56.12  ? 35  LYS A O   1 
ATOM   265  C CB  . LYS A 1 35  ? -6.138  -6.214  -0.009  1.00 51.98  ? 35  LYS A CB  1 
ATOM   266  C CG  . LYS A 1 35  ? -4.637  -6.019  -0.150  1.00 54.35  ? 35  LYS A CG  1 
ATOM   267  C CD  . LYS A 1 35  ? -4.069  -6.764  -1.368  1.00 58.52  ? 35  LYS A CD  1 
ATOM   268  C CE  . LYS A 1 35  ? -2.555  -6.773  -1.369  1.00 59.77  ? 35  LYS A CE  1 
ATOM   269  N NZ  . LYS A 1 35  ? -1.992  -5.562  -2.026  1.00 61.62  ? 35  LYS A NZ  1 
ATOM   270  N N   . GLU A 1 36  ? -6.652  -6.724  -3.118  1.00 53.78  ? 36  GLU A N   1 
ATOM   271  C CA  . GLU A 1 36  ? -6.166  -6.930  -4.486  1.00 56.06  ? 36  GLU A CA  1 
ATOM   272  C C   . GLU A 1 36  ? -6.848  -5.996  -5.498  1.00 55.67  ? 36  GLU A C   1 
ATOM   273  O O   . GLU A 1 36  ? -6.221  -5.570  -6.464  1.00 53.14  ? 36  GLU A O   1 
ATOM   274  C CB  . GLU A 1 36  ? -6.387  -8.384  -4.924  1.00 56.27  ? 36  GLU A CB  1 
ATOM   275  C CG  . GLU A 1 36  ? -5.359  -9.365  -4.394  1.00 57.60  ? 36  GLU A CG  1 
ATOM   276  C CD  . GLU A 1 36  ? -4.322  -9.745  -5.430  1.00 63.69  ? 36  GLU A CD  1 
ATOM   277  O OE1 . GLU A 1 36  ? -3.758  -8.827  -6.069  1.00 63.45  ? 36  GLU A OE1 1 
ATOM   278  O OE2 . GLU A 1 36  ? -4.065  -10.959 -5.600  1.00 60.54  ? 36  GLU A OE2 1 
ATOM   279  N N   . LEU A 1 37  ? -8.140  -5.715  -5.298  1.00 53.26  ? 37  LEU A N   1 
ATOM   280  C CA  . LEU A 1 37  ? -8.900  -4.878  -6.216  1.00 55.42  ? 37  LEU A CA  1 
ATOM   281  C C   . LEU A 1 37  ? -8.565  -3.396  -6.069  1.00 53.95  ? 37  LEU A C   1 
ATOM   282  O O   . LEU A 1 37  ? -8.403  -2.715  -7.074  1.00 53.54  ? 37  LEU A O   1 
ATOM   283  C CB  . LEU A 1 37  ? -10.410 -5.122  -6.017  1.00 56.02  ? 37  LEU A CB  1 
ATOM   284  C CG  . LEU A 1 37  ? -11.460 -4.305  -6.823  1.00 53.68  ? 37  LEU A CG  1 
ATOM   285  C CD1 . LEU A 1 37  ? -11.344 -4.560  -8.281  1.00 52.78  ? 37  LEU A CD1 1 
ATOM   286  C CD2 . LEU A 1 37  ? -12.901 -4.476  -6.345  1.00 45.66  ? 37  LEU A CD2 1 
ATOM   287  N N   . TYR A 1 38  ? -8.426  -2.905  -4.840  1.00 55.99  ? 38  TYR A N   1 
ATOM   288  C CA  . TYR A 1 38  ? -8.127  -1.492  -4.607  1.00 55.94  ? 38  TYR A CA  1 
ATOM   289  C C   . TYR A 1 38  ? -6.626  -1.144  -4.726  1.00 55.38  ? 38  TYR A C   1 
ATOM   290  O O   . TYR A 1 38  ? -6.239  0.014   -4.538  1.00 53.76  ? 38  TYR A O   1 
ATOM   291  C CB  . TYR A 1 38  ? -8.714  -1.023  -3.265  1.00 61.27  ? 38  TYR A CB  1 
ATOM   292  C CG  . TYR A 1 38  ? -10.209 -1.249  -3.155  1.00 68.04  ? 38  TYR A CG  1 
ATOM   293  C CD1 . TYR A 1 38  ? -11.007 -1.324  -4.288  1.00 69.82  ? 38  TYR A CD1 1 
ATOM   294  C CD2 . TYR A 1 38  ? -10.827 -1.367  -1.920  1.00 78.93  ? 38  TYR A CD2 1 
ATOM   295  C CE1 . TYR A 1 38  ? -12.381 -1.525  -4.194  1.00 86.13  ? 38  TYR A CE1 1 
ATOM   296  C CE2 . TYR A 1 38  ? -12.194 -1.603  -1.814  1.00 86.90  ? 38  TYR A CE2 1 
ATOM   297  C CZ  . TYR A 1 38  ? -12.971 -1.673  -2.954  1.00 94.91  ? 38  TYR A CZ  1 
ATOM   298  O OH  . TYR A 1 38  ? -14.329 -1.892  -2.859  1.00 104.20 ? 38  TYR A OH  1 
ATOM   299  N N   . SER A 1 39  ? -5.789  -2.131  -5.080  1.00 53.81  ? 39  SER A N   1 
ATOM   300  C CA  . SER A 1 39  ? -4.358  -1.893  -5.252  1.00 54.81  ? 39  SER A CA  1 
ATOM   301  C C   . SER A 1 39  ? -3.927  -1.730  -6.728  1.00 52.19  ? 39  SER A C   1 
ATOM   302  O O   . SER A 1 39  ? -2.748  -1.475  -6.990  1.00 54.59  ? 39  SER A O   1 
ATOM   303  C CB  . SER A 1 39  ? -3.555  -3.022  -4.612  1.00 57.69  ? 39  SER A CB  1 
ATOM   304  O OG  . SER A 1 39  ? -3.549  -4.189  -5.422  1.00 56.95  ? 39  SER A OG  1 
ATOM   305  N N   . GLY A 1 40  ? -4.853  -1.899  -7.670  1.00 54.27  ? 40  GLY A N   1 
ATOM   306  C CA  . GLY A 1 40  ? -4.525  -1.861  -9.091  1.00 51.95  ? 40  GLY A CA  1 
ATOM   307  C C   . GLY A 1 40  ? -4.104  -3.216  -9.650  1.00 53.61  ? 40  GLY A C   1 
ATOM   308  O O   . GLY A 1 40  ? -3.794  -3.327  -10.837 1.00 50.12  ? 40  GLY A O   1 
ATOM   309  N N   . SER A 1 41  ? -4.094  -4.268  -8.801  1.00 62.84  ? 41  SER A N   1 
ATOM   310  C CA  . SER A 1 41  ? -3.703  -5.634  -9.185  1.00 63.95  ? 41  SER A CA  1 
ATOM   311  C C   . SER A 1 41  ? -4.675  -6.221  -10.201 1.00 62.49  ? 41  SER A C   1 
ATOM   312  O O   . SER A 1 41  ? -4.253  -6.864  -11.165 1.00 60.73  ? 41  SER A O   1 
ATOM   313  C CB  . SER A 1 41  ? -3.655  -6.548  -7.959  1.00 62.42  ? 41  SER A CB  1 
ATOM   314  O OG  . SER A 1 41  ? -2.834  -6.026  -6.927  1.00 66.44  ? 41  SER A OG  1 
ATOM   315  N N   . ILE A 1 42  ? -5.980  -6.030  -9.967  1.00 51.87  ? 42  ILE A N   1 
ATOM   316  C CA  . ILE A 1 42  ? -6.994  -6.553  -10.870 1.00 46.54  ? 42  ILE A CA  1 
ATOM   317  C C   . ILE A 1 42  ? -7.347  -5.483  -11.900 1.00 49.80  ? 42  ILE A C   1 
ATOM   318  O O   . ILE A 1 42  ? -7.985  -4.488  -11.562 1.00 47.45  ? 42  ILE A O   1 
ATOM   319  C CB  . ILE A 1 42  ? -8.215  -7.023  -10.064 1.00 43.94  ? 42  ILE A CB  1 
ATOM   320  C CG1 . ILE A 1 42  ? -7.847  -8.205  -9.140  1.00 51.46  ? 42  ILE A CG1 1 
ATOM   321  C CG2 . ILE A 1 42  ? -9.349  -7.385  -10.977 1.00 44.85  ? 42  ILE A CG2 1 
ATOM   322  C CD1 . ILE A 1 42  ? -8.696  -8.284  -7.829  1.00 49.15  ? 42  ILE A CD1 1 
ATOM   323  N N   . VAL A 1 43  ? -6.920  -5.684  -13.145 1.00 45.85  ? 43  VAL A N   1 
ATOM   324  C CA  . VAL A 1 43  ? -7.128  -4.736  -14.240 1.00 45.59  ? 43  VAL A CA  1 
ATOM   325  C C   . VAL A 1 43  ? -8.434  -4.942  -15.013 1.00 43.89  ? 43  VAL A C   1 
ATOM   326  O O   . VAL A 1 43  ? -9.109  -3.969  -15.330 1.00 48.47  ? 43  VAL A O   1 
ATOM   327  C CB  . VAL A 1 43  ? -5.921  -4.779  -15.202 1.00 47.90  ? 43  VAL A CB  1 
ATOM   328  C CG1 . VAL A 1 43  ? -6.208  -4.014  -16.487 1.00 43.28  ? 43  VAL A CG1 1 
ATOM   329  C CG2 . VAL A 1 43  ? -4.666  -4.251  -14.523 1.00 45.99  ? 43  VAL A CG2 1 
ATOM   330  N N   . THR A 1 44  ? -8.780  -6.184  -15.342 1.00 45.67  ? 44  THR A N   1 
ATOM   331  C CA  . THR A 1 44  ? -9.969  -6.454  -16.152 1.00 47.85  ? 44  THR A CA  1 
ATOM   332  C C   . THR A 1 44  ? -11.130 -7.052  -15.336 1.00 48.39  ? 44  THR A C   1 
ATOM   333  O O   . THR A 1 44  ? -10.919 -7.547  -14.225 1.00 47.15  ? 44  THR A O   1 
ATOM   334  C CB  . THR A 1 44  ? -9.618  -7.321  -17.392 1.00 50.12  ? 44  THR A CB  1 
ATOM   335  O OG1 . THR A 1 44  ? -9.043  -8.566  -16.996 1.00 50.54  ? 44  THR A OG1 1 
ATOM   336  C CG2 . THR A 1 44  ? -8.709  -6.607  -18.406 1.00 49.20  ? 44  THR A CG2 1 
ATOM   337  N N   . ASP A 1 45  ? -12.349 -7.007  -15.894 1.00 45.09  ? 45  ASP A N   1 
ATOM   338  C CA  . ASP A 1 45  ? -13.512 -7.628  -15.261 1.00 48.64  ? 45  ASP A CA  1 
ATOM   339  C C   . ASP A 1 45  ? -13.388 -9.161  -15.294 1.00 47.56  ? 45  ASP A C   1 
ATOM   340  O O   . ASP A 1 45  ? -13.938 -9.846  -14.426 1.00 45.51  ? 45  ASP A O   1 
ATOM   341  C CB  . ASP A 1 45  ? -14.818 -7.177  -15.930 1.00 49.88  ? 45  ASP A CB  1 
ATOM   342  C CG  . ASP A 1 45  ? -15.121 -5.699  -15.757 1.00 54.59  ? 45  ASP A CG  1 
ATOM   343  O OD1 . ASP A 1 45  ? -14.452 -5.044  -14.912 1.00 49.12  ? 45  ASP A OD1 1 
ATOM   344  O OD2 . ASP A 1 45  ? -16.015 -5.189  -16.472 1.00 54.93  ? 45  ASP A OD2 1 
ATOM   345  N N   . GLU A 1 46  ? -12.627 -9.687  -16.264 1.00 48.41  ? 46  GLU A N   1 
ATOM   346  C CA  . GLU A 1 46  ? -12.322 -11.105 -16.406 1.00 47.85  ? 46  GLU A CA  1 
ATOM   347  C C   . GLU A 1 46  ? -11.446 -11.553 -15.222 1.00 46.60  ? 46  GLU A C   1 
ATOM   348  O O   . GLU A 1 46  ? -11.795 -12.525 -14.550 1.00 49.49  ? 46  GLU A O   1 
ATOM   349  C CB  . GLU A 1 46  ? -11.598 -11.354 -17.749 1.00 49.18  ? 46  GLU A CB  1 
ATOM   350  C CG  . GLU A 1 46  ? -12.520 -11.449 -18.956 1.00 50.13  ? 46  GLU A CG  1 
ATOM   351  C CD  . GLU A 1 46  ? -13.213 -10.167 -19.381 1.00 55.56  ? 46  GLU A CD  1 
ATOM   352  O OE1 . GLU A 1 46  ? -12.698 -9.072  -19.054 1.00 54.45  ? 46  GLU A OE1 1 
ATOM   353  O OE2 . GLU A 1 46  ? -14.276 -10.259 -20.037 1.00 58.67  ? 46  GLU A OE2 1 
ATOM   354  N N   . GLU A 1 47  ? -10.346 -10.825 -14.931 1.00 45.50  ? 47  GLU A N   1 
ATOM   355  C CA  . GLU A 1 47  ? -9.457  -11.138 -13.809 1.00 45.89  ? 47  GLU A CA  1 
ATOM   356  C C   . GLU A 1 47  ? -10.142 -10.980 -12.462 1.00 46.29  ? 47  GLU A C   1 
ATOM   357  O O   . GLU A 1 47  ? -9.749  -11.629 -11.502 1.00 47.31  ? 47  GLU A O   1 
ATOM   358  C CB  . GLU A 1 47  ? -8.192  -10.264 -13.844 1.00 48.52  ? 47  GLU A CB  1 
ATOM   359  C CG  . GLU A 1 47  ? -7.348  -10.504 -15.087 1.00 51.58  ? 47  GLU A CG  1 
ATOM   360  C CD  . GLU A 1 47  ? -6.548  -9.311  -15.575 1.00 55.28  ? 47  GLU A CD  1 
ATOM   361  O OE1 . GLU A 1 47  ? -7.075  -8.176  -15.543 1.00 51.57  ? 47  GLU A OE1 1 
ATOM   362  O OE2 . GLU A 1 47  ? -5.383  -9.517  -15.986 1.00 60.13  ? 47  GLU A OE2 1 
ATOM   363  N N   . MET A 1 48  ? -11.154 -10.111 -12.377 1.00 45.94  ? 48  MET A N   1 
ATOM   364  C CA  . MET A 1 48  ? -11.899 -9.898  -11.149 1.00 45.71  ? 48  MET A CA  1 
ATOM   365  C C   . MET A 1 48  ? -12.736 -11.132 -10.817 1.00 45.49  ? 48  MET A C   1 
ATOM   366  O O   . MET A 1 48  ? -12.739 -11.580 -9.673  1.00 43.63  ? 48  MET A O   1 
ATOM   367  C CB  . MET A 1 48  ? -12.799 -8.665  -11.309 1.00 43.15  ? 48  MET A CB  1 
ATOM   368  C CG  . MET A 1 48  ? -13.955 -8.637  -10.360 1.00 42.76  ? 48  MET A CG  1 
ATOM   369  S SD  . MET A 1 48  ? -14.559 -6.975  -9.972  1.00 51.52  ? 48  MET A SD  1 
ATOM   370  C CE  . MET A 1 48  ? -15.347 -6.522  -11.509 1.00 45.48  ? 48  MET A CE  1 
ATOM   371  N N   . GLN A 1 49  ? -13.413 -11.684 -11.814 1.00 45.63  ? 49  GLN A N   1 
ATOM   372  C CA  . GLN A 1 49  ? -14.254 -12.879 -11.568 1.00 45.20  ? 49  GLN A CA  1 
ATOM   373  C C   . GLN A 1 49  ? -13.358 -14.081 -11.257 1.00 48.13  ? 49  GLN A C   1 
ATOM   374  O O   . GLN A 1 49  ? -13.719 -14.837 -10.354 1.00 48.82  ? 49  GLN A O   1 
ATOM   375  C CB  . GLN A 1 49  ? -15.236 -13.101 -12.711 1.00 39.10  ? 49  GLN A CB  1 
ATOM   376  C CG  . GLN A 1 49  ? -16.154 -11.915 -12.948 1.00 47.07  ? 49  GLN A CG  1 
ATOM   377  C CD  . GLN A 1 49  ? -17.392 -11.952 -12.088 1.00 51.25  ? 49  GLN A CD  1 
ATOM   378  O OE1 . GLN A 1 49  ? -17.516 -12.756 -11.168 1.00 53.47  ? 49  GLN A OE1 1 
ATOM   379  N NE2 . GLN A 1 49  ? -18.331 -11.073 -12.393 1.00 48.75  ? 49  GLN A NE2 1 
ATOM   380  N N   . LYS A 1 50  ? -12.222 -14.211 -11.947 1.00 46.18  ? 50  LYS A N   1 
ATOM   381  C CA  . LYS A 1 50  ? -11.314 -15.312 -11.646 1.00 47.72  ? 50  LYS A CA  1 
ATOM   382  C C   . LYS A 1 50  ? -10.776 -15.200 -10.207 1.00 47.51  ? 50  LYS A C   1 
ATOM   383  O O   . LYS A 1 50  ? -10.695 -16.213 -9.515  1.00 46.03  ? 50  LYS A O   1 
ATOM   384  C CB  . LYS A 1 50  ? -10.188 -15.402 -12.686 1.00 49.14  ? 50  LYS A CB  1 
ATOM   385  C CG  . LYS A 1 50  ? -10.583 -16.218 -13.921 1.00 55.22  ? 50  LYS A CG  1 
ATOM   386  C CD  . LYS A 1 50  ? -9.739  -15.918 -15.187 1.00 54.85  ? 50  LYS A CD  1 
ATOM   387  C CE  . LYS A 1 50  ? -8.280  -16.278 -15.051 1.00 61.23  ? 50  LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 50  ? -7.570  -15.417 -14.055 1.00 63.32  ? 50  LYS A NZ  1 
ATOM   389  N N   . LYS A 1 51  ? -10.492 -13.970 -9.726  1.00 45.96  ? 51  LYS A N   1 
ATOM   390  C CA  . LYS A 1 51  ? -10.012 -13.795 -8.354  1.00 48.84  ? 51  LYS A CA  1 
ATOM   391  C C   . LYS A 1 51  ? -11.102 -14.061 -7.316  1.00 49.45  ? 51  LYS A C   1 
ATOM   392  O O   . LYS A 1 51  ? -10.820 -14.677 -6.294  1.00 48.16  ? 51  LYS A O   1 
ATOM   393  C CB  . LYS A 1 51  ? -9.366  -12.421 -8.143  1.00 46.59  ? 51  LYS A CB  1 
ATOM   394  C CG  . LYS A 1 51  ? -7.988  -12.305 -8.761  1.00 46.16  ? 51  LYS A CG  1 
ATOM   395  C CD  . LYS A 1 51  ? -6.992  -13.159 -7.995  1.00 53.42  ? 51  LYS A CD  1 
ATOM   396  C CE  . LYS A 1 51  ? -5.576  -12.647 -8.115  1.00 56.55  ? 51  LYS A CE  1 
ATOM   397  N NZ  . LYS A 1 51  ? -4.575  -13.696 -7.753  1.00 61.13  ? 51  LYS A NZ  1 
ATOM   398  N N   . ALA A 1 52  ? -12.345 -13.616 -7.580  1.00 47.16  ? 52  ALA A N   1 
ATOM   399  C CA  . ALA A 1 52  ? -13.466 -13.853 -6.668  1.00 46.63  ? 52  ALA A CA  1 
ATOM   400  C C   . ALA A 1 52  ? -13.678 -15.360 -6.491  1.00 50.39  ? 52  ALA A C   1 
ATOM   401  O O   . ALA A 1 52  ? -13.927 -15.813 -5.374  1.00 48.73  ? 52  ALA A O   1 
ATOM   402  C CB  . ALA A 1 52  ? -14.737 -13.215 -7.213  1.00 45.86  ? 52  ALA A CB  1 
ATOM   403  N N   . GLU A 1 53  ? -13.589 -16.128 -7.591  1.00 46.08  ? 53  GLU A N   1 
ATOM   404  C CA  . GLU A 1 53  ? -13.735 -17.584 -7.583  1.00 55.39  ? 53  GLU A CA  1 
ATOM   405  C C   . GLU A 1 53  ? -12.639 -18.173 -6.680  1.00 52.85  ? 53  GLU A C   1 
ATOM   406  O O   . GLU A 1 53  ? -12.944 -18.873 -5.713  1.00 55.47  ? 53  GLU A O   1 
ATOM   407  C CB  . GLU A 1 53  ? -13.596 -18.124 -9.025  1.00 58.45  ? 53  GLU A CB  1 
ATOM   408  C CG  . GLU A 1 53  ? -14.132 -19.527 -9.248  1.00 63.21  ? 53  GLU A CG  1 
ATOM   409  C CD  . GLU A 1 53  ? -14.830 -19.689 -10.587 1.00 65.43  ? 53  GLU A CD  1 
ATOM   410  O OE1 . GLU A 1 53  ? -14.275 -20.386 -11.469 1.00 59.92  ? 53  GLU A OE1 1 
ATOM   411  O OE2 . GLU A 1 53  ? -15.931 -19.114 -10.758 1.00 70.71  ? 53  GLU A OE2 1 
ATOM   412  N N   . GLU A 1 54  ? -11.380 -17.782 -6.937  1.00 53.02  ? 54  GLU A N   1 
ATOM   413  C CA  . GLU A 1 54  ? -10.203 -18.199 -6.192  1.00 53.15  ? 54  GLU A CA  1 
ATOM   414  C C   . GLU A 1 54  ? -10.384 -18.000 -4.700  1.00 55.11  ? 54  GLU A C   1 
ATOM   415  O O   . GLU A 1 54  ? -10.148 -18.930 -3.930  1.00 54.87  ? 54  GLU A O   1 
ATOM   416  C CB  . GLU A 1 54  ? -8.985  -17.414 -6.692  1.00 57.26  ? 54  GLU A CB  1 
ATOM   417  C CG  . GLU A 1 54  ? -7.683  -18.192 -6.700  1.00 64.83  ? 54  GLU A CG  1 
ATOM   418  C CD  . GLU A 1 54  ? -6.533  -17.394 -7.279  1.00 68.39  ? 54  GLU A CD  1 
ATOM   419  O OE1 . GLU A 1 54  ? -6.682  -16.866 -8.405  1.00 65.83  ? 54  GLU A OE1 1 
ATOM   420  O OE2 . GLU A 1 54  ? -5.476  -17.305 -6.608  1.00 71.21  ? 54  GLU A OE2 1 
ATOM   421  N N   . PHE A 1 55  ? -10.823 -16.804 -4.279  1.00 52.09  ? 55  PHE A N   1 
ATOM   422  C CA  . PHE A 1 55  ? -11.006 -16.535 -2.856  1.00 53.18  ? 55  PHE A CA  1 
ATOM   423  C C   . PHE A 1 55  ? -12.380 -16.968 -2.297  1.00 51.10  ? 55  PHE A C   1 
ATOM   424  O O   . PHE A 1 55  ? -12.641 -16.765 -1.108  1.00 51.13  ? 55  PHE A O   1 
ATOM   425  C CB  . PHE A 1 55  ? -10.716 -15.061 -2.512  1.00 52.05  ? 55  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 55  ? -9.370  -14.540 -2.967  1.00 57.50  ? 55  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 55  ? -8.210  -15.258 -2.729  1.00 59.42  ? 55  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 55  ? -9.267  -13.327 -3.630  1.00 53.22  ? 55  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 55  ? -6.975  -14.781 -3.164  1.00 64.58  ? 55  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 55  ? -8.032  -12.850 -4.058  1.00 55.15  ? 55  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 55  ? -6.892  -13.572 -3.809  1.00 61.19  ? 55  PHE A CZ  1 
ATOM   432  N N   . GLY A 1 56  ? -13.224 -17.571 -3.134  1.00 49.50  ? 56  GLY A N   1 
ATOM   433  C CA  . GLY A 1 56  ? -14.545 -18.024 -2.722  1.00 48.48  ? 56  GLY A CA  1 
ATOM   434  C C   . GLY A 1 56  ? -15.488 -16.900 -2.340  1.00 46.54  ? 56  GLY A C   1 
ATOM   435  O O   . GLY A 1 56  ? -16.271 -17.042 -1.405  1.00 49.94  ? 56  GLY A O   1 
ATOM   436  N N   . VAL A 1 57  ? -15.417 -15.770 -3.061  1.00 46.49  ? 57  VAL A N   1 
ATOM   437  C CA  . VAL A 1 57  ? -16.258 -14.596 -2.831  1.00 44.40  ? 57  VAL A CA  1 
ATOM   438  C C   . VAL A 1 57  ? -17.197 -14.407 -4.018  1.00 43.83  ? 57  VAL A C   1 
ATOM   439  O O   . VAL A 1 57  ? -16.729 -14.334 -5.151  1.00 45.46  ? 57  VAL A O   1 
ATOM   440  C CB  . VAL A 1 57  ? -15.392 -13.316 -2.645  1.00 43.17  ? 57  VAL A CB  1 
ATOM   441  C CG1 . VAL A 1 57  ? -16.262 -12.089 -2.398  1.00 43.19  ? 57  VAL A CG1 1 
ATOM   442  C CG2 . VAL A 1 57  ? -14.366 -13.493 -1.530  1.00 44.89  ? 57  VAL A CG2 1 
ATOM   443  N N   . LYS A 1 58  ? -18.509 -14.318 -3.774  1.00 40.81  ? 58  LYS A N   1 
ATOM   444  C CA  . LYS A 1 58  ? -19.453 -14.035 -4.853  1.00 44.67  ? 58  LYS A CA  1 
ATOM   445  C C   . LYS A 1 58  ? -19.494 -12.500 -5.046  1.00 46.90  ? 58  LYS A C   1 
ATOM   446  O O   . LYS A 1 58  ? -19.615 -11.767 -4.068  1.00 46.87  ? 58  LYS A O   1 
ATOM   447  C CB  . LYS A 1 58  ? -20.850 -14.601 -4.549  1.00 48.44  ? 58  LYS A CB  1 
ATOM   448  C CG  . LYS A 1 58  ? -21.932 -14.008 -5.448  1.00 52.62  ? 58  LYS A CG  1 
ATOM   449  C CD  . LYS A 1 58  ? -23.314 -14.029 -4.798  1.00 58.30  ? 58  LYS A CD  1 
ATOM   450  C CE  . LYS A 1 58  ? -24.387 -13.552 -5.752  1.00 60.04  ? 58  LYS A CE  1 
ATOM   451  N NZ  . LYS A 1 58  ? -24.295 -14.231 -7.087  1.00 59.88  ? 58  LYS A NZ  1 
ATOM   452  N N   . ILE A 1 59  ? -19.294 -12.018 -6.273  1.00 42.94  ? 59  ILE A N   1 
ATOM   453  C CA  . ILE A 1 59  ? -19.289 -10.581 -6.538  1.00 46.52  ? 59  ILE A CA  1 
ATOM   454  C C   . ILE A 1 59  ? -20.311 -10.153 -7.597  1.00 46.22  ? 59  ILE A C   1 
ATOM   455  O O   . ILE A 1 59  ? -20.381 -10.758 -8.667  1.00 47.47  ? 59  ILE A O   1 
ATOM   456  C CB  . ILE A 1 59  ? -17.873 -10.068 -6.903  1.00 50.52  ? 59  ILE A CB  1 
ATOM   457  C CG1 . ILE A 1 59  ? -17.469 -10.493 -8.318  1.00 50.23  ? 59  ILE A CG1 1 
ATOM   458  C CG2 . ILE A 1 59  ? -16.823 -10.497 -5.885  1.00 47.66  ? 59  ILE A CG2 1 
ATOM   459  C CD1 . ILE A 1 59  ? -18.035 -9.657  -9.350  1.00 49.67  ? 59  ILE A CD1 1 
ATOM   460  N N   . THR A 1 60  ? -21.114 -9.118  -7.291  1.00 44.67  ? 60  THR A N   1 
ATOM   461  C CA  . THR A 1 60  ? -22.040 -8.559  -8.269  1.00 44.84  ? 60  THR A CA  1 
ATOM   462  C C   . THR A 1 60  ? -21.523 -7.172  -8.643  1.00 41.07  ? 60  THR A C   1 
ATOM   463  O O   . THR A 1 60  ? -21.166 -6.379  -7.775  1.00 40.86  ? 60  THR A O   1 
ATOM   464  C CB  . THR A 1 60  ? -23.519 -8.533  -7.791  1.00 45.85  ? 60  THR A CB  1 
ATOM   465  O OG1 . THR A 1 60  ? -24.004 -9.852  -7.520  1.00 53.79  ? 60  THR A OG1 1 
ATOM   466  C CG2 . THR A 1 60  ? -24.444 -7.847  -8.751  1.00 47.21  ? 60  THR A CG2 1 
ATOM   467  N N   . VAL A 1 61  ? -21.471 -6.891  -9.925  1.00 43.45  ? 61  VAL A N   1 
ATOM   468  C CA  . VAL A 1 61  ? -20.993 -5.602  -10.406 1.00 40.36  ? 61  VAL A CA  1 
ATOM   469  C C   . VAL A 1 61  ? -22.130 -4.878  -11.114 1.00 42.31  ? 61  VAL A C   1 
ATOM   470  O O   . VAL A 1 61  ? -22.754 -5.473  -11.988 1.00 41.77  ? 61  VAL A O   1 
ATOM   471  C CB  . VAL A 1 61  ? -19.772 -5.790  -11.321 1.00 42.24  ? 61  VAL A CB  1 
ATOM   472  C CG1 . VAL A 1 61  ? -19.225 -4.446  -11.769 1.00 41.19  ? 61  VAL A CG1 1 
ATOM   473  C CG2 . VAL A 1 61  ? -18.689 -6.613  -10.621 1.00 48.90  ? 61  VAL A CG2 1 
ATOM   474  N N   . ALA A 1 62  ? -22.441 -3.631  -10.727 1.00 38.45  ? 62  ALA A N   1 
ATOM   475  C CA  . ALA A 1 62  ? -23.501 -2.878  -11.402 1.00 43.81  ? 62  ALA A CA  1 
ATOM   476  C C   . ALA A 1 62  ? -22.883 -1.598  -11.963 1.00 40.50  ? 62  ALA A C   1 
ATOM   477  O O   . ALA A 1 62  ? -22.252 -0.858  -11.203 1.00 36.00  ? 62  ALA A O   1 
ATOM   478  C CB  . ALA A 1 62  ? -24.640 -2.564  -10.434 1.00 41.74  ? 62  ALA A CB  1 
ATOM   479  N N   . ASP A 1 63  ? -23.025 -1.335  -13.283 1.00 35.65  ? 63  ASP A N   1 
ATOM   480  C CA  . ASP A 1 63  ? -22.385 -0.160  -13.872 1.00 36.86  ? 63  ASP A CA  1 
ATOM   481  C C   . ASP A 1 63  ? -23.349 0.957   -14.325 1.00 37.86  ? 63  ASP A C   1 
ATOM   482  O O   . ASP A 1 63  ? -23.134 1.555   -15.380 1.00 39.52  ? 63  ASP A O   1 
ATOM   483  C CB  . ASP A 1 63  ? -21.455 -0.580  -15.032 1.00 39.82  ? 63  ASP A CB  1 
ATOM   484  C CG  . ASP A 1 63  ? -20.250 -1.393  -14.589 1.00 39.14  ? 63  ASP A CG  1 
ATOM   485  O OD1 . ASP A 1 63  ? -19.784 -1.186  -13.460 1.00 37.60  ? 63  ASP A OD1 1 
ATOM   486  O OD2 . ASP A 1 63  ? -19.765 -2.212  -15.388 1.00 40.52  ? 63  ASP A OD2 1 
ATOM   487  N N   . CYS A 1 64  ? -24.339 1.289   -13.513 1.00 31.09  ? 64  CYS A N   1 
ATOM   488  C CA  . CYS A 1 64  ? -25.277 2.359   -13.844 1.00 35.52  ? 64  CYS A CA  1 
ATOM   489  C C   . CYS A 1 64  ? -25.525 3.289   -12.642 1.00 37.47  ? 64  CYS A C   1 
ATOM   490  O O   . CYS A 1 64  ? -26.626 3.829   -12.525 1.00 39.02  ? 64  CYS A O   1 
ATOM   491  C CB  . CYS A 1 64  ? -26.587 1.757   -14.334 1.00 37.00  ? 64  CYS A CB  1 
ATOM   492  S SG  . CYS A 1 64  ? -27.259 0.510   -13.210 1.00 57.91  ? 64  CYS A SG  1 
ATOM   493  N N   . LYS A 1 65  ? -24.537 3.472   -11.750 1.00 34.90  ? 65  LYS A N   1 
ATOM   494  C CA  . LYS A 1 65  ? -24.732 4.329   -10.586 1.00 35.69  ? 65  LYS A CA  1 
ATOM   495  C C   . LYS A 1 65  ? -24.346 5.773   -10.883 1.00 34.70  ? 65  LYS A C   1 
ATOM   496  O O   . LYS A 1 65  ? -23.172 6.066   -11.105 1.00 35.83  ? 65  LYS A O   1 
ATOM   497  C CB  . LYS A 1 65  ? -23.948 3.772   -9.378  1.00 37.03  ? 65  LYS A CB  1 
ATOM   498  C CG  . LYS A 1 65  ? -23.562 4.797   -8.301  1.00 42.70  ? 65  LYS A CG  1 
ATOM   499  C CD  . LYS A 1 65  ? -24.570 4.888   -7.131  1.00 49.07  ? 65  LYS A CD  1 
ATOM   500  C CE  . LYS A 1 65  ? -24.531 3.703   -6.185  1.00 61.28  ? 65  LYS A CE  1 
ATOM   501  N NZ  . LYS A 1 65  ? -23.208 3.580   -5.494  1.00 81.31  ? 65  LYS A NZ  1 
ATOM   502  N N   . GLU A 1 66  ? -25.318 6.679   -10.876 1.00 36.42  ? 66  GLU A N   1 
ATOM   503  C CA  . GLU A 1 66  ? -25.031 8.106   -11.057 1.00 34.70  ? 66  GLU A CA  1 
ATOM   504  C C   . GLU A 1 66  ? -24.447 8.639   -9.742  1.00 31.92  ? 66  GLU A C   1 
ATOM   505  O O   . GLU A 1 66  ? -25.101 8.601   -8.701  1.00 29.59  ? 66  GLU A O   1 
ATOM   506  C CB  . GLU A 1 66  ? -26.279 8.872   -11.490 1.00 35.10  ? 66  GLU A CB  1 
ATOM   507  C CG  . GLU A 1 66  ? -26.912 8.195   -12.688 1.00 41.56  ? 66  GLU A CG  1 
ATOM   508  C CD  . GLU A 1 66  ? -27.466 9.096   -13.766 1.00 48.36  ? 66  GLU A CD  1 
ATOM   509  O OE1 . GLU A 1 66  ? -28.148 10.089  -13.425 1.00 51.72  ? 66  GLU A OE1 1 
ATOM   510  O OE2 . GLU A 1 66  ? -27.237 8.793   -14.959 1.00 51.66  ? 66  GLU A OE2 1 
ATOM   511  N N   . LYS A 1 67  ? -23.158 8.989   -9.784  1.00 27.49  ? 67  LYS A N   1 
ATOM   512  C CA  . LYS A 1 67  ? -22.370 9.476   -8.666  1.00 28.71  ? 67  LYS A CA  1 
ATOM   513  C C   . LYS A 1 67  ? -22.217 10.991  -8.666  1.00 32.65  ? 67  LYS A C   1 
ATOM   514  O O   . LYS A 1 67  ? -21.683 11.541  -7.701  1.00 29.77  ? 67  LYS A O   1 
ATOM   515  C CB  . LYS A 1 67  ? -20.984 8.798   -8.648  1.00 25.79  ? 67  LYS A CB  1 
ATOM   516  C CG  . LYS A 1 67  ? -21.085 7.295   -8.406  1.00 30.49  ? 67  LYS A CG  1 
ATOM   517  C CD  . LYS A 1 67  ? -19.724 6.664   -8.206  1.00 30.24  ? 67  LYS A CD  1 
ATOM   518  C CE  . LYS A 1 67  ? -19.828 5.169   -8.371  1.00 35.87  ? 67  LYS A CE  1 
ATOM   519  N NZ  . LYS A 1 67  ? -18.500 4.519   -8.360  1.00 38.99  ? 67  LYS A NZ  1 
ATOM   520  N N   . VAL A 1 68  ? -22.650 11.671  -9.728  1.00 28.86  ? 68  VAL A N   1 
ATOM   521  C CA  . VAL A 1 68  ? -22.580 13.119  -9.791  1.00 29.59  ? 68  VAL A CA  1 
ATOM   522  C C   . VAL A 1 68  ? -23.933 13.664  -10.266 1.00 30.83  ? 68  VAL A C   1 
ATOM   523  O O   . VAL A 1 68  ? -24.690 12.981  -10.963 1.00 31.37  ? 68  VAL A O   1 
ATOM   524  C CB  . VAL A 1 68  ? -21.386 13.625  -10.643 1.00 31.19  ? 68  VAL A CB  1 
ATOM   525  C CG1 . VAL A 1 68  ? -20.037 13.184  -10.050 1.00 25.99  ? 68  VAL A CG1 1 
ATOM   526  C CG2 . VAL A 1 68  ? -21.502 13.156  -12.093 1.00 26.46  ? 68  VAL A CG2 1 
ATOM   527  N N   . SER A 1 69  ? -24.285 14.829  -9.787  1.00 27.38  ? 69  SER A N   1 
ATOM   528  C CA  . SER A 1 69  ? -25.514 15.513  -10.184 1.00 34.40  ? 69  SER A CA  1 
ATOM   529  C C   . SER A 1 69  ? -25.325 17.033  -10.010 1.00 31.87  ? 69  SER A C   1 
ATOM   530  O O   . SER A 1 69  ? -24.302 17.485  -9.492  1.00 31.49  ? 69  SER A O   1 
ATOM   531  C CB  . SER A 1 69  ? -26.718 15.000  -9.389  1.00 34.18  ? 69  SER A CB  1 
ATOM   532  O OG  . SER A 1 69  ? -26.479 15.189  -8.010  1.00 36.82  ? 69  SER A OG  1 
ATOM   533  N N   . GLU A 1 70  ? -26.303 17.808  -10.451 1.00 32.43  ? 70  GLU A N   1 
ATOM   534  C CA  . GLU A 1 70  ? -26.253 19.243  -10.357 1.00 42.05  ? 70  GLU A CA  1 
ATOM   535  C C   . GLU A 1 70  ? -27.560 19.761  -9.807  1.00 48.42  ? 70  GLU A C   1 
ATOM   536  O O   . GLU A 1 70  ? -28.596 19.644  -10.464 1.00 45.96  ? 70  GLU A O   1 
ATOM   537  C CB  . GLU A 1 70  ? -25.980 19.853  -11.726 1.00 43.83  ? 70  GLU A CB  1 
ATOM   538  C CG  . GLU A 1 70  ? -25.698 21.344  -11.656 1.00 51.88  ? 70  GLU A CG  1 
ATOM   539  C CD  . GLU A 1 70  ? -25.266 21.932  -12.987 1.00 57.49  ? 70  GLU A CD  1 
ATOM   540  O OE1 . GLU A 1 70  ? -26.101 21.968  -13.921 1.00 54.47  ? 70  GLU A OE1 1 
ATOM   541  O OE2 . GLU A 1 70  ? -24.089 22.351  -13.094 1.00 51.44  ? 70  GLU A OE2 1 
ATOM   542  N N   . ARG A 1 71  ? -27.489 20.344  -8.600  1.00 46.67  ? 71  ARG A N   1 
ATOM   543  C CA  . ARG A 1 71  ? -28.595 20.919  -7.852  1.00 49.48  ? 71  ARG A CA  1 
ATOM   544  C C   . ARG A 1 71  ? -28.339 22.414  -7.614  1.00 53.63  ? 71  ARG A C   1 
ATOM   545  O O   . ARG A 1 71  ? -27.402 22.756  -6.889  1.00 51.66  ? 71  ARG A O   1 
ATOM   546  C CB  . ARG A 1 71  ? -28.696 20.225  -6.476  1.00 56.23  ? 71  ARG A CB  1 
ATOM   547  C CG  . ARG A 1 71  ? -28.619 18.694  -6.529  1.00 55.04  ? 71  ARG A CG  1 
ATOM   548  C CD  . ARG A 1 71  ? -28.094 18.070  -5.239  1.00 59.25  ? 71  ARG A CD  1 
ATOM   549  N NE  . ARG A 1 71  ? -28.671 18.693  -4.047  1.00 62.69  ? 71  ARG A NE  1 
ATOM   550  C CZ  . ARG A 1 71  ? -28.556 18.219  -2.812  1.00 62.04  ? 71  ARG A CZ  1 
ATOM   551  N NH1 . ARG A 1 71  ? -27.896 17.088  -2.585  1.00 57.42  ? 71  ARG A NH1 1 
ATOM   552  N NH2 . ARG A 1 71  ? -29.114 18.863  -1.795  1.00 59.94  ? 71  ARG A NH2 1 
ATOM   553  N N   . ASN A 1 72  ? -29.157 23.297  -8.226  1.00 54.05  ? 72  ASN A N   1 
ATOM   554  C CA  . ASN A 1 72  ? -29.120 24.748  -8.023  1.00 52.37  ? 72  ASN A CA  1 
ATOM   555  C C   . ASN A 1 72  ? -27.805 25.420  -8.408  1.00 47.47  ? 72  ASN A C   1 
ATOM   556  O O   . ASN A 1 72  ? -27.340 26.326  -7.710  1.00 50.38  ? 72  ASN A O   1 
ATOM   557  C CB  . ASN A 1 72  ? -29.479 25.050  -6.564  1.00 55.98  ? 72  ASN A CB  1 
ATOM   558  C CG  . ASN A 1 72  ? -30.569 24.147  -6.018  1.00 63.03  ? 72  ASN A CG  1 
ATOM   559  O OD1 . ASN A 1 72  ? -31.764 24.301  -6.333  1.00 64.08  ? 72  ASN A OD1 1 
ATOM   560  N ND2 . ASN A 1 72  ? -30.184 23.175  -5.196  1.00 64.66  ? 72  ASN A ND2 1 
ATOM   561  N N   . GLY A 1 73  ? -27.198 24.966  -9.494  1.00 42.83  ? 73  GLY A N   1 
ATOM   562  C CA  . GLY A 1 73  ? -25.904 25.491  -9.912  1.00 40.98  ? 73  GLY A CA  1 
ATOM   563  C C   . GLY A 1 73  ? -24.723 24.924  -9.143  1.00 41.72  ? 73  GLY A C   1 
ATOM   564  O O   . GLY A 1 73  ? -23.576 25.275  -9.426  1.00 42.03  ? 73  GLY A O   1 
ATOM   565  N N   . VAL A 1 74  ? -24.970 24.015  -8.192  1.00 35.87  ? 74  VAL A N   1 
ATOM   566  C CA  . VAL A 1 74  ? -23.906 23.382  -7.427  1.00 32.25  ? 74  VAL A CA  1 
ATOM   567  C C   . VAL A 1 74  ? -23.757 21.929  -7.914  1.00 31.95  ? 74  VAL A C   1 
ATOM   568  O O   . VAL A 1 74  ? -24.761 21.240  -8.067  1.00 33.22  ? 74  VAL A O   1 
ATOM   569  C CB  . VAL A 1 74  ? -24.207 23.468  -5.896  1.00 32.12  ? 74  VAL A CB  1 
ATOM   570  C CG1 . VAL A 1 74  ? -23.451 22.409  -5.100  1.00 29.87  ? 74  VAL A CG1 1 
ATOM   571  C CG2 . VAL A 1 74  ? -23.924 24.858  -5.352  1.00 35.10  ? 74  VAL A CG2 1 
ATOM   572  N N   . LEU A 1 75  ? -22.533 21.481  -8.180  1.00 23.78  ? 75  LEU A N   1 
ATOM   573  C CA  . LEU A 1 75  ? -22.299 20.082  -8.565  1.00 28.08  ? 75  LEU A CA  1 
ATOM   574  C C   . LEU A 1 75  ? -22.093 19.278  -7.296  1.00 26.17  ? 75  LEU A C   1 
ATOM   575  O O   . LEU A 1 75  ? -21.432 19.740  -6.381  1.00 21.19  ? 75  LEU A O   1 
ATOM   576  C CB  . LEU A 1 75  ? -21.050 19.948  -9.444  1.00 27.54  ? 75  LEU A CB  1 
ATOM   577  C CG  . LEU A 1 75  ? -20.984 20.897  -10.633 1.00 30.94  ? 75  LEU A CG  1 
ATOM   578  C CD1 . LEU A 1 75  ? -19.626 20.830  -11.302 1.00 29.20  ? 75  LEU A CD1 1 
ATOM   579  C CD2 . LEU A 1 75  ? -22.080 20.604  -11.611 1.00 35.15  ? 75  LEU A CD2 1 
ATOM   580  N N   . VAL A 1 76  ? -22.661 18.089  -7.226  1.00 30.48  ? 76  VAL A N   1 
ATOM   581  C CA  . VAL A 1 76  ? -22.526 17.224  -6.063  1.00 24.21  ? 76  VAL A CA  1 
ATOM   582  C C   . VAL A 1 76  ? -22.051 15.829  -6.524  1.00 29.66  ? 76  VAL A C   1 
ATOM   583  O O   . VAL A 1 76  ? -22.699 15.200  -7.371  1.00 23.94  ? 76  VAL A O   1 
ATOM   584  C CB  . VAL A 1 76  ? -23.840 17.147  -5.240  1.00 26.91  ? 76  VAL A CB  1 
ATOM   585  C CG1 . VAL A 1 76  ? -23.585 16.487  -3.891  1.00 28.91  ? 76  VAL A CG1 1 
ATOM   586  C CG2 . VAL A 1 76  ? -24.459 18.535  -5.035  1.00 31.12  ? 76  VAL A CG2 1 
ATOM   587  N N   . GLY A 1 77  ? -20.890 15.409  -6.005  1.00 21.77  ? 77  GLY A N   1 
ATOM   588  C CA  . GLY A 1 77  ? -20.303 14.105  -6.253  1.00 27.17  ? 77  GLY A CA  1 
ATOM   589  C C   . GLY A 1 77  ? -20.264 13.284  -4.984  1.00 32.05  ? 77  GLY A C   1 
ATOM   590  O O   . GLY A 1 77  ? -20.017 13.830  -3.895  1.00 29.45  ? 77  GLY A O   1 
ATOM   591  N N   . GLU A 1 78  ? -20.498 11.964  -5.101  1.00 28.59  ? 78  GLU A N   1 
ATOM   592  C CA  . GLU A 1 78  ? -20.480 11.133  -3.907  1.00 33.59  ? 78  GLU A CA  1 
ATOM   593  C C   . GLU A 1 78  ? -19.934 9.743   -4.118  1.00 30.82  ? 78  GLU A C   1 
ATOM   594  O O   . GLU A 1 78  ? -20.151 9.118   -5.161  1.00 24.28  ? 78  GLU A O   1 
ATOM   595  C CB  . GLU A 1 78  ? -21.857 11.084  -3.223  1.00 40.25  ? 78  GLU A CB  1 
ATOM   596  C CG  . GLU A 1 78  ? -22.949 10.382  -3.989  1.00 41.23  ? 78  GLU A CG  1 
ATOM   597  C CD  . GLU A 1 78  ? -24.181 10.169  -3.128  1.00 53.27  ? 78  GLU A CD  1 
ATOM   598  O OE1 . GLU A 1 78  ? -25.309 10.285  -3.660  1.00 59.93  ? 78  GLU A OE1 1 
ATOM   599  O OE2 . GLU A 1 78  ? -24.013 9.882   -1.919  1.00 52.02  ? 78  GLU A OE2 1 
ATOM   600  N N   . VAL A 1 79  ? -19.150 9.309   -3.149  1.00 26.07  ? 79  VAL A N   1 
ATOM   601  C CA  . VAL A 1 79  ? -18.605 7.957   -3.052  1.00 39.87  ? 79  VAL A CA  1 
ATOM   602  C C   . VAL A 1 79  ? -19.151 7.390   -1.724  1.00 43.34  ? 79  VAL A C   1 
ATOM   603  O O   . VAL A 1 79  ? -19.313 8.140   -0.763  1.00 38.05  ? 79  VAL A O   1 
ATOM   604  C CB  . VAL A 1 79  ? -17.053 7.885   -3.147  1.00 39.81  ? 79  VAL A CB  1 
ATOM   605  C CG1 . VAL A 1 79  ? -16.560 8.336   -4.519  1.00 38.10  ? 79  VAL A CG1 1 
ATOM   606  C CG2 . VAL A 1 79  ? -16.380 8.697   -2.039  1.00 43.58  ? 79  VAL A CG2 1 
ATOM   607  N N   . SER A 1 80  ? -19.509 6.107   -1.687  1.00 52.79  ? 80  SER A N   1 
ATOM   608  C CA  . SER A 1 80  ? -20.081 5.501   -0.477  1.00 54.12  ? 80  SER A CA  1 
ATOM   609  C C   . SER A 1 80  ? -19.698 4.033   -0.304  1.00 65.95  ? 80  SER A C   1 
ATOM   610  O O   . SER A 1 80  ? -19.381 3.359   -1.281  1.00 74.70  ? 80  SER A O   1 
ATOM   611  C CB  . SER A 1 80  ? -21.598 5.635   -0.474  1.00 48.72  ? 80  SER A CB  1 
ATOM   612  O OG  . SER A 1 80  ? -22.133 5.092   -1.665  1.00 58.26  ? 80  SER A OG  1 
ATOM   613  N N   . SER A 1 81  ? -19.739 3.549   0.944   1.00 56.95  ? 81  SER A N   1 
ATOM   614  C CA  . SER A 1 81  ? -19.394 2.179   1.344   1.00 64.00  ? 81  SER A CA  1 
ATOM   615  C C   . SER A 1 81  ? -20.449 1.574   2.279   1.00 59.71  ? 81  SER A C   1 
ATOM   616  O O   . SER A 1 81  ? -21.350 2.276   2.759   1.00 58.27  ? 81  SER A O   1 
ATOM   617  C CB  . SER A 1 81  ? -18.060 2.176   2.089   1.00 66.93  ? 81  SER A CB  1 
ATOM   618  O OG  . SER A 1 81  ? -16.962 2.236   1.197   1.00 86.50  ? 81  SER A OG  1 
ATOM   619  N N   . ALA A 1 82  ? -20.306 0.265   2.546   1.00 64.56  ? 82  ALA A N   1 
ATOM   620  C CA  . ALA A 1 82  ? -21.082 -0.521  3.503   1.00 63.77  ? 82  ALA A CA  1 
ATOM   621  C C   . ALA A 1 82  ? -20.097 -1.577  4.050   1.00 71.03  ? 82  ALA A C   1 
ATOM   622  O O   . ALA A 1 82  ? -19.560 -2.371  3.280   1.00 70.07  ? 82  ALA A O   1 
ATOM   623  C CB  . ALA A 1 82  ? -22.252 -1.202  2.814   1.00 67.31  ? 82  ALA A CB  1 
ATOM   624  N N   . GLU A 1 83  ? -19.793 -1.530  5.351   1.00 76.19  ? 83  GLU A N   1 
ATOM   625  C CA  . GLU A 1 83  ? -18.860 -2.480  5.963   1.00 78.41  ? 83  GLU A CA  1 
ATOM   626  C C   . GLU A 1 83  ? -19.246 -2.684  7.411   1.00 75.23  ? 83  GLU A C   1 
ATOM   627  O O   . GLU A 1 83  ? -19.251 -1.715  8.169   1.00 74.37  ? 83  GLU A O   1 
ATOM   628  C CB  . GLU A 1 83  ? -17.417 -1.952  5.896   1.00 82.89  ? 83  GLU A CB  1 
ATOM   629  C CG  . GLU A 1 83  ? -16.390 -2.910  6.482   1.00 88.79  ? 83  GLU A CG  1 
ATOM   630  C CD  . GLU A 1 83  ? -14.938 -2.483  6.381   1.00 95.21  ? 83  GLU A CD  1 
ATOM   631  O OE1 . GLU A 1 83  ? -14.571 -1.869  5.352   1.00 94.21  ? 83  GLU A OE1 1 
ATOM   632  O OE2 . GLU A 1 83  ? -14.161 -2.783  7.317   1.00 91.90  ? 83  GLU A OE2 1 
ATOM   633  N N   . GLY A 1 84  ? -19.536 -3.927  7.785   1.00 80.08  ? 84  GLY A N   1 
ATOM   634  C CA  . GLY A 1 84  ? -19.912 -4.295  9.147   1.00 78.43  ? 84  GLY A CA  1 
ATOM   635  C C   . GLY A 1 84  ? -20.996 -3.424  9.753   1.00 76.91  ? 84  GLY A C   1 
ATOM   636  O O   . GLY A 1 84  ? -20.851 -2.951  10.882  1.00 80.55  ? 84  GLY A O   1 
ATOM   637  N N   . GLY A 1 85  ? -22.053 -3.165  8.984   1.00 82.64  ? 85  GLY A N   1 
ATOM   638  C CA  . GLY A 1 85  ? -23.175 -2.334  9.411   1.00 75.19  ? 85  GLY A CA  1 
ATOM   639  C C   . GLY A 1 85  ? -22.915 -0.837  9.413   1.00 73.76  ? 85  GLY A C   1 
ATOM   640  O O   . GLY A 1 85  ? -23.813 -0.052  9.737   1.00 74.70  ? 85  GLY A O   1 
ATOM   641  N N   . VAL A 1 86  ? -21.695 -0.421  9.052   1.00 66.58  ? 86  VAL A N   1 
ATOM   642  C CA  . VAL A 1 86  ? -21.303 0.985   9.024   1.00 63.70  ? 86  VAL A CA  1 
ATOM   643  C C   . VAL A 1 86  ? -21.448 1.544   7.604   1.00 65.05  ? 86  VAL A C   1 
ATOM   644  O O   . VAL A 1 86  ? -20.684 1.145   6.714   1.00 63.27  ? 86  VAL A O   1 
ATOM   645  C CB  . VAL A 1 86  ? -19.830 1.199   9.497   1.00 64.10  ? 86  VAL A CB  1 
ATOM   646  C CG1 . VAL A 1 86  ? -19.595 2.640   9.941   1.00 57.70  ? 86  VAL A CG1 1 
ATOM   647  C CG2 . VAL A 1 86  ? -19.412 0.212   10.588  1.00 63.35  ? 86  VAL A CG2 1 
ATOM   648  N N   . VAL A 1 87  ? -22.388 2.486   7.392   1.00 56.69  ? 87  VAL A N   1 
ATOM   649  C CA  . VAL A 1 87  ? -22.503 3.126   6.088   1.00 58.39  ? 87  VAL A CA  1 
ATOM   650  C C   . VAL A 1 87  ? -21.582 4.336   6.093   1.00 55.48  ? 87  VAL A C   1 
ATOM   651  O O   . VAL A 1 87  ? -21.716 5.209   6.952   1.00 53.52  ? 87  VAL A O   1 
ATOM   652  C CB  . VAL A 1 87  ? -23.946 3.505   5.701   1.00 57.26  ? 87  VAL A CB  1 
ATOM   653  C CG1 . VAL A 1 87  ? -23.964 4.595   4.623   1.00 52.37  ? 87  VAL A CG1 1 
ATOM   654  C CG2 . VAL A 1 87  ? -24.719 2.276   5.238   1.00 59.83  ? 87  VAL A CG2 1 
ATOM   655  N N   . LYS A 1 88  ? -20.632 4.374   5.160   1.00 52.00  ? 88  LYS A N   1 
ATOM   656  C CA  . LYS A 1 88  ? -19.748 5.520   5.026   1.00 51.64  ? 88  LYS A CA  1 
ATOM   657  C C   . LYS A 1 88  ? -20.031 6.276   3.704   1.00 49.80  ? 88  LYS A C   1 
ATOM   658  O O   . LYS A 1 88  ? -20.392 5.653   2.700   1.00 46.61  ? 88  LYS A O   1 
ATOM   659  C CB  . LYS A 1 88  ? -18.278 5.119   5.215   1.00 55.34  ? 88  LYS A CB  1 
ATOM   660  C CG  . LYS A 1 88  ? -17.957 4.781   6.675   1.00 56.71  ? 88  LYS A CG  1 
ATOM   661  C CD  . LYS A 1 88  ? -16.468 4.621   6.957   1.00 57.63  ? 88  LYS A CD  1 
ATOM   662  C CE  . LYS A 1 88  ? -15.589 5.710   6.367   1.00 67.40  ? 88  LYS A CE  1 
ATOM   663  N NZ  . LYS A 1 88  ? -15.880 7.062   6.923   1.00 62.19  ? 88  LYS A NZ  1 
ATOM   664  N N   . LYS A 1 89  ? -19.948 7.623   3.719   1.00 42.88  ? 89  LYS A N   1 
ATOM   665  C CA  . LYS A 1 89  ? -20.243 8.431   2.535   1.00 39.52  ? 89  LYS A CA  1 
ATOM   666  C C   . LYS A 1 89  ? -19.454 9.719   2.555   1.00 38.37  ? 89  LYS A C   1 
ATOM   667  O O   . LYS A 1 89  ? -19.382 10.388  3.590   1.00 33.34  ? 89  LYS A O   1 
ATOM   668  C CB  . LYS A 1 89  ? -21.719 8.853   2.523   1.00 40.67  ? 89  LYS A CB  1 
ATOM   669  C CG  . LYS A 1 89  ? -22.692 7.820   2.038   1.00 46.57  ? 89  LYS A CG  1 
ATOM   670  C CD  . LYS A 1 89  ? -24.091 8.406   1.884   1.00 51.05  ? 89  LYS A CD  1 
ATOM   671  C CE  . LYS A 1 89  ? -25.137 7.434   2.384   1.00 50.91  ? 89  LYS A CE  1 
ATOM   672  N NZ  . LYS A 1 89  ? -26.521 7.914   2.100   1.00 55.40  ? 89  LYS A NZ  1 
ATOM   673  N N   . ARG A 1 90  ? -18.922 10.103  1.412   1.00 30.45  ? 90  ARG A N   1 
ATOM   674  C CA  . ARG A 1 90  ? -18.229 11.372  1.294   1.00 33.47  ? 90  ARG A CA  1 
ATOM   675  C C   . ARG A 1 90  ? -18.813 12.148  0.104   1.00 32.34  ? 90  ARG A C   1 
ATOM   676  O O   . ARG A 1 90  ? -19.004 11.569  -0.966  1.00 29.93  ? 90  ARG A O   1 
ATOM   677  C CB  . ARG A 1 90  ? -16.724 11.156  1.161   1.00 36.17  ? 90  ARG A CB  1 
ATOM   678  C CG  . ARG A 1 90  ? -15.966 12.465  1.358   1.00 42.82  ? 90  ARG A CG  1 
ATOM   679  C CD  . ARG A 1 90  ? -14.731 12.311  2.221   1.00 44.44  ? 90  ARG A CD  1 
ATOM   680  N NE  . ARG A 1 90  ? -13.947 11.154  1.808   1.00 51.13  ? 90  ARG A NE  1 
ATOM   681  C CZ  . ARG A 1 90  ? -13.355 10.308  2.640   1.00 56.89  ? 90  ARG A CZ  1 
ATOM   682  N NH1 . ARG A 1 90  ? -13.430 10.492  3.953   1.00 58.83  ? 90  ARG A NH1 1 
ATOM   683  N NH2 . ARG A 1 90  ? -12.671 9.280   2.170   1.00 68.41  ? 90  ARG A NH2 1 
ATOM   684  N N   . ARG A 1 91  ? -19.134 13.424  0.294   1.00 28.37  ? 91  ARG A N   1 
ATOM   685  C CA  . ARG A 1 91  ? -19.656 14.263  -0.776  1.00 28.15  ? 91  ARG A CA  1 
ATOM   686  C C   . ARG A 1 91  ? -18.769 15.462  -1.060  1.00 31.57  ? 91  ARG A C   1 
ATOM   687  O O   . ARG A 1 91  ? -18.220 16.068  -0.139  1.00 25.03  ? 91  ARG A O   1 
ATOM   688  C CB  . ARG A 1 91  ? -21.066 14.767  -0.469  1.00 31.43  ? 91  ARG A CB  1 
ATOM   689  C CG  . ARG A 1 91  ? -22.133 13.725  -0.690  1.00 37.33  ? 91  ARG A CG  1 
ATOM   690  C CD  . ARG A 1 91  ? -23.515 14.271  -0.464  1.00 37.81  ? 91  ARG A CD  1 
ATOM   691  N NE  . ARG A 1 91  ? -24.497 13.198  -0.571  1.00 39.68  ? 91  ARG A NE  1 
ATOM   692  C CZ  . ARG A 1 91  ? -25.812 13.368  -0.546  1.00 45.61  ? 91  ARG A CZ  1 
ATOM   693  N NH1 . ARG A 1 91  ? -26.326 14.582  -0.400  1.00 49.08  ? 91  ARG A NH1 1 
ATOM   694  N NH2 . ARG A 1 91  ? -26.624 12.326  -0.652  1.00 47.87  ? 91  ARG A NH2 1 
ATOM   695  N N   . LEU A 1 92  ? -18.714 15.852  -2.336  1.00 25.68  ? 92  LEU A N   1 
ATOM   696  C CA  . LEU A 1 92  ? -17.973 16.981  -2.870  1.00 23.73  ? 92  LEU A CA  1 
ATOM   697  C C   . LEU A 1 92  ? -18.983 17.911  -3.479  1.00 25.99  ? 92  LEU A C   1 
ATOM   698  O O   . LEU A 1 92  ? -19.829 17.489  -4.273  1.00 24.25  ? 92  LEU A O   1 
ATOM   699  C CB  . LEU A 1 92  ? -16.991 16.481  -3.946  1.00 29.10  ? 92  LEU A CB  1 
ATOM   700  C CG  . LEU A 1 92  ? -16.135 17.514  -4.671  1.00 25.29  ? 92  LEU A CG  1 
ATOM   701  C CD1 . LEU A 1 92  ? -15.272 18.287  -3.705  1.00 26.37  ? 92  LEU A CD1 1 
ATOM   702  C CD2 . LEU A 1 92  ? -15.249 16.831  -5.678  1.00 28.05  ? 92  LEU A CD2 1 
ATOM   703  N N   . TYR A 1 93  ? -18.919 19.177  -3.112  1.00 23.17  ? 93  TYR A N   1 
ATOM   704  C CA  . TYR A 1 93  ? -19.825 20.204  -3.612  1.00 24.50  ? 93  TYR A CA  1 
ATOM   705  C C   . TYR A 1 93  ? -18.947 21.223  -4.328  1.00 27.26  ? 93  TYR A C   1 
ATOM   706  O O   . TYR A 1 93  ? -17.931 21.646  -3.766  1.00 23.61  ? 93  TYR A O   1 
ATOM   707  C CB  . TYR A 1 93  ? -20.577 20.880  -2.441  1.00 25.78  ? 93  TYR A CB  1 
ATOM   708  C CG  . TYR A 1 93  ? -21.306 19.911  -1.531  1.00 26.88  ? 93  TYR A CG  1 
ATOM   709  C CD1 . TYR A 1 93  ? -20.613 19.126  -0.622  1.00 29.25  ? 93  TYR A CD1 1 
ATOM   710  C CD2 . TYR A 1 93  ? -22.690 19.793  -1.570  1.00 31.31  ? 93  TYR A CD2 1 
ATOM   711  C CE1 . TYR A 1 93  ? -21.273 18.217  0.196   1.00 32.70  ? 93  TYR A CE1 1 
ATOM   712  C CE2 . TYR A 1 93  ? -23.365 18.900  -0.741  1.00 31.30  ? 93  TYR A CE2 1 
ATOM   713  C CZ  . TYR A 1 93  ? -22.652 18.127  0.154   1.00 33.86  ? 93  TYR A CZ  1 
ATOM   714  O OH  . TYR A 1 93  ? -23.281 17.227  0.976   1.00 33.81  ? 93  TYR A OH  1 
ATOM   715  N N   . ALA A 1 94  ? -19.280 21.570  -5.575  1.00 25.32  ? 94  ALA A N   1 
ATOM   716  C CA  . ALA A 1 94  ? -18.453 22.502  -6.317  1.00 28.74  ? 94  ALA A CA  1 
ATOM   717  C C   . ALA A 1 94  ? -19.239 23.471  -7.169  1.00 28.61  ? 94  ALA A C   1 
ATOM   718  O O   . ALA A 1 94  ? -20.230 23.119  -7.790  1.00 27.27  ? 94  ALA A O   1 
ATOM   719  C CB  . ALA A 1 94  ? -17.471 21.740  -7.202  1.00 25.55  ? 94  ALA A CB  1 
ATOM   720  N N   . SER A 1 95  ? -18.770 24.688  -7.206  1.00 23.17  ? 95  SER A N   1 
ATOM   721  C CA  . SER A 1 95  ? -19.269 25.695  -8.140  1.00 29.92  ? 95  SER A CA  1 
ATOM   722  C C   . SER A 1 95  ? -18.073 26.595  -8.535  1.00 30.91  ? 95  SER A C   1 
ATOM   723  O O   . SER A 1 95  ? -16.916 26.251  -8.223  1.00 27.30  ? 95  SER A O   1 
ATOM   724  C CB  . SER A 1 95  ? -20.474 26.452  -7.584  1.00 35.88  ? 95  SER A CB  1 
ATOM   725  O OG  . SER A 1 95  ? -20.089 27.395  -6.599  1.00 39.13  ? 95  SER A OG  1 
ATOM   726  N N   . ALA A 1 96  ? -18.314 27.698  -9.259  1.00 33.32  ? 96  ALA A N   1 
ATOM   727  C CA  . ALA A 1 96  ? -17.242 28.603  -9.661  1.00 34.96  ? 96  ALA A CA  1 
ATOM   728  C C   . ALA A 1 96  ? -16.475 29.137  -8.454  1.00 31.80  ? 96  ALA A C   1 
ATOM   729  O O   . ALA A 1 96  ? -17.079 29.712  -7.551  1.00 32.35  ? 96  ALA A O   1 
ATOM   730  C CB  . ALA A 1 96  ? -17.801 29.760  -10.471 1.00 34.16  ? 96  ALA A CB  1 
ATOM   731  N N   . GLY A 1 97  ? -15.164 28.875  -8.409  1.00 31.58  ? 97  GLY A N   1 
ATOM   732  C CA  . GLY A 1 97  ? -14.311 29.368  -7.307  1.00 33.50  ? 97  GLY A CA  1 
ATOM   733  C C   . GLY A 1 97  ? -14.767 28.907  -5.932  1.00 35.22  ? 97  GLY A C   1 
ATOM   734  O O   . GLY A 1 97  ? -14.314 29.508  -4.942  1.00 34.61  ? 97  GLY A O   1 
ATOM   735  N N   . ASN A 1 98  ? -15.639 27.895  -5.859  1.00 30.48  ? 98  ASN A N   1 
ATOM   736  C CA  . ASN A 1 98  ? -16.184 27.455  -4.545  1.00 36.25  ? 98  ASN A CA  1 
ATOM   737  C C   . ASN A 1 98  ? -16.163 25.925  -4.451  1.00 31.27  ? 98  ASN A C   1 
ATOM   738  O O   . ASN A 1 98  ? -16.461 25.277  -5.471  1.00 29.48  ? 98  ASN A O   1 
ATOM   739  C CB  . ASN A 1 98  ? -17.593 28.010  -4.319  1.00 30.04  ? 98  ASN A CB  1 
ATOM   740  C CG  . ASN A 1 98  ? -17.966 28.149  -2.858  1.00 41.01  ? 98  ASN A CG  1 
ATOM   741  O OD1 . ASN A 1 98  ? -19.082 28.547  -2.535  1.00 48.93  ? 98  ASN A OD1 1 
ATOM   742  N ND2 . ASN A 1 98  ? -17.042 27.831  -1.967  1.00 50.94  ? 98  ASN A ND2 1 
ATOM   743  N N   . PHE A 1 99  ? -15.839 25.373  -3.274  1.00 30.89  ? 99  PHE A N   1 
ATOM   744  C CA  . PHE A 1 99  ? -15.893 23.898  -3.079  1.00 26.56  ? 99  PHE A CA  1 
ATOM   745  C C   . PHE A 1 99  ? -16.058 23.573  -1.592  1.00 31.92  ? 99  PHE A C   1 
ATOM   746  O O   . PHE A 1 99  ? -15.697 24.438  -0.778  1.00 24.88  ? 99  PHE A O   1 
ATOM   747  C CB  . PHE A 1 99  ? -14.690 23.193  -3.719  1.00 24.32  ? 99  PHE A CB  1 
ATOM   748  C CG  . PHE A 1 99  ? -13.484 22.961  -2.840  1.00 33.97  ? 99  PHE A CG  1 
ATOM   749  C CD1 . PHE A 1 99  ? -13.446 21.913  -1.931  1.00 31.83  ? 99  PHE A CD1 1 
ATOM   750  C CD2 . PHE A 1 99  ? -12.356 23.757  -2.961  1.00 34.26  ? 99  PHE A CD2 1 
ATOM   751  C CE1 . PHE A 1 99  ? -12.334 21.696  -1.133  1.00 32.23  ? 99  PHE A CE1 1 
ATOM   752  C CE2 . PHE A 1 99  ? -11.240 23.532  -2.171  1.00 36.21  ? 99  PHE A CE2 1 
ATOM   753  C CZ  . PHE A 1 99  ? -11.230 22.504  -1.258  1.00 35.78  ? 99  PHE A CZ  1 
ATOM   754  N N   . ALA A 1 100 ? -16.605 22.396  -1.260  1.00 27.12  ? 100 ALA A N   1 
ATOM   755  C CA  . ALA A 1 100 ? -16.717 21.952  0.121   1.00 30.15  ? 100 ALA A CA  1 
ATOM   756  C C   . ALA A 1 100 ? -16.716 20.415  0.105   1.00 28.85  ? 100 ALA A C   1 
ATOM   757  O O   . ALA A 1 100 ? -17.098 19.774  -0.888  1.00 23.91  ? 100 ALA A O   1 
ATOM   758  C CB  . ALA A 1 100 ? -17.983 22.492  0.791   1.00 24.33  ? 100 ALA A CB  1 
ATOM   759  N N   . ILE A 1 101 ? -16.237 19.836  1.183   1.00 25.40  ? 101 ILE A N   1 
ATOM   760  C CA  . ILE A 1 101 ? -16.190 18.404  1.349   1.00 25.97  ? 101 ILE A CA  1 
ATOM   761  C C   . ILE A 1 101 ? -16.899 18.034  2.642   1.00 32.99  ? 101 ILE A C   1 
ATOM   762  O O   . ILE A 1 101 ? -16.656 18.663  3.676   1.00 28.59  ? 101 ILE A O   1 
ATOM   763  C CB  . ILE A 1 101 ? -14.740 17.866  1.300   1.00 30.09  ? 101 ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 101 ? -14.123 18.040  -0.104  1.00 26.95  ? 101 ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 101 ? -14.719 16.384  1.676   1.00 32.69  ? 101 ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 101 ? -12.630 17.624  -0.151  1.00 27.76  ? 101 ILE A CD1 1 
ATOM   767  N N   . ALA A 1 102 ? -17.828 17.080  2.588   1.00 27.33  ? 102 ALA A N   1 
ATOM   768  C CA  . ALA A 1 102 ? -18.551 16.645  3.781   1.00 29.56  ? 102 ALA A CA  1 
ATOM   769  C C   . ALA A 1 102 ? -18.542 15.106  3.879   1.00 35.33  ? 102 ALA A C   1 
ATOM   770  O O   . ALA A 1 102 ? -18.488 14.428  2.857   1.00 29.79  ? 102 ALA A O   1 
ATOM   771  C CB  . ALA A 1 102 ? -19.973 17.179  3.760   1.00 29.36  ? 102 ALA A CB  1 
ATOM   772  N N   . GLU A 1 103 ? -18.513 14.585  5.108   1.00 27.75  ? 103 GLU A N   1 
ATOM   773  C CA  . GLU A 1 103 ? -18.507 13.112  5.314   1.00 32.64  ? 103 GLU A CA  1 
ATOM   774  C C   . GLU A 1 103 ? -19.755 12.743  6.115   1.00 33.70  ? 103 GLU A C   1 
ATOM   775  O O   . GLU A 1 103 ? -20.202 13.580  6.917   1.00 30.71  ? 103 GLU A O   1 
ATOM   776  C CB  . GLU A 1 103 ? -17.260 12.681  6.085   1.00 36.67  ? 103 GLU A CB  1 
ATOM   777  C CG  . GLU A 1 103 ? -15.964 13.145  5.452   1.00 41.92  ? 103 GLU A CG  1 
ATOM   778  C CD  . GLU A 1 103 ? -14.709 12.707  6.187   1.00 48.26  ? 103 GLU A CD  1 
ATOM   779  O OE1 . GLU A 1 103 ? -13.608 13.112  5.765   1.00 53.25  ? 103 GLU A OE1 1 
ATOM   780  O OE2 . GLU A 1 103 ? -14.837 11.960  7.177   1.00 48.37  ? 103 GLU A OE2 1 
ATOM   781  N N   . LEU A 1 104 ? -20.273 11.527  5.933   1.00 28.65  ? 104 LEU A N   1 
ATOM   782  C CA  . LEU A 1 104 ? -21.429 11.108  6.762   1.00 34.67  ? 104 LEU A CA  1 
ATOM   783  C C   . LEU A 1 104 ? -20.883 10.543  8.073   1.00 34.09  ? 104 LEU A C   1 
ATOM   784  O O   . LEU A 1 104 ? -20.391 9.399   8.067   1.00 31.42  ? 104 LEU A O   1 
ATOM   785  C CB  . LEU A 1 104 ? -22.233 10.045  6.008   1.00 33.69  ? 104 LEU A CB  1 
ATOM   786  C CG  . LEU A 1 104 ? -23.501 9.565   6.713   1.00 33.19  ? 104 LEU A CG  1 
ATOM   787  C CD1 . LEU A 1 104 ? -24.537 10.676  6.784   1.00 36.30  ? 104 LEU A CD1 1 
ATOM   788  C CD2 . LEU A 1 104 ? -24.079 8.343   6.018   1.00 41.40  ? 104 LEU A CD2 1 
ATOM   789  N N   . ILE A 1 105 ? -20.975 11.321  9.152   1.00 35.82  ? 105 ILE A N   1 
ATOM   790  C CA  . ILE A 1 105 ? -20.550 10.800  10.482  1.00 31.47  ? 105 ILE A CA  1 
ATOM   791  C C   . ILE A 1 105 ? -21.840 10.401  11.193  1.00 35.84  ? 105 ILE A C   1 
ATOM   792  O O   . ILE A 1 105 ? -22.668 11.301  11.440  1.00 29.54  ? 105 ILE A O   1 
ATOM   793  C CB  . ILE A 1 105 ? -19.764 11.872  11.263  1.00 32.67  ? 105 ILE A CB  1 
ATOM   794  C CG1 . ILE A 1 105 ? -18.658 12.500  10.411  1.00 33.69  ? 105 ILE A CG1 1 
ATOM   795  C CG2 . ILE A 1 105 ? -19.218 11.301  12.563  1.00 31.26  ? 105 ILE A CG2 1 
ATOM   796  C CD1 . ILE A 1 105 ? -17.575 11.531  9.994   1.00 32.36  ? 105 ILE A CD1 1 
ATOM   797  N N   . ASN A 1 106 ? -22.013 9.107   11.477  1.00 31.34  ? 106 ASN A N   1 
ATOM   798  C CA  . ASN A 1 106 ? -23.297 8.647   12.068  1.00 40.03  ? 106 ASN A CA  1 
ATOM   799  C C   . ASN A 1 106 ? -24.424 9.064   11.112  1.00 41.32  ? 106 ASN A C   1 
ATOM   800  O O   . ASN A 1 106 ? -24.363 8.658   9.935   1.00 44.58  ? 106 ASN A O   1 
ATOM   801  C CB  . ASN A 1 106 ? -23.452 9.060   13.535  1.00 36.66  ? 106 ASN A CB  1 
ATOM   802  C CG  . ASN A 1 106 ? -24.417 8.177   14.298  1.00 42.99  ? 106 ASN A CG  1 
ATOM   803  O OD1 . ASN A 1 106 ? -24.941 7.206   13.756  1.00 44.50  ? 106 ASN A OD1 1 
ATOM   804  N ND2 . ASN A 1 106 ? -24.656 8.504   15.557  1.00 44.27  ? 106 ASN A ND2 1 
ATOM   805  N N   . THR A 1 107 ? -25.416 9.822   11.589  1.00 40.53  ? 107 THR A N   1 
ATOM   806  C CA  . THR A 1 107 ? -26.583 10.172  10.733  1.00 42.20  ? 107 THR A CA  1 
ATOM   807  C C   . THR A 1 107 ? -26.450 11.573  10.117  1.00 43.66  ? 107 THR A C   1 
ATOM   808  O O   . THR A 1 107 ? -27.410 11.990  9.438   1.00 51.28  ? 107 THR A O   1 
ATOM   809  C CB  . THR A 1 107 ? -27.893 10.068  11.524  1.00 47.99  ? 107 THR A CB  1 
ATOM   810  O OG1 . THR A 1 107 ? -27.879 11.081  12.530  1.00 55.06  ? 107 THR A OG1 1 
ATOM   811  C CG2 . THR A 1 107 ? -28.091 8.711   12.163  1.00 44.31  ? 107 THR A CG2 1 
ATOM   812  N N   . GLU A 1 108 ? -25.332 12.278  10.332  1.00 42.82  ? 108 GLU A N   1 
ATOM   813  C CA  . GLU A 1 108 ? -25.224 13.674  9.829   1.00 41.65  ? 108 GLU A CA  1 
ATOM   814  C C   . GLU A 1 108 ? -24.113 13.886  8.801   1.00 36.87  ? 108 GLU A C   1 
ATOM   815  O O   . GLU A 1 108 ? -22.970 13.532  9.090   1.00 33.26  ? 108 GLU A O   1 
ATOM   816  C CB  . GLU A 1 108 ? -25.020 14.646  10.987  1.00 43.83  ? 108 GLU A CB  1 
ATOM   817  C CG  . GLU A 1 108 ? -26.154 14.647  11.993  1.00 51.63  ? 108 GLU A CG  1 
ATOM   818  C CD  . GLU A 1 108 ? -26.238 15.914  12.826  1.00 57.53  ? 108 GLU A CD  1 
ATOM   819  O OE1 . GLU A 1 108 ? -25.497 16.869  12.524  1.00 52.49  ? 108 GLU A OE1 1 
ATOM   820  O OE2 . GLU A 1 108 ? -27.047 15.942  13.768  1.00 62.59  ? 108 GLU A OE2 1 
ATOM   821  N N   . MET A 1 109 ? -24.453 14.501  7.667   1.00 38.39  ? 109 MET A N   1 
ATOM   822  C CA  . MET A 1 109 ? -23.450 14.825  6.650   1.00 34.02  ? 109 MET A CA  1 
ATOM   823  C C   . MET A 1 109 ? -22.741 16.063  7.209   1.00 36.70  ? 109 MET A C   1 
ATOM   824  O O   . MET A 1 109 ? -23.357 17.107  7.404   1.00 40.38  ? 109 MET A O   1 
ATOM   825  C CB  . MET A 1 109 ? -24.127 15.106  5.292   1.00 39.88  ? 109 MET A CB  1 
ATOM   826  C CG  . MET A 1 109 ? -23.132 15.393  4.148   1.00 38.14  ? 109 MET A CG  1 
ATOM   827  S SD  . MET A 1 109 ? -22.100 13.991  3.617   1.00 38.73  ? 109 MET A SD  1 
ATOM   828  C CE  . MET A 1 109 ? -23.339 12.676  3.582   1.00 37.78  ? 109 MET A CE  1 
ATOM   829  N N   . THR A 1 110 ? -21.477 15.901  7.559   1.00 31.96  ? 110 THR A N   1 
ATOM   830  C CA  . THR A 1 110 ? -20.683 16.881  8.269   1.00 33.65  ? 110 THR A CA  1 
ATOM   831  C C   . THR A 1 110 ? -19.600 17.467  7.376   1.00 33.23  ? 110 THR A C   1 
ATOM   832  O O   . THR A 1 110 ? -18.794 16.722  6.834   1.00 29.31  ? 110 THR A O   1 
ATOM   833  C CB  . THR A 1 110 ? -19.996 16.143  9.451   1.00 32.31  ? 110 THR A CB  1 
ATOM   834  O OG1 . THR A 1 110 ? -20.943 15.329  10.169  1.00 34.73  ? 110 THR A OG1 1 
ATOM   835  C CG2 . THR A 1 110 ? -19.237 17.080  10.381  1.00 32.51  ? 110 THR A CG2 1 
ATOM   836  N N   . LEU A 1 111 ? -19.524 18.788  7.315   1.00 32.65  ? 111 LEU A N   1 
ATOM   837  C CA  . LEU A 1 111 ? -18.535 19.516  6.547   1.00 34.33  ? 111 LEU A CA  1 
ATOM   838  C C   . LEU A 1 111 ? -17.145 19.314  7.140   1.00 36.94  ? 111 LEU A C   1 
ATOM   839  O O   . LEU A 1 111 ? -16.959 19.580  8.329   1.00 29.82  ? 111 LEU A O   1 
ATOM   840  C CB  . LEU A 1 111 ? -18.886 21.000  6.588   1.00 34.02  ? 111 LEU A CB  1 
ATOM   841  C CG  . LEU A 1 111 ? -17.935 21.910  5.791   1.00 36.74  ? 111 LEU A CG  1 
ATOM   842  C CD1 . LEU A 1 111 ? -18.195 21.762  4.319   1.00 33.08  ? 111 LEU A CD1 1 
ATOM   843  C CD2 . LEU A 1 111 ? -18.121 23.364  6.185   1.00 41.07  ? 111 LEU A CD2 1 
ATOM   844  N N   . THR A 1 112 ? -16.178 18.833  6.351   1.00 24.78  ? 112 THR A N   1 
ATOM   845  C CA  . THR A 1 112 ? -14.824 18.614  6.847   1.00 33.67  ? 112 THR A CA  1 
ATOM   846  C C   . THR A 1 112 ? -13.839 19.622  6.274   1.00 36.53  ? 112 THR A C   1 
ATOM   847  O O   . THR A 1 112 ? -12.845 19.929  6.925   1.00 38.52  ? 112 THR A O   1 
ATOM   848  C CB  . THR A 1 112 ? -14.373 17.158  6.669   1.00 38.23  ? 112 THR A CB  1 
ATOM   849  O OG1 . THR A 1 112 ? -14.398 16.799  5.295   1.00 33.50  ? 112 THR A OG1 1 
ATOM   850  C CG2 . THR A 1 112 ? -15.237 16.179  7.468   1.00 34.13  ? 112 THR A CG2 1 
ATOM   851  N N   . SER A 1 113 ? -14.118 20.169  5.089   1.00 38.41  ? 113 SER A N   1 
ATOM   852  C CA  . SER A 1 113 ? -13.264 21.197  4.504   1.00 34.86  ? 113 SER A CA  1 
ATOM   853  C C   . SER A 1 113 ? -13.963 21.973  3.394   1.00 34.91  ? 113 SER A C   1 
ATOM   854  O O   . SER A 1 113 ? -15.077 21.650  2.999   1.00 29.70  ? 113 SER A O   1 
ATOM   855  C CB  . SER A 1 113 ? -11.914 20.637  4.051   1.00 35.80  ? 113 SER A CB  1 
ATOM   856  O OG  . SER A 1 113 ? -12.014 19.597  3.093   1.00 41.63  ? 113 SER A OG  1 
ATOM   857  N N   . GLN A 1 114 ? -13.332 23.053  2.962   1.00 36.78  ? 114 GLN A N   1 
ATOM   858  C CA  . GLN A 1 114 ? -13.803 23.887  1.874   1.00 38.38  ? 114 GLN A CA  1 
ATOM   859  C C   . GLN A 1 114 ? -12.661 24.787  1.437   1.00 37.18  ? 114 GLN A C   1 
ATOM   860  O O   . GLN A 1 114 ? -11.639 24.876  2.112   1.00 36.61  ? 114 GLN A O   1 
ATOM   861  C CB  . GLN A 1 114 ? -15.066 24.702  2.247   1.00 40.60  ? 114 GLN A CB  1 
ATOM   862  C CG  . GLN A 1 114 ? -14.787 25.966  3.036   1.00 48.61  ? 114 GLN A CG  1 
ATOM   863  C CD  . GLN A 1 114 ? -15.288 25.843  4.439   1.00 53.34  ? 114 GLN A CD  1 
ATOM   864  O OE1 . GLN A 1 114 ? -14.729 25.113  5.265   1.00 55.69  ? 114 GLN A OE1 1 
ATOM   865  N NE2 . GLN A 1 114 ? -16.352 26.576  4.745   1.00 57.94  ? 114 GLN A NE2 1 
ATOM   866  N N   . GLY A 1 115 ? -12.842 25.441  0.306   1.00 39.50  ? 115 GLY A N   1 
ATOM   867  C CA  . GLY A 1 115 ? -11.832 26.338  -0.213  1.00 40.43  ? 115 GLY A CA  1 
ATOM   868  C C   . GLY A 1 115 ? -12.339 27.214  -1.320  1.00 40.08  ? 115 GLY A C   1 
ATOM   869  O O   . GLY A 1 115 ? -13.402 26.970  -1.888  1.00 37.54  ? 115 GLY A O   1 
ATOM   870  N N   . LYS A 1 116 ? -11.580 28.255  -1.614  1.00 41.58  ? 116 LYS A N   1 
ATOM   871  C CA  . LYS A 1 116 ? -11.896 29.180  -2.681  1.00 41.30  ? 116 LYS A CA  1 
ATOM   872  C C   . LYS A 1 116 ? -10.810 29.077  -3.776  1.00 41.71  ? 116 LYS A C   1 
ATOM   873  O O   . LYS A 1 116 ? -9.760  28.481  -3.554  1.00 42.93  ? 116 LYS A O   1 
ATOM   874  C CB  . LYS A 1 116 ? -12.007 30.603  -2.103  1.00 42.25  ? 116 LYS A CB  1 
ATOM   875  C CG  . LYS A 1 116 ? -13.083 30.749  -1.026  1.00 44.13  ? 116 LYS A CG  1 
ATOM   876  C CD  . LYS A 1 116 ? -14.454 30.275  -1.506  1.00 45.03  ? 116 LYS A CD  1 
ATOM   877  C CE  . LYS A 1 116 ? -15.521 30.424  -0.444  1.00 47.88  ? 116 LYS A CE  1 
ATOM   878  N NZ  . LYS A 1 116 ? -15.241 29.549  0.724   1.00 51.37  ? 116 LYS A NZ  1 
ATOM   879  N N   . GLY A 1 117 ? -11.069 29.643  -4.941  1.00 40.71  ? 117 GLY A N   1 
ATOM   880  C CA  . GLY A 1 117 ? -10.087 29.681  -6.017  1.00 42.02  ? 117 GLY A CA  1 
ATOM   881  C C   . GLY A 1 117 ? -10.027 28.412  -6.839  1.00 41.70  ? 117 GLY A C   1 
ATOM   882  O O   . GLY A 1 117 ? -10.996 27.652  -6.886  1.00 38.60  ? 117 GLY A O   1 
ATOM   883  N N   . SER A 1 118 ? -8.877  28.160  -7.467  1.00 38.99  ? 118 SER A N   1 
ATOM   884  C CA  . SER A 1 118 ? -8.720  27.020  -8.344  1.00 38.42  ? 118 SER A CA  1 
ATOM   885  C C   . SER A 1 118 ? -8.165  25.769  -7.664  1.00 39.84  ? 118 SER A C   1 
ATOM   886  O O   . SER A 1 118 ? -7.198  25.846  -6.898  1.00 37.70  ? 118 SER A O   1 
ATOM   887  C CB  . SER A 1 118 ? -7.886  27.396  -9.559  1.00 41.26  ? 118 SER A CB  1 
ATOM   888  O OG  . SER A 1 118 ? -8.112  26.435  -10.578 1.00 46.68  ? 118 SER A OG  1 
ATOM   889  N N   . ASN A 1 119 ? -8.788  24.602  -7.959  1.00 36.38  ? 119 ASN A N   1 
ATOM   890  C CA  . ASN A 1 119 ? -8.448  23.324  -7.342  1.00 36.05  ? 119 ASN A CA  1 
ATOM   891  C C   . ASN A 1 119 ? -8.783  22.091  -8.208  1.00 33.71  ? 119 ASN A C   1 
ATOM   892  O O   . ASN A 1 119 ? -9.688  22.114  -9.026  1.00 31.94  ? 119 ASN A O   1 
ATOM   893  C CB  . ASN A 1 119 ? -9.243  23.178  -6.021  1.00 35.18  ? 119 ASN A CB  1 
ATOM   894  C CG  . ASN A 1 119 ? -8.880  24.146  -4.911  1.00 38.72  ? 119 ASN A CG  1 
ATOM   895  O OD1 . ASN A 1 119 ? -7.880  23.971  -4.221  1.00 43.92  ? 119 ASN A OD1 1 
ATOM   896  N ND2 . ASN A 1 119 ? -9.702  25.167  -4.687  1.00 40.85  ? 119 ASN A ND2 1 
ATOM   897  N N   . PHE A 1 120 ? -8.086  20.999  -7.967  1.00 32.25  ? 120 PHE A N   1 
ATOM   898  C CA  . PHE A 1 120 ? -8.389  19.709  -8.565  1.00 32.94  ? 120 PHE A CA  1 
ATOM   899  C C   . PHE A 1 120 ? -8.576  18.766  -7.386  1.00 33.55  ? 120 PHE A C   1 
ATOM   900  O O   . PHE A 1 120 ? -7.702  18.684  -6.520  1.00 31.11  ? 120 PHE A O   1 
ATOM   901  C CB  . PHE A 1 120 ? -7.287  19.199  -9.504  1.00 33.97  ? 120 PHE A CB  1 
ATOM   902  C CG  . PHE A 1 120 ? -7.487  17.748  -9.925  1.00 32.95  ? 120 PHE A CG  1 
ATOM   903  C CD1 . PHE A 1 120 ? -8.350  17.422  -10.954 1.00 29.83  ? 120 PHE A CD1 1 
ATOM   904  C CD2 . PHE A 1 120 ? -6.826  16.722  -9.275  1.00 33.32  ? 120 PHE A CD2 1 
ATOM   905  C CE1 . PHE A 1 120 ? -8.531  16.100  -11.343 1.00 31.79  ? 120 PHE A CE1 1 
ATOM   906  C CE2 . PHE A 1 120 ? -7.024  15.391  -9.654  1.00 33.84  ? 120 PHE A CE2 1 
ATOM   907  C CZ  . PHE A 1 120 ? -7.871  15.091  -10.693 1.00 30.71  ? 120 PHE A CZ  1 
ATOM   908  N N   . ILE A 1 121 ? -9.718  18.077  -7.337  1.00 29.68  ? 121 ILE A N   1 
ATOM   909  C CA  . ILE A 1 121 ? -10.012 17.197  -6.167  1.00 32.08  ? 121 ILE A CA  1 
ATOM   910  C C   . ILE A 1 121 ? -10.321 15.785  -6.669  1.00 31.21  ? 121 ILE A C   1 
ATOM   911  O O   . ILE A 1 121 ? -11.236 15.643  -7.499  1.00 25.88  ? 121 ILE A O   1 
ATOM   912  C CB  . ILE A 1 121 ? -11.168 17.783  -5.334  1.00 30.40  ? 121 ILE A CB  1 
ATOM   913  C CG1 . ILE A 1 121 ? -10.881 19.231  -4.935  1.00 34.44  ? 121 ILE A CG1 1 
ATOM   914  C CG2 . ILE A 1 121 ? -11.459 16.916  -4.120  1.00 29.72  ? 121 ILE A CG2 1 
ATOM   915  C CD1 . ILE A 1 121 ? -12.054 19.926  -4.313  1.00 33.33  ? 121 ILE A CD1 1 
ATOM   916  N N   . ALA A 1 122 ? -9.581  14.787  -6.177  1.00 30.12  ? 122 ALA A N   1 
ATOM   917  C CA  . ALA A 1 122 ? -9.803  13.389  -6.608  1.00 28.37  ? 122 ALA A CA  1 
ATOM   918  C C   . ALA A 1 122 ? -10.322 12.553  -5.436  1.00 32.82  ? 122 ALA A C   1 
ATOM   919  O O   . ALA A 1 122 ? -9.666  12.548  -4.378  1.00 32.57  ? 122 ALA A O   1 
ATOM   920  C CB  . ALA A 1 122 ? -8.527  12.814  -7.172  1.00 27.72  ? 122 ALA A CB  1 
ATOM   921  N N   . PHE A 1 123 ? -11.456 11.874  -5.622  1.00 27.26  ? 123 PHE A N   1 
ATOM   922  C CA  . PHE A 1 123 ? -11.999 10.967  -4.579  1.00 31.61  ? 123 PHE A CA  1 
ATOM   923  C C   . PHE A 1 123 ? -11.815 9.544   -5.105  1.00 34.59  ? 123 PHE A C   1 
ATOM   924  O O   . PHE A 1 123 ? -12.295 9.264   -6.213  1.00 34.38  ? 123 PHE A O   1 
ATOM   925  C CB  . PHE A 1 123 ? -13.506 11.179  -4.414  1.00 30.52  ? 123 PHE A CB  1 
ATOM   926  C CG  . PHE A 1 123 ? -13.941 12.321  -3.530  1.00 31.22  ? 123 PHE A CG  1 
ATOM   927  C CD1 . PHE A 1 123 ? -13.185 13.476  -3.418  1.00 37.22  ? 123 PHE A CD1 1 
ATOM   928  C CD2 . PHE A 1 123 ? -15.133 12.247  -2.827  1.00 34.03  ? 123 PHE A CD2 1 
ATOM   929  C CE1 . PHE A 1 123 ? -13.603 14.521  -2.609  1.00 36.86  ? 123 PHE A CE1 1 
ATOM   930  C CE2 . PHE A 1 123 ? -15.551 13.294  -2.022  1.00 35.23  ? 123 PHE A CE2 1 
ATOM   931  C CZ  . PHE A 1 123 ? -14.782 14.428  -1.910  1.00 34.86  ? 123 PHE A CZ  1 
ATOM   932  N N   . GLY A 1 124 ? -11.147 8.681   -4.340  1.00 32.67  ? 124 GLY A N   1 
ATOM   933  C CA  . GLY A 1 124 ? -10.985 7.280   -4.771  1.00 40.92  ? 124 GLY A CA  1 
ATOM   934  C C   . GLY A 1 124 ? -10.068 6.509   -3.846  1.00 46.17  ? 124 GLY A C   1 
ATOM   935  O O   . GLY A 1 124 ? -9.669  7.073   -2.809  1.00 44.04  ? 124 GLY A O   1 
ATOM   936  N N   . ASN A 1 125 ? -9.761  5.257   -4.191  1.00 43.45  ? 125 ASN A N   1 
ATOM   937  C CA  . ASN A 1 125 ? -8.794  4.479   -3.400  1.00 48.33  ? 125 ASN A CA  1 
ATOM   938  C C   . ASN A 1 125 ? -7.390  5.096   -3.678  1.00 44.03  ? 125 ASN A C   1 
ATOM   939  O O   . ASN A 1 125 ? -7.253  5.939   -4.578  1.00 37.55  ? 125 ASN A O   1 
ATOM   940  C CB  . ASN A 1 125 ? -8.869  2.977   -3.705  1.00 48.44  ? 125 ASN A CB  1 
ATOM   941  C CG  . ASN A 1 125 ? -8.602  2.633   -5.130  1.00 43.26  ? 125 ASN A CG  1 
ATOM   942  O OD1 . ASN A 1 125 ? -7.541  2.929   -5.655  1.00 43.03  ? 125 ASN A OD1 1 
ATOM   943  N ND2 . ASN A 1 125 ? -9.558  1.984   -5.793  1.00 43.70  ? 125 ASN A ND2 1 
ATOM   944  N N   . GLU A 1 126 ? -6.349  4.696   -2.922  1.00 41.00  ? 126 GLU A N   1 
ATOM   945  C CA  . GLU A 1 126 ? -5.009  5.269   -3.118  1.00 44.33  ? 126 GLU A CA  1 
ATOM   946  C C   . GLU A 1 126 ? -4.504  5.122   -4.564  1.00 42.23  ? 126 GLU A C   1 
ATOM   947  O O   . GLU A 1 126 ? -3.941  6.077   -5.097  1.00 39.62  ? 126 GLU A O   1 
ATOM   948  C CB  . GLU A 1 126 ? -3.971  4.759   -2.089  1.00 46.31  ? 126 GLU A CB  1 
ATOM   949  C CG  . GLU A 1 126 ? -4.050  5.422   -0.718  1.00 52.99  ? 126 GLU A CG  1 
ATOM   950  C CD  . GLU A 1 126 ? -4.074  6.943   -0.638  1.00 56.35  ? 126 GLU A CD  1 
ATOM   951  O OE1 . GLU A 1 126 ? -3.155  7.602   -1.180  1.00 58.12  ? 126 GLU A OE1 1 
ATOM   952  O OE2 . GLU A 1 126 ? -5.003  7.477   0.012   1.00 55.86  ? 126 GLU A OE2 1 
ATOM   953  N N   . PHE A 1 127 ? -4.814  4.007   -5.230  1.00 40.45  ? 127 PHE A N   1 
ATOM   954  C CA  . PHE A 1 127 ? -4.402  3.803   -6.614  1.00 39.47  ? 127 PHE A CA  1 
ATOM   955  C C   . PHE A 1 127 ? -5.104  4.757   -7.620  1.00 39.85  ? 127 PHE A C   1 
ATOM   956  O O   . PHE A 1 127 ? -4.417  5.454   -8.380  1.00 40.18  ? 127 PHE A O   1 
ATOM   957  C CB  . PHE A 1 127 ? -4.589  2.327   -7.018  1.00 42.91  ? 127 PHE A CB  1 
ATOM   958  C CG  . PHE A 1 127 ? -4.177  1.973   -8.427  1.00 38.50  ? 127 PHE A CG  1 
ATOM   959  C CD1 . PHE A 1 127 ? -2.846  1.758   -8.745  1.00 43.41  ? 127 PHE A CD1 1 
ATOM   960  C CD2 . PHE A 1 127 ? -5.119  1.860   -9.434  1.00 38.74  ? 127 PHE A CD2 1 
ATOM   961  C CE1 . PHE A 1 127 ? -2.467  1.433   -10.039 1.00 38.25  ? 127 PHE A CE1 1 
ATOM   962  C CE2 . PHE A 1 127 ? -4.738  1.563   -10.734 1.00 39.01  ? 127 PHE A CE2 1 
ATOM   963  C CZ  . PHE A 1 127 ? -3.412  1.328   -11.027 1.00 39.06  ? 127 PHE A CZ  1 
ATOM   964  N N   . THR A 1 128 ? -6.460  4.770   -7.643  1.00 36.67  ? 128 THR A N   1 
ATOM   965  C CA  . THR A 1 128 ? -7.203  5.615   -8.581  1.00 39.93  ? 128 THR A CA  1 
ATOM   966  C C   . THR A 1 128 ? -6.893  7.101   -8.363  1.00 36.21  ? 128 THR A C   1 
ATOM   967  O O   . THR A 1 128 ? -6.785  7.833   -9.334  1.00 35.92  ? 128 THR A O   1 
ATOM   968  C CB  . THR A 1 128 ? -8.711  5.293   -8.585  1.00 36.50  ? 128 THR A CB  1 
ATOM   969  O OG1 . THR A 1 128 ? -9.304  5.690   -7.360  1.00 37.23  ? 128 THR A OG1 1 
ATOM   970  C CG2 . THR A 1 128 ? -8.991  3.827   -8.875  1.00 36.81  ? 128 THR A CG2 1 
ATOM   971  N N   . LYS A 1 129 ? -6.666  7.519   -7.110  1.00 37.36  ? 129 LYS A N   1 
ATOM   972  C CA  . LYS A 1 129 ? -6.294  8.894   -6.805  1.00 37.46  ? 129 LYS A CA  1 
ATOM   973  C C   . LYS A 1 129 ? -4.931  9.258   -7.386  1.00 39.41  ? 129 LYS A C   1 
ATOM   974  O O   . LYS A 1 129 ? -4.811  10.319  -7.975  1.00 35.72  ? 129 LYS A O   1 
ATOM   975  C CB  . LYS A 1 129 ? -6.262  9.149   -5.299  1.00 37.20  ? 129 LYS A CB  1 
ATOM   976  C CG  . LYS A 1 129 ? -7.625  9.160   -4.640  1.00 37.65  ? 129 LYS A CG  1 
ATOM   977  C CD  . LYS A 1 129 ? -7.492  9.667   -3.206  1.00 40.03  ? 129 LYS A CD  1 
ATOM   978  C CE  . LYS A 1 129 ? -6.720  8.698   -2.335  1.00 44.50  ? 129 LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 129 ? -5.777  9.419   -1.431  1.00 50.48  ? 129 LYS A NZ  1 
ATOM   980  N N   . GLN A 1 130 ? -3.907  8.392   -7.227  1.00 39.64  ? 130 GLN A N   1 
ATOM   981  C CA  . GLN A 1 130 ? -2.568  8.696   -7.744  1.00 38.40  ? 130 GLN A CA  1 
ATOM   982  C C   . GLN A 1 130 ? -2.567  8.732   -9.268  1.00 38.08  ? 130 GLN A C   1 
ATOM   983  O O   . GLN A 1 130 ? -1.896  9.576   -9.853  1.00 35.94  ? 130 GLN A O   1 
ATOM   984  C CB  . GLN A 1 130 ? -1.511  7.701   -7.212  1.00 42.69  ? 130 GLN A CB  1 
ATOM   985  C CG  . GLN A 1 130 ? -0.044  8.085   -7.536  1.00 53.34  ? 130 GLN A CG  1 
ATOM   986  C CD  . GLN A 1 130 ? 0.324   9.543   -7.232  1.00 58.75  ? 130 GLN A CD  1 
ATOM   987  O OE1 . GLN A 1 130 ? 0.464   10.402  -8.145  1.00 54.17  ? 130 GLN A OE1 1 
ATOM   988  N NE2 . GLN A 1 130 ? 0.492   9.858   -5.941  1.00 59.58  ? 130 GLN A NE2 1 
ATOM   989  N N   . VAL A 1 131 ? -3.335  7.844   -9.905  1.00 36.74  ? 131 VAL A N   1 
ATOM   990  C CA  . VAL A 1 131 ? -3.401  7.784   -11.367 1.00 36.38  ? 131 VAL A CA  1 
ATOM   991  C C   . VAL A 1 131 ? -4.085  9.049   -11.923 1.00 37.33  ? 131 VAL A C   1 
ATOM   992  O O   . VAL A 1 131 ? -3.570  9.665   -12.850 1.00 32.83  ? 131 VAL A O   1 
ATOM   993  C CB  . VAL A 1 131 ? -4.085  6.466   -11.841 1.00 38.96  ? 131 VAL A CB  1 
ATOM   994  C CG1 . VAL A 1 131 ? -4.457  6.518   -13.327 1.00 35.06  ? 131 VAL A CG1 1 
ATOM   995  C CG2 . VAL A 1 131 ? -3.193  5.259   -11.563 1.00 35.42  ? 131 VAL A CG2 1 
ATOM   996  N N   . ALA A 1 132 ? -5.224  9.462   -11.327 1.00 37.42  ? 132 ALA A N   1 
ATOM   997  C CA  . ALA A 1 132 ? -5.939  10.646  -11.794 1.00 34.30  ? 132 ALA A CA  1 
ATOM   998  C C   . ALA A 1 132 ? -5.110  11.902  -11.535 1.00 37.70  ? 132 ALA A C   1 
ATOM   999  O O   . ALA A 1 132 ? -5.065  12.767  -12.397 1.00 33.45  ? 132 ALA A O   1 
ATOM   1000 C CB  . ALA A 1 132 ? -7.295  10.766  -11.112 1.00 30.60  ? 132 ALA A CB  1 
ATOM   1001 N N   . ASN A 1 133 ? -4.463  11.990  -10.361 1.00 34.21  ? 133 ASN A N   1 
ATOM   1002 C CA  . ASN A 1 133 ? -3.621  13.123  -10.030 1.00 37.46  ? 133 ASN A CA  1 
ATOM   1003 C C   . ASN A 1 133 ? -2.453  13.224  -11.027 1.00 38.70  ? 133 ASN A C   1 
ATOM   1004 O O   . ASN A 1 133 ? -2.134  14.333  -11.469 1.00 35.21  ? 133 ASN A O   1 
ATOM   1005 C CB  . ASN A 1 133 ? -3.095  13.018  -8.605  1.00 39.77  ? 133 ASN A CB  1 
ATOM   1006 C CG  . ASN A 1 133 ? -2.186  14.161  -8.221  1.00 43.65  ? 133 ASN A CG  1 
ATOM   1007 O OD1 . ASN A 1 133 ? -2.556  15.345  -8.299  1.00 45.01  ? 133 ASN A OD1 1 
ATOM   1008 N ND2 . ASN A 1 133 ? -0.962  13.827  -7.852  1.00 44.11  ? 133 ASN A ND2 1 
ATOM   1009 N N   . LYS A 1 134 ? -1.837  12.077  -11.382 1.00 37.56  ? 134 LYS A N   1 
ATOM   1010 C CA  . LYS A 1 134 ? -0.757  12.054  -12.359 1.00 39.63  ? 134 LYS A CA  1 
ATOM   1011 C C   . LYS A 1 134 ? -1.246  12.514  -13.737 1.00 39.98  ? 134 LYS A C   1 
ATOM   1012 O O   . LYS A 1 134 ? -0.619  13.362  -14.344 1.00 36.94  ? 134 LYS A O   1 
ATOM   1013 C CB  . LYS A 1 134 ? -0.105  10.667  -12.450 1.00 38.85  ? 134 LYS A CB  1 
ATOM   1014 C CG  . LYS A 1 134 ? 1.242   10.702  -13.172 1.00 38.89  ? 134 LYS A CG  1 
ATOM   1015 C CD  . LYS A 1 134 ? 1.603   9.342   -13.775 1.00 44.58  ? 134 LYS A CD  1 
ATOM   1016 C CE  . LYS A 1 134 ? 2.665   9.449   -14.851 1.00 48.29  ? 134 LYS A CE  1 
ATOM   1017 N NZ  . LYS A 1 134 ? 3.566   8.253   -14.869 1.00 52.31  ? 134 LYS A NZ  1 
ATOM   1018 N N   . CYS A 1 135 ? -2.385  11.986  -14.212 1.00 34.99  ? 135 CYS A N   1 
ATOM   1019 C CA  . CYS A 1 135 ? -2.971  12.414  -15.474 1.00 35.14  ? 135 CYS A CA  1 
ATOM   1020 C C   . CYS A 1 135 ? -3.288  13.925  -15.463 1.00 38.35  ? 135 CYS A C   1 
ATOM   1021 O O   . CYS A 1 135 ? -2.937  14.602  -16.426 1.00 37.16  ? 135 CYS A O   1 
ATOM   1022 C CB  . CYS A 1 135 ? -4.199  11.576  -15.828 1.00 36.99  ? 135 CYS A CB  1 
ATOM   1023 S SG  . CYS A 1 135 ? -4.811  11.822  -17.520 1.00 44.07  ? 135 CYS A SG  1 
ATOM   1024 N N   . PHE A 1 136 ? -3.900  14.469  -14.383 1.00 34.39  ? 136 PHE A N   1 
ATOM   1025 C CA  . PHE A 1 136 ? -4.195  15.913  -14.331 1.00 38.46  ? 136 PHE A CA  1 
ATOM   1026 C C   . PHE A 1 136 ? -2.931  16.787  -14.427 1.00 39.61  ? 136 PHE A C   1 
ATOM   1027 O O   . PHE A 1 136 ? -2.856  17.642  -15.308 1.00 34.72  ? 136 PHE A O   1 
ATOM   1028 C CB  . PHE A 1 136 ? -4.997  16.303  -13.079 1.00 35.73  ? 136 PHE A CB  1 
ATOM   1029 C CG  . PHE A 1 136 ? -5.558  17.700  -13.173 1.00 36.44  ? 136 PHE A CG  1 
ATOM   1030 C CD1 . PHE A 1 136 ? -6.719  17.953  -13.886 1.00 37.24  ? 136 PHE A CD1 1 
ATOM   1031 C CD2 . PHE A 1 136 ? -4.908  18.768  -12.573 1.00 35.29  ? 136 PHE A CD2 1 
ATOM   1032 C CE1 . PHE A 1 136 ? -7.233  19.246  -13.968 1.00 36.99  ? 136 PHE A CE1 1 
ATOM   1033 C CE2 . PHE A 1 136 ? -5.420  20.052  -12.669 1.00 36.29  ? 136 PHE A CE2 1 
ATOM   1034 C CZ  . PHE A 1 136 ? -6.580  20.280  -13.356 1.00 39.75  ? 136 PHE A CZ  1 
ATOM   1035 N N   . LYS A 1 137 ? -1.950  16.573  -13.528 1.00 37.48  ? 137 LYS A N   1 
ATOM   1036 C CA  . LYS A 1 137 ? -0.687  17.331  -13.514 1.00 41.43  ? 137 LYS A CA  1 
ATOM   1037 C C   . LYS A 1 137 ? 0.039   17.259  -14.858 1.00 42.38  ? 137 LYS A C   1 
ATOM   1038 O O   . LYS A 1 137 ? 0.655   18.236  -15.282 1.00 41.51  ? 137 LYS A O   1 
ATOM   1039 C CB  . LYS A 1 137 ? 0.235   16.848  -12.381 1.00 43.41  ? 137 LYS A CB  1 
ATOM   1040 C CG  . LYS A 1 137 ? -0.152  17.391  -11.019 1.00 43.35  ? 137 LYS A CG  1 
ATOM   1041 C CD  . LYS A 1 137 ? 0.916   17.105  -9.970  1.00 48.10  ? 137 LYS A CD  1 
ATOM   1042 C CE  . LYS A 1 137 ? 0.298   16.782  -8.625  1.00 53.76  ? 137 LYS A CE  1 
ATOM   1043 N NZ  . LYS A 1 137 ? 1.307   16.331  -7.614  1.00 49.09  ? 137 LYS A NZ  1 
ATOM   1044 N N   . ASP A 1 138 ? -0.060  16.115  -15.536 1.00 40.55  ? 138 ASP A N   1 
ATOM   1045 C CA  . ASP A 1 138 ? 0.560   15.926  -16.840 1.00 43.37  ? 138 ASP A CA  1 
ATOM   1046 C C   . ASP A 1 138 ? -0.067  16.753  -17.955 1.00 39.89  ? 138 ASP A C   1 
ATOM   1047 O O   . ASP A 1 138 ? 0.661   17.179  -18.844 1.00 44.52  ? 138 ASP A O   1 
ATOM   1048 C CB  . ASP A 1 138 ? 0.543   14.446  -17.249 1.00 44.07  ? 138 ASP A CB  1 
ATOM   1049 C CG  . ASP A 1 138 ? 1.664   13.605  -16.652 1.00 55.38  ? 138 ASP A CG  1 
ATOM   1050 O OD1 . ASP A 1 138 ? 2.255   14.039  -15.623 1.00 58.91  ? 138 ASP A OD1 1 
ATOM   1051 O OD2 . ASP A 1 138 ? 1.932   12.506  -17.190 1.00 53.88  ? 138 ASP A OD2 1 
ATOM   1052 N N   . ASN A 1 139 ? -1.395  16.965  -17.946 1.00 40.32  ? 139 ASN A N   1 
ATOM   1053 C CA  . ASN A 1 139 ? -2.039  17.667  -19.060 1.00 41.97  ? 139 ASN A CA  1 
ATOM   1054 C C   . ASN A 1 139 ? -2.480  19.104  -18.773 1.00 43.55  ? 139 ASN A C   1 
ATOM   1055 O O   . ASN A 1 139 ? -2.587  19.906  -19.710 1.00 44.23  ? 139 ASN A O   1 
ATOM   1056 C CB  . ASN A 1 139 ? -3.190  16.844  -19.585 1.00 40.37  ? 139 ASN A CB  1 
ATOM   1057 C CG  . ASN A 1 139 ? -2.705  15.523  -20.116 1.00 39.79  ? 139 ASN A CG  1 
ATOM   1058 O OD1 . ASN A 1 139 ? -2.141  15.430  -21.220 1.00 42.21  ? 139 ASN A OD1 1 
ATOM   1059 N ND2 . ASN A 1 139 ? -2.864  14.476  -19.333 1.00 38.42  ? 139 ASN A ND2 1 
ATOM   1060 N N   . TRP A 1 140 ? -2.685  19.454  -17.507 1.00 40.60  ? 140 TRP A N   1 
ATOM   1061 C CA  . TRP A 1 140 ? -3.111  20.799  -17.154 1.00 42.33  ? 140 TRP A CA  1 
ATOM   1062 C C   . TRP A 1 140 ? -2.009  21.821  -17.320 1.00 45.68  ? 140 TRP A C   1 
ATOM   1063 O O   . TRP A 1 140 ? -0.875  21.599  -16.893 1.00 46.86  ? 140 TRP A O   1 
ATOM   1064 C CB  . TRP A 1 140 ? -3.656  20.853  -15.725 1.00 41.20  ? 140 TRP A CB  1 
ATOM   1065 C CG  . TRP A 1 140 ? -4.291  22.161  -15.394 1.00 44.15  ? 140 TRP A CG  1 
ATOM   1066 C CD1 . TRP A 1 140 ? -3.753  23.171  -14.659 1.00 42.66  ? 140 TRP A CD1 1 
ATOM   1067 C CD2 . TRP A 1 140 ? -5.567  22.624  -15.841 1.00 43.67  ? 140 TRP A CD2 1 
ATOM   1068 N NE1 . TRP A 1 140 ? -4.639  24.214  -14.574 1.00 44.28  ? 140 TRP A NE1 1 
ATOM   1069 C CE2 . TRP A 1 140 ? -5.751  23.917  -15.318 1.00 42.77  ? 140 TRP A CE2 1 
ATOM   1070 C CE3 . TRP A 1 140 ? -6.595  22.053  -16.600 1.00 43.14  ? 140 TRP A CE3 1 
ATOM   1071 C CZ2 . TRP A 1 140 ? -6.900  24.667  -15.563 1.00 42.80  ? 140 TRP A CZ2 1 
ATOM   1072 C CZ3 . TRP A 1 140 ? -7.742  22.792  -16.828 1.00 44.35  ? 140 TRP A CZ3 1 
ATOM   1073 C CH2 . TRP A 1 140 ? -7.888  24.078  -16.306 1.00 41.56  ? 140 TRP A CH2 1 
ATOM   1074 N N   . THR A 1 141 ? -2.362  22.958  -17.910 1.00 46.68  ? 141 THR A N   1 
ATOM   1075 C CA  . THR A 1 141 ? -1.469  24.105  -18.078 1.00 49.48  ? 141 THR A CA  1 
ATOM   1076 C C   . THR A 1 141 ? -2.063  25.302  -17.324 1.00 51.53  ? 141 THR A C   1 
ATOM   1077 O O   . THR A 1 141 ? -3.291  25.404  -17.194 1.00 48.30  ? 141 THR A O   1 
ATOM   1078 C CB  . THR A 1 141 ? -1.195  24.382  -19.566 1.00 47.16  ? 141 THR A CB  1 
ATOM   1079 O OG1 . THR A 1 141 ? -2.403  24.807  -20.207 1.00 48.14  ? 141 THR A OG1 1 
ATOM   1080 C CG2 . THR A 1 141 ? -0.652  23.160  -20.283 1.00 44.62  ? 141 THR A CG2 1 
ATOM   1081 N N   . LYS A 1 142 ? -1.194  26.198  -16.819 1.00 53.47  ? 142 LYS A N   1 
ATOM   1082 C CA  . LYS A 1 142 ? -1.573  27.365  -16.025 1.00 54.59  ? 142 LYS A CA  1 
ATOM   1083 C C   . LYS A 1 142 ? -2.764  28.181  -16.561 1.00 55.40  ? 142 LYS A C   1 
ATOM   1084 O O   . LYS A 1 142 ? -3.657  28.502  -15.764 1.00 57.46  ? 142 LYS A O   1 
ATOM   1085 C CB  . LYS A 1 142 ? -0.376  28.306  -15.790 1.00 59.01  ? 142 LYS A CB  1 
ATOM   1086 C CG  . LYS A 1 142 ? 0.870   27.656  -15.177 1.00 59.51  ? 142 LYS A CG  1 
ATOM   1087 C CD  . LYS A 1 142 ? 2.012   28.678  -14.882 1.00 56.34  ? 142 LYS A CD  1 
ATOM   1088 C CE  . LYS A 1 142 ? 2.075   29.854  -15.855 1.00 61.27  ? 142 LYS A CE  1 
ATOM   1089 N NZ  . LYS A 1 142 ? 3.044   30.914  -15.443 1.00 58.98  ? 142 LYS A NZ  1 
ATOM   1090 N N   . LYS A 1 143 ? -2.790  28.534  -17.863 1.00 49.08  ? 143 LYS A N   1 
ATOM   1091 C CA  . LYS A 1 143 ? -3.902  29.349  -18.364 1.00 47.13  ? 143 LYS A CA  1 
ATOM   1092 C C   . LYS A 1 143 ? -5.004  28.540  -19.035 1.00 50.21  ? 143 LYS A C   1 
ATOM   1093 O O   . LYS A 1 143 ? -5.785  29.113  -19.792 1.00 52.24  ? 143 LYS A O   1 
ATOM   1094 C CB  . LYS A 1 143 ? -3.425  30.498  -19.278 1.00 51.48  ? 143 LYS A CB  1 
ATOM   1095 C CG  . LYS A 1 143 ? -2.713  31.614  -18.520 1.00 49.04  ? 143 LYS A CG  1 
ATOM   1096 C CD  . LYS A 1 143 ? -2.809  32.973  -19.224 1.00 62.33  ? 143 LYS A CD  1 
ATOM   1097 C CE  . LYS A 1 143 ? -3.125  34.122  -18.289 1.00 60.27  ? 143 LYS A CE  1 
ATOM   1098 N NZ  . LYS A 1 143 ? -4.588  34.304  -18.093 1.00 63.61  ? 143 LYS A NZ  1 
ATOM   1099 N N   . SER A 1 144 ? -5.120  27.233  -18.714 1.00 44.33  ? 144 SER A N   1 
ATOM   1100 C CA  . SER A 1 144 ? -6.180  26.405  -19.279 1.00 47.19  ? 144 SER A CA  1 
ATOM   1101 C C   . SER A 1 144 ? -7.551  26.836  -18.757 1.00 49.35  ? 144 SER A C   1 
ATOM   1102 O O   . SER A 1 144 ? -7.685  27.276  -17.604 1.00 45.29  ? 144 SER A O   1 
ATOM   1103 C CB  . SER A 1 144 ? -5.948  24.929  -18.977 1.00 46.47  ? 144 SER A CB  1 
ATOM   1104 O OG  . SER A 1 144 ? -4.888  24.363  -19.733 1.00 48.72  ? 144 SER A OG  1 
ATOM   1105 N N   . ASN A 1 145 ? -8.563  26.748  -19.620 1.00 46.78  ? 145 ASN A N   1 
ATOM   1106 C CA  . ASN A 1 145 ? -9.910  27.151  -19.251 1.00 47.89  ? 145 ASN A CA  1 
ATOM   1107 C C   . ASN A 1 145 ? -10.796 25.953  -18.829 1.00 46.26  ? 145 ASN A C   1 
ATOM   1108 O O   . ASN A 1 145 ? -10.320 24.822  -18.714 1.00 42.81  ? 145 ASN A O   1 
ATOM   1109 C CB  . ASN A 1 145 ? -10.550 28.003  -20.370 1.00 48.18  ? 145 ASN A CB  1 
ATOM   1110 C CG  . ASN A 1 145 ? -10.646 27.326  -21.713 1.00 47.08  ? 145 ASN A CG  1 
ATOM   1111 O OD1 . ASN A 1 145 ? -11.101 26.189  -21.845 1.00 45.37  ? 145 ASN A OD1 1 
ATOM   1112 N ND2 . ASN A 1 145 ? -10.224 28.021  -22.753 1.00 49.31  ? 145 ASN A ND2 1 
ATOM   1113 N N   . LEU A 1 146 ? -12.069 26.219  -18.573 1.00 44.04  ? 146 LEU A N   1 
ATOM   1114 C CA  . LEU A 1 146 ? -13.031 25.215  -18.172 1.00 44.74  ? 146 LEU A CA  1 
ATOM   1115 C C   . LEU A 1 146 ? -13.266 24.183  -19.284 1.00 42.93  ? 146 LEU A C   1 
ATOM   1116 O O   . LEU A 1 146 ? -13.470 23.014  -18.987 1.00 36.91  ? 146 LEU A O   1 
ATOM   1117 C CB  . LEU A 1 146 ? -14.330 25.914  -17.799 1.00 46.32  ? 146 LEU A CB  1 
ATOM   1118 C CG  . LEU A 1 146 ? -15.321 25.073  -17.046 1.00 46.60  ? 146 LEU A CG  1 
ATOM   1119 C CD1 . LEU A 1 146 ? -14.923 24.954  -15.568 1.00 38.76  ? 146 LEU A CD1 1 
ATOM   1120 C CD2 . LEU A 1 146 ? -16.709 25.647  -17.195 1.00 48.21  ? 146 LEU A CD2 1 
ATOM   1121 N N   . GLN A 1 147 ? -13.172 24.593  -20.555 1.00 41.49  ? 147 GLN A N   1 
ATOM   1122 C CA  . GLN A 1 147 ? -13.338 23.665  -21.671 1.00 43.97  ? 147 GLN A CA  1 
ATOM   1123 C C   . GLN A 1 147 ? -12.197 22.647  -21.761 1.00 40.91  ? 147 GLN A C   1 
ATOM   1124 O O   . GLN A 1 147 ? -12.436 21.460  -22.004 1.00 35.85  ? 147 GLN A O   1 
ATOM   1125 C CB  . GLN A 1 147 ? -13.536 24.411  -23.010 1.00 45.47  ? 147 GLN A CB  1 
ATOM   1126 C CG  . GLN A 1 147 ? -14.206 23.567  -24.099 1.00 45.56  ? 147 GLN A CG  1 
ATOM   1127 C CD  . GLN A 1 147 ? -15.145 22.534  -23.521 1.00 48.17  ? 147 GLN A CD  1 
ATOM   1128 O OE1 . GLN A 1 147 ? -14.883 21.327  -23.522 1.00 50.32  ? 147 GLN A OE1 1 
ATOM   1129 N NE2 . GLN A 1 147 ? -16.301 22.991  -23.088 1.00 50.49  ? 147 GLN A NE2 1 
ATOM   1130 N N   . ASP A 1 148 ? -10.960 23.103  -21.516 1.00 42.39  ? 148 ASP A N   1 
ATOM   1131 C CA  . ASP A 1 148 ? -9.804  22.210  -21.478 1.00 39.00  ? 148 ASP A CA  1 
ATOM   1132 C C   . ASP A 1 148 ? -9.963  21.241  -20.297 1.00 39.91  ? 148 ASP A C   1 
ATOM   1133 O O   . ASP A 1 148 ? -9.637  20.070  -20.433 1.00 36.09  ? 148 ASP A O   1 
ATOM   1134 C CB  . ASP A 1 148 ? -8.522  23.017  -21.284 1.00 39.37  ? 148 ASP A CB  1 
ATOM   1135 C CG  . ASP A 1 148 ? -8.246  23.959  -22.438 1.00 47.75  ? 148 ASP A CG  1 
ATOM   1136 O OD1 . ASP A 1 148 ? -8.221  23.485  -23.600 1.00 50.19  ? 148 ASP A OD1 1 
ATOM   1137 O OD2 . ASP A 1 148 ? -8.070  25.166  -22.187 1.00 42.60  ? 148 ASP A OD2 1 
ATOM   1138 N N   . ALA A 1 149 ? -10.475 21.732  -19.144 1.00 38.27  ? 149 ALA A N   1 
ATOM   1139 C CA  . ALA A 1 149 ? -10.707 20.884  -17.985 1.00 38.64  ? 149 ALA A CA  1 
ATOM   1140 C C   . ALA A 1 149 ? -11.673 19.739  -18.306 1.00 35.74  ? 149 ALA A C   1 
ATOM   1141 O O   . ALA A 1 149 ? -11.498 18.646  -17.776 1.00 30.80  ? 149 ALA A O   1 
ATOM   1142 C CB  . ALA A 1 149 ? -11.211 21.707  -16.810 1.00 39.12  ? 149 ALA A CB  1 
ATOM   1143 N N   . VAL A 1 150 ? -12.662 19.958  -19.175 1.00 32.03  ? 150 VAL A N   1 
ATOM   1144 C CA  . VAL A 1 150 ? -13.579 18.880  -19.591 1.00 35.76  ? 150 VAL A CA  1 
ATOM   1145 C C   . VAL A 1 150 ? -12.794 17.751  -20.284 1.00 34.94  ? 150 VAL A C   1 
ATOM   1146 O O   . VAL A 1 150 ? -12.858 16.598  -19.846 1.00 29.67  ? 150 VAL A O   1 
ATOM   1147 C CB  . VAL A 1 150 ? -14.736 19.405  -20.488 1.00 40.46  ? 150 VAL A CB  1 
ATOM   1148 C CG1 . VAL A 1 150 ? -15.500 18.257  -21.140 1.00 36.79  ? 150 VAL A CG1 1 
ATOM   1149 C CG2 . VAL A 1 150 ? -15.677 20.317  -19.704 1.00 38.29  ? 150 VAL A CG2 1 
ATOM   1150 N N   . LYS A 1 151 ? -11.993 18.099  -21.317 1.00 33.62  ? 151 LYS A N   1 
ATOM   1151 C CA  . LYS A 1 151 ? -11.150 17.119  -22.021 1.00 33.52  ? 151 LYS A CA  1 
ATOM   1152 C C   . LYS A 1 151 ? -10.223 16.373  -21.053 1.00 35.96  ? 151 LYS A C   1 
ATOM   1153 O O   . LYS A 1 151 ? -10.106 15.145  -21.157 1.00 35.07  ? 151 LYS A O   1 
ATOM   1154 C CB  . LYS A 1 151 ? -10.286 17.789  -23.102 1.00 35.82  ? 151 LYS A CB  1 
ATOM   1155 C CG  . LYS A 1 151 ? -10.677 17.464  -24.530 1.00 42.22  ? 151 LYS A CG  1 
ATOM   1156 C CD  . LYS A 1 151 ? -9.759  18.154  -25.562 1.00 46.08  ? 151 LYS A CD  1 
ATOM   1157 C CE  . LYS A 1 151 ? -8.548  17.331  -25.932 1.00 49.16  ? 151 LYS A CE  1 
ATOM   1158 N NZ  . LYS A 1 151 ? -7.637  18.066  -26.858 1.00 53.20  ? 151 LYS A NZ  1 
ATOM   1159 N N   . ILE A 1 152 ? -9.548  17.110  -20.138 1.00 32.06  ? 152 ILE A N   1 
ATOM   1160 C CA  . ILE A 1 152 ? -8.633  16.510  -19.171 1.00 33.60  ? 152 ILE A CA  1 
ATOM   1161 C C   . ILE A 1 152 ? -9.341  15.492  -18.275 1.00 33.57  ? 152 ILE A C   1 
ATOM   1162 O O   . ILE A 1 152 ? -8.847  14.376  -18.110 1.00 31.52  ? 152 ILE A O   1 
ATOM   1163 C CB  . ILE A 1 152 ? -7.865  17.548  -18.293 1.00 35.72  ? 152 ILE A CB  1 
ATOM   1164 C CG1 . ILE A 1 152 ? -7.097  18.624  -19.097 1.00 36.93  ? 152 ILE A CG1 1 
ATOM   1165 C CG2 . ILE A 1 152 ? -6.944  16.846  -17.325 1.00 37.34  ? 152 ILE A CG2 1 
ATOM   1166 C CD1 . ILE A 1 152 ? -6.610  18.237  -20.456 1.00 42.22  ? 152 ILE A CD1 1 
ATOM   1167 N N   . LEU A 1 153 ? -10.496 15.866  -17.685 1.00 31.92  ? 153 LEU A N   1 
ATOM   1168 C CA  . LEU A 1 153 ? -11.218 14.950  -16.812 1.00 30.10  ? 153 LEU A CA  1 
ATOM   1169 C C   . LEU A 1 153 ? -11.670 13.713  -17.572 1.00 30.45  ? 153 LEU A C   1 
ATOM   1170 O O   . LEU A 1 153 ? -11.623 12.632  -17.015 1.00 26.94  ? 153 LEU A O   1 
ATOM   1171 C CB  . LEU A 1 153 ? -12.379 15.650  -16.090 1.00 32.48  ? 153 LEU A CB  1 
ATOM   1172 C CG  . LEU A 1 153 ? -12.089 16.258  -14.693 1.00 31.25  ? 153 LEU A CG  1 
ATOM   1173 C CD1 . LEU A 1 153 ? -10.795 17.027  -14.651 1.00 29.90  ? 153 LEU A CD1 1 
ATOM   1174 C CD2 . LEU A 1 153 ? -13.214 17.144  -14.258 1.00 30.25  ? 153 LEU A CD2 1 
ATOM   1175 N N   . ILE A 1 154 ? -12.010 13.833  -18.862 1.00 31.14  ? 154 ILE A N   1 
ATOM   1176 C CA  . ILE A 1 154 ? -12.379 12.676  -19.682 1.00 31.15  ? 154 ILE A CA  1 
ATOM   1177 C C   . ILE A 1 154 ? -11.166 11.752  -19.825 1.00 32.52  ? 154 ILE A C   1 
ATOM   1178 O O   . ILE A 1 154 ? -11.262 10.539  -19.618 1.00 29.85  ? 154 ILE A O   1 
ATOM   1179 C CB  . ILE A 1 154 ? -12.959 13.141  -21.061 1.00 31.38  ? 154 ILE A CB  1 
ATOM   1180 C CG1 . ILE A 1 154 ? -14.398 13.699  -20.887 1.00 33.18  ? 154 ILE A CG1 1 
ATOM   1181 C CG2 . ILE A 1 154 ? -12.937 12.011  -22.107 1.00 35.53  ? 154 ILE A CG2 1 
ATOM   1182 C CD1 . ILE A 1 154 ? -14.886 14.543  -22.002 1.00 31.09  ? 154 ILE A CD1 1 
ATOM   1183 N N   . LEU A 1 155 ? -10.006 12.339  -20.102 1.00 32.17  ? 155 LEU A N   1 
ATOM   1184 C CA  . LEU A 1 155 ? -8.770  11.562  -20.188 1.00 34.38  ? 155 LEU A CA  1 
ATOM   1185 C C   . LEU A 1 155 ? -8.431  10.876  -18.818 1.00 35.03  ? 155 LEU A C   1 
ATOM   1186 O O   . LEU A 1 155 ? -8.027  9.720   -18.801 1.00 30.42  ? 155 LEU A O   1 
ATOM   1187 C CB  . LEU A 1 155 ? -7.637  12.483  -20.659 1.00 33.36  ? 155 LEU A CB  1 
ATOM   1188 C CG  . LEU A 1 155 ? -6.343  11.806  -21.081 1.00 37.00  ? 155 LEU A CG  1 
ATOM   1189 C CD1 . LEU A 1 155 ? -6.600  10.577  -21.985 1.00 37.00  ? 155 LEU A CD1 1 
ATOM   1190 C CD2 . LEU A 1 155 ? -5.398  12.797  -21.720 1.00 34.43  ? 155 LEU A CD2 1 
ATOM   1191 N N   . CYS A 1 156 ? -8.648  11.568  -17.677 1.00 28.63  ? 156 CYS A N   1 
ATOM   1192 C CA  . CYS A 1 156 ? -8.378  10.997  -16.348 1.00 32.25  ? 156 CYS A CA  1 
ATOM   1193 C C   . CYS A 1 156 ? -9.255  9.770   -16.132 1.00 32.88  ? 156 CYS A C   1 
ATOM   1194 O O   . CYS A 1 156 ? -8.767  8.737   -15.661 1.00 32.25  ? 156 CYS A O   1 
ATOM   1195 C CB  . CYS A 1 156 ? -8.627  12.026  -15.241 1.00 31.26  ? 156 CYS A CB  1 
ATOM   1196 S SG  . CYS A 1 156 ? -7.391  13.343  -15.104 1.00 34.26  ? 156 CYS A SG  1 
ATOM   1197 N N   . MET A 1 157 ? -10.566 9.911   -16.426 1.00 29.52  ? 157 MET A N   1 
ATOM   1198 C CA  . MET A 1 157 ? -11.564 8.855   -16.254 1.00 31.67  ? 157 MET A CA  1 
ATOM   1199 C C   . MET A 1 157 ? -11.265 7.662   -17.163 1.00 31.07  ? 157 MET A C   1 
ATOM   1200 O O   . MET A 1 157 ? -11.430 6.526   -16.740 1.00 30.86  ? 157 MET A O   1 
ATOM   1201 C CB  . MET A 1 157 ? -13.000 9.405   -16.474 1.00 30.06  ? 157 MET A CB  1 
ATOM   1202 C CG  . MET A 1 157 ? -13.435 10.406  -15.406 1.00 35.08  ? 157 MET A CG  1 
ATOM   1203 S SD  . MET A 1 157 ? -13.112 9.857   -13.681 1.00 32.61  ? 157 MET A SD  1 
ATOM   1204 C CE  . MET A 1 157 ? -14.370 8.596   -13.543 1.00 32.74  ? 157 MET A CE  1 
ATOM   1205 N N   . GLU A 1 158 ? -10.794 7.907   -18.394 1.00 32.49  ? 158 GLU A N   1 
ATOM   1206 C CA  . GLU A 1 158 ? -10.466 6.821   -19.320 1.00 36.16  ? 158 GLU A CA  1 
ATOM   1207 C C   . GLU A 1 158 ? -9.191  6.080   -18.902 1.00 35.60  ? 158 GLU A C   1 
ATOM   1208 O O   . GLU A 1 158 ? -9.121  4.850   -19.007 1.00 34.82  ? 158 GLU A O   1 
ATOM   1209 C CB  . GLU A 1 158 ? -10.309 7.358   -20.756 1.00 36.75  ? 158 GLU A CB  1 
ATOM   1210 C CG  . GLU A 1 158 ? -11.592 7.881   -21.375 1.00 35.97  ? 158 GLU A CG  1 
ATOM   1211 C CD  . GLU A 1 158 ? -11.402 8.591   -22.704 1.00 42.93  ? 158 GLU A CD  1 
ATOM   1212 O OE1 . GLU A 1 158 ? -10.292 9.118   -22.953 1.00 39.94  ? 158 GLU A OE1 1 
ATOM   1213 O OE2 . GLU A 1 158 ? -12.377 8.638   -23.488 1.00 45.46  ? 158 GLU A OE2 1 
ATOM   1214 N N   . THR A 1 159 ? -8.180  6.828   -18.478 1.00 34.99  ? 159 THR A N   1 
ATOM   1215 C CA  . THR A 1 159 ? -6.911  6.251   -18.047 1.00 38.73  ? 159 THR A CA  1 
ATOM   1216 C C   . THR A 1 159 ? -7.107  5.375   -16.799 1.00 37.34  ? 159 THR A C   1 
ATOM   1217 O O   . THR A 1 159 ? -6.522  4.293   -16.706 1.00 34.45  ? 159 THR A O   1 
ATOM   1218 C CB  . THR A 1 159 ? -5.909  7.373   -17.718 1.00 39.84  ? 159 THR A CB  1 
ATOM   1219 O OG1 . THR A 1 159 ? -5.932  8.363   -18.738 1.00 37.90  ? 159 THR A OG1 1 
ATOM   1220 C CG2 . THR A 1 159 ? -4.480  6.838   -17.493 1.00 42.13  ? 159 THR A CG2 1 
ATOM   1221 N N   . VAL A 1 160 ? -7.941  5.836   -15.848 1.00 34.60  ? 160 VAL A N   1 
ATOM   1222 C CA  . VAL A 1 160 ? -8.177  5.050   -14.637 1.00 37.11  ? 160 VAL A CA  1 
ATOM   1223 C C   . VAL A 1 160 ? -8.918  3.743   -14.951 1.00 36.34  ? 160 VAL A C   1 
ATOM   1224 O O   . VAL A 1 160 ? -8.480  2.690   -14.494 1.00 32.49  ? 160 VAL A O   1 
ATOM   1225 C CB  . VAL A 1 160 ? -8.835  5.839   -13.483 1.00 31.45  ? 160 VAL A CB  1 
ATOM   1226 C CG1 . VAL A 1 160 ? -9.137  4.911   -12.307 1.00 32.83  ? 160 VAL A CG1 1 
ATOM   1227 C CG2 . VAL A 1 160 ? -7.941  6.988   -13.027 1.00 34.58  ? 160 VAL A CG2 1 
ATOM   1228 N N   . ALA A 1 161 ? -9.962  3.787   -15.807 1.00 34.01  ? 161 ALA A N   1 
ATOM   1229 C CA  . ALA A 1 161 ? -10.738 2.585   -16.132 1.00 37.14  ? 161 ALA A CA  1 
ATOM   1230 C C   . ALA A 1 161 ? -9.920  1.527   -16.892 1.00 40.44  ? 161 ALA A C   1 
ATOM   1231 O O   . ALA A 1 161 ? -10.200 0.330   -16.795 1.00 43.79  ? 161 ALA A O   1 
ATOM   1232 C CB  . ALA A 1 161 ? -11.987 2.965   -16.902 1.00 39.38  ? 161 ALA A CB  1 
ATOM   1233 N N   . ARG A 1 162 ? -8.873  1.964   -17.593 1.00 37.94  ? 162 ARG A N   1 
ATOM   1234 C CA  . ARG A 1 162 ? -7.958  1.068   -18.283 1.00 38.04  ? 162 ARG A CA  1 
ATOM   1235 C C   . ARG A 1 162 ? -7.029  0.350   -17.305 1.00 36.40  ? 162 ARG A C   1 
ATOM   1236 O O   . ARG A 1 162 ? -6.455  -0.661  -17.683 1.00 44.95  ? 162 ARG A O   1 
ATOM   1237 C CB  . ARG A 1 162 ? -7.044  1.872   -19.219 1.00 42.27  ? 162 ARG A CB  1 
ATOM   1238 C CG  . ARG A 1 162 ? -7.531  2.000   -20.643 1.00 47.68  ? 162 ARG A CG  1 
ATOM   1239 C CD  . ARG A 1 162 ? -6.403  2.475   -21.552 1.00 49.77  ? 162 ARG A CD  1 
ATOM   1240 N NE  . ARG A 1 162 ? -5.898  3.809   -21.208 1.00 52.96  ? 162 ARG A NE  1 
ATOM   1241 C CZ  . ARG A 1 162 ? -6.355  4.942   -21.736 1.00 52.55  ? 162 ARG A CZ  1 
ATOM   1242 N NH1 . ARG A 1 162 ? -7.354  4.921   -22.614 1.00 54.32  ? 162 ARG A NH1 1 
ATOM   1243 N NH2 . ARG A 1 162 ? -5.826  6.110   -21.378 1.00 45.07  ? 162 ARG A NH2 1 
ATOM   1244 N N   . LYS A 1 163 ? -6.801  0.898   -16.109 1.00 35.88  ? 163 LYS A N   1 
ATOM   1245 C CA  . LYS A 1 163 ? -5.850  0.347   -15.170 1.00 40.77  ? 163 LYS A CA  1 
ATOM   1246 C C   . LYS A 1 163 ? -6.433  -0.463  -14.016 1.00 38.50  ? 163 LYS A C   1 
ATOM   1247 O O   . LYS A 1 163 ? -5.675  -1.127  -13.309 1.00 41.83  ? 163 LYS A O   1 
ATOM   1248 C CB  . LYS A 1 163 ? -4.978  1.473   -14.620 1.00 41.98  ? 163 LYS A CB  1 
ATOM   1249 C CG  . LYS A 1 163 ? -3.966  1.973   -15.633 1.00 42.95  ? 163 LYS A CG  1 
ATOM   1250 C CD  . LYS A 1 163 ? -3.301  3.265   -15.157 1.00 42.67  ? 163 LYS A CD  1 
ATOM   1251 C CE  . LYS A 1 163 ? -1.857  3.358   -15.606 1.00 45.72  ? 163 LYS A CE  1 
ATOM   1252 N NZ  . LYS A 1 163 ? -1.711  4.070   -16.907 1.00 47.20  ? 163 LYS A NZ  1 
ATOM   1253 N N   . THR A 1 164 ? -7.756  -0.388  -13.789 1.00 36.09  ? 164 THR A N   1 
ATOM   1254 C CA  . THR A 1 164 ? -8.366  -1.097  -12.671 1.00 39.23  ? 164 THR A CA  1 
ATOM   1255 C C   . THR A 1 164 ? -9.802  -1.502  -12.925 1.00 38.39  ? 164 THR A C   1 
ATOM   1256 O O   . THR A 1 164 ? -10.554 -0.809  -13.618 1.00 38.28  ? 164 THR A O   1 
ATOM   1257 C CB  . THR A 1 164 ? -8.263  -0.264  -11.386 1.00 40.05  ? 164 THR A CB  1 
ATOM   1258 O OG1 . THR A 1 164 ? -8.878  -0.969  -10.306 1.00 38.36  ? 164 THR A OG1 1 
ATOM   1259 C CG2 . THR A 1 164 ? -8.871  1.114   -11.534 1.00 37.83  ? 164 THR A CG2 1 
ATOM   1260 N N   . ALA A 1 165 ? -10.189 -2.632  -12.325 1.00 36.19  ? 165 ALA A N   1 
ATOM   1261 C CA  . ALA A 1 165 ? -11.553 -3.132  -12.391 1.00 38.53  ? 165 ALA A CA  1 
ATOM   1262 C C   . ALA A 1 165 ? -12.425 -2.560  -11.229 1.00 37.82  ? 165 ALA A C   1 
ATOM   1263 O O   . ALA A 1 165 ? -13.604 -2.888  -11.144 1.00 35.57  ? 165 ALA A O   1 
ATOM   1264 C CB  . ALA A 1 165 ? -11.554 -4.647  -12.385 1.00 40.05  ? 165 ALA A CB  1 
ATOM   1265 N N   . SER A 1 166 ? -11.862 -1.677  -10.377 1.00 36.35  ? 166 SER A N   1 
ATOM   1266 C CA  . SER A 1 166 ? -12.607 -1.003  -9.324  1.00 41.08  ? 166 SER A CA  1 
ATOM   1267 C C   . SER A 1 166 ? -13.415 0.203   -9.862  1.00 44.21  ? 166 SER A C   1 
ATOM   1268 O O   . SER A 1 166 ? -14.218 0.776   -9.132  1.00 47.44  ? 166 SER A O   1 
ATOM   1269 C CB  . SER A 1 166 ? -11.670 -0.550  -8.209  1.00 44.10  ? 166 SER A CB  1 
ATOM   1270 O OG  . SER A 1 166 ? -10.829 0.504   -8.649  1.00 43.89  ? 166 SER A OG  1 
ATOM   1271 N N   . VAL A 1 167 ? -13.180 0.599   -11.123 1.00 36.02  ? 167 VAL A N   1 
ATOM   1272 C CA  . VAL A 1 167 ? -13.884 1.668   -11.809 1.00 37.54  ? 167 VAL A CA  1 
ATOM   1273 C C   . VAL A 1 167 ? -14.527 1.082   -13.094 1.00 37.53  ? 167 VAL A C   1 
ATOM   1274 O O   . VAL A 1 167 ? -14.034 0.098   -13.627 1.00 42.28  ? 167 VAL A O   1 
ATOM   1275 C CB  . VAL A 1 167 ? -12.851 2.801   -12.105 1.00 36.46  ? 167 VAL A CB  1 
ATOM   1276 C CG1 . VAL A 1 167 ? -13.453 3.920   -12.918 1.00 38.45  ? 167 VAL A CG1 1 
ATOM   1277 C CG2 . VAL A 1 167 ? -12.247 3.343   -10.815 1.00 36.74  ? 167 VAL A CG2 1 
ATOM   1278 N N   . SER A 1 168 ? -15.658 1.633   -13.554 1.00 39.97  ? 168 SER A N   1 
ATOM   1279 C CA  . SER A 1 168 ? -16.300 1.191   -14.788 1.00 38.45  ? 168 SER A CA  1 
ATOM   1280 C C   . SER A 1 168 ? -15.750 2.012   -15.955 1.00 39.90  ? 168 SER A C   1 
ATOM   1281 O O   . SER A 1 168 ? -15.264 3.121   -15.762 1.00 36.18  ? 168 SER A O   1 
ATOM   1282 C CB  . SER A 1 168 ? -17.813 1.396   -14.708 1.00 35.44  ? 168 SER A CB  1 
ATOM   1283 O OG  . SER A 1 168 ? -18.109 2.756   -14.431 1.00 35.96  ? 168 SER A OG  1 
ATOM   1284 N N   . LYS A 1 169 ? -15.881 1.482   -17.176 1.00 40.69  ? 169 LYS A N   1 
ATOM   1285 C CA  . LYS A 1 169 ? -15.458 2.254   -18.377 1.00 38.44  ? 169 LYS A CA  1 
ATOM   1286 C C   . LYS A 1 169 ? -16.425 3.427   -18.565 1.00 34.33  ? 169 LYS A C   1 
ATOM   1287 O O   . LYS A 1 169 ? -15.958 4.516   -18.954 1.00 32.17  ? 169 LYS A O   1 
ATOM   1288 C CB  . LYS A 1 169 ? -15.422 1.353   -19.615 1.00 40.18  ? 169 LYS A CB  1 
ATOM   1289 C CG  . LYS A 1 169 ? -14.355 0.265   -19.602 1.00 44.33  ? 169 LYS A CG  1 
ATOM   1290 C CD  . LYS A 1 169 ? -14.355 -0.628  -20.826 1.00 46.50  ? 169 LYS A CD  1 
ATOM   1291 C CE  . LYS A 1 169 ? -13.273 -1.688  -20.807 1.00 54.90  ? 169 LYS A CE  1 
ATOM   1292 N NZ  . LYS A 1 169 ? -13.316 -2.558  -22.006 1.00 53.53  ? 169 LYS A NZ  1 
ATOM   1293 N N   . GLN A 1 170 ? -17.718 3.211   -18.299 1.00 33.46  ? 170 GLN A N   1 
ATOM   1294 C CA  . GLN A 1 170 ? -18.711 4.277   -18.406 1.00 34.00  ? 170 GLN A CA  1 
ATOM   1295 C C   . GLN A 1 170 ? -18.544 5.289   -17.280 1.00 32.95  ? 170 GLN A C   1 
ATOM   1296 O O   . GLN A 1 170 ? -18.288 4.909   -16.134 1.00 31.25  ? 170 GLN A O   1 
ATOM   1297 C CB  . GLN A 1 170 ? -20.140 3.700   -18.274 1.00 41.70  ? 170 GLN A CB  1 
ATOM   1298 C CG  . GLN A 1 170 ? -20.467 2.550   -19.223 1.00 48.58  ? 170 GLN A CG  1 
ATOM   1299 C CD  . GLN A 1 170 ? -20.426 1.186   -18.546 1.00 48.05  ? 170 GLN A CD  1 
ATOM   1300 O OE1 . GLN A 1 170 ? -19.362 0.688   -18.136 1.00 45.69  ? 170 GLN A OE1 1 
ATOM   1301 N NE2 . GLN A 1 170 ? -21.594 0.545   -18.439 1.00 48.11  ? 170 GLN A NE2 1 
ATOM   1302 N N   . PHE A 1 171 ? -18.758 6.569   -17.587 1.00 27.92  ? 171 PHE A N   1 
ATOM   1303 C CA  . PHE A 1 171 ? -18.668 7.621   -16.588 1.00 27.21  ? 171 PHE A CA  1 
ATOM   1304 C C   . PHE A 1 171 ? -19.600 8.780   -16.931 1.00 31.38  ? 171 PHE A C   1 
ATOM   1305 O O   . PHE A 1 171 ? -20.140 8.852   -18.046 1.00 25.67  ? 171 PHE A O   1 
ATOM   1306 C CB  . PHE A 1 171 ? -17.198 8.083   -16.378 1.00 29.04  ? 171 PHE A CB  1 
ATOM   1307 C CG  . PHE A 1 171 ? -16.591 8.753   -17.586 1.00 31.94  ? 171 PHE A CG  1 
ATOM   1308 C CD1 . PHE A 1 171 ? -15.963 8.008   -18.569 1.00 32.17  ? 171 PHE A CD1 1 
ATOM   1309 C CD2 . PHE A 1 171 ? -16.615 10.132  -17.720 1.00 29.44  ? 171 PHE A CD2 1 
ATOM   1310 C CE1 . PHE A 1 171 ? -15.420 8.625   -19.687 1.00 31.99  ? 171 PHE A CE1 1 
ATOM   1311 C CE2 . PHE A 1 171 ? -16.033 10.746  -18.819 1.00 30.19  ? 171 PHE A CE2 1 
ATOM   1312 C CZ  . PHE A 1 171 ? -15.453 9.990   -19.798 1.00 32.31  ? 171 PHE A CZ  1 
ATOM   1313 N N   . MET A 1 172 ? -19.805 9.683   -15.979 1.00 27.71  ? 172 MET A N   1 
ATOM   1314 C CA  . MET A 1 172 ? -20.652 10.852  -16.164 1.00 28.62  ? 172 MET A CA  1 
ATOM   1315 C C   . MET A 1 172 ? -19.864 12.123  -15.980 1.00 27.89  ? 172 MET A C   1 
ATOM   1316 O O   . MET A 1 172 ? -18.987 12.163  -15.138 1.00 25.69  ? 172 MET A O   1 
ATOM   1317 C CB  . MET A 1 172 ? -21.752 10.878  -15.111 1.00 33.20  ? 172 MET A CB  1 
ATOM   1318 C CG  . MET A 1 172 ? -22.970 10.138  -15.495 1.00 40.56  ? 172 MET A CG  1 
ATOM   1319 S SD  . MET A 1 172 ? -24.121 10.157  -14.092 1.00 54.19  ? 172 MET A SD  1 
ATOM   1320 C CE  . MET A 1 172 ? -24.793 11.799  -14.236 1.00 37.56  ? 172 MET A CE  1 
ATOM   1321 N N   . ILE A 1 173 ? -20.314 13.197  -16.612 1.00 25.30  ? 173 ILE A N   1 
ATOM   1322 C CA  . ILE A 1 173 ? -19.712 14.492  -16.419 1.00 29.66  ? 173 ILE A CA  1 
ATOM   1323 C C   . ILE A 1 173 ? -20.780 15.563  -16.301 1.00 32.82  ? 173 ILE A C   1 
ATOM   1324 O O   . ILE A 1 173 ? -21.732 15.592  -17.076 1.00 29.61  ? 173 ILE A O   1 
ATOM   1325 C CB  . ILE A 1 173 ? -18.642 14.771  -17.493 1.00 31.53  ? 173 ILE A CB  1 
ATOM   1326 C CG1 . ILE A 1 173 ? -17.571 15.731  -17.012 1.00 34.33  ? 173 ILE A CG1 1 
ATOM   1327 C CG2 . ILE A 1 173 ? -19.259 15.225  -18.790 1.00 36.36  ? 173 ILE A CG2 1 
ATOM   1328 C CD1 . ILE A 1 173 ? -16.251 15.423  -17.648 1.00 35.16  ? 173 ILE A CD1 1 
ATOM   1329 N N   . VAL A 1 174 ? -20.704 16.358  -15.236 1.00 31.17  ? 174 VAL A N   1 
ATOM   1330 C CA  . VAL A 1 174 ? -21.602 17.497  -14.994 1.00 28.78  ? 174 VAL A CA  1 
ATOM   1331 C C   . VAL A 1 174 ? -20.735 18.743  -14.918 1.00 31.72  ? 174 VAL A C   1 
ATOM   1332 O O   . VAL A 1 174 ? -19.597 18.691  -14.436 1.00 24.95  ? 174 VAL A O   1 
ATOM   1333 C CB  . VAL A 1 174 ? -22.435 17.360  -13.698 1.00 34.46  ? 174 VAL A CB  1 
ATOM   1334 C CG1 . VAL A 1 174 ? -23.532 16.296  -13.826 1.00 30.75  ? 174 VAL A CG1 1 
ATOM   1335 C CG2 . VAL A 1 174 ? -21.535 17.086  -12.494 1.00 29.32  ? 174 VAL A CG2 1 
ATOM   1336 N N   . GLN A 1 175 ? -21.262 19.878  -15.382 1.00 35.01  ? 175 GLN A N   1 
ATOM   1337 C CA  . GLN A 1 175 ? -20.511 21.124  -15.327 1.00 33.77  ? 175 GLN A CA  1 
ATOM   1338 C C   . GLN A 1 175 ? -21.397 22.307  -15.075 1.00 36.71  ? 175 GLN A C   1 
ATOM   1339 O O   . GLN A 1 175 ? -22.599 22.255  -15.320 1.00 34.29  ? 175 GLN A O   1 
ATOM   1340 C CB  . GLN A 1 175 ? -19.628 21.317  -16.559 1.00 33.92  ? 175 GLN A CB  1 
ATOM   1341 C CG  . GLN A 1 175 ? -20.385 21.618  -17.816 1.00 40.65  ? 175 GLN A CG  1 
ATOM   1342 C CD  . GLN A 1 175 ? -19.412 21.847  -18.946 1.00 42.67  ? 175 GLN A CD  1 
ATOM   1343 O OE1 . GLN A 1 175 ? -18.857 22.929  -19.110 1.00 44.86  ? 175 GLN A OE1 1 
ATOM   1344 N NE2 . GLN A 1 175 ? -19.167 20.813  -19.720 1.00 39.81  ? 175 GLN A NE2 1 
ATOM   1345 N N   . THR A 1 176 ? -20.807 23.354  -14.501 1.00 33.23  ? 176 THR A N   1 
ATOM   1346 C CA  . THR A 1 176 ? -21.546 24.556  -14.201 1.00 38.09  ? 176 THR A CA  1 
ATOM   1347 C C   . THR A 1 176 ? -20.676 25.789  -14.341 1.00 34.38  ? 176 THR A C   1 
ATOM   1348 O O   . THR A 1 176 ? -19.457 25.744  -14.158 1.00 35.31  ? 176 THR A O   1 
ATOM   1349 C CB  . THR A 1 176 ? -22.148 24.481  -12.780 1.00 39.45  ? 176 THR A CB  1 
ATOM   1350 O OG1 . THR A 1 176 ? -23.063 25.563  -12.626 1.00 40.87  ? 176 THR A OG1 1 
ATOM   1351 C CG2 . THR A 1 176 ? -21.083 24.517  -11.679 1.00 33.85  ? 176 THR A CG2 1 
ATOM   1352 N N   . ALA A 1 177 ? -21.325 26.884  -14.683 1.00 36.59  ? 177 ALA A N   1 
ATOM   1353 C CA  . ALA A 1 177 ? -20.720 28.215  -14.759 1.00 36.68  ? 177 ALA A CA  1 
ATOM   1354 C C   . ALA A 1 177 ? -21.155 29.091  -13.549 1.00 40.03  ? 177 ALA A C   1 
ATOM   1355 O O   . ALA A 1 177 ? -20.643 30.199  -13.372 1.00 43.40  ? 177 ALA A O   1 
ATOM   1356 C CB  . ALA A 1 177 ? -21.135 28.889  -16.057 1.00 39.56  ? 177 ALA A CB  1 
ATOM   1357 N N   . SER A 1 178 ? -22.131 28.616  -12.761 1.00 37.05  ? 178 SER A N   1 
ATOM   1358 C CA  . SER A 1 178 ? -22.707 29.295  -11.618 1.00 43.43  ? 178 SER A CA  1 
ATOM   1359 C C   . SER A 1 178 ? -21.704 29.449  -10.478 1.00 41.74  ? 178 SER A C   1 
ATOM   1360 O O   . SER A 1 178 ? -20.871 28.576  -10.264 1.00 39.53  ? 178 SER A O   1 
ATOM   1361 C CB  . SER A 1 178 ? -23.931 28.511  -11.144 1.00 42.91  ? 178 SER A CB  1 
ATOM   1362 O OG  . SER A 1 178 ? -24.559 29.056  -9.995  1.00 45.64  ? 178 SER A OG  1 
ATOM   1363 N N   . ASN A 1 179 ? -21.807 30.550  -9.740  1.00 41.09  ? 179 ASN A N   1 
ATOM   1364 C CA  . ASN A 1 179 ? -20.972 30.752  -8.570  1.00 43.93  ? 179 ASN A CA  1 
ATOM   1365 C C   . ASN A 1 179 ? -21.800 30.640  -7.289  1.00 48.44  ? 179 ASN A C   1 
ATOM   1366 O O   . ASN A 1 179 ? -21.476 31.294  -6.305  1.00 51.20  ? 179 ASN A O   1 
ATOM   1367 C CB  . ASN A 1 179 ? -20.191 32.066  -8.632  1.00 47.50  ? 179 ASN A CB  1 
ATOM   1368 C CG  . ASN A 1 179 ? -21.028 33.316  -8.610  1.00 53.89  ? 179 ASN A CG  1 
ATOM   1369 O OD1 . ASN A 1 179 ? -22.272 33.287  -8.588  1.00 53.86  ? 179 ASN A OD1 1 
ATOM   1370 N ND2 . ASN A 1 179 ? -20.348 34.454  -8.609  1.00 60.25  ? 179 ASN A ND2 1 
ATOM   1371 N N   . ALA A 1 180 ? -22.870 29.821  -7.297  1.00 44.67  ? 180 ALA A N   1 
ATOM   1372 C CA  . ALA A 1 180 ? -23.712 29.619  -6.124  1.00 47.15  ? 180 ALA A CA  1 
ATOM   1373 C C   . ALA A 1 180 ? -22.870 29.092  -4.955  1.00 46.15  ? 180 ALA A C   1 
ATOM   1374 O O   . ALA A 1 180 ? -21.902 28.343  -5.160  1.00 41.12  ? 180 ALA A O   1 
ATOM   1375 C CB  . ALA A 1 180 ? -24.833 28.645  -6.444  1.00 46.23  ? 180 ALA A CB  1 
ATOM   1376 N N   . ASP A 1 181 ? -23.177 29.563  -3.750  1.00 45.85  ? 181 ASP A N   1 
ATOM   1377 C CA  . ASP A 1 181 ? -22.420 29.176  -2.570  1.00 45.76  ? 181 ASP A CA  1 
ATOM   1378 C C   . ASP A 1 181 ? -22.699 27.705  -2.242  1.00 42.56  ? 181 ASP A C   1 
ATOM   1379 O O   . ASP A 1 181 ? -23.855 27.318  -2.033  1.00 44.87  ? 181 ASP A O   1 
ATOM   1380 C CB  . ASP A 1 181 ? -22.778 30.105  -1.398  1.00 48.44  ? 181 ASP A CB  1 
ATOM   1381 C CG  . ASP A 1 181 ? -22.266 29.657  -0.046  1.00 50.99  ? 181 ASP A CG  1 
ATOM   1382 O OD1 . ASP A 1 181 ? -21.165 29.045  0.009   1.00 46.87  ? 181 ASP A OD1 1 
ATOM   1383 O OD2 . ASP A 1 181 ? -22.956 29.919  0.963   1.00 55.89  ? 181 ASP A OD2 1 
ATOM   1384 N N   . VAL A 1 182 ? -21.652 26.869  -2.274  1.00 42.36  ? 182 VAL A N   1 
ATOM   1385 C CA  . VAL A 1 182 ? -21.805 25.453  -1.969  1.00 39.34  ? 182 VAL A CA  1 
ATOM   1386 C C   . VAL A 1 182 ? -22.182 25.220  -0.499  1.00 42.68  ? 182 VAL A C   1 
ATOM   1387 O O   . VAL A 1 182 ? -22.892 24.263  -0.214  1.00 40.57  ? 182 VAL A O   1 
ATOM   1388 C CB  . VAL A 1 182 ? -20.539 24.634  -2.337  1.00 36.96  ? 182 VAL A CB  1 
ATOM   1389 C CG1 . VAL A 1 182 ? -20.268 24.688  -3.829  1.00 34.31  ? 182 VAL A CG1 1 
ATOM   1390 C CG2 . VAL A 1 182 ? -19.325 25.089  -1.527  1.00 34.68  ? 182 VAL A CG2 1 
ATOM   1391 N N   . LEU A 1 183 ? -21.699 26.078  0.427   1.00 43.71  ? 183 LEU A N   1 
ATOM   1392 C CA  . LEU A 1 183 ? -21.971 25.936  1.861   1.00 45.16  ? 183 LEU A CA  1 
ATOM   1393 C C   . LEU A 1 183 ? -23.471 25.896  2.172   1.00 46.42  ? 183 LEU A C   1 
ATOM   1394 O O   . LEU A 1 183 ? -23.877 25.209  3.105   1.00 42.44  ? 183 LEU A O   1 
ATOM   1395 C CB  . LEU A 1 183 ? -21.226 27.005  2.696   1.00 45.46  ? 183 LEU A CB  1 
ATOM   1396 C CG  . LEU A 1 183 ? -19.657 27.004  2.743   1.00 51.64  ? 183 LEU A CG  1 
ATOM   1397 C CD1 . LEU A 1 183 ? -19.036 28.207  3.491   1.00 41.37  ? 183 LEU A CD1 1 
ATOM   1398 C CD2 . LEU A 1 183 ? -19.102 25.685  3.232   1.00 51.14  ? 183 LEU A CD2 1 
ATOM   1399 N N   . LYS A 1 184 ? -24.290 26.564  1.341   1.00 49.20  ? 184 LYS A N   1 
ATOM   1400 C CA  . LYS A 1 184 ? -25.756 26.584  1.420   1.00 42.33  ? 184 LYS A CA  1 
ATOM   1401 C C   . LYS A 1 184 ? -26.307 25.153  1.235   1.00 44.96  ? 184 LYS A C   1 
ATOM   1402 O O   . LYS A 1 184 ? -27.164 24.700  2.002   1.00 42.69  ? 184 LYS A O   1 
ATOM   1403 C CB  . LYS A 1 184 ? -26.306 27.517  0.315   1.00 49.46  ? 184 LYS A CB  1 
ATOM   1404 C CG  . LYS A 1 184 ? -27.506 28.350  0.739   1.00 59.63  ? 184 LYS A CG  1 
ATOM   1405 C CD  . LYS A 1 184 ? -28.255 28.970  -0.454  1.00 65.68  ? 184 LYS A CD  1 
ATOM   1406 C CE  . LYS A 1 184 ? -28.264 30.488  -0.457  1.00 72.72  ? 184 LYS A CE  1 
ATOM   1407 N NZ  . LYS A 1 184 ? -28.852 31.047  -1.717  1.00 73.29  ? 184 LYS A NZ  1 
ATOM   1408 N N   . VAL A 1 185 ? -25.784 24.436  0.223   1.00 40.59  ? 185 VAL A N   1 
ATOM   1409 C CA  . VAL A 1 185 ? -26.178 23.068  -0.118  1.00 38.98  ? 185 VAL A CA  1 
ATOM   1410 C C   . VAL A 1 185 ? -25.773 22.082  0.970   1.00 42.22  ? 185 VAL A C   1 
ATOM   1411 O O   . VAL A 1 185 ? -26.596 21.234  1.360   1.00 43.00  ? 185 VAL A O   1 
ATOM   1412 C CB  . VAL A 1 185 ? -25.621 22.675  -1.508  1.00 39.07  ? 185 VAL A CB  1 
ATOM   1413 C CG1 . VAL A 1 185 ? -26.088 21.283  -1.912  1.00 41.07  ? 185 VAL A CG1 1 
ATOM   1414 C CG2 . VAL A 1 185 ? -26.026 23.708  -2.553  1.00 38.64  ? 185 VAL A CG2 1 
ATOM   1415 N N   . VAL A 1 186 ? -24.530 22.223  1.498   1.00 39.72  ? 186 VAL A N   1 
ATOM   1416 C CA  . VAL A 1 186 ? -24.021 21.395  2.602   1.00 42.54  ? 186 VAL A CA  1 
ATOM   1417 C C   . VAL A 1 186 ? -24.936 21.570  3.831   1.00 45.38  ? 186 VAL A C   1 
ATOM   1418 O O   . VAL A 1 186 ? -25.218 20.595  4.521   1.00 43.29  ? 186 VAL A O   1 
ATOM   1419 C CB  . VAL A 1 186 ? -22.557 21.732  2.984   1.00 41.35  ? 186 VAL A CB  1 
ATOM   1420 C CG1 . VAL A 1 186 ? -21.957 20.646  3.888   1.00 38.76  ? 186 VAL A CG1 1 
ATOM   1421 C CG2 . VAL A 1 186 ? -21.692 21.930  1.748   1.00 36.73  ? 186 VAL A CG2 1 
ATOM   1422 N N   . GLU A 1 187 ? -25.426 22.788  4.085   1.00 43.75  ? 187 GLU A N   1 
ATOM   1423 C CA  . GLU A 1 187 ? -26.356 23.018  5.230   1.00 49.20  ? 187 GLU A CA  1 
ATOM   1424 C C   . GLU A 1 187 ? -27.667 22.257  4.996   1.00 51.49  ? 187 GLU A C   1 
ATOM   1425 O O   . GLU A 1 187 ? -28.126 21.582  5.935   1.00 54.68  ? 187 GLU A O   1 
ATOM   1426 C CB  . GLU A 1 187 ? -26.610 24.514  5.423   1.00 50.72  ? 187 GLU A CB  1 
ATOM   1427 C CG  . GLU A 1 187 ? -25.415 25.257  5.988   1.00 58.65  ? 187 GLU A CG  1 
ATOM   1428 C CD  . GLU A 1 187 ? -25.464 26.762  5.795   1.00 66.48  ? 187 GLU A CD  1 
ATOM   1429 O OE1 . GLU A 1 187 ? -24.528 27.446  6.254   1.00 71.07  ? 187 GLU A OE1 1 
ATOM   1430 O OE2 . GLU A 1 187 ? -26.436 27.246  5.181   1.00 69.38  ? 187 GLU A OE2 1 
ATOM   1431 N N   . LYS A 1 188 ? -28.261 22.387  3.809   1.00 46.31  ? 188 LYS A N   1 
ATOM   1432 C CA  . LYS A 1 188 ? -29.488 21.673  3.447   1.00 48.68  ? 188 LYS A CA  1 
ATOM   1433 C C   . LYS A 1 188 ? -29.344 20.147  3.686   1.00 53.91  ? 188 LYS A C   1 
ATOM   1434 O O   . LYS A 1 188 ? -30.257 19.512  4.215   1.00 55.50  ? 188 LYS A O   1 
ATOM   1435 C CB  . LYS A 1 188 ? -29.837 21.972  1.979   1.00 52.66  ? 188 LYS A CB  1 
ATOM   1436 C CG  . LYS A 1 188 ? -30.963 21.129  1.384   1.00 53.01  ? 188 LYS A CG  1 
ATOM   1437 C CD  . LYS A 1 188 ? -32.337 21.637  1.786   1.00 55.43  ? 188 LYS A CD  1 
ATOM   1438 C CE  . LYS A 1 188 ? -33.401 20.567  1.702   1.00 57.80  ? 188 LYS A CE  1 
ATOM   1439 N NZ  . LYS A 1 188 ? -34.087 20.385  3.006   1.00 50.05  ? 188 LYS A NZ  1 
ATOM   1440 N N   . ASP A 1 189 ? -28.179 19.574  3.346   1.00 50.20  ? 189 ASP A N   1 
ATOM   1441 C CA  . ASP A 1 189 ? -27.914 18.163  3.556   1.00 52.49  ? 189 ASP A CA  1 
ATOM   1442 C C   . ASP A 1 189 ? -27.647 17.810  5.021   1.00 54.26  ? 189 ASP A C   1 
ATOM   1443 O O   . ASP A 1 189 ? -27.918 16.678  5.404   1.00 56.20  ? 189 ASP A O   1 
ATOM   1444 C CB  . ASP A 1 189 ? -26.719 17.702  2.694   1.00 44.06  ? 189 ASP A CB  1 
ATOM   1445 C CG  . ASP A 1 189 ? -26.981 17.695  1.196   1.00 48.36  ? 189 ASP A CG  1 
ATOM   1446 O OD1 . ASP A 1 189 ? -28.146 17.925  0.793   1.00 52.66  ? 189 ASP A OD1 1 
ATOM   1447 O OD2 . ASP A 1 189 ? -26.022 17.463  0.425   1.00 43.67  ? 189 ASP A OD2 1 
ATOM   1448 N N   . ARG A 1 190 ? -27.089 18.744  5.822   1.00 53.40  ? 190 ARG A N   1 
ATOM   1449 C CA  . ARG A 1 190 ? -26.709 18.515  7.228   1.00 63.10  ? 190 ARG A CA  1 
ATOM   1450 C C   . ARG A 1 190 ? -27.706 17.648  8.002   1.00 70.16  ? 190 ARG A C   1 
ATOM   1451 O O   . ARG A 1 190 ? -27.302 16.654  8.610   1.00 63.69  ? 190 ARG A O   1 
ATOM   1452 C CB  . ARG A 1 190 ? -26.427 19.827  7.964   1.00 63.80  ? 190 ARG A CB  1 
ATOM   1453 C CG  . ARG A 1 190 ? -25.716 19.610  9.286   1.00 68.67  ? 190 ARG A CG  1 
ATOM   1454 C CD  . ARG A 1 190 ? -25.359 20.917  9.954   1.00 67.74  ? 190 ARG A CD  1 
ATOM   1455 N NE  . ARG A 1 190 ? -26.261 21.981  9.524   1.00 72.20  ? 190 ARG A NE  1 
ATOM   1456 C CZ  . ARG A 1 190 ? -27.350 22.363  10.190  1.00 73.79  ? 190 ARG A CZ  1 
ATOM   1457 N NH1 . ARG A 1 190 ? -27.696 21.753  11.319  1.00 70.28  ? 190 ARG A NH1 1 
ATOM   1458 N NH2 . ARG A 1 190 ? -28.103 23.352  9.728   1.00 69.99  ? 190 ARG A NH2 1 
ATOM   1459 N N   . ASN A 1 191 ? -28.994 17.986  7.891   1.00 83.80  ? 191 ASN A N   1 
ATOM   1460 C CA  . ASN A 1 191 ? -30.049 17.146  8.516   1.00 86.39  ? 191 ASN A CA  1 
ATOM   1461 C C   . ASN A 1 191 ? -30.488 16.105  7.484   1.00 92.97  ? 191 ASN A C   1 
ATOM   1462 O O   . ASN A 1 191 ? -30.592 16.505  6.321   1.00 90.69  ? 191 ASN A O   1 
ATOM   1463 C CB  . ASN A 1 191 ? -31.220 17.994  9.018   1.00 91.32  ? 191 ASN A CB  1 
ATOM   1464 C CG  . ASN A 1 191 ? -30.797 19.050  10.018  1.00 97.43  ? 191 ASN A CG  1 
ATOM   1465 O OD1 . ASN A 1 191 ? -29.663 19.045  10.493  1.00 91.31  ? 191 ASN A OD1 1 
ATOM   1466 N ND2 . ASN A 1 191 ? -31.702 19.957  10.346  1.00 88.44  ? 191 ASN A ND2 1 
ATOM   1467 N N   . SER A 1 192 ? -30.710 14.847  7.882   1.00 90.20  ? 192 SER A N   1 
ATOM   1468 C CA  . SER A 1 192 ? -31.118 13.727  7.024   1.00 87.68  ? 192 SER A CA  1 
ATOM   1469 C C   . SER A 1 192 ? -30.139 13.522  5.864   1.00 83.20  ? 192 SER A C   1 
ATOM   1470 O O   . SER A 1 192 ? -30.261 14.164  4.820   1.00 78.85  ? 192 SER A O   1 
ATOM   1471 C CB  . SER A 1 192 ? -32.550 13.884  6.516   1.00 83.33  ? 192 SER A CB  1 
ATOM   1472 O OG  . SER A 1 192 ? -32.658 14.841  5.474   1.00 82.50  ? 192 SER A OG  1 
ATOM   1473 N N   . ALA B 2 4   ? -21.514 -5.877  1.619   1.00 79.61  ? 4   ALA C N   1 
ATOM   1474 C CA  . ALA B 2 4   ? -20.357 -4.966  1.454   1.00 79.98  ? 4   ALA C CA  1 
ATOM   1475 C C   . ALA B 2 4   ? -20.577 -4.071  0.230   1.00 80.24  ? 4   ALA C C   1 
ATOM   1476 O O   . ALA B 2 4   ? -20.076 -4.424  -0.855  1.00 80.46  ? 4   ALA C O   1 
ATOM   1477 C CB  . ALA B 2 4   ? -19.084 -5.767  1.335   1.00 80.13  ? 4   ALA C CB  1 
ATOM   1478 N N   . SER B 2 5   ? -21.504 -3.107  0.327   1.00 80.23  ? 5   SER C N   1 
ATOM   1479 C CA  . SER B 2 5   ? -21.908 -2.338  -0.883  1.00 80.51  ? 5   SER C CA  1 
ATOM   1480 C C   . SER B 2 5   ? -20.911 -1.292  -1.379  1.00 80.86  ? 5   SER C C   1 
ATOM   1481 O O   . SER B 2 5   ? -20.751 -0.301  -0.642  1.00 80.79  ? 5   SER C O   1 
ATOM   1482 C CB  . SER B 2 5   ? -23.272 -1.737  -0.707  1.00 82.77  ? 5   SER C CB  1 
ATOM   1483 O OG  . SER B 2 5   ? -24.261 -2.734  -0.490  1.00 88.55  ? 5   SER C OG  1 
ATOM   1484 N N   . LYS B 2 6   ? -20.607 -1.366  -2.684  1.00 83.07  ? 6   LYS C N   1 
ATOM   1485 C CA  . LYS B 2 6   ? -19.770 -0.356  -3.391  1.00 104.53 ? 6   LYS C CA  1 
ATOM   1486 C C   . LYS B 2 6   ? -18.281 -0.708  -3.382  1.00 107.50 ? 6   LYS C C   1 
ATOM   1487 O O   . LYS B 2 6   ? -17.813 -1.400  -2.456  1.00 101.49 ? 6   LYS C O   1 
ATOM   1488 C CB  . LYS B 2 6   ? -20.187 1.094   -3.116  1.00 118.94 ? 6   LYS C CB  1 
ATOM   1489 C CG  . LYS B 2 6   ? -21.249 1.649   -4.054  1.00 100.67 ? 6   LYS C CG  1 
ATOM   1490 C CD  . LYS B 2 6   ? -20.707 2.680   -5.019  1.00 93.21  ? 6   LYS C CD  1 
ATOM   1491 C CE  . LYS B 2 6   ? -20.615 4.058   -4.401  1.00 98.04  ? 6   LYS C CE  1 
ATOM   1492 N NZ  . LYS B 2 6   ? -19.612 4.911   -5.080  1.00 85.10  ? 6   LYS C NZ  1 
ATOM   1493 N N   . ASP B 2 7   ? -17.597 -0.221  -4.420  1.00 148.32 ? 7   ASP C N   1 
ATOM   1494 C CA  . ASP B 2 7   ? -16.147 -0.427  -4.661  1.00 149.75 ? 7   ASP C CA  1 
ATOM   1495 C C   . ASP B 2 7   ? -15.291 0.796   -4.291  1.00 159.42 ? 7   ASP C C   1 
ATOM   1496 O O   . ASP B 2 7   ? -14.190 0.883   -4.866  1.00 149.19 ? 7   ASP C O   1 
ATOM   1497 C CB  . ASP B 2 7   ? -15.903 -0.630  -6.153  1.00 149.11 ? 7   ASP C CB  1 
ATOM   1498 C CG  . ASP B 2 7   ? -16.654 0.371   -7.014  1.00 146.90 ? 7   ASP C CG  1 
ATOM   1499 O OD1 . ASP B 2 7   ? -17.192 1.356   -6.469  1.00 140.78 ? 7   ASP C OD1 1 
ATOM   1500 O OD2 . ASP B 2 7   ? -16.696 0.160   -8.222  1.00 146.04 ? 7   ASP C OD2 1 
ATOM   1501 N N   . PRO B 2 8   ? -15.674 1.777   -3.430  1.00 263.97 ? 8   PRO C N   1 
ATOM   1502 C CA  . PRO B 2 8   ? -14.828 2.925   -3.174  1.00 264.13 ? 8   PRO C CA  1 
ATOM   1503 C C   . PRO B 2 8   ? -14.026 2.901   -1.880  1.00 267.07 ? 8   PRO C C   1 
ATOM   1504 O O   . PRO B 2 8   ? -14.603 2.830   -0.808  1.00 267.12 ? 8   PRO C O   1 
ATOM   1505 C CB  . PRO B 2 8   ? -15.827 4.077   -2.976  1.00 263.91 ? 8   PRO C CB  1 
ATOM   1506 C CG  . PRO B 2 8   ? -17.167 3.428   -3.175  1.00 259.63 ? 8   PRO C CG  1 
ATOM   1507 C CD  . PRO B 2 8   ? -16.920 2.008   -2.721  1.00 260.59 ? 8   PRO C CD  1 
ATOM   1508 N N   . GLY B 2 9   ? -12.708 2.993   -2.015  1.00 165.91 ? 9   GLY C N   1 
ATOM   1509 C CA  . GLY B 2 9   ? -11.904 3.193   -0.804  1.00 158.14 ? 9   GLY C CA  1 
ATOM   1510 C C   . GLY B 2 9   ? -11.942 4.687   -0.635  1.00 159.04 ? 9   GLY C C   1 
ATOM   1511 O O   . GLY B 2 9   ? -11.373 5.200   0.324   1.00 157.31 ? 9   GLY C O   1 
ATOM   1512 N N   . ALA B 2 10  ? -12.647 5.342   -1.555  1.00 130.31 ? 10  ALA C N   1 
ATOM   1513 C CA  . ALA B 2 10  ? -12.794 6.806   -1.543  1.00 101.85 ? 10  ALA C CA  1 
ATOM   1514 C C   . ALA B 2 10  ? -13.448 7.254   -0.244  1.00 95.65  ? 10  ALA C C   1 
ATOM   1515 O O   . ALA B 2 10  ? -13.262 8.419   0.068   1.00 83.39  ? 10  ALA C O   1 
ATOM   1516 C CB  . ALA B 2 10  ? -13.646 7.175   -2.719  1.00 90.52  ? 10  ALA C CB  1 
ATOM   1517 N N   . VAL B 2 11  ? -14.355 6.458   0.325   1.00 107.31 ? 11  VAL C N   1 
ATOM   1518 C CA  . VAL B 2 11  ? -14.949 6.773   1.661   1.00 94.21  ? 11  VAL C CA  1 
ATOM   1519 C C   . VAL B 2 11  ? -13.903 6.602   2.775   1.00 88.38  ? 11  VAL C C   1 
ATOM   1520 O O   . VAL B 2 11  ? -13.949 7.390   3.740   1.00 82.58  ? 11  VAL C O   1 
ATOM   1521 C CB  . VAL B 2 11  ? -16.215 5.938   1.904   1.00 82.70  ? 11  VAL C CB  1 
ATOM   1522 C CG1 . VAL B 2 11  ? -16.788 5.481   0.578   1.00 82.00  ? 11  VAL C CG1 1 
ATOM   1523 C CG2 . VAL B 2 11  ? -15.936 4.742   2.794   1.00 83.92  ? 11  VAL C CG2 1 
ATOM   1524 N N   . ASP B 2 12  ? -13.021 5.599   2.674   1.00 92.27  ? 12  ASP C N   1 
ATOM   1525 C CA  . ASP B 2 12  ? -12.027 5.320   3.748   1.00 84.70  ? 12  ASP C CA  1 
ATOM   1526 C C   . ASP B 2 12  ? -10.772 6.152   3.481   1.00 79.17  ? 12  ASP C C   1 
ATOM   1527 O O   . ASP B 2 12  ? -10.498 7.068   4.283   1.00 73.30  ? 12  ASP C O   1 
ATOM   1528 C CB  . ASP B 2 12  ? -11.677 3.831   3.798   1.00 88.10  ? 12  ASP C CB  1 
ATOM   1529 C CG  . ASP B 2 12  ? -12.884 2.928   3.981   1.00 90.11  ? 12  ASP C CG  1 
ATOM   1530 O OD1 . ASP B 2 12  ? -13.661 3.175   4.923   1.00 95.63  ? 12  ASP C OD1 1 
ATOM   1531 O OD2 . ASP B 2 12  ? -13.041 1.991   3.174   1.00 91.38  ? 12  ASP C OD2 1 
ATOM   1532 N N   . ALA B 2 13  ? -10.038 5.834   2.410   1.00 77.05  ? 13  ALA C N   1 
ATOM   1533 C CA  . ALA B 2 13  ? -8.858  6.620   2.014   1.00 66.61  ? 13  ALA C CA  1 
ATOM   1534 C C   . ALA B 2 13  ? -9.270  8.100   1.973   1.00 60.76  ? 13  ALA C C   1 
ATOM   1535 O O   . ALA B 2 13  ? -10.402 8.387   1.594   1.00 65.83  ? 13  ALA C O   1 
ATOM   1536 C CB  . ALA B 2 13  ? -8.392  6.187   0.631   1.00 59.53  ? 13  ALA C CB  1 
ATOM   1537 N N   . LYS B 2 14  ? -8.384  9.030   2.335   1.00 52.46  ? 14  LYS C N   1 
ATOM   1538 C CA  . LYS B 2 14  ? -8.738  10.453  2.353   1.00 52.45  ? 14  LYS C CA  1 
ATOM   1539 C C   . LYS B 2 14  ? -8.767  11.115  0.948   1.00 50.14  ? 14  LYS C C   1 
ATOM   1540 O O   . LYS B 2 14  ? -8.087  10.661  0.030   1.00 46.38  ? 14  LYS C O   1 
ATOM   1541 C CB  . LYS B 2 14  ? -7.826  11.223  3.325   1.00 54.40  ? 14  LYS C CB  1 
ATOM   1542 C CG  . LYS B 2 14  ? -7.959  10.765  4.780   1.00 54.41  ? 14  LYS C CG  1 
ATOM   1543 C CD  . LYS B 2 14  ? -9.277  11.189  5.405   1.00 49.17  ? 14  LYS C CD  1 
ATOM   1544 C CE  . LYS B 2 14  ? -9.238  11.067  6.904   1.00 53.65  ? 14  LYS C CE  1 
ATOM   1545 N NZ  . LYS B 2 14  ? -7.841  10.948  7.396   1.00 51.92  ? 14  LYS C NZ  1 
ATOM   1546 N N   . PRO B 2 15  ? -9.612  12.145  0.755   1.00 48.18  ? 15  PRO C N   1 
ATOM   1547 C CA  . PRO B 2 15  ? -9.681  12.784  -0.560  1.00 45.92  ? 15  PRO C CA  1 
ATOM   1548 C C   . PRO B 2 15  ? -8.406  13.525  -0.905  1.00 43.65  ? 15  PRO C C   1 
ATOM   1549 O O   . PRO B 2 15  ? -7.747  14.091  -0.031  1.00 39.97  ? 15  PRO C O   1 
ATOM   1550 C CB  . PRO B 2 15  ? -10.846 13.766  -0.429  1.00 42.94  ? 15  PRO C CB  1 
ATOM   1551 C CG  . PRO B 2 15  ? -11.015 13.992  1.007   1.00 46.52  ? 15  PRO C CG  1 
ATOM   1552 C CD  . PRO B 2 15  ? -10.547 12.761  1.713   1.00 49.82  ? 15  PRO C CD  1 
ATOM   1553 N N   . LEU B 2 16  ? -8.064  13.514  -2.180  1.00 36.24  ? 16  LEU C N   1 
ATOM   1554 C CA  . LEU B 2 16  ? -6.897  14.227  -2.666  1.00 38.32  ? 16  LEU C CA  1 
ATOM   1555 C C   . LEU B 2 16  ? -7.344  15.647  -3.046  1.00 38.35  ? 16  LEU C C   1 
ATOM   1556 O O   . LEU B 2 16  ? -8.347  15.791  -3.734  1.00 37.02  ? 16  LEU C O   1 
ATOM   1557 C CB  . LEU B 2 16  ? -6.320  13.481  -3.879  1.00 41.46  ? 16  LEU C CB  1 
ATOM   1558 C CG  . LEU B 2 16  ? -5.276  14.216  -4.697  1.00 39.97  ? 16  LEU C CG  1 
ATOM   1559 C CD1 . LEU B 2 16  ? -4.057  14.607  -3.842  1.00 40.30  ? 16  LEU C CD1 1 
ATOM   1560 C CD2 . LEU B 2 16  ? -4.872  13.384  -5.864  1.00 42.50  ? 16  LEU C CD2 1 
ATOM   1561 N N   . VAL B 2 17  ? -6.681  16.685  -2.493  1.00 38.77  ? 17  VAL C N   1 
ATOM   1562 C CA  . VAL B 2 17  ? -6.984  18.092  -2.765  1.00 38.63  ? 17  VAL C CA  1 
ATOM   1563 C C   . VAL B 2 17  ? -5.714  18.776  -3.278  1.00 39.15  ? 17  VAL C C   1 
ATOM   1564 O O   . VAL B 2 17  ? -4.733  18.913  -2.539  1.00 43.61  ? 17  VAL C O   1 
ATOM   1565 C CB  . VAL B 2 17  ? -7.552  18.851  -1.528  1.00 36.94  ? 17  VAL C CB  1 
ATOM   1566 C CG1 . VAL B 2 17  ? -7.611  20.345  -1.806  1.00 37.51  ? 17  VAL C CG1 1 
ATOM   1567 C CG2 . VAL B 2 17  ? -8.928  18.319  -1.128  1.00 35.06  ? 17  VAL C CG2 1 
ATOM   1568 N N   . VAL B 2 18  ? -5.715  19.179  -4.538  1.00 39.58  ? 18  VAL C N   1 
ATOM   1569 C CA  . VAL B 2 18  ? -4.562  19.831  -5.152  1.00 44.26  ? 18  VAL C CA  1 
ATOM   1570 C C   . VAL B 2 18  ? -4.875  21.310  -5.399  1.00 45.12  ? 18  VAL C C   1 
ATOM   1571 O O   . VAL B 2 18  ? -5.883  21.623  -6.026  1.00 41.21  ? 18  VAL C O   1 
ATOM   1572 C CB  . VAL B 2 18  ? -4.146  19.101  -6.455  1.00 42.43  ? 18  VAL C CB  1 
ATOM   1573 C CG1 . VAL B 2 18  ? -3.013  19.831  -7.174  1.00 45.85  ? 18  VAL C CG1 1 
ATOM   1574 C CG2 . VAL B 2 18  ? -3.761  17.666  -6.164  1.00 40.51  ? 18  VAL C CG2 1 
ATOM   1575 N N   . GLU B 2 19  ? -4.043  22.216  -4.867  1.00 48.88  ? 19  GLU C N   1 
ATOM   1576 C CA  . GLU B 2 19  ? -4.258  23.649  -5.059  1.00 52.94  ? 19  GLU C CA  1 
ATOM   1577 C C   . GLU B 2 19  ? -3.733  24.064  -6.421  1.00 52.06  ? 19  GLU C C   1 
ATOM   1578 O O   . GLU B 2 19  ? -2.683  23.578  -6.849  1.00 54.76  ? 19  GLU C O   1 
ATOM   1579 C CB  . GLU B 2 19  ? -3.550  24.460  -3.967  1.00 56.57  ? 19  GLU C CB  1 
ATOM   1580 C CG  . GLU B 2 19  ? -3.998  24.088  -2.570  1.00 59.57  ? 19  GLU C CG  1 
ATOM   1581 C CD  . GLU B 2 19  ? -5.400  24.563  -2.255  1.00 63.69  ? 19  GLU C CD  1 
ATOM   1582 O OE1 . GLU B 2 19  ? -5.642  25.789  -2.343  1.00 65.03  ? 19  GLU C OE1 1 
ATOM   1583 O OE2 . GLU B 2 19  ? -6.260  23.713  -1.933  1.00 63.14  ? 19  GLU C OE2 1 
ATOM   1584 N N   . ILE B 2 20  ? -4.463  24.931  -7.117  1.00 50.33  ? 20  ILE C N   1 
ATOM   1585 C CA  . ILE B 2 20  ? -4.043  25.378  -8.448  1.00 54.99  ? 20  ILE C CA  1 
ATOM   1586 C C   . ILE B 2 20  ? -3.839  26.902  -8.521  1.00 58.05  ? 20  ILE C C   1 
ATOM   1587 O O   . ILE B 2 20  ? -3.929  27.608  -7.513  1.00 55.89  ? 20  ILE C O   1 
ATOM   1588 C CB  . ILE B 2 20  ? -5.000  24.862  -9.553  1.00 48.76  ? 20  ILE C CB  1 
ATOM   1589 C CG1 . ILE B 2 20  ? -4.868  23.337  -9.756  1.00 44.63  ? 20  ILE C CG1 1 
ATOM   1590 C CG2 . ILE B 2 20  ? -4.768  25.615  -10.874 1.00 52.41  ? 20  ILE C CG2 1 
ATOM   1591 C CD1 . ILE B 2 20  ? -5.861  22.795  -10.708 1.00 36.96  ? 20  ILE C CD1 1 
HETATM 1592 O O   . HOH C 3 .   ? 2.548   19.196  -16.068 1.00 45.93  ? 201 HOH A O   1 
HETATM 1593 O O   . HOH C 3 .   ? -1.050  -1.329  -8.562  1.00 50.43  ? 202 HOH A O   1 
HETATM 1594 O O   . HOH C 3 .   ? -27.707 6.895   -16.333 1.00 44.05  ? 203 HOH A O   1 
HETATM 1595 O O   . HOH C 3 .   ? -2.968  7.829   -3.756  1.00 46.74  ? 204 HOH A O   1 
HETATM 1596 O O   . HOH C 3 .   ? -0.274  16.240  -5.788  1.00 52.24  ? 205 HOH A O   1 
HETATM 1597 O O   . HOH C 3 .   ? -15.311 25.633  7.578   1.00 57.01  ? 206 HOH A O   1 
HETATM 1598 O O   . HOH C 3 .   ? -25.038 -6.378  -12.318 1.00 50.10  ? 207 HOH A O   1 
HETATM 1599 O O   . HOH C 3 .   ? -9.928  -16.585 0.276   1.00 55.60  ? 208 HOH A O   1 
HETATM 1600 O O   . HOH C 3 .   ? -12.342 -0.666  -15.437 1.00 40.72  ? 209 HOH A O   1 
HETATM 1601 O O   . HOH C 3 .   ? -10.762 21.303  7.495   1.00 46.40  ? 210 HOH A O   1 
HETATM 1602 O O   . HOH C 3 .   ? 0.083   20.656  -14.592 1.00 49.41  ? 211 HOH A O   1 
HETATM 1603 O O   . HOH C 3 .   ? -4.229  21.658  -20.663 1.00 44.01  ? 212 HOH A O   1 
HETATM 1604 O O   . HOH C 3 .   ? -3.158  -1.784  -13.444 1.00 46.41  ? 213 HOH A O   1 
HETATM 1605 O O   . HOH C 3 .   ? -9.896  -2.459  -17.323 1.00 45.81  ? 214 HOH A O   1 
HETATM 1606 O O   . HOH C 3 .   ? -24.365 0.683   -10.941 1.00 42.07  ? 215 HOH A O   1 
HETATM 1607 O O   . HOH C 3 .   ? -17.083 -1.611  -16.721 1.00 49.78  ? 216 HOH A O   1 
HETATM 1608 O O   . HOH C 3 .   ? -19.642 25.105  -17.851 1.00 45.85  ? 217 HOH A O   1 
HETATM 1609 O O   . HOH C 3 .   ? -6.256  27.686  -5.253  1.00 51.13  ? 218 HOH A O   1 
HETATM 1610 O O   . HOH C 3 .   ? -11.461 17.144  3.916   1.00 46.79  ? 219 HOH A O   1 
HETATM 1611 O O   . HOH C 3 .   ? -21.852 15.786  12.639  1.00 39.47  ? 220 HOH A O   1 
HETATM 1612 O O   . HOH C 3 .   ? -10.963 3.477   -20.395 1.00 42.91  ? 221 HOH A O   1 
HETATM 1613 O O   . HOH C 3 .   ? -9.919  13.797  -23.476 1.00 39.83  ? 222 HOH A O   1 
HETATM 1614 O O   . HOH C 3 .   ? -23.993 -2.978  -15.182 1.00 37.05  ? 223 HOH A O   1 
HETATM 1615 O O   . HOH C 3 .   ? -18.723 20.918  -22.401 1.00 34.74  ? 224 HOH A O   1 
HETATM 1616 O O   . HOH C 3 .   ? -15.228 29.049  4.521   1.00 57.77  ? 225 HOH A O   1 
HETATM 1617 O O   . HOH C 3 .   ? -1.678  8.776   -14.631 1.00 33.62  ? 226 HOH A O   1 
HETATM 1618 O O   . HOH C 3 .   ? -24.009 27.039  -15.279 1.00 41.03  ? 227 HOH A O   1 
HETATM 1619 O O   . HOH C 3 .   ? -24.875 13.531  -6.506  1.00 35.40  ? 228 HOH A O   1 
HETATM 1620 O O   . HOH C 3 .   ? -13.262 -18.274 5.329   1.00 43.83  ? 229 HOH A O   1 
HETATM 1621 O O   . HOH C 3 .   ? -18.617 8.502   6.152   1.00 36.42  ? 230 HOH A O   1 
HETATM 1622 O O   . HOH C 3 .   ? -27.929 6.089   -10.197 1.00 42.20  ? 231 HOH A O   1 
HETATM 1623 O O   . HOH C 3 .   ? -21.680 8.460   -12.059 1.00 29.85  ? 232 HOH A O   1 
HETATM 1624 O O   . HOH C 3 .   ? -9.491  28.960  0.058   1.00 49.56  ? 233 HOH A O   1 
HETATM 1625 O O   . HOH C 3 .   ? 1.150   19.396  -20.476 1.00 47.59  ? 234 HOH A O   1 
HETATM 1626 O O   . HOH C 3 .   ? -25.429 24.686  -14.342 1.00 49.95  ? 235 HOH A O   1 
HETATM 1627 O O   . HOH C 3 .   ? -14.082 27.172  -21.334 1.00 48.43  ? 236 HOH A O   1 
HETATM 1628 O O   . HOH C 3 .   ? -22.283 12.896  13.796  1.00 30.52  ? 237 HOH A O   1 
HETATM 1629 O O   . HOH C 3 .   ? -24.101 32.109  -10.561 1.00 47.29  ? 238 HOH A O   1 
HETATM 1630 O O   . HOH C 3 .   ? -12.677 -4.964  -17.932 1.00 49.19  ? 239 HOH A O   1 
HETATM 1631 O O   . HOH C 3 .   ? -14.279 5.866   -15.839 1.00 39.32  ? 240 HOH A O   1 
HETATM 1632 O O   . HOH C 3 .   ? -13.878 -2.362  -15.916 1.00 52.88  ? 241 HOH A O   1 
HETATM 1633 O O   . HOH C 3 .   ? -28.350 5.108   -14.509 1.00 38.83  ? 242 HOH A O   1 
HETATM 1634 O O   . HOH C 3 .   ? -15.978 -16.664 1.480   1.00 44.46  ? 243 HOH A O   1 
HETATM 1635 O O   . HOH C 3 .   ? -23.231 -4.098  -6.900  1.00 43.16  ? 244 HOH A O   1 
HETATM 1636 O O   . HOH C 3 .   ? -27.686 12.192  -11.429 1.00 41.24  ? 245 HOH A O   1 
HETATM 1637 O O   . HOH C 3 .   ? -12.320 28.833  -14.962 1.00 37.69  ? 246 HOH A O   1 
HETATM 1638 O O   . HOH C 3 .   ? -7.058  3.072   -0.571  1.00 49.96  ? 247 HOH A O   1 
HETATM 1639 O O   . HOH C 3 .   ? 1.602   21.031  -18.456 1.00 44.54  ? 248 HOH A O   1 
HETATM 1640 O O   . HOH C 3 .   ? -25.491 11.227  14.323  1.00 49.81  ? 249 HOH A O   1 
HETATM 1641 O O   . HOH C 3 .   ? -22.827 32.243  -13.906 1.00 44.12  ? 250 HOH A O   1 
HETATM 1642 O O   . HOH C 3 .   ? -21.634 -9.256  -11.932 1.00 46.91  ? 251 HOH A O   1 
HETATM 1643 O O   . HOH C 3 .   ? -10.504 -19.075 -10.721 1.00 49.26  ? 252 HOH A O   1 
HETATM 1644 O O   . HOH C 3 .   ? -13.043 5.403   -19.687 1.00 42.61  ? 253 HOH A O   1 
HETATM 1645 O O   . HOH C 3 .   ? -22.459 -10.230 -4.580  1.00 51.13  ? 254 HOH A O   1 
HETATM 1646 O O   . HOH C 3 .   ? -21.295 18.420  -19.146 1.00 41.21  ? 255 HOH A O   1 
HETATM 1647 O O   . HOH C 3 .   ? -27.560 12.342  4.938   1.00 58.49  ? 256 HOH A O   1 
HETATM 1648 O O   . HOH C 3 .   ? -14.383 -21.113 -14.650 1.00 43.76  ? 257 HOH A O   1 
HETATM 1649 O O   . HOH C 3 .   ? -18.289 -18.439 0.864   1.00 48.44  ? 258 HOH A O   1 
HETATM 1650 O O   . HOH C 3 .   ? -10.807 23.693  5.251   1.00 43.55  ? 259 HOH A O   1 
HETATM 1651 O O   . HOH C 3 .   ? -28.950 10.006  3.680   1.00 57.79  ? 260 HOH A O   1 
HETATM 1652 O O   . HOH C 3 .   ? 0.216   -4.169  -7.647  1.00 50.35  ? 261 HOH A O   1 
HETATM 1653 O O   . HOH C 3 .   ? -19.799 24.160  -22.969 1.00 48.76  ? 262 HOH A O   1 
HETATM 1654 O O   . HOH C 3 .   ? -23.071 22.355  7.691   1.00 48.68  ? 263 HOH A O   1 
HETATM 1655 O O   . HOH C 3 .   ? -0.785  24.262  -13.562 1.00 56.10  ? 264 HOH A O   1 
HETATM 1656 O O   . HOH C 3 .   ? -0.152  12.037  -20.439 1.00 49.68  ? 265 HOH A O   1 
HETATM 1657 O O   . HOH D 3 .   ? -1.842  21.680  -3.389  1.00 50.74  ? 101 HOH C O   1 
HETATM 1658 O O   . HOH D 3 .   ? -11.065 9.481   -1.136  1.00 41.22  ? 102 HOH C O   1 
HETATM 1659 O O   . HOH D 3 .   ? -4.771  16.320  -0.478  1.00 46.80  ? 103 HOH C O   1 
HETATM 1660 O O   . HOH D 3 .   ? -8.402  26.263  -2.141  1.00 49.86  ? 104 HOH C O   1 
HETATM 1661 O O   . HOH D 3 .   ? -23.406 -7.926  1.157   1.00 56.95  ? 105 HOH C O   1 
HETATM 1662 O O   . HOH D 3 .   ? -5.699  8.293   2.874   1.00 56.10  ? 106 HOH C O   1 
HETATM 1663 O O   . HOH D 3 .   ? -4.998  12.691  0.165   1.00 52.66  ? 107 HOH C O   1 
HETATM 1664 O O   . HOH D 3 .   ? -9.646  1.789   0.022   1.00 83.75  ? 108 HOH C 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   ? 0.8248 0.8228 0.8341 -0.0093 -0.0466 0.0031  1   ALA A N   
2    C CA  . ALA A 1   ? 0.7979 0.7981 0.7975 -0.0107 -0.0438 -0.0009 1   ALA A CA  
3    C C   . ALA A 1   ? 0.5699 0.5753 0.5621 -0.0107 -0.0455 0.0011  1   ALA A C   
4    O O   . ALA A 1   ? 0.5126 0.5182 0.5048 -0.0119 -0.0499 0.0072  1   ALA A O   
5    C CB  . ALA A 1   ? 1.0710 1.0617 1.0613 -0.0155 -0.0402 0.0021  1   ALA A CB  
6    N N   . LEU A 2   ? 0.4946 0.5049 0.4832 -0.0094 -0.0425 -0.0030 2   LEU A N   
7    C CA  . LEU A 2   ? 0.4304 0.4451 0.4142 -0.0092 -0.0428 -0.0010 2   LEU A CA  
8    C C   . LEU A 2   ? 0.3981 0.4141 0.3764 -0.0090 -0.0384 -0.0033 2   LEU A C   
9    O O   . LEU A 2   ? 0.2916 0.3133 0.2746 -0.0054 -0.0367 -0.0075 2   LEU A O   
10   C CB  . LEU A 2   ? 0.4204 0.4444 0.4136 -0.0035 -0.0433 -0.0018 2   LEU A CB  
11   C CG  . LEU A 2   ? 0.3970 0.4269 0.3895 -0.0028 -0.0426 0.0016  2   LEU A CG  
12   C CD1 . LEU A 2   ? 0.3899 0.4177 0.3850 -0.0075 -0.0478 0.0089  2   LEU A CD1 
13   C CD2 . LEU A 2   ? 0.3907 0.4291 0.3900 0.0044  -0.0391 -0.0002 2   LEU A CD2 
14   N N   . VAL A 3   ? 0.3447 0.3541 0.3128 -0.0131 -0.0369 -0.0003 3   VAL A N   
15   C CA  . VAL A 3   ? 0.3395 0.3490 0.3041 -0.0125 -0.0315 -0.0011 3   VAL A CA  
16   C C   . VAL A 3   ? 0.3700 0.3803 0.3321 -0.0140 -0.0333 0.0019  3   VAL A C   
17   O O   . VAL A 3   ? 0.2731 0.2766 0.2292 -0.0193 -0.0379 0.0045  3   VAL A O   
18   C CB  . VAL A 3   ? 0.3265 0.3240 0.2823 -0.0160 -0.0249 -0.0012 3   VAL A CB  
19   C CG1 . VAL A 3   ? 0.3336 0.3313 0.2892 -0.0144 -0.0184 -0.0009 3   VAL A CG1 
20   C CG2 . VAL A 3   ? 0.3227 0.3212 0.2868 -0.0145 -0.0223 -0.0028 3   VAL A CG2 
21   N N   . ILE A 4   ? 0.2932 0.3123 0.2608 -0.0096 -0.0305 0.0023  4   ILE A N   
22   C CA  . ILE A 4   ? 0.2995 0.3197 0.2683 -0.0109 -0.0307 0.0059  4   ILE A CA  
23   C C   . ILE A 4   ? 0.3479 0.3674 0.3157 -0.0091 -0.0238 0.0066  4   ILE A C   
24   O O   . ILE A 4   ? 0.2833 0.3073 0.2535 -0.0045 -0.0202 0.0054  4   ILE A O   
25   C CB  . ILE A 4   ? 0.3539 0.3857 0.3339 -0.0066 -0.0329 0.0085  4   ILE A CB  
26   C CG1 . ILE A 4   ? 0.3357 0.3775 0.3184 0.0016  -0.0286 0.0069  4   ILE A CG1 
27   C CG2 . ILE A 4   ? 0.3025 0.3345 0.2870 -0.0075 -0.0386 0.0087  4   ILE A CG2 
28   C CD1 . ILE A 4   ? 0.3345 0.3850 0.3248 0.0072  -0.0277 0.0085  4   ILE A CD1 
29   N N   . ALA A 5   ? 0.3191 0.3321 0.2848 -0.0132 -0.0226 0.0089  5   ALA A N   
30   C CA  . ALA A 5   ? 0.3447 0.3548 0.3111 -0.0117 -0.0151 0.0105  5   ALA A CA  
31   C C   . ALA A 5   ? 0.3419 0.3521 0.3140 -0.0139 -0.0149 0.0145  5   ALA A C   
32   O O   . ALA A 5   ? 0.3369 0.3439 0.3095 -0.0200 -0.0214 0.0152  5   ALA A O   
33   C CB  . ALA A 5   ? 0.3058 0.2993 0.2611 -0.0159 -0.0095 0.0073  5   ALA A CB  
34   N N   . PHE A 6   ? 0.3229 0.3373 0.3014 -0.0090 -0.0081 0.0182  6   PHE A N   
35   C CA  . PHE A 6   ? 0.3512 0.3640 0.3373 -0.0111 -0.0057 0.0228  6   PHE A CA  
36   C C   . PHE A 6   ? 0.3611 0.3606 0.3439 -0.0124 0.0027  0.0224  6   PHE A C   
37   O O   . PHE A 6   ? 0.3189 0.3215 0.3033 -0.0061 0.0088  0.0239  6   PHE A O   
38   C CB  . PHE A 6   ? 0.3324 0.3613 0.3302 -0.0031 -0.0028 0.0297  6   PHE A CB  
39   C CG  . PHE A 6   ? 0.3833 0.4096 0.3912 -0.0044 0.0029  0.0360  6   PHE A CG  
40   C CD1 . PHE A 6   ? 0.3599 0.3819 0.3761 -0.0122 -0.0010 0.0375  6   PHE A CD1 
41   C CD2 . PHE A 6   ? 0.3800 0.4065 0.3904 0.0012  0.0114  0.0408  6   PHE A CD2 
42   C CE1 . PHE A 6   ? 0.4455 0.4635 0.4732 -0.0144 0.0042  0.0430  6   PHE A CE1 
43   C CE2 . PHE A 6   ? 0.4054 0.4278 0.4266 -0.0001 0.0176  0.0470  6   PHE A CE2 
44   C CZ  . PHE A 6   ? 0.4242 0.4417 0.4540 -0.0082 0.0143  0.0475  6   PHE A CZ  
45   N N   . ILE A 7   ? 0.3442 0.3284 0.3236 -0.0208 0.0027  0.0206  7   ILE A N   
46   C CA  . ILE A 7   ? 0.3830 0.3509 0.3593 -0.0223 0.0123  0.0194  7   ILE A CA  
47   C C   . ILE A 7   ? 0.4422 0.4108 0.4323 -0.0234 0.0150  0.0252  7   ILE A C   
48   O O   . ILE A 7   ? 0.3993 0.3679 0.3942 -0.0302 0.0077  0.0257  7   ILE A O   
49   C CB  . ILE A 7   ? 0.4468 0.3906 0.4026 -0.0317 0.0120  0.0106  7   ILE A CB  
50   C CG1 . ILE A 7   ? 0.3995 0.3436 0.3441 -0.0292 0.0120  0.0069  7   ILE A CG1 
51   C CG2 . ILE A 7   ? 0.4367 0.3604 0.3892 -0.0332 0.0241  0.0086  7   ILE A CG2 
52   C CD1 . ILE A 7   ? 0.3882 0.3352 0.3241 -0.0342 -0.0003 0.0045  7   ILE A CD1 
53   N N   . GLY A 8   ? 0.4136 0.3851 0.4135 -0.0161 0.0251  0.0311  8   GLY A N   
54   C CA  . GLY A 8   ? 0.4716 0.4427 0.4863 -0.0161 0.0302  0.0381  8   GLY A CA  
55   C C   . GLY A 8   ? 0.4860 0.4378 0.5014 -0.0173 0.0415  0.0373  8   GLY A C   
56   O O   . GLY A 8   ? 0.4640 0.4041 0.4690 -0.0165 0.0469  0.0321  8   GLY A O   
57   N N   . LYS A 9   ? 0.5070 0.4560 0.5371 -0.0177 0.0472  0.0438  9   LYS A N   
58   C CA  . LYS A 9   ? 0.5430 0.4724 0.5774 -0.0181 0.0597  0.0442  9   LYS A CA  
59   C C   . LYS A 9   ? 0.4870 0.4238 0.5277 -0.0056 0.0699  0.0515  9   LYS A C   
60   O O   . LYS A 9   ? 0.4647 0.3838 0.5051 -0.0050 0.0808  0.0492  9   LYS A O   
61   C CB  . LYS A 9   ? 0.5662 0.4936 0.6196 -0.0207 0.0633  0.0517  9   LYS A CB  
62   C CG  . LYS A 9   ? 0.6753 0.6166 0.7375 -0.0257 0.0524  0.0546  9   LYS A CG  
63   C CD  . LYS A 9   ? 0.7460 0.6731 0.7974 -0.0406 0.0400  0.0432  9   LYS A CD  
64   C CE  . LYS A 9   ? 0.8201 0.7582 0.8910 -0.0464 0.0319  0.0490  9   LYS A CE  
65   N NZ  . LYS A 9   ? 0.8044 0.7291 0.8932 -0.0530 0.0374  0.0524  9   LYS A NZ  
66   N N   . ASN A 10  ? 0.4784 0.4404 0.5251 0.0043  0.0664  0.0603  10  ASN A N   
67   C CA  . ASN A 10  ? 0.4783 0.4498 0.5330 0.0155  0.0728  0.0690  10  ASN A CA  
68   C C   . ASN A 10  ? 0.4584 0.4405 0.5054 0.0193  0.0670  0.0654  10  ASN A C   
69   O O   . ASN A 10  ? 0.4552 0.4487 0.5113 0.0282  0.0692  0.0736  10  ASN A O   
70   C CB  . ASN A 10  ? 0.5043 0.4938 0.5712 0.0244  0.0741  0.0837  10  ASN A CB  
71   C CG  . ASN A 10  ? 0.5517 0.5311 0.6318 0.0218  0.0823  0.0900  10  ASN A CG  
72   O OD1 . ASN A 10  ? 0.5613 0.5522 0.6474 0.0241  0.0815  0.0984  10  ASN A OD1 
73   N ND2 . ASN A 10  ? 0.5556 0.5119 0.6403 0.0168  0.0915  0.0857  10  ASN A ND2 
74   N N   . GLY A 11  ? 0.4399 0.4196 0.4722 0.0127  0.0586  0.0546  11  GLY A N   
75   C CA  . GLY A 11  ? 0.4238 0.4124 0.4505 0.0153  0.0533  0.0510  11  GLY A CA  
76   C C   . GLY A 11  ? 0.4118 0.4013 0.4241 0.0088  0.0427  0.0417  11  GLY A C   
77   O O   . GLY A 11  ? 0.4444 0.4260 0.4506 0.0012  0.0391  0.0376  11  GLY A O   
78   N N   . ALA A 12  ? 0.3357 0.3348 0.3449 0.0112  0.0374  0.0392  12  ALA A N   
79   C CA  . ALA A 12  ? 0.3422 0.3421 0.3395 0.0060  0.0280  0.0314  12  ALA A CA  
80   C C   . ALA A 12  ? 0.3832 0.4018 0.3827 0.0117  0.0204  0.0323  12  ALA A C   
81   O O   . ALA A 12  ? 0.3041 0.3304 0.3118 0.0173  0.0219  0.0362  12  ALA A O   
82   C CB  . ALA A 12  ? 0.3531 0.3337 0.3386 -0.0007 0.0315  0.0234  12  ALA A CB  
83   N N   . VAL A 13  ? 0.3213 0.3458 0.3143 0.0096  0.0119  0.0286  13  VAL A N   
84   C CA  . VAL A 13  ? 0.3290 0.3673 0.3214 0.0138  0.0047  0.0272  13  VAL A CA  
85   C C   . VAL A 13  ? 0.2884 0.3213 0.2737 0.0082  -0.0007 0.0195  13  VAL A C   
86   O O   . VAL A 13  ? 0.3453 0.3687 0.3251 0.0021  -0.0017 0.0170  13  VAL A O   
87   C CB  . VAL A 13  ? 0.2879 0.3394 0.2801 0.0196  0.0021  0.0318  13  VAL A CB  
88   C CG1 . VAL A 13  ? 0.3796 0.4283 0.3714 0.0162  0.0024  0.0321  13  VAL A CG1 
89   C CG2 . VAL A 13  ? 0.3465 0.4083 0.3337 0.0231  -0.0055 0.0280  13  VAL A CG2 
90   N N   . MET A 14  ? 0.2560 0.2941 0.2427 0.0098  -0.0044 0.0166  14  MET A N   
91   C CA  . MET A 14  ? 0.3222 0.3548 0.3038 0.0052  -0.0084 0.0107  14  MET A CA  
92   C C   . MET A 14  ? 0.3007 0.3442 0.2850 0.0083  -0.0156 0.0075  14  MET A C   
93   O O   . MET A 14  ? 0.2494 0.3011 0.2401 0.0120  -0.0173 0.0087  14  MET A O   
94   C CB  . MET A 14  ? 0.2719 0.2915 0.2523 0.0014  -0.0019 0.0094  14  MET A CB  
95   C CG  . MET A 14  ? 0.3449 0.3563 0.3178 -0.0036 -0.0045 0.0049  14  MET A CG  
96   S SD  . MET A 14  ? 0.3455 0.3408 0.3153 -0.0065 0.0065  0.0044  14  MET A SD  
97   C CE  . MET A 14  ? 0.3636 0.3392 0.3166 -0.0116 0.0129  0.0035  14  MET A CE  
98   N N   . ALA A 15  ? 0.2974 0.3402 0.2777 0.0065  -0.0203 0.0038  15  ALA A N   
99   C CA  . ALA A 15  ? 0.3238 0.3729 0.3053 0.0087  -0.0262 -0.0007 15  ALA A CA  
100  C C   . ALA A 15  ? 0.3574 0.3990 0.3394 0.0041  -0.0283 -0.0044 15  ALA A C   
101  O O   . ALA A 15  ? 0.2709 0.3040 0.2487 -0.0001 -0.0272 -0.0030 15  ALA A O   
102  C CB  . ALA A 15  ? 0.2928 0.3480 0.2703 0.0130  -0.0277 -0.0009 15  ALA A CB  
103  N N   . GLY A 16  ? 0.2816 0.3256 0.2688 0.0044  -0.0319 -0.0084 16  GLY A N   
104  C CA  . GLY A 16  ? 0.2736 0.3104 0.2632 0.0006  -0.0331 -0.0109 16  GLY A CA  
105  C C   . GLY A 16  ? 0.3365 0.3769 0.3309 0.0021  -0.0387 -0.0168 16  GLY A C   
106  O O   . GLY A 16  ? 0.2530 0.3008 0.2496 0.0045  -0.0424 -0.0195 16  GLY A O   
107  N N   . ASP A 17  ? 0.3379 0.3726 0.3335 0.0006  -0.0399 -0.0189 17  ASP A N   
108  C CA  . ASP A 17  ? 0.3547 0.3893 0.3554 0.0015  -0.0442 -0.0257 17  ASP A CA  
109  C C   . ASP A 17  ? 0.3390 0.3719 0.3515 -0.0026 -0.0453 -0.0268 17  ASP A C   
110  O O   . ASP A 17  ? 0.3108 0.3422 0.3266 -0.0049 -0.0410 -0.0216 17  ASP A O   
111  C CB  . ASP A 17  ? 0.3780 0.4068 0.3795 0.0023  -0.0438 -0.0266 17  ASP A CB  
112  C CG  . ASP A 17  ? 0.4484 0.4689 0.4567 -0.0020 -0.0430 -0.0234 17  ASP A CG  
113  O OD1 . ASP A 17  ? 0.4347 0.4517 0.4389 -0.0052 -0.0405 -0.0171 17  ASP A OD1 
114  O OD2 . ASP A 17  ? 0.4102 0.4260 0.4260 -0.0021 -0.0442 -0.0271 17  ASP A OD2 
115  N N   . MET A 18  ? 0.3248 0.3568 0.3445 -0.0034 -0.0502 -0.0334 18  MET A N   
116  C CA  . MET A 18  ? 0.3804 0.4122 0.4161 -0.0077 -0.0519 -0.0339 18  MET A CA  
117  C C   . MET A 18  ? 0.4297 0.4522 0.4754 -0.0108 -0.0509 -0.0356 18  MET A C   
118  O O   . MET A 18  ? 0.3865 0.4085 0.4485 -0.0147 -0.0520 -0.0360 18  MET A O   
119  C CB  . MET A 18  ? 0.3639 0.4043 0.4033 -0.0076 -0.0607 -0.0394 18  MET A CB  
120  C CG  . MET A 18  ? 0.4082 0.4579 0.4388 -0.0039 -0.0609 -0.0352 18  MET A CG  
121  S SD  . MET A 18  ? 0.4936 0.5540 0.5243 -0.0033 -0.0734 -0.0393 18  MET A SD  
122  C CE  . MET A 18  ? 0.4762 0.5439 0.5365 -0.0078 -0.0743 -0.0325 18  MET A CE  
123  N N   . ARG A 19  ? 0.4370 0.4524 0.4758 -0.0091 -0.0485 -0.0350 19  ARG A N   
124  C CA  . ARG A 19  ? 0.5375 0.5434 0.5860 -0.0110 -0.0472 -0.0352 19  ARG A CA  
125  C C   . ARG A 19  ? 0.5577 0.5573 0.6109 -0.0144 -0.0412 -0.0259 19  ARG A C   
126  O O   . ARG A 19  ? 0.5645 0.5626 0.6060 -0.0144 -0.0374 -0.0188 19  ARG A O   
127  C CB  . ARG A 19  ? 0.4823 0.4838 0.5250 -0.0070 -0.0467 -0.0367 19  ARG A CB  
128  C CG  . ARG A 19  ? 0.4998 0.4910 0.5550 -0.0080 -0.0454 -0.0373 19  ARG A CG  
129  C CD  . ARG A 19  ? 0.4888 0.4762 0.5419 -0.0029 -0.0447 -0.0423 19  ARG A CD  
130  N NE  . ARG A 19  ? 0.4751 0.4605 0.5261 -0.0024 -0.0480 -0.0556 19  ARG A NE  
131  C CZ  . ARG A 19  ? 0.5204 0.4970 0.5705 0.0012  -0.0460 -0.0637 19  ARG A CZ  
132  N NH1 . ARG A 19  ? 0.4803 0.4520 0.5363 0.0056  -0.0399 -0.0584 19  ARG A NH1 
133  N NH2 . ARG A 19  ? 0.5081 0.4801 0.5515 0.0003  -0.0500 -0.0769 19  ARG A NH2 
134  N N   . GLU A 20  ? 0.4912 0.4857 0.5604 -0.0177 -0.0401 -0.0262 20  GLU A N   
135  C CA  . GLU A 20  ? 0.5707 0.5571 0.6448 -0.0206 -0.0330 -0.0173 20  GLU A CA  
136  C C   . GLU A 20  ? 0.5972 0.5748 0.6835 -0.0213 -0.0334 -0.0179 20  GLU A C   
137  O O   . GLU A 20  ? 0.4810 0.4585 0.5816 -0.0225 -0.0378 -0.0265 20  GLU A O   
138  C CB  . GLU A 20  ? 0.5291 0.5189 0.6175 -0.0238 -0.0291 -0.0153 20  GLU A CB  
139  C CG  . GLU A 20  ? 0.6578 0.6379 0.7569 -0.0268 -0.0206 -0.0072 20  GLU A CG  
140  C CD  . GLU A 20  ? 0.6802 0.6641 0.8020 -0.0299 -0.0155 -0.0048 20  GLU A CD  
141  O OE1 . GLU A 20  ? 0.7170 0.7046 0.8349 -0.0291 -0.0095 -0.0008 20  GLU A OE1 
142  O OE2 . GLU A 20  ? 0.6262 0.6089 0.7721 -0.0333 -0.0171 -0.0064 20  GLU A OE2 
143  N N   . ILE A 21  ? 0.7181 0.6875 0.7977 -0.0206 -0.0299 -0.0091 21  ILE A N   
144  C CA  . ILE A 21  ? 0.6565 0.6170 0.7487 -0.0203 -0.0294 -0.0075 21  ILE A CA  
145  C C   . ILE A 21  ? 0.6532 0.6045 0.7497 -0.0231 -0.0223 0.0038  21  ILE A C   
146  O O   . ILE A 21  ? 0.7897 0.7381 0.8684 -0.0234 -0.0189 0.0131  21  ILE A O   
147  C CB  . ILE A 21  ? 0.6839 0.6434 0.7685 -0.0157 -0.0323 -0.0052 21  ILE A CB  
148  C CG1 . ILE A 21  ? 0.7191 0.6869 0.7975 -0.0120 -0.0367 -0.0154 21  ILE A CG1 
149  C CG2 . ILE A 21  ? 0.6386 0.5881 0.7400 -0.0145 -0.0306 -0.0028 21  ILE A CG2 
150  C CD1 . ILE A 21  ? 0.6691 0.6346 0.7512 -0.0067 -0.0373 -0.0162 21  ILE A CD1 
151  N N   . THR A 22  ? 0.5386 0.4839 0.6572 -0.0254 -0.0197 0.0030  22  THR A N   
152  C CA  . THR A 22  ? 0.6137 0.5488 0.7377 -0.0275 -0.0114 0.0155  22  THR A CA  
153  C C   . THR A 22  ? 0.5809 0.5068 0.7155 -0.0255 -0.0119 0.0195  22  THR A C   
154  O O   . THR A 22  ? 0.5061 0.4313 0.6555 -0.0245 -0.0160 0.0096  22  THR A O   
155  C CB  . THR A 22  ? 0.5860 0.5209 0.7306 -0.0320 -0.0049 0.0159  22  THR A CB  
156  O OG1 . THR A 22  ? 0.5845 0.5133 0.7567 -0.0344 -0.0048 0.0133  22  THR A OG1 
157  C CG2 . THR A 22  ? 0.5593 0.5065 0.7071 -0.0335 -0.0081 0.0073  22  THR A CG2 
158  N N   . PHE A 23  ? 0.6193 0.5368 0.7452 -0.0249 -0.0073 0.0343  23  PHE A N   
159  C CA  . PHE A 23  ? 0.5503 0.4590 0.6876 -0.0225 -0.0071 0.0418  23  PHE A CA  
160  C C   . PHE A 23  ? 0.5986 0.4962 0.7481 -0.0252 0.0024  0.0531  23  PHE A C   
161  O O   . PHE A 23  ? 0.6029 0.4983 0.7406 -0.0277 0.0096  0.0602  23  PHE A O   
162  C CB  . PHE A 23  ? 0.5425 0.4517 0.6598 -0.0189 -0.0124 0.0522  23  PHE A CB  
163  C CG  . PHE A 23  ? 0.5921 0.5126 0.6960 -0.0164 -0.0205 0.0446  23  PHE A CG  
164  C CD1 . PHE A 23  ? 0.6659 0.5925 0.7469 -0.0185 -0.0220 0.0426  23  PHE A CD1 
165  C CD2 . PHE A 23  ? 0.5951 0.5188 0.7098 -0.0116 -0.0251 0.0414  23  PHE A CD2 
166  C CE1 . PHE A 23  ? 0.6657 0.6022 0.7364 -0.0165 -0.0288 0.0369  23  PHE A CE1 
167  C CE2 . PHE A 23  ? 0.5627 0.4968 0.6668 -0.0091 -0.0309 0.0364  23  PHE A CE2 
168  C CZ  . PHE A 23  ? 0.6239 0.5646 0.7063 -0.0119 -0.0332 0.0345  23  PHE A CZ  
169  N N   . GLU A 24  ? 0.5291 0.4183 0.7031 -0.0243 0.0043  0.0549  24  GLU A N   
170  C CA  . GLU A 24  ? 0.5565 0.4343 0.7452 -0.0265 0.0143  0.0674  24  GLU A CA  
171  C C   . GLU A 24  ? 0.5594 0.4276 0.7604 -0.0225 0.0140  0.0769  24  GLU A C   
172  O O   . GLU A 24  ? 0.5165 0.3845 0.7335 -0.0200 0.0096  0.0669  24  GLU A O   
173  C CB  . GLU A 24  ? 0.6091 0.4864 0.8275 -0.0318 0.0186  0.0578  24  GLU A CB  
174  C CG  . GLU A 24  ? 0.6789 0.5689 0.8927 -0.0349 0.0150  0.0450  24  GLU A CG  
175  C CD  . GLU A 24  ? 0.7239 0.6150 0.9634 -0.0408 0.0215  0.0441  24  GLU A CD  
176  O OE1 . GLU A 24  ? 0.7536 0.6523 0.9847 -0.0421 0.0253  0.0454  24  GLU A OE1 
177  O OE2 . GLU A 24  ? 0.7565 0.6406 1.0271 -0.0441 0.0233  0.0425  24  GLU A OE2 
178  N N   . GLY A 25  ? 0.5719 0.4317 0.7638 -0.0214 0.0192  0.0964  25  GLY A N   
179  C CA  . GLY A 25  ? 0.6186 0.4696 0.8222 -0.0171 0.0190  0.1098  25  GLY A CA  
180  C C   . GLY A 25  ? 0.6414 0.4897 0.8159 -0.0150 0.0168  0.1305  25  GLY A C   
181  O O   . GLY A 25  ? 0.6694 0.5203 0.8118 -0.0175 0.0161  0.1328  25  GLY A O   
182  N N   . GLU A 26  ? 0.5888 0.4307 0.7735 -0.0107 0.0151  0.1459  26  GLU A N   
183  C CA  . GLU A 26  ? 0.6341 0.4730 0.7912 -0.0092 0.0101  0.1671  26  GLU A CA  
184  C C   . GLU A 26  ? 0.6180 0.4686 0.7440 -0.0096 -0.0031 0.1635  26  GLU A C   
185  O O   . GLU A 26  ? 0.5525 0.4142 0.6885 -0.0077 -0.0098 0.1498  26  GLU A O   
186  C CB  . GLU A 26  ? 0.6374 0.4702 0.8172 -0.0036 0.0084  0.1841  26  GLU A CB  
187  C CG  . GLU A 26  ? 0.5961 0.4162 0.8114 -0.0032 0.0216  0.1866  26  GLU A CG  
188  C CD  . GLU A 26  ? 0.7229 0.5346 0.9340 -0.0087 0.0349  0.1873  26  GLU A CD  
189  O OE1 . GLU A 26  ? 0.7921 0.5954 0.9805 -0.0093 0.0398  0.2065  26  GLU A OE1 
190  O OE2 . GLU A 26  ? 0.8188 0.6320 1.0496 -0.0125 0.0405  0.1693  26  GLU A OE2 
191  N N   . LYS A 27  ? 0.6721 0.5185 0.7592 -0.0123 -0.0062 0.1759  27  LYS A N   
192  C CA  . LYS A 27  ? 0.6546 0.5090 0.7088 -0.0143 -0.0191 0.1737  27  LYS A CA  
193  C C   . LYS A 27  ? 0.6049 0.4710 0.6716 -0.0105 -0.0348 0.1779  27  LYS A C   
194  O O   . LYS A 27  ? 0.6022 0.4801 0.6652 -0.0111 -0.0420 0.1652  27  LYS A O   
195  C CB  . LYS A 27  ? 0.7212 0.5636 0.7289 -0.0185 -0.0192 0.1874  27  LYS A CB  
196  C CG  . LYS A 27  ? 0.8112 0.6584 0.7819 -0.0225 -0.0309 0.1816  27  LYS A CG  
197  C CD  . LYS A 27  ? 0.8357 0.6676 0.7594 -0.0275 -0.0231 0.1842  27  LYS A CD  
198  C CE  . LYS A 27  ? 0.9859 0.8165 0.8673 -0.0321 -0.0388 0.1862  27  LYS A CE  
199  N NZ  . LYS A 27  ? 0.9731 0.8119 0.8629 -0.0309 -0.0588 0.1997  27  LYS A NZ  
200  N N   . PRO A 28  ? 0.6262 0.4902 0.7106 -0.0061 -0.0395 0.1960  28  PRO A N   
201  C CA  . PRO A 28  ? 0.6308 0.5078 0.7331 -0.0019 -0.0532 0.2004  28  PRO A CA  
202  C C   . PRO A 28  ? 0.6151 0.5014 0.7504 0.0023  -0.0486 0.1811  28  PRO A C   
203  O O   . PRO A 28  ? 0.5680 0.4672 0.7090 0.0042  -0.0575 0.1774  28  PRO A O   
204  C CB  . PRO A 28  ? 0.6561 0.5271 0.7784 0.0029  -0.0549 0.2239  28  PRO A CB  
205  C CG  . PRO A 28  ? 0.6800 0.5346 0.7807 -0.0002 -0.0458 0.2346  28  PRO A CG  
206  C CD  . PRO A 28  ? 0.6791 0.5295 0.7728 -0.0042 -0.0317 0.2141  28  PRO A CD  
207  N N   . ASP A 29  ? 0.5822 0.4610 0.7388 0.0034  -0.0346 0.1692  29  ASP A N   
208  C CA  . ASP A 29  ? 0.6019 0.4850 0.7851 0.0068  -0.0293 0.1496  29  ASP A CA  
209  C C   . ASP A 29  ? 0.5501 0.4428 0.7136 0.0030  -0.0314 0.1300  29  ASP A C   
210  O O   . ASP A 29  ? 0.5412 0.4439 0.7126 0.0063  -0.0349 0.1205  29  ASP A O   
211  C CB  . ASP A 29  ? 0.5634 0.4334 0.7712 0.0069  -0.0159 0.1433  29  ASP A CB  
212  C CG  . ASP A 29  ? 0.6030 0.4627 0.8339 0.0113  -0.0125 0.1629  29  ASP A CG  
213  O OD1 . ASP A 29  ? 0.5955 0.4596 0.8435 0.0177  -0.0177 0.1726  29  ASP A OD1 
214  O OD2 . ASP A 29  ? 0.5761 0.4236 0.8109 0.0088  -0.0040 0.1694  29  ASP A OD2 
215  N N   . ARG A 30  ? 0.5541 0.4436 0.6926 -0.0031 -0.0282 0.1258  30  ARG A N   
216  C CA  . ARG A 30  ? 0.5437 0.4416 0.6635 -0.0066 -0.0297 0.1097  30  ARG A CA  
217  C C   . ARG A 30  ? 0.5871 0.4956 0.6886 -0.0065 -0.0419 0.1134  30  ARG A C   
218  O O   . ARG A 30  ? 0.5570 0.4758 0.6616 -0.0052 -0.0444 0.1008  30  ARG A O   
219  C CB  . ARG A 30  ? 0.5738 0.4650 0.6726 -0.0124 -0.0225 0.1083  30  ARG A CB  
220  C CG  . ARG A 30  ? 0.5522 0.4366 0.6739 -0.0137 -0.0110 0.1008  30  ARG A CG  
221  C CD  . ARG A 30  ? 0.6493 0.5291 0.7559 -0.0188 -0.0023 0.1001  30  ARG A CD  
222  N NE  . ARG A 30  ? 0.6685 0.5353 0.7644 -0.0199 0.0048  0.1184  30  ARG A NE  
223  C CZ  . ARG A 30  ? 0.7052 0.5666 0.7647 -0.0218 0.0043  0.1290  30  ARG A CZ  
224  N NH1 . ARG A 30  ? 0.6434 0.5114 0.6762 -0.0231 -0.0038 0.1231  30  ARG A NH1 
225  N NH2 . ARG A 30  ? 0.7290 0.5766 0.7767 -0.0224 0.0121  0.1456  30  ARG A NH2 
226  N N   . GLU A 31  ? 0.5951 0.5011 0.6795 -0.0081 -0.0501 0.1315  31  GLU A N   
227  C CA  . GLU A 31  ? 0.6121 0.5276 0.6816 -0.0094 -0.0643 0.1374  31  GLU A CA  
228  C C   . GLU A 31  ? 0.6049 0.5332 0.7054 -0.0033 -0.0694 0.1369  31  GLU A C   
229  O O   . GLU A 31  ? 0.5952 0.5347 0.6909 -0.0041 -0.0770 0.1325  31  GLU A O   
230  C CB  . GLU A 31  ? 0.6030 0.5113 0.6492 -0.0127 -0.0739 0.1582  31  GLU A CB  
231  C CG  . GLU A 31  ? 0.7022 0.5968 0.7088 -0.0190 -0.0685 0.1582  31  GLU A CG  
232  C CD  . GLU A 31  ? 0.8323 0.7188 0.8028 -0.0238 -0.0806 0.1753  31  GLU A CD  
233  O OE1 . GLU A 31  ? 0.7656 0.6504 0.7450 -0.0216 -0.0876 0.1939  31  GLU A OE1 
234  O OE2 . GLU A 31  ? 0.8834 0.7642 0.8159 -0.0300 -0.0831 0.1701  31  GLU A OE2 
235  N N   . LYS A 32  ? 0.5733 0.4989 0.7066 0.0031  -0.0640 0.1419  32  LYS A N   
236  C CA  . LYS A 32  ? 0.5795 0.5148 0.7447 0.0103  -0.0649 0.1416  32  LYS A CA  
237  C C   . LYS A 32  ? 0.5995 0.5393 0.7696 0.0123  -0.0568 0.1187  32  LYS A C   
238  O O   . LYS A 32  ? 0.6363 0.5875 0.8149 0.0155  -0.0597 0.1157  32  LYS A O   
239  C CB  . LYS A 32  ? 0.6215 0.5490 0.8199 0.0171  -0.0583 0.1518  32  LYS A CB  
240  C CG  . LYS A 32  ? 0.6678 0.6023 0.9014 0.0258  -0.0546 0.1499  32  LYS A CG  
241  C CD  . LYS A 32  ? 0.7573 0.6842 1.0250 0.0330  -0.0496 0.1647  32  LYS A CD  
242  C CE  . LYS A 32  ? 0.7860 0.6977 1.0478 0.0299  -0.0456 0.1723  32  LYS A CE  
243  N NZ  . LYS A 32  ? 0.8623 0.7648 1.1613 0.0376  -0.0381 0.1845  32  LYS A NZ  
244  N N   . LEU A 33  ? 0.6055 0.5366 0.7708 0.0103  -0.0469 0.1037  33  LEU A N   
245  C CA  . LEU A 33  ? 0.5779 0.5122 0.7436 0.0114  -0.0411 0.0826  33  LEU A CA  
246  C C   . LEU A 33  ? 0.5913 0.5365 0.7318 0.0073  -0.0475 0.0771  33  LEU A C   
247  O O   . LEU A 33  ? 0.6118 0.5658 0.7562 0.0106  -0.0475 0.0695  33  LEU A O   
248  C CB  . LEU A 33  ? 0.5090 0.4323 0.6762 0.0086  -0.0323 0.0695  33  LEU A CB  
249  C CG  . LEU A 33  ? 0.5140 0.4398 0.6785 0.0087  -0.0286 0.0481  33  LEU A CG  
250  C CD1 . LEU A 33  ? 0.5446 0.4700 0.7270 0.0163  -0.0242 0.0411  33  LEU A CD1 
251  C CD2 . LEU A 33  ? 0.5126 0.4291 0.6799 0.0041  -0.0234 0.0375  33  LEU A CD2 
252  N N   . GLU A 34  ? 0.5700 0.5132 0.6848 0.0007  -0.0517 0.0819  34  GLU A N   
253  C CA  . GLU A 34  ? 0.6317 0.5821 0.7216 -0.0037 -0.0572 0.0775  34  GLU A CA  
254  C C   . GLU A 34  ? 0.6595 0.6218 0.7545 -0.0018 -0.0662 0.0836  34  GLU A C   
255  O O   . GLU A 34  ? 0.6866 0.6574 0.7797 -0.0010 -0.0659 0.0739  34  GLU A O   
256  C CB  . GLU A 34  ? 0.6992 0.6417 0.7604 -0.0105 -0.0600 0.0856  34  GLU A CB  
257  C CG  . GLU A 34  ? 0.7552 0.6914 0.8036 -0.0140 -0.0508 0.0752  34  GLU A CG  
258  C CD  . GLU A 34  ? 0.8595 0.7866 0.8758 -0.0199 -0.0514 0.0827  34  GLU A CD  
259  O OE1 . GLU A 34  ? 0.8950 0.8248 0.8899 -0.0232 -0.0555 0.0789  34  GLU A OE1 
260  O OE2 . GLU A 34  ? 0.8568 0.7725 0.8686 -0.0211 -0.0468 0.0922  34  GLU A OE2 
261  N N   . LYS A 35  ? 0.6526 0.6161 0.7569 -0.0010 -0.0745 0.1009  35  LYS A N   
262  C CA  . LYS A 35  ? 0.6351 0.6113 0.7511 0.0005  -0.0844 0.1095  35  LYS A CA  
263  C C   . LYS A 35  ? 0.6473 0.6319 0.7895 0.0083  -0.0761 0.1001  35  LYS A C   
264  O O   . LYS A 35  ? 0.6651 0.6604 0.8070 0.0081  -0.0788 0.0967  35  LYS A O   
265  C CB  . LYS A 35  ? 0.6234 0.5996 0.7521 0.0011  -0.0944 0.1311  35  LYS A CB  
266  C CG  . LYS A 35  ? 0.6400 0.6314 0.7936 0.0039  -0.1044 0.1427  35  LYS A CG  
267  C CD  . LYS A 35  ? 0.6780 0.6750 0.8703 0.0145  -0.0923 0.1387  35  LYS A CD  
268  C CE  . LYS A 35  ? 0.6781 0.6903 0.9026 0.0183  -0.1006 0.1546  35  LYS A CE  
269  N NZ  . LYS A 35  ? 0.6972 0.7223 0.9218 0.0168  -0.1029 0.1482  35  LYS A NZ  
270  N N   . GLU A 36  ? 0.6341 0.6123 0.7971 0.0149  -0.0649 0.0951  36  GLU A N   
271  C CA  . GLU A 36  ? 0.6550 0.6370 0.8379 0.0228  -0.0548 0.0850  36  GLU A CA  
272  C C   . GLU A 36  ? 0.6561 0.6398 0.8193 0.0212  -0.0497 0.0661  36  GLU A C   
273  O O   . GLU A 36  ? 0.6193 0.6103 0.7894 0.0259  -0.0452 0.0607  36  GLU A O   
274  C CB  . GLU A 36  ? 0.6547 0.6245 0.8588 0.0291  -0.0434 0.0814  36  GLU A CB  
275  C CG  . GLU A 36  ? 0.6611 0.6314 0.8961 0.0348  -0.0445 0.0998  36  GLU A CG  
276  C CD  . GLU A 36  ? 0.7274 0.7013 0.9913 0.0449  -0.0343 0.0983  36  GLU A CD  
277  O OE1 . GLU A 36  ? 0.7214 0.7065 0.9831 0.0463  -0.0341 0.0943  36  GLU A OE1 
278  O OE2 . GLU A 36  ? 0.6821 0.6465 0.9715 0.0519  -0.0251 0.1015  36  GLU A OE2 
279  N N   . LEU A 37  ? 0.6353 0.6124 0.7760 0.0153  -0.0495 0.0572  37  LEU A N   
280  C CA  . LEU A 37  ? 0.6676 0.6466 0.7914 0.0137  -0.0458 0.0409  37  LEU A CA  
281  C C   . LEU A 37  ? 0.6509 0.6403 0.7586 0.0100  -0.0524 0.0429  37  LEU A C   
282  O O   . LEU A 37  ? 0.6446 0.6403 0.7495 0.0126  -0.0490 0.0344  37  LEU A O   
283  C CB  . LEU A 37  ? 0.6825 0.6519 0.7942 0.0088  -0.0434 0.0328  37  LEU A CB  
284  C CG  . LEU A 37  ? 0.6565 0.6263 0.7569 0.0076  -0.0396 0.0157  37  LEU A CG  
285  C CD1 . LEU A 37  ? 0.6476 0.6273 0.7306 0.0055  -0.0431 0.0140  37  LEU A CD1 
286  C CD2 . LEU A 37  ? 0.5530 0.5185 0.6635 0.0131  -0.0330 0.0027  37  LEU A CD2 
287  N N   . TYR A 38  ? 0.6805 0.6704 0.7766 0.0040  -0.0616 0.0542  38  TYR A N   
288  C CA  . TYR A 38  ? 0.6828 0.6798 0.7628 -0.0008 -0.0684 0.0554  38  TYR A CA  
289  C C   . TYR A 38  ? 0.6660 0.6749 0.7634 0.0013  -0.0745 0.0650  38  TYR A C   
290  O O   . TYR A 38  ? 0.6467 0.6614 0.7345 -0.0032 -0.0810 0.0667  38  TYR A O   
291  C CB  . TYR A 38  ? 0.7615 0.7503 0.8162 -0.0090 -0.0748 0.0608  38  TYR A CB  
292  C CG  . TYR A 38  ? 0.8550 0.8337 0.8965 -0.0109 -0.0669 0.0526  38  TYR A CG  
293  C CD1 . TYR A 38  ? 0.8752 0.8552 0.9222 -0.0077 -0.0584 0.0391  38  TYR A CD1 
294  C CD2 . TYR A 38  ? 1.0027 0.9701 1.0262 -0.0161 -0.0680 0.0592  38  TYR A CD2 
295  C CE1 . TYR A 38  ? 1.0865 1.0592 1.1270 -0.0100 -0.0524 0.0329  38  TYR A CE1 
296  C CE2 . TYR A 38  ? 1.1087 1.0677 1.1255 -0.0174 -0.0591 0.0533  38  TYR A CE2 
297  C CZ  . TYR A 38  ? 1.2052 1.1680 1.2331 -0.0146 -0.0519 0.0404  38  TYR A CZ  
298  O OH  . TYR A 38  ? 1.3255 1.2818 1.3519 -0.0165 -0.0443 0.0357  38  TYR A OH  
299  N N   . SER A 39  ? 0.6357 0.6478 0.7611 0.0083  -0.0715 0.0711  39  SER A N   
300  C CA  . SER A 39  ? 0.6361 0.6610 0.7853 0.0113  -0.0756 0.0818  39  SER A CA  
301  C C   . SER A 39  ? 0.5960 0.6272 0.7596 0.0195  -0.0630 0.0731  39  SER A C   
302  O O   . SER A 39  ? 0.6150 0.6576 0.8014 0.0228  -0.0635 0.0819  39  SER A O   
303  C CB  . SER A 39  ? 0.6635 0.6893 0.8390 0.0146  -0.0800 0.0978  39  SER A CB  
304  O OG  . SER A 39  ? 0.6489 0.6696 0.8452 0.0240  -0.0663 0.0933  39  SER A OG  
305  N N   . GLY A 40  ? 0.6292 0.6528 0.7799 0.0226  -0.0518 0.0571  40  GLY A N   
306  C CA  . GLY A 40  ? 0.5968 0.6226 0.7546 0.0307  -0.0389 0.0481  40  GLY A CA  
307  C C   . GLY A 40  ? 0.6127 0.6316 0.7925 0.0398  -0.0277 0.0473  40  GLY A C   
308  O O   . GLY A 40  ? 0.5679 0.5851 0.7513 0.0473  -0.0148 0.0394  40  GLY A O   
309  N N   . SER A 41  ? 0.7272 0.7401 0.9203 0.0395  -0.0312 0.0556  41  SER A N   
310  C CA  . SER A 41  ? 0.7363 0.7403 0.9532 0.0480  -0.0202 0.0561  41  SER A CA  
311  C C   . SER A 41  ? 0.7281 0.7166 0.9296 0.0504  -0.0089 0.0360  41  SER A C   
312  O O   . SER A 41  ? 0.7049 0.6857 0.9168 0.0589  0.0049  0.0292  41  SER A O   
313  C CB  . SER A 41  ? 0.7133 0.7137 0.9449 0.0459  -0.0279 0.0703  41  SER A CB  
314  O OG  . SER A 41  ? 0.7564 0.7701 0.9980 0.0420  -0.0419 0.0892  41  SER A OG  
315  N N   . ILE A 42  ? 0.6036 0.5863 0.7808 0.0429  -0.0147 0.0265  42  ILE A N   
316  C CA  . ILE A 42  ? 0.5453 0.5142 0.7087 0.0431  -0.0078 0.0077  42  ILE A CA  
317  C C   . ILE A 42  ? 0.5931 0.5667 0.7325 0.0426  -0.0064 -0.0046 42  ILE A C   
318  O O   . ILE A 42  ? 0.5664 0.5476 0.6890 0.0361  -0.0148 -0.0046 42  ILE A O   
319  C CB  . ILE A 42  ? 0.5172 0.4782 0.6740 0.0355  -0.0143 0.0061  42  ILE A CB  
320  C CG1 . ILE A 42  ? 0.6067 0.5609 0.7875 0.0371  -0.0139 0.0190  42  ILE A CG1 
321  C CG2 . ILE A 42  ? 0.5370 0.4865 0.6803 0.0335  -0.0107 -0.0130 42  ILE A CG2 
322  C CD1 . ILE A 42  ? 0.5801 0.5325 0.7548 0.0290  -0.0226 0.0276  42  ILE A CD1 
323  N N   . VAL A 43  ? 0.5456 0.5136 0.6828 0.0500  0.0052  -0.0144 43  VAL A N   
324  C CA  . VAL A 43  ? 0.5491 0.5205 0.6628 0.0510  0.0080  -0.0247 43  VAL A CA  
325  C C   . VAL A 43  ? 0.5394 0.4995 0.6287 0.0472  0.0062  -0.0431 43  VAL A C   
326  O O   . VAL A 43  ? 0.6018 0.5687 0.6711 0.0432  0.0002  -0.0474 43  VAL A O   
327  C CB  . VAL A 43  ? 0.5761 0.5467 0.6973 0.0615  0.0228  -0.0243 43  VAL A CB  
328  C CG1 . VAL A 43  ? 0.5275 0.4969 0.6201 0.0636  0.0279  -0.0364 43  VAL A CG1 
329  C CG2 . VAL A 43  ? 0.5380 0.5246 0.6847 0.0639  0.0219  -0.0049 43  VAL A CG2 
330  N N   . THR A 44  ? 0.5667 0.5096 0.6590 0.0482  0.0108  -0.0535 44  THR A N   
331  C CA  . THR A 44  ? 0.6053 0.5367 0.6760 0.0438  0.0074  -0.0716 44  THR A CA  
332  C C   . THR A 44  ? 0.6109 0.5380 0.6897 0.0349  -0.0022 -0.0728 44  THR A C   
333  O O   . THR A 44  ? 0.5878 0.5158 0.6880 0.0339  -0.0029 -0.0609 44  THR A O   
334  C CB  . THR A 44  ? 0.6439 0.5554 0.7049 0.0504  0.0198  -0.0868 44  THR A CB  
335  O OG1 . THR A 44  ? 0.6504 0.5443 0.7258 0.0490  0.0222  -0.0927 44  THR A OG1 
336  C CG2 . THR A 44  ? 0.6298 0.5427 0.6968 0.0615  0.0351  -0.0805 44  THR A CG2 
337  N N   . ASP A 45  ? 0.5759 0.4988 0.6387 0.0286  -0.0096 -0.0860 45  ASP A N   
338  C CA  . ASP A 45  ? 0.6187 0.5369 0.6923 0.0201  -0.0173 -0.0880 45  ASP A CA  
339  C C   . ASP A 45  ? 0.6065 0.5045 0.6959 0.0212  -0.0108 -0.0944 45  ASP A C   
340  O O   . ASP A 45  ? 0.5757 0.4697 0.6839 0.0163  -0.0134 -0.0895 45  ASP A O   
341  C CB  . ASP A 45  ? 0.6392 0.5597 0.6963 0.0130  -0.0279 -0.0996 45  ASP A CB  
342  C CG  . ASP A 45  ? 0.6960 0.6358 0.7423 0.0114  -0.0340 -0.0919 45  ASP A CG  
343  O OD1 . ASP A 45  ? 0.6212 0.5717 0.6734 0.0139  -0.0314 -0.0776 45  ASP A OD1 
344  O OD2 . ASP A 45  ? 0.7038 0.6474 0.7360 0.0075  -0.0421 -0.0999 45  ASP A OD2 
345  N N   . GLU A 46  ? 0.6244 0.5084 0.7066 0.0282  -0.0007 -0.1044 46  GLU A N   
346  C CA  . GLU A 46  ? 0.6198 0.4818 0.7163 0.0311  0.0086  -0.1111 46  GLU A CA  
347  C C   . GLU A 46  ? 0.5924 0.4586 0.7197 0.0359  0.0149  -0.0916 46  GLU A C   
348  O O   . GLU A 46  ? 0.6253 0.4819 0.7731 0.0329  0.0149  -0.0886 46  GLU A O   
349  C CB  . GLU A 46  ? 0.6485 0.4946 0.7257 0.0390  0.0208  -0.1256 46  GLU A CB  
350  C CG  . GLU A 46  ? 0.6754 0.5074 0.7220 0.0333  0.0145  -0.1481 46  GLU A CG  
351  C CD  . GLU A 46  ? 0.7467 0.5958 0.7684 0.0285  0.0017  -0.1496 46  GLU A CD  
352  O OE1 . GLU A 46  ? 0.7261 0.5953 0.7473 0.0324  0.0023  -0.1356 46  GLU A OE1 
353  O OE2 . GLU A 46  ? 0.7943 0.6364 0.7986 0.0205  -0.0097 -0.1642 46  GLU A OE2 
354  N N   . GLU A 47  ? 0.5720 0.4532 0.7037 0.0427  0.0188  -0.0772 47  GLU A N   
355  C CA  . GLU A 47  ? 0.5652 0.4529 0.7254 0.0469  0.0216  -0.0569 47  GLU A CA  
356  C C   . GLU A 47  ? 0.5644 0.4617 0.7326 0.0389  0.0100  -0.0438 47  GLU A C   
357  O O   . GLU A 47  ? 0.5704 0.4664 0.7610 0.0403  0.0110  -0.0294 47  GLU A O   
358  C CB  . GLU A 47  ? 0.5922 0.4958 0.7555 0.0541  0.0255  -0.0446 47  GLU A CB  
359  C CG  . GLU A 47  ? 0.6357 0.5290 0.7952 0.0640  0.0411  -0.0542 47  GLU A CG  
360  C CD  . GLU A 47  ? 0.6804 0.5892 0.8307 0.0688  0.0442  -0.0492 47  GLU A CD  
361  O OE1 . GLU A 47  ? 0.6354 0.5577 0.7663 0.0629  0.0337  -0.0494 47  GLU A OE1 
362  O OE2 . GLU A 47  ? 0.7374 0.6447 0.9025 0.0788  0.0582  -0.0442 47  GLU A OE2 
363  N N   . MET A 48  ? 0.5632 0.4694 0.7127 0.0310  0.0000  -0.0478 48  MET A N   
364  C CA  . MET A 48  ? 0.5569 0.4699 0.7102 0.0237  -0.0085 -0.0368 48  MET A CA  
365  C C   . MET A 48  ? 0.5541 0.4519 0.7227 0.0194  -0.0072 -0.0400 48  MET A C   
366  O O   . MET A 48  ? 0.5258 0.4229 0.7092 0.0181  -0.0077 -0.0255 48  MET A O   
367  C CB  . MET A 48  ? 0.5278 0.4525 0.6594 0.0176  -0.0167 -0.0417 48  MET A CB  
368  C CG  . MET A 48  ? 0.5215 0.4475 0.6557 0.0095  -0.0223 -0.0366 48  MET A CG  
369  S SD  . MET A 48  ? 0.6335 0.5764 0.7478 0.0047  -0.0294 -0.0323 48  MET A SD  
370  C CE  . MET A 48  ? 0.5613 0.5057 0.6611 0.0032  -0.0327 -0.0514 48  MET A CE  
371  N N   . GLN A 49  ? 0.5616 0.4463 0.7260 0.0169  -0.0061 -0.0587 49  GLN A N   
372  C CA  . GLN A 49  ? 0.5556 0.4245 0.7373 0.0118  -0.0051 -0.0634 49  GLN A CA  
373  C C   . GLN A 49  ? 0.5895 0.4445 0.7946 0.0182  0.0049  -0.0563 49  GLN A C   
374  O O   . GLN A 49  ? 0.5937 0.4427 0.8186 0.0156  0.0059  -0.0464 49  GLN A O   
375  C CB  . GLN A 49  ? 0.4858 0.3431 0.6567 0.0064  -0.0085 -0.0862 49  GLN A CB  
376  C CG  . GLN A 49  ? 0.5872 0.4592 0.7421 -0.0010 -0.0199 -0.0901 49  GLN A CG  
377  C CD  . GLN A 49  ? 0.6327 0.5117 0.8029 -0.0081 -0.0242 -0.0782 49  GLN A CD  
378  O OE1 . GLN A 49  ? 0.6564 0.5266 0.8486 -0.0095 -0.0197 -0.0700 49  GLN A OE1 
379  N NE2 . GLN A 49  ? 0.5995 0.4939 0.7590 -0.0125 -0.0315 -0.0766 49  GLN A NE2 
380  N N   . LYS A 50  ? 0.5665 0.4172 0.7711 0.0275  0.0136  -0.0591 50  LYS A N   
381  C CA  . LYS A 50  ? 0.5813 0.4198 0.8121 0.0351  0.0244  -0.0505 50  LYS A CA  
382  C C   . LYS A 50  ? 0.5683 0.4203 0.8164 0.0369  0.0212  -0.0240 50  LYS A C   
383  O O   . LYS A 50  ? 0.5449 0.3872 0.8169 0.0381  0.0251  -0.0136 50  LYS A O   
384  C CB  . LYS A 50  ? 0.6025 0.4341 0.8305 0.0455  0.0364  -0.0581 50  LYS A CB  
385  C CG  . LYS A 50  ? 0.6914 0.4972 0.9097 0.0451  0.0441  -0.0830 50  LYS A CG  
386  C CD  . LYS A 50  ? 0.6950 0.4946 0.8946 0.0538  0.0553  -0.0952 50  LYS A CD  
387  C CE  . LYS A 50  ? 0.7679 0.5670 0.9916 0.0667  0.0705  -0.0817 50  LYS A CE  
388  N NZ  . LYS A 50  ? 0.7804 0.6076 1.0180 0.0692  0.0639  -0.0567 50  LYS A NZ  
389  N N   . LYS A 51  ? 0.5462 0.4192 0.7807 0.0359  0.0129  -0.0132 51  LYS A N   
390  C CA  . LYS A 51  ? 0.5755 0.4600 0.8201 0.0361  0.0073  0.0108  51  LYS A CA  
391  C C   . LYS A 51  ? 0.5844 0.4656 0.8288 0.0280  0.0022  0.0177  51  LYS A C   
392  O O   . LYS A 51  ? 0.5636 0.4423 0.8238 0.0292  0.0023  0.0355  51  LYS A O   
393  C CB  . LYS A 51  ? 0.5453 0.4503 0.7747 0.0365  -0.0003 0.0190  51  LYS A CB  
394  C CG  . LYS A 51  ? 0.5342 0.4446 0.7751 0.0460  0.0058  0.0220  51  LYS A CG  
395  C CD  . LYS A 51  ? 0.6160 0.5256 0.8881 0.0522  0.0082  0.0421  51  LYS A CD  
396  C CE  . LYS A 51  ? 0.6463 0.5705 0.9321 0.0594  0.0086  0.0539  51  LYS A CE  
397  N NZ  . LYS A 51  ? 0.6930 0.6137 1.0161 0.0679  0.0147  0.0703  51  LYS A NZ  
398  N N   . ALA A 52  ? 0.5609 0.4422 0.7890 0.0201  -0.0016 0.0050  52  ALA A N   
399  C CA  . ALA A 52  ? 0.5545 0.4325 0.7847 0.0126  -0.0039 0.0111  52  ALA A CA  
400  C C   . ALA A 52  ? 0.5993 0.4589 0.8563 0.0132  0.0035  0.0129  52  ALA A C   
401  O O   . ALA A 52  ? 0.5761 0.4326 0.8428 0.0113  0.0043  0.0290  52  ALA A O   
402  C CB  . ALA A 52  ? 0.5486 0.4297 0.7640 0.0049  -0.0080 -0.0042 52  ALA A CB  
403  N N   . GLU A 53  ? 0.5461 0.3917 0.8132 0.0156  0.0095  -0.0038 53  GLU A N   
404  C CA  . GLU A 53  ? 0.6619 0.4869 0.9558 0.0163  0.0177  -0.0050 53  GLU A CA  
405  C C   . GLU A 53  ? 0.6233 0.4476 0.9372 0.0244  0.0225  0.0178  53  GLU A C   
406  O O   . GLU A 53  ? 0.6531 0.4712 0.9833 0.0228  0.0244  0.0326  53  GLU A O   
407  C CB  . GLU A 53  ? 0.7060 0.5149 1.0001 0.0186  0.0237  -0.0286 53  GLU A CB  
408  C CG  . GLU A 53  ? 0.7668 0.5510 1.0839 0.0157  0.0305  -0.0376 53  GLU A CG  
409  C CD  . GLU A 53  ? 0.8038 0.5741 1.1082 0.0099  0.0288  -0.0661 53  GLU A CD  
410  O OE1 . GLU A 53  ? 0.7397 0.4907 1.0462 0.0149  0.0376  -0.0799 53  GLU A OE1 
411  O OE2 . GLU A 53  ? 0.8722 0.6503 1.1642 0.0004  0.0185  -0.0744 53  GLU A OE2 
412  N N   . GLU A 54  ? 0.6230 0.4560 0.9355 0.0329  0.0235  0.0228  54  GLU A N   
413  C CA  . GLU A 54  ? 0.6166 0.4528 0.9498 0.0411  0.0258  0.0453  54  GLU A CA  
414  C C   . GLU A 54  ? 0.6393 0.4846 0.9700 0.0374  0.0175  0.0688  54  GLU A C   
415  O O   . GLU A 54  ? 0.6316 0.4691 0.9843 0.0403  0.0207  0.0859  54  GLU A O   
416  C CB  . GLU A 54  ? 0.6657 0.5161 0.9940 0.0484  0.0249  0.0469  54  GLU A CB  
417  C CG  . GLU A 54  ? 0.7522 0.5990 1.1120 0.0597  0.0336  0.0597  54  GLU A CG  
418  C CD  . GLU A 54  ? 0.7928 0.6543 1.1512 0.0666  0.0343  0.0607  54  GLU A CD  
419  O OE1 . GLU A 54  ? 0.7673 0.6273 1.1068 0.0666  0.0385  0.0403  54  GLU A OE1 
420  O OE2 . GLU A 54  ? 0.8180 0.6925 1.1952 0.0720  0.0303  0.0829  54  GLU A OE2 
421  N N   . PHE A 55  ? 0.6056 0.4654 0.9081 0.0310  0.0076  0.0700  55  PHE A N   
422  C CA  . PHE A 55  ? 0.6208 0.4864 0.9134 0.0271  0.0005  0.0910  55  PHE A CA  
423  C C   . PHE A 55  ? 0.5986 0.4534 0.8894 0.0197  0.0040  0.0908  55  PHE A C   
424  O O   . PHE A 55  ? 0.6023 0.4592 0.8813 0.0166  0.0005  0.1077  55  PHE A O   
425  C CB  . PHE A 55  ? 0.6104 0.4940 0.8734 0.0242  -0.0107 0.0946  55  PHE A CB  
426  C CG  . PHE A 55  ? 0.6738 0.5701 0.9409 0.0305  -0.0148 0.0971  55  PHE A CG  
427  C CD1 . PHE A 55  ? 0.6889 0.5857 0.9830 0.0383  -0.0139 0.1131  55  PHE A CD1 
428  C CD2 . PHE A 55  ? 0.6222 0.5304 0.8695 0.0288  -0.0189 0.0850  55  PHE A CD2 
429  C CE1 . PHE A 55  ? 0.7470 0.6567 1.0501 0.0442  -0.0167 0.1166  55  PHE A CE1 
430  C CE2 . PHE A 55  ? 0.6404 0.5605 0.8948 0.0345  -0.0213 0.0883  55  PHE A CE2 
431  C CZ  . PHE A 55  ? 0.7069 0.6282 0.9899 0.0420  -0.0202 0.1043  55  PHE A CZ  
432  N N   . GLY A 56  ? 0.5785 0.4213 0.8812 0.0169  0.0109  0.0725  56  GLY A N   
433  C CA  . GLY A 56  ? 0.5669 0.4002 0.8749 0.0095  0.0148  0.0717  56  GLY A CA  
434  C C   . GLY A 56  ? 0.5475 0.3913 0.8296 0.0021  0.0100  0.0698  56  GLY A C   
435  O O   . GLY A 56  ? 0.5919 0.4321 0.8734 -0.0022 0.0132  0.0811  56  GLY A O   
436  N N   . VAL A 57  ? 0.5495 0.4058 0.8109 0.0012  0.0039  0.0564  57  VAL A N   
437  C CA  . VAL A 57  ? 0.5275 0.3941 0.7654 -0.0048 0.0000  0.0533  57  VAL A CA  
438  C C   . VAL A 57  ? 0.5191 0.3863 0.7598 -0.0095 -0.0008 0.0309  57  VAL A C   
439  O O   . VAL A 57  ? 0.5398 0.4081 0.7792 -0.0068 -0.0032 0.0160  57  VAL A O   
440  C CB  . VAL A 57  ? 0.5161 0.3973 0.7270 -0.0023 -0.0077 0.0578  57  VAL A CB  
441  C CG1 . VAL A 57  ? 0.5215 0.4110 0.7086 -0.0081 -0.0099 0.0544  57  VAL A CG1 
442  C CG2 . VAL A 57  ? 0.5387 0.4202 0.7466 0.0016  -0.0104 0.0799  57  VAL A CG2 
443  N N   . LYS A 58  ? 0.4798 0.3464 0.7244 -0.0166 0.0011  0.0291  58  LYS A N   
444  C CA  . LYS A 58  ? 0.5266 0.3965 0.7743 -0.0220 -0.0027 0.0097  58  LYS A CA  
445  C C   . LYS A 58  ? 0.5584 0.4446 0.7791 -0.0221 -0.0085 0.0064  58  LYS A C   
446  O O   . LYS A 58  ? 0.5609 0.4527 0.7672 -0.0226 -0.0066 0.0190  58  LYS A O   
447  C CB  . LYS A 58  ? 0.5687 0.4328 0.8390 -0.0296 0.0015  0.0104  58  LYS A CB  
448  C CG  . LYS A 58  ? 0.6182 0.4908 0.8902 -0.0361 -0.0050 -0.0053 58  LYS A CG  
449  C CD  . LYS A 58  ? 0.6834 0.5578 0.9738 -0.0430 -0.0002 0.0021  58  LYS A CD  
450  C CE  . LYS A 58  ? 0.6995 0.5834 0.9985 -0.0497 -0.0085 -0.0124 58  LYS A CE  
451  N NZ  . LYS A 58  ? 0.6972 0.5738 1.0042 -0.0525 -0.0179 -0.0325 58  LYS A NZ  
452  N N   . ILE A 59  ? 0.5093 0.4013 0.7210 -0.0212 -0.0146 -0.0099 59  ILE A N   
453  C CA  . ILE A 59  ? 0.5575 0.4642 0.7458 -0.0209 -0.0197 -0.0127 59  ILE A CA  
454  C C   . ILE A 59  ? 0.5515 0.4642 0.7406 -0.0258 -0.0256 -0.0282 59  ILE A C   
455  O O   . ILE A 59  ? 0.5672 0.4737 0.7627 -0.0268 -0.0293 -0.0429 59  ILE A O   
456  C CB  . ILE A 59  ? 0.6121 0.5239 0.7835 -0.0138 -0.0219 -0.0127 59  ILE A CB  
457  C CG1 . ILE A 59  ? 0.6094 0.5165 0.7826 -0.0109 -0.0234 -0.0296 59  ILE A CG1 
458  C CG2 . ILE A 59  ? 0.5764 0.4842 0.7502 -0.0093 -0.0187 0.0040  59  ILE A CG2 
459  C CD1 . ILE A 59  ? 0.6042 0.5194 0.7638 -0.0133 -0.0294 -0.0433 59  ILE A CD1 
460  N N   . THR A 60  ? 0.5305 0.4542 0.7127 -0.0288 -0.0267 -0.0247 60  THR A N   
461  C CA  . THR A 60  ? 0.5293 0.4618 0.7128 -0.0329 -0.0339 -0.0366 60  THR A CA  
462  C C   . THR A 60  ? 0.4860 0.4307 0.6439 -0.0289 -0.0373 -0.0377 60  THR A C   
463  O O   . THR A 60  ? 0.4864 0.4352 0.6311 -0.0266 -0.0330 -0.0266 60  THR A O   
464  C CB  . THR A 60  ? 0.5339 0.4700 0.7382 -0.0396 -0.0320 -0.0319 60  THR A CB  
465  O OG1 . THR A 60  ? 0.6349 0.5815 0.8273 -0.0386 -0.0284 -0.0230 60  THR A OG1 
466  C CG2 . THR A 60  ? 0.5475 0.4720 0.7741 -0.0422 -0.0237 -0.0225 60  THR A CG2 
467  N N   . VAL A 61  ? 0.5175 0.4663 0.6670 -0.0283 -0.0448 -0.0510 61  VAL A N   
468  C CA  . VAL A 61  ? 0.4822 0.4421 0.6093 -0.0243 -0.0476 -0.0520 61  VAL A CA  
469  C C   . VAL A 61  ? 0.5027 0.4734 0.6316 -0.0282 -0.0550 -0.0576 61  VAL A C   
470  O O   . VAL A 61  ? 0.4937 0.4619 0.6314 -0.0323 -0.0626 -0.0685 61  VAL A O   
471  C CB  . VAL A 61  ? 0.5121 0.4679 0.6247 -0.0185 -0.0484 -0.0601 61  VAL A CB  
472  C CG1 . VAL A 61  ? 0.5022 0.4694 0.5935 -0.0142 -0.0499 -0.0593 61  VAL A CG1 
473  C CG2 . VAL A 61  ? 0.5980 0.5441 0.7159 -0.0144 -0.0415 -0.0530 61  VAL A CG2 
474  N N   . ALA A 62  ? 0.4524 0.4341 0.5745 -0.0274 -0.0533 -0.0499 62  ALA A N   
475  C CA  . ALA A 62  ? 0.5148 0.5083 0.6416 -0.0302 -0.0602 -0.0529 62  ALA A CA  
476  C C   . ALA A 62  ? 0.4777 0.4799 0.5812 -0.0250 -0.0618 -0.0530 62  ALA A C   
477  O O   . ALA A 62  ? 0.4242 0.4271 0.5164 -0.0217 -0.0546 -0.0446 62  ALA A O   
478  C CB  . ALA A 62  ? 0.4806 0.4786 0.6269 -0.0337 -0.0544 -0.0425 62  ALA A CB  
479  N N   . ASP A 63  ? 0.4172 0.4250 0.5122 -0.0245 -0.0714 -0.0622 63  ASP A N   
480  C CA  . ASP A 63  ? 0.4374 0.4526 0.5106 -0.0191 -0.0718 -0.0614 63  ASP A CA  
481  C C   . ASP A 63  ? 0.4444 0.4735 0.5206 -0.0198 -0.0774 -0.0580 63  ASP A C   
482  O O   . ASP A 63  ? 0.4689 0.5035 0.5291 -0.0169 -0.0832 -0.0617 63  ASP A O   
483  C CB  . ASP A 63  ? 0.4834 0.4925 0.5371 -0.0154 -0.0751 -0.0722 63  ASP A CB  
484  C CG  . ASP A 63  ? 0.4795 0.4770 0.5305 -0.0121 -0.0671 -0.0725 63  ASP A CG  
485  O OD1 . ASP A 63  ? 0.4587 0.4560 0.5139 -0.0110 -0.0599 -0.0623 63  ASP A OD1 
486  O OD2 . ASP A 63  ? 0.5027 0.4905 0.5463 -0.0104 -0.0680 -0.0827 63  ASP A OD2 
487  N N   . CYS A 64  ? 0.3504 0.3847 0.4464 -0.0228 -0.0740 -0.0497 64  CYS A N   
488  C CA  . CYS A 64  ? 0.3991 0.4469 0.5034 -0.0227 -0.0775 -0.0443 64  CYS A CA  
489  C C   . CYS A 64  ? 0.4215 0.4705 0.5319 -0.0211 -0.0643 -0.0324 64  CYS A C   
490  O O   . CYS A 64  ? 0.4316 0.4893 0.5616 -0.0222 -0.0636 -0.0260 64  CYS A O   
491  C CB  . CYS A 64  ? 0.4073 0.4614 0.5371 -0.0290 -0.0887 -0.0471 64  CYS A CB  
492  S SG  . CYS A 64  ? 0.6650 0.7108 0.8247 -0.0352 -0.0824 -0.0447 64  CYS A SG  
493  N N   . LYS A 65  ? 0.3974 0.4370 0.4917 -0.0186 -0.0542 -0.0292 65  LYS A N   
494  C CA  . LYS A 65  ? 0.4086 0.4451 0.5025 -0.0178 -0.0416 -0.0197 65  LYS A CA  
495  C C   . LYS A 65  ? 0.3992 0.4407 0.4785 -0.0136 -0.0396 -0.0168 65  LYS A C   
496  O O   . LYS A 65  ? 0.4211 0.4600 0.4803 -0.0110 -0.0406 -0.0190 65  LYS A O   
497  C CB  . LYS A 65  ? 0.4339 0.4563 0.5168 -0.0187 -0.0335 -0.0171 65  LYS A CB  
498  C CG  . LYS A 65  ? 0.5137 0.5287 0.5798 -0.0175 -0.0227 -0.0102 65  LYS A CG  
499  C CD  . LYS A 65  ? 0.5938 0.6016 0.6692 -0.0195 -0.0099 -0.0027 65  LYS A CD  
500  C CE  . LYS A 65  ? 0.7516 0.7480 0.8289 -0.0224 -0.0055 0.0001  65  LYS A CE  
501  N NZ  . LYS A 65  ? 1.0175 1.0031 1.0690 -0.0223 -0.0059 0.0013  65  LYS A NZ  
502  N N   . GLU A 66  ? 0.4143 0.4628 0.5065 -0.0126 -0.0359 -0.0109 66  GLU A N   
503  C CA  . GLU A 66  ? 0.3953 0.4467 0.4763 -0.0085 -0.0320 -0.0070 66  GLU A CA  
504  C C   . GLU A 66  ? 0.3703 0.4073 0.4353 -0.0087 -0.0188 -0.0035 66  GLU A C   
505  O O   . GLU A 66  ? 0.3411 0.3701 0.4129 -0.0104 -0.0081 0.0009  66  GLU A O   
506  C CB  . GLU A 66  ? 0.3891 0.4524 0.4921 -0.0069 -0.0320 -0.0008 66  GLU A CB  
507  C CG  . GLU A 66  ? 0.4616 0.5380 0.5796 -0.0085 -0.0480 -0.0044 66  GLU A CG  
508  C CD  . GLU A 66  ? 0.5402 0.6314 0.6658 -0.0054 -0.0562 0.0000  66  GLU A CD  
509  O OE1 . GLU A 66  ? 0.5764 0.6717 0.7170 -0.0026 -0.0477 0.0094  66  GLU A OE1 
510  O OE2 . GLU A 66  ? 0.5831 0.6808 0.6990 -0.0054 -0.0706 -0.0054 66  GLU A OE2 
511  N N   . LYS A 67  ? 0.3230 0.3555 0.3660 -0.0076 -0.0203 -0.0057 67  LYS A N   
512  C CA  . LYS A 67  ? 0.3494 0.3681 0.3734 -0.0091 -0.0124 -0.0037 67  LYS A CA  
513  C C   . LYS A 67  ? 0.4026 0.4196 0.4183 -0.0070 -0.0066 -0.0008 67  LYS A C   
514  O O   . LYS A 67  ? 0.3763 0.3798 0.3753 -0.0092 -0.0001 0.0002  67  LYS A O   
515  C CB  . LYS A 67  ? 0.3182 0.3334 0.3282 -0.0101 -0.0190 -0.0069 67  LYS A CB  
516  C CG  . LYS A 67  ? 0.3761 0.3887 0.3938 -0.0122 -0.0222 -0.0089 67  LYS A CG  
517  C CD  . LYS A 67  ? 0.3780 0.3861 0.3848 -0.0126 -0.0268 -0.0098 67  LYS A CD  
518  C CE  . LYS A 67  ? 0.4458 0.4532 0.4641 -0.0132 -0.0307 -0.0128 67  LYS A CE  
519  N NZ  . LYS A 67  ? 0.4879 0.4927 0.5006 -0.0122 -0.0348 -0.0130 67  LYS A NZ  
520  N N   . VAL A 68  ? 0.3471 0.3764 0.3732 -0.0032 -0.0094 0.0006  68  VAL A N   
521  C CA  . VAL A 68  ? 0.3582 0.3858 0.3802 -0.0007 -0.0030 0.0044  68  VAL A CA  
522  C C   . VAL A 68  ? 0.3632 0.4004 0.4076 0.0028  0.0003  0.0099  68  VAL A C   
523  O O   . VAL A 68  ? 0.3602 0.4100 0.4219 0.0034  -0.0077 0.0101  68  VAL A O   
524  C CB  . VAL A 68  ? 0.3807 0.4133 0.3910 0.0014  -0.0093 0.0033  68  VAL A CB  
525  C CG1 . VAL A 68  ? 0.3234 0.3471 0.3170 -0.0021 -0.0117 0.0000  68  VAL A CG1 
526  C CG2 . VAL A 68  ? 0.3132 0.3616 0.3305 0.0050  -0.0200 0.0020  68  VAL A CG2 
527  N N   . SER A 69  ? 0.3215 0.3514 0.3673 0.0045  0.0121  0.0144  69  SER A N   
528  C CA  . SER A 69  ? 0.3993 0.4381 0.4696 0.0089  0.0170  0.0219  69  SER A CA  
529  C C   . SER A 69  ? 0.3718 0.4020 0.4370 0.0119  0.0282  0.0258  69  SER A C   
530  O O   . SER A 69  ? 0.3793 0.3955 0.4216 0.0094  0.0317  0.0217  69  SER A O   
531  C CB  . SER A 69  ? 0.3911 0.4270 0.4807 0.0078  0.0261  0.0248  69  SER A CB  
532  O OG  . SER A 69  ? 0.4378 0.4517 0.5094 0.0052  0.0410  0.0228  69  SER A OG  
533  N N   . GLU A 70  ? 0.3684 0.4070 0.4568 0.0170  0.0331  0.0341  70  GLU A N   
534  C CA  . GLU A 70  ? 0.4931 0.5233 0.5813 0.0206  0.0447  0.0387  70  GLU A CA  
535  C C   . GLU A 70  ? 0.5669 0.5932 0.6796 0.0243  0.0607  0.0460  70  GLU A C   
536  O O   . GLU A 70  ? 0.5196 0.5640 0.6629 0.0281  0.0565  0.0544  70  GLU A O   
537  C CB  . GLU A 70  ? 0.5085 0.5548 0.6021 0.0253  0.0345  0.0444  70  GLU A CB  
538  C CG  . GLU A 70  ? 0.6144 0.6505 0.7062 0.0286  0.0463  0.0489  70  GLU A CG  
539  C CD  . GLU A 70  ? 0.6802 0.7306 0.7736 0.0331  0.0369  0.0553  70  GLU A CD  
540  O OE1 . GLU A 70  ? 0.6290 0.6977 0.7429 0.0381  0.0296  0.0644  70  GLU A OE1 
541  O OE2 . GLU A 70  ? 0.6122 0.6555 0.6867 0.0315  0.0364  0.0521  70  GLU A OE2 
542  N N   . ARG A 71  ? 0.5575 0.5592 0.6563 0.0229  0.0792  0.0429  71  ARG A N   
543  C CA  . ARG A 71  ? 0.5909 0.5816 0.7074 0.0267  0.1002  0.0485  71  ARG A CA  
544  C C   . ARG A 71  ? 0.6520 0.6250 0.7608 0.0296  0.1150  0.0494  71  ARG A C   
545  O O   . ARG A 71  ? 0.6455 0.5960 0.7213 0.0246  0.1194  0.0404  71  ARG A O   
546  C CB  . ARG A 71  ? 0.6893 0.6595 0.7878 0.0219  0.1121  0.0421  71  ARG A CB  
547  C CG  . ARG A 71  ? 0.6706 0.6522 0.7684 0.0174  0.0978  0.0390  71  ARG A CG  
548  C CD  . ARG A 71  ? 0.7424 0.7012 0.8076 0.0113  0.1044  0.0312  71  ARG A CD  
549  N NE  . ARG A 71  ? 0.7972 0.7308 0.8539 0.0126  0.1293  0.0319  71  ARG A NE  
550  C CZ  . ARG A 71  ? 0.8053 0.7166 0.8352 0.0085  0.1397  0.0275  71  ARG A CZ  
551  N NH1 . ARG A 71  ? 0.7520 0.6648 0.7647 0.0029  0.1265  0.0233  71  ARG A NH1 
552  N NH2 . ARG A 71  ? 0.7906 0.6768 0.8100 0.0104  0.1642  0.0279  71  ARG A NH2 
553  N N   . ASN A 72  ? 0.6435 0.6264 0.7839 0.0373  0.1215  0.0607  72  ASN A N   
554  C CA  . ASN A 72  ? 0.6279 0.5934 0.7683 0.0413  0.1384  0.0632  72  ASN A CA  
555  C C   . ASN A 72  ? 0.5762 0.5353 0.6920 0.0383  0.1304  0.0581  72  ASN A C   
556  O O   . ASN A 72  ? 0.6281 0.5609 0.7253 0.0363  0.1440  0.0525  72  ASN A O   
557  C CB  . ASN A 72  ? 0.6890 0.6226 0.8154 0.0401  0.1637  0.0575  72  ASN A CB  
558  C CG  . ASN A 72  ? 0.7709 0.7085 0.9155 0.0414  0.1719  0.0610  72  ASN A CG  
559  O OD1 . ASN A 72  ? 0.7656 0.7173 0.9519 0.0486  0.1798  0.0732  72  ASN A OD1 
560  N ND2 . ASN A 72  ? 0.8045 0.7310 0.9212 0.0345  0.1700  0.0517  72  ASN A ND2 
561  N N   . GLY A 73  ? 0.5103 0.4916 0.6254 0.0376  0.1091  0.0597  73  GLY A N   
562  C CA  . GLY A 73  ? 0.4950 0.4725 0.5897 0.0348  0.1016  0.0560  73  GLY A CA  
563  C C   . GLY A 73  ? 0.5210 0.4834 0.5808 0.0254  0.0961  0.0427  73  GLY A C   
564  O O   . GLY A 73  ? 0.5306 0.4905 0.5758 0.0221  0.0893  0.0397  73  GLY A O   
565  N N   . VAL A 74  ? 0.4609 0.4401 0.4618 0.0301  0.0057  0.0118  74  VAL A N   
566  C CA  . VAL A 74  ? 0.4220 0.3911 0.4122 0.0234  0.0091  0.0011  74  VAL A CA  
567  C C   . VAL A 74  ? 0.4266 0.3930 0.3944 0.0170  0.0005  -0.0002 74  VAL A C   
568  O O   . VAL A 74  ? 0.4403 0.4162 0.4058 0.0122  -0.0075 0.0011  74  VAL A O   
569  C CB  . VAL A 74  ? 0.4142 0.3899 0.4164 0.0198  0.0145  -0.0083 74  VAL A CB  
570  C CG1 . VAL A 74  ? 0.3916 0.3637 0.3795 0.0121  0.0130  -0.0158 74  VAL A CG1 
571  C CG2 . VAL A 74  ? 0.4484 0.4181 0.4671 0.0247  0.0255  -0.0124 74  VAL A CG2 
572  N N   . LEU A 75  ? 0.3323 0.2857 0.2855 0.0168  0.0027  -0.0031 75  LEU A N   
573  C CA  . LEU A 75  ? 0.3968 0.3416 0.3286 0.0125  -0.0030 -0.0064 75  LEU A CA  
574  C C   . LEU A 75  ? 0.3730 0.3158 0.3054 0.0076  -0.0026 -0.0125 75  LEU A C   
575  O O   . LEU A 75  ? 0.3059 0.2513 0.2478 0.0090  0.0029  -0.0152 75  LEU A O   
576  C CB  . LEU A 75  ? 0.3987 0.3316 0.3160 0.0172  0.0015  -0.0063 75  LEU A CB  
577  C CG  . LEU A 75  ? 0.4422 0.3764 0.3571 0.0225  0.0040  0.0020  75  LEU A CG  
578  C CD1 . LEU A 75  ? 0.4267 0.3524 0.3304 0.0266  0.0120  0.0018  75  LEU A CD1 
579  C CD2 . LEU A 75  ? 0.4982 0.4373 0.4000 0.0204  -0.0059 0.0064  75  LEU A CD2 
580  N N   . VAL A 76  ? 0.4330 0.3709 0.3544 0.0008  -0.0087 -0.0140 76  VAL A N   
581  C CA  . VAL A 76  ? 0.3557 0.2892 0.2749 -0.0039 -0.0084 -0.0164 76  VAL A CA  
582  C C   . VAL A 76  ? 0.4390 0.3504 0.3376 -0.0051 -0.0112 -0.0183 76  VAL A C   
583  O O   . VAL A 76  ? 0.3732 0.2764 0.2599 -0.0108 -0.0166 -0.0199 76  VAL A O   
584  C CB  . VAL A 76  ? 0.3816 0.3294 0.3113 -0.0125 -0.0104 -0.0152 76  VAL A CB  
585  C CG1 . VAL A 76  ? 0.4089 0.3542 0.3355 -0.0165 -0.0081 -0.0154 76  VAL A CG1 
586  C CG2 . VAL A 76  ? 0.4215 0.3888 0.3720 -0.0087 -0.0065 -0.0142 76  VAL A CG2 
587  N N   . GLY A 77  ? 0.3432 0.2457 0.2384 0.0010  -0.0074 -0.0186 77  GLY A N   
588  C CA  . GLY A 77  ? 0.4249 0.3038 0.3038 0.0036  -0.0075 -0.0198 77  GLY A CA  
589  C C   . GLY A 77  ? 0.4885 0.3619 0.3672 0.0011  -0.0084 -0.0155 77  GLY A C   
590  O O   . GLY A 77  ? 0.4462 0.3369 0.3359 0.0019  -0.0073 -0.0123 77  GLY A O   
591  N N   . GLU A 78  ? 0.4581 0.3058 0.3223 -0.0028 -0.0102 -0.0151 78  GLU A N   
592  C CA  . GLU A 78  ? 0.5249 0.3643 0.3870 -0.0050 -0.0106 -0.0076 78  GLU A CA  
593  C C   . GLU A 78  ? 0.5065 0.3107 0.3540 0.0003  -0.0092 -0.0059 78  GLU A C   
594  O O   . GLU A 78  ? 0.4362 0.2158 0.2705 -0.0022 -0.0088 -0.0134 78  GLU A O   
595  C CB  . GLU A 78  ? 0.6050 0.4538 0.4705 -0.0210 -0.0133 -0.0045 78  GLU A CB  
596  C CG  . GLU A 78  ? 0.6251 0.4586 0.4828 -0.0347 -0.0169 -0.0085 78  GLU A CG  
597  C CD  . GLU A 78  ? 0.7715 0.6165 0.6358 -0.0507 -0.0179 -0.0030 78  GLU A CD  
598  O OE1 . GLU A 78  ? 0.8504 0.7063 0.7205 -0.0631 -0.0218 -0.0066 78  GLU A OE1 
599  O OE2 . GLU A 78  ? 0.7554 0.6016 0.6194 -0.0509 -0.0148 0.0059  78  GLU A OE2 
600  N N   . VAL A 79  ? 0.4464 0.2484 0.2957 0.0091  -0.0081 0.0036  79  VAL A N   
601  C CA  . VAL A 79  ? 0.6362 0.4038 0.4748 0.0171  -0.0060 0.0095  79  VAL A CA  
602  C C   . VAL A 79  ? 0.6820 0.4468 0.5178 0.0085  -0.0085 0.0231  79  VAL A C   
603  O O   . VAL A 79  ? 0.6019 0.3982 0.4456 0.0046  -0.0107 0.0282  79  VAL A O   
604  C CB  . VAL A 79  ? 0.6327 0.4023 0.4778 0.0391  -0.0023 0.0123  79  VAL A CB  
605  C CG1 . VAL A 79  ? 0.6108 0.3808 0.4559 0.0463  0.0028  -0.0004 79  VAL A CG1 
606  C CG2 . VAL A 79  ? 0.6623 0.4704 0.5229 0.0444  -0.0058 0.0210  79  VAL A CG2 
607  N N   . SER A 80  ? 0.8187 0.5451 0.6418 0.0036  -0.0071 0.0281  80  SER A N   
608  C CA  . SER A 80  ? 0.8390 0.5598 0.6575 -0.0063 -0.0080 0.0434  80  SER A CA  
609  C C   . SER A 80  ? 1.0086 0.6822 0.8151 0.0003  -0.0050 0.0546  80  SER A C   
610  O O   . SER A 80  ? 1.1336 0.7714 0.9333 0.0066  -0.0014 0.0458  80  SER A O   
611  C CB  . SER A 80  ? 0.7684 0.4960 0.5868 -0.0305 -0.0089 0.0393  80  SER A CB  
612  O OG  . SER A 80  ? 0.9009 0.6001 0.7124 -0.0398 -0.0090 0.0268  80  SER A OG  
613  N N   . SER A 81  ? 0.8963 0.5686 0.6987 -0.0009 -0.0056 0.0742  81  SER A N   
614  C CA  . SER A 81  ? 1.0041 0.6316 0.7959 0.0064  -0.0026 0.0908  81  SER A CA  
615  C C   . SER A 81  ? 0.9569 0.5726 0.7391 -0.0141 -0.0013 0.1061  81  SER A C   
616  O O   . SER A 81  ? 0.9263 0.5761 0.7118 -0.0315 -0.0024 0.1046  81  SER A O   
617  C CB  . SER A 81  ? 1.0345 0.6772 0.8313 0.0314  -0.0054 0.1070  81  SER A CB  
618  O OG  . SER A 81  ? 1.2809 0.9192 1.0865 0.0529  -0.0034 0.0974  81  SER A OG  
619  N N   . ALA A 82  ? 1.0384 0.6049 0.8097 -0.0109 0.0026  0.1217  82  ALA A N   
620  C CA  . ALA A 82  ? 1.0384 0.5855 0.7991 -0.0275 0.0056  0.1421  82  ALA A CA  
621  C C   . ALA A 82  ? 1.1435 0.6567 0.8987 -0.0054 0.0072  0.1653  82  ALA A C   
622  O O   . ALA A 82  ? 1.1396 0.6200 0.9026 0.0073  0.0107  0.1577  82  ALA A O   
623  C CB  . ALA A 82  ? 1.0973 0.6065 0.8535 -0.0538 0.0102  0.1313  82  ALA A CB  
624  N N   . GLU A 83  ? 1.2022 0.7399 0.9530 0.0009  0.0039  0.1903  83  GLU A N   
625  C CA  . GLU A 83  ? 1.2319 0.7582 0.9891 0.0224  0.0029  0.2130  83  GLU A CA  
626  C C   . GLU A 83  ? 1.1883 0.7342 0.9359 0.0133  0.0016  0.2406  83  GLU A C   
627  O O   . GLU A 83  ? 1.1662 0.7564 0.9033 0.0109  -0.0035 0.2454  83  GLU A O   
628  C CB  . GLU A 83  ? 1.2768 0.8295 1.0431 0.0528  -0.0042 0.2138  83  GLU A CB  
629  C CG  . GLU A 83  ? 1.3501 0.8962 1.1271 0.0752  -0.0082 0.2369  83  GLU A CG  
630  C CD  . GLU A 83  ? 1.4162 0.9931 1.2084 0.1044  -0.0155 0.2371  83  GLU A CD  
631  O OE1 . GLU A 83  ? 1.3988 0.9810 1.1997 0.1124  -0.0125 0.2147  83  GLU A OE1 
632  O OE2 . GLU A 83  ? 1.3663 0.9632 1.1622 0.1184  -0.0246 0.2595  83  GLU A OE2 
633  N N   . GLY A 84  ? 1.2595 0.7731 1.0099 0.0083  0.0063  0.2581  84  GLY A N   
634  C CA  . GLY A 84  ? 1.2367 0.7651 0.9782 -0.0002 0.0068  0.2873  84  GLY A CA  
635  C C   . GLY A 84  ? 1.2100 0.7746 0.9375 -0.0236 0.0114  0.2843  84  GLY A C   
636  O O   . GLY A 84  ? 1.2471 0.8516 0.9618 -0.0208 0.0089  0.3003  84  GLY A O   
637  N N   . GLY A 85  ? 1.2851 0.8397 1.0152 -0.0465 0.0173  0.2616  85  GLY A N   
638  C CA  . GLY A 85  ? 1.1812 0.7715 0.9041 -0.0712 0.0211  0.2549  85  GLY A CA  
639  C C   . GLY A 85  ? 1.1497 0.7861 0.8666 -0.0681 0.0137  0.2404  85  GLY A C   
640  O O   . GLY A 85  ? 1.1507 0.8217 0.8657 -0.0874 0.0171  0.2330  85  GLY A O   
641  N N   . VAL A 86  ? 1.0571 0.6975 0.7750 -0.0438 0.0045  0.2355  86  VAL A N   
642  C CA  . VAL A 86  ? 0.9986 0.6953 0.7265 -0.0367 -0.0019 0.2161  86  VAL A CA  
643  C C   . VAL A 86  ? 1.0099 0.7043 0.7574 -0.0378 -0.0019 0.1854  86  VAL A C   
644  O O   . VAL A 86  ? 0.9948 0.6602 0.7489 -0.0218 -0.0039 0.1794  86  VAL A O   
645  C CB  . VAL A 86  ? 0.9972 0.7149 0.7235 -0.0095 -0.0122 0.2266  86  VAL A CB  
646  C CG1 . VAL A 86  ? 0.8942 0.6739 0.6242 -0.0095 -0.0178 0.2118  86  VAL A CG1 
647  C CG2 . VAL A 86  ? 0.9995 0.7009 0.7064 -0.0007 -0.0143 0.2624  86  VAL A CG2 
648  N N   . VAL A 87  ? 0.8903 0.6166 0.6469 -0.0548 0.0008  0.1667  87  VAL A N   
649  C CA  . VAL A 87  ? 0.9051 0.6348 0.6786 -0.0546 -0.0005 0.1401  87  VAL A CA  
650  C C   . VAL A 87  ? 0.8521 0.6219 0.6342 -0.0382 -0.0064 0.1289  87  VAL A C   
651  O O   . VAL A 87  ? 0.8142 0.6246 0.5948 -0.0417 -0.0067 0.1285  87  VAL A O   
652  C CB  . VAL A 87  ? 0.8833 0.6260 0.6663 -0.0787 0.0042  0.1267  87  VAL A CB  
653  C CG1 . VAL A 87  ? 0.8083 0.5735 0.6081 -0.0750 0.0009  0.1018  87  VAL A CG1 
654  C CG2 . VAL A 87  ? 0.9323 0.6293 0.7118 -0.0959 0.0083  0.1313  87  VAL A CG2 
655  N N   . LYS A 88  ? 0.8091 0.5670 0.5995 -0.0212 -0.0099 0.1195  88  LYS A N   
656  C CA  . LYS A 88  ? 0.7888 0.5830 0.5905 -0.0080 -0.0147 0.1081  88  LYS A CA  
657  C C   . LYS A 88  ? 0.7597 0.5574 0.5752 -0.0109 -0.0132 0.0847  88  LYS A C   
658  O O   . LYS A 88  ? 0.7305 0.4955 0.5451 -0.0145 -0.0107 0.0781  88  LYS A O   
659  C CB  . LYS A 88  ? 0.8363 0.6273 0.6390 0.0154  -0.0199 0.1197  88  LYS A CB  
660  C CG  . LYS A 88  ? 0.8533 0.6588 0.6427 0.0185  -0.0244 0.1431  88  LYS A CG  
661  C CD  . LYS A 88  ? 0.8588 0.6768 0.6540 0.0423  -0.0324 0.1548  88  LYS A CD  
662  C CE  . LYS A 88  ? 0.9648 0.8161 0.7798 0.0515  -0.0361 0.1367  88  LYS A CE  
663  N NZ  . LYS A 88  ? 0.8837 0.7798 0.6994 0.0380  -0.0387 0.1235  88  LYS A NZ  
664  N N   . LYS A 89  ? 0.6556 0.4918 0.4819 -0.0110 -0.0144 0.0721  89  LYS A N   
665  C CA  . LYS A 89  ? 0.6071 0.4488 0.4455 -0.0131 -0.0131 0.0534  89  LYS A CA  
666  C C   . LYS A 89  ? 0.5776 0.4523 0.4280 -0.0046 -0.0149 0.0443  89  LYS A C   
667  O O   . LYS A 89  ? 0.5045 0.4074 0.3547 -0.0072 -0.0159 0.0457  89  LYS A O   
668  C CB  . LYS A 89  ? 0.6167 0.4699 0.4588 -0.0316 -0.0099 0.0471  89  LYS A CB  
669  C CG  . LYS A 89  ? 0.7030 0.5269 0.5397 -0.0450 -0.0084 0.0493  89  LYS A CG  
670  C CD  . LYS A 89  ? 0.7489 0.5945 0.5964 -0.0617 -0.0063 0.0420  89  LYS A CD  
671  C CE  . LYS A 89  ? 0.7531 0.5862 0.5953 -0.0801 -0.0031 0.0521  89  LYS A CE  
672  N NZ  . LYS A 89  ? 0.7965 0.6541 0.6542 -0.0962 -0.0015 0.0451  89  LYS A NZ  
673  N N   . ARG A 90  ? 0.4755 0.3465 0.3348 0.0035  -0.0144 0.0340  90  ARG A N   
674  C CA  . ARG A 90  ? 0.4999 0.3992 0.3726 0.0089  -0.0148 0.0250  90  ARG A CA  
675  C C   . ARG A 90  ? 0.4831 0.3820 0.3635 0.0048  -0.0116 0.0122  90  ARG A C   
676  O O   . ARG A 90  ? 0.4620 0.3378 0.3375 0.0059  -0.0106 0.0095  90  ARG A O   
677  C CB  . ARG A 90  ? 0.5313 0.4332 0.4098 0.0252  -0.0169 0.0290  90  ARG A CB  
678  C CG  . ARG A 90  ? 0.5993 0.5351 0.4925 0.0267  -0.0180 0.0215  90  ARG A CG  
679  C CD  . ARG A 90  ? 0.6112 0.5680 0.5092 0.0359  -0.0241 0.0303  90  ARG A CD  
680  N NE  . ARG A 90  ? 0.7019 0.6404 0.6005 0.0519  -0.0242 0.0406  90  ARG A NE  
681  C CZ  . ARG A 90  ? 0.7753 0.7160 0.6703 0.0613  -0.0299 0.0563  90  ARG A CZ  
682  N NH1 . ARG A 90  ? 0.7948 0.7582 0.6824 0.0548  -0.0370 0.0637  90  ARG A NH1 
683  N NH2 . ARG A 90  ? 0.9270 0.8473 0.8249 0.0784  -0.0281 0.0650  90  ARG A NH2 
684  N N   . ARG A 91  ? 0.4216 0.3442 0.3122 -0.0001 -0.0100 0.0046  91  ARG A N   
685  C CA  . ARG A 91  ? 0.4153 0.3397 0.3145 -0.0020 -0.0074 -0.0042 91  ARG A CA  
686  C C   . ARG A 91  ? 0.4493 0.3889 0.3611 0.0041  -0.0051 -0.0103 91  ARG A C   
687  O O   . ARG A 91  ? 0.3588 0.3162 0.2761 0.0036  -0.0052 -0.0120 91  ARG A O   
688  C CB  . ARG A 91  ? 0.4516 0.3871 0.3554 -0.0127 -0.0056 -0.0067 91  ARG A CB  
689  C CG  . ARG A 91  ? 0.5337 0.4550 0.4298 -0.0218 -0.0074 -0.0024 91  ARG A CG  
690  C CD  . ARG A 91  ? 0.5302 0.4695 0.4367 -0.0315 -0.0051 -0.0043 91  ARG A CD  
691  N NE  . ARG A 91  ? 0.5591 0.4881 0.4604 -0.0433 -0.0072 0.0004  91  ARG A NE  
692  C CZ  . ARG A 91  ? 0.6250 0.5704 0.5375 -0.0536 -0.0061 0.0004  91  ARG A CZ  
693  N NH1 . ARG A 91  ? 0.6546 0.6260 0.5841 -0.0506 -0.0021 -0.0039 91  ARG A NH1 
694  N NH2 . ARG A 91  ? 0.6580 0.5942 0.5667 -0.0670 -0.0085 0.0046  91  ARG A NH2 
695  N N   . LEU A 92  ? 0.3758 0.3089 0.2911 0.0075  -0.0030 -0.0139 92  LEU A N   
696  C CA  . LEU A 92  ? 0.3439 0.2867 0.2711 0.0118  0.0009  -0.0181 92  LEU A CA  
697  C C   . LEU A 92  ? 0.3699 0.3145 0.3029 0.0080  0.0031  -0.0208 92  LEU A C   
698  O O   . LEU A 92  ? 0.3534 0.2887 0.2792 0.0063  0.0009  -0.0193 92  LEU A O   
699  C CB  . LEU A 92  ? 0.4167 0.3489 0.3401 0.0211  0.0030  -0.0167 92  LEU A CB  
700  C CG  . LEU A 92  ? 0.3615 0.3029 0.2964 0.0249  0.0088  -0.0188 92  LEU A CG  
701  C CD1 . LEU A 92  ? 0.3628 0.3252 0.3138 0.0229  0.0092  -0.0206 92  LEU A CD1 
702  C CD2 . LEU A 92  ? 0.4017 0.3338 0.3305 0.0346  0.0128  -0.0174 92  LEU A CD2 
703  N N   . TYR A 93  ? 0.3258 0.2824 0.2723 0.0065  0.0071  -0.0249 93  TYR A N   
704  C CA  . TYR A 93  ? 0.3390 0.2970 0.2948 0.0058  0.0103  -0.0257 93  TYR A CA  
705  C C   . TYR A 93  ? 0.3716 0.3280 0.3362 0.0096  0.0156  -0.0259 93  TYR A C   
706  O O   . TYR A 93  ? 0.3210 0.2834 0.2926 0.0080  0.0183  -0.0299 93  TYR A O   
707  C CB  . TYR A 93  ? 0.3487 0.3175 0.3134 0.0011  0.0135  -0.0310 93  TYR A CB  
708  C CG  . TYR A 93  ? 0.3639 0.3376 0.3199 -0.0043 0.0104  -0.0299 93  TYR A CG  
709  C CD1 . TYR A 93  ? 0.3969 0.3723 0.3422 -0.0066 0.0075  -0.0292 93  TYR A CD1 
710  C CD2 . TYR A 93  ? 0.4170 0.3959 0.3768 -0.0073 0.0105  -0.0278 93  TYR A CD2 
711  C CE1 . TYR A 93  ? 0.4431 0.4207 0.3786 -0.0122 0.0056  -0.0253 93  TYR A CE1 
712  C CE2 . TYR A 93  ? 0.4175 0.4016 0.3704 -0.0143 0.0093  -0.0255 93  TYR A CE2 
713  C CZ  . TYR A 93  ? 0.4553 0.4368 0.3946 -0.0170 0.0074  -0.0240 93  TYR A CZ  
714  O OH  . TYR A 93  ? 0.4567 0.4409 0.3871 -0.0245 0.0071  -0.0190 93  TYR A OH  
715  N N   . ALA A 94  ? 0.3496 0.2994 0.3131 0.0134  0.0168  -0.0205 94  ALA A N   
716  C CA  . ALA A 94  ? 0.3916 0.3384 0.3620 0.0162  0.0232  -0.0179 94  ALA A CA  
717  C C   . ALA A 94  ? 0.3897 0.3321 0.3653 0.0194  0.0257  -0.0111 94  ALA A C   
718  O O   . ALA A 94  ? 0.3750 0.3178 0.3432 0.0215  0.0202  -0.0060 94  ALA A O   
719  C CB  . ALA A 94  ? 0.3564 0.2994 0.3150 0.0201  0.0239  -0.0150 94  ALA A CB  
720  N N   . SER A 95  ? 0.3176 0.2561 0.3066 0.0193  0.0336  -0.0103 95  SER A N   
721  C CA  . SER A 95  ? 0.4040 0.3348 0.3982 0.0244  0.0375  0.0000  95  SER A CA  
722  C C   . SER A 95  ? 0.4166 0.3396 0.4183 0.0222  0.0474  0.0030  95  SER A C   
723  O O   . SER A 95  ? 0.3688 0.2973 0.3712 0.0171  0.0494  -0.0029 95  SER A O   
724  C CB  . SER A 95  ? 0.4746 0.4053 0.4834 0.0274  0.0384  -0.0005 95  SER A CB  
725  O OG  . SER A 95  ? 0.5128 0.4370 0.5369 0.0234  0.0468  -0.0101 95  SER A OG  
726  N N   . ALA A 96  ? 0.4486 0.3603 0.4570 0.0259  0.0535  0.0138  96  ALA A N   
727  C CA  . ALA A 96  ? 0.4698 0.3721 0.4865 0.0217  0.0643  0.0184  96  ALA A CA  
728  C C   . ALA A 96  ? 0.4242 0.3255 0.4584 0.0112  0.0696  0.0039  96  ALA A C   
729  O O   . ALA A 96  ? 0.4298 0.3245 0.4747 0.0100  0.0707  -0.0047 96  ALA A O   
730  C CB  . ALA A 96  ? 0.4633 0.3494 0.4853 0.0279  0.0702  0.0340  96  ALA A CB  
731  N N   . GLY A 97  ? 0.4174 0.3293 0.4533 0.0041  0.0718  0.0003  97  GLY A N   
732  C CA  . GLY A 97  ? 0.4343 0.3526 0.4861 -0.0083 0.0747  -0.0126 97  GLY A CA  
733  C C   . GLY A 97  ? 0.4530 0.3806 0.5045 -0.0115 0.0669  -0.0281 97  GLY A C   
734  O O   . GLY A 97  ? 0.4411 0.3698 0.5041 -0.0224 0.0689  -0.0406 97  GLY A O   
735  N N   . ASN A 98  ? 0.3954 0.3302 0.4323 -0.0038 0.0581  -0.0275 98  ASN A N   
736  C CA  . ASN A 98  ? 0.4670 0.4098 0.5007 -0.0063 0.0519  -0.0393 98  ASN A CA  
737  C C   . ASN A 98  ? 0.4050 0.3602 0.4227 -0.0012 0.0420  -0.0370 98  ASN A C   
738  O O   . ASN A 98  ? 0.3876 0.3382 0.3943 0.0063  0.0393  -0.0282 98  ASN A O   
739  C CB  . ASN A 98  ? 0.3919 0.3209 0.4286 -0.0017 0.0553  -0.0402 98  ASN A CB  
740  C CG  . ASN A 98  ? 0.5293 0.4631 0.5659 -0.0055 0.0545  -0.0539 98  ASN A CG  
741  O OD1 . ASN A 98  ? 0.6304 0.5622 0.6667 0.0008  0.0551  -0.0533 98  ASN A OD1 
742  N ND2 . ASN A 98  ? 0.6518 0.5949 0.6888 -0.0161 0.0533  -0.0667 98  ASN A ND2 
743  N N   . PHE A 99  ? 0.3962 0.3659 0.4117 -0.0059 0.0364  -0.0446 99  PHE A N   
744  C CA  . PHE A 99  ? 0.3439 0.3204 0.3448 -0.0013 0.0282  -0.0414 99  PHE A CA  
745  C C   . PHE A 99  ? 0.4096 0.3971 0.4059 -0.0070 0.0233  -0.0494 99  PHE A C   
746  O O   . PHE A 99  ? 0.3153 0.3112 0.3189 -0.0152 0.0245  -0.0590 99  PHE A O   
747  C CB  . PHE A 99  ? 0.3143 0.2975 0.3123 0.0041  0.0259  -0.0350 99  PHE A CB  
748  C CG  . PHE A 99  ? 0.4268 0.4306 0.4334 0.0004  0.0222  -0.0386 99  PHE A CG  
749  C CD1 . PHE A 99  ? 0.3991 0.4130 0.3971 0.0015  0.0137  -0.0385 99  PHE A CD1 
750  C CD2 . PHE A 99  ? 0.4207 0.4363 0.4448 -0.0044 0.0267  -0.0401 99  PHE A CD2 
751  C CE1 . PHE A 99  ? 0.3936 0.4312 0.4000 -0.0010 0.0082  -0.0398 99  PHE A CE1 
752  C CE2 . PHE A 99  ? 0.4331 0.4743 0.4683 -0.0085 0.0214  -0.0429 99  PHE A CE2 
753  C CZ  . PHE A 99  ? 0.4267 0.4799 0.4527 -0.0058 0.0113  -0.0423 99  PHE A CZ  
754  N N   . ALA A 100 ? 0.3533 0.3411 0.3358 -0.0040 0.0178  -0.0454 100 ALA A N   
755  C CA  . ALA A 100 ? 0.3908 0.3904 0.3645 -0.0089 0.0131  -0.0494 100 ALA A CA  
756  C C   . ALA A 100 ? 0.3794 0.3772 0.3397 -0.0035 0.0064  -0.0391 100 ALA A C   
757  O O   . ALA A 100 ? 0.3229 0.3068 0.2788 0.0020  0.0063  -0.0325 100 ALA A O   
758  C CB  . ALA A 100 ? 0.3182 0.3161 0.2900 -0.0129 0.0178  -0.0562 100 ALA A CB  
759  N N   . ILE A 101 ? 0.3340 0.3445 0.2868 -0.0054 0.0005  -0.0377 101 ILE A N   
760  C CA  . ILE A 101 ? 0.3470 0.3526 0.2872 -0.0001 -0.0052 -0.0266 101 ILE A CA  
761  C C   . ILE A 101 ? 0.4385 0.4506 0.3645 -0.0065 -0.0075 -0.0252 101 ILE A C   
762  O O   . ILE A 101 ? 0.3775 0.4073 0.3015 -0.0129 -0.0085 -0.0322 101 ILE A O   
763  C CB  . ILE A 101 ? 0.3940 0.4097 0.3396 0.0076  -0.0103 -0.0205 101 ILE A CB  
764  C CG1 . ILE A 101 ? 0.3529 0.3609 0.3102 0.0149  -0.0053 -0.0204 101 ILE A CG1 
765  C CG2 . ILE A 101 ? 0.4342 0.4417 0.3663 0.0145  -0.0157 -0.0078 101 ILE A CG2 
766  C CD1 . ILE A 101 ? 0.3541 0.3782 0.3227 0.0236  -0.0082 -0.0150 101 ILE A CD1 
767  N N   . ALA A 102 ? 0.3751 0.3733 0.2902 -0.0067 -0.0073 -0.0175 102 ALA A N   
768  C CA  . ALA A 102 ? 0.4061 0.4103 0.3068 -0.0135 -0.0076 -0.0136 102 ALA A CA  
769  C C   . ALA A 102 ? 0.4885 0.4776 0.3762 -0.0102 -0.0120 0.0020  102 ALA A C   
770  O O   . ALA A 102 ? 0.4245 0.3929 0.3142 -0.0046 -0.0124 0.0060  102 ALA A O   
771  C CB  . ALA A 102 ? 0.4026 0.4065 0.3065 -0.0204 0.0002  -0.0199 102 ALA A CB  
772  N N   . GLU A 103 ? 0.3947 0.3923 0.2673 -0.0135 -0.0149 0.0107  103 GLU A N   
773  C CA  . GLU A 103 ? 0.4668 0.4474 0.3260 -0.0105 -0.0183 0.0280  103 GLU A CA  
774  C C   . GLU A 103 ? 0.4845 0.4657 0.3301 -0.0222 -0.0136 0.0334  103 GLU A C   
775  O O   . GLU A 103 ? 0.4405 0.4444 0.2817 -0.0294 -0.0101 0.0261  103 GLU A O   
776  C CB  . GLU A 103 ? 0.5155 0.5110 0.3669 -0.0031 -0.0269 0.0391  103 GLU A CB  
777  C CG  . GLU A 103 ? 0.5730 0.5797 0.4402 0.0082  -0.0324 0.0358  103 GLU A CG  
778  C CD  . GLU A 103 ? 0.6524 0.6659 0.5155 0.0200  -0.0415 0.0533  103 GLU A CD  
779  O OE1 . GLU A 103 ? 0.7031 0.7405 0.5798 0.0270  -0.0477 0.0515  103 GLU A OE1 
780  O OE2 . GLU A 103 ? 0.6648 0.6601 0.5129 0.0224  -0.0424 0.0700  103 GLU A OE2 
781  N N   . LEU A 104 ? 0.4312 0.3875 0.2698 -0.0250 -0.0123 0.0455  104 LEU A N   
782  C CA  . LEU A 104 ? 0.5110 0.4689 0.3373 -0.0381 -0.0066 0.0538  104 LEU A CA  
783  C C   . LEU A 104 ? 0.5078 0.4744 0.3133 -0.0366 -0.0104 0.0698  104 LEU A C   
784  O O   . LEU A 104 ? 0.4826 0.4296 0.2816 -0.0276 -0.0163 0.0853  104 LEU A O   
785  C CB  . LEU A 104 ? 0.5089 0.4354 0.3358 -0.0443 -0.0044 0.0611  104 LEU A CB  
786  C CG  . LEU A 104 ? 0.5053 0.4325 0.3234 -0.0602 0.0026  0.0711  104 LEU A CG  
787  C CD1 . LEU A 104 ? 0.5315 0.4840 0.3638 -0.0704 0.0103  0.0577  104 LEU A CD1 
788  C CD2 . LEU A 104 ? 0.6231 0.5124 0.4375 -0.0665 0.0025  0.0823  104 LEU A CD2 
789  N N   . ILE A 105 ? 0.5234 0.5192 0.3185 -0.0435 -0.0073 0.0654  105 ILE A N   
790  C CA  . ILE A 105 ? 0.4726 0.4807 0.2425 -0.0439 -0.0114 0.0820  105 ILE A CA  
791  C C   . ILE A 105 ? 0.5329 0.5401 0.2886 -0.0582 -0.0007 0.0915  105 ILE A C   
792  O O   . ILE A 105 ? 0.4456 0.4727 0.2042 -0.0675 0.0092  0.0770  105 ILE A O   
793  C CB  . ILE A 105 ? 0.4783 0.5214 0.2414 -0.0430 -0.0161 0.0696  105 ILE A CB  
794  C CG1 . ILE A 105 ? 0.4829 0.5298 0.2676 -0.0328 -0.0235 0.0561  105 ILE A CG1 
795  C CG2 . ILE A 105 ? 0.4645 0.5230 0.2002 -0.0420 -0.0239 0.0882  105 ILE A CG2 
796  C CD1 . ILE A 105 ? 0.4691 0.4992 0.2612 -0.0183 -0.0330 0.0712  105 ILE A CD1 
797  N N   . ASN A 106 ? 0.4880 0.4713 0.2314 -0.0598 -0.0011 0.1150  106 ASN A N   
798  C CA  . ASN A 106 ? 0.6025 0.5833 0.3349 -0.0760 0.0107  0.1260  106 ASN A CA  
799  C C   . ASN A 106 ? 0.6114 0.5899 0.3685 -0.0856 0.0196  0.1097  106 ASN A C   
800  O O   . ASN A 106 ? 0.6575 0.6070 0.4293 -0.0844 0.0165  0.1095  106 ASN A O   
801  C CB  . ASN A 106 ? 0.5579 0.5713 0.2639 -0.0829 0.0156  0.1306  106 ASN A CB  
802  C CG  . ASN A 106 ? 0.6440 0.6538 0.3356 -0.0987 0.0281  0.1484  106 ASN A CG  
803  O OD1 . ASN A 106 ? 0.6744 0.6517 0.3646 -0.1019 0.0280  0.1687  106 ASN A OD1 
804  N ND2 . ASN A 106 ? 0.6531 0.6949 0.3342 -0.1090 0.0403  0.1404  106 ASN A ND2 
805  N N   . THR A 107 ? 0.5901 0.5986 0.3512 -0.0944 0.0303  0.0967  107 THR A N   
806  C CA  . THR A 107 ? 0.6012 0.6136 0.3888 -0.1027 0.0384  0.0845  107 THR A CA  
807  C C   . THR A 107 ? 0.6071 0.6367 0.4149 -0.0939 0.0380  0.0600  107 THR A C   
808  O O   . THR A 107 ? 0.6931 0.7316 0.5239 -0.0984 0.0442  0.0505  107 THR A O   
809  C CB  . THR A 107 ? 0.6685 0.7020 0.4528 -0.1186 0.0537  0.0903  107 THR A CB  
810  O OG1 . THR A 107 ? 0.7503 0.8168 0.5248 -0.1161 0.0615  0.0779  107 THR A OG1 
811  C CG2 . THR A 107 ? 0.6351 0.6519 0.3967 -0.1288 0.0559  0.1168  107 THR A CG2 
812  N N   . GLU A 108 ? 0.5970 0.6320 0.3981 -0.0825 0.0309  0.0513  108 GLU A N   
813  C CA  . GLU A 108 ? 0.5715 0.6200 0.3909 -0.0757 0.0324  0.0287  108 GLU A CA  
814  C C   . GLU A 108 ? 0.5127 0.5454 0.3428 -0.0639 0.0209  0.0234  108 GLU A C   
815  O O   . GLU A 108 ? 0.4727 0.5009 0.2902 -0.0577 0.0118  0.0301  108 GLU A O   
816  C CB  . GLU A 108 ? 0.5954 0.6697 0.4002 -0.0764 0.0383  0.0167  108 GLU A CB  
817  C CG  . GLU A 108 ? 0.6910 0.7853 0.4854 -0.0869 0.0534  0.0182  108 GLU A CG  
818  C CD  . GLU A 108 ? 0.7603 0.8784 0.5473 -0.0867 0.0635  -0.0024 108 GLU A CD  
819  O OE1 . GLU A 108 ? 0.6946 0.8112 0.4884 -0.0796 0.0588  -0.0191 108 GLU A OE1 
820  O OE2 . GLU A 108 ? 0.8224 0.9592 0.5964 -0.0943 0.0774  -0.0024 108 GLU A OE2 
821  N N   . MET A 109 ? 0.5256 0.5541 0.3790 -0.0604 0.0219  0.0123  109 MET A N   
822  C CA  . MET A 109 ? 0.4710 0.4870 0.3344 -0.0499 0.0137  0.0066  109 MET A CA  
823  C C   . MET A 109 ? 0.4992 0.5328 0.3623 -0.0464 0.0147  -0.0076 109 MET A C   
824  O O   . MET A 109 ? 0.5388 0.5851 0.4105 -0.0484 0.0235  -0.0208 109 MET A O   
825  C CB  . MET A 109 ? 0.5410 0.5486 0.4257 -0.0486 0.0147  0.0010  109 MET A CB  
826  C CG  . MET A 109 ? 0.5208 0.5149 0.4134 -0.0383 0.0080  -0.0035 109 MET A CG  
827  S SD  . MET A 109 ? 0.5412 0.5082 0.4221 -0.0322 -0.0011 0.0087  109 MET A SD  
828  C CE  . MET A 109 ? 0.5370 0.4874 0.4109 -0.0442 0.0004  0.0196  109 MET A CE  
829  N N   . THR A 110 ? 0.4419 0.4772 0.2951 -0.0420 0.0061  -0.0045 110 THR A N   
830  C CA  . THR A 110 ? 0.4585 0.5125 0.3075 -0.0424 0.0046  -0.0169 110 THR A CA  
831  C C   . THR A 110 ? 0.4488 0.4989 0.3147 -0.0354 -0.0011 -0.0239 110 THR A C   
832  O O   . THR A 110 ? 0.4012 0.4426 0.2697 -0.0280 -0.0090 -0.0133 110 THR A O   
833  C CB  . THR A 110 ? 0.4456 0.5118 0.2702 -0.0441 -0.0033 -0.0047 110 THR A CB  
834  O OG1 . THR A 110 ? 0.4822 0.5477 0.2895 -0.0506 0.0021  0.0078  110 THR A OG1 
835  C CG2 . THR A 110 ? 0.4432 0.5338 0.2581 -0.0483 -0.0067 -0.0183 110 THR A CG2 
836  N N   . LEU A 111 ? 0.4358 0.4924 0.3123 -0.0376 0.0039  -0.0414 111 LEU A N   
837  C CA  . LEU A 111 ? 0.4522 0.5067 0.3455 -0.0339 0.0008  -0.0487 111 LEU A CA  
838  C C   . LEU A 111 ? 0.4814 0.5532 0.3689 -0.0343 -0.0104 -0.0462 111 LEU A C   
839  O O   . LEU A 111 ? 0.3901 0.4805 0.2624 -0.0419 -0.0129 -0.0524 111 LEU A O   
840  C CB  . LEU A 111 ? 0.4447 0.4997 0.3483 -0.0384 0.0104  -0.0679 111 LEU A CB  
841  C CG  . LEU A 111 ? 0.4745 0.5249 0.3967 -0.0372 0.0096  -0.0756 111 LEU A CG  
842  C CD1 . LEU A 111 ? 0.4289 0.4615 0.3665 -0.0286 0.0117  -0.0671 111 LEU A CD1 
843  C CD2 . LEU A 111 ? 0.5279 0.5769 0.4558 -0.0441 0.0188  -0.0957 111 LEU A CD2 
844  N N   . THR A 112 ? 0.3245 0.3935 0.2237 -0.0260 -0.0170 -0.0373 112 THR A N   
845  C CA  . THR A 112 ? 0.4295 0.5205 0.3293 -0.0245 -0.0283 -0.0328 112 THR A CA  
846  C C   . THR A 112 ? 0.4553 0.5557 0.3771 -0.0267 -0.0286 -0.0440 112 THR A C   
847  O O   . THR A 112 ? 0.4708 0.5974 0.3953 -0.0319 -0.0370 -0.0478 112 THR A O   
848  C CB  . THR A 112 ? 0.4901 0.5761 0.3861 -0.0122 -0.0355 -0.0118 112 THR A CB  
849  O OG1 . THR A 112 ? 0.4334 0.4964 0.3429 -0.0028 -0.0307 -0.0080 112 THR A OG1 
850  C CG2 . THR A 112 ? 0.4487 0.5269 0.3210 -0.0133 -0.0358 0.0007  112 THR A CG2 
851  N N   . SER A 113 ? 0.4802 0.5615 0.4176 -0.0242 -0.0197 -0.0487 113 SER A N   
852  C CA  . SER A 113 ? 0.4263 0.5134 0.3847 -0.0281 -0.0174 -0.0581 113 SER A CA  
853  C C   . SER A 113 ? 0.4317 0.4942 0.4005 -0.0271 -0.0056 -0.0632 113 SER A C   
854  O O   . SER A 113 ? 0.3741 0.4184 0.3359 -0.0224 -0.0008 -0.0591 113 SER A O   
855  C CB  . SER A 113 ? 0.4280 0.5313 0.4010 -0.0204 -0.0242 -0.0479 113 SER A CB  
856  O OG  . SER A 113 ? 0.5074 0.5937 0.4805 -0.0060 -0.0221 -0.0342 113 SER A OG  
857  N N   . GLN A 114 ? 0.4492 0.5130 0.4353 -0.0330 -0.0013 -0.0717 114 GLN A N   
858  C CA  . GLN A 114 ? 0.4732 0.5147 0.4704 -0.0315 0.0094  -0.0736 114 GLN A CA  
859  C C   . GLN A 114 ? 0.4491 0.4972 0.4664 -0.0386 0.0122  -0.0782 114 GLN A C   
860  O O   . GLN A 114 ? 0.4319 0.5039 0.4553 -0.0468 0.0055  -0.0831 114 GLN A O   
861  C CB  . GLN A 114 ? 0.5083 0.5339 0.5005 -0.0351 0.0175  -0.0839 114 GLN A CB  
862  C CG  . GLN A 114 ? 0.6075 0.6347 0.6046 -0.0482 0.0218  -0.1022 114 GLN A CG  
863  C CD  . GLN A 114 ? 0.6702 0.7078 0.6486 -0.0542 0.0196  -0.1127 114 GLN A CD  
864  O OE1 . GLN A 114 ? 0.6965 0.7566 0.6627 -0.0576 0.0091  -0.1107 114 GLN A OE1 
865  N NE2 . GLN A 114 ? 0.7344 0.7568 0.7101 -0.0548 0.0303  -0.1234 114 GLN A NE2 
866  N N   . GLY A 115 ? 0.4814 0.5105 0.5090 -0.0361 0.0217  -0.0752 115 GLY A N   
867  C CA  . GLY A 115 ? 0.4855 0.5177 0.5330 -0.0440 0.0269  -0.0775 115 GLY A CA  
868  C C   . GLY A 115 ? 0.4879 0.4930 0.5420 -0.0416 0.0388  -0.0734 115 GLY A C   
869  O O   . GLY A 115 ? 0.4646 0.4528 0.5090 -0.0311 0.0412  -0.0663 115 GLY A O   
870  N N   . LYS A 116 ? 0.5019 0.5044 0.5735 -0.0522 0.0457  -0.0769 116 LYS A N   
871  C CA  . LYS A 116 ? 0.5047 0.4809 0.5836 -0.0507 0.0576  -0.0701 116 LYS A CA  
872  C C   . LYS A 116 ? 0.5027 0.4890 0.5932 -0.0505 0.0623  -0.0577 116 LYS A C   
873  O O   . LYS A 116 ? 0.5061 0.5208 0.6042 -0.0533 0.0570  -0.0579 116 LYS A O   
874  C CB  . LYS A 116 ? 0.5197 0.4767 0.6088 -0.0643 0.0653  -0.0843 116 LYS A CB  
875  C CG  . LYS A 116 ? 0.5507 0.4983 0.6279 -0.0633 0.0638  -0.0982 116 LYS A CG  
876  C CD  . LYS A 116 ? 0.5699 0.5054 0.6356 -0.0457 0.0646  -0.0875 116 LYS A CD  
877  C CE  . LYS A 116 ? 0.6106 0.5409 0.6677 -0.0443 0.0656  -0.1005 116 LYS A CE  
878  N NZ  . LYS A 116 ? 0.6508 0.6071 0.6941 -0.0501 0.0553  -0.1095 116 LYS A NZ  
879  N N   . GLY A 117 ? 0.5917 0.4118 0.5433 -0.0737 0.0434  -0.0565 117 GLY A N   
880  C CA  . GLY A 117 ? 0.6050 0.4225 0.5692 -0.0842 0.0457  -0.0435 117 GLY A CA  
881  C C   . GLY A 117 ? 0.5897 0.4369 0.5577 -0.0775 0.0422  -0.0255 117 GLY A C   
882  O O   . GLY A 117 ? 0.5485 0.4087 0.5093 -0.0619 0.0396  -0.0191 117 GLY A O   
883  N N   . SER A 118 ? 0.5472 0.4059 0.5282 -0.0900 0.0431  -0.0187 118 SER A N   
884  C CA  . SER A 118 ? 0.5307 0.4133 0.5155 -0.0843 0.0423  -0.0036 118 SER A CA  
885  C C   . SER A 118 ? 0.5322 0.4556 0.5260 -0.0866 0.0323  -0.0070 118 SER A C   
886  O O   . SER A 118 ? 0.4961 0.4349 0.5016 -0.1002 0.0267  -0.0172 118 SER A O   
887  C CB  . SER A 118 ? 0.5678 0.4393 0.5605 -0.0935 0.0522  0.0077  118 SER A CB  
888  O OG  . SER A 118 ? 0.6334 0.5187 0.6217 -0.0836 0.0539  0.0220  118 SER A OG  
889  N N   . ASN A 119 ? 0.4841 0.4249 0.4732 -0.0733 0.0294  0.0021  119 ASN A N   
890  C CA  . ASN A 119 ? 0.4663 0.4411 0.4625 -0.0721 0.0205  0.0019  119 ASN A CA  
891  C C   . ASN A 119 ? 0.4323 0.4196 0.4291 -0.0614 0.0218  0.0142  119 ASN A C   
892  O O   . ASN A 119 ? 0.4181 0.3914 0.4040 -0.0521 0.0262  0.0210  119 ASN A O   
893  C CB  . ASN A 119 ? 0.4575 0.4381 0.4411 -0.0669 0.0132  -0.0068 119 ASN A CB  
894  C CG  . ASN A 119 ? 0.5058 0.4800 0.4856 -0.0779 0.0097  -0.0230 119 ASN A CG  
895  O OD1 . ASN A 119 ? 0.5619 0.5565 0.5504 -0.0890 0.0015  -0.0291 119 ASN A OD1 
896  N ND2 . ASN A 119 ? 0.5462 0.4928 0.5132 -0.0746 0.0153  -0.0312 119 ASN A ND2 
897  N N   . PHE A 120 ? 0.4006 0.4145 0.4104 -0.0623 0.0167  0.0162  120 PHE A N   
898  C CA  . PHE A 120 ? 0.4050 0.4302 0.4164 -0.0527 0.0173  0.0247  120 PHE A CA  
899  C C   . PHE A 120 ? 0.4059 0.4506 0.4184 -0.0486 0.0074  0.0240  120 PHE A C   
900  O O   . PHE A 120 ? 0.3658 0.4276 0.3888 -0.0548 0.0002  0.0206  120 PHE A O   
901  C CB  . PHE A 120 ? 0.4088 0.4449 0.4371 -0.0561 0.0235  0.0293  120 PHE A CB  
902  C CG  . PHE A 120 ? 0.3908 0.4386 0.4226 -0.0467 0.0236  0.0348  120 PHE A CG  
903  C CD1 . PHE A 120 ? 0.3602 0.3954 0.3776 -0.0397 0.0289  0.0387  120 PHE A CD1 
904  C CD2 . PHE A 120 ? 0.3821 0.4524 0.4314 -0.0447 0.0175  0.0358  120 PHE A CD2 
905  C CE1 . PHE A 120 ? 0.3815 0.4244 0.4020 -0.0329 0.0294  0.0410  120 PHE A CE1 
906  C CE2 . PHE A 120 ? 0.3855 0.4613 0.4390 -0.0360 0.0188  0.0403  120 PHE A CE2 
907  C CZ  . PHE A 120 ? 0.3556 0.4167 0.3947 -0.0310 0.0253  0.0415  120 PHE A CZ  
908  N N   . ILE A 121 ? 0.3610 0.4038 0.3627 -0.0391 0.0066  0.0276  121 ILE A N   
909  C CA  . ILE A 121 ? 0.3870 0.4451 0.3868 -0.0356 -0.0008 0.0293  121 ILE A CA  
910  C C   . ILE A 121 ? 0.3719 0.4363 0.3776 -0.0283 0.0001  0.0378  121 ILE A C   
911  O O   . ILE A 121 ? 0.3089 0.3630 0.3115 -0.0244 0.0057  0.0395  121 ILE A O   
912  C CB  . ILE A 121 ? 0.3744 0.4244 0.3561 -0.0333 -0.0012 0.0238  121 ILE A CB  
913  C CG1 . ILE A 121 ? 0.4304 0.4715 0.4067 -0.0414 -0.0019 0.0126  121 ILE A CG1 
914  C CG2 . ILE A 121 ? 0.3629 0.4279 0.3385 -0.0301 -0.0064 0.0274  121 ILE A CG2 
915  C CD1 . ILE A 121 ? 0.4257 0.4537 0.3870 -0.0381 0.0015  0.0054  121 ILE A CD1 
916  N N   . ALA A 122 ? 0.3501 0.4302 0.3640 -0.0266 -0.0059 0.0432  122 ALA A N   
917  C CA  . ALA A 122 ? 0.3252 0.4068 0.3458 -0.0202 -0.0043 0.0507  122 ALA A CA  
918  C C   . ALA A 122 ? 0.3801 0.4705 0.3965 -0.0175 -0.0104 0.0578  122 ALA A C   
919  O O   . ALA A 122 ? 0.3719 0.4757 0.3899 -0.0192 -0.0184 0.0605  122 ALA A O   
920  C CB  . ALA A 122 ? 0.3079 0.3961 0.3493 -0.0190 -0.0020 0.0530  122 ALA A CB  
921  N N   . PHE A 123 ? 0.3137 0.3976 0.3244 -0.0141 -0.0069 0.0616  123 PHE A N   
922  C CA  . PHE A 123 ? 0.3684 0.4574 0.3752 -0.0122 -0.0096 0.0708  123 PHE A CA  
923  C C   . PHE A 123 ? 0.4024 0.4862 0.4256 -0.0081 -0.0071 0.0776  123 PHE A C   
924  O O   . PHE A 123 ? 0.4019 0.4755 0.4291 -0.0077 -0.0010 0.0728  123 PHE A O   
925  C CB  . PHE A 123 ? 0.3603 0.4449 0.3542 -0.0127 -0.0045 0.0695  123 PHE A CB  
926  C CG  . PHE A 123 ? 0.3740 0.4615 0.3509 -0.0147 -0.0041 0.0626  123 PHE A CG  
927  C CD1 . PHE A 123 ? 0.4510 0.5416 0.4217 -0.0179 -0.0088 0.0559  123 PHE A CD1 
928  C CD2 . PHE A 123 ? 0.4122 0.4993 0.3816 -0.0139 0.0019  0.0610  123 PHE A CD2 
929  C CE1 . PHE A 123 ? 0.4523 0.5418 0.4064 -0.0199 -0.0071 0.0466  123 PHE A CE1 
930  C CE2 . PHE A 123 ? 0.4317 0.5204 0.3866 -0.0143 0.0045  0.0527  123 PHE A CE2 
931  C CZ  . PHE A 123 ? 0.4303 0.5183 0.3761 -0.0171 0.0002  0.0450  123 PHE A CZ  
932  N N   . GLY A 124 ? 0.3732 0.4632 0.4051 -0.0047 -0.0119 0.0884  124 GLY A N   
933  C CA  . GLY A 124 ? 0.4747 0.5562 0.5238 0.0004  -0.0087 0.0950  124 GLY A CA  
934  C C   . GLY A 124 ? 0.5350 0.6248 0.5946 0.0063  -0.0161 0.1094  124 GLY A C   
935  O O   . GLY A 124 ? 0.5066 0.6108 0.5558 0.0052  -0.0251 0.1149  124 GLY A O   
936  N N   . ASN A 125 ? 0.4972 0.5774 0.5764 0.0131  -0.0129 0.1156  125 ASN A N   
937  C CA  . ASN A 125 ? 0.5513 0.6398 0.6450 0.0216  -0.0209 0.1312  125 ASN A CA  
938  C C   . ASN A 125 ? 0.4840 0.5926 0.5964 0.0247  -0.0260 0.1257  125 ASN A C   
939  O O   . ASN A 125 ? 0.4012 0.5111 0.5146 0.0198  -0.0203 0.1109  125 ASN A O   
940  C CB  . ASN A 125 ? 0.5539 0.6221 0.6646 0.0290  -0.0148 0.1404  125 ASN A CB  
941  C CG  . ASN A 125 ? 0.4863 0.5420 0.6152 0.0316  -0.0040 0.1269  125 ASN A CG  
942  O OD1 . ASN A 125 ? 0.4740 0.5411 0.6200 0.0362  -0.0036 0.1208  125 ASN A OD1 
943  N ND2 . ASN A 125 ? 0.5006 0.5335 0.6263 0.0277  0.0054  0.1211  125 ASN A ND2 
944  N N   . GLU A 126 ? 0.4346 0.5601 0.5629 0.0325  -0.0369 0.1385  126 GLU A N   
945  C CA  . GLU A 126 ? 0.4611 0.6111 0.6124 0.0343  -0.0425 0.1335  126 GLU A CA  
946  C C   . GLU A 126 ? 0.4284 0.5721 0.6041 0.0375  -0.0286 0.1216  126 GLU A C   
947  O O   . GLU A 126 ? 0.3889 0.5454 0.5709 0.0314  -0.0261 0.1098  126 GLU A O   
948  C CB  . GLU A 126 ? 0.4724 0.6457 0.6413 0.0437  -0.0584 0.1504  126 GLU A CB  
949  C CG  . GLU A 126 ? 0.5596 0.7512 0.7026 0.0370  -0.0747 0.1563  126 GLU A CG  
950  C CD  . GLU A 126 ? 0.6037 0.8072 0.7300 0.0226  -0.0774 0.1389  126 GLU A CD  
951  O OE1 . GLU A 126 ? 0.6134 0.8331 0.7619 0.0192  -0.0777 0.1282  126 GLU A OE1 
952  O OE2 . GLU A 126 ? 0.6115 0.8079 0.7032 0.0145  -0.0783 0.1360  126 GLU A OE2 
953  N N   . PHE A 127 ? 0.4101 0.5316 0.5951 0.0448  -0.0180 0.1229  127 PHE A N   
954  C CA  . PHE A 127 ? 0.3943 0.5080 0.5972 0.0477  -0.0032 0.1098  127 PHE A CA  
955  C C   . PHE A 127 ? 0.4101 0.5140 0.5900 0.0357  0.0065  0.0928  127 PHE A C   
956  O O   . PHE A 127 ? 0.4080 0.5224 0.5963 0.0327  0.0129  0.0829  127 PHE A O   
957  C CB  . PHE A 127 ? 0.4415 0.5307 0.6582 0.0581  0.0057  0.1135  127 PHE A CB  
958  C CG  . PHE A 127 ? 0.3838 0.4629 0.6163 0.0619  0.0224  0.0982  127 PHE A CG  
959  C CD1 . PHE A 127 ? 0.4285 0.5247 0.6960 0.0726  0.0269  0.0973  127 PHE A CD1 
960  C CD2 . PHE A 127 ? 0.4015 0.4565 0.6139 0.0547  0.0339  0.0841  127 PHE A CD2 
961  C CE1 . PHE A 127 ? 0.3622 0.4494 0.6419 0.0761  0.0449  0.0819  127 PHE A CE1 
962  C CE2 . PHE A 127 ? 0.4050 0.4511 0.6262 0.0573  0.0496  0.0686  127 PHE A CE2 
963  C CZ  . PHE A 127 ? 0.3897 0.4507 0.6436 0.0682  0.0563  0.0673  127 PHE A CZ  
964  N N   . THR A 128 ? 0.3851 0.4701 0.5379 0.0291  0.0079  0.0906  128 THR A N   
965  C CA  . THR A 128 ? 0.4365 0.5126 0.5680 0.0199  0.0149  0.0771  128 THR A CA  
966  C C   . THR A 128 ? 0.3871 0.4790 0.5096 0.0124  0.0102  0.0734  128 THR A C   
967  O O   . THR A 128 ? 0.3860 0.4756 0.5031 0.0078  0.0178  0.0638  128 THR A O   
968  C CB  . THR A 128 ? 0.4062 0.4641 0.5166 0.0152  0.0156  0.0763  128 THR A CB  
969  O OG1 . THR A 128 ? 0.4178 0.4824 0.5145 0.0119  0.0064  0.0850  128 THR A OG1 
970  C CG2 . THR A 128 ? 0.4128 0.4519 0.5340 0.0200  0.0213  0.0780  128 THR A CG2 
971  N N   . LYS A 129 ? 0.3973 0.5042 0.5181 0.0110  -0.0017 0.0811  129 LYS A N   
972  C CA  . LYS A 129 ? 0.3963 0.5164 0.5106 0.0029  -0.0065 0.0759  129 LYS A CA  
973  C C   . LYS A 129 ? 0.4075 0.5433 0.5467 0.0022  -0.0028 0.0715  129 LYS A C   
974  O O   . LYS A 129 ? 0.3632 0.4976 0.4965 -0.0059 0.0025  0.0631  129 LYS A O   
975  C CB  . LYS A 129 ? 0.3911 0.5252 0.4973 0.0011  -0.0207 0.0831  129 LYS A CB  
976  C CG  . LYS A 129 ? 0.4101 0.5321 0.4885 -0.0011 -0.0222 0.0856  129 LYS A CG  
977  C CD  . LYS A 129 ? 0.4396 0.5766 0.5045 -0.0047 -0.0346 0.0893  129 LYS A CD  
978  C CE  . LYS A 129 ? 0.4870 0.6393 0.5645 0.0024  -0.0454 0.1041  129 LYS A CE  
979  N NZ  . LYS A 129 ? 0.5542 0.7313 0.6326 -0.0022 -0.0596 0.1030  129 LYS A NZ  
980  N N   . GLN A 130 ? 0.3954 0.5464 0.5645 0.0109  -0.0049 0.0779  130 GLN A N   
981  C CA  . GLN A 130 ? 0.3629 0.5343 0.5620 0.0105  -0.0003 0.0738  130 GLN A CA  
982  C C   . GLN A 130 ? 0.3634 0.5210 0.5623 0.0095  0.0187  0.0638  130 GLN A C   
983  O O   . GLN A 130 ? 0.3305 0.4977 0.5374 0.0022  0.0260  0.0575  130 GLN A O   
984  C CB  . GLN A 130 ? 0.3979 0.5911 0.6331 0.0227  -0.0071 0.0839  130 GLN A CB  
985  C CG  . GLN A 130 ? 0.5098 0.7336 0.7831 0.0219  -0.0045 0.0803  130 GLN A CG  
986  C CD  . GLN A 130 ? 0.5743 0.8145 0.8436 0.0056  -0.0106 0.0736  130 GLN A CD  
987  O OE1 . GLN A 130 ? 0.5188 0.7541 0.7854 -0.0045 0.0026  0.0636  130 GLN A OE1 
988  N NE2 . GLN A 130 ? 0.5795 0.8378 0.8464 0.0021  -0.0303 0.0788  130 GLN A NE2 
989  N N   . VAL A 131 ? 0.3579 0.4927 0.5454 0.0154  0.0268  0.0622  131 VAL A N   
990  C CA  . VAL A 131 ? 0.3599 0.4810 0.5412 0.0145  0.0441  0.0517  131 VAL A CA  
991  C C   . VAL A 131 ? 0.3858 0.4963 0.5364 0.0028  0.0470  0.0459  131 VAL A C   
992  O O   . VAL A 131 ? 0.3282 0.4406 0.4786 -0.0022 0.0586  0.0403  131 VAL A O   
993  C CB  . VAL A 131 ? 0.4018 0.5007 0.5781 0.0225  0.0501  0.0494  131 VAL A CB  
994  C CG1 . VAL A 131 ? 0.3641 0.4465 0.5214 0.0189  0.0653  0.0365  131 VAL A CG1 
995  C CG2 . VAL A 131 ? 0.3427 0.4489 0.5542 0.0359  0.0518  0.0543  131 VAL A CG2 
996  N N   . ALA A 132 ? 0.3987 0.4985 0.5245 -0.0012 0.0372  0.0485  132 ALA A N   
997  C CA  . ALA A 132 ? 0.3719 0.4602 0.4710 -0.0096 0.0389  0.0446  132 ALA A CA  
998  C C   . ALA A 132 ? 0.4086 0.5088 0.5149 -0.0179 0.0381  0.0442  132 ALA A C   
999  O O   . ALA A 132 ? 0.3612 0.4534 0.4565 -0.0242 0.0468  0.0411  132 ALA A O   
1000 C CB  . ALA A 132 ? 0.3356 0.4135 0.4133 -0.0101 0.0293  0.0471  132 ALA A CB  
1001 N N   . ASN A 133 ? 0.3523 0.4712 0.4763 -0.0189 0.0273  0.0477  133 ASN A N   
1002 C CA  . ASN A 133 ? 0.3856 0.5176 0.5200 -0.0290 0.0251  0.0454  133 ASN A CA  
1003 C C   . ASN A 133 ? 0.3899 0.5331 0.5475 -0.0319 0.0389  0.0427  133 ASN A C   
1004 O O   . ASN A 133 ? 0.3477 0.4877 0.5024 -0.0427 0.0456  0.0396  133 ASN A O   
1005 C CB  . ASN A 133 ? 0.4025 0.5566 0.5519 -0.0292 0.0091  0.0488  133 ASN A CB  
1006 C CG  . ASN A 133 ? 0.4420 0.6118 0.6046 -0.0419 0.0051  0.0439  133 ASN A CG  
1007 O OD1 . ASN A 133 ? 0.4701 0.6251 0.6151 -0.0520 0.0073  0.0382  133 ASN A OD1 
1008 N ND2 . ASN A 133 ? 0.4265 0.6264 0.6231 -0.0416 -0.0003 0.0459  133 ASN A ND2 
1009 N N   . LYS A 134 ? 0.3640 0.5186 0.5446 -0.0223 0.0447  0.0440  134 LYS A N   
1010 C CA  . LYS A 134 ? 0.3783 0.5452 0.5822 -0.0235 0.0609  0.0405  134 LYS A CA  
1011 C C   . LYS A 134 ? 0.3997 0.5438 0.5755 -0.0282 0.0776  0.0362  134 LYS A C   
1012 O O   . LYS A 134 ? 0.3586 0.5066 0.5385 -0.0378 0.0889  0.0347  134 LYS A O   
1013 C CB  . LYS A 134 ? 0.3538 0.5346 0.5879 -0.0095 0.0649  0.0416  134 LYS A CB  
1014 C CG  . LYS A 134 ? 0.3349 0.5387 0.6038 -0.0103 0.0808  0.0379  134 LYS A CG  
1015 C CD  . LYS A 134 ? 0.4001 0.6050 0.6886 0.0051  0.0930  0.0352  134 LYS A CD  
1016 C CE  . LYS A 134 ? 0.4342 0.6546 0.7459 0.0036  0.1160  0.0285  134 LYS A CE  
1017 N NZ  . LYS A 134 ? 0.4641 0.7038 0.8195 0.0201  0.1227  0.0275  134 LYS A NZ  
1018 N N   . CYS A 135 ? 0.3542 0.4748 0.5006 -0.0224 0.0784  0.0349  135 CYS A N   
1019 C CA  . CYS A 135 ? 0.3735 0.4735 0.4883 -0.0262 0.0904  0.0319  135 CYS A CA  
1020 C C   . CYS A 135 ? 0.4241 0.5136 0.5196 -0.0374 0.0882  0.0355  135 CYS A C   
1021 O O   . CYS A 135 ? 0.4141 0.4978 0.5000 -0.0442 0.1018  0.0359  135 CYS A O   
1022 C CB  . CYS A 135 ? 0.4117 0.4925 0.5012 -0.0192 0.0872  0.0293  135 CYS A CB  
1023 S SG  . CYS A 135 ? 0.5211 0.5817 0.5717 -0.0222 0.1006  0.0247  135 CYS A SG  
1024 N N   . PHE A 136 ? 0.3770 0.4627 0.4668 -0.0393 0.0728  0.0380  136 PHE A N   
1025 C CA  . PHE A 136 ? 0.4386 0.5105 0.5124 -0.0488 0.0717  0.0401  136 PHE A CA  
1026 C C   . PHE A 136 ? 0.4425 0.5253 0.5374 -0.0609 0.0802  0.0399  136 PHE A C   
1027 O O   . PHE A 136 ? 0.3898 0.4582 0.4710 -0.0681 0.0919  0.0427  136 PHE A O   
1028 C CB  . PHE A 136 ? 0.4079 0.4752 0.4744 -0.0482 0.0557  0.0401  136 PHE A CB  
1029 C CG  . PHE A 136 ? 0.4308 0.4766 0.4772 -0.0545 0.0561  0.0412  136 PHE A CG  
1030 C CD1 . PHE A 136 ? 0.4574 0.4819 0.4758 -0.0494 0.0575  0.0446  136 PHE A CD1 
1031 C CD2 . PHE A 136 ? 0.4123 0.4590 0.4696 -0.0656 0.0547  0.0387  136 PHE A CD2 
1032 C CE1 . PHE A 136 ? 0.4667 0.4697 0.4692 -0.0528 0.0578  0.0472  136 PHE A CE1 
1033 C CE2 . PHE A 136 ? 0.4388 0.4609 0.4791 -0.0707 0.0564  0.0395  136 PHE A CE2 
1034 C CZ  . PHE A 136 ? 0.4991 0.4988 0.5126 -0.0630 0.0582  0.0446  136 PHE A CZ  
1035 N N   . LYS A 137 ? 0.3955 0.5046 0.5241 -0.0636 0.0739  0.0376  137 LYS A N   
1036 C CA  . LYS A 137 ? 0.4306 0.5566 0.5869 -0.0769 0.0803  0.0361  137 LYS A CA  
1037 C C   . LYS A 137 ? 0.4392 0.5685 0.6025 -0.0797 0.1024  0.0374  137 LYS A C   
1038 O O   . LYS A 137 ? 0.4267 0.5545 0.5961 -0.0933 0.1135  0.0385  137 LYS A O   
1039 C CB  . LYS A 137 ? 0.4316 0.5921 0.6258 -0.0766 0.0676  0.0337  137 LYS A CB  
1040 C CG  . LYS A 137 ? 0.4333 0.5932 0.6207 -0.0812 0.0481  0.0311  137 LYS A CG  
1041 C CD  . LYS A 137 ? 0.4688 0.6662 0.6927 -0.0839 0.0345  0.0292  137 LYS A CD  
1042 C CE  . LYS A 137 ? 0.5442 0.7440 0.7544 -0.0782 0.0138  0.0295  137 LYS A CE  
1043 N NZ  . LYS A 137 ? 0.4612 0.6999 0.7040 -0.0780 -0.0021 0.0303  137 LYS A NZ  
1044 N N   . ASP A 138 ? 0.4162 0.5479 0.5768 -0.0676 0.1101  0.0366  138 ASP A N   
1045 C CA  . ASP A 138 ? 0.4504 0.5849 0.6127 -0.0688 0.1329  0.0359  138 ASP A CA  
1046 C C   . ASP A 138 ? 0.4299 0.5351 0.5508 -0.0750 0.1447  0.0404  138 ASP A C   
1047 O O   . ASP A 138 ? 0.4868 0.5948 0.6101 -0.0833 0.1641  0.0423  138 ASP A O   
1048 C CB  . ASP A 138 ? 0.4554 0.5963 0.6227 -0.0536 0.1379  0.0311  138 ASP A CB  
1049 C CG  . ASP A 138 ? 0.5707 0.7455 0.7880 -0.0469 0.1370  0.0284  138 ASP A CG  
1050 O OD1 . ASP A 138 ? 0.5987 0.7947 0.8449 -0.0526 0.1245  0.0306  138 ASP A OD1 
1051 O OD2 . ASP A 138 ? 0.5466 0.7266 0.7742 -0.0355 0.1476  0.0237  138 ASP A OD2 
1052 N N   . ASN A 139 ? 0.4566 0.5352 0.5403 -0.0706 0.1338  0.0433  139 ASN A N   
1053 C CA  . ASN A 139 ? 0.4998 0.5517 0.5431 -0.0737 0.1429  0.0497  139 ASN A CA  
1054 C C   . ASN A 139 ? 0.5319 0.5619 0.5608 -0.0823 0.1373  0.0574  139 ASN A C   
1055 O O   . ASN A 139 ? 0.5554 0.5657 0.5594 -0.0879 0.1487  0.0659  139 ASN A O   
1056 C CB  . ASN A 139 ? 0.4944 0.5336 0.5060 -0.0619 0.1374  0.0477  139 ASN A CB  
1057 C CG  . ASN A 139 ? 0.4787 0.5325 0.5004 -0.0550 0.1476  0.0390  139 ASN A CG  
1058 O OD1 . ASN A 139 ? 0.5120 0.5672 0.5246 -0.0576 0.1669  0.0376  139 ASN A OD1 
1059 N ND2 . ASN A 139 ? 0.4515 0.5156 0.4926 -0.0459 0.1365  0.0330  139 ASN A ND2 
1060 N N   . TRP A 140 ? 0.4891 0.5209 0.5327 -0.0835 0.1214  0.0547  140 TRP A N   
1061 C CA  . TRP A 140 ? 0.5227 0.5310 0.5548 -0.0907 0.1168  0.0592  140 TRP A CA  
1062 C C   . TRP A 140 ? 0.5594 0.5670 0.6092 -0.1078 0.1297  0.0617  140 TRP A C   
1063 O O   . TRP A 140 ? 0.5532 0.5882 0.6390 -0.1157 0.1325  0.0559  140 TRP A O   
1064 C CB  . TRP A 140 ? 0.5049 0.5154 0.5450 -0.0874 0.0976  0.0528  140 TRP A CB  
1065 C CG  . TRP A 140 ? 0.5568 0.5389 0.5817 -0.0916 0.0935  0.0553  140 TRP A CG  
1066 C CD1 . TRP A 140 ? 0.5345 0.5115 0.5748 -0.1044 0.0922  0.0508  140 TRP A CD1 
1067 C CD2 . TRP A 140 ? 0.5706 0.5248 0.5639 -0.0826 0.0909  0.0622  140 TRP A CD2 
1068 N NE1 . TRP A 140 ? 0.5729 0.5170 0.5924 -0.1030 0.0900  0.0537  140 TRP A NE1 
1069 C CE2 . TRP A 140 ? 0.5675 0.4983 0.5593 -0.0888 0.0892  0.0620  140 TRP A CE2 
1070 C CE3 . TRP A 140 ? 0.5744 0.5225 0.5422 -0.0698 0.0887  0.0677  140 TRP A CE3 
1071 C CZ2 . TRP A 140 ? 0.5858 0.4869 0.5535 -0.0805 0.0866  0.0688  140 TRP A CZ2 
1072 C CZ3 . TRP A 140 ? 0.6058 0.5289 0.5503 -0.0625 0.0840  0.0746  140 TRP A CZ3 
1073 C CH2 . TRP A 140 ? 0.5778 0.4777 0.5234 -0.0666 0.0833  0.0759  140 TRP A CH2 
1074 N N   . THR A 141 ? 0.5902 0.5668 0.6168 -0.1136 0.1370  0.0711  141 THR A N   
1075 C CA  . THR A 141 ? 0.6242 0.5914 0.6643 -0.1320 0.1500  0.0753  141 THR A CA  
1076 C C   . THR A 141 ? 0.6624 0.5997 0.6959 -0.1363 0.1403  0.0751  141 THR A C   
1077 O O   . THR A 141 ? 0.6369 0.5537 0.6447 -0.1232 0.1296  0.0776  141 THR A O   
1078 C CB  . THR A 141 ? 0.6065 0.5606 0.6249 -0.1364 0.1719  0.0885  141 THR A CB  
1079 O OG1 . THR A 141 ? 0.6446 0.5650 0.6195 -0.1265 0.1688  0.1002  141 THR A OG1 
1080 C CG2 . THR A 141 ? 0.5630 0.5458 0.5863 -0.1311 0.1828  0.0852  141 THR A CG2 
1081 N N   . LYS A 142 ? 0.6789 0.6146 0.7379 -0.1547 0.1444  0.0708  142 LYS A N   
1082 C CA  . LYS A 142 ? 0.7033 0.6100 0.7608 -0.1615 0.1370  0.0665  142 LYS A CA  
1083 C C   . LYS A 142 ? 0.7412 0.6018 0.7618 -0.1518 0.1384  0.0789  142 LYS A C   
1084 O O   . LYS A 142 ? 0.7754 0.6201 0.7876 -0.1433 0.1254  0.0726  142 LYS A O   
1085 C CB  . LYS A 142 ? 0.7493 0.6556 0.8371 -0.1865 0.1465  0.0622  142 LYS A CB  
1086 C CG  . LYS A 142 ? 0.7249 0.6802 0.8560 -0.1974 0.1430  0.0499  142 LYS A CG  
1087 C CD  . LYS A 142 ? 0.6731 0.6297 0.8378 -0.2249 0.1505  0.0438  142 LYS A CD  
1088 C CE  . LYS A 142 ? 0.7540 0.6726 0.9016 -0.2313 0.1649  0.0577  142 LYS A CE  
1089 N NZ  . LYS A 142 ? 0.7160 0.6336 0.8913 -0.2525 0.1645  0.0506  142 LYS A NZ  
1090 N N   . LYS A 143 ? 0.6753 0.5153 0.6740 -0.1523 0.1540  0.0966  143 LYS A N   
1091 C CA  . LYS A 143 ? 0.6760 0.4732 0.6415 -0.1417 0.1535  0.1108  143 LYS A CA  
1092 C C   . LYS A 143 ? 0.7241 0.5255 0.6583 -0.1201 0.1458  0.1189  143 LYS A C   
1093 O O   . LYS A 143 ? 0.7693 0.5411 0.6743 -0.1112 0.1473  0.1351  143 LYS A O   
1094 C CB  . LYS A 143 ? 0.7443 0.5105 0.7014 -0.1535 0.1700  0.1272  143 LYS A CB  
1095 C CG  . LYS A 143 ? 0.7089 0.4605 0.6938 -0.1717 0.1716  0.1182  143 LYS A CG  
1096 C CD  . LYS A 143 ? 0.8952 0.6069 0.8663 -0.1738 0.1778  0.1339  143 LYS A CD  
1097 C CE  . LYS A 143 ? 0.8779 0.5533 0.8587 -0.1783 0.1726  0.1254  143 LYS A CE  
1098 N NZ  . LYS A 143 ? 0.9384 0.5836 0.8950 -0.1570 0.1635  0.1299  143 LYS A NZ  
1099 N N   . SER A 144 ? 0.6353 0.4726 0.5763 -0.1114 0.1362  0.1078  144 SER A N   
1100 C CA  . SER A 144 ? 0.6784 0.5215 0.5931 -0.0932 0.1278  0.1124  144 SER A CA  
1101 C C   . SER A 144 ? 0.7161 0.5400 0.6191 -0.0787 0.1127  0.1132  144 SER A C   
1102 O O   . SER A 144 ? 0.6605 0.4794 0.5807 -0.0800 0.1056  0.1027  144 SER A O   
1103 C CB  . SER A 144 ? 0.6518 0.5335 0.5803 -0.0889 0.1221  0.0995  144 SER A CB  
1104 O OG  . SER A 144 ? 0.6720 0.5723 0.6067 -0.0969 0.1372  0.1000  144 SER A OG  
1105 N N   . ASN A 145 ? 0.6964 0.5106 0.5702 -0.0648 0.1082  0.1254  145 ASN A N   
1106 C CA  . ASN A 145 ? 0.7181 0.5176 0.5838 -0.0491 0.0947  0.1279  145 ASN A CA  
1107 C C   . ASN A 145 ? 0.6870 0.5154 0.5552 -0.0368 0.0799  0.1175  145 ASN A C   
1108 O O   . ASN A 145 ? 0.6311 0.4873 0.5082 -0.0406 0.0799  0.1076  145 ASN A O   
1109 C CB  . ASN A 145 ? 0.7417 0.5111 0.5778 -0.0409 0.0967  0.1500  145 ASN A CB  
1110 C CG  . ASN A 145 ? 0.7339 0.5146 0.5403 -0.0376 0.0985  0.1610  145 ASN A CG  
1111 O OD1 . ASN A 145 ? 0.7047 0.5126 0.5066 -0.0310 0.0895  0.1531  145 ASN A OD1 
1112 N ND2 . ASN A 145 ? 0.7773 0.5357 0.5608 -0.0432 0.1108  0.1795  145 ASN A ND2 
1113 N N   . LEU A 146 ? 0.6628 0.4841 0.5262 -0.0220 0.0685  0.1198  146 LEU A N   
1114 C CA  . LEU A 146 ? 0.6620 0.5085 0.5294 -0.0112 0.0554  0.1114  146 LEU A CA  
1115 C C   . LEU A 146 ? 0.6394 0.5038 0.4880 -0.0083 0.0523  0.1157  146 LEU A C   
1116 O O   . LEU A 146 ? 0.5522 0.4416 0.4087 -0.0073 0.0465  0.1049  146 LEU A O   
1117 C CB  . LEU A 146 ? 0.6858 0.5199 0.5541 0.0039  0.0462  0.1150  146 LEU A CB  
1118 C CG  . LEU A 146 ? 0.6768 0.5364 0.5573 0.0131  0.0349  0.1043  146 LEU A CG  
1119 C CD1 . LEU A 146 ? 0.5680 0.4351 0.4697 0.0065  0.0366  0.0878  146 LEU A CD1 
1120 C CD2 . LEU A 146 ? 0.7003 0.5531 0.5786 0.0304  0.0261  0.1124  146 LEU A CD2 
1121 N N   . GLN A 147 ? 0.6347 0.4850 0.4569 -0.0082 0.0572  0.1308  147 GLN A N   
1122 C CA  . GLN A 147 ? 0.6686 0.5345 0.4676 -0.0069 0.0550  0.1329  147 GLN A CA  
1123 C C   . GLN A 147 ? 0.6215 0.5053 0.4274 -0.0187 0.0660  0.1210  147 GLN A C   
1124 O O   . GLN A 147 ? 0.5516 0.4558 0.3545 -0.0170 0.0614  0.1115  147 GLN A O   
1125 C CB  . GLN A 147 ? 0.7059 0.5522 0.4696 -0.0036 0.0572  0.1534  147 GLN A CB  
1126 C CG  . GLN A 147 ? 0.7111 0.5740 0.4459 0.0019  0.0478  0.1552  147 GLN A CG  
1127 C CD  . GLN A 147 ? 0.7298 0.6190 0.4814 0.0085  0.0323  0.1402  147 GLN A CD  
1128 O OE1 . GLN A 147 ? 0.7490 0.6581 0.5048 0.0029  0.0334  0.1253  147 GLN A OE1 
1129 N NE2 . GLN A 147 ? 0.7559 0.6451 0.5174 0.0209  0.0183  0.1447  147 GLN A NE2 
1130 N N   . ASP A 148 ? 0.6383 0.5151 0.4574 -0.0306 0.0805  0.1205  148 ASP A N   
1131 C CA  . ASP A 148 ? 0.5839 0.4802 0.4178 -0.0403 0.0914  0.1093  148 ASP A CA  
1132 C C   . ASP A 148 ? 0.5788 0.4970 0.4407 -0.0373 0.0815  0.0936  148 ASP A C   
1133 O O   . ASP A 148 ? 0.5222 0.4592 0.3899 -0.0378 0.0835  0.0843  148 ASP A O   
1134 C CB  . ASP A 148 ? 0.5860 0.4739 0.4361 -0.0540 0.1068  0.1119  148 ASP A CB  
1135 C CG  . ASP A 148 ? 0.7089 0.5734 0.5319 -0.0592 0.1199  0.1294  148 ASP A CG  
1136 O OD1 . ASP A 148 ? 0.7478 0.6163 0.5431 -0.0583 0.1265  0.1342  148 ASP A OD1 
1137 O OD2 . ASP A 148 ? 0.6501 0.4907 0.4777 -0.0645 0.1241  0.1381  148 ASP A OD2 
1138 N N   . ALA A 149 ? 0.5542 0.4682 0.4319 -0.0340 0.0718  0.0908  149 ALA A N   
1139 C CA  . ALA A 149 ? 0.5451 0.4783 0.4446 -0.0311 0.0626  0.0786  149 ALA A CA  
1140 C C   . ALA A 149 ? 0.5069 0.4534 0.3977 -0.0226 0.0535  0.0750  149 ALA A C   
1141 O O   . ALA A 149 ? 0.4335 0.3972 0.3395 -0.0228 0.0513  0.0659  149 ALA A O   
1142 C CB  . ALA A 149 ? 0.5505 0.4748 0.4611 -0.0286 0.0554  0.0764  149 ALA A CB  
1143 N N   . VAL A 150 ? 0.4701 0.4092 0.3377 -0.0155 0.0479  0.0824  150 VAL A N   
1144 C CA  . VAL A 150 ? 0.5154 0.4685 0.3749 -0.0100 0.0386  0.0777  150 VAL A CA  
1145 C C   . VAL A 150 ? 0.5032 0.4660 0.3582 -0.0157 0.0471  0.0699  150 VAL A C   
1146 O O   . VAL A 150 ? 0.4271 0.4034 0.2967 -0.0157 0.0443  0.0594  150 VAL A O   
1147 C CB  . VAL A 150 ? 0.5852 0.5318 0.4205 -0.0018 0.0291  0.0878  150 VAL A CB  
1148 C CG1 . VAL A 150 ? 0.5367 0.4996 0.3615 0.0001  0.0201  0.0811  150 VAL A CG1 
1149 C CG2 . VAL A 150 ? 0.5560 0.4964 0.4024 0.0072  0.0203  0.0931  150 VAL A CG2 
1150 N N   . LYS A 151 ? 0.4956 0.4500 0.3320 -0.0208 0.0594  0.0750  151 LYS A N   
1151 C CA  . LYS A 151 ? 0.4929 0.4556 0.3250 -0.0257 0.0712  0.0664  151 LYS A CA  
1152 C C   . LYS A 151 ? 0.5077 0.4834 0.3752 -0.0285 0.0767  0.0564  151 LYS A C   
1153 O O   . LYS A 151 ? 0.4911 0.4764 0.3651 -0.0273 0.0783  0.0456  151 LYS A O   
1154 C CB  . LYS A 151 ? 0.5327 0.4852 0.3429 -0.0318 0.0874  0.0747  151 LYS A CB  
1155 C CG  . LYS A 151 ? 0.6281 0.5780 0.3980 -0.0310 0.0891  0.0756  151 LYS A CG  
1156 C CD  . LYS A 151 ? 0.6885 0.6281 0.4343 -0.0380 0.1081  0.0855  151 LYS A CD  
1157 C CE  . LYS A 151 ? 0.7210 0.6718 0.4752 -0.0441 0.1281  0.0735  151 LYS A CE  
1158 N NZ  . LYS A 151 ? 0.7816 0.7244 0.5154 -0.0522 0.1492  0.0840  151 LYS A NZ  
1159 N N   . ILE A 152 ? 0.4510 0.4263 0.3410 -0.0323 0.0792  0.0598  152 ILE A N   
1160 C CA  . ILE A 152 ? 0.4541 0.4447 0.3779 -0.0345 0.0817  0.0525  152 ILE A CA  
1161 C C   . ILE A 152 ? 0.4461 0.4461 0.3832 -0.0283 0.0691  0.0460  152 ILE A C   
1162 O O   . ILE A 152 ? 0.4111 0.4220 0.3645 -0.0268 0.0720  0.0391  152 ILE A O   
1163 C CB  . ILE A 152 ? 0.4743 0.4646 0.4184 -0.0413 0.0833  0.0562  152 ILE A CB  
1164 C CG1 . ILE A 152 ? 0.4963 0.4754 0.4315 -0.0502 0.0975  0.0638  152 ILE A CG1 
1165 C CG2 . ILE A 152 ? 0.4766 0.4873 0.4547 -0.0428 0.0827  0.0493  152 ILE A CG2 
1166 C CD1 . ILE A 152 ? 0.5687 0.5486 0.4871 -0.0521 0.1128  0.0647  152 ILE A CD1 
1167 N N   . LEU A 153 ? 0.4287 0.4239 0.3602 -0.0243 0.0564  0.0488  153 LEU A N   
1168 C CA  . LEU A 153 ? 0.3987 0.4028 0.3422 -0.0198 0.0463  0.0442  153 LEU A CA  
1169 C C   . LEU A 153 ? 0.4048 0.4113 0.3407 -0.0177 0.0462  0.0378  153 LEU A C   
1170 O O   . LEU A 153 ? 0.3528 0.3660 0.3049 -0.0164 0.0446  0.0328  153 LEU A O   
1171 C CB  . LEU A 153 ? 0.4311 0.4316 0.3712 -0.0161 0.0356  0.0478  153 LEU A CB  
1172 C CG  . LEU A 153 ? 0.4096 0.4126 0.3653 -0.0176 0.0328  0.0480  153 LEU A CG  
1173 C CD1 . LEU A 153 ? 0.3911 0.3911 0.3540 -0.0246 0.0404  0.0489  153 LEU A CD1 
1174 C CD2 . LEU A 153 ? 0.4017 0.3974 0.3503 -0.0130 0.0264  0.0504  153 LEU A CD2 
1175 N N   . ILE A 154 ? 0.4242 0.4240 0.3348 -0.0181 0.0486  0.0376  154 ILE A N   
1176 C CA  . ILE A 154 ? 0.4274 0.4284 0.3277 -0.0181 0.0488  0.0282  154 ILE A CA  
1177 C C   . ILE A 154 ? 0.4392 0.4428 0.3536 -0.0194 0.0620  0.0202  154 ILE A C   
1178 O O   . ILE A 154 ? 0.4006 0.4059 0.3275 -0.0181 0.0616  0.0117  154 ILE A O   
1179 C CB  . ILE A 154 ? 0.4444 0.4391 0.3090 -0.0187 0.0473  0.0302  154 ILE A CB  
1180 C CG1 . ILE A 154 ? 0.4688 0.4653 0.3264 -0.0146 0.0309  0.0366  154 ILE A CG1 
1181 C CG2 . ILE A 154 ? 0.5021 0.4967 0.3511 -0.0212 0.0519  0.0173  154 ILE A CG2 
1182 C CD1 . ILE A 154 ? 0.4550 0.4457 0.2806 -0.0129 0.0269  0.0449  154 ILE A CD1 
1183 N N   . LEU A 155 ? 0.4338 0.4378 0.3506 -0.0218 0.0745  0.0234  155 LEU A N   
1184 C CA  . LEU A 155 ? 0.4530 0.4637 0.3898 -0.0215 0.0882  0.0165  155 LEU A CA  
1185 C C   . LEU A 155 ? 0.4459 0.4661 0.4191 -0.0176 0.0825  0.0164  155 LEU A C   
1186 O O   . LEU A 155 ? 0.3814 0.4037 0.3706 -0.0137 0.0875  0.0092  155 LEU A O   
1187 C CB  . LEU A 155 ? 0.4393 0.4524 0.3757 -0.0263 0.1026  0.0216  155 LEU A CB  
1188 C CG  . LEU A 155 ? 0.4762 0.4988 0.4307 -0.0259 0.1206  0.0140  155 LEU A CG  
1189 C CD1 . LEU A 155 ? 0.4830 0.4997 0.4230 -0.0223 0.1272  0.0002  155 LEU A CD1 
1190 C CD2 . LEU A 155 ? 0.4444 0.4696 0.3943 -0.0328 0.1363  0.0197  155 LEU A CD2 
1191 N N   . CYS A 156 ? 0.3599 0.3843 0.3436 -0.0182 0.0719  0.0246  156 CYS A N   
1192 C CA  . CYS A 156 ? 0.3931 0.4273 0.4048 -0.0149 0.0649  0.0266  156 CYS A CA  
1193 C C   . CYS A 156 ? 0.4025 0.4316 0.4150 -0.0109 0.0589  0.0229  156 CYS A C   
1194 O O   . CYS A 156 ? 0.3863 0.4188 0.4204 -0.0064 0.0603  0.0218  156 CYS A O   
1195 C CB  . CYS A 156 ? 0.3786 0.4164 0.3927 -0.0173 0.0547  0.0338  156 CYS A CB  
1196 S SG  . CYS A 156 ? 0.4109 0.4555 0.4352 -0.0244 0.0604  0.0372  156 CYS A SG  
1197 N N   . MET A 157 ? 0.3696 0.3911 0.3611 -0.0124 0.0517  0.0219  157 MET A N   
1198 C CA  . MET A 157 ? 0.3979 0.4151 0.3904 -0.0117 0.0457  0.0181  157 MET A CA  
1199 C C   . MET A 157 ? 0.3929 0.4020 0.3858 -0.0111 0.0545  0.0069  157 MET A C   
1200 O O   . MET A 157 ? 0.3869 0.3912 0.3946 -0.0095 0.0537  0.0043  157 MET A O   
1201 C CB  . MET A 157 ? 0.3842 0.4002 0.3576 -0.0140 0.0360  0.0190  157 MET A CB  
1202 C CG  . MET A 157 ? 0.4447 0.4667 0.4213 -0.0130 0.0284  0.0280  157 MET A CG  
1203 S SD  . MET A 157 ? 0.4030 0.4324 0.4037 -0.0113 0.0254  0.0339  157 MET A SD  
1204 C CE  . MET A 157 ? 0.4039 0.4313 0.4088 -0.0128 0.0213  0.0313  157 MET A CE  
1205 N N   . GLU A 158 ? 0.4175 0.4234 0.3936 -0.0126 0.0641  0.0002  158 GLU A N   
1206 C CA  . GLU A 158 ? 0.4679 0.4650 0.4411 -0.0120 0.0747  -0.0136 158 GLU A CA  
1207 C C   . GLU A 158 ? 0.4498 0.4491 0.4540 -0.0055 0.0856  -0.0147 158 GLU A C   
1208 O O   . GLU A 158 ? 0.4393 0.4286 0.4551 -0.0023 0.0906  -0.0236 158 GLU A O   
1209 C CB  . GLU A 158 ? 0.4868 0.4811 0.4284 -0.0156 0.0833  -0.0200 158 GLU A CB  
1210 C CG  . GLU A 158 ? 0.4882 0.4804 0.3980 -0.0204 0.0715  -0.0198 158 GLU A CG  
1211 C CD  . GLU A 158 ? 0.5889 0.5790 0.4632 -0.0233 0.0784  -0.0211 158 GLU A CD  
1212 O OE1 . GLU A 158 ? 0.5501 0.5421 0.4255 -0.0227 0.0923  -0.0172 158 GLU A OE1 
1213 O OE2 . GLU A 158 ? 0.6312 0.6193 0.4768 -0.0267 0.0695  -0.0250 158 GLU A OE2 
1214 N N   . THR A 159 ? 0.4326 0.4449 0.4517 -0.0035 0.0894  -0.0062 159 THR A N   
1215 C CA  . THR A 159 ? 0.4658 0.4868 0.5191 0.0037  0.0979  -0.0054 159 THR A CA  
1216 C C   . THR A 159 ? 0.4403 0.4602 0.5181 0.0095  0.0876  0.0015  159 THR A C   
1217 O O   . THR A 159 ? 0.3972 0.4133 0.4985 0.0175  0.0941  -0.0015 159 THR A O   
1218 C CB  . THR A 159 ? 0.4694 0.5088 0.5354 0.0020  0.1002  0.0032  159 THR A CB  
1219 O OG1 . THR A 159 ? 0.4547 0.4918 0.4935 -0.0052 0.1078  0.0013  159 THR A OG1 
1220 C CG2 . THR A 159 ? 0.4806 0.5351 0.5849 0.0095  0.1102  0.0029  159 THR A CG2 
1221 N N   . VAL A 160 ? 0.4069 0.4290 0.4786 0.0061  0.0729  0.0113  160 VAL A N   
1222 C CA  . VAL A 160 ? 0.4331 0.4540 0.5229 0.0105  0.0639  0.0200  160 VAL A CA  
1223 C C   . VAL A 160 ? 0.4303 0.4311 0.5192 0.0111  0.0662  0.0130  160 VAL A C   
1224 O O   . VAL A 160 ? 0.3761 0.3703 0.4879 0.0184  0.0685  0.0162  160 VAL A O   
1225 C CB  . VAL A 160 ? 0.3609 0.3903 0.4437 0.0067  0.0501  0.0314  160 VAL A CB  
1226 C CG1 . VAL A 160 ? 0.3748 0.4013 0.4712 0.0105  0.0428  0.0412  160 VAL A CG1 
1227 C CG2 . VAL A 160 ? 0.3925 0.4398 0.4815 0.0057  0.0477  0.0369  160 VAL A CG2 
1228 N N   . ALA A 161 ? 0.4125 0.4031 0.4765 0.0035  0.0659  0.0028  161 ALA A N   
1229 C CA  . ALA A 161 ? 0.4588 0.4305 0.5220 0.0008  0.0671  -0.0064 161 ALA A CA  
1230 C C   . ALA A 161 ? 0.5015 0.4586 0.5765 0.0065  0.0815  -0.0192 161 ALA A C   
1231 O O   . ALA A 161 ? 0.5464 0.4846 0.6330 0.0073  0.0840  -0.0239 161 ALA A O   
1232 C CB  . ALA A 161 ? 0.4970 0.4668 0.5325 -0.0092 0.0614  -0.0151 161 ALA A CB  
1233 N N   . ARG A 162 ? 0.4672 0.4324 0.5417 0.0107  0.0925  -0.0246 162 ARG A N   
1234 C CA  . ARG A 162 ? 0.4673 0.4223 0.5558 0.0182  0.1089  -0.0373 162 ARG A CA  
1235 C C   . ARG A 162 ? 0.4326 0.3892 0.5615 0.0312  0.1107  -0.0262 162 ARG A C   
1236 O O   . ARG A 162 ? 0.5394 0.4822 0.6862 0.0395  0.1233  -0.0357 162 ARG A O   
1237 C CB  . ARG A 162 ? 0.5196 0.4881 0.5983 0.0188  0.1217  -0.0436 162 ARG A CB  
1238 C CG  . ARG A 162 ? 0.6039 0.5631 0.6447 0.0106  0.1291  -0.0611 162 ARG A CG  
1239 C CD  . ARG A 162 ? 0.6284 0.5980 0.6647 0.0131  0.1476  -0.0675 162 ARG A CD  
1240 N NE  . ARG A 162 ? 0.6608 0.6522 0.6992 0.0111  0.1447  -0.0520 162 ARG A NE  
1241 C CZ  . ARG A 162 ? 0.6654 0.6607 0.6706 0.0023  0.1410  -0.0481 162 ARG A CZ  
1242 N NH1 . ARG A 162 ? 0.7046 0.6878 0.6714 -0.0046 0.1373  -0.0572 162 ARG A NH1 
1243 N NH2 . ARG A 162 ? 0.5634 0.5746 0.5744 0.0001  0.1399  -0.0347 162 ARG A NH2 
1244 N N   . LYS A 163 ? 0.4153 0.3896 0.5583 0.0338  0.0988  -0.0071 163 LYS A N   
1245 C CA  . LYS A 163 ? 0.4626 0.4442 0.6423 0.0467  0.0976  0.0059  163 LYS A CA  
1246 C C   . LYS A 163 ? 0.4347 0.4037 0.6245 0.0494  0.0865  0.0203  163 LYS A C   
1247 O O   . LYS A 163 ? 0.4664 0.4369 0.6860 0.0619  0.0855  0.0319  163 LYS A O   
1248 C CB  . LYS A 163 ? 0.4639 0.4769 0.6541 0.0479  0.0919  0.0170  163 LYS A CB  
1249 C CG  . LYS A 163 ? 0.4698 0.4964 0.6656 0.0490  0.1071  0.0061  163 LYS A CG  
1250 C CD  . LYS A 163 ? 0.4544 0.5106 0.6564 0.0448  0.1008  0.0155  163 LYS A CD  
1251 C CE  . LYS A 163 ? 0.4757 0.5532 0.7085 0.0513  0.1147  0.0118  163 LYS A CE  
1252 N NZ  . LYS A 163 ? 0.5015 0.5793 0.7127 0.0428  0.1310  -0.0009 163 LYS A NZ  
1253 N N   . THR A 164 ? 0.4154 0.3739 0.5818 0.0381  0.0782  0.0214  164 THR A N   
1254 C CA  . THR A 164 ? 0.4565 0.4040 0.6302 0.0385  0.0696  0.0366  164 THR A CA  
1255 C C   . THR A 164 ? 0.4584 0.3865 0.6136 0.0259  0.0684  0.0294  164 THR A C   
1256 O O   . THR A 164 ? 0.4634 0.3965 0.5947 0.0153  0.0668  0.0180  164 THR A O   
1257 C CB  . THR A 164 ? 0.4593 0.4306 0.6317 0.0389  0.0557  0.0559  164 THR A CB  
1258 O OG1 . THR A 164 ? 0.4407 0.4011 0.6158 0.0388  0.0490  0.0718  164 THR A OG1 
1259 C CG2 . THR A 164 ? 0.4348 0.4222 0.5805 0.0279  0.0500  0.0516  164 THR A CG2 
1260 N N   . ALA A 165 ? 0.4335 0.3401 0.6016 0.0269  0.0685  0.0376  165 ALA A N   
1261 C CA  . ALA A 165 ? 0.4723 0.3618 0.6297 0.0134  0.0673  0.0330  165 ALA A CA  
1262 C C   . ALA A 165 ? 0.4617 0.3665 0.6089 0.0063  0.0560  0.0504  165 ALA A C   
1263 O O   . ALA A 165 ? 0.4378 0.3343 0.5793 -0.0056 0.0549  0.0489  165 ALA A O   
1264 C CB  . ALA A 165 ? 0.4965 0.3516 0.6737 0.0160  0.0755  0.0322  165 ALA A CB  
1265 N N   . SER A 166 ? 0.4357 0.3645 0.5807 0.0126  0.0485  0.0648  166 SER A N   
1266 C CA  . SER A 166 ? 0.4948 0.4396 0.6265 0.0066  0.0397  0.0781  166 SER A CA  
1267 C C   . SER A 166 ? 0.5361 0.4974 0.6465 -0.0027 0.0363  0.0662  166 SER A C   
1268 O O   . SER A 166 ? 0.5764 0.5499 0.6761 -0.0082 0.0311  0.0732  166 SER A O   
1269 C CB  . SER A 166 ? 0.5258 0.4886 0.6614 0.0162  0.0323  0.0957  166 SER A CB  
1270 O OG  . SER A 166 ? 0.5174 0.4997 0.6505 0.0199  0.0304  0.0879  166 SER A OG  
1271 N N   . VAL A 167 ? 0.4343 0.3961 0.5383 -0.0034 0.0399  0.0491  167 VAL A N   
1272 C CA  . VAL A 167 ? 0.4561 0.4301 0.5402 -0.0104 0.0365  0.0388  167 VAL A CA  
1273 C C   . VAL A 167 ? 0.4625 0.4228 0.5408 -0.0178 0.0405  0.0207  167 VAL A C   
1274 O O   . VAL A 167 ? 0.5256 0.4676 0.6133 -0.0156 0.0481  0.0126  167 VAL A O   
1275 C CB  . VAL A 167 ? 0.4396 0.4281 0.5176 -0.0045 0.0365  0.0376  167 VAL A CB  
1276 C CG1 . VAL A 167 ? 0.4690 0.4660 0.5258 -0.0099 0.0340  0.0289  167 VAL A CG1 
1277 C CG2 . VAL A 167 ? 0.4363 0.4394 0.5202 0.0006  0.0308  0.0528  167 VAL A CG2 
1278 N N   . SER A 168 ? 0.4953 0.4644 0.5590 -0.0264 0.0348  0.0139  168 SER A N   
1279 C CA  . SER A 168 ? 0.4817 0.4427 0.5366 -0.0346 0.0353  -0.0039 168 SER A CA  
1280 C C   . SER A 168 ? 0.5051 0.4715 0.5395 -0.0316 0.0368  -0.0140 168 SER A C   
1281 O O   . SER A 168 ? 0.4561 0.4353 0.4832 -0.0260 0.0353  -0.0060 168 SER A O   
1282 C CB  . SER A 168 ? 0.4405 0.4135 0.4926 -0.0449 0.0265  -0.0049 168 SER A CB  
1283 O OG  . SER A 168 ? 0.4435 0.4377 0.4852 -0.0414 0.0199  0.0028  168 SER A OG  
1284 N N   . LYS A 169 ? 0.5223 0.4784 0.5452 -0.0366 0.0399  -0.0317 169 LYS A N   
1285 C CA  . LYS A 169 ? 0.5007 0.4613 0.4984 -0.0353 0.0421  -0.0410 169 LYS A CA  
1286 C C   . LYS A 169 ? 0.4484 0.4278 0.4282 -0.0385 0.0298  -0.0360 169 LYS A C   
1287 O O   . LYS A 169 ? 0.4237 0.4108 0.3879 -0.0339 0.0304  -0.0310 169 LYS A O   
1288 C CB  . LYS A 169 ? 0.5321 0.4767 0.5179 -0.0413 0.0479  -0.0630 169 LYS A CB  
1289 C CG  . LYS A 169 ? 0.5860 0.5099 0.5884 -0.0350 0.0632  -0.0701 169 LYS A CG  
1290 C CD  . LYS A 169 ? 0.6047 0.5222 0.6400 -0.0287 0.0647  -0.0545 169 LYS A CD  
1291 C CE  . LYS A 169 ? 0.7115 0.6134 0.7613 -0.0374 0.0615  -0.0569 169 LYS A CE  
1292 N NZ  . LYS A 169 ? 0.6889 0.5772 0.7678 -0.0293 0.0668  -0.0427 169 LYS A NZ  
1293 N N   . GLN A 170 ? 0.4329 0.4201 0.4184 -0.0459 0.0194  -0.0360 170 GLN A N   
1294 C CA  . GLN A 170 ? 0.4366 0.4436 0.4116 -0.0468 0.0071  -0.0304 170 GLN A CA  
1295 C C   . GLN A 170 ? 0.4171 0.4341 0.4006 -0.0390 0.0065  -0.0130 170 GLN A C   
1296 O O   . GLN A 170 ? 0.3903 0.4045 0.3927 -0.0373 0.0105  -0.0049 170 GLN A O   
1297 C CB  . GLN A 170 ? 0.5268 0.5433 0.5143 -0.0570 -0.0026 -0.0352 170 GLN A CB  
1298 C CG  . GLN A 170 ? 0.6188 0.6247 0.6021 -0.0682 -0.0033 -0.0550 170 GLN A CG  
1299 C CD  . GLN A 170 ? 0.6100 0.5975 0.6184 -0.0745 0.0045  -0.0582 170 GLN A CD  
1300 O OE1 . GLN A 170 ? 0.5838 0.5523 0.6000 -0.0682 0.0164  -0.0550 170 GLN A OE1 
1301 N NE2 . GLN A 170 ? 0.6038 0.5970 0.6273 -0.0873 -0.0021 -0.0641 170 GLN A NE2 
1302 N N   . PHE A 171 ? 0.3549 0.3826 0.3233 -0.0345 0.0008  -0.0072 171 PHE A N   
1303 C CA  . PHE A 171 ? 0.3415 0.3765 0.3159 -0.0278 0.0003  0.0062  171 PHE A CA  
1304 C C   . PHE A 171 ? 0.3934 0.4412 0.3576 -0.0245 -0.0093 0.0106  171 PHE A C   
1305 O O   . PHE A 171 ? 0.3247 0.3766 0.2738 -0.0265 -0.0164 0.0052  171 PHE A O   
1306 C CB  . PHE A 171 ? 0.3686 0.3948 0.3400 -0.0225 0.0096  0.0111  171 PHE A CB  
1307 C CG  . PHE A 171 ? 0.4145 0.4358 0.3633 -0.0211 0.0128  0.0084  171 PHE A CG  
1308 C CD1 . PHE A 171 ? 0.4235 0.4358 0.3628 -0.0237 0.0201  -0.0020 171 PHE A CD1 
1309 C CD2 . PHE A 171 ? 0.3861 0.4099 0.3225 -0.0171 0.0103  0.0167  171 PHE A CD2 
1310 C CE1 . PHE A 171 ? 0.4305 0.4392 0.3456 -0.0231 0.0251  -0.0036 171 PHE A CE1 
1311 C CE2 . PHE A 171 ? 0.4053 0.4227 0.3192 -0.0167 0.0149  0.0169  171 PHE A CE2 
1312 C CZ  . PHE A 171 ? 0.4381 0.4494 0.3403 -0.0200 0.0224  0.0071  171 PHE A CZ  
1313 N N   . MET A 172 ? 0.3424 0.3964 0.3142 -0.0189 -0.0100 0.0202  172 MET A N   
1314 C CA  . MET A 172 ? 0.3524 0.4162 0.3190 -0.0129 -0.0176 0.0256  172 MET A CA  
1315 C C   . MET A 172 ? 0.3498 0.4037 0.3063 -0.0061 -0.0131 0.0333  172 MET A C   
1316 O O   . MET A 172 ? 0.3221 0.3694 0.2845 -0.0063 -0.0058 0.0351  172 MET A O   
1317 C CB  . MET A 172 ? 0.3980 0.4775 0.3859 -0.0117 -0.0204 0.0285  172 MET A CB  
1318 C CG  . MET A 172 ? 0.4819 0.5778 0.4814 -0.0175 -0.0285 0.0229  172 MET A CG  
1319 S SD  . MET A 172 ? 0.6383 0.7543 0.6663 -0.0169 -0.0267 0.0272  172 MET A SD  
1320 C CE  . MET A 172 ? 0.4247 0.5514 0.4509 -0.0028 -0.0327 0.0335  172 MET A CE  
1321 N N   . ILE A 173 ? 0.3208 0.3750 0.2653 0.0001  -0.0187 0.0385  173 ILE A N   
1322 C CA  . ILE A 173 ? 0.3828 0.4245 0.3196 0.0058  -0.0142 0.0461  173 ILE A CA  
1323 C C   . ILE A 173 ? 0.4200 0.4668 0.3602 0.0155  -0.0210 0.0526  173 ILE A C   
1324 O O   . ILE A 173 ? 0.3768 0.4344 0.3138 0.0191  -0.0311 0.0544  173 ILE A O   
1325 C CB  . ILE A 173 ? 0.4188 0.4458 0.3333 0.0035  -0.0088 0.0479  173 ILE A CB  
1326 C CG1 . ILE A 173 ? 0.4592 0.4720 0.3731 0.0039  0.0002  0.0529  173 ILE A CG1 
1327 C CG2 . ILE A 173 ? 0.4871 0.5143 0.3802 0.0071  -0.0168 0.0527  173 ILE A CG2 
1328 C CD1 . ILE A 173 ? 0.4756 0.4803 0.3801 -0.0024 0.0100  0.0509  173 ILE A CD1 
1329 N N   . VAL A 174 ? 0.3976 0.4394 0.3474 0.0199  -0.0161 0.0548  174 VAL A N   
1330 C CA  . VAL A 174 ? 0.3651 0.4075 0.3209 0.0311  -0.0194 0.0600  174 VAL A CA  
1331 C C   . VAL A 174 ? 0.4142 0.4320 0.3591 0.0337  -0.0126 0.0648  174 VAL A C   
1332 O O   . VAL A 174 ? 0.3326 0.3402 0.2750 0.0261  -0.0047 0.0614  174 VAL A O   
1333 C CB  . VAL A 174 ? 0.4246 0.4823 0.4026 0.0338  -0.0174 0.0555  174 VAL A CB  
1334 C CG1 . VAL A 174 ? 0.3639 0.4474 0.3572 0.0313  -0.0241 0.0523  174 VAL A CG1 
1335 C CG2 . VAL A 174 ? 0.3609 0.4124 0.3408 0.0268  -0.0080 0.0505  174 VAL A CG2 
1336 N N   . GLN A 175 ? 0.4605 0.4685 0.4010 0.0443  -0.0158 0.0731  175 GLN A N   
1337 C CA  . GLN A 175 ? 0.4571 0.4374 0.3887 0.0460  -0.0086 0.0780  175 GLN A CA  
1338 C C   . GLN A 175 ? 0.4945 0.4659 0.4344 0.0604  -0.0100 0.0830  175 GLN A C   
1339 O O   . GLN A 175 ? 0.4550 0.4432 0.4048 0.0711  -0.0186 0.0864  175 GLN A O   
1340 C CB  . GLN A 175 ? 0.4719 0.4364 0.3804 0.0409  -0.0067 0.0863  175 GLN A CB  
1341 C CG  . GLN A 175 ? 0.5619 0.5269 0.4556 0.0498  -0.0164 0.0984  175 GLN A CG  
1342 C CD  . GLN A 175 ? 0.6023 0.5499 0.4690 0.0433  -0.0113 0.1069  175 GLN A CD  
1343 O OE1 . GLN A 175 ? 0.6415 0.5634 0.4995 0.0440  -0.0041 0.1161  175 GLN A OE1 
1344 N NE2 . GLN A 175 ? 0.5663 0.5269 0.4195 0.0360  -0.0133 0.1031  175 GLN A NE2 
1345 N N   . THR A 176 ? 0.4591 0.4051 0.3982 0.0605  -0.0011 0.0818  176 THR A N   
1346 C CA  . THR A 176 ? 0.5227 0.4539 0.4706 0.0748  0.0002  0.0849  176 THR A CA  
1347 C C   . THR A 176 ? 0.4921 0.3850 0.4293 0.0727  0.0084  0.0897  176 THR A C   
1348 O O   . THR A 176 ? 0.5100 0.3919 0.4396 0.0580  0.0154  0.0851  176 THR A O   
1349 C CB  . THR A 176 ? 0.5291 0.4732 0.4965 0.0783  0.0048  0.0712  176 THR A CB  
1350 O OG1 . THR A 176 ? 0.5469 0.4801 0.5260 0.0955  0.0061  0.0739  176 THR A OG1 
1351 C CG2 . THR A 176 ? 0.4628 0.3965 0.4268 0.0651  0.0143  0.0584  176 THR A CG2 
1352 N N   . ALA A 177 ? 0.5259 0.3991 0.4652 0.0877  0.0075  0.0996  177 ALA A N   
1353 C CA  . ALA A 177 ? 0.5433 0.3745 0.4760 0.0879  0.0163  0.1051  177 ALA A CA  
1354 C C   . ALA A 177 ? 0.5852 0.4006 0.5352 0.0962  0.0240  0.0923  177 ALA A C   
1355 O O   . ALA A 177 ? 0.6412 0.4190 0.5889 0.0946  0.0329  0.0918  177 ALA A O   
1356 C CB  . ALA A 177 ? 0.5894 0.4036 0.5101 0.1004  0.0104  0.1276  177 ALA A CB  
1357 N N   . SER A 178 ? 0.5325 0.3755 0.4997 0.1050  0.0218  0.0818  178 SER A N   
1358 C CA  . SER A 178 ? 0.6108 0.4456 0.5939 0.1146  0.0302  0.0680  178 SER A CA  
1359 C C   . SER A 178 ? 0.5959 0.4171 0.5728 0.0978  0.0404  0.0489  178 SER A C   
1360 O O   . SER A 178 ? 0.5654 0.4028 0.5337 0.0807  0.0387  0.0438  178 SER A O   
1361 C CB  . SER A 178 ? 0.5843 0.4599 0.5862 0.1247  0.0262  0.0625  178 SER A CB  
1362 O OG  . SER A 178 ? 0.6140 0.4955 0.6246 0.1237  0.0366  0.0429  178 SER A OG  
1363 N N   . ASN A 179 ? 0.5956 0.3879 0.5777 0.1035  0.0504  0.0377  179 ASN A N   
1364 C CA  . ASN A 179 ? 0.6374 0.4190 0.6129 0.0878  0.0586  0.0167  179 ASN A CA  
1365 C C   . ASN A 179 ? 0.6859 0.4846 0.6699 0.0954  0.0651  -0.0018 179 ASN A C   
1366 O O   . ASN A 179 ? 0.7290 0.5081 0.7082 0.0900  0.0741  -0.0208 179 ASN A O   
1367 C CB  . ASN A 179 ? 0.7008 0.4331 0.6710 0.0817  0.0665  0.0137  179 ASN A CB  
1368 C CG  . ASN A 179 ? 0.7894 0.4874 0.7707 0.1016  0.0742  0.0135  179 ASN A CG  
1369 O OD1 . ASN A 179 ? 0.7793 0.4920 0.7750 0.1230  0.0736  0.0165  179 ASN A OD1 
1370 N ND2 . ASN A 179 ? 0.8869 0.5379 0.8644 0.0949  0.0823  0.0098  179 ASN A ND2 
1371 N N   . ALA A 180 ? 0.6219 0.4575 0.6179 0.1067  0.0611  0.0027  180 ALA A N   
1372 C CA  . ALA A 180 ? 0.6434 0.4999 0.6480 0.1134  0.0692  -0.0131 180 ALA A CA  
1373 C C   . ALA A 180 ? 0.6337 0.4992 0.6206 0.0938  0.0726  -0.0299 180 ALA A C   
1374 O O   . ALA A 180 ? 0.5708 0.4455 0.5461 0.0771  0.0648  -0.0251 180 ALA A O   
1375 C CB  . ALA A 180 ? 0.6120 0.5109 0.6336 0.1234  0.0633  -0.0032 180 ALA A CB  
1376 N N   . ASP A 181 ? 0.6325 0.4932 0.6163 0.0962  0.0844  -0.0499 181 ASP A N   
1377 C CA  . ASP A 181 ? 0.6356 0.5042 0.5988 0.0785  0.0866  -0.0663 181 ASP A CA  
1378 C C   . ASP A 181 ? 0.5809 0.4936 0.5427 0.0734  0.0821  -0.0598 181 ASP A C   
1379 O O   . ASP A 181 ? 0.5977 0.5343 0.5727 0.0851  0.0875  -0.0583 181 ASP A O   
1380 C CB  . ASP A 181 ? 0.6775 0.5287 0.6344 0.0835  0.1015  -0.0907 181 ASP A CB  
1381 C CG  . ASP A 181 ? 0.7130 0.5790 0.6454 0.0677  0.1041  -0.1083 181 ASP A CG  
1382 O OD1 . ASP A 181 ? 0.6626 0.5371 0.5810 0.0494  0.0930  -0.1048 181 ASP A OD1 
1383 O OD2 . ASP A 181 ? 0.7755 0.6458 0.7022 0.0742  0.1173  -0.1255 181 ASP A OD2 
1384 N N   . VAL A 182 ? 0.5788 0.5023 0.5282 0.0562  0.0723  -0.0544 182 VAL A N   
1385 C CA  . VAL A 182 ? 0.5292 0.4887 0.4768 0.0505  0.0680  -0.0470 182 VAL A CA  
1386 C C   . VAL A 182 ? 0.5707 0.5461 0.5048 0.0482  0.0774  -0.0609 182 VAL A C   
1387 O O   . VAL A 182 ? 0.5329 0.5368 0.4718 0.0500  0.0797  -0.0545 182 VAL A O   
1388 C CB  . VAL A 182 ? 0.4999 0.4650 0.4394 0.0348  0.0560  -0.0378 182 VAL A CB  
1389 C CG1 . VAL A 182 ? 0.4663 0.4207 0.4168 0.0370  0.0489  -0.0232 182 VAL A CG1 
1390 C CG2 . VAL A 182 ? 0.4813 0.4336 0.4027 0.0204  0.0544  -0.0511 182 VAL A CG2 
1391 N N   . LEU A 183 ? 0.5962 0.5528 0.5119 0.0429  0.0832  -0.0800 183 LEU A N   
1392 C CA  . LEU A 183 ? 0.6168 0.5868 0.5123 0.0395  0.0925  -0.0950 183 LEU A CA  
1393 C C   . LEU A 183 ? 0.6229 0.6093 0.5316 0.0551  0.1075  -0.0971 183 LEU A C   
1394 O O   . LEU A 183 ? 0.5683 0.5791 0.4650 0.0520  0.1145  -0.0992 183 LEU A O   
1395 C CB  . LEU A 183 ? 0.6368 0.5807 0.5098 0.0309  0.0957  -0.1184 183 LEU A CB  
1396 C CG  . LEU A 183 ? 0.7219 0.6672 0.5729 0.0101  0.0822  -0.1221 183 LEU A CG  
1397 C CD1 . LEU A 183 ? 0.5816 0.5570 0.4333 0.0026  0.0692  -0.1012 183 LEU A CD1 
1398 C CD2 . LEU A 183 ? 0.7248 0.6376 0.5807 0.0025  0.0766  -0.1288 183 LEU A CD2 
1399 N N   . LYS A 184 ? 0.6528 0.6285 0.5881 0.0720  0.1118  -0.0939 184 LYS A N   
1400 C CA  . LYS A 184 ? 0.5518 0.5464 0.5100 0.0893  0.1247  -0.0940 184 LYS A CA  
1401 C C   . LYS A 184 ? 0.5678 0.6023 0.5380 0.0860  0.1206  -0.0767 184 LYS A C   
1402 O O   . LYS A 184 ? 0.5293 0.5899 0.5027 0.0885  0.1332  -0.0800 184 LYS A O   
1403 C CB  . LYS A 184 ? 0.6392 0.6142 0.6259 0.1078  0.1237  -0.0884 184 LYS A CB  
1404 C CG  . LYS A 184 ? 0.7619 0.7362 0.7676 0.1283  0.1414  -0.1010 184 LYS A CG  
1405 C CD  . LYS A 184 ? 0.8294 0.7961 0.8699 0.1494  0.1373  -0.0882 184 LYS A CD  
1406 C CE  . LYS A 184 ? 0.9318 0.8548 0.9764 0.1636  0.1463  -0.1007 184 LYS A CE  
1407 N NZ  . LYS A 184 ? 0.9321 0.8455 1.0072 0.1839  0.1386  -0.0830 184 LYS A NZ  
1408 N N   . VAL A 185 ? 0.5094 0.5473 0.4855 0.0792  0.1043  -0.0591 185 VAL A N   
1409 C CA  . VAL A 185 ? 0.4745 0.5438 0.4626 0.0741  0.0985  -0.0431 185 VAL A CA  
1410 C C   . VAL A 185 ? 0.5180 0.6030 0.4830 0.0594  0.1014  -0.0433 185 VAL A C   
1411 O O   . VAL A 185 ? 0.5158 0.6284 0.4897 0.0584  0.1086  -0.0378 185 VAL A O   
1412 C CB  . VAL A 185 ? 0.4751 0.5380 0.4714 0.0708  0.0813  -0.0276 185 VAL A CB  
1413 C CG1 . VAL A 185 ? 0.4861 0.5783 0.4962 0.0654  0.0758  -0.0139 185 VAL A CG1 
1414 C CG2 . VAL A 185 ? 0.4693 0.5154 0.4836 0.0860  0.0782  -0.0252 185 VAL A CG2 
1415 N N   . VAL A 186 ? 0.5015 0.5700 0.4378 0.0478  0.0959  -0.0491 186 VAL A N   
1416 C CA  . VAL A 186 ? 0.5417 0.6232 0.4516 0.0348  0.0964  -0.0483 186 VAL A CA  
1417 C C   . VAL A 186 ? 0.5767 0.6720 0.4756 0.0384  0.1153  -0.0599 186 VAL A C   
1418 O O   . VAL A 186 ? 0.5461 0.6632 0.4356 0.0320  0.1203  -0.0520 186 VAL A O   
1419 C CB  . VAL A 186 ? 0.5413 0.6050 0.4248 0.0232  0.0861  -0.0552 186 VAL A CB  
1420 C CG1 . VAL A 186 ? 0.5106 0.5914 0.3707 0.0108  0.0811  -0.0474 186 VAL A CG1 
1421 C CG2 . VAL A 186 ? 0.4841 0.5307 0.3808 0.0214  0.0722  -0.0481 186 VAL A CG2 
1422 N N   . GLU A 187 ? 0.5599 0.6414 0.4609 0.0493  0.1271  -0.0779 187 GLU A N   
1423 C CA  . GLU A 187 ? 0.6277 0.7216 0.5200 0.0548  0.1482  -0.0917 187 GLU A CA  
1424 C C   . GLU A 187 ? 0.6360 0.7623 0.5582 0.0617  0.1586  -0.0799 187 GLU A C   
1425 O O   . GLU A 187 ? 0.6733 0.8219 0.5826 0.0557  0.1705  -0.0779 187 GLU A O   
1426 C CB  . GLU A 187 ? 0.6548 0.7235 0.5486 0.0670  0.1592  -0.1144 187 GLU A CB  
1427 C CG  . GLU A 187 ? 0.7618 0.8360 0.6307 0.0681  0.1804  -0.1350 187 GLU A CG  
1428 C CD  . GLU A 187 ? 0.8729 0.9567 0.6964 0.0502  0.1781  -0.1365 187 GLU A CD  
1429 O OE1 . GLU A 187 ? 0.9457 1.0104 0.7441 0.0387  0.1637  -0.1423 187 GLU A OE1 
1430 O OE2 . GLU A 187 ? 0.9035 1.0149 0.7175 0.0476  0.1906  -0.1310 187 GLU A OE2 
1431 N N   . LYS A 188 ? 0.5563 0.6864 0.5170 0.0723  0.1529  -0.0707 188 LYS A N   
1432 C CA  . LYS A 188 ? 0.5634 0.7267 0.5593 0.0776  0.1588  -0.0594 188 LYS A CA  
1433 C C   . LYS A 188 ? 0.6252 0.8095 0.6136 0.0610  0.1550  -0.0429 188 LYS A C   
1434 O O   . LYS A 188 ? 0.6323 0.8446 0.6317 0.0590  0.1691  -0.0391 188 LYS A O   
1435 C CB  . LYS A 188 ? 0.6027 0.7632 0.6348 0.0890  0.1457  -0.0508 188 LYS A CB  
1436 C CG  . LYS A 188 ? 0.5824 0.7788 0.6531 0.0914  0.1450  -0.0380 188 LYS A CG  
1437 C CD  . LYS A 188 ? 0.5946 0.8157 0.6958 0.1067  0.1639  -0.0465 188 LYS A CD  
1438 C CE  . LYS A 188 ? 0.5994 0.8634 0.7332 0.1019  0.1685  -0.0360 188 LYS A CE  
1439 N NZ  . LYS A 188 ? 0.4946 0.7815 0.6255 0.0997  0.1943  -0.0440 188 LYS A NZ  
1440 N N   . ASP A 189 ? 0.5891 0.7588 0.5594 0.0492  0.1376  -0.0332 189 ASP A N   
1441 C CA  . ASP A 189 ? 0.6163 0.7991 0.5789 0.0350  0.1333  -0.0171 189 ASP A CA  
1442 C C   . ASP A 189 ? 0.6493 0.8372 0.5751 0.0257  0.1441  -0.0187 189 ASP A C   
1443 O O   . ASP A 189 ? 0.6688 0.8732 0.5934 0.0165  0.1485  -0.0048 189 ASP A O   
1444 C CB  . ASP A 189 ? 0.5170 0.6823 0.4747 0.0278  0.1120  -0.0069 189 ASP A CB  
1445 C CG  . ASP A 189 ? 0.5614 0.7253 0.5506 0.0336  0.1006  -0.0011 189 ASP A CG  
1446 O OD1 . ASP A 189 ? 0.6009 0.7809 0.6190 0.0428  0.1065  -0.0025 189 ASP A OD1 
1447 O OD2 . ASP A 189 ? 0.5087 0.6572 0.4936 0.0292  0.0856  0.0049  189 ASP A OD2 
1448 N N   . ARG A 190 ? 0.6540 0.8266 0.5484 0.0268  0.1477  -0.0350 190 ARG A N   
1449 C CA  . ARG A 190 ? 0.7899 0.9663 0.6414 0.0176  0.1553  -0.0380 190 ARG A CA  
1450 C C   . ARG A 190 ? 0.8706 1.0741 0.7212 0.0136  0.1740  -0.0285 190 ARG A C   
1451 O O   . ARG A 190 ? 0.7944 1.0039 0.6216 0.0022  0.1716  -0.0134 190 ARG A O   
1452 C CB  . ARG A 190 ? 0.8131 0.9734 0.6374 0.0217  0.1621  -0.0631 190 ARG A CB  
1453 C CG  . ARG A 190 ? 0.8913 1.0528 0.6648 0.0100  0.1625  -0.0665 190 ARG A CG  
1454 C CD  . ARG A 190 ? 0.8950 1.0383 0.6405 0.0118  0.1672  -0.0944 190 ARG A CD  
1455 N NE  . ARG A 190 ? 0.9451 1.0796 0.7188 0.0270  0.1819  -0.1115 190 ARG A NE  
1456 C CZ  . ARG A 190 ? 0.9615 1.1073 0.7349 0.0354  0.2069  -0.1248 190 ARG A CZ  
1457 N NH1 . ARG A 190 ? 0.9200 1.0869 0.6633 0.0283  0.2214  -0.1227 190 ARG A NH1 
1458 N NH2 . ARG A 190 ? 0.9063 1.0430 0.7101 0.0515  0.2184  -0.1392 190 ARG A NH2 
1459 N N   . ASN A 191 ? 1.0279 1.2486 0.9076 0.0231  0.1923  -0.0350 191 ASN A N   
1460 C CA  . ASN A 191 ? 1.0485 1.2982 0.9357 0.0182  0.2119  -0.0251 191 ASN A CA  
1461 C C   . ASN A 191 ? 1.1124 1.3763 1.0438 0.0148  0.2043  -0.0063 191 ASN A C   
1462 O O   . ASN A 191 ? 1.0729 1.3338 1.0393 0.0234  0.1932  -0.0086 191 ASN A O   
1463 C CB  . ASN A 191 ? 1.1028 1.3691 0.9980 0.0289  0.2391  -0.0432 191 ASN A CB  
1464 C CG  . ASN A 191 ? 1.1900 1.4358 1.0762 0.0425  0.2422  -0.0694 191 ASN A CG  
1465 O OD1 . ASN A 191 ? 1.1146 1.3653 0.9895 0.0490  0.2646  -0.0866 191 ASN A OD1 
1466 N ND2 . ASN A 191 ? 1.0831 1.3021 0.9752 0.0469  0.2211  -0.0730 191 ASN A ND2 
1467 N N   . SER A 192 ? 1.0745 1.3512 1.0013 0.0013  0.2090  0.0125  192 SER A N   
1468 C CA  . SER A 192 ? 1.0269 1.3142 0.9904 -0.0061 0.2023  0.0299  192 SER A CA  
1469 C C   . SER A 192 ? 0.9755 1.2401 0.9457 -0.0064 0.1753  0.0352  192 SER A C   
1470 O O   . SER A 192 ? 0.9129 1.1739 0.9089 0.0033  0.1652  0.0268  192 SER A O   
1471 C CB  . SER A 192 ? 0.9452 1.2615 0.9594 0.0001  0.2146  0.0252  192 SER A CB  
1472 O OG  . SER A 192 ? 0.9274 1.2389 0.9683 0.0148  0.2027  0.0131  192 SER A OG  
1473 N N   . ALA B 4   ? 1.6284 0.7838 0.6127 -0.3078 -0.0502 -0.2075 4   ALA C N   
1474 C CA  . ALA B 4   ? 1.6298 0.7956 0.6136 -0.3127 -0.0487 -0.2106 4   ALA C CA  
1475 C C   . ALA B 4   ? 1.6333 0.8030 0.6126 -0.3184 -0.0479 -0.2099 4   ALA C C   
1476 O O   . ALA B 4   ? 1.6308 0.8121 0.6142 -0.3186 -0.0487 -0.2144 4   ALA C O   
1477 C CB  . ALA B 4   ? 1.6247 0.8033 0.6166 -0.3098 -0.0496 -0.2173 4   ALA C CB  
1478 N N   . SER B 5   ? 1.6390 0.7992 0.6100 -0.3228 -0.0463 -0.2044 5   SER C N   
1479 C CA  . SER B 5   ? 1.6434 0.8068 0.6088 -0.3288 -0.0452 -0.2034 5   SER C CA  
1480 C C   . SER B 5   ? 1.6467 0.8161 0.6094 -0.3344 -0.0430 -0.2048 5   SER C C   
1481 O O   . SER B 5   ? 1.6484 0.8119 0.6094 -0.3351 -0.0419 -0.2030 5   SER C O   
1482 C CB  . SER B 5   ? 1.6790 0.8290 0.6367 -0.3307 -0.0447 -0.1968 5   SER C CB  
1483 O OG  . SER B 5   ? 1.7545 0.8955 0.7144 -0.3250 -0.0464 -0.1946 5   SER C OG  
1484 N N   . LYS B 6   ? 1.6710 0.8510 0.6342 -0.3379 -0.0422 -0.2081 6   LYS C N   
1485 C CA  . LYS B 6   ? 1.9400 1.1295 0.9020 -0.3432 -0.0404 -0.2109 6   LYS C CA  
1486 C C   . LYS B 6   ? 1.9737 1.1691 0.9416 -0.3414 -0.0402 -0.2149 6   LYS C C   
1487 O O   . LYS B 6   ? 1.9010 1.0881 0.8670 -0.3414 -0.0394 -0.2125 6   LYS C O   
1488 C CB  . LYS B 6   ? 2.1284 1.3103 1.0803 -0.3501 -0.0381 -0.2058 6   LYS C CB  
1489 C CG  . LYS B 6   ? 1.8996 1.0789 0.8464 -0.3517 -0.0385 -0.2029 6   LYS C CG  
1490 C CD  . LYS B 6   ? 1.8131 0.9781 0.7503 -0.3556 -0.0370 -0.1959 6   LYS C CD  
1491 C CE  . LYS B 6   ? 1.8764 1.0427 0.8059 -0.3634 -0.0343 -0.1945 6   LYS C CE  
1492 N NZ  . LYS B 6   ? 1.7202 0.8717 0.6416 -0.3670 -0.0325 -0.1884 6   LYS C NZ  
1493 N N   . ASP B 7   ? 2.4883 1.6946 1.4524 -0.3472 -0.0396 -0.2164 7   ASP C N   
1494 C CA  . ASP B 7   ? 2.5061 1.7188 1.4648 -0.3538 -0.0379 -0.2166 7   ASP C CA  
1495 C C   . ASP B 7   ? 2.6311 1.8410 1.5851 -0.3593 -0.0352 -0.2152 7   ASP C C   
1496 O O   . ASP B 7   ? 2.4971 1.7180 1.4533 -0.3619 -0.0343 -0.2193 7   ASP C O   
1497 C CB  . ASP B 7   ? 2.5012 1.7107 1.4537 -0.3561 -0.0380 -0.2132 7   ASP C CB  
1498 C CG  . ASP B 7   ? 2.4714 1.6906 1.4197 -0.3620 -0.0364 -0.2147 7   ASP C CG  
1499 O OD1 . ASP B 7   ? 2.3982 1.6121 1.3386 -0.3680 -0.0341 -0.2112 7   ASP C OD1 
1500 O OD2 . ASP B 7   ? 2.4545 1.6865 1.4077 -0.3607 -0.0376 -0.2194 7   ASP C OD2 
1501 N N   . PRO B 8   ? 3.9619 3.1581 2.9098 -0.3614 -0.0339 -0.2098 8   PRO C N   
1502 C CA  . PRO B 8   ? 3.9657 3.1594 2.9106 -0.3660 -0.0315 -0.2092 8   PRO C CA  
1503 C C   . PRO B 8   ? 4.0003 3.1949 2.9522 -0.3614 -0.0323 -0.2121 8   PRO C C   
1504 O O   . PRO B 8   ? 4.0052 3.1889 2.9551 -0.3608 -0.0318 -0.2089 8   PRO C O   
1505 C CB  . PRO B 8   ? 3.9712 3.1487 2.9075 -0.3689 -0.0301 -0.2024 8   PRO C CB  
1506 C CG  . PRO B 8   ? 3.9195 3.0929 2.8523 -0.3680 -0.0312 -0.1993 8   PRO C CG  
1507 C CD  . PRO B 8   ? 3.9257 3.1084 2.8672 -0.3615 -0.0340 -0.2038 8   PRO C CD  
1508 N N   . GLY B 9   ? 2.7121 1.9194 1.6721 -0.3581 -0.0337 -0.2181 9   GLY C N   
1509 C CA  . GLY B 9   ? 2.6112 1.8202 1.5773 -0.3545 -0.0341 -0.2210 9   GLY C CA  
1510 C C   . GLY B 9   ? 2.6251 1.8314 1.5865 -0.3607 -0.0315 -0.2200 9   GLY C C   
1511 O O   . GLY B 9   ? 2.6020 1.8084 1.5667 -0.3595 -0.0312 -0.2218 9   GLY C O   
1512 N N   . ALA B 10  ? 2.2643 1.4685 1.2183 -0.3671 -0.0296 -0.2172 10  ALA C N   
1513 C CA  . ALA B 10  ? 1.9072 1.1072 0.8556 -0.3738 -0.0268 -0.2156 10  ALA C CA  
1514 C C   . ALA B 10  ? 1.8333 1.0206 0.7802 -0.3728 -0.0263 -0.2123 10  ALA C C   
1515 O O   . ALA B 10  ? 1.6791 0.8649 0.6243 -0.3770 -0.0243 -0.2127 10  ALA C O   
1516 C CB  . ALA B 10  ? 1.7684 0.9634 0.7078 -0.3795 -0.0253 -0.2112 10  ALA C CB  
1517 N N   . VAL B 11  ? 1.9843 1.1622 0.9310 -0.3680 -0.0278 -0.2089 11  VAL C N   
1518 C CA  . VAL B 11  ? 1.8234 0.9883 0.7678 -0.3672 -0.0272 -0.2052 11  VAL C CA  
1519 C C   . VAL B 11  ? 1.7458 0.9156 0.6968 -0.3644 -0.0276 -0.2095 11  VAL C C   
1520 O O   . VAL B 11  ? 1.6754 0.8380 0.6242 -0.3665 -0.0262 -0.2080 11  VAL C O   
1521 C CB  . VAL B 11  ? 1.6817 0.8357 0.6249 -0.3621 -0.0289 -0.2009 11  VAL C CB  
1522 C CG1 . VAL B 11  ? 1.6763 0.8259 0.6136 -0.3643 -0.0289 -0.1969 11  VAL C CG1 
1523 C CG2 . VAL B 11  ? 1.6926 0.8518 0.6440 -0.3542 -0.0316 -0.2041 11  VAL C CG2 
1524 N N   . ASP B 12  ? 1.1836 1.2363 1.0859 -0.1425 0.1104  0.0156  12  ASP C N   
1525 C CA  . ASP B 12  ? 1.0896 1.1486 0.9799 -0.1429 0.1020  0.0245  12  ASP C CA  
1526 C C   . ASP B 12  ? 1.0199 1.0746 0.9136 -0.1453 0.0864  0.0275  12  ASP C C   
1527 O O   . ASP B 12  ? 0.9496 1.0067 0.8289 -0.1455 0.0747  0.0251  12  ASP C O   
1528 C CB  . ASP B 12  ? 1.1294 1.1957 1.0222 -0.1428 0.1127  0.0411  12  ASP C CB  
1529 C CG  . ASP B 12  ? 1.1548 1.2251 1.0439 -0.1406 0.1279  0.0377  12  ASP C CG  
1530 O OD1 . ASP B 12  ? 1.2287 1.3043 1.1003 -0.1385 0.1277  0.0313  12  ASP C OD1 
1531 O OD2 . ASP B 12  ? 1.1667 1.2348 1.0703 -0.1410 0.1401  0.0417  12  ASP C OD2 
1532 N N   . ALA B 13  ? 0.9890 1.0372 0.9014 -0.1471 0.0860  0.0321  13  ALA C N   
1533 C CA  . ALA B 13  ? 0.8566 0.9002 0.7742 -0.1494 0.0716  0.0345  13  ALA C CA  
1534 C C   . ALA B 13  ? 0.7876 0.8258 0.6954 -0.1490 0.0606  0.0167  13  ALA C C   
1535 O O   . ALA B 13  ? 0.8531 0.8880 0.7600 -0.1472 0.0661  0.0038  13  ALA C O   
1536 C CB  . ALA B 13  ? 0.7619 0.7986 0.7016 -0.1510 0.0754  0.0409  13  ALA C CB  
1537 N N   . LYS B 14  ? 0.6851 0.7223 0.5861 -0.1505 0.0453  0.0160  14  LYS C N   
1538 C CA  . LYS B 14  ? 0.6900 0.7218 0.5809 -0.1501 0.0347  -0.0007 14  LYS C CA  
1539 C C   . LYS B 14  ? 0.6594 0.6807 0.5650 -0.1508 0.0316  -0.0087 14  LYS C C   
1540 O O   . LYS B 14  ? 0.6070 0.6250 0.5302 -0.1524 0.0331  0.0006  14  LYS C O   
1541 C CB  . LYS B 14  ? 0.7187 0.7531 0.5952 -0.1517 0.0195  0.0008  14  LYS C CB  
1542 C CG  . LYS B 14  ? 0.7214 0.7657 0.5801 -0.1507 0.0216  0.0056  14  LYS C CG  
1543 C CD  . LYS B 14  ? 0.6604 0.7054 0.5024 -0.1477 0.0257  -0.0092 14  LYS C CD  
1544 C CE  . LYS B 14  ? 0.7211 0.7746 0.5427 -0.1469 0.0236  -0.0062 14  LYS C CE  
1545 N NZ  . LYS B 14  ? 0.6980 0.7558 0.5189 -0.1498 0.0137  0.0075  14  LYS C NZ  
1546 N N   . PRO B 15  ? 0.6386 0.6546 0.5373 -0.1493 0.0285  -0.0258 15  PRO C N   
1547 C CA  . PRO B 15  ? 0.6087 0.6150 0.5210 -0.1496 0.0258  -0.0336 15  PRO C CA  
1548 C C   . PRO B 15  ? 0.5799 0.5813 0.4974 -0.1523 0.0115  -0.0300 15  PRO C C   
1549 O O   . PRO B 15  ? 0.5365 0.5404 0.4417 -0.1536 0.0003  -0.0290 15  PRO C O   
1550 C CB  . PRO B 15  ? 0.5761 0.5792 0.4764 -0.1471 0.0248  -0.0524 15  PRO C CB  
1551 C CG  . PRO B 15  ? 0.6264 0.6359 0.5052 -0.1462 0.0213  -0.0546 15  PRO C CG  
1552 C CD  . PRO B 15  ? 0.6653 0.6837 0.5438 -0.1469 0.0276  -0.0385 15  PRO C CD  
1553 N N   . LEU B 16  ? 0.4822 0.4766 0.4180 -0.1533 0.0120  -0.0281 16  LEU C N   
1554 C CA  . LEU B 16  ? 0.5080 0.4969 0.4510 -0.1558 -0.0009 -0.0252 16  LEU C CA  
1555 C C   . LEU B 16  ? 0.5128 0.4937 0.4507 -0.1550 -0.0095 -0.0426 16  LEU C C   
1556 O O   . LEU B 16  ? 0.4960 0.4725 0.4379 -0.1530 -0.0027 -0.0529 16  LEU C O   
1557 C CB  . LEU B 16  ? 0.5416 0.5267 0.5071 -0.1570 0.0046  -0.0142 16  LEU C CB  
1558 C CG  . LEU B 16  ? 0.5215 0.4991 0.4980 -0.1592 -0.0067 -0.0125 16  LEU C CG  
1559 C CD1 . LEU B 16  ? 0.5268 0.5085 0.4959 -0.1617 -0.0200 -0.0047 16  LEU C CD1 
1560 C CD2 . LEU B 16  ? 0.5478 0.5217 0.5454 -0.1598 0.0008  -0.0022 16  LEU C CD2 
1561 N N   . VAL B 17  ? 0.5221 0.5016 0.4495 -0.1566 -0.0240 -0.0462 17  VAL C N   
1562 C CA  . VAL B 17  ? 0.5250 0.4965 0.4464 -0.1560 -0.0333 -0.0621 17  VAL C CA  
1563 C C   . VAL B 17  ? 0.5305 0.4963 0.4605 -0.1590 -0.0464 -0.0580 17  VAL C C   
1564 O O   . VAL B 17  ? 0.5878 0.5574 0.5116 -0.1616 -0.0559 -0.0505 17  VAL C O   
1565 C CB  . VAL B 17  ? 0.5107 0.4847 0.4082 -0.1548 -0.0385 -0.0733 17  VAL C CB  
1566 C CG1 . VAL B 17  ? 0.5226 0.4878 0.4146 -0.1547 -0.0498 -0.0880 17  VAL C CG1 
1567 C CG2 . VAL B 17  ? 0.4880 0.4665 0.3775 -0.1514 -0.0254 -0.0795 17  VAL C CG2 
1568 N N   . VAL B 18  ? 0.5341 0.4913 0.4785 -0.1589 -0.0469 -0.0625 18  VAL C N   
1569 C CA  . VAL B 18  ? 0.5922 0.5433 0.5464 -0.1615 -0.0586 -0.0590 18  VAL C CA  
1570 C C   . VAL B 18  ? 0.6081 0.5506 0.5556 -0.1609 -0.0681 -0.0756 18  VAL C C   
1571 O O   . VAL B 18  ? 0.5596 0.4972 0.5089 -0.1582 -0.0625 -0.0873 18  VAL C O   
1572 C CB  . VAL B 18  ? 0.5624 0.5098 0.5398 -0.1620 -0.0520 -0.0493 18  VAL C CB  
1573 C CG1 . VAL B 18  ? 0.6045 0.5450 0.5928 -0.1644 -0.0637 -0.0465 18  VAL C CG1 
1574 C CG2 . VAL B 18  ? 0.5333 0.4889 0.5169 -0.1626 -0.0430 -0.0324 18  VAL C CG2 
1575 N N   . GLU B 19  ? 0.6591 0.6001 0.5981 -0.1634 -0.0824 -0.0767 19  GLU C N   
1576 C CA  . GLU B 19  ? 0.7156 0.6480 0.6477 -0.1631 -0.0920 -0.0921 19  GLU C CA  
1577 C C   . GLU B 19  ? 0.7013 0.6247 0.6520 -0.1638 -0.0955 -0.0918 19  GLU C C   
1578 O O   . GLU B 19  ? 0.7306 0.6548 0.6952 -0.1662 -0.0976 -0.0784 19  GLU C O   
1579 C CB  . GLU B 19  ? 0.7666 0.7004 0.6823 -0.1658 -0.1061 -0.0934 19  GLU C CB  
1580 C CG  . GLU B 19  ? 0.8082 0.7508 0.7044 -0.1651 -0.1035 -0.0933 19  GLU C CG  
1581 C CD  . GLU B 19  ? 0.8659 0.8064 0.7478 -0.1614 -0.0981 -0.1095 19  GLU C CD  
1582 O OE1 . GLU B 19  ? 0.8880 0.8207 0.7623 -0.1609 -0.1057 -0.1231 19  GLU C OE1 
1583 O OE2 . GLU B 19  ? 0.8580 0.8045 0.7367 -0.1588 -0.0861 -0.1085 19  GLU C OE2 
1584 N N   . ILE B 20  ? 0.6786 0.5981 0.6355 -0.1542 -0.0926 -0.1037 20  ILE C N   
1585 C CA  . ILE B 20  ? 0.7305 0.6479 0.7111 -0.1458 -0.0911 -0.1022 20  ILE C CA  
1586 C C   . ILE B 20  ? 0.7681 0.6868 0.7506 -0.1375 -0.0971 -0.1117 20  ILE C C   
1587 O O   . ILE B 20  ? 0.7459 0.6655 0.7121 -0.1379 -0.1039 -0.1182 20  ILE C O   
1588 C CB  . ILE B 20  ? 0.6476 0.5629 0.6423 -0.1397 -0.0795 -0.1038 20  ILE C CB  
1589 C CG1 . ILE B 20  ? 0.5934 0.5094 0.5931 -0.1479 -0.0710 -0.0920 20  ILE C CG1 
1590 C CG2 . ILE B 20  ? 0.6862 0.6017 0.7036 -0.1286 -0.0784 -0.1061 20  ILE C CG2 
1591 C CD1 . ILE B 20  ? 0.4931 0.4076 0.5036 -0.1420 -0.0594 -0.0933 20  ILE C CD1 
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