data_8VLF
# 
_entry.id   8VLF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8VLF         pdb_00008vlf 10.2210/pdb8vlf/pdb 
WWPDB D_1000280509 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VLF 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Ash1L PHD finger in complex with histone H3K4me2' 
_pdbx_database_related.db_id          8VLD 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tatiana.kutateladze@cuanschutz.edu 
_pdbx_contact_author.name_first         Tatiana 
_pdbx_contact_author.name_last          Kutateladze 
_pdbx_contact_author.name_mi            G 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7375-6990 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vann, K.R.'        1 0000-0002-6366-6112 
'Kutateladze, T.G.' 2 0000-0001-7375-6990 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2235 
_citation.page_last                 2235 
_citation.title                     'Structure-function relationship of ASH1L and histone H3K36 and H3K4 methylation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57556-5 
_citation.pdbx_database_id_PubMed   40044670 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vann, K.R.'        1  0000-0002-6366-6112 
primary 'Sharma, R.'        2  ?                   
primary 'Hsu, C.C.'         3  ?                   
primary 'Devoucoux, M.'     4  0000-0002-0965-2852 
primary 'Tencer, A.H.'      5  ?                   
primary 'Zeng, L.'          6  0000-0002-4236-6735 
primary 'Lin, K.'           7  ?                   
primary 'Zhu, L.'           8  ?                   
primary 'Li, Q.'            9  ?                   
primary 'Lachance, C.'      10 ?                   
primary 'Ospina, R.R.'      11 ?                   
primary 'Tong, Q.'          12 ?                   
primary 'Cheung, K.L.'      13 ?                   
primary 'Yang, S.'          14 ?                   
primary 'Biswas, S.'        15 ?                   
primary 'Xuan, H.'          16 ?                   
primary 'Gatchalian, J.'    17 ?                   
primary 'Alamillo, L.'      18 0000-0002-2622-0277 
primary 'Wang, J.'          19 0000-0002-1317-6457 
primary 'Jang, S.M.'        20 ?                   
primary 'Klein, B.J.'       21 ?                   
primary 'Lu, Y.'            22 ?                   
primary 'Ernst, P.'         23 ?                   
primary 'Strahl, B.D.'      24 0000-0002-4947-6259 
primary 'Rothbart, S.B.'    25 0000-0003-1631-5392 
primary 'Walsh, M.J.'       26 0000-0001-8339-8285 
primary 'Cleary, M.L.'      27 0000-0001-7127-3223 
primary 'Cote, J.'          28 0000-0001-6751-555X 
primary 'Shi, X.'           29 0000-0001-5242-8189 
primary 'Zhou, M.M.'        30 0000-0002-7049-0573 
primary 'Kutateladze, T.G.' 31 0000-0001-7375-6990 
# 
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 'Histone-lysine N-methyltransferase ASH1L' 6470.484 2   ? ? ? ? 
2 polymer     syn 'Histone H3.3C'                            1350.568 2   ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                 65.409   4   ? ? ? ? 
4 water       nat water                                      18.015   123 ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        'Histone H3.5' 
# 
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  GPLDVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDRE 
GPLDVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDRE A,B ? 
2 'polypeptide(L)' no yes 'ART(M3L)QTARKSTG'                                       ARTKQTARKSTG P,T ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'ZINC ION' ZN  
4 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  PRO n 
1 3  LEU n 
1 4  ASP n 
1 5  VAL n 
1 6  ILE n 
1 7  ARG n 
1 8  CYS n 
1 9  ILE n 
1 10 CYS n 
1 11 GLY n 
1 12 LEU n 
1 13 TYR n 
1 14 LYS n 
1 15 ASP n 
1 16 GLU n 
1 17 GLY n 
1 18 LEU n 
1 19 MET n 
1 20 ILE n 
1 21 GLN n 
1 22 CYS n 
1 23 ASP n 
1 24 LYS n 
1 25 CYS n 
1 26 MET n 
1 27 VAL n 
1 28 TRP n 
1 29 GLN n 
1 30 HIS n 
1 31 CYS n 
1 32 ASP n 
1 33 CYS n 
1 34 MET n 
1 35 GLY n 
1 36 VAL n 
1 37 ASN n 
1 38 SER n 
1 39 ASP n 
1 40 VAL n 
1 41 GLU n 
1 42 HIS n 
1 43 TYR n 
1 44 LEU n 
1 45 CYS n 
1 46 GLU n 
1 47 GLN n 
1 48 CYS n 
1 49 ASP n 
1 50 PRO n 
1 51 ARG n 
1 52 PRO n 
1 53 VAL n 
1 54 ASP n 
1 55 ARG n 
1 56 GLU n 
2 1  ALA n 
2 2  ARG n 
2 3  THR n 
2 4  M3L n 
2 5  GLN n 
2 6  THR n 
2 7  ALA n 
2 8  ARG n 
2 9  LYS n 
2 10 SER n 
2 11 THR n 
2 12 GLY 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                   56 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ASH1L 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_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       12 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                Synpeptide 
# 
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  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
M3L 'L-peptide linking' n N-TRIMETHYLLYSINE ? 'C9 H21 N2 O2 1' 189.275 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
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 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
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  GLY 1  1  1  GLY GLY A . n 
A 1 2  PRO 2  2  2  PRO PRO A . n 
A 1 3  LEU 3  3  3  LEU LEU A . n 
A 1 4  ASP 4  4  4  ASP ASP A . n 
A 1 5  VAL 5  5  5  VAL VAL A . n 
A 1 6  ILE 6  6  6  ILE ILE A . n 
A 1 7  ARG 7  7  7  ARG ARG A . n 
A 1 8  CYS 8  8  8  CYS CYS A . n 
A 1 9  ILE 9  9  9  ILE ILE A . n 
A 1 10 CYS 10 10 10 CYS CYS A . n 
A 1 11 GLY 11 11 11 GLY GLY A . n 
A 1 12 LEU 12 12 12 LEU LEU A . n 
A 1 13 TYR 13 13 13 TYR TYR A . n 
A 1 14 LYS 14 14 14 LYS LYS A . n 
A 1 15 ASP 15 15 15 ASP ASP A . n 
A 1 16 GLU 16 16 16 GLU GLU A . n 
A 1 17 GLY 17 17 17 GLY GLY A . n 
A 1 18 LEU 18 18 18 LEU LEU A . n 
A 1 19 MET 19 19 19 MET MET A . n 
A 1 20 ILE 20 20 20 ILE ILE A . n 
A 1 21 GLN 21 21 21 GLN GLN A . n 
A 1 22 CYS 22 22 22 CYS CYS A . n 
A 1 23 ASP 23 23 23 ASP ASP A . n 
A 1 24 LYS 24 24 24 LYS LYS A . n 
A 1 25 CYS 25 25 25 CYS CYS A . n 
A 1 26 MET 26 26 26 MET MET A . n 
A 1 27 VAL 27 27 27 VAL VAL A . n 
A 1 28 TRP 28 28 28 TRP TRP A . n 
A 1 29 GLN 29 29 29 GLN GLN A . n 
A 1 30 HIS 30 30 30 HIS HIS A . n 
A 1 31 CYS 31 31 31 CYS CYS A . n 
A 1 32 ASP 32 32 32 ASP ASP A . n 
A 1 33 CYS 33 33 33 CYS CYS A . n 
A 1 34 MET 34 34 34 MET MET A . n 
A 1 35 GLY 35 35 35 GLY GLY A . n 
A 1 36 VAL 36 36 36 VAL VAL A . n 
A 1 37 ASN 37 37 37 ASN ASN A . n 
A 1 38 SER 38 38 38 SER SER A . n 
A 1 39 ASP 39 39 39 ASP ASP A . n 
A 1 40 VAL 40 40 40 VAL VAL A . n 
A 1 41 GLU 41 41 41 GLU GLU A . n 
A 1 42 HIS 42 42 42 HIS HIS A . n 
A 1 43 TYR 43 43 43 TYR TYR A . n 
A 1 44 LEU 44 44 44 LEU LEU A . n 
A 1 45 CYS 45 45 45 CYS CYS A . n 
A 1 46 GLU 46 46 46 GLU GLU A . n 
A 1 47 GLN 47 47 47 GLN GLN A . n 
A 1 48 CYS 48 48 48 CYS CYS A . n 
A 1 49 ASP 49 49 49 ASP ASP A . n 
A 1 50 PRO 50 50 50 PRO PRO A . n 
A 1 51 ARG 51 51 51 ARG ARG A . n 
A 1 52 PRO 52 52 52 PRO PRO A . n 
A 1 53 VAL 53 53 53 VAL VAL A . n 
A 1 54 ASP 54 54 ?  ?   ?   A . n 
A 1 55 ARG 55 55 ?  ?   ?   A . n 
A 1 56 GLU 56 56 ?  ?   ?   A . n 
B 1 1  GLY 1  1  1  GLY GLY B . n 
B 1 2  PRO 2  2  2  PRO PRO B . n 
B 1 3  LEU 3  3  3  LEU LEU B . n 
B 1 4  ASP 4  4  4  ASP ASP B . n 
B 1 5  VAL 5  5  5  VAL VAL B . n 
B 1 6  ILE 6  6  6  ILE ILE B . n 
B 1 7  ARG 7  7  7  ARG ARG B . n 
B 1 8  CYS 8  8  8  CYS CYS B . n 
B 1 9  ILE 9  9  9  ILE ILE B . n 
B 1 10 CYS 10 10 10 CYS CYS B . n 
B 1 11 GLY 11 11 11 GLY GLY B . n 
B 1 12 LEU 12 12 12 LEU LEU B . n 
B 1 13 TYR 13 13 13 TYR TYR B . n 
B 1 14 LYS 14 14 14 LYS LYS B . n 
B 1 15 ASP 15 15 15 ASP ASP B . n 
B 1 16 GLU 16 16 16 GLU GLU B . n 
B 1 17 GLY 17 17 17 GLY GLY B . n 
B 1 18 LEU 18 18 18 LEU LEU B . n 
B 1 19 MET 19 19 19 MET MET B . n 
B 1 20 ILE 20 20 20 ILE ILE B . n 
B 1 21 GLN 21 21 21 GLN GLN B . n 
B 1 22 CYS 22 22 22 CYS CYS B . n 
B 1 23 ASP 23 23 23 ASP ASP B . n 
B 1 24 LYS 24 24 24 LYS LYS B . n 
B 1 25 CYS 25 25 25 CYS CYS B . n 
B 1 26 MET 26 26 26 MET MET B . n 
B 1 27 VAL 27 27 27 VAL VAL B . n 
B 1 28 TRP 28 28 28 TRP TRP B . n 
B 1 29 GLN 29 29 29 GLN GLN B . n 
B 1 30 HIS 30 30 30 HIS HIS B . n 
B 1 31 CYS 31 31 31 CYS CYS B . n 
B 1 32 ASP 32 32 32 ASP ASP B . n 
B 1 33 CYS 33 33 33 CYS CYS B . n 
B 1 34 MET 34 34 34 MET MET B . n 
B 1 35 GLY 35 35 35 GLY GLY B . n 
B 1 36 VAL 36 36 36 VAL VAL B . n 
B 1 37 ASN 37 37 37 ASN ASN B . n 
B 1 38 SER 38 38 38 SER SER B . n 
B 1 39 ASP 39 39 39 ASP ASP B . n 
B 1 40 VAL 40 40 40 VAL VAL B . n 
B 1 41 GLU 41 41 41 GLU GLU B . n 
B 1 42 HIS 42 42 42 HIS HIS B . n 
B 1 43 TYR 43 43 43 TYR TYR B . n 
B 1 44 LEU 44 44 44 LEU LEU B . n 
B 1 45 CYS 45 45 45 CYS CYS B . n 
B 1 46 GLU 46 46 46 GLU GLU B . n 
B 1 47 GLN 47 47 47 GLN GLN B . n 
B 1 48 CYS 48 48 48 CYS CYS B . n 
B 1 49 ASP 49 49 49 ASP ASP B . n 
B 1 50 PRO 50 50 50 PRO PRO B . n 
B 1 51 ARG 51 51 51 ARG ARG B . n 
B 1 52 PRO 52 52 52 PRO PRO B . n 
B 1 53 VAL 53 53 53 VAL VAL B . n 
B 1 54 ASP 54 54 ?  ?   ?   B . n 
B 1 55 ARG 55 55 ?  ?   ?   B . n 
B 1 56 GLU 56 56 ?  ?   ?   B . n 
C 2 1  ALA 1  1  1  ALA ALA P . n 
C 2 2  ARG 2  2  2  ARG ARG P . n 
C 2 3  THR 3  3  3  THR THR P . n 
C 2 4  M3L 4  4  4  M3L M3L P . n 
C 2 5  GLN 5  5  5  GLN GLN P . n 
C 2 6  THR 6  6  6  THR THR P . n 
C 2 7  ALA 7  7  7  ALA ALA P . n 
C 2 8  ARG 8  8  8  ARG ARG P . n 
C 2 9  LYS 9  9  9  LYS LYS P . n 
C 2 10 SER 10 10 10 SER SER P . n 
C 2 11 THR 11 11 11 THR THR P . n 
C 2 12 GLY 12 12 12 GLY GLY P . n 
D 2 1  ALA 1  1  1  ALA ALA T . n 
D 2 2  ARG 2  2  2  ARG ARG T . n 
D 2 3  THR 3  3  3  THR THR T . n 
D 2 4  M3L 4  4  4  M3L M3L T . n 
D 2 5  GLN 5  5  5  GLN GLN T . n 
D 2 6  THR 6  6  6  THR THR T . n 
D 2 7  ALA 7  7  7  ALA ALA T . n 
D 2 8  ARG 8  8  8  ARG ARG T . n 
D 2 9  LYS 9  9  9  LYS LYS T . n 
D 2 10 SER 10 10 10 SER SER T . n 
D 2 11 THR 11 11 11 THR THR T . n 
D 2 12 GLY 12 12 12 GLY GLY T . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        M3L 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   M3L 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
E 3 ZN  1  101 101 ZN  ZN  A . 
F 3 ZN  1  102 102 ZN  ZN  A . 
G 3 ZN  1  101 101 ZN  ZN  B . 
H 3 ZN  1  102 102 ZN  ZN  B . 
I 4 HOH 1  201 201 HOH HOH A . 
I 4 HOH 2  202 202 HOH HOH A . 
I 4 HOH 3  203 203 HOH HOH A . 
I 4 HOH 4  204 204 HOH HOH A . 
I 4 HOH 5  205 205 HOH HOH A . 
I 4 HOH 6  206 206 HOH HOH A . 
I 4 HOH 7  207 207 HOH HOH A . 
I 4 HOH 8  208 208 HOH HOH A . 
I 4 HOH 9  209 209 HOH HOH A . 
I 4 HOH 10 210 210 HOH HOH A . 
I 4 HOH 11 211 211 HOH HOH A . 
I 4 HOH 12 212 212 HOH HOH A . 
I 4 HOH 13 213 213 HOH HOH A . 
I 4 HOH 14 214 214 HOH HOH A . 
I 4 HOH 15 215 215 HOH HOH A . 
I 4 HOH 16 216 216 HOH HOH A . 
I 4 HOH 17 217 217 HOH HOH A . 
I 4 HOH 18 218 218 HOH HOH A . 
I 4 HOH 19 219 219 HOH HOH A . 
I 4 HOH 20 220 220 HOH HOH A . 
I 4 HOH 21 221 221 HOH HOH A . 
I 4 HOH 22 222 222 HOH HOH A . 
I 4 HOH 23 223 223 HOH HOH A . 
I 4 HOH 24 224 224 HOH HOH A . 
I 4 HOH 25 225 225 HOH HOH A . 
I 4 HOH 26 226 226 HOH HOH A . 
I 4 HOH 27 227 227 HOH HOH A . 
I 4 HOH 28 228 228 HOH HOH A . 
I 4 HOH 29 229 229 HOH HOH A . 
I 4 HOH 30 230 230 HOH HOH A . 
I 4 HOH 31 231 231 HOH HOH A . 
I 4 HOH 32 232 232 HOH HOH A . 
I 4 HOH 33 233 233 HOH HOH A . 
I 4 HOH 34 234 234 HOH HOH A . 
I 4 HOH 35 235 235 HOH HOH A . 
I 4 HOH 36 236 236 HOH HOH A . 
I 4 HOH 37 237 237 HOH HOH A . 
I 4 HOH 38 238 238 HOH HOH A . 
I 4 HOH 39 239 239 HOH HOH A . 
I 4 HOH 40 240 240 HOH HOH A . 
I 4 HOH 41 241 241 HOH HOH A . 
I 4 HOH 42 242 242 HOH HOH A . 
I 4 HOH 43 243 243 HOH HOH A . 
I 4 HOH 44 244 244 HOH HOH A . 
I 4 HOH 45 245 245 HOH HOH A . 
J 4 HOH 1  201 201 HOH HOH B . 
J 4 HOH 2  202 202 HOH HOH B . 
J 4 HOH 3  203 203 HOH HOH B . 
J 4 HOH 4  204 204 HOH HOH B . 
J 4 HOH 5  205 205 HOH HOH B . 
J 4 HOH 6  206 206 HOH HOH B . 
J 4 HOH 7  207 207 HOH HOH B . 
J 4 HOH 8  208 208 HOH HOH B . 
J 4 HOH 9  209 209 HOH HOH B . 
J 4 HOH 10 210 210 HOH HOH B . 
J 4 HOH 11 211 211 HOH HOH B . 
J 4 HOH 12 212 212 HOH HOH B . 
J 4 HOH 13 213 213 HOH HOH B . 
J 4 HOH 14 214 214 HOH HOH B . 
J 4 HOH 15 215 215 HOH HOH B . 
J 4 HOH 16 216 216 HOH HOH B . 
J 4 HOH 17 217 217 HOH HOH B . 
J 4 HOH 18 218 218 HOH HOH B . 
J 4 HOH 19 219 219 HOH HOH B . 
J 4 HOH 20 220 220 HOH HOH B . 
J 4 HOH 21 221 221 HOH HOH B . 
J 4 HOH 22 222 222 HOH HOH B . 
J 4 HOH 23 223 223 HOH HOH B . 
J 4 HOH 24 224 224 HOH HOH B . 
J 4 HOH 25 225 225 HOH HOH B . 
J 4 HOH 26 226 226 HOH HOH B . 
J 4 HOH 27 227 227 HOH HOH B . 
J 4 HOH 28 228 228 HOH HOH B . 
J 4 HOH 29 229 229 HOH HOH B . 
J 4 HOH 30 230 230 HOH HOH B . 
J 4 HOH 31 231 231 HOH HOH B . 
J 4 HOH 32 232 232 HOH HOH B . 
J 4 HOH 33 233 233 HOH HOH B . 
J 4 HOH 34 234 234 HOH HOH B . 
J 4 HOH 35 235 235 HOH HOH B . 
J 4 HOH 36 236 236 HOH HOH B . 
J 4 HOH 37 237 237 HOH HOH B . 
J 4 HOH 38 238 238 HOH HOH B . 
J 4 HOH 39 239 239 HOH HOH B . 
J 4 HOH 40 240 240 HOH HOH B . 
J 4 HOH 41 241 241 HOH HOH B . 
J 4 HOH 42 242 242 HOH HOH B . 
J 4 HOH 43 243 243 HOH HOH B . 
J 4 HOH 44 244 244 HOH HOH B . 
J 4 HOH 45 245 245 HOH HOH B . 
J 4 HOH 46 246 246 HOH HOH B . 
J 4 HOH 47 247 247 HOH HOH B . 
J 4 HOH 48 248 248 HOH HOH B . 
J 4 HOH 49 249 249 HOH HOH B . 
J 4 HOH 50 250 250 HOH HOH B . 
J 4 HOH 51 251 251 HOH HOH B . 
J 4 HOH 52 252 252 HOH HOH B . 
J 4 HOH 53 253 253 HOH HOH B . 
J 4 HOH 54 254 254 HOH HOH B . 
J 4 HOH 55 255 255 HOH HOH B . 
K 4 HOH 1  101 101 HOH HOH P . 
K 4 HOH 2  102 102 HOH HOH P . 
K 4 HOH 3  103 103 HOH HOH P . 
K 4 HOH 4  104 104 HOH HOH P . 
K 4 HOH 5  105 105 HOH HOH P . 
K 4 HOH 6  106 106 HOH HOH P . 
K 4 HOH 7  107 107 HOH HOH P . 
K 4 HOH 8  108 108 HOH HOH P . 
K 4 HOH 9  109 109 HOH HOH P . 
K 4 HOH 10 110 110 HOH HOH P . 
K 4 HOH 11 111 111 HOH HOH P . 
K 4 HOH 12 112 112 HOH HOH P . 
K 4 HOH 13 113 113 HOH HOH P . 
L 4 HOH 1  101 101 HOH HOH T . 
L 4 HOH 2  102 102 HOH HOH T . 
L 4 HOH 3  103 103 HOH HOH T . 
L 4 HOH 4  104 104 HOH HOH T . 
L 4 HOH 5  105 105 HOH HOH T . 
L 4 HOH 6  106 106 HOH HOH T . 
L 4 HOH 7  107 107 HOH HOH T . 
L 4 HOH 8  108 108 HOH HOH T . 
L 4 HOH 9  109 109 HOH HOH T . 
L 4 HOH 10 110 110 HOH HOH T . 
# 
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  ? ? ? 1.18.2_3874 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA   ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VLF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.800 
_cell.length_a_esd                 ? 
_cell.length_b                     49.800 
_cell.length_b_esd                 ? 
_cell.length_c                     46.290 
_cell.length_c_esd                 ? 
_cell.volume                       114800.591 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VLF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
_symmetry.space_group_name_Hall            'P 4cw' 
_symmetry.space_group_name_H-M             'P 43' 
_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                   8VLF 
_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             1.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          32.96 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.6 M sodium citrate pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   6.5 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-08-03 
_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   1.28 
_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                        'NSLS BEAMLINE X25' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.28 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X25 
_diffrn_source.pdbx_synchrotron_site       NSLS 
# 
_reflns.B_iso_Wilson_estimate                          15.78 
_reflns.entry_id                                       8VLF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.34 
_reflns.d_resolution_low                               20.07 
_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                                     49203 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052 
_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                                    1.34 
_reflns_shell.d_res_low                                     1.39 
_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                             2524 
_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                                  ? 
_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                                  0.41 
_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                               29.61 
_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                                 8VLF 
_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                            1.34 
_refine.ls_d_res_low                             20.07 
_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                     49203 
_refine.ls_number_reflns_R_free                  2654 
_refine.ls_number_reflns_R_work                  46549 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.31 
_refine.ls_percent_reflns_R_free                 5.39 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1568 
_refine.ls_R_factor_R_free                       0.1884 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1549 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7U7P 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.4216 
_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                            0.1296 
_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.details                          ? 
_refine_hist.d_res_high                       1.34 
_refine_hist.d_res_low                        20.07 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               1141 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1014 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0057 ? 1028 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9561 ? 1384 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0898 ? 150  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0096 ? 178  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.0478 ? 146  ? f_dihedral_angle_d ? ? 
# 
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' 1.34 1.36  . . 102 2311 92.74 . . . . 0.2352 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 1.36 1.39  . . 142 2421 95.53 . . . . 0.2153 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 1.39 1.42  . . 134 2446 97.84 . . . . 0.1857 . . . . . . . . . . . 0.2648 
'X-RAY DIFFRACTION' 1.42 1.45  . . 137 2451 97.92 . . . . 0.1734 . . . . . . . . . . . 0.1863 
'X-RAY DIFFRACTION' 1.45 1.48  . . 183 2386 98.20 . . . . 0.1729 . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 1.48 1.52  . . 148 2398 97.59 . . . . 0.1582 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 1.52 1.56  . . 124 2494 98.57 . . . . 0.1599 . . . . . . . . . . . 0.1901 
'X-RAY DIFFRACTION' 1.56 1.61  . . 152 2398 98.23 . . . . 0.1482 . . . . . . . . . . . 0.1820 
'X-RAY DIFFRACTION' 1.61 1.66  . . 122 2545 98.85 . . . . 0.1466 . . . . . . . . . . . 0.2012 
'X-RAY DIFFRACTION' 1.66 1.72  . . 160 2410 98.43 . . . . 0.1401 . . . . . . . . . . . 0.1574 
'X-RAY DIFFRACTION' 1.72 1.79  . . 108 2483 98.59 . . . . 0.1364 . . . . . . . . . . . 0.1797 
'X-RAY DIFFRACTION' 1.79 1.87  . . 163 2420 99.04 . . . . 0.1670 . . . . . . . . . . . 0.1814 
'X-RAY DIFFRACTION' 1.87 1.97  . . 187 2438 99.43 . . . . 0.1767 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 1.97 2.09  . . 158 2442 99.12 . . . . 0.1732 . . . . . . . . . . . 0.1839 
'X-RAY DIFFRACTION' 2.09 2.25  . . 93  2547 99.32 . . . . 0.1591 . . . . . . . . . . . 0.1737 
'X-RAY DIFFRACTION' 2.25 2.48  . . 76  2572 99.74 . . . . 0.1770 . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 2.48 2.83  . . 165 2448 99.77 . . . . 0.1822 . . . . . . . . . . . 0.2444 
'X-RAY DIFFRACTION' 2.83 3.57  . . 126 2499 99.39 . . . . 0.1500 . . . . . . . . . . . 0.1645 
'X-RAY DIFFRACTION' 3.57 20.07 . . 174 2440 99.58 . . . . 0.1175 . . . . . . . . . . . 0.1728 
# 
_struct.entry_id                     8VLF 
_struct.title                        'Crystal structure of Ash1L PHD finger in complex with histone H3K4me3' 
_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        8VLF 
_struct_keywords.text            'Ash1L, H3K4me2, zinc finger, transcriptional regulation, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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 ASH1L_HUMAN Q9NR48 ? 1 DVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDRE 2584 
2 UNP H3C_HUMAN   Q6NXT2 ? 2 ARTKQTARKSTG                                          2    
# 
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 8VLF A 4 ? 56 ? Q9NR48 2584 ? 2636 ? 4 56 
2 1 8VLF B 4 ? 56 ? Q9NR48 2584 ? 2636 ? 4 56 
3 2 8VLF P 1 ? 12 ? Q6NXT2 2    ? 13   ? 1 12 
4 2 8VLF T 1 ? 12 ? Q6NXT2 2    ? 13   ? 1 12 
# 
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 8VLF GLY A 1 ? UNP Q9NR48 ? ? 'expression tag' 1 1 
1 8VLF PRO A 2 ? UNP Q9NR48 ? ? 'expression tag' 2 2 
1 8VLF LEU A 3 ? UNP Q9NR48 ? ? 'expression tag' 3 3 
2 8VLF GLY B 1 ? UNP Q9NR48 ? ? 'expression tag' 1 4 
2 8VLF PRO B 2 ? UNP Q9NR48 ? ? 'expression tag' 2 5 
2 8VLF LEU B 3 ? UNP Q9NR48 ? ? 'expression tag' 3 6 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 2810 ? 
1 MORE         -41  ? 
1 'SSA (A^2)'  8820 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 CYS A 31 ? GLY A 35 ? CYS A 31 GLY A 35 1 ? 5 
HELX_P HELX_P2 AA2 CYS B 31 ? GLY B 35 ? CYS B 31 GLY B 35 1 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? C THR 3  C   ? ? ? 1_555 C M3L 4 N  ? ? P THR 3  P M3L 4   1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale2  covale both ? C M3L 4  C   ? ? ? 1_555 C GLN 5 N  ? ? P M3L 4  P GLN 5   1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale3  covale both ? D THR 3  C   ? ? ? 1_555 D M3L 4 N  ? ? T THR 3  T M3L 4   1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale4  covale both ? D M3L 4  C   ? ? ? 1_555 D GLN 5 N  ? ? T M3L 4  T GLN 5   1_555 ? ? ? ? ? ? ? 1.327 ? ? 
metalc1  metalc ?    ? A CYS 8  SG  ? ? ? 1_555 F ZN  . ZN ? ? A CYS 8  A ZN  102 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc2  metalc ?    ? A CYS 10 SG  ? ? ? 1_555 F ZN  . ZN ? ? A CYS 10 A ZN  102 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc3  metalc ?    ? A CYS 22 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 22 A ZN  101 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc4  metalc ?    ? A CYS 25 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 25 A ZN  101 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc5  metalc ?    ? A HIS 30 ND1 ? ? ? 1_555 F ZN  . ZN ? ? A HIS 30 A ZN  102 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc6  metalc ?    ? A CYS 33 SG  ? ? ? 1_555 F ZN  . ZN ? ? A CYS 33 A ZN  102 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc7  metalc ?    ? A CYS 45 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 45 A ZN  101 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc8  metalc ?    ? A CYS 48 SG  ? ? ? 1_555 E ZN  . ZN ? ? A CYS 48 A ZN  101 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc9  metalc ?    ? B CYS 8  SG  ? ? ? 1_555 G ZN  . ZN ? ? B CYS 8  B ZN  101 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc10 metalc ?    ? B CYS 10 SG  ? ? ? 1_555 G ZN  . ZN ? ? B CYS 10 B ZN  101 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc11 metalc ?    ? B CYS 22 SG  ? ? ? 1_555 H ZN  . ZN ? ? B CYS 22 B ZN  102 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc12 metalc ?    ? B CYS 25 SG  ? ? ? 1_555 H ZN  . ZN ? ? B CYS 25 B ZN  102 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc13 metalc ?    ? B HIS 30 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 30 B ZN  101 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc14 metalc ?    ? B CYS 33 SG  ? ? ? 1_555 G ZN  . ZN ? ? B CYS 33 B ZN  101 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc15 metalc ?    ? B CYS 45 SG  ? ? ? 1_555 H ZN  . ZN ? ? B CYS 45 B ZN  102 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc16 metalc ?    ? B CYS 48 SG  ? ? ? 1_555 H ZN  . ZN ? ? B CYS 48 B ZN  102 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 8  ? A CYS 8  ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 SG  ? A CYS 10 ? A CYS 10 ? 1_555 113.4 ? 
2  SG  ? A CYS 8  ? A CYS 8  ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 ND1 ? A HIS 30 ? A HIS 30 ? 1_555 103.5 ? 
3  SG  ? A CYS 10 ? A CYS 10 ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 ND1 ? A HIS 30 ? A HIS 30 ? 1_555 101.6 ? 
4  SG  ? A CYS 8  ? A CYS 8  ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 SG  ? A CYS 33 ? A CYS 33 ? 1_555 108.9 ? 
5  SG  ? A CYS 10 ? A CYS 10 ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 SG  ? A CYS 33 ? A CYS 33 ? 1_555 114.9 ? 
6  ND1 ? A HIS 30 ? A HIS 30 ? 1_555 ZN ? F ZN . ? A ZN 102 ? 1_555 SG  ? A CYS 33 ? A CYS 33 ? 1_555 113.7 ? 
7  SG  ? A CYS 22 ? A CYS 22 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 25 ? A CYS 25 ? 1_555 107.7 ? 
8  SG  ? A CYS 22 ? A CYS 22 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 45 ? A CYS 45 ? 1_555 113.6 ? 
9  SG  ? A CYS 25 ? A CYS 25 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 45 ? A CYS 45 ? 1_555 108.0 ? 
10 SG  ? A CYS 22 ? A CYS 22 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 48 ? A CYS 48 ? 1_555 105.8 ? 
11 SG  ? A CYS 25 ? A CYS 25 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 48 ? A CYS 48 ? 1_555 114.6 ? 
12 SG  ? A CYS 45 ? A CYS 45 ? 1_555 ZN ? E ZN . ? A ZN 101 ? 1_555 SG  ? A CYS 48 ? A CYS 48 ? 1_555 107.2 ? 
13 SG  ? B CYS 8  ? B CYS 8  ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 SG  ? B CYS 10 ? B CYS 10 ? 1_555 113.6 ? 
14 SG  ? B CYS 8  ? B CYS 8  ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 ND1 ? B HIS 30 ? B HIS 30 ? 1_555 103.0 ? 
15 SG  ? B CYS 10 ? B CYS 10 ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 ND1 ? B HIS 30 ? B HIS 30 ? 1_555 101.9 ? 
16 SG  ? B CYS 8  ? B CYS 8  ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 SG  ? B CYS 33 ? B CYS 33 ? 1_555 108.9 ? 
17 SG  ? B CYS 10 ? B CYS 10 ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 SG  ? B CYS 33 ? B CYS 33 ? 1_555 115.0 ? 
18 ND1 ? B HIS 30 ? B HIS 30 ? 1_555 ZN ? G ZN . ? B ZN 101 ? 1_555 SG  ? B CYS 33 ? B CYS 33 ? 1_555 113.8 ? 
19 SG  ? B CYS 22 ? B CYS 22 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 25 ? B CYS 25 ? 1_555 107.1 ? 
20 SG  ? B CYS 22 ? B CYS 22 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 45 ? B CYS 45 ? 1_555 113.6 ? 
21 SG  ? B CYS 25 ? B CYS 25 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 45 ? B CYS 45 ? 1_555 107.6 ? 
22 SG  ? B CYS 22 ? B CYS 22 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 48 ? B CYS 48 ? 1_555 106.2 ? 
23 SG  ? B CYS 25 ? B CYS 25 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 48 ? B CYS 48 ? 1_555 115.3 ? 
24 SG  ? B CYS 45 ? B CYS 45 ? 1_555 ZN ? H ZN . ? B ZN 102 ? 1_555 SG  ? B CYS 48 ? B CYS 48 ? 1_555 107.3 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 M3L C 4 ? . . . . M3L P 4 ? 1_555 . . . . . . . LYS 1 M3L Methylation 'Named protein modification' 
2 M3L D 4 ? . . . . M3L T 4 ? 1_555 . . . . . . . LYS 1 M3L Methylation 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? 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 TRP A 28 ? HIS A 30 ? TRP A 28 HIS A 30 
AA1 2 MET A 19 ? GLN A 21 ? MET A 19 GLN A 21 
AA1 3 THR D 3  ? M3L D 4  ? THR T 3  M3L T 4  
AA2 1 TRP B 28 ? HIS B 30 ? TRP B 28 HIS B 30 
AA2 2 MET B 19 ? GLN B 21 ? MET B 19 GLN B 21 
AA2 3 THR C 3  ? M3L C 4  ? THR P 3  M3L P 4  
# 
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 GLN A 29 ? O GLN A 29 N ILE A 20 ? N ILE A 20 
AA1 2 3 N MET A 19 ? N MET A 19 O M3L D 4  ? O M3L T 4  
AA2 1 2 O GLN B 29 ? O GLN B 29 N ILE B 20 ? N ILE B 20 
AA2 2 3 N MET B 19 ? N MET B 19 O M3L C 4  ? O M3L P 4  
# 
_pdbx_entry_details.entry_id                   8VLF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA P 7 ? ? -108.00 57.36 
2 1 ALA T 7 ? ? -111.94 60.77 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C M3L 4 P M3L 4 ? LYS 'modified residue' 
2 D M3L 4 T M3L 4 ? LYS 'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -y,x,z+3/4  
3 y,-x,z+1/4  
4 -x,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASP 54 ? A ASP 54 
2 1 Y 1 A ARG 55 ? A ARG 55 
3 1 Y 1 A GLU 56 ? A GLU 56 
4 1 Y 1 B ASP 54 ? B ASP 54 
5 1 Y 1 B ARG 55 ? B ARG 55 
6 1 Y 1 B GLU 56 ? B GLU 56 
# 
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 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
M3L N    N  N N 230 
M3L CA   C  N S 231 
M3L CB   C  N N 232 
M3L CG   C  N N 233 
M3L CD   C  N N 234 
M3L CE   C  N N 235 
M3L NZ   N  N N 236 
M3L C    C  N N 237 
M3L O    O  N N 238 
M3L OXT  O  N N 239 
M3L CM1  C  N N 240 
M3L CM2  C  N N 241 
M3L CM3  C  N N 242 
M3L H    H  N N 243 
M3L H2   H  N N 244 
M3L HA   H  N N 245 
M3L HB2  H  N N 246 
M3L HB3  H  N N 247 
M3L HG2  H  N N 248 
M3L HG3  H  N N 249 
M3L HD2  H  N N 250 
M3L HD3  H  N N 251 
M3L HE2  H  N N 252 
M3L HE3  H  N N 253 
M3L HXT  H  N N 254 
M3L HM11 H  N N 255 
M3L HM12 H  N N 256 
M3L HM13 H  N N 257 
M3L HM21 H  N N 258 
M3L HM22 H  N N 259 
M3L HM23 H  N N 260 
M3L HM31 H  N N 261 
M3L HM32 H  N N 262 
M3L HM33 H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
ZN  ZN   ZN N N 402 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
M3L N   CA   sing N N 218 
M3L N   H    sing N N 219 
M3L N   H2   sing N N 220 
M3L CA  CB   sing N N 221 
M3L CA  C    sing N N 222 
M3L CA  HA   sing N N 223 
M3L CB  CG   sing N N 224 
M3L CB  HB2  sing N N 225 
M3L CB  HB3  sing N N 226 
M3L CG  CD   sing N N 227 
M3L CG  HG2  sing N N 228 
M3L CG  HG3  sing N N 229 
M3L CD  CE   sing N N 230 
M3L CD  HD2  sing N N 231 
M3L CD  HD3  sing N N 232 
M3L CE  NZ   sing N N 233 
M3L CE  HE2  sing N N 234 
M3L CE  HE3  sing N N 235 
M3L NZ  CM1  sing N N 236 
M3L NZ  CM2  sing N N 237 
M3L NZ  CM3  sing N N 238 
M3L C   O    doub N N 239 
M3L C   OXT  sing N N 240 
M3L OXT HXT  sing N N 241 
M3L CM1 HM11 sing N N 242 
M3L CM1 HM12 sing N N 243 
M3L CM1 HM13 sing N N 244 
M3L CM2 HM21 sing N N 245 
M3L CM2 HM22 sing N N 246 
M3L CM2 HM23 sing N N 247 
M3L CM3 HM31 sing N N 248 
M3L CM3 HM32 sing N N 249 
M3L CM3 HM33 sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PRO N   CA   sing N N 270 
PRO N   CD   sing N N 271 
PRO N   H    sing N N 272 
PRO CA  C    sing N N 273 
PRO CA  CB   sing N N 274 
PRO CA  HA   sing N N 275 
PRO C   O    doub N N 276 
PRO C   OXT  sing N N 277 
PRO CB  CG   sing N N 278 
PRO CB  HB2  sing N N 279 
PRO CB  HB3  sing N N 280 
PRO CG  CD   sing N N 281 
PRO CG  HG2  sing N N 282 
PRO CG  HG3  sing N N 283 
PRO CD  HD2  sing N N 284 
PRO CD  HD3  sing N N 285 
PRO OXT HXT  sing N N 286 
SER N   CA   sing N N 287 
SER N   H    sing N N 288 
SER N   H2   sing N N 289 
SER CA  C    sing N N 290 
SER CA  CB   sing N N 291 
SER CA  HA   sing N N 292 
SER C   O    doub N N 293 
SER C   OXT  sing N N 294 
SER CB  OG   sing N N 295 
SER CB  HB2  sing N N 296 
SER CB  HB3  sing N N 297 
SER OG  HG   sing N N 298 
SER OXT HXT  sing N N 299 
THR N   CA   sing N N 300 
THR N   H    sing N N 301 
THR N   H2   sing N N 302 
THR CA  C    sing N N 303 
THR CA  CB   sing N N 304 
THR CA  HA   sing N N 305 
THR C   O    doub N N 306 
THR C   OXT  sing N N 307 
THR CB  OG1  sing N N 308 
THR CB  CG2  sing N N 309 
THR CB  HB   sing N N 310 
THR OG1 HG1  sing N N 311 
THR CG2 HG21 sing N N 312 
THR CG2 HG22 sing N N 313 
THR CG2 HG23 sing N N 314 
THR OXT HXT  sing N N 315 
TRP N   CA   sing N N 316 
TRP N   H    sing N N 317 
TRP N   H2   sing N N 318 
TRP CA  C    sing N N 319 
TRP CA  CB   sing N N 320 
TRP CA  HA   sing N N 321 
TRP C   O    doub N N 322 
TRP C   OXT  sing N N 323 
TRP CB  CG   sing N N 324 
TRP CB  HB2  sing N N 325 
TRP CB  HB3  sing N N 326 
TRP CG  CD1  doub Y N 327 
TRP CG  CD2  sing Y N 328 
TRP CD1 NE1  sing Y N 329 
TRP CD1 HD1  sing N N 330 
TRP CD2 CE2  doub Y N 331 
TRP CD2 CE3  sing Y N 332 
TRP NE1 CE2  sing Y N 333 
TRP NE1 HE1  sing N N 334 
TRP CE2 CZ2  sing Y N 335 
TRP CE3 CZ3  doub Y N 336 
TRP CE3 HE3  sing N N 337 
TRP CZ2 CH2  doub Y N 338 
TRP CZ2 HZ2  sing N N 339 
TRP CZ3 CH2  sing Y N 340 
TRP CZ3 HZ3  sing N N 341 
TRP CH2 HH2  sing N N 342 
TRP OXT HXT  sing N N 343 
TYR N   CA   sing N N 344 
TYR N   H    sing N N 345 
TYR N   H2   sing N N 346 
TYR CA  C    sing N N 347 
TYR CA  CB   sing N N 348 
TYR CA  HA   sing N N 349 
TYR C   O    doub N N 350 
TYR C   OXT  sing N N 351 
TYR CB  CG   sing N N 352 
TYR CB  HB2  sing N N 353 
TYR CB  HB3  sing N N 354 
TYR CG  CD1  doub Y N 355 
TYR CG  CD2  sing Y N 356 
TYR CD1 CE1  sing Y N 357 
TYR CD1 HD1  sing N N 358 
TYR CD2 CE2  doub Y N 359 
TYR CD2 HD2  sing N N 360 
TYR CE1 CZ   doub Y N 361 
TYR CE1 HE1  sing N N 362 
TYR CE2 CZ   sing Y N 363 
TYR CE2 HE2  sing N N 364 
TYR CZ  OH   sing N N 365 
TYR OH  HH   sing N N 366 
TYR OXT HXT  sing N N 367 
VAL N   CA   sing N N 368 
VAL N   H    sing N N 369 
VAL N   H2   sing N N 370 
VAL CA  C    sing N N 371 
VAL CA  CB   sing N N 372 
VAL CA  HA   sing N N 373 
VAL C   O    doub N N 374 
VAL C   OXT  sing N N 375 
VAL CB  CG1  sing N N 376 
VAL CB  CG2  sing N N 377 
VAL CB  HB   sing N N 378 
VAL CG1 HG11 sing N N 379 
VAL CG1 HG12 sing N N 380 
VAL CG1 HG13 sing N N 381 
VAL CG2 HG21 sing N N 382 
VAL CG2 HG22 sing N N 383 
VAL CG2 HG23 sing N N 384 
VAL OXT HXT  sing N N 385 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_space_group.name_H-M_alt     'P 43' 
_space_group.name_Hall        'P 4cw' 
_space_group.IT_number        78 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8VLF 
_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]   0.020080 
_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]   0.020080 
_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]   0.021603 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLY A 1 1  ? 27.01846 14.46860  28.64095 0.600 29.31853  ? 1   GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1  ? 27.49285 14.72311  27.29219 0.602 29.19602  ? 1   GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1  ? 26.69558 13.99775  26.22487 0.697 29.10466  ? 1   GLY A C   1 
ATOM   4    O  O   . GLY A 1 1  ? 25.65753 13.42560  26.52085 0.876 28.22240  ? 1   GLY A O   1 
ATOM   5    N  N   . PRO A 1 2  ? 27.20468 14.01660  24.98978 0.770 29.88861  ? 2   PRO A N   1 
ATOM   6    C  CA  . PRO A 1 2  ? 26.46257 13.43471  23.85083 0.841 30.99206  ? 2   PRO A CA  1 
ATOM   7    C  C   . PRO A 1 2  ? 25.98260 12.00759  24.06278 1.000 32.11466  ? 2   PRO A C   1 
ATOM   8    O  O   . PRO A 1 2  ? 24.88900 11.64436  23.60918 0.727 32.42239  ? 2   PRO A O   1 
ATOM   9    C  CB  . PRO A 1 2  ? 27.49286 13.49207  22.71615 0.784 31.05090  ? 2   PRO A CB  1 
ATOM   10   C  CG  . PRO A 1 2  ? 28.37654 14.63265  23.06489 1.000 31.09101  ? 2   PRO A CG  1 
ATOM   11   C  CD  . PRO A 1 2  ? 28.39964 14.76373  24.56204 0.815 30.08268  ? 2   PRO A CD  1 
ATOM   12   N  N   . LEU A 1 3  ? 26.78587 11.18592  24.73810 0.731 31.09448  ? 3   LEU A N   1 
ATOM   13   C  CA  . LEU A 1 3  ? 26.47234 9.78029   24.94392 0.904 31.39773  ? 3   LEU A CA  1 
ATOM   14   C  C   . LEU A 1 3  ? 25.49244 9.55950   26.08746 0.551 29.39613  ? 3   LEU A C   1 
ATOM   15   O  O   . LEU A 1 3  ? 24.95890 8.45272   26.22024 0.929 30.76071  ? 3   LEU A O   1 
ATOM   16   C  CB  . LEU A 1 3  ? 27.76516 9.02059   25.24284 1.000 32.76085  ? 3   LEU A CB  1 
ATOM   17   C  CG  . LEU A 1 3  ? 28.81939 9.10244   24.13941 0.287 33.80316  ? 3   LEU A CG  1 
ATOM   18   C  CD1 . LEU A 1 3  ? 30.19083 8.65541   24.63703 0.709 34.20345  ? 3   LEU A CD1 1 
ATOM   19   C  CD2 . LEU A 1 3  ? 28.36828 8.26993   22.95615 0.870 34.21766  ? 3   LEU A CD2 1 
ATOM   20   N  N   . ASP A 1 4  ? 25.25617 10.57321  26.91915 0.926 25.69015  ? 4   ASP A N   1 
ATOM   21   C  CA  . ASP A 1 4  ? 24.32347 10.46169  28.02973 1.000 23.39746  ? 4   ASP A CA  1 
ATOM   22   C  C   . ASP A 1 4  ? 22.96623 10.94713  27.55464 0.864 22.66358  ? 4   ASP A C   1 
ATOM   23   O  O   . ASP A 1 4  ? 22.87251 11.95249  26.84540 0.467 23.90132  ? 4   ASP A O   1 
ATOM   24   C  CB  . ASP A 1 4  ? 24.77926 11.33483  29.19808 0.871 23.94498  ? 4   ASP A CB  1 
ATOM   25   C  CG  . ASP A 1 4  ? 26.19210 11.02240  29.64108 0.652 24.63870  ? 4   ASP A CG  1 
ATOM   26   O  OD1 . ASP A 1 4  ? 26.54701 9.82804   29.69982 0.653 25.09071  ? 4   ASP A OD1 1 
ATOM   27   O  OD2 . ASP A 1 4  ? 26.94591 11.97505  29.93976 0.529 25.34051  ? 4   ASP A OD2 1 
ATOM   28   N  N   . VAL A 1 5  ? 21.91530 10.23085  27.93391 1.000 19.45623  ? 5   VAL A N   1 
ATOM   29   C  CA  . VAL A 1 5  ? 20.55740 10.56789  27.50981 1.000 17.64447  ? 5   VAL A CA  1 
ATOM   30   C  C   . VAL A 1 5  ? 19.85541 11.23371  28.67854 0.959 16.68763  ? 5   VAL A C   1 
ATOM   31   O  O   . VAL A 1 5  ? 19.77719 10.66196  29.76909 1.000 17.40886  ? 5   VAL A O   1 
ATOM   32   C  CB  . VAL A 1 5  ? 19.76737 9.33401   27.04414 1.000 18.17849  ? 5   VAL A CB  1 
ATOM   33   C  CG1 . VAL A 1 5  ? 18.33087 9.73556   26.69151 1.000 19.03632  ? 5   VAL A CG1 1 
ATOM   34   C  CG2 . VAL A 1 5  ? 20.44732 8.68167   25.83349 1.000 19.62706  ? 5   VAL A CG2 1 
ATOM   35   N  N   . ILE A 1 6  ? 19.34909 12.43881  28.45769 1.000 15.96212  ? 6   ILE A N   1 
ATOM   36   C  CA  . ILE A 1 6  ? 18.49601 13.12452  29.41991 1.000 15.11685  ? 6   ILE A CA  1 
ATOM   37   C  C   . ILE A 1 6  ? 17.05264 12.83307  29.02793 1.000 14.47097  ? 6   ILE A C   1 
ATOM   38   O  O   . ILE A 1 6  ? 16.63947 13.11857  27.89959 1.000 16.49670  ? 6   ILE A O   1 
ATOM   39   C  CB  . ILE A 1 6  ? 18.77397 14.63753  29.44168 1.000 16.14209  ? 6   ILE A CB  1 
ATOM   40   C  CG1 . ILE A 1 6  ? 20.21332 14.90655  29.90320 0.799 16.19270  ? 6   ILE A CG1 1 
ATOM   41   C  CG2 . ILE A 1 6  ? 17.77571 15.34927  30.35285 0.982 16.69396  ? 6   ILE A CG2 1 
ATOM   42   C  CD1 . ILE A 1 6  ? 20.60287 16.36677  29.89033 0.656 16.98952  ? 6   ILE A CD1 1 
ATOM   43   N  N   . ARG A 1 7  ? 16.27859 12.24856  29.93627 1.000 13.54641  ? 7   ARG A N   1 
ATOM   44   C  CA  . ARG A 1 7  ? 14.84849 12.04724  29.67242 1.000 13.64346  ? 7   ARG A CA  1 
ATOM   45   C  C   . ARG A 1 7  ? 14.11902 12.21969  30.99506 0.901 14.88316  ? 7   ARG A C   1 
ATOM   46   O  O   . ARG A 1 7  ? 13.88140 11.24589  31.70657 1.000 15.80049  ? 7   ARG A O   1 
ATOM   47   C  CB  . ARG A 1 7  ? 14.52652 10.69774  29.05025 1.000 14.23830  ? 7   ARG A CB  1 
ATOM   48   C  CG  . ARG A 1 7  ? 13.09047 10.67996  28.53675 1.000 14.48504  ? 7   ARG A CG  1 
ATOM   49   C  CD  . ARG A 1 7  ? 12.51818 9.28781   28.37700 0.886 15.42492  ? 7   ARG A CD  1 
ATOM   50   N  NE  . ARG A 1 7  ? 12.47983 8.55187   29.63643 0.897 15.26931  ? 7   ARG A NE  1 
ATOM   51   C  CZ  . ARG A 1 7  ? 11.62605 8.78130   30.63886 0.835 14.95691  ? 7   ARG A CZ  1 
ATOM   52   N  NH1 . ARG A 1 7  ? 10.72815 9.75883   30.56056 0.809 16.08975  ? 7   ARG A NH1 1 
ATOM   53   N  NH2 . ARG A 1 7  ? 11.68146 8.03320   31.74358 0.860 16.53701  ? 7   ARG A NH2 1 
ATOM   54   N  N   . CYS A 1 8  ? 13.78266 13.45693  31.31649 1.000 15.70140  ? 8   CYS A N   1 
ATOM   55   C  CA  . CYS A 1 8  ? 13.10241 13.77763  32.55748 1.000 16.13282  ? 8   CYS A CA  1 
ATOM   56   C  C   . CYS A 1 8  ? 11.62154 13.99628  32.28317 0.935 17.40358  ? 8   CYS A C   1 
ATOM   57   O  O   . CYS A 1 8  ? 11.20959 14.21961  31.14414 1.000 18.80990  ? 8   CYS A O   1 
ATOM   58   C  CB  . CYS A 1 8  ? 13.72793 15.03244  33.17011 1.000 15.02033  ? 8   CYS A CB  1 
ATOM   59   S  SG  . CYS A 1 8  ? 13.16765 15.37147  34.82391 0.871 15.24389  ? 8   CYS A SG  1 
ATOM   60   N  N   . ILE A 1 9  ? 10.81582 13.95809  33.34988 1.000 17.70880  ? 9   ILE A N   1 
ATOM   61   C  CA  . ILE A 1 9  ? 9.38971  14.20469  33.17158 0.938 19.25587  ? 9   ILE A CA  1 
ATOM   62   C  C   . ILE A 1 9  ? 9.11320  15.61991  32.68437 0.939 19.49408  ? 9   ILE A C   1 
ATOM   63   O  O   . ILE A 1 9  ? 8.06418  15.86756  32.08251 0.625 21.31514  ? 9   ILE A O   1 
ATOM   64   C  CB  . ILE A 1 9  ? 8.57088  13.89829  34.44438 0.962 20.15306  ? 9   ILE A CB  1 
ATOM   65   C  CG1 . ILE A 1 9  ? 8.96574  14.83752  35.59317 0.900 19.83586  ? 9   ILE A CG1 1 
ATOM   66   C  CG2 . ILE A 1 9  ? 8.69720  12.42527  34.81553 0.458 20.85230  ? 9   ILE A CG2 1 
ATOM   67   C  CD1 . ILE A 1 9  ? 8.19068  14.60411  36.85532 0.342 20.33818  ? 9   ILE A CD1 1 
ATOM   68   N  N   . CYS A 1 10 ? 10.02561 16.56443  32.93688 1.000 19.44215  ? 10  CYS A N   1 
ATOM   69   C  CA  . CYS A 1 10 ? 9.82780  17.92907  32.45541 0.820 19.73426  ? 10  CYS A CA  1 
ATOM   70   C  C   . CYS A 1 10 ? 9.96703  18.04771  30.94330 1.000 20.55664  ? 10  CYS A C   1 
ATOM   71   O  O   . CYS A 1 10 ? 9.48689  19.03335  30.37860 1.000 22.96352  ? 10  CYS A O   1 
ATOM   72   C  CB  . CYS A 1 10 ? 10.78630 18.89521  33.15596 0.861 19.21610  ? 10  CYS A CB  1 
ATOM   73   S  SG  . CYS A 1 10 ? 12.52879 18.57334  32.73057 1.000 17.96871  ? 10  CYS A SG  1 
ATOM   74   N  N   . GLY A 1 11 ? 10.61703 17.08751  30.27645 1.000 18.51716  ? 11  GLY A N   1 
ATOM   75   C  CA  . GLY A 1 11 ? 10.73986 17.14744  28.83208 1.000 18.94551  ? 11  GLY A CA  1 
ATOM   76   C  C   . GLY A 1 11 ? 11.74698 18.14903  28.32161 1.000 18.86238  ? 11  GLY A C   1 
ATOM   77   O  O   . GLY A 1 11 ? 11.82561 18.35705  27.10983 0.796 20.14624  ? 11  GLY A O   1 
ATOM   78   N  N   . LEU A 1 12 ? 12.51948 18.78541  29.20655 0.934 17.85263  ? 12  LEU A N   1 
ATOM   79   C  CA  . LEU A 1 12 ? 13.55096 19.73306  28.80357 1.000 18.33126  ? 12  LEU A CA  1 
ATOM   80   C  C   . LEU A 1 12 ? 14.88134 19.00063  28.75196 1.000 18.04833  ? 12  LEU A C   1 
ATOM   81   O  O   . LEU A 1 12 ? 15.29788 18.39697  29.74660 1.000 18.01962  ? 12  LEU A O   1 
ATOM   82   C  CB  . LEU A 1 12 ? 13.63490 20.91031  29.77223 1.000 20.84346  ? 12  LEU A CB  1 
ATOM   83   C  CG  . LEU A 1 12 ? 12.45077 21.87267  29.67573 0.763 21.45054  ? 12  LEU A CG  1 
ATOM   84   C  CD1 . LEU A 1 12 ? 12.52956 22.92515  30.77395 0.813 22.14696  ? 12  LEU A CD1 1 
ATOM   85   C  CD2 . LEU A 1 12 ? 12.36971 22.53328  28.30274 0.574 21.75385  ? 12  LEU A CD2 1 
ATOM   86   N  N   . TYR A 1 13 ? 15.54475 19.05847  27.59617 0.938 18.43777  ? 13  TYR A N   1 
ATOM   87   C  CA  . TYR A 1 13 ? 16.84082 18.41454  27.39681 1.000 18.69717  ? 13  TYR A CA  1 
ATOM   88   C  C   . TYR A 1 13 ? 17.90986 19.37401  27.89347 0.797 19.21264  ? 13  TYR A C   1 
ATOM   89   O  O   . TYR A 1 13 ? 18.60951 20.03383  27.13015 0.696 19.45970  ? 13  TYR A O   1 
ATOM   90   C  CB  . TYR A 1 13 ? 17.05040 18.02123  25.93183 1.000 18.77606  ? 13  TYR A CB  1 
ATOM   91   C  CG  . TYR A 1 13 ? 18.01488 16.86325  25.81800 1.000 18.16846  ? 13  TYR A CG  1 
ATOM   92   C  CD1 . TYR A 1 13 ? 19.39032 17.05425  25.94850 0.847 18.33397  ? 13  TYR A CD1 1 
ATOM   93   C  CD2 . TYR A 1 13 ? 17.54610 15.56273  25.64495 1.000 17.64566  ? 13  TYR A CD2 1 
ATOM   94   C  CE1 . TYR A 1 13 ? 20.26379 15.98215  25.87293 0.832 18.33028  ? 13  TYR A CE1 1 
ATOM   95   C  CE2 . TYR A 1 13 ? 18.41501 14.48326  25.56216 1.000 17.94761  ? 13  TYR A CE2 1 
ATOM   96   C  CZ  . TYR A 1 13 ? 19.76778 14.69679  25.69526 1.000 18.84940  ? 13  TYR A CZ  1 
ATOM   97   O  OH  . TYR A 1 13 ? 20.61905 13.62360  25.63447 0.713 20.91135  ? 13  TYR A OH  1 
ATOM   98   N  N   . LYS A 1 14 ? 18.02930 19.47337  29.20115 1.000 20.39843  ? 14  LYS A N   1 
ATOM   99   C  CA  . LYS A 1 14 ? 19.05176 20.34934  29.74568 0.776 21.67525  ? 14  LYS A CA  1 
ATOM   100  C  C   . LYS A 1 14 ? 19.73198 19.71288  30.94473 0.848 19.38038  ? 14  LYS A C   1 
ATOM   101  O  O   . LYS A 1 14 ? 19.08904 19.07785  31.79062 1.000 20.98037  ? 14  LYS A O   1 
ATOM   102  C  CB  . LYS A 1 14 ? 18.55219 21.75051  30.08767 0.742 24.96912  ? 14  LYS A CB  1 
ATOM   103  C  CG  . LYS A 1 14 ? 17.55050 21.82938  31.18580 0.645 27.11768  ? 14  LYS A CG  1 
ATOM   104  C  CD  . LYS A 1 14 ? 17.17041 23.28737  31.33660 0.699 28.57301  ? 14  LYS A CD  1 
ATOM   105  C  CE  . LYS A 1 14 ? 16.18660 23.46238  32.44026 0.466 28.60752  ? 14  LYS A CE  1 
ATOM   106  N  NZ  . LYS A 1 14 ? 15.70200 24.83614  32.73574 0.339 28.80073  ? 14  LYS A NZ  1 
ATOM   107  N  N   . ASP A 1 15 ? 21.04861 19.88269  30.98997 0.751 19.28090  ? 15  ASP A N   1 
ATOM   108  C  CA  . ASP A 1 15 ? 21.88950 19.43886  32.09269 1.000 22.56535  ? 15  ASP A CA  1 
ATOM   109  C  C   . ASP A 1 15 ? 21.88370 20.57432  33.10694 0.821 23.97530  ? 15  ASP A C   1 
ATOM   110  O  O   . ASP A 1 15 ? 22.55548 21.59039  32.92195 0.619 24.70751  ? 15  ASP A O   1 
ATOM   111  C  CB  . ASP A 1 15 ? 23.28377 19.17832  31.53954 0.777 24.25290  ? 15  ASP A CB  1 
ATOM   112  C  CG  . ASP A 1 15 ? 24.23850 18.64945  32.58733 0.639 25.56733  ? 15  ASP A CG  1 
ATOM   113  O  OD1 . ASP A 1 15 ? 23.77784 18.14082  33.62374 0.581 25.33965  ? 15  ASP A OD1 1 
ATOM   114  O  OD2 . ASP A 1 15 ? 25.46546 18.76290  32.35615 0.492 26.87545  ? 15  ASP A OD2 1 
ATOM   115  N  N   . GLU A 1 16 ? 21.10763 20.41360  34.17768 1.000 24.00817  ? 16  GLU A N   1 
ATOM   116  C  CA  . GLU A 1 16 ? 20.98200 21.44724  35.19487 1.000 25.99623  ? 16  GLU A CA  1 
ATOM   117  C  C   . GLU A 1 16 ? 20.77865 20.79915  36.55221 1.000 25.03570  ? 16  GLU A C   1 
ATOM   118  O  O   . GLU A 1 16 ? 19.99043 19.85872  36.68479 1.000 25.49946  ? 16  GLU A O   1 
ATOM   119  C  CB  . GLU A 1 16 ? 19.81279 22.40270  34.91392 0.641 28.43382  ? 16  GLU A CB  1 
ATOM   120  C  CG  . GLU A 1 16 ? 19.39571 23.22589  36.13135 0.556 30.55142  ? 16  GLU A CG  1 
ATOM   121  C  CD  . GLU A 1 16 ? 17.98611 23.77677  36.03284 0.464 32.07535  ? 16  GLU A CD  1 
ATOM   122  O  OE1 . GLU A 1 16 ? 17.30098 23.91065  37.07268 0.599 32.67037  ? 16  GLU A OE1 1 
ATOM   123  O  OE2 . GLU A 1 16 ? 17.59012 24.14650  34.91439 0.513 32.43050  ? 16  GLU A OE2 1 
ATOM   124  N  N   . GLY A 1 17 ? 21.49132 21.31005  37.55181 1.000 23.56840  ? 17  GLY A N   1 
ATOM   125  C  CA  . GLY A 1 17 ? 21.26092 20.90447  38.92101 0.815 22.43592  ? 17  GLY A CA  1 
ATOM   126  C  C   . GLY A 1 17 ? 21.72485 19.48168  39.17452 1.000 21.08429  ? 17  GLY A C   1 
ATOM   127  O  O   . GLY A 1 17 ? 22.43603 18.85895  38.37973 0.640 20.30158  ? 17  GLY A O   1 
ATOM   128  N  N   . LEU A 1 18 ? 21.28982 18.96488  40.31746 0.757 20.52153  ? 18  LEU A N   1 
ATOM   129  C  CA  . LEU A 1 18 ? 21.54001 17.57215  40.64928 1.000 20.82286  ? 18  LEU A CA  1 
ATOM   130  C  C   . LEU A 1 18 ? 20.67246 16.67471  39.77469 1.000 20.61423  ? 18  LEU A C   1 
ATOM   131  O  O   . LEU A 1 18 ? 19.44691 16.82551  39.71670 0.799 19.83218  ? 18  LEU A O   1 
ATOM   132  C  CB  . LEU A 1 18 ? 21.20241 17.31522  42.11273 0.707 22.81186  ? 18  LEU A CB  1 
ATOM   133  C  CG  . LEU A 1 18 ? 21.84341 16.08186  42.74592 0.671 23.31890  ? 18  LEU A CG  1 
ATOM   134  C  CD1 . LEU A 1 18 ? 23.34614 15.97024  42.46201 0.589 24.17033  ? 18  LEU A CD1 1 
ATOM   135  C  CD2 . LEU A 1 18 ? 21.55909 16.04965  44.23027 0.589 22.98275  ? 18  LEU A CD2 1 
ATOM   136  N  N   . MET A 1 19 ? 21.30281 15.71966  39.11943 0.878 19.38223  ? 19  MET A N   1 
ATOM   137  C  CA  . MET A 1 19 ? 20.59711 14.82379  38.22722 0.931 18.75768  ? 19  MET A CA  1 
ATOM   138  C  C   . MET A 1 19 ? 20.91202 13.40089  38.66509 0.784 17.98739  ? 19  MET A C   1 
ATOM   139  O  O   . MET A 1 19 ? 21.96256 13.13720  39.26067 0.666 18.98250  ? 19  MET A O   1 
ATOM   140  C  CB  . MET A 1 19 ? 21.06509 15.08009  36.79365 1.000 19.14841  ? 19  MET A CB  1 
ATOM   141  C  CG  . MET A 1 19 ? 20.62419 16.44385  36.28275 0.921 19.27901  ? 19  MET A CG  1 
ATOM   142  S  SD  . MET A 1 19 ? 20.74310 16.64601  34.50047 0.732 17.84853  ? 19  MET A SD  1 
ATOM   143  C  CE  . MET A 1 19 ? 19.34610 15.68220  33.92641 0.934 18.97957  ? 19  MET A CE  1 
ATOM   144  N  N   . ILE A 1 20 ? 19.99365 12.48593  38.37569 0.785 17.84670  ? 20  ILE A N   1 
ATOM   145  C  CA  . ILE A 1 20 ? 20.07254 11.11085  38.85535 0.756 18.39064  ? 20  ILE A CA  1 
ATOM   146  C  C   . ILE A 1 20 ? 19.80178 10.17919  37.68345 0.819 18.74196  ? 20  ILE A C   1 
ATOM   147  O  O   . ILE A 1 20 ? 18.98620 10.49233  36.81132 0.769 16.86927  ? 20  ILE A O   1 
ATOM   148  C  CB  . ILE A 1 20 ? 19.09404 10.87603  40.03664 1.000 21.11756  ? 20  ILE A CB  1 
ATOM   149  C  CG1 . ILE A 1 20 ? 19.32278 9.50648   40.68605 1.000 21.94118  ? 20  ILE A CG1 1 
ATOM   150  C  CG2 . ILE A 1 20 ? 17.63596 11.09613  39.60060 1.000 21.16133  ? 20  ILE A CG2 1 
ATOM   151  C  CD1 . ILE A 1 20 ? 18.73187 9.42347   42.08864 0.884 21.75543  ? 20  ILE A CD1 1 
ATOM   152  N  N   . GLN A 1 21 ? 20.49022 9.04498   37.65952 1.000 21.71472  ? 21  GLN A N   1 
ATOM   153  C  CA  . GLN A 1 21 ? 20.40455 8.10428   36.55280 1.000 22.49046  ? 21  GLN A CA  1 
ATOM   154  C  C   . GLN A 1 21 ? 19.50221 6.92660   36.90832 1.000 22.86828  ? 21  GLN A C   1 
ATOM   155  O  O   . GLN A 1 21 ? 19.59336 6.36175   38.00325 1.000 24.29927  ? 21  GLN A O   1 
ATOM   156  C  CB  . GLN A 1 21 ? 21.79115 7.57642   36.18765 0.885 23.16260  ? 21  GLN A CB  1 
ATOM   157  C  CG  . GLN A 1 21 ? 21.76640 6.60906   35.01688 1.000 23.76002  ? 21  GLN A CG  1 
ATOM   158  C  CD  . GLN A 1 21 ? 23.15225 6.29284   34.50669 1.000 24.84305  ? 21  GLN A CD  1 
ATOM   159  O  OE1 . GLN A 1 21 ? 24.06189 5.97882   35.27896 0.594 24.36000  ? 21  GLN A OE1 1 
ATOM   160  N  NE2 . GLN A 1 21 ? 23.33543 6.40164   33.20324 0.784 24.06060  ? 21  GLN A NE2 1 
ATOM   161  N  N   . CYS A 1 22 ? 18.63285 6.55094   35.97609 1.000 23.53062  ? 22  CYS A N   1 
ATOM   162  C  CA  . CYS A 1 22 ? 17.83926 5.34222   36.14933 1.000 24.12705  ? 22  CYS A CA  1 
ATOM   163  C  C   . CYS A 1 22 ? 18.75282 4.12258   36.13041 0.857 24.80530  ? 22  CYS A C   1 
ATOM   164  O  O   . CYS A 1 22 ? 19.57911 3.96107   35.22173 0.887 25.54822  ? 22  CYS A O   1 
ATOM   165  C  CB  . CYS A 1 22 ? 16.77789 5.21932   35.04947 1.000 24.50890  ? 22  CYS A CB  1 
ATOM   166  S  SG  . CYS A 1 22 ? 15.71761 3.72963   35.24867 1.000 25.31524  ? 22  CYS A SG  1 
ATOM   167  N  N   . ASP A 1 23 ? 18.59839 3.25911   37.13992 0.979 27.08975  ? 23  ASP A N   1 
ATOM   168  C  CA  . ASP A 1 23 ? 19.45622 2.08484   37.25559 1.000 27.89486  ? 23  ASP A CA  1 
ATOM   169  C  C   . ASP A 1 23 ? 19.31778 1.14551   36.06810 1.000 28.09662  ? 23  ASP A C   1 
ATOM   170  O  O   . ASP A 1 23 ? 20.26334 0.41489   35.74982 0.738 29.75199  ? 23  ASP A O   1 
ATOM   171  C  CB  . ASP A 1 23 ? 19.10800 1.31356   38.52964 1.000 28.58837  ? 23  ASP A CB  1 
ATOM   172  C  CG  . ASP A 1 23 ? 19.62036 1.98880   39.77602 0.665 29.01197  ? 23  ASP A CG  1 
ATOM   173  O  OD1 . ASP A 1 23 ? 20.65325 2.68729   39.69097 0.564 29.28157  ? 23  ASP A OD1 1 
ATOM   174  O  OD2 . ASP A 1 23 ? 19.00035 1.78915   40.84044 0.614 29.57525  ? 23  ASP A OD2 1 
ATOM   175  N  N   . LYS A 1 24 ? 18.15042 1.12381   35.42469 0.836 26.88664  ? 24  LYS A N   1 
ATOM   176  C  CA  . LYS A 1 24 ? 17.84837 0.12907   34.39857 1.000 26.93434  ? 24  LYS A CA  1 
ATOM   177  C  C   . LYS A 1 24 ? 18.01436 0.66320   32.97704 1.000 26.73306  ? 24  LYS A C   1 
ATOM   178  O  O   . LYS A 1 24 ? 18.77686 0.09312   32.19209 0.669 27.38487  ? 24  LYS A O   1 
ATOM   179  C  CB  . LYS A 1 24 ? 16.43912 -0.43819  34.60952 1.000 27.91146  ? 24  LYS A CB  1 
ATOM   180  C  CG  . LYS A 1 24 ? 16.36471 -1.47459  35.72158 0.569 28.06435  ? 24  LYS A CG  1 
ATOM   181  C  CD  . LYS A 1 24 ? 16.97382 -2.80951  35.34076 0.776 28.50405  ? 24  LYS A CD  1 
ATOM   182  C  CE  . LYS A 1 24 ? 16.47059 -3.88735  36.27759 0.617 29.35442  ? 24  LYS A CE  1 
ATOM   183  N  NZ  . LYS A 1 24 ? 17.25932 -5.14143  36.14441 0.327 29.52904  ? 24  LYS A NZ  1 
ATOM   184  N  N   . CYS A 1 25 ? 17.29668 1.73222   32.61865 1.000 25.96502  ? 25  CYS A N   1 
ATOM   185  C  CA  . CYS A 1 25 ? 17.34206 2.26988   31.25918 1.000 24.87560  ? 25  CYS A CA  1 
ATOM   186  C  C   . CYS A 1 25 ? 18.41858 3.32913   31.05104 1.000 24.10124  ? 25  CYS A C   1 
ATOM   187  O  O   . CYS A 1 25 ? 18.67389 3.71534   29.90388 1.000 25.07591  ? 25  CYS A O   1 
ATOM   188  C  CB  . CYS A 1 25 ? 15.96198 2.79883   30.83635 1.000 23.28387  ? 25  CYS A CB  1 
ATOM   189  S  SG  . CYS A 1 25 ? 15.51047 4.37975   31.57367 0.948 23.41995  ? 25  CYS A SG  1 
ATOM   190  N  N   . MET A 1 26 ? 19.04372 3.81778   32.12109 1.000 23.49399  ? 26  MET A N   1 
ATOM   191  C  CA  . MET A 1 26 ? 20.21213 4.70558   32.08835 0.851 22.57451  ? 26  MET A CA  1 
ATOM   192  C  C   . MET A 1 26 ? 19.92998 6.15720   31.72097 1.000 20.68997  ? 26  MET A C   1 
ATOM   193  O  O   . MET A 1 26 ? 20.88559 6.93169   31.58924 0.812 20.73308  ? 26  MET A O   1 
ATOM   194  C  CB  . MET A 1 26 ? 21.40753 4.15165   31.29888 0.673 24.49176  ? 26  MET A CB  1 
ATOM   195  C  CG  . MET A 1 26 ? 21.59148 2.66266   31.52595 0.707 27.17455  ? 26  MET A CG  1 
ATOM   196  S  SD  . MET A 1 26 ? 22.22604 2.37942   33.19201 0.455 29.81000  ? 26  MET A SD  1 
ATOM   197  C  CE  . MET A 1 26 ? 23.82604 3.16964   33.10578 0.517 30.16192  ? 26  MET A CE  1 
ATOM   198  N  N   . VAL A 1 27 ? 18.66767 6.56148   31.55774 0.918 19.39006  ? 27  VAL A N   1 
ATOM   199  C  CA  . VAL A 1 27 ? 18.39611 7.97584   31.34513 1.000 18.27784  ? 27  VAL A CA  1 
ATOM   200  C  C   . VAL A 1 27 ? 18.69154 8.77841   32.60781 1.000 17.68502  ? 27  VAL A C   1 
ATOM   201  O  O   . VAL A 1 27 ? 18.68825 8.26592   33.73381 1.000 19.46688  ? 27  VAL A O   1 
ATOM   202  C  CB  . VAL A 1 27 ? 16.96779 8.23977   30.84601 1.000 18.24908  ? 27  VAL A CB  1 
ATOM   203  C  CG1 . VAL A 1 27 ? 16.68685 7.41822   29.62310 1.000 19.15745  ? 27  VAL A CG1 1 
ATOM   204  C  CG2 . VAL A 1 27 ? 15.93371 8.00525   31.94624 1.000 19.18065  ? 27  VAL A CG2 1 
ATOM   205  N  N   . TRP A 1 28 ? 18.95359 10.06183  32.40893 1.000 16.37514  ? 28  TRP A N   1 
ATOM   206  C  CA  . TRP A 1 28 ? 19.17697 11.00456  33.49346 1.000 16.06874  ? 28  TRP A CA  1 
ATOM   207  C  C   . TRP A 1 28 ? 17.95365 11.89531  33.66562 0.814 14.81358  ? 28  TRP A C   1 
ATOM   208  O  O   . TRP A 1 28 ? 17.33846 12.33767  32.68401 0.967 15.11157  ? 28  TRP A O   1 
ATOM   209  C  CB  . TRP A 1 28 ? 20.39830 11.86973  33.18109 1.000 18.46511  ? 28  TRP A CB  1 
ATOM   210  C  CG  . TRP A 1 28 ? 21.67926 11.10837  33.20807 1.000 19.14209  ? 28  TRP A CG  1 
ATOM   211  C  CD1 . TRP A 1 28 ? 22.25909 10.42741  32.16864 0.952 19.87022  ? 28  TRP A CD1 1 
ATOM   212  C  CD2 . TRP A 1 28 ? 22.54465 10.92478  34.33769 1.000 20.61743  ? 28  TRP A CD2 1 
ATOM   213  N  NE1 . TRP A 1 28 ? 23.42915 9.84925   32.58130 0.836 20.26677  ? 28  TRP A NE1 1 
ATOM   214  C  CE2 . TRP A 1 28 ? 23.62621 10.13389  33.90831 0.853 20.54088  ? 28  TRP A CE2 1 
ATOM   215  C  CE3 . TRP A 1 28 ? 22.50716 11.35283  35.67740 0.965 21.84192  ? 28  TRP A CE3 1 
ATOM   216  C  CZ2 . TRP A 1 28 ? 24.66266 9.76487   34.76585 0.870 21.51872  ? 28  TRP A CZ2 1 
ATOM   217  C  CZ3 . TRP A 1 28 ? 23.53199 10.98281  36.52002 0.918 22.98471  ? 28  TRP A CZ3 1 
ATOM   218  C  CH2 . TRP A 1 28 ? 24.59785 10.20189  36.06415 0.722 22.17230  ? 28  TRP A CH2 1 
ATOM   219  N  N   . GLN A 1 29 ? 17.60854 12.15824  34.91786 0.875 15.14106  ? 29  GLN A N   1 
ATOM   220  C  CA  . GLN A 1 29 ? 16.46120 12.97685  35.26205 1.000 15.66877  ? 29  GLN A CA  1 
ATOM   221  C  C   . GLN A 1 29 ? 16.88207 14.01048  36.30021 0.890 15.25170  ? 29  GLN A C   1 
ATOM   222  O  O   . GLN A 1 29 ? 17.85992 13.81689  37.02884 0.812 16.54298  ? 29  GLN A O   1 
ATOM   223  C  CB  . GLN A 1 29 ? 15.32865 12.10184  35.80464 1.000 16.54922  ? 29  GLN A CB  1 
ATOM   224  C  CG  . GLN A 1 29 ? 15.02608 10.90728  34.91093 0.912 16.98586  ? 29  GLN A CG  1 
ATOM   225  C  CD  . GLN A 1 29 ? 13.65912 10.30285  35.16106 0.875 15.90222  ? 29  GLN A CD  1 
ATOM   226  O  OE1 . GLN A 1 29 ? 13.39613 9.79711   36.24560 1.000 18.88912  ? 29  GLN A OE1 1 
ATOM   227  N  NE2 . GLN A 1 29 ? 12.77172 10.36185  34.16596 1.000 17.55814  ? 29  GLN A NE2 1 
ATOM   228  N  N   . HIS A 1 30 ? 16.15371 15.12733  36.35901 1.000 15.89306  ? 30  HIS A N   1 
ATOM   229  C  CA  . HIS A 1 30 ? 16.44524 16.14044  37.37058 1.000 16.73063  ? 30  HIS A CA  1 
ATOM   230  C  C   . HIS A 1 30 ? 15.87844 15.68495  38.70633 1.000 17.39833  ? 30  HIS A C   1 
ATOM   231  O  O   . HIS A 1 30 ? 14.69105 15.37055  38.81069 0.852 16.48443  ? 30  HIS A O   1 
ATOM   232  C  CB  . HIS A 1 30 ? 15.84668 17.49841  36.98710 1.000 16.71978  ? 30  HIS A CB  1 
ATOM   233  C  CG  . HIS A 1 30 ? 16.23998 17.96108  35.61741 1.000 16.38972  ? 30  HIS A CG  1 
ATOM   234  N  ND1 . HIS A 1 30 ? 15.33978 18.05465  34.57147 1.000 16.02275  ? 30  HIS A ND1 1 
ATOM   235  C  CD2 . HIS A 1 30 ? 17.44206 18.33229  35.11316 0.921 16.97171  ? 30  HIS A CD2 1 
ATOM   236  C  CE1 . HIS A 1 30 ? 15.97466 18.46252  33.48647 0.856 16.27473  ? 30  HIS A CE1 1 
ATOM   237  N  NE2 . HIS A 1 30 ? 17.24831 18.64763  33.78932 0.912 17.16615  ? 30  HIS A NE2 1 
ATOM   238  N  N   . CYS A 1 31 ? 16.72296 15.67333  39.73942 1.000 18.77208  ? 31  CYS A N   1 
ATOM   239  C  CA  . CYS A 1 31 ? 16.24565 15.26796  41.05976 1.000 20.52898  ? 31  CYS A CA  1 
ATOM   240  C  C   . CYS A 1 31 ? 15.05878 16.11294  41.51274 0.852 21.35861  ? 31  CYS A C   1 
ATOM   241  O  O   . CYS A 1 31 ? 14.09601 15.58693  42.08023 0.940 22.45339  ? 31  CYS A O   1 
ATOM   242  C  CB  . CYS A 1 31 ? 17.37668 15.35427  42.08272 0.857 21.90122  ? 31  CYS A CB  1 
ATOM   243  S  SG  . CYS A 1 31 ? 18.66502 14.14059  41.80238 0.684 21.16781  ? 31  CYS A SG  1 
ATOM   244  N  N   . ASP A 1 32 ? 15.09827 17.42280  41.25616 1.000 20.99585  ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32 ? 14.00174 18.28320  41.68715 0.863 20.37918  ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32 ? 12.69408 17.94541  40.97599 1.000 20.53154  ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32 ? 11.61986 17.98687  41.58892 0.714 20.74961  ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32 ? 14.36285 19.75077  41.47556 0.844 20.68735  ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32 ? 15.42576 20.23700  42.43961 0.638 21.14497  ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32 ? 15.68676 19.54010  43.44613 0.465 21.32461  ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32 ? 15.99002 21.31924  42.18641 0.471 22.41929  ? 32  ASP A OD2 1 
ATOM   252  N  N   . CYS A 1 33 ? 12.75514 17.63435  39.67654 1.000 19.63056  ? 33  CYS A N   1 
ATOM   253  C  CA  . CYS A 1 33 ? 11.53631 17.28305  38.95540 0.847 19.89376  ? 33  CYS A CA  1 
ATOM   254  C  C   . CYS A 1 33 ? 10.95944 15.98380  39.48272 0.815 20.45151  ? 33  CYS A C   1 
ATOM   255  O  O   . CYS A 1 33 ? 9.73525  15.80959  39.53233 0.611 20.81439  ? 33  CYS A O   1 
ATOM   256  C  CB  . CYS A 1 33 ? 11.83347 17.10994  37.46837 0.984 18.84147  ? 33  CYS A CB  1 
ATOM   257  S  SG  . CYS A 1 33 ? 12.34649 18.58107  36.60468 0.829 17.27567  ? 33  CYS A SG  1 
ATOM   258  N  N   . MET A 1 34 ? 11.82510 15.05503  39.87319 0.861 21.06997  ? 34  MET A N   1 
ATOM   259  C  CA  . MET A 1 34 ? 11.37633 13.73202  40.27572 0.842 22.82998  ? 34  MET A CA  1 
ATOM   260  C  C   . MET A 1 34 ? 11.13584 13.60147  41.77514 0.930 25.56997  ? 34  MET A C   1 
ATOM   261  O  O   . MET A 1 34 ? 10.65109 12.55606  42.21234 0.750 26.64675  ? 34  MET A O   1 
ATOM   262  C  CB  . MET A 1 34 ? 12.37332 12.65216  39.82945 1.000 21.83337  ? 34  MET A CB  1 
ATOM   263  C  CG  . MET A 1 34 ? 12.72202 12.63133  38.34872 1.000 20.86758  ? 34  MET A CG  1 
ATOM   264  S  SD  . MET A 1 34 ? 11.27855 12.64819  37.26236 0.773 20.30647  ? 34  MET A SD  1 
ATOM   265  C  CE  . MET A 1 34 ? 10.58530 11.01886  37.59094 0.800 21.43078  ? 34  MET A CE  1 
ATOM   266  N  N   . GLY A 1 35 ? 11.47793 14.61494  42.56994 1.000 28.47810  ? 35  GLY A N   1 
ATOM   267  C  CA  . GLY A 1 35 ? 11.24845 14.55358  44.00340 1.000 30.60158  ? 35  GLY A CA  1 
ATOM   268  C  C   . GLY A 1 35 ? 12.20319 13.68419  44.79920 1.000 32.41936  ? 35  GLY A C   1 
ATOM   269  O  O   . GLY A 1 35 ? 11.80901 13.14758  45.84072 0.713 32.87049  ? 35  GLY A O   1 
ATOM   270  N  N   . VAL A 1 36 ? 13.45870 13.55415  44.36629 1.000 33.16794  ? 36  VAL A N   1 
ATOM   271  C  CA  . VAL A 1 36 ? 14.46954 12.73374  45.03037 1.000 32.95640  ? 36  VAL A CA  1 
ATOM   272  C  C   . VAL A 1 36 ? 15.74201 13.55609  45.24425 1.000 33.91585  ? 36  VAL A C   1 
ATOM   273  O  O   . VAL A 1 36 ? 15.84628 14.70327  44.81256 0.573 32.82675  ? 36  VAL A O   1 
ATOM   274  C  CB  . VAL A 1 36 ? 14.78361 11.43862  44.25064 1.000 32.62168  ? 36  VAL A CB  1 
ATOM   275  C  CG1 . VAL A 1 36 ? 13.56412 10.54255  44.18621 0.692 32.18118  ? 36  VAL A CG1 1 
ATOM   276  C  CG2 . VAL A 1 36 ? 15.27170 11.76881  42.83983 1.000 32.21083  ? 36  VAL A CG2 1 
ATOM   277  N  N   . ASN A 1 37 ? 16.71690 12.94619  45.92566 0.598 36.07413  ? 37  ASN A N   1 
ATOM   278  C  CA  . ASN A 1 37 ? 18.03951 13.53816  46.11841 1.000 37.97144  ? 37  ASN A CA  1 
ATOM   279  C  C   . ASN A 1 37 ? 19.10427 12.44133  46.12287 0.655 38.04357  ? 37  ASN A C   1 
ATOM   280  O  O   . ASN A 1 37 ? 18.80518 11.25569  45.96302 0.913 37.73306  ? 37  ASN A O   1 
ATOM   281  C  CB  . ASN A 1 37 ? 18.07683 14.53506  47.29492 0.713 39.63556  ? 37  ASN A CB  1 
ATOM   282  C  CG  . ASN A 1 37 ? 18.00051 13.86333  48.66096 0.508 40.78040  ? 37  ASN A CG  1 
ATOM   283  O  OD1 . ASN A 1 37 ? 18.50082 12.76186  48.86429 0.741 41.03432  ? 37  ASN A OD1 1 
ATOM   284  N  ND2 . ASN A 1 37 ? 17.38996 14.55648  49.61811 0.643 41.53947  ? 37  ASN A ND2 1 
ATOM   285  N  N   . SER A 1 38 ? 20.36425 12.84502  46.31066 1.000 38.16199  ? 38  SER A N   1 
ATOM   286  C  CA  . SER A 1 38 ? 21.46679 11.89003  46.21766 0.610 37.24199  ? 38  SER A CA  1 
ATOM   287  C  C   . SER A 1 38 ? 21.51572 10.90628  47.38008 0.305 36.29381  ? 38  SER A C   1 
ATOM   288  O  O   . SER A 1 38 ? 22.45595 10.10646  47.45435 0.720 35.80444  ? 38  SER A O   1 
ATOM   289  C  CB  . SER A 1 38 ? 22.80459 12.62258  46.08997 0.727 37.19836  ? 38  SER A CB  1 
ATOM   290  O  OG  . SER A 1 38 ? 23.10955 13.33424  47.27645 0.534 37.26831  ? 38  SER A OG  1 
ATOM   291  N  N   . ASP A 1 39 ? 20.53863 10.92958  48.27981 1.000 35.67536  ? 39  ASP A N   1 
ATOM   292  C  CA  . ASP A 1 39 ? 20.55736 10.02750  49.42083 1.000 35.60552  ? 39  ASP A CA  1 
ATOM   293  C  C   . ASP A 1 39 ? 19.92005 8.67641   49.11912 1.000 34.49360  ? 39  ASP A C   1 
ATOM   294  O  O   . ASP A 1 39 ? 20.11841 7.73251   49.89223 0.708 34.96365  ? 39  ASP A O   1 
ATOM   295  C  CB  . ASP A 1 39 ? 19.85407 10.67219  50.61788 1.000 36.45124  ? 39  ASP A CB  1 
ATOM   296  C  CG  . ASP A 1 39 ? 20.58865 11.89310  51.13815 0.114 36.87926  ? 39  ASP A CG  1 
ATOM   297  O  OD1 . ASP A 1 39 ? 21.81662 11.99141  50.93013 0.340 37.16978  ? 39  ASP A OD1 1 
ATOM   298  O  OD2 . ASP A 1 39 ? 19.93097 12.76316  51.74572 0.296 37.06405  ? 39  ASP A OD2 1 
ATOM   299  N  N   . VAL A 1 40 ? 19.16082 8.55565   48.02533 1.000 32.49690  ? 40  VAL A N   1 
ATOM   300  C  CA  . VAL A 1 40 ? 18.48367 7.29549   47.73629 1.000 32.14045  ? 40  VAL A CA  1 
ATOM   301  C  C   . VAL A 1 40 ? 19.49705 6.25284   47.28927 0.901 32.88845  ? 40  VAL A C   1 
ATOM   302  O  O   . VAL A 1 40 ? 20.45657 6.55391   46.56305 0.754 33.97745  ? 40  VAL A O   1 
ATOM   303  C  CB  . VAL A 1 40 ? 17.35802 7.46918   46.69943 1.000 32.50087  ? 40  VAL A CB  1 
ATOM   304  C  CG1 . VAL A 1 40 ? 16.27446 8.38900   47.23488 0.808 33.08330  ? 40  VAL A CG1 1 
ATOM   305  C  CG2 . VAL A 1 40 ? 17.90874 7.97117   45.36815 0.673 32.29162  ? 40  VAL A CG2 1 
ATOM   306  N  N   . GLU A 1 41 ? 19.27307 5.00691   47.70633 1.000 32.85843  ? 41  GLU A N   1 
ATOM   307  C  CA  . GLU A 1 41 ? 20.21485 3.93407   47.40311 1.000 32.68620  ? 41  GLU A CA  1 
ATOM   308  C  C   . GLU A 1 41 ? 20.08979 3.46196   45.96271 0.773 32.87049  ? 41  GLU A C   1 
ATOM   309  O  O   . GLU A 1 41 ? 21.10038 3.19333   45.30457 0.674 34.53494  ? 41  GLU A O   1 
ATOM   310  C  CB  . GLU A 1 41 ? 20.01699 2.77531   48.37904 0.854 33.27123  ? 41  GLU A CB  1 
ATOM   311  C  CG  . GLU A 1 41 ? 21.22703 1.88169   48.50798 0.682 33.34788  ? 41  GLU A CG  1 
ATOM   312  C  CD  . GLU A 1 41 ? 20.95139 0.64716   49.34143 0.482 33.51936  ? 41  GLU A CD  1 
ATOM   313  O  OE1 . GLU A 1 41 ? 21.68588 -0.34974  49.18514 0.270 33.99352  ? 41  GLU A OE1 1 
ATOM   314  O  OE2 . GLU A 1 41 ? 20.01137 0.68085   50.16411 0.344 33.41739  ? 41  GLU A OE2 1 
ATOM   315  N  N   . HIS A 1 42 ? 18.86416 3.35004   45.46765 1.000 32.11548  ? 42  HIS A N   1 
ATOM   316  C  CA  . HIS A 1 42 ? 18.61949 2.94332   44.09291 1.000 31.94922  ? 42  HIS A CA  1 
ATOM   317  C  C   . HIS A 1 42 ? 17.57557 3.87344   43.49428 0.840 29.94245  ? 42  HIS A C   1 
ATOM   318  O  O   . HIS A 1 42 ? 16.79926 4.50973   44.21311 0.874 30.32927  ? 42  HIS A O   1 
ATOM   319  C  CB  . HIS A 1 42 ? 18.13616 1.49363   44.01933 0.616 33.26670  ? 42  HIS A CB  1 
ATOM   320  C  CG  . HIS A 1 42 ? 19.11396 0.50711   44.57346 0.536 34.50612  ? 42  HIS A CG  1 
ATOM   321  N  ND1 . HIS A 1 42 ? 20.36302 0.30634   44.02591 0.439 35.06273  ? 42  HIS A ND1 1 
ATOM   322  C  CD2 . HIS A 1 42 ? 19.02548 -0.33706  45.62854 0.576 35.49296  ? 42  HIS A CD2 1 
ATOM   323  C  CE1 . HIS A 1 42 ? 21.00168 -0.61905  44.72049 0.412 35.75699  ? 42  HIS A CE1 1 
ATOM   324  N  NE2 . HIS A 1 42 ? 20.21145 -1.02692  45.69686 0.572 36.24284  ? 42  HIS A NE2 1 
ATOM   325  N  N   . TYR A 1 43 ? 17.56259 3.96174   42.16476 1.000 29.49342  ? 43  TYR A N   1 
ATOM   326  C  CA  . TYR A 1 43 ? 16.62564 4.84622   41.48864 1.000 27.46993  ? 43  TYR A CA  1 
ATOM   327  C  C   . TYR A 1 43 ? 16.15189 4.22087   40.18653 1.000 26.28517  ? 43  TYR A C   1 
ATOM   328  O  O   . TYR A 1 43 ? 16.96707 3.72443   39.40255 0.825 26.67273  ? 43  TYR A O   1 
ATOM   329  C  CB  . TYR A 1 43 ? 17.24658 6.21336   41.18212 0.821 26.63447  ? 43  TYR A CB  1 
ATOM   330  C  CG  . TYR A 1 43 ? 16.22920 7.12310   40.56250 0.910 25.39610  ? 43  TYR A CG  1 
ATOM   331  C  CD1 . TYR A 1 43 ? 15.20670 7.66771   41.32523 1.000 24.61389  ? 43  TYR A CD1 1 
ATOM   332  C  CD2 . TYR A 1 43 ? 16.23625 7.36816   39.20217 1.000 24.15824  ? 43  TYR A CD2 1 
ATOM   333  C  CE1 . TYR A 1 43 ? 14.24795 8.47425   40.76126 0.973 24.58973  ? 43  TYR A CE1 1 
ATOM   334  C  CE2 . TYR A 1 43 ? 15.28389 8.17015   38.62619 1.000 23.92262  ? 43  TYR A CE2 1 
ATOM   335  C  CZ  . TYR A 1 43 ? 14.28861 8.71420   39.40601 1.000 23.78863  ? 43  TYR A CZ  1 
ATOM   336  O  OH  . TYR A 1 43 ? 13.32539 9.49499   38.84461 1.000 23.82222  ? 43  TYR A OH  1 
ATOM   337  N  N   . LEU A 1 44 ? 14.84043 4.29236   39.94874 0.857 25.86185  ? 44  LEU A N   1 
ATOM   338  C  CA  . LEU A 1 44 ? 14.23308 3.97770   38.65985 0.873 25.17941  ? 44  LEU A CA  1 
ATOM   339  C  C   . LEU A 1 44 ? 13.39193 5.15270   38.18226 1.000 24.21107  ? 44  LEU A C   1 
ATOM   340  O  O   . LEU A 1 44 ? 12.71837 5.81607   38.97325 0.874 23.30140  ? 44  LEU A O   1 
ATOM   341  C  CB  . LEU A 1 44 ? 13.32519 2.74537   38.78155 0.809 25.50703  ? 44  LEU A CB  1 
ATOM   342  C  CG  . LEU A 1 44 ? 14.02540 1.41886   39.05105 0.805 25.87517  ? 44  LEU A CG  1 
ATOM   343  C  CD1 . LEU A 1 44 ? 13.00547 0.29630   39.29202 0.520 25.89070  ? 44  LEU A CD1 1 
ATOM   344  C  CD2 . LEU A 1 44 ? 14.99047 1.04781   37.93656 0.625 25.88981  ? 44  LEU A CD2 1 
ATOM   345  N  N   . CYS A 1 45 ? 13.41376 5.39873   36.87871 1.000 23.26302  ? 45  CYS A N   1 
ATOM   346  C  CA  . CYS A 1 45 ? 12.59361 6.44828   36.29993 0.926 22.91698  ? 45  CYS A CA  1 
ATOM   347  C  C   . CYS A 1 45 ? 11.10841 6.07050   36.34902 1.000 22.49862  ? 45  CYS A C   1 
ATOM   348  O  O   . CYS A 1 45 ? 10.72918 4.95779   36.73210 1.000 24.67566  ? 45  CYS A O   1 
ATOM   349  C  CB  . CYS A 1 45 ? 13.05611 6.74111   34.87062 1.000 21.72952  ? 45  CYS A CB  1 
ATOM   350  S  SG  . CYS A 1 45 ? 12.61031 5.48426   33.65642 0.962 21.21278  ? 45  CYS A SG  1 
ATOM   351  N  N   . GLU A 1 46 ? 10.26445 7.02443   35.93317 0.816 22.74885  ? 46  GLU A N   1 
ATOM   352  C  CA  . GLU A 1 46 ? 8.81117  6.88222   35.94503 1.000 23.51596  ? 46  GLU A CA  1 
ATOM   353  C  C   . GLU A 1 46 ? 8.27853  6.01349   34.80940 0.953 24.08248  ? 46  GLU A C   1 
ATOM   354  O  O   . GLU A 1 46 ? 7.09320  5.65795   34.82710 0.780 24.37228  ? 46  GLU A O   1 
ATOM   355  C  CB  . GLU A 1 46 ? 8.14666  8.27236   35.91529 0.876 22.68034  ? 46  GLU A CB  1 
ATOM   356  C  CG  . GLU A 1 46 ? 7.78178  8.83102   34.51635 1.000 22.69825  ? 46  GLU A CG  1 
ATOM   357  C  CD  . GLU A 1 46 ? 8.96828  9.17150   33.64717 0.664 22.47304  ? 46  GLU A CD  1 
ATOM   358  O  OE1 . GLU A 1 46 ? 10.12848 9.02153   34.09054 1.000 22.73397  ? 46  GLU A OE1 1 
ATOM   359  O  OE2 . GLU A 1 46 ? 8.72217  9.60658   32.50293 0.781 22.40857  ? 46  GLU A OE2 1 
ATOM   360  N  N   . GLN A 1 47 ? 9.11150  5.64527   33.83771 1.000 23.61334  ? 47  GLN A N   1 
ATOM   361  C  CA  . GLN A 1 47 ? 8.68422  4.67297   32.84136 1.000 24.32698  ? 47  GLN A CA  1 
ATOM   362  C  C   . GLN A 1 47 ? 9.04981  3.25771   33.28295 0.651 24.79168  ? 47  GLN A C   1 
ATOM   363  O  O   . GLN A 1 47 ? 8.25128  2.32745   33.12672 0.685 24.82972  ? 47  GLN A O   1 
ATOM   364  C  CB  . GLN A 1 47 ? 9.27966  5.01850   31.47321 1.000 24.87068  ? 47  GLN A CB  1 
ATOM   365  C  CG  . GLN A 1 47 ? 8.72545  6.31403   30.87385 0.922 26.22350  ? 47  GLN A CG  1 
ATOM   366  C  CD  . GLN A 1 47 ? 7.22730  6.28387   30.60995 1.000 27.42665  ? 47  GLN A CD  1 
ATOM   367  O  OE1 . GLN A 1 47 ? 6.65763  5.24875   30.28693 0.752 27.48802  ? 47  GLN A OE1 1 
ATOM   368  N  NE2 . GLN A 1 47 ? 6.58279  7.44276   30.74731 0.778 27.14845  ? 47  GLN A NE2 1 
ATOM   369  N  N   . CYS A 1 48 ? 10.23057 3.08787   33.88503 1.000 25.48817  ? 48  CYS A N   1 
ATOM   370  C  CA  . CYS A 1 48 ? 10.59990 1.79179   34.44295 1.000 27.29941  ? 48  CYS A CA  1 
ATOM   371  C  C   . CYS A 1 48 ? 9.74710  1.42563   35.65359 0.784 26.32605  ? 48  CYS A C   1 
ATOM   372  O  O   . CYS A 1 48 ? 9.52139  0.23715   35.90944 0.765 26.84712  ? 48  CYS A O   1 
ATOM   373  C  CB  . CYS A 1 48 ? 12.09705 1.75717   34.77613 1.000 27.36505  ? 48  CYS A CB  1 
ATOM   374  S  SG  . CYS A 1 48 ? 13.19013 1.79368   33.31584 1.000 27.41611  ? 48  CYS A SG  1 
ATOM   375  N  N   . ASP A 1 49 ? 9.26558  2.41851   36.40614 0.950 27.45394  ? 49  ASP A N   1 
ATOM   376  C  CA  . ASP A 1 49 ? 8.47669  2.19788   37.62140 1.000 29.39980  ? 49  ASP A CA  1 
ATOM   377  C  C   . ASP A 1 49 ? 7.37039  3.24226   37.68113 1.000 30.37510  ? 49  ASP A C   1 
ATOM   378  O  O   . ASP A 1 49 ? 7.49279  4.26552   38.36852 0.894 30.71028  ? 49  ASP A O   1 
ATOM   379  C  CB  . ASP A 1 49 ? 9.36606  2.27495   38.86342 1.000 29.90000  ? 49  ASP A CB  1 
ATOM   380  C  CG  . ASP A 1 49 ? 8.63841  1.89973   40.12842 0.871 30.41504  ? 49  ASP A CG  1 
ATOM   381  O  OD1 . ASP A 1 49 ? 7.52374  1.33604   40.05432 0.737 30.11510  ? 49  ASP A OD1 1 
ATOM   382  O  OD2 . ASP A 1 49 ? 9.19025  2.18354   41.21008 0.621 30.53197  ? 49  ASP A OD2 1 
ATOM   383  N  N   . PRO A 1 50 ? 6.26122  3.00750   36.97494 1.000 30.96896  ? 50  PRO A N   1 
ATOM   384  C  CA  . PRO A 1 50 ? 5.21276  4.02992   36.87200 0.759 31.20370  ? 50  PRO A CA  1 
ATOM   385  C  C   . PRO A 1 50 ? 4.67416  4.41815   38.23897 0.664 31.01748  ? 50  PRO A C   1 
ATOM   386  O  O   . PRO A 1 50 ? 4.41234  3.56233   39.08595 0.592 30.09711  ? 50  PRO A O   1 
ATOM   387  C  CB  . PRO A 1 50 ? 4.12924  3.32749   36.05547 0.559 31.38620  ? 50  PRO A CB  1 
ATOM   388  C  CG  . PRO A 1 50 ? 4.86134  2.35924   35.22109 0.398 31.60356  ? 50  PRO A CG  1 
ATOM   389  C  CD  . PRO A 1 50 ? 6.13094  1.97916   35.92956 1.000 31.36471  ? 50  PRO A CD  1 
ATOM   390  N  N   . ARG A 1 51 ? 4.48222  5.72595   38.43924 0.799 31.44438  ? 51  ARG A N   1 
ATOM   391  C  CA  . ARG A 1 51 ? 4.00997  6.23585   39.72060 0.793 32.56188  ? 51  ARG A CA  1 
ATOM   392  C  C   . ARG A 1 51 ? 3.62617  7.70339   39.58210 0.624 34.02883  ? 51  ARG A C   1 
ATOM   393  O  O   . ARG A 1 51 ? 4.10468  8.38543   38.66790 0.586 33.45245  ? 51  ARG A O   1 
ATOM   394  C  CB  . ARG A 1 51 ? 5.12708  6.11619   40.75350 1.000 31.92058  ? 51  ARG A CB  1 
ATOM   395  C  CG  . ARG A 1 51 ? 6.38416  6.86571   40.36262 0.766 30.40831  ? 51  ARG A CG  1 
ATOM   396  C  CD  . ARG A 1 51 ? 7.57559  6.44995   41.20663 0.948 28.74965  ? 51  ARG A CD  1 
ATOM   397  N  NE  . ARG A 1 51 ? 8.72120  7.32655   40.99454 0.726 27.57945  ? 51  ARG A NE  1 
ATOM   398  C  CZ  . ARG A 1 51 ? 9.71158  7.05692   40.14947 0.906 26.67186  ? 51  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A 1 51 ? 9.67662  5.94759   39.42101 1.000 27.64451  ? 51  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A 1 51 ? 10.72549 7.89998   40.01038 0.918 26.97566  ? 51  ARG A NH2 1 
ATOM   401  N  N   . PRO A 1 52 ? 2.74156  8.21739   40.43580 0.714 36.03360  ? 52  PRO A N   1 
ATOM   402  C  CA  . PRO A 1 52 ? 2.58373  9.67091   40.53299 0.827 37.20577  ? 52  PRO A CA  1 
ATOM   403  C  C   . PRO A 1 52 ? 3.91617  10.31625  40.88412 1.000 38.01410  ? 52  PRO A C   1 
ATOM   404  O  O   . PRO A 1 52 ? 4.71441  9.76134   41.64315 0.326 38.01045  ? 52  PRO A O   1 
ATOM   405  C  CB  . PRO A 1 52 ? 1.59036  9.81991   41.68694 0.736 37.38910  ? 52  PRO A CB  1 
ATOM   406  C  CG  . PRO A 1 52 ? 0.67347  8.64463   41.50764 0.605 37.17287  ? 52  PRO A CG  1 
ATOM   407  C  CD  . PRO A 1 52 ? 1.51988  7.52236   40.88709 0.554 36.57665  ? 52  PRO A CD  1 
ATOM   408  N  N   . VAL A 1 53 ? 4.15832  11.49427  40.32387 0.782 38.61132  ? 53  VAL A N   1 
ATOM   409  C  CA  . VAL A 1 53 ? 5.36218  12.23654  40.68313 1.000 39.68786  ? 53  VAL A CA  1 
ATOM   410  C  C   . VAL A 1 53 ? 5.02718  13.56844  41.35311 1.000 40.30868  ? 53  VAL A C   1 
ATOM   411  O  O   . VAL A 1 53 ? 3.96078  14.13983  41.12905 0.375 40.23589  ? 53  VAL A O   1 
ATOM   412  C  CB  . VAL A 1 53 ? 6.30545  12.43090  39.48712 0.476 39.73801  ? 53  VAL A CB  1 
ATOM   413  C  CG1 . VAL A 1 53 ? 7.56316  13.15553  39.94375 0.632 39.87728  ? 53  VAL A CG1 1 
ATOM   414  C  CG2 . VAL A 1 53 ? 6.64178  11.09011  38.84297 0.703 39.64797  ? 53  VAL A CG2 1 
ATOM   415  N  N   . GLY B 1 1  ? 10.40126 -2.08635  24.45087 0.603 29.06716  ? 1   GLY B N   1 
ATOM   416  C  CA  . GLY B 1 1  ? 10.22718 -2.62723  25.78637 0.610 29.51299  ? 1   GLY B CA  1 
ATOM   417  C  C   . GLY B 1 1  ? 10.93216 -1.81419  26.85426 0.705 29.66975  ? 1   GLY B C   1 
ATOM   418  O  O   . GLY B 1 1  ? 11.50911 -0.77707  26.55047 0.886 28.58049  ? 1   GLY B O   1 
ATOM   419  N  N   . PRO B 1 2  ? 10.89117 -2.30195  28.09714 1.000 31.13307  ? 2   PRO B N   1 
ATOM   420  C  CA  . PRO B 1 2  ? 11.43886 -1.53379  29.23308 0.919 31.79867  ? 2   PRO B CA  1 
ATOM   421  C  C   . PRO B 1 2  ? 12.86977 -1.05482  29.05466 0.624 32.08896  ? 2   PRO B C   1 
ATOM   422  O  O   . PRO B 1 2  ? 13.21351 0.03290   29.53576 0.816 32.85212  ? 2   PRO B O   1 
ATOM   423  C  CB  . PRO B 1 2  ? 11.33111 -2.52742  30.39669 0.866 31.97810  ? 2   PRO B CB  1 
ATOM   424  C  CG  . PRO B 1 2  ? 10.16363 -3.37613  30.04647 1.000 32.06925  ? 2   PRO B CG  1 
ATOM   425  C  CD  . PRO B 1 2  ? 10.11146 -3.47071  28.53982 1.000 31.87783  ? 2   PRO B CD  1 
ATOM   426  N  N   . LEU B 1 3  ? 13.71789 -1.83374  28.38434 0.755 31.17165  ? 3   LEU B N   1 
ATOM   427  C  CA  . LEU B 1 3  ? 15.11071 -1.45880  28.18419 0.809 30.93054  ? 3   LEU B CA  1 
ATOM   428  C  C   . LEU B 1 3  ? 15.31969 -0.52758  26.99800 0.717 28.53262  ? 3   LEU B C   1 
ATOM   429  O  O   . LEU B 1 3  ? 16.42342 0.00660   26.84289 0.910 29.63382  ? 3   LEU B O   1 
ATOM   430  C  CB  . LEU B 1 3  ? 15.97123 -2.70953  28.00200 1.000 32.12222  ? 3   LEU B CB  1 
ATOM   431  C  CG  . LEU B 1 3  ? 15.81679 -3.75948  29.09982 0.525 33.27215  ? 3   LEU B CG  1 
ATOM   432  C  CD1 . LEU B 1 3  ? 16.25303 -5.13623  28.60484 0.778 33.59692  ? 3   LEU B CD1 1 
ATOM   433  C  CD2 . LEU B 1 3  ? 16.60406 -3.33526  30.32469 1.000 34.20419  ? 3   LEU B CD2 1 
ATOM   434  N  N   . ASP B 1 4  ? 14.30635 -0.32891  26.15756 1.000 25.12366  ? 4   ASP B N   1 
ATOM   435  C  CA  . ASP B 1 4  ? 14.41429 0.57744   25.02382 1.000 22.95197  ? 4   ASP B CA  1 
ATOM   436  C  C   . ASP B 1 4  ? 13.92865 1.94254   25.48037 0.861 22.30372  ? 4   ASP B C   1 
ATOM   437  O  O   . ASP B 1 4  ? 12.88095 2.04584   26.12624 0.435 23.87321  ? 4   ASP B O   1 
ATOM   438  C  CB  . ASP B 1 4  ? 13.53318 0.09534   23.87487 0.889 23.05928  ? 4   ASP B CB  1 
ATOM   439  C  CG  . ASP B 1 4  ? 13.85472 -1.32066  23.44862 0.753 22.91920  ? 4   ASP B CG  1 
ATOM   440  O  OD1 . ASP B 1 4  ? 15.05024 -1.66675  23.38128 0.559 22.54214  ? 4   ASP B OD1 1 
ATOM   441  O  OD2 . ASP B 1 4  ? 12.90582 -2.08121  23.16042 0.497 23.53921  ? 4   ASP B OD2 1 
ATOM   442  N  N   . VAL B 1 5  ? 14.67994 2.98542   25.15156 1.000 19.36456  ? 5   VAL B N   1 
ATOM   443  C  CA  . VAL B 1 5  ? 14.34066 4.34427   25.56956 1.000 17.74053  ? 5   VAL B CA  1 
ATOM   444  C  C   . VAL B 1 5  ? 13.66900 5.04675   24.39934 0.980 16.95224  ? 5   VAL B C   1 
ATOM   445  O  O   . VAL B 1 5  ? 14.23636 5.12545   23.30372 1.000 17.10001  ? 5   VAL B O   1 
ATOM   446  C  CB  . VAL B 1 5  ? 15.57539 5.13057   26.03702 1.000 18.32613  ? 5   VAL B CB  1 
ATOM   447  C  CG1 . VAL B 1 5  ? 15.17415 6.57131   26.37835 1.000 18.59695  ? 5   VAL B CG1 1 
ATOM   448  C  CG2 . VAL B 1 5  ? 16.21956 4.45357   27.25773 1.000 19.85377  ? 5   VAL B CG2 1 
ATOM   449  N  N   . ILE B 1 6  ? 12.46022 5.55048   24.62223 1.000 15.85613  ? 6   ILE B N   1 
ATOM   450  C  CA  . ILE B 1 6  ? 11.76976 6.40354   23.65839 1.000 14.82708  ? 6   ILE B CA  1 
ATOM   451  C  C   . ILE B 1 6  ? 12.06014 7.84672   24.05264 1.000 14.25173  ? 6   ILE B C   1 
ATOM   452  O  O   . ILE B 1 6  ? 11.76914 8.25832   25.17937 0.850 14.59952  ? 6   ILE B O   1 
ATOM   453  C  CB  . ILE B 1 6  ? 10.25628 6.12517   23.63505 0.945 15.82400  ? 6   ILE B CB  1 
ATOM   454  C  CG1 . ILE B 1 6  ? 9.99062  4.68398   23.17046 0.818 16.68010  ? 6   ILE B CG1 1 
ATOM   455  C  CG2 . ILE B 1 6  ? 9.54564  7.11818   22.72013 0.998 17.20717  ? 6   ILE B CG2 1 
ATOM   456  C  CD1 . ILE B 1 6  ? 8.54120  4.27853   23.19556 0.763 17.49636  ? 6   ILE B CD1 1 
ATOM   457  N  N   . ARG B 1 7  ? 12.65636 8.61809   23.14937 1.000 13.79467  ? 7   ARG B N   1 
ATOM   458  C  CA  . ARG B 1 7  ? 12.85769 10.04679  23.40697 1.000 13.45379  ? 7   ARG B CA  1 
ATOM   459  C  C   . ARG B 1 7  ? 12.68087 10.77106  22.07859 1.000 15.31697  ? 7   ARG B C   1 
ATOM   460  O  O   . ARG B 1 7  ? 13.65225 11.01115  21.36223 0.974 15.78158  ? 7   ARG B O   1 
ATOM   461  C  CB  . ARG B 1 7  ? 14.20880 10.36769  24.02826 1.000 14.00797  ? 7   ARG B CB  1 
ATOM   462  C  CG  . ARG B 1 7  ? 14.22820 11.80408  24.53626 1.000 14.90825  ? 7   ARG B CG  1 
ATOM   463  C  CD  . ARG B 1 7  ? 15.61516 12.38842  24.70168 0.963 16.31327  ? 7   ARG B CD  1 
ATOM   464  N  NE  . ARG B 1 7  ? 16.35752 12.42352  23.44552 1.000 16.66945  ? 7   ARG B NE  1 
ATOM   465  C  CZ  . ARG B 1 7  ? 16.12516 13.26626  22.43261 0.869 15.39705  ? 7   ARG B CZ  1 
ATOM   466  N  NH1 . ARG B 1 7  ? 15.14330 14.15899  22.49550 0.862 17.37011  ? 7   ARG B NH1 1 
ATOM   467  N  NH2 . ARG B 1 7  ? 16.87658 13.20901  21.33344 0.875 16.46869  ? 7   ARG B NH2 1 
ATOM   468  N  N   . CYS B 1 8  ? 11.44309 11.10933  21.76087 1.000 15.72894  ? 8   CYS B N   1 
ATOM   469  C  CA  . CYS B 1 8  ? 11.13076 11.80307  20.52493 1.000 16.10033  ? 8   CYS B CA  1 
ATOM   470  C  C   . CYS B 1 8  ? 10.91100 13.28407  20.80330 1.000 17.03748  ? 8   CYS B C   1 
ATOM   471  O  O   . CYS B 1 8  ? 10.68075 13.69733  21.94028 1.000 18.05230  ? 8   CYS B O   1 
ATOM   472  C  CB  . CYS B 1 8  ? 9.87317  11.18676  19.91039 1.000 15.60062  ? 8   CYS B CB  1 
ATOM   473  S  SG  . CYS B 1 8  ? 9.52450  11.72955  18.24582 1.000 16.50390  ? 8   CYS B SG  1 
ATOM   474  N  N   . ILE B 1 9  ? 10.95932 14.09045  19.73859 1.000 17.99575  ? 9   ILE B N   1 
ATOM   475  C  CA  . ILE B 1 9  ? 10.69547 15.51596  19.90429 1.000 19.74758  ? 9   ILE B CA  1 
ATOM   476  C  C   . ILE B 1 9  ? 9.27590  15.79001  20.38366 1.000 19.68031  ? 9   ILE B C   1 
ATOM   477  O  O   . ILE B 1 9  ? 9.02068  16.84241  20.97498 0.583 20.86216  ? 9   ILE B O   1 
ATOM   478  C  CB  . ILE B 1 9  ? 11.02390 16.32024  18.62876 1.000 20.50185  ? 9   ILE B CB  1 
ATOM   479  C  CG1 . ILE B 1 9  ? 10.09744 15.92151  17.46978 1.000 20.90722  ? 9   ILE B CG1 1 
ATOM   480  C  CG2 . ILE B 1 9  ? 12.50088 16.18403  18.27860 0.439 20.76203  ? 9   ILE B CG2 1 
ATOM   481  C  CD1 . ILE B 1 9  ? 10.08274 16.91236  16.33714 0.492 22.12051  ? 9   ILE B CD1 1 
ATOM   482  N  N   . CYS B 1 10 ? 8.33824  14.86812  20.14575 1.000 19.12938  ? 10  CYS B N   1 
ATOM   483  C  CA  . CYS B 1 10 ? 6.96925  15.08277  20.60483 0.793 19.47442  ? 10  CYS B CA  1 
ATOM   484  C  C   . CYS B 1 10 ? 6.84131  14.95712  22.11847 1.000 19.96505  ? 10  CYS B C   1 
ATOM   485  O  O   . CYS B 1 10 ? 5.85516  15.44306  22.67610 0.894 20.95784  ? 10  CYS B O   1 
ATOM   486  C  CB  . CYS B 1 10 ? 5.99774  14.11778  19.91166 0.960 19.33801  ? 10  CYS B CB  1 
ATOM   487  S  SG  . CYS B 1 10 ? 6.32381  12.37199  20.33242 1.000 18.04854  ? 10  CYS B SG  1 
ATOM   488  N  N   . GLY B 1 11 ? 7.79655  14.30615  22.79336 1.000 18.67834  ? 11  GLY B N   1 
ATOM   489  C  CA  . GLY B 1 11 ? 7.73743  14.16735  24.23619 0.942 19.36755  ? 11  GLY B CA  1 
ATOM   490  C  C   . GLY B 1 11 ? 6.74931  13.14588  24.74848 0.973 19.35205  ? 11  GLY B C   1 
ATOM   491  O  O   . GLY B 1 11 ? 6.55631  13.05748  25.96193 0.853 20.96226  ? 11  GLY B O   1 
ATOM   492  N  N   . LEU B 1 12 ? 6.11472  12.36824  23.86803 1.000 18.07617  ? 12  LEU B N   1 
ATOM   493  C  CA  . LEU B 1 12 ? 5.16718  11.33726  24.27539 1.000 18.83402  ? 12  LEU B CA  1 
ATOM   494  C  C   . LEU B 1 12 ? 5.89609  10.00320  24.33200 1.000 18.50128  ? 12  LEU B C   1 
ATOM   495  O  O   . LEU B 1 12 ? 6.49702  9.57893   23.33930 1.000 18.22803  ? 12  LEU B O   1 
ATOM   496  C  CB  . LEU B 1 12 ? 3.98835  11.26752  23.30693 1.000 21.16872  ? 12  LEU B CB  1 
ATOM   497  C  CG  . LEU B 1 12 ? 3.02217  12.44755  23.41218 0.763 21.88948  ? 12  LEU B CG  1 
ATOM   498  C  CD1 . LEU B 1 12 ? 1.97466  12.37542  22.30234 0.849 22.51727  ? 12  LEU B CD1 1 
ATOM   499  C  CD2 . LEU B 1 12 ? 2.34929  12.50461  24.78332 0.616 22.26617  ? 12  LEU B CD2 1 
ATOM   500  N  N   . TYR B 1 13 ? 5.84153  9.34754   25.49328 1.000 19.01689  ? 13  TYR B N   1 
ATOM   501  C  CA  . TYR B 1 13 ? 6.50084  8.05977   25.70205 1.000 18.68287  ? 13  TYR B CA  1 
ATOM   502  C  C   . TYR B 1 13 ? 5.55239  6.97814   25.21014 0.807 19.53113  ? 13  TYR B C   1 
ATOM   503  O  O   . TYR B 1 13 ? 4.86070  6.30116   25.97599 0.694 19.39116  ? 13  TYR B O   1 
ATOM   504  C  CB  . TYR B 1 13 ? 6.89865  7.85397   27.16215 1.000 18.73887  ? 13  TYR B CB  1 
ATOM   505  C  CG  . TYR B 1 13 ? 8.05293  6.88977   27.26972 1.000 17.79806  ? 13  TYR B CG  1 
ATOM   506  C  CD1 . TYR B 1 13 ? 7.85906  5.51766   27.14469 0.894 18.48766  ? 13  TYR B CD1 1 
ATOM   507  C  CD2 . TYR B 1 13 ? 9.35576  7.36010   27.40810 0.888 17.06331  ? 13  TYR B CD2 1 
ATOM   508  C  CE1 . TYR B 1 13 ? 8.92659  4.64200   27.21259 0.771 18.38796  ? 13  TYR B CE1 1 
ATOM   509  C  CE2 . TYR B 1 13 ? 10.43186 6.49536   27.47738 0.935 17.89505  ? 13  TYR B CE2 1 
ATOM   510  C  CZ  . TYR B 1 13 ? 10.21353 5.14104   27.35730 1.000 18.96129  ? 13  TYR B CZ  1 
ATOM   511  O  OH  . TYR B 1 13 ? 11.28331 4.28630   27.41293 0.680 20.88620  ? 13  TYR B OH  1 
ATOM   512  N  N   . LYS B 1 14 ? 5.50271  6.83132   23.89491 1.000 20.81678  ? 14  LYS B N   1 
ATOM   513  C  CA  . LYS B 1 14 ? 4.58284  5.87175   23.31443 0.822 21.93840  ? 14  LYS B CA  1 
ATOM   514  C  C   . LYS B 1 14 ? 5.18280  5.18146   22.10437 0.849 19.96639  ? 14  LYS B C   1 
ATOM   515  O  O   . LYS B 1 14 ? 5.83197  5.80486   21.25979 1.000 20.90850  ? 14  LYS B O   1 
ATOM   516  C  CB  . LYS B 1 14 ? 3.18398  6.46087   23.08882 0.768 24.97694  ? 14  LYS B CB  1 
ATOM   517  C  CG  . LYS B 1 14 ? 3.01102  7.38292   21.92430 0.501 27.21206  ? 14  LYS B CG  1 
ATOM   518  C  CD  . LYS B 1 14 ? 1.52848  7.51462   21.61442 0.721 28.95799  ? 14  LYS B CD  1 
ATOM   519  C  CE  . LYS B 1 14 ? 1.25370  8.80789   20.89311 0.439 29.83623  ? 14  LYS B CE  1 
ATOM   520  N  NZ  . LYS B 1 14 ? 0.06082  8.74462   20.01070 0.433 29.97592  ? 14  LYS B NZ  1 
ATOM   521  N  N   . ASP B 1 15 ? 4.98662  3.87184   22.06918 0.764 19.78458  ? 15  ASP B N   1 
ATOM   522  C  CA  . ASP B 1 15 ? 5.44844  3.01803   20.98488 1.000 22.24514  ? 15  ASP B CA  1 
ATOM   523  C  C   . ASP B 1 15 ? 4.32087  3.00166   19.96288 0.868 23.49218  ? 15  ASP B C   1 
ATOM   524  O  O   . ASP B 1 15 ? 3.31080  2.31798   20.14580 0.575 24.12955  ? 15  ASP B O   1 
ATOM   525  C  CB  . ASP B 1 15 ? 5.72549  1.62366   21.54087 0.866 23.72259  ? 15  ASP B CB  1 
ATOM   526  C  CG  . ASP B 1 15 ? 6.22135  0.66277   20.48806 0.654 25.06750  ? 15  ASP B CG  1 
ATOM   527  O  OD1 . ASP B 1 15 ? 6.73039  1.13136   19.45016 0.563 24.74402  ? 15  ASP B OD1 1 
ATOM   528  O  OD2 . ASP B 1 15 ? 6.08998  -0.56428  20.69541 0.509 26.21375  ? 15  ASP B OD2 1 
ATOM   529  N  N   . GLU B 1 16 ? 4.48283  3.77314   18.88778 1.000 23.28035  ? 16  GLU B N   1 
ATOM   530  C  CA  . GLU B 1 16 ? 3.44338  3.91537   17.88182 1.000 24.67180  ? 16  GLU B CA  1 
ATOM   531  C  C   . GLU B 1 16 ? 4.09909  4.12037   16.52765 0.803 23.07944  ? 16  GLU B C   1 
ATOM   532  O  O   . GLU B 1 16 ? 5.04019  4.90743   16.40102 0.768 21.82353  ? 16  GLU B O   1 
ATOM   533  C  CB  . GLU B 1 16 ? 2.52299  5.11133   18.17471 0.577 26.53603  ? 16  GLU B CB  1 
ATOM   534  C  CG  . GLU B 1 16 ? 1.74317  5.58689   16.94672 0.573 28.27114  ? 16  GLU B CG  1 
ATOM   535  C  CD  . GLU B 1 16 ? 1.04652  6.92108   17.13749 0.405 29.98541  ? 16  GLU B CD  1 
ATOM   536  O  OE1 . GLU B 1 16 ? 0.74371  7.27539   18.29080 0.425 30.33624  ? 16  GLU B OE1 1 
ATOM   537  O  OE2 . GLU B 1 16 ? 0.80004  7.61951   16.12910 0.597 30.92842  ? 16  GLU B OE2 1 
ATOM   538  N  N   . GLY B 1 17 ? 3.59211  3.41557   15.52011 1.000 22.93573  ? 17  GLY B N   1 
ATOM   539  C  CA  . GLY B 1 17 ? 4.01114  3.65330   14.15807 1.000 22.89700  ? 17  GLY B CA  1 
ATOM   540  C  C   . GLY B 1 17 ? 5.43146  3.17913   13.91020 1.000 21.05019  ? 17  GLY B C   1 
ATOM   541  O  O   . GLY B 1 17 ? 6.05680  2.48583   14.71695 0.714 21.09910  ? 17  GLY B O   1 
ATOM   542  N  N   . LEU B 1 18 ? 5.94047  3.58470   12.75242 0.697 20.08860  ? 18  LEU B N   1 
ATOM   543  C  CA  . LEU B 1 18 ? 7.33603  3.35135   12.42363 1.000 20.93397  ? 18  LEU B CA  1 
ATOM   544  C  C   . LEU B 1 18 ? 8.22644  4.22667   13.29530 0.851 20.12126  ? 18  LEU B C   1 
ATOM   545  O  O   . LEU B 1 18 ? 8.07152  5.45222   13.35047 0.857 19.97904  ? 18  LEU B O   1 
ATOM   546  C  CB  . LEU B 1 18 ? 7.59844  3.67236   10.95812 1.000 24.20994  ? 18  LEU B CB  1 
ATOM   547  C  CG  . LEU B 1 18 ? 8.82397  2.99536   10.34526 0.738 24.43741  ? 18  LEU B CG  1 
ATOM   548  C  CD1 . LEU B 1 18 ? 8.83624  1.47679   10.55006 0.629 25.52929  ? 18  LEU B CD1 1 
ATOM   549  C  CD2 . LEU B 1 18 ? 8.94947  3.36443   8.88242  0.619 23.85988  ? 18  LEU B CD2 1 
ATOM   550  N  N   . MET B 1 19 ? 9.17783  3.59729   13.95287 1.000 20.29063  ? 19  MET B N   1 
ATOM   551  C  CA  . MET B 1 19 ? 10.07251 4.29173   14.85268 1.000 19.44826  ? 19  MET B CA  1 
ATOM   552  C  C   . MET B 1 19 ? 11.49488 3.96815   14.42259 0.795 18.76757  ? 19  MET B C   1 
ATOM   553  O  O   . MET B 1 19 ? 11.75762 2.91506   13.82891 0.710 19.51012  ? 19  MET B O   1 
ATOM   554  C  CB  . MET B 1 19 ? 9.81170  3.81392   16.27897 1.000 19.21437  ? 19  MET B CB  1 
ATOM   555  C  CG  . MET B 1 19 ? 8.45703  4.28447   16.79141 0.866 19.20835  ? 19  MET B CG  1 
ATOM   556  S  SD  . MET B 1 19 ? 8.24883  4.15293   18.56768 0.796 18.79202  ? 19  MET B SD  1 
ATOM   557  C  CE  . MET B 1 19 ? 9.19935  5.54986   19.16207 1.000 19.96789  ? 19  MET B CE  1 
ATOM   558  N  N   . ILE B 1 20 ? 12.40964 4.88747   14.70945 1.000 19.69886  ? 20  ILE B N   1 
ATOM   559  C  CA  . ILE B 1 20 ? 13.78634 4.81418   14.23056 0.777 18.75471  ? 20  ILE B CA  1 
ATOM   560  C  C   . ILE B 1 20 ? 14.71657 5.09466   15.40246 0.824 18.66604  ? 20  ILE B C   1 
ATOM   561  O  O   . ILE B 1 20 ? 14.39886 5.90992   16.27456 1.000 18.69898  ? 20  ILE B O   1 
ATOM   562  C  CB  . ILE B 1 20 ? 14.01529 5.79302   13.04811 0.852 20.25925  ? 20  ILE B CB  1 
ATOM   563  C  CG1 . ILE B 1 20 ? 15.38168 5.57123   12.38436 1.000 21.27647  ? 20  ILE B CG1 1 
ATOM   564  C  CG2 . ILE B 1 20 ? 13.79092 7.24697   13.47538 1.000 21.47675  ? 20  ILE B CG2 1 
ATOM   565  C  CD1 . ILE B 1 20 ? 15.46854 6.18581   10.97735 0.937 21.74789  ? 20  ILE B CD1 1 
ATOM   566  N  N   . GLN B 1 21 ? 15.84964 4.40801   15.43144 0.817 20.33312  ? 21  GLN B N   1 
ATOM   567  C  CA  . GLN B 1 21 ? 16.79024 4.49449   16.53853 0.893 21.38938  ? 21  GLN B CA  1 
ATOM   568  C  C   . GLN B 1 21 ? 17.97113 5.38534   16.17400 1.000 21.91547  ? 21  GLN B C   1 
ATOM   569  O  O   . GLN B 1 21 ? 18.52320 5.28617   15.07166 0.782 21.93977  ? 21  GLN B O   1 
ATOM   570  C  CB  . GLN B 1 21 ? 17.31010 3.10562   16.90483 0.808 22.51768  ? 21  GLN B CB  1 
ATOM   571  C  CG  . GLN B 1 21 ? 18.28580 3.11362   18.07762 1.000 23.92629  ? 21  GLN B CG  1 
ATOM   572  C  CD  . GLN B 1 21 ? 18.59390 1.71830   18.57363 1.000 25.42297  ? 21  GLN B CD  1 
ATOM   573  O  OE1 . GLN B 1 21 ? 18.99304 0.84308   17.79979 0.641 24.87293  ? 21  GLN B OE1 1 
ATOM   574  N  NE2 . GLN B 1 21 ? 18.42851 1.50192   19.86818 1.000 25.91113  ? 21  GLN B NE2 1 
ATOM   575  N  N   . CYS B 1 22 ? 18.35716 6.25928   17.09984 0.888 22.52269  ? 22  CYS B N   1 
ATOM   576  C  CA  . CYS B 1 22 ? 19.55469 7.06515   16.90239 1.000 24.20583  ? 22  CYS B CA  1 
ATOM   577  C  C   . CYS B 1 22 ? 20.78661 6.16797   16.93188 1.000 25.17191  ? 22  CYS B C   1 
ATOM   578  O  O   . CYS B 1 22 ? 20.95593 5.35134   17.84770 0.831 25.17782  ? 22  CYS B O   1 
ATOM   579  C  CB  . CYS B 1 22 ? 19.66911 8.14351   17.98524 1.000 24.38534  ? 22  CYS B CB  1 
ATOM   580  S  SG  . CYS B 1 22 ? 21.16711 9.18257   17.83727 1.000 25.69195  ? 22  CYS B SG  1 
ATOM   581  N  N   . ASP B 1 23 ? 21.64977 6.32343   15.92038 0.957 26.93962  ? 23  ASP B N   1 
ATOM   582  C  CA  . ASP B 1 23 ? 22.83369 5.47631   15.80736 1.000 27.50895  ? 23  ASP B CA  1 
ATOM   583  C  C   . ASP B 1 23 ? 23.77793 5.63749   16.98986 1.000 27.88717  ? 23  ASP B C   1 
ATOM   584  O  O   . ASP B 1 23 ? 24.52233 4.70418   17.31176 0.655 29.24136  ? 23  ASP B O   1 
ATOM   585  C  CB  . ASP B 1 23 ? 23.59207 5.80737   14.51972 1.000 28.77019  ? 23  ASP B CB  1 
ATOM   586  C  CG  . ASP B 1 23 ? 22.91340 5.26328   13.28873 0.673 29.79072  ? 23  ASP B CG  1 
ATOM   587  O  OD1 . ASP B 1 23 ? 22.20849 4.23696   13.40359 0.583 30.27189  ? 23  ASP B OD1 1 
ATOM   588  O  OD2 . ASP B 1 23 ? 23.11344 5.85330   12.20772 0.731 30.33791  ? 23  ASP B OD2 1 
ATOM   589  N  N   . LYS B 1 24 ? 23.79052 6.81135   17.62439 1.000 27.89443  ? 24  LYS B N   1 
ATOM   590  C  CA  . LYS B 1 24 ? 24.77436 7.12225   18.66093 1.000 27.51115  ? 24  LYS B CA  1 
ATOM   591  C  C   . LYS B 1 24 ? 24.23734 6.94253   20.07974 1.000 26.53563  ? 24  LYS B C   1 
ATOM   592  O  O   . LYS B 1 24 ? 24.81693 6.18670   20.86238 0.740 26.61104  ? 24  LYS B O   1 
ATOM   593  C  CB  . LYS B 1 24 ? 25.35303 8.52908   18.46008 1.000 28.66427  ? 24  LYS B CB  1 
ATOM   594  C  CG  . LYS B 1 24 ? 26.38895 8.61689   17.34513 0.661 29.40437  ? 24  LYS B CG  1 
ATOM   595  C  CD  . LYS B 1 24 ? 27.71781 8.00114   17.74216 1.000 31.06450  ? 24  LYS B CD  1 
ATOM   596  C  CE  . LYS B 1 24 ? 28.77687 8.34633   16.71863 0.748 32.01438  ? 24  LYS B CE  1 
ATOM   597  N  NZ  . LYS B 1 24 ? 30.02422 7.57939   16.95385 0.611 32.30428  ? 24  LYS B NZ  1 
ATOM   598  N  N   . CYS B 1 25 ? 23.15019 7.63113   20.43763 1.000 25.22846  ? 25  CYS B N   1 
ATOM   599  C  CA  . CYS B 1 25 ? 22.63667 7.57028   21.80747 1.000 24.41494  ? 25  CYS B CA  1 
ATOM   600  C  C   . CYS B 1 25 ? 21.58259 6.48893   22.01877 1.000 24.01443  ? 25  CYS B C   1 
ATOM   601  O  O   . CYS B 1 25 ? 21.17970 6.25362   23.16378 1.000 24.93967  ? 25  CYS B O   1 
ATOM   602  C  CB  . CYS B 1 25 ? 22.09130 8.93530   22.25072 1.000 23.55713  ? 25  CYS B CB  1 
ATOM   603  S  SG  . CYS B 1 25 ? 20.51839 9.39757   21.50036 0.976 23.51445  ? 25  CYS B SG  1 
ATOM   604  N  N   . MET B 1 26 ? 21.10639 5.84523   20.95133 1.000 24.37587  ? 26  MET B N   1 
ATOM   605  C  CA  . MET B 1 26 ? 20.21282 4.67937   20.99537 0.947 24.35414  ? 26  MET B CA  1 
ATOM   606  C  C   . MET B 1 26 ? 18.75947 4.97662   21.34777 1.000 22.13633  ? 26  MET B C   1 
ATOM   607  O  O   . MET B 1 26 ? 17.98532 4.02831   21.49096 1.000 22.81600  ? 26  MET B O   1 
ATOM   608  C  CB  . MET B 1 26 ? 20.75546 3.51195   21.83561 0.808 26.49779  ? 26  MET B CB  1 
ATOM   609  C  CG  . MET B 1 26 ? 22.23838 3.26139   21.59038 0.814 28.52540  ? 26  MET B CG  1 
ATOM   610  S  SD  . MET B 1 26 ? 22.52858 2.70404   19.89654 0.460 30.87373  ? 26  MET B SD  1 
ATOM   611  C  CE  . MET B 1 26 ? 21.71922 1.11128   19.91638 0.627 30.93291  ? 26  MET B CE  1 
ATOM   612  N  N   . VAL B 1 27 ? 18.35199 6.24333   21.49026 0.949 20.31692  ? 27  VAL B N   1 
ATOM   613  C  CA  . VAL B 1 27 ? 16.93550 6.52110   21.71618 1.000 18.75574  ? 27  VAL B CA  1 
ATOM   614  C  C   . VAL B 1 27 ? 16.12486 6.22860   20.45950 1.000 18.09427  ? 27  VAL B C   1 
ATOM   615  O  O   . VAL B 1 27 ? 16.62847 6.25838   19.33610 1.000 20.14963  ? 27  VAL B O   1 
ATOM   616  C  CB  . VAL B 1 27 ? 16.67447 7.95037   22.21840 1.000 18.60143  ? 27  VAL B CB  1 
ATOM   617  C  CG1 . VAL B 1 27 ? 17.49046 8.23491   23.46432 1.000 18.89578  ? 27  VAL B CG1 1 
ATOM   618  C  CG2 . VAL B 1 27 ? 16.90199 8.99376   21.11807 1.000 19.05755  ? 27  VAL B CG2 1 
ATOM   619  N  N   . TRP B 1 28 ? 14.84281 5.94911   20.66367 1.000 16.75483  ? 28  TRP B N   1 
ATOM   620  C  CA  . TRP B 1 28 ? 13.89418 5.71751   19.58597 1.000 16.29032  ? 28  TRP B CA  1 
ATOM   621  C  C   . TRP B 1 28 ? 12.99907 6.93705   19.41179 0.797 14.68511  ? 28  TRP B C   1 
ATOM   622  O  O   . TRP B 1 28 ? 12.55360 7.55521   20.39046 0.950 14.76933  ? 28  TRP B O   1 
ATOM   623  C  CB  . TRP B 1 28 ? 13.03075 4.49672   19.90781 1.000 18.24634  ? 28  TRP B CB  1 
ATOM   624  C  CG  . TRP B 1 28 ? 13.78911 3.21445   19.87341 1.000 18.64303  ? 28  TRP B CG  1 
ATOM   625  C  CD1 . TRP B 1 28 ? 14.46693 2.62547   20.90586 0.979 19.43357  ? 28  TRP B CD1 1 
ATOM   626  C  CD2 . TRP B 1 28 ? 13.96293 2.35090   18.73945 1.000 19.66132  ? 28  TRP B CD2 1 
ATOM   627  N  NE1 . TRP B 1 28 ? 15.03853 1.45734   20.48682 0.834 19.84063  ? 28  TRP B NE1 1 
ATOM   628  C  CE2 . TRP B 1 28 ? 14.75311 1.26672   19.15978 0.787 20.07173  ? 28  TRP B CE2 1 
ATOM   629  C  CE3 . TRP B 1 28 ? 13.52895 2.39612   17.40286 0.846 20.01188  ? 28  TRP B CE3 1 
ATOM   630  C  CZ2 . TRP B 1 28 ? 15.11378 0.23094   18.29737 0.849 20.56583  ? 28  TRP B CZ2 1 
ATOM   631  C  CZ3 . TRP B 1 28 ? 13.88853 1.37375   16.55566 0.742 20.71597  ? 28  TRP B CZ3 1 
ATOM   632  C  CH2 . TRP B 1 28 ? 14.67157 0.30437   17.00165 0.690 20.50546  ? 28  TRP B CH2 1 
ATOM   633  N  N   . GLN B 1 29 ? 12.73467 7.27594   18.16174 0.811 13.98526  ? 29  GLN B N   1 
ATOM   634  C  CA  . GLN B 1 29 ? 11.92358 8.42615   17.81044 1.000 15.48348  ? 29  GLN B CA  1 
ATOM   635  C  C   . GLN B 1 29 ? 10.88828 8.00812   16.77324 0.940 15.87391  ? 29  GLN B C   1 
ATOM   636  O  O   . GLN B 1 29 ? 11.08603 7.03901   16.03155 0.880 16.73222  ? 29  GLN B O   1 
ATOM   637  C  CB  . GLN B 1 29 ? 12.80835 9.56921   17.28343 1.000 16.80339  ? 29  GLN B CB  1 
ATOM   638  C  CG  . GLN B 1 29 ? 14.00599 9.88191   18.19009 1.000 17.41092  ? 29  GLN B CG  1 
ATOM   639  C  CD  . GLN B 1 29 ? 14.59881 11.25430  17.92801 0.852 16.19307  ? 29  GLN B CD  1 
ATOM   640  O  OE1 . GLN B 1 29 ? 15.10611 11.51165  16.84013 1.000 18.85857  ? 29  GLN B OE1 1 
ATOM   641  N  NE2 . GLN B 1 29 ? 14.54152 12.14542  18.91460 1.000 16.76558  ? 29  GLN B NE2 1 
ATOM   642  N  N   . HIS B 1 30 ? 9.76909  8.73349   16.72316 1.000 16.03724  ? 30  HIS B N   1 
ATOM   643  C  CA  . HIS B 1 30 ? 8.75697  8.43838   15.71150 1.000 17.34253  ? 30  HIS B CA  1 
ATOM   644  C  C   . HIS B 1 30 ? 9.19991  9.00901   14.37452 1.000 17.73769  ? 30  HIS B C   1 
ATOM   645  O  O   . HIS B 1 30 ? 9.50040  10.20025  14.27226 0.849 16.37199  ? 30  HIS B O   1 
ATOM   646  C  CB  . HIS B 1 30 ? 7.39245  9.02599   16.08305 1.000 16.77738  ? 30  HIS B CB  1 
ATOM   647  C  CG  . HIS B 1 30 ? 6.92764  8.64953   17.45296 1.000 16.49530  ? 30  HIS B CG  1 
ATOM   648  N  ND1 . HIS B 1 30 ? 6.85454  9.55522   18.49428 1.000 15.87495  ? 30  HIS B ND1 1 
ATOM   649  C  CD2 . HIS B 1 30 ? 6.52364  7.45879   17.95712 0.926 16.59931  ? 30  HIS B CD2 1 
ATOM   650  C  CE1 . HIS B 1 30 ? 6.44478  8.92860   19.58428 0.953 16.45504  ? 30  HIS B CE1 1 
ATOM   651  N  NE2 . HIS B 1 30 ? 6.22506  7.65970   19.28386 0.902 16.88492  ? 30  HIS B NE2 1 
ATOM   652  N  N   . CYS B 1 31 ? 9.21854  8.16518   13.33996 0.979 18.98860  ? 31  CYS B N   1 
ATOM   653  C  CA  . CYS B 1 31 ? 9.63185  8.64298   12.02130 1.000 20.36794  ? 31  CYS B CA  1 
ATOM   654  C  C   . CYS B 1 31 ? 8.78973  9.83043   11.56450 0.740 20.60092  ? 31  CYS B C   1 
ATOM   655  O  O   . CYS B 1 31 ? 9.32003  10.79646  11.00788 0.822 21.55259  ? 31  CYS B O   1 
ATOM   656  C  CB  . CYS B 1 31 ? 9.54703  7.51541   10.99574 0.750 21.37615  ? 31  CYS B CB  1 
ATOM   657  S  SG  . CYS B 1 31 ? 10.75796 6.22094   11.27809 0.698 21.44181  ? 31  CYS B SG  1 
ATOM   658  N  N   . ASP B 1 32 ? 7.47819  9.79139   11.81683 1.000 20.87969  ? 32  ASP B N   1 
ATOM   659  C  CA  . ASP B 1 32 ? 6.61798  10.89380  11.39903 0.937 21.24318  ? 32  ASP B CA  1 
ATOM   660  C  C   . ASP B 1 32 ? 6.96063  12.19774  12.11126 0.907 21.15249  ? 32  ASP B C   1 
ATOM   661  O  O   . ASP B 1 32 ? 6.91863  13.27038  11.49637 0.770 21.95182  ? 32  ASP B O   1 
ATOM   662  C  CB  . ASP B 1 32 ? 5.15377  10.53798  11.61945 0.857 21.66554  ? 32  ASP B CB  1 
ATOM   663  C  CG  . ASP B 1 32 ? 4.66109  9.48150   10.66273 0.674 22.17601  ? 32  ASP B CG  1 
ATOM   664  O  OD1 . ASP B 1 32 ? 5.35762  9.20712   9.66119  0.453 22.23702  ? 32  ASP B OD1 1 
ATOM   665  O  OD2 . ASP B 1 32 ? 3.57467  8.92995   10.91842 0.512 23.00815  ? 32  ASP B OD2 1 
ATOM   666  N  N   . CYS B 1 33 ? 7.27040  12.13951  13.41112 1.000 20.17004  ? 33  CYS B N   1 
ATOM   667  C  CA  . CYS B 1 33 ? 7.63450  13.36260  14.12414 0.866 20.62469  ? 33  CYS B CA  1 
ATOM   668  C  C   . CYS B 1 33 ? 8.92999  13.94205  13.58672 0.864 21.60905  ? 33  CYS B C   1 
ATOM   669  O  O   . CYS B 1 33 ? 9.10444  15.16536  13.54648 0.666 21.80070  ? 33  CYS B O   1 
ATOM   670  C  CB  . CYS B 1 33 ? 7.79995  13.09880  15.62126 0.971 20.15624  ? 33  CYS B CB  1 
ATOM   671  S  SG  . CYS B 1 33 ? 6.32400  12.55177  16.47160 1.000 19.29123  ? 33  CYS B SG  1 
ATOM   672  N  N   . MET B 1 34 ? 9.85253  13.08126  13.17913 1.000 22.97211  ? 34  MET B N   1 
ATOM   673  C  CA  . MET B 1 34 ? 11.17893 13.51785  12.77664 0.890 23.74150  ? 34  MET B CA  1 
ATOM   674  C  C   . MET B 1 34 ? 11.31457 13.76083  11.27852 1.000 26.31373  ? 34  MET B C   1 
ATOM   675  O  O   . MET B 1 34 ? 12.35508 14.26389  10.84964 0.640 27.13550  ? 34  MET B O   1 
ATOM   676  C  CB  . MET B 1 34 ? 12.22929 12.49236  13.21866 1.000 22.57486  ? 34  MET B CB  1 
ATOM   677  C  CG  . MET B 1 34 ? 12.25353 12.18149  14.70819 1.000 21.40160  ? 34  MET B CG  1 
ATOM   678  S  SD  . MET B 1 34 ? 12.25995 13.62097  15.81474 0.853 20.94264  ? 34  MET B SD  1 
ATOM   679  C  CE  . MET B 1 34 ? 13.88313 14.32808  15.49023 0.876 21.78383  ? 34  MET B CE  1 
ATOM   680  N  N   . GLY B 1 35 ? 10.31220 13.39819  10.47866 1.000 28.35599  ? 35  GLY B N   1 
ATOM   681  C  CA  . GLY B 1 35 ? 10.37927 13.62751  9.04640  1.000 29.83901  ? 35  GLY B CA  1 
ATOM   682  C  C   . GLY B 1 35 ? 11.21370 12.65058  8.23990  0.786 30.85103  ? 35  GLY B C   1 
ATOM   683  O  O   . GLY B 1 35 ? 11.69834 13.01585  7.16267  0.701 31.37017  ? 35  GLY B O   1 
ATOM   684  N  N   . VAL B 1 36 ? 11.36109 11.40605  8.69613  1.000 32.08462  ? 36  VAL B N   1 
ATOM   685  C  CA  . VAL B 1 36 ? 12.17302 10.38304  8.03728  1.000 32.24898  ? 36  VAL B CA  1 
ATOM   686  C  C   . VAL B 1 36 ? 11.33300 9.12266   7.81727  0.623 33.10271  ? 36  VAL B C   1 
ATOM   687  O  O   . VAL B 1 36 ? 10.18129 9.03807   8.23940  0.538 31.95819  ? 36  VAL B O   1 
ATOM   688  C  CB  . VAL B 1 36 ? 13.45967 10.04757  8.82685  0.996 32.04605  ? 36  VAL B CB  1 
ATOM   689  C  CG1 . VAL B 1 36 ? 14.40291 11.23478  8.86100  0.780 31.85757  ? 36  VAL B CG1 1 
ATOM   690  C  CG2 . VAL B 1 36 ? 13.13138 9.60062   10.25059 1.000 31.76990  ? 36  VAL B CG2 1 
ATOM   691  N  N   . ASN B 1 37 ? 11.92933 8.13701   7.13758  0.705 35.63624  ? 37  ASN B N   1 
ATOM   692  C  CA  . ASN B 1 37 ? 11.33170 6.81130   6.98400  1.000 37.78491  ? 37  ASN B CA  1 
ATOM   693  C  C   . ASN B 1 37 ? 12.43563 5.75470   6.96735  0.780 37.13805  ? 37  ASN B C   1 
ATOM   694  O  O   . ASN B 1 37 ? 13.61803 6.06183   7.13521  1.000 36.47959  ? 37  ASN B O   1 
ATOM   695  C  CB  . ASN B 1 37 ? 10.32489 6.74234   5.81815  0.668 40.15781  ? 37  ASN B CB  1 
ATOM   696  C  CG  . ASN B 1 37 ? 10.97326 6.89303   4.44331  0.393 42.00120  ? 37  ASN B CG  1 
ATOM   697  O  OD1 . ASN B 1 37 ? 12.15479 6.61255   4.25262  1.000 43.06416  ? 37  ASN B OD1 1 
ATOM   698  N  ND2 . ASN B 1 37 ? 10.17714 7.32357   3.46890  0.697 42.56629  ? 37  ASN B ND2 1 
ATOM   699  N  N   . SER B 1 38 ? 12.04478 4.49211   6.75733  0.777 36.81967  ? 38  SER B N   1 
ATOM   700  C  CA  . SER B 1 38 ? 13.05102 3.42394   6.83766  0.552 35.74966  ? 38  SER B CA  1 
ATOM   701  C  C   . SER B 1 38 ? 14.03051 3.41489   5.66128  0.457 34.94728  ? 38  SER B C   1 
ATOM   702  O  O   . SER B 1 38 ? 14.85472 2.49296   5.55525  0.732 34.45099  ? 38  SER B O   1 
ATOM   703  C  CB  . SER B 1 38 ? 12.39285 2.05183   7.00735  0.858 35.53828  ? 38  SER B CB  1 
ATOM   704  O  OG  . SER B 1 38 ? 11.51755 1.76328   5.93219  0.566 35.31330  ? 38  SER B OG  1 
ATOM   705  N  N   . ASP B 1 39 ? 13.99138 4.41026   4.77790  1.000 34.65488  ? 39  ASP B N   1 
ATOM   706  C  CA  . ASP B 1 39 ? 14.88477 4.41631   3.62794  0.886 34.54311  ? 39  ASP B CA  1 
ATOM   707  C  C   . ASP B 1 39 ? 16.24434 5.03201   3.94292  1.000 33.82796  ? 39  ASP B C   1 
ATOM   708  O  O   . ASP B 1 39 ? 17.19188 4.82335   3.17696  0.661 34.20503  ? 39  ASP B O   1 
ATOM   709  C  CB  . ASP B 1 39 ? 14.23576 5.15510   2.45471  0.484 34.90442  ? 39  ASP B CB  1 
ATOM   710  C  CG  . ASP B 1 39 ? 13.06647 4.39145   1.85606  0.347 35.78561  ? 39  ASP B CG  1 
ATOM   711  O  OD1 . ASP B 1 39 ? 12.91955 3.18638   2.15004  0.404 36.30932  ? 39  ASP B OD1 1 
ATOM   712  O  OD2 . ASP B 1 39 ? 12.28452 5.00389   1.09945  0.221 36.20644  ? 39  ASP B OD2 1 
ATOM   713  N  N   . VAL B 1 40 ? 16.36816 5.78256   5.04229  1.000 32.71319  ? 40  VAL B N   1 
ATOM   714  C  CA  . VAL B 1 40 ? 17.63661 6.43933   5.33936  1.000 32.13872  ? 40  VAL B CA  1 
ATOM   715  C  C   . VAL B 1 40 ? 18.67360 5.40742   5.76173  0.866 32.28922  ? 40  VAL B C   1 
ATOM   716  O  O   . VAL B 1 40 ? 18.36486 4.43232   6.46385  0.661 32.77061  ? 40  VAL B O   1 
ATOM   717  C  CB  . VAL B 1 40 ? 17.47351 7.55343   6.39226  1.000 32.78989  ? 40  VAL B CB  1 
ATOM   718  C  CG1 . VAL B 1 40 ? 16.51875 8.62496   5.89142  0.767 33.82059  ? 40  VAL B CG1 1 
ATOM   719  C  CG2 . VAL B 1 40 ? 17.01246 6.98853   7.74097  0.916 33.01927  ? 40  VAL B CG2 1 
ATOM   720  N  N   . GLU B 1 41 ? 19.92325 5.63342   5.35081  0.815 32.21162  ? 41  GLU B N   1 
ATOM   721  C  CA  . GLU B 1 41 ? 21.00654 4.71192   5.68724  1.000 32.91412  ? 41  GLU B CA  1 
ATOM   722  C  C   . GLU B 1 41 ? 21.41216 4.83136   7.14857  0.853 32.55976  ? 41  GLU B C   1 
ATOM   723  O  O   . GLU B 1 41 ? 21.60936 3.82095   7.83353  0.592 33.84703  ? 41  GLU B O   1 
ATOM   724  C  CB  . GLU B 1 41 ? 22.21014 4.96172   4.77844  1.000 34.12365  ? 41  GLU B CB  1 
ATOM   725  C  CG  . GLU B 1 41 ? 23.02135 3.72002   4.50812  0.487 35.28876  ? 41  GLU B CG  1 
ATOM   726  C  CD  . GLU B 1 41 ? 24.26398 4.01088   3.69835  0.621 36.20329  ? 41  GLU B CD  1 
ATOM   727  O  OE1 . GLU B 1 41 ? 24.24388 4.98365   2.91470  0.414 36.60672  ? 41  GLU B OE1 1 
ATOM   728  O  OE2 . GLU B 1 41 ? 25.26099 3.27412   3.85119  0.299 36.78851  ? 41  GLU B OE2 1 
ATOM   729  N  N   . HIS B 1 42 ? 21.57769 6.05582   7.62774  1.000 32.24472  ? 42  HIS B N   1 
ATOM   730  C  CA  . HIS B 1 42 ? 21.97899 6.30889   9.00050  1.000 33.23073  ? 42  HIS B CA  1 
ATOM   731  C  C   . HIS B 1 42 ? 21.03555 7.34237   9.59926  0.704 30.68075  ? 42  HIS B C   1 
ATOM   732  O  O   . HIS B 1 42 ? 20.39793 8.11958   8.88239  0.931 31.51310  ? 42  HIS B O   1 
ATOM   733  C  CB  . HIS B 1 42 ? 23.42034 6.82461   9.06989  0.665 35.37614  ? 42  HIS B CB  1 
ATOM   734  C  CG  . HIS B 1 42 ? 24.42073 5.91482   8.42908  1.000 37.86696  ? 42  HIS B CG  1 
ATOM   735  N  ND1 . HIS B 1 42 ? 24.54848 4.58460   8.76851  0.352 38.31128  ? 42  HIS B ND1 1 
ATOM   736  C  CD2 . HIS B 1 42 ? 25.35094 6.14930   7.47323  0.677 38.41386  ? 42  HIS B CD2 1 
ATOM   737  C  CE1 . HIS B 1 42 ? 25.51077 4.03810   8.04508  0.552 38.77068  ? 42  HIS B CE1 1 
ATOM   738  N  NE2 . HIS B 1 42 ? 26.01467 4.96655   7.25243  0.510 38.84376  ? 42  HIS B NE2 1 
ATOM   739  N  N   . TYR B 1 43 ? 20.93920 7.34984   10.92820 1.000 29.16983  ? 43  TYR B N   1 
ATOM   740  C  CA  . TYR B 1 43 ? 20.05809 8.29139   11.60214 1.000 26.98675  ? 43  TYR B CA  1 
ATOM   741  C  C   . TYR B 1 43 ? 20.68001 8.77831   12.90309 1.000 26.21299  ? 43  TYR B C   1 
ATOM   742  O  O   . TYR B 1 43 ? 21.18261 7.97340   13.69443 0.784 26.12277  ? 43  TYR B O   1 
ATOM   743  C  CB  . TYR B 1 43 ? 18.69014 7.66968   11.89821 0.827 26.27515  ? 43  TYR B CB  1 
ATOM   744  C  CG  . TYR B 1 43 ? 17.77899 8.67802   12.52078 0.816 25.05338  ? 43  TYR B CG  1 
ATOM   745  C  CD1 . TYR B 1 43 ? 17.23328 9.70330   11.76470 1.000 24.36097  ? 43  TYR B CD1 1 
ATOM   746  C  CD2 . TYR B 1 43 ? 17.52230 8.65136   13.87938 1.000 23.55879  ? 43  TYR B CD2 1 
ATOM   747  C  CE1 . TYR B 1 43 ? 16.42041 10.65166  12.33363 0.944 24.13425  ? 43  TYR B CE1 1 
ATOM   748  C  CE2 . TYR B 1 43 ? 16.71208 9.59342   14.46285 1.000 23.14373  ? 43  TYR B CE2 1 
ATOM   749  C  CZ  . TYR B 1 43 ? 16.17301 10.59707  13.68675 1.000 22.99372  ? 43  TYR B CZ  1 
ATOM   750  O  OH  . TYR B 1 43 ? 15.37822 11.55071  14.24469 0.799 21.98675  ? 43  TYR B OH  1 
ATOM   751  N  N   . LEU B 1 44 ? 20.60402 10.08943  13.12835 0.842 26.15045  ? 44  LEU B N   1 
ATOM   752  C  CA  . LEU B 1 44 ? 20.93647 10.71121  14.40499 0.902 25.41430  ? 44  LEU B CA  1 
ATOM   753  C  C   . LEU B 1 44 ? 19.75728 11.54001  14.89263 0.987 24.37647  ? 44  LEU B C   1 
ATOM   754  O  O   . LEU B 1 44 ? 19.08698 12.21656  14.11106 0.911 24.07734  ? 44  LEU B O   1 
ATOM   755  C  CB  . LEU B 1 44 ? 22.14785 11.63369  14.22999 0.828 25.94171  ? 44  LEU B CB  1 
ATOM   756  C  CG  . LEU B 1 44 ? 23.47712 10.93350  13.97472 0.792 26.82686  ? 44  LEU B CG  1 
ATOM   757  C  CD1 . LEU B 1 44 ? 24.59529 11.95635  13.73257 0.609 27.18877  ? 44  LEU B CD1 1 
ATOM   758  C  CD2 . LEU B 1 44 ? 23.83755 9.98790   15.11052 0.697 27.09280  ? 44  LEU B CD2 1 
ATOM   759  N  N   . CYS B 1 45 ? 19.50784 11.49686  16.19277 1.000 23.58306  ? 45  CYS B N   1 
ATOM   760  C  CA  . CYS B 1 45 ? 18.46402 12.31387  16.77720 0.977 22.88729  ? 45  CYS B CA  1 
ATOM   761  C  C   . CYS B 1 45 ? 18.84788 13.79674  16.75307 1.000 22.48820  ? 45  CYS B C   1 
ATOM   762  O  O   . CYS B 1 45 ? 19.96226 14.17824  16.37358 1.000 24.08612  ? 45  CYS B O   1 
ATOM   763  C  CB  . CYS B 1 45 ? 18.16240 11.82124  18.18979 1.000 21.79135  ? 45  CYS B CB  1 
ATOM   764  S  SG  . CYS B 1 45 ? 19.41501 12.29366  19.41722 0.966 21.41446  ? 45  CYS B SG  1 
ATOM   765  N  N   . GLU B 1 46 ? 17.89253 14.63692  17.17213 0.785 22.24335  ? 46  GLU B N   1 
ATOM   766  C  CA  . GLU B 1 46 ? 18.02249 16.09197  17.14691 0.975 23.00452  ? 46  GLU B CA  1 
ATOM   767  C  C   . GLU B 1 46 ? 18.87342 16.64315  18.28797 0.916 23.14958  ? 46  GLU B C   1 
ATOM   768  O  O   . GLU B 1 46 ? 19.19653 17.83743  18.28118 0.705 23.18328  ? 46  GLU B O   1 
ATOM   769  C  CB  . GLU B 1 46 ? 16.62932 16.74198  17.15439 0.987 22.41774  ? 46  GLU B CB  1 
ATOM   770  C  CG  . GLU B 1 46 ? 16.07631 17.11153  18.53967 1.000 21.90210  ? 46  GLU B CG  1 
ATOM   771  C  CD  . GLU B 1 46 ? 15.72548 15.92076  19.40649 0.663 21.26834  ? 46  GLU B CD  1 
ATOM   772  O  OE1 . GLU B 1 46 ? 15.87649 14.75819  18.96748 0.831 20.96559  ? 46  GLU B OE1 1 
ATOM   773  O  OE2 . GLU B 1 46 ? 15.28406 16.16552  20.54650 0.721 21.38475  ? 46  GLU B OE2 1 
ATOM   774  N  N   . GLN B 1 47 ? 19.25185 15.81761  19.26009 1.000 22.63228  ? 47  GLN B N   1 
ATOM   775  C  CA  . GLN B 1 47 ? 20.24259 16.24090  20.23979 1.000 23.65031  ? 47  GLN B CA  1 
ATOM   776  C  C   . GLN B 1 47 ? 21.65174 15.86945  19.79024 0.662 24.33740  ? 47  GLN B C   1 
ATOM   777  O  O   . GLN B 1 47 ? 22.58029 16.66595  19.94965 0.690 24.14719  ? 47  GLN B O   1 
ATOM   778  C  CB  . GLN B 1 47 ? 19.90535 15.67497  21.62331 1.000 23.91534  ? 47  GLN B CB  1 
ATOM   779  C  CG  . GLN B 1 47 ? 18.59650 16.20655  22.20076 1.000 24.81676  ? 47  GLN B CG  1 
ATOM   780  C  CD  . GLN B 1 47 ? 18.59829 17.70911  22.44822 1.000 26.22489  ? 47  GLN B CD  1 
ATOM   781  O  OE1 . GLN B 1 47 ? 19.62757 18.30304  22.74704 0.748 26.62657  ? 47  GLN B OE1 1 
ATOM   782  N  NE2 . GLN B 1 47 ? 17.42864 18.32981  22.31083 0.867 26.91866  ? 47  GLN B NE2 1 
ATOM   783  N  N   . CYS B 1 48 ? 21.81750 14.69345  19.17519 1.000 25.01280  ? 48  CYS B N   1 
ATOM   784  C  CA  . CYS B 1 48 ? 23.11783 14.30996  18.63587 1.000 26.67525  ? 48  CYS B CA  1 
ATOM   785  C  C   . CYS B 1 48 ? 23.48924 15.14648  17.41683 0.804 25.67588  ? 48  CYS B C   1 
ATOM   786  O  O   . CYS B 1 48 ? 24.67970 15.38514  17.16843 0.804 26.83752  ? 48  CYS B O   1 
ATOM   787  C  CB  . CYS B 1 48 ? 23.11313 12.81918  18.28056 1.000 26.68608  ? 48  CYS B CB  1 
ATOM   788  S  SG  . CYS B 1 48 ? 23.09949 11.72562  19.74147 1.000 27.53725  ? 48  CYS B SG  1 
ATOM   789  N  N   . ASP B 1 49 ? 22.49446 15.59587  16.64714 0.914 26.93221  ? 49  ASP B N   1 
ATOM   790  C  CA  . ASP B 1 49 ? 22.70507 16.35040  15.40820 1.000 29.32062  ? 49  ASP B CA  1 
ATOM   791  C  C   . ASP B 1 49 ? 21.65075 17.44776  15.33959 1.000 30.95733  ? 49  ASP B C   1 
ATOM   792  O  O   . ASP B 1 49 ? 20.63159 17.31836  14.64771 1.000 31.40284  ? 49  ASP B O   1 
ATOM   793  C  CB  . ASP B 1 49 ? 22.61054 15.42823  14.19050 1.000 30.43365  ? 49  ASP B CB  1 
ATOM   794  C  CG  . ASP B 1 49 ? 23.00377 16.11022  12.91457 0.718 31.91926  ? 49  ASP B CG  1 
ATOM   795  O  OD1 . ASP B 1 49 ? 23.51947 17.24974  12.96748 0.849 31.93360  ? 49  ASP B OD1 1 
ATOM   796  O  OD2 . ASP B 1 49 ? 22.77662 15.50250  11.84973 0.714 32.07552  ? 49  ASP B OD2 1 
ATOM   797  N  N   . PRO B 1 50 ? 21.86680 18.55229  16.05253 0.942 30.44728  ? 50  PRO B N   1 
ATOM   798  C  CA  . PRO B 1 50 ? 20.81681 19.56860  16.18583 0.836 30.65851  ? 50  PRO B CA  1 
ATOM   799  C  C   . PRO B 1 50 ? 20.47236 20.20324  14.84978 0.795 30.16952  ? 50  PRO B C   1 
ATOM   800  O  O   . PRO B 1 50 ? 21.34921 20.46967  14.02596 0.610 29.18329  ? 50  PRO B O   1 
ATOM   801  C  CB  . PRO B 1 50 ? 21.43633 20.58262  17.14842 0.599 31.17351  ? 50  PRO B CB  1 
ATOM   802  C  CG  . PRO B 1 50 ? 22.40009 19.77177  17.94419 0.529 31.19692  ? 50  PRO B CG  1 
ATOM   803  C  CD  . PRO B 1 50 ? 22.96587 18.75936  17.00797 1.000 30.93560  ? 50  PRO B CD  1 
ATOM   804  N  N   . ARG B 1 51 ? 19.18291 20.45536  14.64786 0.825 30.18247  ? 51  ARG B N   1 
ATOM   805  C  CA  . ARG B 1 51 ? 18.67663 20.90525  13.35845 0.870 31.54968  ? 51  ARG B CA  1 
ATOM   806  C  C   . ARG B 1 51 ? 17.21392 21.30498  13.52949 0.640 33.53770  ? 51  ARG B C   1 
ATOM   807  O  O   . ARG B 1 51 ? 16.56156 20.87641  14.48536 0.722 32.43777  ? 51  ARG B O   1 
ATOM   808  C  CB  . ARG B 1 51 ? 18.77932 19.78558  12.31440 1.000 30.80573  ? 51  ARG B CB  1 
ATOM   809  C  CG  . ARG B 1 51 ? 18.02395 18.52576  12.70075 0.687 28.92984  ? 51  ARG B CG  1 
ATOM   810  C  CD  . ARG B 1 51 ? 18.42307 17.34123  11.83849 0.970 27.61035  ? 51  ARG B CD  1 
ATOM   811  N  NE  . ARG B 1 51 ? 17.55501 16.18874  12.05623 0.649 25.81263  ? 51  ARG B NE  1 
ATOM   812  C  CZ  . ARG B 1 51 ? 17.81486 15.21773  12.92782 0.863 25.12485  ? 51  ARG B CZ  1 
ATOM   813  N  NH1 . ARG B 1 51 ? 18.91476 15.27199  13.66738 1.000 26.37281  ? 51  ARG B NH1 1 
ATOM   814  N  NH2 . ARG B 1 51 ? 16.98065 14.19875  13.06947 0.796 25.53809  ? 51  ARG B NH2 1 
ATOM   815  N  N   . PRO B 1 52 ? 16.68262 22.11740  12.61633 0.706 36.77818  ? 52  PRO B N   1 
ATOM   816  C  CA  . PRO B 1 52 ? 15.23116 22.32805  12.58190 1.000 38.96280  ? 52  PRO B CA  1 
ATOM   817  C  C   . PRO B 1 52 ? 14.53036 21.04490  12.16957 0.935 40.60272  ? 52  PRO B C   1 
ATOM   818  O  O   . PRO B 1 52 ? 14.96264 20.35010  11.24660 0.564 41.12586  ? 52  PRO B O   1 
ATOM   819  C  CB  . PRO B 1 52 ? 15.05665 23.41154  11.51093 0.708 38.59350  ? 52  PRO B CB  1 
ATOM   820  C  CG  . PRO B 1 52 ? 16.39127 24.09195  11.43986 0.551 37.98677  ? 52  PRO B CG  1 
ATOM   821  C  CD  . PRO B 1 52 ? 17.38947 23.00060  11.67580 0.777 37.46025  ? 52  PRO B CD  1 
ATOM   822  N  N   . VAL B 1 53 ? 13.44366 20.72924  12.86504 1.000 41.64052  ? 53  VAL B N   1 
ATOM   823  C  CA  . VAL B 1 53 ? 12.66259 19.54299  12.53094 1.000 42.83249  ? 53  VAL B CA  1 
ATOM   824  C  C   . VAL B 1 53 ? 11.27433 19.92187  12.01632 1.000 43.32268  ? 53  VAL B C   1 
ATOM   825  O  O   . VAL B 1 53 ? 11.14091 20.51974  10.94647 0.644 43.95267  ? 53  VAL B O   1 
ATOM   826  C  CB  . VAL B 1 53 ? 12.58534 18.55236  13.70972 1.000 43.26340  ? 53  VAL B CB  1 
ATOM   827  C  CG1 . VAL B 1 53 ? 11.95759 17.24745  13.25417 0.704 43.28799  ? 53  VAL B CG1 1 
ATOM   828  C  CG2 . VAL B 1 53 ? 13.97172 18.30779  14.29979 0.817 43.16993  ? 53  VAL B CG2 1 
ATOM   829  N  N   . ALA C 2 1  ? 19.63644 2.45330   8.87621  0.417 34.83683  ? 1   ALA P N   1 
ATOM   830  C  CA  . ALA C 2 1  ? 19.16568 2.80811   10.21147 1.000 35.10974  ? 1   ALA P CA  1 
ATOM   831  C  C   . ALA C 2 1  ? 18.29488 1.69131   10.78306 0.372 34.43791  ? 1   ALA P C   1 
ATOM   832  O  O   . ALA C 2 1  ? 17.63383 0.97139   10.03730 0.839 35.05912  ? 1   ALA P O   1 
ATOM   833  C  CB  . ALA C 2 1  ? 18.40060 4.11487   10.16271 0.749 35.19638  ? 1   ALA P CB  1 
ATOM   834  N  N   . ARG C 2 2  ? 18.30076 1.53079   12.10358 1.000 32.95766  ? 2   ARG P N   1 
ATOM   835  C  CA  . ARG C 2 2  ? 17.45438 0.52357   12.72515 1.000 31.36854  ? 2   ARG P CA  1 
ATOM   836  C  C   . ARG C 2 2  ? 16.05377 1.08322   12.92202 1.000 28.63016  ? 2   ARG P C   1 
ATOM   837  O  O   . ARG C 2 2  ? 15.88050 2.15907   13.50547 1.000 28.04201  ? 2   ARG P O   1 
ATOM   838  C  CB  . ARG C 2 2  ? 18.02010 0.06450   14.06659 1.000 32.95900  ? 2   ARG P CB  1 
ATOM   839  C  CG  . ARG C 2 2  ? 17.21493 -1.08896  14.64615 0.659 34.94718  ? 2   ARG P CG  1 
ATOM   840  C  CD  . ARG C 2 2  ? 17.95665 -1.87436  15.70950 0.599 36.58986  ? 2   ARG P CD  1 
ATOM   841  N  NE  . ARG C 2 2  ? 17.06646 -2.84607  16.33852 0.623 37.96323  ? 2   ARG P NE  1 
ATOM   842  C  CZ  . ARG C 2 2  ? 17.16898 -3.25257  17.59967 0.383 38.61469  ? 2   ARG P CZ  1 
ATOM   843  N  NH1 . ARG C 2 2  ? 18.12541 -2.76888  18.38001 0.479 38.87265  ? 2   ARG P NH1 1 
ATOM   844  N  NH2 . ARG C 2 2  ? 16.30895 -4.13795  18.08428 0.442 38.82211  ? 2   ARG P NH2 1 
ATOM   845  N  N   . THR C 2 3  ? 15.06033 0.36135   12.41581 0.843 28.15161  ? 3   THR P N   1 
ATOM   846  C  CA  . THR C 2 3  ? 13.67474 0.76671   12.56063 1.000 28.30523  ? 3   THR P CA  1 
ATOM   847  C  C   . THR C 2 3  ? 12.81850 -0.35802  13.12278 0.882 27.58954  ? 3   THR P C   1 
ATOM   848  O  O   . THR C 2 3  ? 13.23072 -1.51837  13.17726 0.664 28.17879  ? 3   THR P O   1 
ATOM   849  C  CB  . THR C 2 3  ? 13.06940 1.27203   11.21908 0.732 28.79501  ? 3   THR P CB  1 
ATOM   850  O  OG1 . THR C 2 3  ? 12.99013 0.19380   10.27399 0.703 29.92387  ? 3   THR P OG1 1 
ATOM   851  C  CG2 . THR C 2 3  ? 13.90707 2.41011   10.63090 0.848 28.74138  ? 3   THR P CG2 1 
HETATM 852  N  N   . M3L C 2 4  ? 11.61992 -0.00211  13.55343 1.000 28.16184  ? 4   M3L P N   1 
HETATM 853  C  CA  . M3L C 2 4  ? 10.69712 -0.97638  14.04467 1.000 28.93308  ? 4   M3L P CA  1 
HETATM 854  C  CB  . M3L C 2 4  ? 10.92282 -1.34448  15.52650 0.824 27.92909  ? 4   M3L P CB  1 
HETATM 855  C  CG  . M3L C 2 4  ? 10.54777 -0.21920  16.47482 1.000 26.93215  ? 4   M3L P CG  1 
HETATM 856  C  CD  . M3L C 2 4  ? 10.86672 -0.56442  17.91839 1.000 27.10257  ? 4   M3L P CD  1 
HETATM 857  C  CE  . M3L C 2 4  ? 10.40745 0.59832   18.78393 0.885 26.72874  ? 4   M3L P CE  1 
HETATM 858  N  NZ  . M3L C 2 4  ? 10.45599 0.38010   20.27855 1.000 26.42726  ? 4   M3L P NZ  1 
HETATM 859  C  C   . M3L C 2 4  ? 9.28003  -0.47064  13.87017 0.664 30.06213  ? 4   M3L P C   1 
HETATM 860  O  O   . M3L C 2 4  ? 9.01031  0.72206   13.71921 1.000 30.10635  ? 4   M3L P O   1 
HETATM 861  C  CM1 . M3L C 2 4  ? 11.82622 -0.03117  20.70158 0.703 27.47568  ? 4   M3L P CM1 1 
HETATM 862  C  CM2 . M3L C 2 4  ? 9.46826  -0.65868  20.71206 0.905 27.30450  ? 4   M3L P CM2 1 
HETATM 863  C  CM3 . M3L C 2 4  ? 10.10447 1.69599   20.89897 1.000 26.35023  ? 4   M3L P CM3 1 
ATOM   864  N  N   . GLN C 2 5  ? 8.35147  -1.41923  13.87359 1.000 32.26054  ? 5   GLN P N   1 
ATOM   865  C  CA  . GLN C 2 5  ? 6.93425  -1.10758  13.95522 1.000 34.41775  ? 5   GLN P CA  1 
ATOM   866  C  C   . GLN C 2 5  ? 6.25171  -2.26547  14.67660 1.000 35.61217  ? 5   GLN P C   1 
ATOM   867  O  O   . GLN C 2 5  ? 6.02843  -3.33347  14.10157 0.748 35.06754  ? 5   GLN P O   1 
ATOM   868  C  CB  . GLN C 2 5  ? 6.32896  -0.87919  12.57138 1.000 35.98308  ? 5   GLN P CB  1 
ATOM   869  C  CG  . GLN C 2 5  ? 4.92084  -0.31060  12.61788 1.000 37.41187  ? 5   GLN P CG  1 
ATOM   870  C  CD  . GLN C 2 5  ? 4.38716  0.02592   11.24601 1.000 38.42090  ? 5   GLN P CD  1 
ATOM   871  O  OE1 . GLN C 2 5  ? 3.36212  0.69319   11.11489 0.497 38.76180  ? 5   GLN P OE1 1 
ATOM   872  N  NE2 . GLN C 2 5  ? 5.06187  -0.46709  10.20885 0.499 38.52604  ? 5   GLN P NE2 1 
ATOM   873  N  N   . THR C 2 6  ? 5.92749  -2.03497  15.94899 1.000 37.69755  ? 6   THR P N   1 
ATOM   874  C  CA  . THR C 2 6  ? 5.49977  -3.11985  16.82593 0.769 38.62229  ? 6   THR P CA  1 
ATOM   875  C  C   . THR C 2 6  ? 4.15009  -3.68913  16.39868 0.171 39.99252  ? 6   THR P C   1 
ATOM   876  O  O   . THR C 2 6  ? 3.99059  -4.90967  16.28013 0.758 40.22133  ? 6   THR P O   1 
ATOM   877  C  CB  . THR C 2 6  ? 5.45074  -2.61619  18.26642 0.636 38.30565  ? 6   THR P CB  1 
ATOM   878  O  OG1 . THR C 2 6  ? 6.77989  -2.30175  18.69840 0.846 38.12911  ? 6   THR P OG1 1 
ATOM   879  C  CG2 . THR C 2 6  ? 4.87319  -3.68041  19.17790 0.680 38.01570  ? 6   THR P CG2 1 
ATOM   880  N  N   . ALA C 2 7  ? 3.16537  -2.82277  16.16140 1.000 41.11048  ? 7   ALA P N   1 
ATOM   881  C  CA  . ALA C 2 7  ? 1.81840  -3.28379  15.83986 1.000 42.53213  ? 7   ALA P CA  1 
ATOM   882  C  C   . ALA C 2 7  ? 1.47725  -3.04951  14.37464 0.592 43.22679  ? 7   ALA P C   1 
ATOM   883  O  O   . ALA C 2 7  ? 0.48158  -2.38823  14.06150 0.669 43.45747  ? 7   ALA P O   1 
ATOM   884  C  CB  . ALA C 2 7  ? 0.79103  -2.58993  16.73690 0.512 42.35292  ? 7   ALA P CB  1 
ATOM   885  N  N   . ARG C 2 8  ? 2.28292  -3.60113  13.47185 1.000 43.54578  ? 8   ARG P N   1 
ATOM   886  C  CA  . ARG C 2 8  ? 2.10096  -3.33788  12.05229 1.000 44.02761  ? 8   ARG P CA  1 
ATOM   887  C  C   . ARG C 2 8  ? 0.89597  -4.09495  11.50762 0.049 45.16077  ? 8   ARG P C   1 
ATOM   888  O  O   . ARG C 2 8  ? 0.67171  -5.26402  11.83274 0.580 45.67859  ? 8   ARG P O   1 
ATOM   889  C  CB  . ARG C 2 8  ? 3.35641  -3.74093  11.28651 0.772 42.86202  ? 8   ARG P CB  1 
ATOM   890  C  CG  . ARG C 2 8  ? 3.29564  -3.46491  9.80409  0.733 41.48998  ? 8   ARG P CG  1 
ATOM   891  C  CD  . ARG C 2 8  ? 4.42389  -4.19233  9.10876  0.875 39.84286  ? 8   ARG P CD  1 
ATOM   892  N  NE  . ARG C 2 8  ? 4.20809  -5.63533  9.09834  0.532 38.62718  ? 8   ARG P NE  1 
ATOM   893  C  CZ  . ARG C 2 8  ? 3.41209  -6.26737  8.24189  0.607 37.21196  ? 8   ARG P CZ  1 
ATOM   894  N  NH1 . ARG C 2 8  ? 2.75830  -5.58619  7.31259  0.554 37.17946  ? 8   ARG P NH1 1 
ATOM   895  N  NH2 . ARG C 2 8  ? 3.27345  -7.58307  8.31215  0.658 36.66795  ? 8   ARG P NH2 1 
ATOM   896  N  N   . LYS C 2 9  ? 0.12340  -3.41718  10.66465 1.000 45.26863  ? 9   LYS P N   1 
ATOM   897  C  CA  . LYS C 2 9  ? -1.07211 -4.00098  10.07608 0.780 44.94491  ? 9   LYS P CA  1 
ATOM   898  C  C   . LYS C 2 9  ? -0.69337 -4.89284  8.89897  0.425 42.96716  ? 9   LYS P C   1 
ATOM   899  O  O   . LYS C 2 9  ? 0.07046  -4.48463  8.01732  0.568 42.83970  ? 9   LYS P O   1 
ATOM   900  C  CB  . LYS C 2 9  ? -1.99001 -2.88408  9.59660  0.464 46.06417  ? 9   LYS P CB  1 
ATOM   901  C  CG  . LYS C 2 9  ? -3.32177 -3.36764  9.10175  0.542 46.88714  ? 9   LYS P CG  1 
ATOM   902  C  CD  . LYS C 2 9  ? -4.19461 -2.18828  8.76527  0.374 47.44309  ? 9   LYS P CD  1 
ATOM   903  C  CE  . LYS C 2 9  ? -5.54603 -2.65101  8.32404  0.316 47.74700  ? 9   LYS P CE  1 
ATOM   904  N  NZ  . LYS C 2 9  ? -6.41456 -1.49995  7.99216  0.679 48.21194  ? 9   LYS P NZ  1 
ATOM   905  N  N   . SER C 2 10 ? -1.24411 -6.10405  8.87601  0.891 41.08014  ? 10  SER P N   1 
ATOM   906  C  CA  . SER C 2 10 ? -0.86884 -7.11987  7.90509  1.000 39.78704  ? 10  SER P CA  1 
ATOM   907  C  C   . SER C 2 10 ? -2.04767 -7.48652  7.01099  0.755 38.12855  ? 10  SER P C   1 
ATOM   908  O  O   . SER C 2 10 ? -3.21494 -7.29286  7.35858  0.665 38.97257  ? 10  SER P O   1 
ATOM   909  C  CB  . SER C 2 10 ? -0.33782 -8.37766  8.61004  0.654 39.73322  ? 10  SER P CB  1 
ATOM   910  O  OG  . SER C 2 10 ? -0.28374 -9.48462  7.72815  0.717 39.69611  ? 10  SER P OG  1 
ATOM   911  N  N   . THR C 2 11 ? -1.71613 -8.03606  5.84426  0.772 35.74240  ? 11  THR P N   1 
ATOM   912  C  CA  . THR C 2 11 ? -2.71909 -8.46321  4.87955  0.629 34.31433  ? 11  THR P CA  1 
ATOM   913  C  C   . THR C 2 11 ? -3.25123 -9.86299  5.15998  0.340 33.74993  ? 11  THR P C   1 
ATOM   914  O  O   . THR C 2 11 ? -4.28309 -10.24627 4.59514  1.000 32.50980  ? 11  THR P O   1 
ATOM   915  C  CB  . THR C 2 11 ? -2.09399 -8.45498  3.48876  1.000 34.28102  ? 11  THR P CB  1 
ATOM   916  O  OG1 . THR C 2 11 ? -0.98096 -9.35153  3.49329  0.828 33.40229  ? 11  THR P OG1 1 
ATOM   917  C  CG2 . THR C 2 11 ? -1.61446 -7.05532  3.13134  0.904 34.56678  ? 11  THR P CG2 1 
ATOM   918  N  N   . GLY C 2 12 ? -2.58012 -10.63102 6.01095  0.755 34.47798  ? 12  GLY P N   1 
ATOM   919  C  CA  . GLY C 2 12 ? -2.94186 -12.01916 6.22425  0.525 35.85199  ? 12  GLY P CA  1 
ATOM   920  C  C   . GLY C 2 12 ? -3.90104 -12.25004 7.37249  0.684 36.92283  ? 12  GLY P C   1 
ATOM   921  O  O   . GLY C 2 12 ? -4.23545 -13.39331 7.68176  0.369 37.57068  ? 12  GLY P O   1 
ATOM   922  N  N   . ALA D 2 1  ? 22.56578 5.38432   44.40270 0.507 36.07110  ? 1   ALA T N   1 
ATOM   923  C  CA  . ALA D 2 1  ? 22.23530 5.62646   43.00347 0.435 36.12864  ? 1   ALA T CA  1 
ATOM   924  C  C   . ALA D 2 1  ? 23.26288 6.56726   42.37710 0.678 35.42087  ? 1   ALA T C   1 
ATOM   925  O  O   . ALA D 2 1  ? 23.97139 7.27500   43.09121 0.867 36.10217  ? 1   ALA T O   1 
ATOM   926  C  CB  . ALA D 2 1  ? 20.84191 6.20065   42.89567 1.000 37.04233  ? 1   ALA T CB  1 
ATOM   927  N  N   . ARG D 2 2  ? 23.36570 6.57548   41.05010 1.000 33.57493  ? 2   ARG T N   1 
ATOM   928  C  CA  . ARG D 2 2  ? 24.35745 7.41160   40.39015 1.000 31.82807  ? 2   ARG T CA  1 
ATOM   929  C  C   . ARG D 2 2  ? 23.80112 8.81037   40.17303 1.000 28.87749  ? 2   ARG T C   1 
ATOM   930  O  O   . ARG D 2 2  ? 22.73680 8.97435   39.56822 1.000 28.10777  ? 2   ARG T O   1 
ATOM   931  C  CB  . ARG D 2 2  ? 24.82172 6.83309   39.05621 1.000 33.83504  ? 2   ARG T CB  1 
ATOM   932  C  CG  . ARG D 2 2  ? 26.05788 7.56782   38.58096 0.748 36.05119  ? 2   ARG T CG  1 
ATOM   933  C  CD  . ARG D 2 2  ? 26.64530 7.04288   37.30046 0.626 37.81291  ? 2   ARG T CD  1 
ATOM   934  N  NE  . ARG D 2 2  ? 27.55121 8.05058   36.76005 0.615 39.05318  ? 2   ARG T NE  1 
ATOM   935  C  CZ  . ARG D 2 2  ? 28.23288 7.92791   35.62828 0.302 39.95908  ? 2   ARG T CZ  1 
ATOM   936  N  NH1 . ARG D 2 2  ? 28.11048 6.83469   34.89002 0.483 40.48811  ? 2   ARG T NH1 1 
ATOM   937  N  NH2 . ARG D 2 2  ? 29.02587 8.91128   35.22778 0.393 40.11546  ? 2   ARG T NH2 1 
ATOM   938  N  N   . THR D 2 3  ? 24.51827 9.81035   40.67665 0.829 28.34226  ? 3   THR T N   1 
ATOM   939  C  CA  . THR D 2 3  ? 24.10811 11.19432  40.52371 1.000 27.93780  ? 3   THR T CA  1 
ATOM   940  C  C   . THR D 2 3  ? 25.23764 12.04285  39.96170 0.727 27.93406  ? 3   THR T C   1 
ATOM   941  O  O   . THR D 2 3  ? 26.39747 11.62948  39.92428 0.666 28.58361  ? 3   THR T O   1 
ATOM   942  C  CB  . THR D 2 3  ? 23.61411 11.81613  41.85907 0.798 28.03224  ? 3   THR T CB  1 
ATOM   943  O  OG1 . THR D 2 3  ? 24.68188 11.84336  42.81820 0.619 28.96177  ? 3   THR T OG1 1 
ATOM   944  C  CG2 . THR D 2 3  ? 22.45203 11.01022  42.42878 0.706 27.30411  ? 3   THR T CG2 1 
HETATM 945  N  N   . M3L D 2 4  ? 24.88464 13.23611  39.51095 1.000 28.78959  ? 4   M3L T N   1 
HETATM 946  C  CA  . M3L D 2 4  ? 25.86178 14.15135  39.01548 1.000 29.20576  ? 4   M3L T CA  1 
HETATM 947  C  CB  . M3L D 2 4  ? 26.22521 13.91080  37.53759 0.917 28.75523  ? 4   M3L T CB  1 
HETATM 948  C  CG  . M3L D 2 4  ? 25.11676 14.34091  36.59670 1.000 27.43881  ? 4   M3L T CG  1 
HETATM 949  C  CD  . M3L D 2 4  ? 25.44195 14.00395  35.15046 0.925 27.51077  ? 4   M3L T CD  1 
HETATM 950  C  CE  . M3L D 2 4  ? 24.30488 14.52061  34.28223 0.834 27.55888  ? 4   M3L T CE  1 
HETATM 951  N  NZ  . M3L D 2 4  ? 24.51625 14.42541  32.79149 1.000 27.04509  ? 4   M3L T NZ  1 
HETATM 952  C  C   . M3L D 2 4  ? 25.36736 15.57416  39.18478 0.656 30.34008  ? 4   M3L T C   1 
HETATM 953  O  O   . M3L D 2 4  ? 24.18141 15.85919  39.37344 1.000 30.66943  ? 4   M3L T O   1 
HETATM 954  C  CM1 . M3L D 2 4  ? 24.91176 13.03480  32.42728 0.771 28.14351  ? 4   M3L T CM1 1 
HETATM 955  C  CM2 . M3L D 2 4  ? 25.54693 15.39783  32.30882 0.910 28.01857  ? 4   M3L T CM2 1 
HETATM 956  C  CM3 . M3L D 2 4  ? 23.19255 14.75995  32.18054 0.905 26.28708  ? 4   M3L T CM3 1 
ATOM   957  N  N   . GLN D 2 5  ? 26.32012 16.49546  39.12157 1.000 31.91412  ? 5   GLN T N   1 
ATOM   958  C  CA  . GLN D 2 5  ? 26.01279 17.91224  39.11478 1.000 33.29829  ? 5   GLN T CA  1 
ATOM   959  C  C   . GLN D 2 5  ? 27.14363 18.62705  38.37624 1.000 34.35349  ? 5   GLN T C   1 
ATOM   960  O  O   . GLN D 2 5  ? 28.20650 18.87444  38.94119 0.619 33.76973  ? 5   GLN T O   1 
ATOM   961  C  CB  . GLN D 2 5  ? 25.88175 18.42095  40.54355 0.742 34.72320  ? 5   GLN T CB  1 
ATOM   962  C  CG  . GLN D 2 5  ? 25.38487 19.83628  40.65691 0.819 36.02966  ? 5   GLN T CG  1 
ATOM   963  C  CD  . GLN D 2 5  ? 25.11187 20.21433  42.09219 0.452 36.51574  ? 5   GLN T CD  1 
ATOM   964  O  OE1 . GLN D 2 5  ? 25.63839 19.59336  43.02381 0.740 36.82601  ? 5   GLN T OE1 1 
ATOM   965  N  NE2 . GLN D 2 5  ? 24.26973 21.22077  42.28551 0.715 36.77751  ? 5   GLN T NE2 1 
ATOM   966  N  N   . THR D 2 6  ? 26.90443 18.95466  37.10411 0.796 35.91470  ? 6   THR T N   1 
ATOM   967  C  CA  . THR D 2 6  ? 27.98693 19.41828  36.23868 0.864 37.64059  ? 6   THR T CA  1 
ATOM   968  C  C   . THR D 2 6  ? 28.52268 20.78456  36.65675 0.239 39.11116  ? 6   THR T C   1 
ATOM   969  O  O   . THR D 2 6  ? 29.74163 20.98860  36.69670 0.617 39.51821  ? 6   THR T O   1 
ATOM   970  C  CB  . THR D 2 6  ? 27.52742 19.43300  34.78297 0.649 37.58499  ? 6   THR T CB  1 
ATOM   971  O  OG1 . THR D 2 6  ? 26.90575 18.18179  34.47070 0.845 37.16514  ? 6   THR T OG1 1 
ATOM   972  C  CG2 . THR D 2 6  ? 28.70557 19.65578  33.85986 0.631 37.40533  ? 6   THR T CG2 1 
ATOM   973  N  N   . ALA D 2 7  ? 27.63995 21.73595  36.95683 1.000 39.97574  ? 7   ALA T N   1 
ATOM   974  C  CA  . ALA D 2 7  ? 28.08751 23.09464  37.24796 0.850 40.96164  ? 7   ALA T CA  1 
ATOM   975  C  C   . ALA D 2 7  ? 27.86226 23.46410  38.70736 0.658 41.70128  ? 7   ALA T C   1 
ATOM   976  O  O   . ALA D 2 7  ? 27.14449 24.42423  39.00588 0.644 41.47923  ? 7   ALA T O   1 
ATOM   977  C  CB  . ALA D 2 7  ? 27.37576 24.09606  36.33578 0.628 40.76365  ? 7   ALA T CB  1 
ATOM   978  N  N   . ARG D 2 8  ? 28.48664 22.72790  39.62222 1.000 42.48918  ? 8   ARG T N   1 
ATOM   979  C  CA  . ARG D 2 8  ? 28.20532 22.89806  41.03993 1.000 55.24325  ? 8   ARG T CA  1 
ATOM   980  C  C   . ARG D 2 8  ? 28.99428 24.06283  41.63026 1.000 79.88438  ? 8   ARG T C   1 
ATOM   981  O  O   . ARG D 2 8  ? 30.17571 24.25870  41.32674 1.000 84.04107  ? 8   ARG T O   1 
ATOM   982  C  CB  . ARG D 2 8  ? 28.52089 21.60994  41.79732 1.000 49.60953  ? 8   ARG T CB  1 
ATOM   983  C  CG  . ARG D 2 8  ? 28.30594 21.70132  43.29663 1.000 55.74735  ? 8   ARG T CG  1 
ATOM   984  C  CD  . ARG D 2 8  ? 29.01570 20.56394  44.00827 1.000 62.62775  ? 8   ARG T CD  1 
ATOM   985  N  NE  . ARG D 2 8  ? 30.46234 20.76372  44.03075 1.000 75.20776  ? 8   ARG T NE  1 
ATOM   986  C  CZ  . ARG D 2 8  ? 31.09824 21.53613  44.90626 1.000 61.94322  ? 8   ARG T CZ  1 
ATOM   987  N  NH1 . ARG D 2 8  ? 30.41767 22.18021  45.84238 1.000 43.01931  ? 8   ARG T NH1 1 
ATOM   988  N  NH2 . ARG D 2 8  ? 32.41658 21.66120  44.84912 1.000 64.65042  ? 8   ARG T NH2 1 
ATOM   989  N  N   . LYS D 2 9  ? 28.32214 24.83091  42.48499 1.000 49.41541  ? 9   LYS T N   1 
ATOM   990  C  CA  . LYS D 2 9  ? 28.92945 25.97735  43.14526 1.000 61.20023  ? 9   LYS T CA  1 
ATOM   991  C  C   . LYS D 2 9  ? 29.96636 25.49279  44.14996 1.000 77.84892  ? 9   LYS T C   1 
ATOM   992  O  O   . LYS D 2 9  ? 29.69320 24.59333  44.95053 1.000 75.87568  ? 9   LYS T O   1 
ATOM   993  C  CB  . LYS D 2 9  ? 27.83920 26.72491  43.90644 1.000 60.94910  ? 9   LYS T CB  1 
ATOM   994  C  CG  . LYS D 2 9  ? 26.79216 27.34948  43.01471 1.000 101.84519 ? 9   LYS T CG  1 
ATOM   995  C  CD  . LYS D 2 9  ? 25.71403 28.07093  43.80955 1.000 96.04783  ? 9   LYS T CD  1 
ATOM   996  C  CE  . LYS D 2 9  ? 24.69141 28.70514  42.87854 1.000 71.48631  ? 9   LYS T CE  1 
ATOM   997  N  NZ  . LYS D 2 9  ? 23.62790 29.41146  43.62502 1.000 90.97399  ? 9   LYS T NZ  1 
ATOM   998  N  N   . SER D 2 10 ? 31.15039 26.09441  44.12629 1.000 65.52897  ? 10  SER T N   1 
ATOM   999  C  CA  . SER D 2 10 ? 32.19458 25.75576  45.07964 1.000 54.07668  ? 10  SER T CA  1 
ATOM   1000 C  C   . SER D 2 10 ? 32.49201 26.94071  45.98869 0.730 47.89674  ? 10  SER T C   1 
ATOM   1001 O  O   . SER D 2 10 ? 32.39426 28.10218  45.58530 0.717 48.05433  ? 10  SER T O   1 
ATOM   1002 C  CB  . SER D 2 10 ? 33.48070 25.31915  44.37392 0.879 49.82033  ? 10  SER T CB  1 
ATOM   1003 O  OG  . SER D 2 10 ? 34.55317 25.23591  45.29641 0.643 47.57068  ? 10  SER T OG  1 
ATOM   1004 N  N   . THR D 2 11 ? 32.86003 26.62930  47.22813 1.000 41.48839  ? 11  THR T N   1 
ATOM   1005 C  CA  . THR D 2 11 ? 33.27372 27.64466  48.18554 1.000 68.14089  ? 11  THR T CA  1 
ATOM   1006 C  C   . THR D 2 11 ? 34.69410 28.14198  47.94162 1.000 60.63576  ? 11  THR T C   1 
ATOM   1007 O  O   . THR D 2 11 ? 35.09432 29.15157  48.53569 1.000 28.40345  ? 11  THR T O   1 
ATOM   1008 C  CB  . THR D 2 11 ? 33.20122 27.05175  49.59110 1.000 38.70291  ? 11  THR T CB  1 
ATOM   1009 O  OG1 . THR D 2 11 ? 34.06874 25.91187  49.65356 1.000 33.17578  ? 11  THR T OG1 1 
ATOM   1010 C  CG2 . THR D 2 11 ? 31.77354 26.61791  49.91578 1.000 37.93731  ? 11  THR T CG2 1 
ATOM   1011 N  N   . GLY D 2 12 ? 35.45853 27.46886  47.08698 1.000 43.18737  ? 12  GLY T N   1 
ATOM   1012 C  CA  . GLY D 2 12 ? 36.88026 27.73241  46.95900 1.000 47.85395  ? 12  GLY T CA  1 
ATOM   1013 C  C   . GLY D 2 12 ? 37.27417 28.93160  46.12326 1.000 68.84843  ? 12  GLY T C   1 
ATOM   1014 O  O   . GLY D 2 12 ? 38.46063 29.24714  46.01507 1.000 85.41822  ? 12  GLY T O   1 
HETATM 1015 ZN ZN  . ZN  E 3 .  ? 14.26276 3.85885   33.42150 1.000 25.30840  ? 101 ZN  A ZN  1 
HETATM 1016 ZN ZN  . ZN  F 3 .  ? 13.30331 17.69563  34.72052 0.864 16.17229  ? 102 ZN  A ZN  1 
HETATM 1017 ZN ZN  . ZN  G 3 .  ? 7.20218  11.59961  18.34958 0.896 16.48073  ? 101 ZN  B ZN  1 
HETATM 1018 ZN ZN  . ZN  H 3 .  ? 21.05163 10.64983  19.65135 1.000 25.46259  ? 102 ZN  B ZN  1 
HETATM 1019 O  O   . HOH I 4 .  ? 9.99862  19.19607  42.87055 1.000 51.93506  ? 201 HOH A O   1 
HETATM 1020 O  O   . HOH I 4 .  ? 14.91681 16.91970  45.18917 1.000 48.71330  ? 202 HOH A O   1 
HETATM 1021 O  O   . HOH I 4 .  ? 6.66914  10.84285  31.90279 1.000 48.25853  ? 203 HOH A O   1 
HETATM 1022 O  O   . HOH I 4 .  ? 21.69368 12.08023  23.99995 1.000 70.09424  ? 204 HOH A O   1 
HETATM 1023 O  O   . HOH I 4 .  ? 5.03353  1.07091   39.07540 1.000 37.15891  ? 205 HOH A O   1 
HETATM 1024 O  O   . HOH I 4 .  ? 24.92881 8.14118   30.82089 1.000 26.29930  ? 206 HOH A O   1 
HETATM 1025 O  O   . HOH I 4 .  ? 6.25449  17.52100  33.01269 1.000 64.61352  ? 207 HOH A O   1 
HETATM 1026 O  O   . HOH I 4 .  ? 24.08486 18.77281  36.15154 1.000 31.87881  ? 208 HOH A O   1 
HETATM 1027 O  O   . HOH I 4 .  ? 21.61640 5.11342   39.37160 1.000 39.07070  ? 209 HOH A O   1 
HETATM 1028 O  O   . HOH I 4 .  ? 18.301   19.048    43.306   1.000 50.44343  ? 210 HOH A O   1 
HETATM 1029 O  O   . HOH I 4 .  ? 23.20812 14.52671  26.24750 1.000 34.82411  ? 211 HOH A O   1 
HETATM 1030 O  O   . HOH I 4 .  ? 28.96483 9.71721   28.57512 1.000 43.28066  ? 212 HOH A O   1 
HETATM 1031 O  O   . HOH I 4 .  ? 28.964   11.868    31.729   1.000 60.82834  ? 213 HOH A O   1 
HETATM 1032 O  O   . HOH I 4 .  ? 23.21374 4.23015   37.15270 1.000 42.23720  ? 214 HOH A O   1 
HETATM 1033 O  O   . HOH I 4 .  ? 10.65723 9.85220   41.99880 1.000 30.12200  ? 215 HOH A O   1 
HETATM 1034 O  O   . HOH I 4 .  ? 10.23016 17.09456  25.21075 1.000 33.28733  ? 216 HOH A O   1 
HETATM 1035 O  O   . HOH I 4 .  ? 17.56340 18.77333  40.36004 1.000 23.73511  ? 217 HOH A O   1 
HETATM 1036 O  O   . HOH I 4 .  ? 14.42733 14.71309  27.33414 1.000 19.38073  ? 218 HOH A O   1 
HETATM 1037 O  O   . HOH I 4 .  ? 10.06260 13.78604  28.64156 1.000 43.76438  ? 219 HOH A O   1 
HETATM 1038 O  O   . HOH I 4 .  ? 19.80288 20.75660  24.70764 1.000 40.29366  ? 220 HOH A O   1 
HETATM 1039 O  O   . HOH I 4 .  ? 22.32450 7.79960   29.34470 1.000 25.49371  ? 221 HOH A O   1 
HETATM 1040 O  O   . HOH I 4 .  ? 13.96049 15.80122  29.76299 1.000 18.04169  ? 222 HOH A O   1 
HETATM 1041 O  O   . HOH I 4 .  ? 13.26128 5.83975   29.69584 1.000 20.23562  ? 223 HOH A O   1 
HETATM 1042 O  O   . HOH I 4 .  ? 18.73454 1.69360   27.92975 1.000 26.57935  ? 224 HOH A O   1 
HETATM 1043 O  O   . HOH I 4 .  ? 12.44418 13.95295  28.61004 1.000 86.61997  ? 225 HOH A O   1 
HETATM 1044 O  O   . HOH I 4 .  ? 22.08852 21.40330  28.81412 1.000 33.73089  ? 226 HOH A O   1 
HETATM 1045 O  O   . HOH I 4 .  ? 17.696   20.442    38.287   1.000 27.60797  ? 227 HOH A O   1 
HETATM 1046 O  O   . HOH I 4 .  ? 2.738    2.834     41.311   1.000 59.52266  ? 228 HOH A O   1 
HETATM 1047 O  O   . HOH I 4 .  ? 9.62546  11.20501  28.30626 1.000 20.90728  ? 229 HOH A O   1 
HETATM 1048 O  O   . HOH I 4 .  ? 28.68351 11.87357  26.83606 1.000 34.40434  ? 230 HOH A O   1 
HETATM 1049 O  O   . HOH I 4 .  ? 19.76409 20.56596  42.21460 1.000 35.36123  ? 231 HOH A O   1 
HETATM 1050 O  O   . HOH I 4 .  ? 12.50774 5.41348   41.85621 1.000 34.08010  ? 232 HOH A O   1 
HETATM 1051 O  O   . HOH I 4 .  ? 7.61235  9.61568   42.49803 1.000 52.66755  ? 233 HOH A O   1 
HETATM 1052 O  O   . HOH I 4 .  ? 22.97578 23.84664  37.21865 1.000 53.46285  ? 234 HOH A O   1 
HETATM 1053 O  O   . HOH I 4 .  ? 21.85804 2.34026   42.38850 1.000 52.68354  ? 235 HOH A O   1 
HETATM 1054 O  O   . HOH I 4 .  ? 19.73718 5.70253   27.95700 1.000 25.27294  ? 236 HOH A O   1 
HETATM 1055 O  O   . HOH I 4 .  ? 24.19765 15.45111  28.85680 1.000 32.72248  ? 237 HOH A O   1 
HETATM 1056 O  O   . HOH I 4 .  ? 22.924   13.531    22.319   1.000 43.25721  ? 238 HOH A O   1 
HETATM 1057 O  O   . HOH I 4 .  ? 15.65013 11.56493  48.53977 1.000 44.91619  ? 239 HOH A O   1 
HETATM 1058 O  O   . HOH I 4 .  ? 7.75395  12.23383  43.44212 1.000 51.68899  ? 240 HOH A O   1 
HETATM 1059 O  O   . HOH I 4 .  ? 13.179   21.241    45.490   1.000 51.71863  ? 241 HOH A O   1 
HETATM 1060 O  O   . HOH I 4 .  ? 19.220   27.060    38.477   1.000 50.80687  ? 242 HOH A O   1 
HETATM 1061 O  O   . HOH I 4 .  ? 22.45750 5.67538   27.73613 1.000 33.01135  ? 243 HOH A O   1 
HETATM 1062 O  O   . HOH I 4 .  ? 11.64944 13.30948  26.58602 1.000 50.51966  ? 244 HOH A O   1 
HETATM 1063 O  O   . HOH I 4 .  ? 24.41828 3.86481   28.80447 1.000 51.31290  ? 245 HOH A O   1 
HETATM 1064 O  O   . HOH J 4 .  ? 5.84725  14.65945  9.97368  1.000 62.20580  ? 201 HOH B O   1 
HETATM 1065 O  O   . HOH J 4 .  ? 15.81600 1.73369   7.59174  1.000 56.89422  ? 202 HOH B O   1 
HETATM 1066 O  O   . HOH J 4 .  ? 9.85208  3.48262   5.34193  1.000 64.75610  ? 203 HOH B O   1 
HETATM 1067 O  O   . HOH J 4 .  ? 12.90296 3.14898   28.93213 1.000 71.49570  ? 204 HOH B O   1 
HETATM 1068 O  O   . HOH J 4 .  ? 14.06510 18.25427  21.20954 1.000 46.06758  ? 205 HOH B O   1 
HETATM 1069 O  O   . HOH J 4 .  ? 20.424   20.493    21.803   1.000 56.99442  ? 206 HOH B O   1 
HETATM 1070 O  O   . HOH J 4 .  ? 23.83779 19.93954  14.09434 1.000 36.72395  ? 207 HOH B O   1 
HETATM 1071 O  O   . HOH J 4 .  ? 19.39116 10.37654  8.26341  1.000 51.87325  ? 208 HOH B O   1 
HETATM 1072 O  O   . HOH J 4 .  ? 20.69009 1.53895   16.02839 1.000 40.67291  ? 209 HOH B O   1 
HETATM 1073 O  O   . HOH J 4 .  ? 10.40692 1.69254   26.80073 1.000 35.15595  ? 210 HOH B O   1 
HETATM 1074 O  O   . HOH J 4 .  ? 16.73986 -0.04549  22.23809 1.000 26.28838  ? 211 HOH B O   1 
HETATM 1075 O  O   . HOH J 4 .  ? 6.17230  0.77943   16.89653 1.000 31.81024  ? 212 HOH B O   1 
HETATM 1076 O  O   . HOH J 4 .  ? 15.11560 -4.07199  24.48465 1.000 41.30955  ? 213 HOH B O   1 
HETATM 1077 O  O   . HOH J 4 .  ? 13.097   -3.876    21.202   1.000 63.50762  ? 214 HOH B O   1 
HETATM 1078 O  O   . HOH J 4 .  ? 10.98943 12.56105  24.33757 1.000 74.35482  ? 215 HOH B O   1 
HETATM 1079 O  O   . HOH J 4 .  ? 24.86058 7.86000   11.84852 1.000 48.46131  ? 216 HOH B O   1 
HETATM 1080 O  O   . HOH J 4 .  ? 19.74054 3.23742   13.75525 1.000 39.69844  ? 217 HOH B O   1 
HETATM 1081 O  O   . HOH J 4 .  ? 15.06354 14.18504  11.04014 1.000 29.43521  ? 218 HOH B O   1 
HETATM 1082 O  O   . HOH J 4 .  ? 4.074    5.095     28.282   1.000 46.43249  ? 219 HOH B O   1 
HETATM 1083 O  O   . HOH J 4 .  ? 7.77745  10.28433  7.91138  1.000 45.15329  ? 220 HOH B O   1 
HETATM 1084 O  O   . HOH J 4 .  ? 6.020    6.569     9.351    1.000 59.67544  ? 221 HOH B O   1 
HETATM 1085 O  O   . HOH J 4 .  ? 12.78500 7.21747   -0.45121 1.000 45.04256  ? 222 HOH B O   1 
HETATM 1086 O  O   . HOH J 4 .  ? 11.23964 14.80156  24.39902 1.000 26.28473  ? 223 HOH B O   1 
HETATM 1087 O  O   . HOH J 4 .  ? 7.80294  14.66902  27.82306 1.000 32.00322  ? 224 HOH B O   1 
HETATM 1088 O  O   . HOH J 4 .  ? 3.59795  2.78959   24.20241 1.000 37.19439  ? 225 HOH B O   1 
HETATM 1089 O  O   . HOH J 4 .  ? 6.15924  7.35804   12.72106 1.000 24.12442  ? 226 HOH B O   1 
HETATM 1090 O  O   . HOH J 4 .  ? 22.204   18.104    23.780   1.000 40.53196  ? 227 HOH B O   1 
HETATM 1091 O  O   . HOH J 4 .  ? 10.18185 10.47637  25.75898 1.000 20.70504  ? 228 HOH B O   1 
HETATM 1092 O  O   . HOH J 4 .  ? 19.05176 11.62490  23.36193 1.000 20.19274  ? 229 HOH B O   1 
HETATM 1093 O  O   . HOH J 4 .  ? 9.10592  10.91627  23.32253 1.000 18.12807  ? 230 HOH B O   1 
HETATM 1094 O  O   . HOH J 4 .  ? 17.09514 2.53307   23.71592 1.000 24.61744  ? 231 HOH B O   1 
HETATM 1095 O  O   . HOH J 4 .  ? 23.19499 6.11344   25.14767 1.000 26.65899  ? 232 HOH B O   1 
HETATM 1096 O  O   . HOH J 4 .  ? 11.356   1.809     30.763   1.000 46.35271  ? 233 HOH B O   1 
HETATM 1097 O  O   . HOH J 4 .  ? 7.54575  18.75390  19.46398 1.000 54.32562  ? 234 HOH B O   1 
HETATM 1098 O  O   . HOH J 4 .  ? 13.71863 15.25580  24.73996 1.000 21.51098  ? 235 HOH B O   1 
HETATM 1099 O  O   . HOH J 4 .  ? 9.55800  0.66146   24.24818 1.000 33.04324  ? 236 HOH B O   1 
HETATM 1100 O  O   . HOH J 4 .  ? 13.29541 9.23892   4.61862  1.000 51.38200  ? 237 HOH B O   1 
HETATM 1101 O  O   . HOH J 4 .  ? 4.34047  5.01485   10.81652 1.000 35.53684  ? 238 HOH B O   1 
HETATM 1102 O  O   . HOH J 4 .  ? 19.49252 12.19010  11.23230 1.000 33.67115  ? 239 HOH B O   1 
HETATM 1103 O  O   . HOH J 4 .  ? 26.44492 3.86333   20.21636 1.000 50.69161  ? 240 HOH B O   1 
HETATM 1104 O  O   . HOH J 4 .  ? 4.400    7.246     14.785   1.000 28.75448  ? 241 HOH B O   1 
HETATM 1105 O  O   . HOH J 4 .  ? 21.99474 8.41854   5.95714  1.000 50.13910  ? 242 HOH B O   1 
HETATM 1106 O  O   . HOH J 4 .  ? 13.09438 -3.79025  26.25703 1.000 35.54224  ? 243 HOH B O   1 
HETATM 1107 O  O   . HOH J 4 .  ? 16.419   3.080     0.899    1.000 52.34110  ? 244 HOH B O   1 
HETATM 1108 O  O   . HOH J 4 .  ? 1.27208  1.55919   15.42999 1.000 50.54323  ? 245 HOH B O   1 
HETATM 1109 O  O   . HOH J 4 .  ? 19.14270 5.12191   25.05879 1.000 25.53401  ? 246 HOH B O   1 
HETATM 1110 O  O   . HOH J 4 .  ? 12.70184 17.01878  9.62555  1.000 43.74439  ? 247 HOH B O   1 
HETATM 1111 O  O   . HOH J 4 .  ? 15.18216 17.29065  10.47790 1.000 64.82093  ? 248 HOH B O   1 
HETATM 1112 O  O   . HOH J 4 .  ? 22.55006 2.83972   10.69660 1.000 47.87994  ? 249 HOH B O   1 
HETATM 1113 O  O   . HOH J 4 .  ? 12.67432 22.70607  15.10952 1.000 47.04392  ? 250 HOH B O   1 
HETATM 1114 O  O   . HOH J 4 .  ? 32.45971 7.70719   14.98878 1.000 51.75681  ? 251 HOH B O   1 
HETATM 1115 O  O   . HOH J 4 .  ? 3.725    11.764    7.557    1.000 48.56190  ? 252 HOH B O   1 
HETATM 1116 O  O   . HOH J 4 .  ? 13.08384 9.44279   1.78761  1.000 50.86827  ? 253 HOH B O   1 
HETATM 1117 O  O   . HOH J 4 .  ? 19.28664 2.49551   25.36023 1.000 30.45212  ? 254 HOH B O   1 
HETATM 1118 O  O   . HOH J 4 .  ? 20.75841 0.41481   24.22184 1.000 47.26421  ? 255 HOH B O   1 
HETATM 1119 O  O   . HOH K 4 .  ? 16.37993 -0.30722  8.24354  1.000 62.26159  ? 101 HOH P O   1 
HETATM 1120 O  O   . HOH K 4 .  ? -6.76649 -13.78592 7.33613  1.000 48.97431  ? 102 HOH P O   1 
HETATM 1121 O  O   . HOH K 4 .  ? -7.04291 -2.71824  5.72017  1.000 43.48523  ? 103 HOH P O   1 
HETATM 1122 O  O   . HOH K 4 .  ? 9.04498  -3.78264  18.52049 1.000 50.92384  ? 104 HOH P O   1 
HETATM 1123 O  O   . HOH K 4 .  ? 3.13599  -0.06323  16.27089 1.000 55.75680  ? 105 HOH P O   1 
HETATM 1124 O  O   . HOH K 4 .  ? 4.731    -0.494    7.387    1.000 64.29643  ? 106 HOH P O   1 
HETATM 1125 O  O   . HOH K 4 .  ? 8.80321  -4.21314  14.13040 1.000 43.69153  ? 107 HOH P O   1 
HETATM 1126 O  O   . HOH K 4 .  ? 16.20642 -3.10213  20.82326 1.000 56.71319  ? 108 HOH P O   1 
HETATM 1127 O  O   . HOH K 4 .  ? -6.82276 -11.37452 5.68875  1.000 40.55881  ? 109 HOH P O   1 
HETATM 1128 O  O   . HOH K 4 .  ? 10.70900 -1.79211  10.28645 1.000 52.15613  ? 110 HOH P O   1 
HETATM 1129 O  O   . HOH K 4 .  ? -4.31064 -9.33262  9.39468  1.000 50.97167  ? 111 HOH P O   1 
HETATM 1130 O  O   . HOH K 4 .  ? -4.31271 -6.34901  10.21386 1.000 58.94436  ? 112 HOH P O   1 
HETATM 1131 O  O   . HOH K 4 .  ? 8.06678  -2.57603  9.89183  1.000 57.89421  ? 113 HOH P O   1 
HETATM 1132 O  O   . HOH L 4 .  ? 38.729   31.767    45.709   1.000 44.60921  ? 101 HOH T O   1 
HETATM 1133 O  O   . HOH L 4 .  ? 25.74403 26.61673  38.78933 1.000 52.46336  ? 102 HOH T O   1 
HETATM 1134 O  O   . HOH L 4 .  ? 27.81837 22.07074  46.55744 1.000 43.62426  ? 103 HOH T O   1 
HETATM 1135 O  O   . HOH L 4 .  ? 24.93421 21.34174  36.67969 1.000 57.55538  ? 104 HOH T O   1 
HETATM 1136 O  O   . HOH L 4 .  ? 28.72997 15.98488  34.33633 1.000 45.74892  ? 105 HOH T O   1 
HETATM 1137 O  O   . HOH L 4 .  ? 26.59385 14.09136  42.45322 1.000 41.93841  ? 106 HOH T O   1 
HETATM 1138 O  O   . HOH L 4 .  ? 31.43853 29.17169  42.95776 1.000 53.82038  ? 107 HOH T O   1 
HETATM 1139 O  O   . HOH L 4 .  ? 26.97728 24.54236  46.28753 1.000 48.41383  ? 108 HOH T O   1 
HETATM 1140 O  O   . HOH L 4 .  ? 36.255   31.756    47.378   1.000 44.15804  ? 109 HOH T O   1 
HETATM 1141 O  O   . HOH L 4 .  ? 27.53719 16.75301  43.04959 1.000 61.07738  ? 110 HOH T 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   . GLY A 1  ? 0.32877 0.43559 0.34961 -0.01065 0.05520  0.05505  1   GLY A N   
2    C  CA  . GLY A 1  ? 0.32445 0.43453 0.35033 -0.00219 0.06397  0.05787  1   GLY A CA  
3    C  C   . GLY A 1  ? 0.32709 0.43528 0.34348 0.01084  0.07227  0.06127  1   GLY A C   
4    O  O   . GLY A 1  ? 0.30736 0.43050 0.33446 0.00373  0.05588  0.06472  1   GLY A O   
5    N  N   . PRO A 2  ? 0.33473 0.44596 0.35494 0.00604  0.11066  0.08590  2   PRO A N   
6    C  CA  . PRO A 2  ? 0.35287 0.46193 0.36275 -0.00387 0.12428  0.08705  2   PRO A CA  
7    C  C   . PRO A 2  ? 0.36738 0.47373 0.37910 0.00671  0.10804  0.06222  2   PRO A C   
8    O  O   . PRO A 2  ? 0.37886 0.48522 0.36782 0.00019  0.06964  0.06343  2   PRO A O   
9    C  CB  . PRO A 2  ? 0.35657 0.46599 0.35723 -0.01260 0.14192  0.08990  2   PRO A CB  
10   C  CG  . PRO A 2  ? 0.34891 0.46817 0.36423 -0.00947 0.13216  0.09073  2   PRO A CG  
11   C  CD  . PRO A 2  ? 0.33647 0.45188 0.35465 -0.00038 0.12763  0.10436  2   PRO A CD  
12   N  N   . LEU A 3  ? 0.37099 0.44625 0.36420 0.01324  0.13977  0.07206  3   LEU A N   
13   C  CA  . LEU A 3  ? 0.37948 0.43656 0.37692 -0.00514 0.14250  0.05380  3   LEU A CA  
14   C  C   . LEU A 3  ? 0.34487 0.43198 0.34006 -0.01506 0.11110  0.03848  3   LEU A C   
15   O  O   . LEU A 3  ? 0.39090 0.43648 0.34139 -0.01844 0.09627  0.03394  3   LEU A O   
16   C  CB  . LEU A 3  ? 0.42307 0.42305 0.39864 -0.00256 0.17074  0.05477  3   LEU A CB  
17   C  CG  . LEU A 3  ? 0.44760 0.42062 0.41614 -0.01470 0.18426  0.05816  3   LEU A CG  
18   C  CD1 . LEU A 3  ? 0.46205 0.41729 0.42024 -0.01721 0.18530  0.07695  3   LEU A CD1 
19   C  CD2 . LEU A 3  ? 0.45452 0.42463 0.42097 -0.02430 0.18766  0.04605  3   LEU A CD2 
20   N  N   . ASP A 4  ? 0.25515 0.42474 0.29622 -0.02088 0.08031  0.03658  4   ASP A N   
21   C  CA  . ASP A 4  ? 0.21712 0.41624 0.25563 -0.01456 0.03935  0.03878  4   ASP A CA  
22   C  C   . ASP A 4  ? 0.20142 0.41388 0.24582 -0.00325 -0.00291 0.05519  4   ASP A C   
23   O  O   . ASP A 4  ? 0.19188 0.41842 0.29784 -0.02558 -0.00930 0.10759  4   ASP A O   
24   C  CB  . ASP A 4  ? 0.23407 0.42327 0.25246 0.01990  0.02986  0.01052  4   ASP A CB  
25   C  CG  . ASP A 4  ? 0.25614 0.42472 0.25529 0.01654  -0.00205 -0.01437 4   ASP A CG  
26   O  OD1 . ASP A 4  ? 0.28490 0.41931 0.24913 0.02334  -0.04326 -0.02507 4   ASP A OD1 
27   O  OD2 . ASP A 4  ? 0.25911 0.42657 0.27714 0.00535  0.03088  -0.02227 4   ASP A OD2 
28   N  N   . VAL A 5  ? 0.20834 0.36695 0.16396 0.01679  0.00194  -0.02710 5   VAL A N   
29   C  CA  . VAL A 5  ? 0.20210 0.31546 0.15284 0.03479  -0.01407 -0.02732 5   VAL A CA  
30   C  C   . VAL A 5  ? 0.20976 0.28818 0.13611 0.02094  -0.00573 -0.02925 5   VAL A C   
31   O  O   . VAL A 5  ? 0.25455 0.27211 0.13480 0.04061  0.00678  -0.00991 5   VAL A O   
32   C  CB  . VAL A 5  ? 0.21130 0.33113 0.14827 0.05209  -0.01950 -0.03848 5   VAL A CB  
33   C  CG1 . VAL A 5  ? 0.21784 0.32423 0.18122 0.04988  -0.04572 -0.02297 5   VAL A CG1 
34   C  CG2 . VAL A 5  ? 0.25305 0.35422 0.13848 0.06675  -0.01035 -0.03874 5   VAL A CG2 
35   N  N   . ILE A 6  ? 0.19422 0.26046 0.15181 0.02309  0.01348  -0.01112 6   ILE A N   
36   C  CA  . ILE A 6  ? 0.17848 0.23556 0.16033 0.02200  -0.00177 -0.00906 6   ILE A CA  
37   C  C   . ILE A 6  ? 0.18360 0.22209 0.14413 0.02627  0.00309  0.00096  6   ILE A C   
38   O  O   . ILE A 6  ? 0.21936 0.24696 0.16047 0.02392  -0.01965 0.01856  6   ILE A O   
39   C  CB  . ILE A 6  ? 0.18221 0.24157 0.18955 0.01066  -0.01293 -0.00777 6   ILE A CB  
40   C  CG1 . ILE A 6  ? 0.17653 0.23673 0.20199 0.00108  -0.01627 -0.01635 6   ILE A CG1 
41   C  CG2 . ILE A 6  ? 0.20574 0.22854 0.20002 0.01356  0.00206  -0.00976 6   ILE A CG2 
42   C  CD1 . ILE A 6  ? 0.17318 0.25452 0.21783 -0.01163 -0.02255 -0.01443 6   ILE A CD1 
43   N  N   . ARG A 7  ? 0.17002 0.19410 0.15058 -0.00584 0.01494  -0.01506 7   ARG A N   
44   C  CA  . ARG A 7  ? 0.17882 0.17645 0.16312 -0.00747 0.00679  -0.01447 7   ARG A CA  
45   C  C   . ARG A 7  ? 0.22380 0.17911 0.16258 0.00054  -0.00455 -0.02761 7   ARG A C   
46   O  O   . ARG A 7  ? 0.26607 0.17117 0.16311 -0.00179 0.02209  -0.01897 7   ARG A O   
47   C  CB  . ARG A 7  ? 0.20543 0.16169 0.17387 -0.00593 -0.01304 -0.01474 7   ARG A CB  
48   C  CG  . ARG A 7  ? 0.22061 0.16275 0.16700 -0.01200 -0.02354 -0.01579 7   ARG A CG  
49   C  CD  . ARG A 7  ? 0.23853 0.17269 0.17486 -0.00848 -0.01681 0.00670  7   ARG A CD  
50   N  NE  . ARG A 7  ? 0.24780 0.18019 0.15218 -0.03010 0.00062  0.01536  7   ARG A NE  
51   C  CZ  . ARG A 7  ? 0.25369 0.14968 0.16493 -0.01236 0.02522  0.01180  7   ARG A CZ  
52   N  NH1 . ARG A 7  ? 0.26271 0.15384 0.19478 -0.00913 0.02146  -0.00116 7   ARG A NH1 
53   N  NH2 . ARG A 7  ? 0.28151 0.15225 0.19457 -0.01239 0.02928  0.00215  7   ARG A NH2 
54   N  N   . CYS A 8  ? 0.23246 0.17798 0.18614 0.00021  0.01222  -0.02696 8   CYS A N   
55   C  CA  . CYS A 8  ? 0.23822 0.16916 0.20560 0.00854  0.02193  -0.03412 8   CYS A CA  
56   C  C   . CYS A 8  ? 0.23448 0.18947 0.23730 -0.02483 0.02423  -0.03512 8   CYS A C   
57   O  O   . CYS A 8  ? 0.25201 0.20451 0.25817 -0.02181 0.00320  -0.03196 8   CYS A O   
58   C  CB  . CYS A 8  ? 0.22031 0.16685 0.18354 -0.01144 0.03403  -0.02706 8   CYS A CB  
59   S  SG  . CYS A 8  ? 0.20728 0.17765 0.19427 -0.00566 0.02134  -0.04387 8   CYS A SG  
60   N  N   . ILE A 9  ? 0.22486 0.20432 0.24368 -0.02812 0.03526  -0.06152 9   ILE A N   
61   C  CA  . ILE A 9  ? 0.24321 0.22223 0.26620 -0.01467 0.03692  -0.06030 9   ILE A CA  
62   C  C   . ILE A 9  ? 0.23455 0.21660 0.28954 -0.01142 0.02426  -0.06061 9   ILE A C   
63   O  O   . ILE A 9  ? 0.22784 0.25496 0.32708 -0.00769 0.01118  -0.05686 9   ILE A O   
64   C  CB  . ILE A 9  ? 0.27166 0.24572 0.24834 -0.02807 0.04927  -0.06461 9   ILE A CB  
65   C  CG1 . ILE A 9  ? 0.24979 0.24092 0.26297 -0.02089 0.09144  -0.07173 9   ILE A CG1 
66   C  CG2 . ILE A 9  ? 0.26823 0.25861 0.26545 -0.03506 0.04766  -0.07441 9   ILE A CG2 
67   C  CD1 . ILE A 9  ? 0.24965 0.25126 0.27185 -0.02315 0.09847  -0.06791 9   ILE A CD1 
68   N  N   . CYS A 10 ? 0.25793 0.19174 0.28905 -0.00972 0.02403  -0.05439 10  CYS A N   
69   C  CA  . CYS A 10 ? 0.25507 0.19669 0.29805 0.01006  -0.02243 -0.04354 10  CYS A CA  
70   C  C   . CYS A 10 ? 0.26922 0.20918 0.30266 0.02207  -0.04896 -0.03863 10  CYS A C   
71   O  O   . CYS A 10 ? 0.30152 0.21737 0.35362 0.02853  -0.04541 -0.02010 10  CYS A O   
72   C  CB  . CYS A 10 ? 0.23233 0.19391 0.30388 0.01304  -0.02763 -0.03867 10  CYS A CB  
73   S  SG  . CYS A 10 ? 0.25065 0.17776 0.25431 0.00307  -0.00700 -0.02889 10  CYS A SG  
74   N  N   . GLY A 11 ? 0.24905 0.20040 0.25412 0.00079  -0.02998 -0.03428 11  GLY A N   
75   C  CA  . GLY A 11 ? 0.26654 0.18525 0.26805 -0.02812 -0.04721 -0.00885 11  GLY A CA  
76   C  C   . GLY A 11 ? 0.26120 0.20368 0.25180 -0.01664 -0.05706 -0.01559 11  GLY A C   
77   O  O   . GLY A 11 ? 0.28112 0.22537 0.25898 -0.02588 -0.05520 -0.02552 11  GLY A O   
78   N  N   . LEU A 12 ? 0.24053 0.18055 0.25724 -0.00219 -0.04345 -0.02618 12  LEU A N   
79   C  CA  . LEU A 12 ? 0.26327 0.18132 0.25192 0.00274  -0.03474 -0.02539 12  LEU A CA  
80   C  C   . LEU A 12 ? 0.25941 0.18065 0.24569 -0.00346 -0.03366 0.01368  12  LEU A C   
81   O  O   . LEU A 12 ? 0.25224 0.19319 0.23924 -0.01033 -0.02282 0.01480  12  LEU A O   
82   C  CB  . LEU A 12 ? 0.31426 0.19004 0.28765 0.01119  -0.04658 -0.04632 12  LEU A CB  
83   C  CG  . LEU A 12 ? 0.34419 0.19439 0.27644 0.03178  -0.05873 -0.04429 12  LEU A CG  
84   C  CD1 . LEU A 12 ? 0.35856 0.19444 0.28849 0.02577  -0.08302 -0.05982 12  LEU A CD1 
85   C  CD2 . LEU A 12 ? 0.35947 0.19863 0.26844 0.04708  -0.05635 -0.01981 12  LEU A CD2 
86   N  N   . TYR A 13 ? 0.25525 0.20599 0.23931 -0.00676 -0.01353 -0.00609 13  TYR A N   
87   C  CA  . TYR A 13 ? 0.26546 0.23863 0.20632 -0.02868 -0.00511 -0.03030 13  TYR A CA  
88   C  C   . TYR A 13 ? 0.27077 0.24337 0.21585 -0.04132 -0.01736 -0.00444 13  TYR A C   
89   O  O   . TYR A 13 ? 0.28489 0.24100 0.21349 -0.05258 0.01582  -0.00394 13  TYR A O   
90   C  CB  . TYR A 13 ? 0.25547 0.26611 0.19183 -0.00078 -0.02346 -0.00798 13  TYR A CB  
91   C  CG  . TYR A 13 ? 0.23472 0.25619 0.19941 -0.02643 -0.01870 -0.00448 13  TYR A CG  
92   C  CD1 . TYR A 13 ? 0.22495 0.26417 0.20748 -0.03756 0.01145  -0.00346 13  TYR A CD1 
93   C  CD2 . TYR A 13 ? 0.24294 0.25551 0.17201 -0.00863 -0.01701 -0.00047 13  TYR A CD2 
94   C  CE1 . TYR A 13 ? 0.21407 0.26813 0.21427 -0.02163 0.02080  -0.01283 13  TYR A CE1 
95   C  CE2 . TYR A 13 ? 0.23432 0.27746 0.17015 -0.00060 -0.01148 -0.02394 13  TYR A CE2 
96   C  CZ  . TYR A 13 ? 0.22952 0.27676 0.20991 0.00256  0.03970  -0.02542 13  TYR A CZ  
97   O  OH  . TYR A 13 ? 0.26409 0.28245 0.24800 0.04686  0.03665  0.01626  13  TYR A OH  
98   N  N   . LYS A 14 ? 0.28315 0.25003 0.24187 -0.04902 -0.03398 0.02006  14  LYS A N   
99   C  CA  . LYS A 14 ? 0.28914 0.27258 0.26184 -0.05939 -0.03388 0.01943  14  LYS A CA  
100  C  C   . LYS A 14 ? 0.26100 0.28360 0.19177 -0.08221 0.02418  0.00462  14  LYS A C   
101  O  O   . LYS A 14 ? 0.28056 0.28813 0.22846 -0.07452 0.03963  0.01378  14  LYS A O   
102  C  CB  . LYS A 14 ? 0.33066 0.30245 0.31560 -0.02120 -0.03999 0.01964  14  LYS A CB  
103  C  CG  . LYS A 14 ? 0.35499 0.30461 0.37075 -0.00226 -0.02650 0.03575  14  LYS A CG  
104  C  CD  . LYS A 14 ? 0.38256 0.30711 0.39597 0.01730  -0.03063 0.06183  14  LYS A CD  
105  C  CE  . LYS A 14 ? 0.38555 0.31267 0.38874 0.03374  -0.03687 0.05342  14  LYS A CE  
106  N  NZ  . LYS A 14 ? 0.39044 0.31401 0.38985 0.03741  -0.03388 0.03695  14  LYS A NZ  
107  N  N   . ASP A 15 ? 0.22439 0.31368 0.19452 -0.08467 0.01146  -0.02149 15  ASP A N   
108  C  CA  . ASP A 15 ? 0.26129 0.34609 0.25000 -0.07379 -0.00505 -0.02755 15  ASP A CA  
109  C  C   . ASP A 15 ? 0.31187 0.34464 0.25444 -0.06683 -0.02134 -0.02203 15  ASP A C   
110  O  O   . ASP A 15 ? 0.34564 0.34519 0.24794 -0.06342 -0.00819 -0.00946 15  ASP A O   
111  C  CB  . ASP A 15 ? 0.25295 0.38498 0.28358 -0.06675 0.01261  -0.03228 15  ASP A CB  
112  C  CG  . ASP A 15 ? 0.23102 0.42016 0.32027 -0.06069 -0.00455 -0.03751 15  ASP A CG  
113  O  OD1 . ASP A 15 ? 0.21737 0.43268 0.31274 -0.05016 -0.01207 -0.04481 15  ASP A OD1 
114  O  OD2 . ASP A 15 ? 0.23946 0.43081 0.35087 -0.06058 -0.00182 -0.03445 15  ASP A OD2 
115  N  N   . GLU A 16 ? 0.31518 0.33013 0.26689 -0.03926 -0.03839 -0.04138 16  GLU A N   
116  C  CA  . GLU A 16 ? 0.35425 0.33887 0.29462 -0.01304 -0.04906 -0.04337 16  GLU A CA  
117  C  C   . GLU A 16 ? 0.33843 0.32698 0.28583 -0.02679 -0.05394 -0.06215 16  GLU A C   
118  O  O   . GLU A 16 ? 0.32095 0.32948 0.31843 -0.05406 -0.04622 -0.08210 16  GLU A O   
119  C  CB  . GLU A 16 ? 0.39002 0.35165 0.33868 0.00278  -0.05916 -0.05058 16  GLU A CB  
120  C  CG  . GLU A 16 ? 0.41767 0.36446 0.37869 0.00425  -0.05671 -0.05372 16  GLU A CG  
121  C  CD  . GLU A 16 ? 0.44368 0.37343 0.40161 -0.00346 -0.07269 -0.05419 16  GLU A CD  
122  O  OE1 . GLU A 16 ? 0.45077 0.37540 0.41515 -0.01583 -0.06821 -0.06461 16  GLU A OE1 
123  O  OE2 . GLU A 16 ? 0.45366 0.37166 0.40688 0.00142  -0.08759 -0.04590 16  GLU A OE2 
124  N  N   . GLY A 17 ? 0.32329 0.31668 0.25553 -0.02512 -0.06375 -0.06709 17  GLY A N   
125  C  CA  . GLY A 17 ? 0.30897 0.30494 0.23856 -0.03582 -0.04752 -0.05894 17  GLY A CA  
126  C  C   . GLY A 17 ? 0.28914 0.29117 0.22080 -0.02265 -0.05597 -0.05200 17  GLY A C   
127  O  O   . GLY A 17 ? 0.27514 0.28468 0.21155 -0.02695 -0.03808 -0.06482 17  GLY A O   
128  N  N   . LEU A 18 ? 0.29683 0.28722 0.19567 -0.01901 -0.06943 -0.04012 18  LEU A N   
129  C  CA  . LEU A 18 ? 0.31828 0.28610 0.18679 0.02840  -0.06372 -0.03851 18  LEU A CA  
130  C  C   . LEU A 18 ? 0.32099 0.28530 0.17696 0.03679  -0.03473 -0.04775 18  LEU A C   
131  O  O   . LEU A 18 ? 0.30592 0.27781 0.16981 0.04050  -0.01666 -0.04511 18  LEU A O   
132  C  CB  . LEU A 18 ? 0.35119 0.29757 0.21799 0.03126  -0.04118 -0.03473 18  LEU A CB  
133  C  CG  . LEU A 18 ? 0.35656 0.29865 0.23081 0.02332  -0.00565 -0.01335 18  LEU A CG  
134  C  CD1 . LEU A 18 ? 0.35204 0.29730 0.26902 0.02230  -0.01156 -0.03134 18  LEU A CD1 
135  C  CD2 . LEU A 18 ? 0.36713 0.31371 0.19240 0.01972  0.01349  0.01870  18  LEU A CD2 
136  N  N   . MET A 19 ? 0.31833 0.29564 0.12246 0.04062  -0.03998 -0.05471 19  MET A N   
137  C  CA  . MET A 19 ? 0.30037 0.27997 0.13237 0.03926  -0.02191 -0.02639 19  MET A CA  
138  C  C   . MET A 19 ? 0.29288 0.26718 0.12338 0.06822  -0.02486 -0.00713 19  MET A C   
139  O  O   . MET A 19 ? 0.27479 0.30103 0.14543 0.08143  -0.04895 -0.00916 19  MET A O   
140  C  CB  . MET A 19 ? 0.28609 0.29167 0.14979 0.03402  -0.00394 -0.00877 19  MET A CB  
141  C  CG  . MET A 19 ? 0.26679 0.29154 0.17418 0.03569  -0.00219 -0.00092 19  MET A CG  
142  S  SD  . MET A 19 ? 0.22844 0.28804 0.16168 0.01860  -0.00880 -0.00215 19  MET A SD  
143  C  CE  . MET A 19 ? 0.25192 0.28814 0.18108 0.01800  -0.01249 -0.04640 19  MET A CE  
144  N  N   . ILE A 20 ? 0.31997 0.22979 0.12833 0.05595  -0.00194 -0.01533 20  ILE A N   
145  C  CA  . ILE A 20 ? 0.36800 0.22852 0.10224 0.05094  0.00561  -0.00617 20  ILE A CA  
146  C  C   . ILE A 20 ? 0.36740 0.23242 0.11230 0.07625  -0.00378 -0.01470 20  ILE A C   
147  O  O   . ILE A 20 ? 0.32901 0.20654 0.10540 0.07687  0.00297  0.00121  20  ILE A O   
148  C  CB  . ILE A 20 ? 0.41374 0.24551 0.14312 0.03805  -0.00553 0.01258  20  ILE A CB  
149  C  CG1 . ILE A 20 ? 0.46171 0.24957 0.12239 0.02490  0.00629  0.02603  20  ILE A CG1 
150  C  CG2 . ILE A 20 ? 0.40296 0.23756 0.16352 0.02686  -0.00689 -0.02708 20  ILE A CG2 
151  C  CD1 . ILE A 20 ? 0.45609 0.25110 0.11943 0.01716  0.02309  0.02143  20  ILE A CD1 
152  N  N   . GLN A 21 ? 0.40419 0.27538 0.14549 0.11422  -0.01937 -0.04212 21  GLN A N   
153  C  CA  . GLN A 21 ? 0.43454 0.27457 0.14542 0.13390  -0.01448 -0.02314 21  GLN A CA  
154  C  C   . GLN A 21 ? 0.48380 0.24882 0.13627 0.10243  -0.00858 0.00657  21  GLN A C   
155  O  O   . GLN A 21 ? 0.50425 0.25653 0.16248 0.09395  0.00170  0.01480  21  GLN A O   
156  C  CB  . GLN A 21 ? 0.41673 0.32437 0.13898 0.15346  -0.02966 -0.03088 21  GLN A CB  
157  C  CG  . GLN A 21 ? 0.40114 0.34885 0.15278 0.15067  -0.01881 -0.05352 21  GLN A CG  
158  C  CD  . GLN A 21 ? 0.37037 0.37969 0.19387 0.16771  -0.02846 -0.02369 21  GLN A CD  
159  O  OE1 . GLN A 21 ? 0.33707 0.39035 0.19815 0.18744  -0.05804 -0.01235 21  GLN A OE1 
160  N  NE2 . GLN A 21 ? 0.36315 0.37434 0.17670 0.16516  -0.03550 -0.03946 21  GLN A NE2 
161  N  N   . CYS A 22 ? 0.51863 0.22831 0.14712 0.08436  -0.00921 0.00763  22  CYS A N   
162  C  CA  . CYS A 22 ? 0.54105 0.21237 0.16330 0.08651  -0.02232 0.02876  22  CYS A CA  
163  C  C   . CYS A 22 ? 0.54035 0.23758 0.16455 0.11355  -0.02385 0.02651  22  CYS A C   
164  O  O   . CYS A 22 ? 0.55911 0.24457 0.16703 0.12136  -0.03329 0.01843  22  CYS A O   
165  C  CB  . CYS A 22 ? 0.56462 0.17694 0.18966 0.07351  -0.03817 0.02105  22  CYS A CB  
166  S  SG  . CYS A 22 ? 0.60524 0.17890 0.17772 0.06191  -0.00365 -0.00408 22  CYS A SG  
167  N  N   . ASP A 23 ? 0.58660 0.24713 0.19556 0.12492  -0.05068 0.02621  23  ASP A N   
168  C  CA  . ASP A 23 ? 0.60232 0.26206 0.19550 0.14132  -0.06664 0.01052  23  ASP A CA  
169  C  C   . ASP A 23 ? 0.61020 0.26471 0.19264 0.14801  -0.06259 -0.00953 23  ASP A C   
170  O  O   . ASP A 23 ? 0.62405 0.27844 0.22795 0.15931  -0.08831 -0.03296 23  ASP A O   
171  C  CB  . ASP A 23 ? 0.61765 0.27495 0.19362 0.13557  -0.07205 0.00816  23  ASP A CB  
172  C  CG  . ASP A 23 ? 0.62626 0.26801 0.20805 0.14148  -0.09039 0.00172  23  ASP A CG  
173  O  OD1 . ASP A 23 ? 0.62373 0.26746 0.22138 0.14622  -0.09491 0.00564  23  ASP A OD1 
174  O  OD2 . ASP A 23 ? 0.64490 0.25670 0.22212 0.15819  -0.06620 -0.01859 23  ASP A OD2 
175  N  N   . LYS A 24 ? 0.59905 0.23796 0.18457 0.13228  -0.03964 -0.00313 24  LYS A N   
176  C  CA  . LYS A 24 ? 0.58778 0.24291 0.19268 0.11434  -0.02113 -0.01693 24  LYS A CA  
177  C  C   . LYS A 24 ? 0.58798 0.23486 0.19290 0.12860  -0.02437 0.01025  24  LYS A C   
178  O  O   . LYS A 24 ? 0.60752 0.23721 0.19578 0.13934  0.00995  0.03259  24  LYS A O   
179  C  CB  . LYS A 24 ? 0.57579 0.25516 0.22955 0.10350  -0.03999 0.01451  24  LYS A CB  
180  C  CG  . LYS A 24 ? 0.56221 0.23715 0.26696 0.10497  -0.06146 0.00697  24  LYS A CG  
181  C  CD  . LYS A 24 ? 0.54912 0.23100 0.30291 0.09622  -0.08503 -0.00547 24  LYS A CD  
182  C  CE  . LYS A 24 ? 0.54340 0.23478 0.33716 0.07815  -0.09158 -0.03116 24  LYS A CE  
183  N  NZ  . LYS A 24 ? 0.53732 0.23142 0.35323 0.08253  -0.09493 -0.04510 24  LYS A NZ  
184  N  N   . CYS A 25 ? 0.56734 0.23387 0.18535 0.12088  -0.03315 0.00063  25  CYS A N   
185  C  CA  . CYS A 25 ? 0.53628 0.23325 0.17563 0.12604  -0.03390 -0.01417 25  CYS A CA  
186  C  C   . CYS A 25 ? 0.51655 0.23725 0.16194 0.13136  0.00571  -0.02167 25  CYS A C   
187  O  O   . CYS A 25 ? 0.52740 0.25539 0.16998 0.13349  -0.00537 -0.00973 25  CYS A O   
188  C  CB  . CYS A 25 ? 0.53204 0.20152 0.15112 0.12942  -0.02984 -0.01607 25  CYS A CB  
189  S  SG  . CYS A 25 ? 0.53133 0.18989 0.16863 0.09647  -0.00411 -0.01522 25  CYS A SG  
190  N  N   . MET A 26 ? 0.48608 0.22293 0.18365 0.13426  -0.01183 -0.02805 26  MET A N   
191  C  CA  . MET A 26 ? 0.44016 0.24348 0.17409 0.14430  -0.01665 -0.03364 26  MET A CA  
192  C  C   . MET A 26 ? 0.38104 0.23848 0.16660 0.11416  -0.02747 -0.01557 26  MET A C   
193  O  O   . MET A 26 ? 0.37051 0.26246 0.15478 0.11790  -0.03126 -0.02280 26  MET A O   
194  C  CB  . MET A 26 ? 0.46623 0.25560 0.20874 0.17665  -0.03157 -0.04081 26  MET A CB  
195  C  CG  . MET A 26 ? 0.48802 0.28596 0.25853 0.19195  -0.02677 -0.00334 26  MET A CG  
196  S  SD  . MET A 26 ? 0.50926 0.32335 0.30003 0.19682  -0.02958 0.02714  26  MET A SD  
197  C  CE  . MET A 26 ? 0.51957 0.32381 0.30264 0.17736  -0.05047 0.02413  26  MET A CE  
198  N  N   . VAL A 27 ? 0.35298 0.22102 0.16273 0.08989  -0.02838 -0.02276 27  VAL A N   
199  C  CA  . VAL A 27 ? 0.32882 0.20137 0.16429 0.07399  -0.00864 -0.02536 27  VAL A CA  
200  C  C   . VAL A 27 ? 0.31655 0.20691 0.14849 0.06150  -0.01758 -0.01469 27  VAL A C   
201  O  O   . VAL A 27 ? 0.36070 0.21712 0.16183 0.05317  -0.01669 -0.00270 27  VAL A O   
202  C  CB  . VAL A 27 ? 0.32112 0.20727 0.16499 0.05787  0.00207  -0.00590 27  VAL A CB  
203  C  CG1 . VAL A 27 ? 0.34646 0.21314 0.16830 0.02859  0.03032  -0.02633 27  VAL A CG1 
204  C  CG2 . VAL A 27 ? 0.33391 0.19542 0.19944 0.02616  0.01691  0.00532  27  VAL A CG2 
205  N  N   . TRP A 28 ? 0.27513 0.20408 0.14297 0.03522  -0.00189 -0.00410 28  TRP A N   
206  C  CA  . TRP A 28 ? 0.24152 0.20944 0.15958 0.04496  0.00891  -0.01715 28  TRP A CA  
207  C  C   . TRP A 28 ? 0.22323 0.20346 0.13616 0.03517  -0.00436 -0.02921 28  TRP A C   
208  O  O   . TRP A 28 ? 0.21614 0.21512 0.14292 0.01759  0.00159  -0.02610 28  TRP A O   
209  C  CB  . TRP A 28 ? 0.24253 0.26708 0.19198 0.05046  0.00751  -0.01843 28  TRP A CB  
210  C  CG  . TRP A 28 ? 0.25505 0.30280 0.16947 0.07896  -0.00957 -0.02332 28  TRP A CG  
211  C  CD1 . TRP A 28 ? 0.25262 0.32849 0.17387 0.07281  -0.01487 -0.03152 28  TRP A CD1 
212  C  CD2 . TRP A 28 ? 0.27222 0.34725 0.16390 0.08635  -0.02540 -0.02087 28  TRP A CD2 
213  N  NE1 . TRP A 28 ? 0.25531 0.34580 0.16893 0.08999  -0.03547 -0.01504 28  TRP A NE1 
214  C  CE2 . TRP A 28 ? 0.26415 0.35022 0.16609 0.09495  -0.03248 -0.00581 28  TRP A CE2 
215  C  CE3 . TRP A 28 ? 0.28942 0.36055 0.17993 0.06850  -0.04977 -0.01255 28  TRP A CE3 
216  C  CZ2 . TRP A 28 ? 0.26423 0.37009 0.18329 0.09440  -0.06708 -0.02693 28  TRP A CZ2 
217  C  CZ3 . TRP A 28 ? 0.29726 0.37458 0.20148 0.08302  -0.05531 -0.02654 28  TRP A CZ3 
218  C  CH2 . TRP A 28 ? 0.28162 0.37000 0.19082 0.09885  -0.06851 -0.03052 28  TRP A CH2 
219  N  N   . GLN A 29 ? 0.24009 0.18956 0.14565 0.03418  0.01090  -0.02670 29  GLN A N   
220  C  CA  . GLN A 29 ? 0.23709 0.19690 0.16135 0.01624  0.01725  -0.02736 29  GLN A CA  
221  C  C   . GLN A 29 ? 0.23319 0.20124 0.14507 0.02487  0.00639  -0.02998 29  GLN A C   
222  O  O   . GLN A 29 ? 0.24421 0.21943 0.16492 0.04176  0.01068  -0.02797 29  GLN A O   
223  C  CB  . GLN A 29 ? 0.26009 0.19434 0.17436 -0.01421 0.03267  -0.03089 29  GLN A CB  
224  C  CG  . GLN A 29 ? 0.29064 0.19286 0.16189 -0.01095 0.04021  -0.02721 29  GLN A CG  
225  C  CD  . GLN A 29 ? 0.32237 0.14414 0.13771 0.00783  0.05098  -0.01129 29  GLN A CD  
226  O  OE1 . GLN A 29 ? 0.37718 0.18101 0.15951 0.00591  0.04714  0.00185  29  GLN A OE1 
227  N  NE2 . GLN A 29 ? 0.32737 0.16216 0.17759 0.02707  0.01861  -0.00993 29  GLN A NE2 
228  N  N   . HIS A 30 ? 0.24746 0.19561 0.16079 0.01613  0.01322  -0.03355 30  HIS A N   
229  C  CA  . HIS A 30 ? 0.26937 0.19715 0.16917 0.00601  0.01859  -0.02395 30  HIS A CA  
230  C  C   . HIS A 30 ? 0.28910 0.19461 0.17735 -0.00515 0.02385  -0.02204 30  HIS A C   
231  O  O   . HIS A 30 ? 0.26109 0.19353 0.17171 -0.01576 0.02328  -0.04572 30  HIS A O   
232  C  CB  . HIS A 30 ? 0.25953 0.19336 0.18239 0.00524  0.00441  -0.02709 30  HIS A CB  
233  C  CG  . HIS A 30 ? 0.25151 0.19608 0.17515 -0.00248 0.00294  -0.02649 30  HIS A CG  
234  N  ND1 . HIS A 30 ? 0.23729 0.18583 0.18567 0.00589  0.00131  -0.02225 30  HIS A ND1 
235  C  CD2 . HIS A 30 ? 0.25082 0.20637 0.18765 -0.01369 -0.00062 -0.01068 30  HIS A CD2 
236  C  CE1 . HIS A 30 ? 0.24428 0.19612 0.17796 -0.00156 -0.00709 -0.01632 30  HIS A CE1 
237  N  NE2 . HIS A 30 ? 0.25180 0.21482 0.18562 -0.00871 -0.01850 0.00628  30  HIS A NE2 
238  N  N   . CYS A 31 ? 0.32944 0.20793 0.17588 0.02003  0.02372  -0.02538 31  CYS A N   
239  C  CA  . CYS A 31 ? 0.37136 0.24159 0.16707 0.04094  0.02268  -0.01914 31  CYS A CA  
240  C  C   . CYS A 31 ? 0.37690 0.23543 0.19921 0.03248  0.04134  -0.01751 31  CYS A C   
241  O  O   . CYS A 31 ? 0.39428 0.25279 0.20606 0.01758  0.07060  -0.01772 31  CYS A O   
242  C  CB  . CYS A 31 ? 0.39960 0.25754 0.17500 0.06460  -0.00162 -0.02527 31  CYS A CB  
243  S  SG  . CYS A 31 ? 0.41372 0.22784 0.16272 0.06997  -0.02299 -0.02977 31  CYS A SG  
244  N  N   . ASP A 32 ? 0.36713 0.22401 0.20661 0.02006  0.04075  -0.05573 32  ASP A N   
245  C  CA  . ASP A 32 ? 0.34957 0.21612 0.20863 0.01686  0.04169  -0.05242 32  ASP A CA  
246  C  C   . ASP A 32 ? 0.32850 0.23317 0.21844 0.00591  0.07820  -0.07049 32  ASP A C   
247  O  O   . ASP A 32 ? 0.30564 0.25798 0.22477 -0.01781 0.10622  -0.07584 32  ASP A O   
248  C  CB  . ASP A 32 ? 0.35810 0.20084 0.22709 0.00573  -0.01096 -0.04084 32  ASP A CB  
249  C  CG  . ASP A 32 ? 0.36111 0.21757 0.22473 0.02768  -0.01765 -0.05329 32  ASP A CG  
250  O  OD1 . ASP A 32 ? 0.36321 0.24515 0.20187 0.04249  -0.04375 -0.05733 32  ASP A OD1 
251  O  OD2 . ASP A 32 ? 0.36660 0.22790 0.25734 0.03158  -0.01028 -0.06107 32  ASP A OD2 
252  N  N   . CYS A 33 ? 0.31074 0.21074 0.22440 -0.00154 0.07202  -0.07792 33  CYS A N   
253  C  CA  . CYS A 33 ? 0.30050 0.21934 0.23603 -0.01928 0.06440  -0.06672 33  CYS A CA  
254  C  C   . CYS A 33 ? 0.31597 0.20786 0.25323 -0.03358 0.08369  -0.06283 33  CYS A C   
255  O  O   . CYS A 33 ? 0.29761 0.19958 0.29366 -0.03569 0.09952  -0.08877 33  CYS A O   
256  C  CB  . CYS A 33 ? 0.27749 0.21692 0.22148 -0.00570 0.04000  -0.06761 33  CYS A CB  
257  S  SG  . CYS A 33 ? 0.23501 0.18344 0.23795 0.00406  0.02006  -0.06870 33  CYS A SG  
258  N  N   . MET A 34 ? 0.35261 0.21958 0.22837 -0.04101 0.09127  -0.04905 34  MET A N   
259  C  CA  . MET A 34 ? 0.40600 0.23528 0.22616 -0.04186 0.12395  -0.04629 34  MET A CA  
260  C  C   . MET A 34 ? 0.46039 0.27519 0.23596 -0.04752 0.15019  -0.08029 34  MET A C   
261  O  O   . MET A 34 ? 0.48250 0.29552 0.23444 -0.05938 0.16726  -0.05393 34  MET A O   
262  C  CB  . MET A 34 ? 0.40108 0.21630 0.21219 -0.01837 0.10180  -0.02465 34  MET A CB  
263  C  CG  . MET A 34 ? 0.37993 0.20272 0.21022 -0.01620 0.08680  -0.01955 34  MET A CG  
264  S  SD  . MET A 34 ? 0.33754 0.18567 0.24834 -0.03142 0.09228  -0.05222 34  MET A SD  
265  C  CE  . MET A 34 ? 0.33190 0.20769 0.27468 -0.04836 0.09189  -0.03258 34  MET A CE  
266  N  N   . GLY A 35 ? 0.50651 0.31003 0.26549 -0.05607 0.16669  -0.09430 35  GLY A N   
267  C  CA  . GLY A 35 ? 0.54834 0.35024 0.26414 -0.04969 0.16376  -0.09796 35  GLY A CA  
268  C  C   . GLY A 35 ? 0.58804 0.37689 0.26685 -0.05358 0.16716  -0.06049 35  GLY A C   
269  O  O   . GLY A 35 ? 0.59811 0.38795 0.26287 -0.05653 0.19297  -0.03010 35  GLY A O   
270  N  N   . VAL A 36 ? 0.60642 0.38357 0.27024 -0.03360 0.13668  -0.07907 36  VAL A N   
271  C  CA  . VAL A 36 ? 0.61506 0.38880 0.24834 -0.03436 0.08789  -0.05257 36  VAL A CA  
272  C  C   . VAL A 36 ? 0.61670 0.40951 0.26243 -0.01736 0.01598  -0.07519 36  VAL A C   
273  O  O   . VAL A 36 ? 0.60411 0.41085 0.23230 -0.02115 0.01283  -0.06002 36  VAL A O   
274  C  CB  . VAL A 36 ? 0.61475 0.37655 0.24817 -0.05718 0.11579  -0.07298 36  VAL A CB  
275  C  CG1 . VAL A 36 ? 0.59997 0.37415 0.24862 -0.06615 0.12786  -0.11027 36  VAL A CG1 
276  C  CG2 . VAL A 36 ? 0.61358 0.37122 0.23906 -0.07270 0.11432  -0.07789 36  VAL A CG2 
277  N  N   . ASN A 37 ? 0.62266 0.43063 0.31736 0.00057  -0.01893 -0.09546 37  ASN A N   
278  C  CA  . ASN A 37 ? 0.63114 0.46164 0.34996 0.01769  -0.06607 -0.09938 37  ASN A CA  
279  C  C   . ASN A 37 ? 0.63048 0.47043 0.34457 0.01886  -0.06594 -0.06689 37  ASN A C   
280  O  O   . ASN A 37 ? 0.65084 0.46415 0.31870 0.03262  -0.07273 -0.06915 37  ASN A O   
281  C  CB  . ASN A 37 ? 0.63901 0.48061 0.38635 0.02631  -0.08391 -0.11850 37  ASN A CB  
282  C  CG  . ASN A 37 ? 0.64364 0.49911 0.40672 0.02720  -0.10273 -0.14191 37  ASN A CG  
283  O  OD1 . ASN A 37 ? 0.64175 0.50868 0.40869 0.02034  -0.11773 -0.14752 37  ASN A OD1 
284  N  ND2 . ASN A 37 ? 0.64920 0.50502 0.42409 0.03024  -0.10020 -0.14544 37  ASN A ND2 
285  N  N   . SER A 38 ? 0.61184 0.47665 0.36149 0.02264  -0.02428 -0.02623 38  SER A N   
286  C  CA  . SER A 38 ? 0.58788 0.47308 0.35407 0.01531  -0.00862 -0.00167 38  SER A CA  
287  C  C   . SER A 38 ? 0.56863 0.45727 0.35310 0.01460  0.02897  0.01707  38  SER A C   
288  O  O   . SER A 38 ? 0.55505 0.46494 0.34041 0.00631  0.04719  0.03469  38  SER A O   
289  C  CB  . SER A 38 ? 0.58439 0.47276 0.35621 0.00358  -0.03323 -0.01194 38  SER A CB  
290  O  OG  . SER A 38 ? 0.58151 0.47273 0.36179 -0.00380 -0.04447 -0.02867 38  SER A OG  
291  N  N   . ASP A 39 ? 0.56470 0.43554 0.35526 0.02485  0.04242  0.02367  39  ASP A N   
292  C  CA  . ASP A 39 ? 0.56220 0.42629 0.36436 0.03742  0.05236  0.01573  39  ASP A CA  
293  C  C   . ASP A 39 ? 0.56600 0.40694 0.33766 0.05941  0.05220  0.01629  39  ASP A C   
294  O  O   . ASP A 39 ? 0.56215 0.40345 0.36285 0.05857  0.05381  0.01863  39  ASP A O   
295  C  CB  . ASP A 39 ? 0.56365 0.42778 0.39355 0.01905  0.03128  -0.01341 39  ASP A CB  
296  C  CG  . ASP A 39 ? 0.56598 0.42220 0.41307 0.00745  0.02550  -0.01517 39  ASP A CG  
297  O  OD1 . ASP A 39 ? 0.56728 0.41950 0.42551 0.00380  0.02266  -0.01189 39  ASP A OD1 
298  O  OD2 . ASP A 39 ? 0.56821 0.42154 0.41851 -0.00186 0.01735  -0.01436 39  ASP A OD2 
299  N  N   . VAL A 40 ? 0.58167 0.39539 0.25768 0.07986  0.06530  0.03193  40  VAL A N   
300  C  CA  . VAL A 40 ? 0.61047 0.39019 0.22052 0.07060  0.01850  0.04877  40  VAL A CA  
301  C  C   . VAL A 40 ? 0.63524 0.38961 0.22476 0.07152  0.04855  0.06529  40  VAL A C   
302  O  O   . VAL A 40 ? 0.64091 0.39094 0.25914 0.05912  0.09417  0.06854  40  VAL A O   
303  C  CB  . VAL A 40 ? 0.61795 0.40428 0.21265 0.07008  -0.01378 0.04063  40  VAL A CB  
304  C  CG1 . VAL A 40 ? 0.61284 0.40966 0.23452 0.07022  -0.03234 0.03788  40  VAL A CG1 
305  C  CG2 . VAL A 40 ? 0.62504 0.39647 0.20542 0.06936  -0.00970 0.04754  40  VAL A CG2 
306  N  N   . GLU A 41 ? 0.64894 0.39328 0.20624 0.08233  0.02794  0.05830  41  GLU A N   
307  C  CA  . GLU A 41 ? 0.65733 0.37398 0.21062 0.10019  0.02938  0.04575  41  GLU A CA  
308  C  C   . GLU A 41 ? 0.67261 0.37017 0.20616 0.10474  0.01301  0.03024  41  GLU A C   
309  O  O   . GLU A 41 ? 0.67498 0.38681 0.25038 0.11100  0.01553  0.01177  41  GLU A O   
310  C  CB  . GLU A 41 ? 0.65197 0.37029 0.24190 0.10234  0.03202  0.06431  41  GLU A CB  
311  C  CG  . GLU A 41 ? 0.64634 0.35220 0.26852 0.10902  0.03672  0.06346  41  GLU A CG  
312  C  CD  . GLU A 41 ? 0.64055 0.34586 0.28717 0.11180  0.03426  0.07443  41  GLU A CD  
313  O  OE1 . GLU A 41 ? 0.64221 0.34473 0.30466 0.11441  0.03569  0.06715  41  GLU A OE1 
314  O  OE2 . GLU A 41 ? 0.63560 0.34088 0.29323 0.10624  0.03436  0.07170  41  GLU A OE2 
315  N  N   . HIS A 42 ? 0.68579 0.34544 0.18902 0.10637  -0.01016 0.03176  42  HIS A N   
316  C  CA  . HIS A 42 ? 0.68952 0.33206 0.19234 0.12734  -0.03367 0.01436  42  HIS A CA  
317  C  C   . HIS A 42 ? 0.66218 0.29892 0.17658 0.10916  -0.03280 0.00161  42  HIS A C   
318  O  O   . HIS A 42 ? 0.66628 0.31196 0.17414 0.10429  0.00751  0.00756  42  HIS A O   
319  C  CB  . HIS A 42 ? 0.70289 0.33611 0.22498 0.15240  -0.04724 0.01826  42  HIS A CB  
320  C  CG  . HIS A 42 ? 0.71994 0.33842 0.25272 0.17010  -0.04806 0.03234  42  HIS A CG  
321  N  ND1 . HIS A 42 ? 0.72734 0.34437 0.26051 0.17441  -0.04555 0.05613  42  HIS A ND1 
322  C  CD2 . HIS A 42 ? 0.73000 0.34394 0.27463 0.17457  -0.05249 0.04922  42  HIS A CD2 
323  C  CE1 . HIS A 42 ? 0.72916 0.34462 0.28482 0.17868  -0.04279 0.05684  42  HIS A CE1 
324  N  NE2 . HIS A 42 ? 0.73095 0.34951 0.29661 0.18111  -0.04603 0.05493  42  HIS A NE2 
325  N  N   . TYR A 43 ? 0.65880 0.28245 0.17937 0.09391  -0.03566 -0.00928 43  TYR A N   
326  C  CA  . TYR A 43 ? 0.63435 0.24586 0.16352 0.06656  -0.01399 -0.01297 43  TYR A CA  
327  C  C   . TYR A 43 ? 0.61784 0.22341 0.15746 0.06464  -0.00858 0.00237  43  TYR A C   
328  O  O   . TYR A 43 ? 0.63325 0.21515 0.16505 0.10369  -0.01569 -0.00370 43  TYR A O   
329  C  CB  . TYR A 43 ? 0.61220 0.23554 0.16425 0.06720  -0.02405 -0.01298 43  TYR A CB  
330  C  CG  . TYR A 43 ? 0.57936 0.21516 0.17041 0.05328  -0.00397 -0.00507 43  TYR A CG  
331  C  CD1 . TYR A 43 ? 0.55948 0.21921 0.15653 0.04278  0.00433  0.00551  43  TYR A CD1 
332  C  CD2 . TYR A 43 ? 0.55581 0.20174 0.16036 0.03507  -0.01001 0.01197  43  TYR A CD2 
333  C  CE1 . TYR A 43 ? 0.55421 0.21813 0.16196 0.02657  0.02616  0.01348  43  TYR A CE1 
334  C  CE2 . TYR A 43 ? 0.54543 0.19987 0.16366 0.02923  0.01027  0.00231  43  TYR A CE2 
335  C  CZ  . TYR A 43 ? 0.54372 0.19259 0.16755 0.02823  0.03127  0.00642  43  TYR A CZ  
336  O  OH  . TYR A 43 ? 0.54219 0.18113 0.18182 0.03522  0.05014  0.00645  43  TYR A OH  
337  N  N   . LEU A 44 ? 0.61167 0.20860 0.16236 0.02998  -0.01710 0.01666  44  LEU A N   
338  C  CA  . LEU A 44 ? 0.59117 0.19642 0.16911 0.01433  0.01004  0.00805  44  LEU A CA  
339  C  C   . LEU A 44 ? 0.56915 0.17453 0.17622 -0.00118 0.03207  -0.01442 44  LEU A C   
340  O  O   . LEU A 44 ? 0.56911 0.15632 0.15992 0.00153  0.06003  -0.00890 44  LEU A O   
341  C  CB  . LEU A 44 ? 0.60291 0.19356 0.17269 -0.00668 0.00491  0.01605  44  LEU A CB  
342  C  CG  . LEU A 44 ? 0.60454 0.19794 0.18066 -0.01442 -0.00605 0.03697  44  LEU A CG  
343  C  CD1 . LEU A 44 ? 0.60056 0.19912 0.18405 -0.02612 -0.01728 0.04005  44  LEU A CD1 
344  C  CD2 . LEU A 44 ? 0.61832 0.18853 0.17684 -0.00278 -0.02301 0.02659  44  LEU A CD2 
345  N  N   . CYS A 45 ? 0.54601 0.16244 0.17544 0.00079  0.02219  -0.00035 45  CYS A N   
346  C  CA  . CYS A 45 ? 0.52429 0.16418 0.18227 -0.02218 0.04363  0.00269  45  CYS A CA  
347  C  C   . CYS A 45 ? 0.51002 0.16484 0.17999 -0.03073 0.09471  0.01615  45  CYS A C   
348  O  O   . CYS A 45 ? 0.54825 0.19833 0.19098 -0.02899 0.09163  0.00514  45  CYS A O   
349  C  CB  . CYS A 45 ? 0.50682 0.15511 0.16370 -0.01401 0.02935  -0.02092 45  CYS A CB  
350  S  SG  . CYS A 45 ? 0.48365 0.15547 0.16687 0.02543  0.03188  0.00081  45  CYS A SG  
351  N  N   . GLU A 46 ? 0.46805 0.19835 0.19795 -0.02236 0.10862  -0.02059 46  GLU A N   
352  C  CA  . GLU A 46 ? 0.45828 0.20783 0.22738 -0.03969 0.09938  -0.01959 46  GLU A CA  
353  C  C   . GLU A 46 ? 0.47853 0.21220 0.22429 -0.06235 0.09987  -0.03737 46  GLU A C   
354  O  O   . GLU A 46 ? 0.46315 0.22335 0.23954 -0.06612 0.08071  -0.03895 46  GLU A O   
355  C  CB  . GLU A 46 ? 0.41433 0.20668 0.24073 -0.04632 0.12628  -0.00190 46  GLU A CB  
356  C  CG  . GLU A 46 ? 0.39504 0.22622 0.24117 -0.03447 0.15265  0.02576  46  GLU A CG  
357  C  CD  . GLU A 46 ? 0.39465 0.20696 0.25226 -0.01326 0.13398  0.04081  46  GLU A CD  
358  O  OE1 . GLU A 46 ? 0.43058 0.18474 0.24846 -0.01094 0.10946  0.01905  46  GLU A OE1 
359  O  OE2 . GLU A 46 ? 0.36835 0.22209 0.26099 0.01360  0.15099  0.04317  46  GLU A OE2 
360  N  N   . GLN A 47 ? 0.51134 0.18940 0.19646 -0.06546 0.09086  -0.04607 47  GLN A N   
361  C  CA  . GLN A 47 ? 0.53417 0.18676 0.20339 -0.06055 0.09435  -0.01759 47  GLN A CA  
362  C  C   . GLN A 47 ? 0.57206 0.17365 0.19627 -0.05344 0.06242  -0.02548 47  GLN A C   
363  O  O   . GLN A 47 ? 0.57484 0.17052 0.19806 -0.06202 0.03043  -0.00695 47  GLN A O   
364  C  CB  . GLN A 47 ? 0.54035 0.19817 0.20645 -0.04428 0.08003  -0.01786 47  GLN A CB  
365  C  CG  . GLN A 47 ? 0.55126 0.22014 0.22498 -0.02685 0.08108  0.00847  47  GLN A CG  
366  C  CD  . GLN A 47 ? 0.57561 0.22149 0.24499 -0.02487 0.07477  0.00214  47  GLN A CD  
367  O  OE1 . GLN A 47 ? 0.57003 0.23507 0.23932 -0.03974 0.07223  0.00185  47  GLN A OE1 
368  N  NE2 . GLN A 47 ? 0.57511 0.21802 0.23838 -0.00331 0.07891  -0.00028 47  GLN A NE2 
369  N  N   . CYS A 48 ? 0.59424 0.17648 0.19772 -0.04481 0.04938  -0.01587 48  CYS A N   
370  C  CA  . CYS A 48 ? 0.62419 0.18918 0.22388 -0.03470 0.05835  -0.01084 48  CYS A CA  
371  C  C   . CYS A 48 ? 0.61278 0.18429 0.20320 -0.07229 0.06894  -0.03225 48  CYS A C   
372  O  O   . CYS A 48 ? 0.59657 0.19103 0.23246 -0.11112 0.06084  -0.03117 48  CYS A O   
373  C  CB  . CYS A 48 ? 0.64853 0.19074 0.20048 -0.00822 0.04603  0.00831  48  CYS A CB  
374  S  SG  . CYS A 48 ? 0.66925 0.17945 0.19298 0.04548  -0.01574 -0.01031 48  CYS A SG  
375  N  N   . ASP A 49 ? 0.62149 0.22593 0.19571 -0.09202 0.10266  -0.03295 49  ASP A N   
376  C  CA  . ASP A 49 ? 0.60970 0.27518 0.23218 -0.11726 0.10928  -0.02316 49  ASP A CA  
377  C  C   . ASP A 49 ? 0.60462 0.28026 0.26924 -0.15192 0.10612  -0.02080 49  ASP A C   
378  O  O   . ASP A 49 ? 0.61915 0.28198 0.26572 -0.14831 0.12982  -0.01256 49  ASP A O   
379  C  CB  . ASP A 49 ? 0.60431 0.29684 0.23492 -0.12461 0.11289  -0.00141 49  ASP A CB  
380  C  CG  . ASP A 49 ? 0.60090 0.31921 0.23552 -0.12213 0.09639  0.00654  49  ASP A CG  
381  O  OD1 . ASP A 49 ? 0.59797 0.30221 0.24406 -0.12632 0.08708  0.05017  49  ASP A OD1 
382  O  OD2 . ASP A 49 ? 0.60190 0.35055 0.20762 -0.12981 0.08104  -0.00710 49  ASP A OD2 
383  N  N   . PRO A 50 ? 0.57636 0.29271 0.30761 -0.17279 0.10865  -0.02465 50  PRO A N   
384  C  CA  . PRO A 50 ? 0.55297 0.30366 0.32897 -0.16700 0.10938  -0.02715 50  PRO A CA  
385  C  C   . PRO A 50 ? 0.54692 0.30372 0.32788 -0.15580 0.12846  -0.03243 50  PRO A C   
386  O  O   . PRO A 50 ? 0.55681 0.27808 0.30866 -0.15623 0.12622  -0.02162 50  PRO A O   
387  C  CB  . PRO A 50 ? 0.54859 0.30246 0.34148 -0.17030 0.09324  -0.03344 50  PRO A CB  
388  C  CG  . PRO A 50 ? 0.55270 0.30884 0.33925 -0.17237 0.08578  -0.04294 50  PRO A CG  
389  C  CD  . PRO A 50 ? 0.56142 0.30672 0.32358 -0.17963 0.09086  -0.04032 50  PRO A CD  
390  N  N   . ARG A 51 ? 0.53414 0.32574 0.33487 -0.14152 0.14330  -0.05144 51  ARG A N   
391  C  CA  . ARG A 51 ? 0.51873 0.34305 0.37542 -0.13665 0.15049  -0.05609 51  ARG A CA  
392  C  C   . ARG A 51 ? 0.50080 0.35444 0.43770 -0.14075 0.17244  -0.07423 51  ARG A C   
393  O  O   . ARG A 51 ? 0.49233 0.35448 0.42423 -0.14270 0.18697  -0.07084 51  ARG A O   
394  C  CB  . ARG A 51 ? 0.52224 0.33479 0.35580 -0.12914 0.13134  -0.03266 51  ARG A CB  
395  C  CG  . ARG A 51 ? 0.53072 0.30757 0.31709 -0.12090 0.12603  -0.02073 51  ARG A CG  
396  C  CD  . ARG A 51 ? 0.52910 0.28852 0.27473 -0.11473 0.11822  -0.01532 51  ARG A CD  
397  N  NE  . ARG A 51 ? 0.53735 0.26163 0.24892 -0.09462 0.11368  -0.03098 51  ARG A NE  
398  C  CZ  . ARG A 51 ? 0.54800 0.23551 0.22990 -0.08110 0.11198  -0.02765 51  ARG A CZ  
399  N  NH1 . ARG A 51 ? 0.57081 0.22094 0.25861 -0.08366 0.08651  -0.03070 51  ARG A NH1 
400  N  NH2 . ARG A 51 ? 0.55668 0.23618 0.23209 -0.08065 0.08116  -0.00335 51  ARG A NH2 
401  N  N   . PRO A 52 ? 0.49069 0.37062 0.50780 -0.13601 0.19087  -0.08972 52  PRO A N   
402  C  CA  . PRO A 52 ? 0.48314 0.38163 0.54888 -0.12828 0.19515  -0.09933 52  PRO A CA  
403  C  C   . PRO A 52 ? 0.47298 0.37859 0.59280 -0.11462 0.19560  -0.10023 52  PRO A C   
404  O  O   . PRO A 52 ? 0.47155 0.37985 0.59282 -0.11154 0.19689  -0.10682 52  PRO A O   
405  C  CB  . PRO A 52 ? 0.49329 0.38664 0.54069 -0.13210 0.20172  -0.09192 52  PRO A CB  
406  C  CG  . PRO A 52 ? 0.49718 0.38393 0.53129 -0.12887 0.20520  -0.09174 52  PRO A CG  
407  C  CD  . PRO A 52 ? 0.49243 0.37876 0.51856 -0.13117 0.20509  -0.08718 52  PRO A CD  
408  N  N   . VAL A 53 ? 0.45881 0.37913 0.62912 -0.10993 0.18220  -0.09812 53  VAL A N   
409  C  CA  . VAL A 53 ? 0.45544 0.38621 0.66630 -0.10288 0.16398  -0.08407 53  VAL A CA  
410  C  C   . VAL A 53 ? 0.46699 0.37278 0.69177 -0.09381 0.14280  -0.09028 53  VAL A C   
411  O  O   . VAL A 53 ? 0.46849 0.35859 0.70169 -0.08342 0.13506  -0.09586 53  VAL A O   
412  C  CB  . VAL A 53 ? 0.44209 0.39410 0.67367 -0.09667 0.17187  -0.06725 53  VAL A CB  
413  C  CG1 . VAL A 53 ? 0.43882 0.39974 0.67660 -0.08876 0.17373  -0.06703 53  VAL A CG1 
414  C  CG2 . VAL A 53 ? 0.43275 0.39400 0.67969 -0.10236 0.17343  -0.05472 53  VAL A CG2 
415  N  N   . GLY B 1  ? 0.47603 0.31113 0.31725 -0.01126 0.02577  0.06713  1   GLY B N   
416  C  CA  . GLY B 1  ? 0.47531 0.31623 0.32982 -0.00455 0.03141  0.07082  1   GLY B CA  
417  C  C   . GLY B 1  ? 0.47269 0.32214 0.33249 -0.00020 0.03255  0.07568  1   GLY B C   
418  O  O   . GLY B 1  ? 0.46774 0.30032 0.31786 -0.00815 0.03113  0.05781  1   GLY B O   
419  N  N   . PRO B 2  ? 0.48167 0.34378 0.35747 -0.00833 0.05364  0.10749  2   PRO B N   
420  C  CA  . PRO B 2  ? 0.48410 0.36558 0.35853 -0.01732 0.06359  0.11608  2   PRO B CA  
421  C  C   . PRO B 2  ? 0.47235 0.38446 0.36242 -0.01532 0.04581  0.10038  2   PRO B C   
422  O  O   . PRO B 2  ? 0.48541 0.41182 0.35099 -0.01905 0.03663  0.06592  2   PRO B O   
423  C  CB  . PRO B 2  ? 0.49299 0.36729 0.35474 -0.01851 0.06084  0.13603  2   PRO B CB  
424  C  CG  . PRO B 2  ? 0.50166 0.35657 0.36026 -0.02523 0.06324  0.13324  2   PRO B CG  
425  C  CD  . PRO B 2  ? 0.49344 0.34971 0.36806 -0.02245 0.06882  0.12150  2   PRO B CD  
426  N  N   . LEU B 3  ? 0.44016 0.38556 0.35865 -0.01126 0.04631  0.12329  3   LEU B N   
427  C  CA  . LEU B 3  ? 0.41481 0.39155 0.36887 -0.02136 0.03541  0.12471  3   LEU B CA  
428  C  C   . LEU B 3  ? 0.40441 0.35462 0.32507 -0.02158 0.01781  0.08973  3   LEU B C   
429  O  O   . LEU B 3  ? 0.41067 0.39699 0.31829 -0.01244 0.00630  0.07643  3   LEU B O   
430  C  CB  . LEU B 3  ? 0.39783 0.43254 0.39013 -0.02478 0.04237  0.16583  3   LEU B CB  
431  C  CG  . LEU B 3  ? 0.40152 0.45523 0.40745 -0.03372 0.04234  0.17918  3   LEU B CG  
432  C  CD1 . LEU B 3  ? 0.40056 0.46586 0.41011 -0.03218 0.06522  0.18402  3   LEU B CD1 
433  C  CD2 . LEU B 3  ? 0.40545 0.46943 0.42473 -0.04324 0.02200  0.15903  3   LEU B CD2 
434  N  N   . ASP B 4  ? 0.39652 0.26879 0.28927 -0.02213 0.01645  0.05289  4   ASP B N   
435  C  CA  . ASP B 4  ? 0.39161 0.21867 0.26179 -0.01871 0.03222  0.01279  4   ASP B CA  
436  C  C   . ASP B 4  ? 0.39051 0.20071 0.25621 -0.00529 0.04542  -0.01695 4   ASP B C   
437  O  O   . ASP B 4  ? 0.39425 0.20078 0.31204 -0.03374 0.09543  -0.01285 4   ASP B O   
438  C  CB  . ASP B 4  ? 0.39357 0.22978 0.25280 0.01240  0.00749  0.00576  4   ASP B CB  
439  C  CG  . ASP B 4  ? 0.39144 0.23620 0.24319 0.00726  -0.00516 -0.01536 4   ASP B CG  
440  O  OD1 . ASP B 4  ? 0.37963 0.25407 0.22280 0.01741  -0.02736 -0.03662 4   ASP B OD1 
441  O  OD2 . ASP B 4  ? 0.39283 0.23964 0.26191 -0.00489 -0.01822 0.00940  4   ASP B OD2 
442  N  N   . VAL B 5  ? 0.35035 0.21432 0.17110 0.01600  -0.03865 0.00352  5   VAL B N   
443  C  CA  . VAL B 5  ? 0.31260 0.20299 0.15847 0.04140  -0.03512 -0.02142 5   VAL B CA  
444  C  C   . VAL B 5  ? 0.28756 0.20737 0.14917 0.02199  -0.03035 -0.00728 5   VAL B C   
445  O  O   . VAL B 5  ? 0.27236 0.23728 0.14008 0.04167  -0.00295 0.00449  5   VAL B O   
446  C  CB  . VAL B 5  ? 0.32985 0.20799 0.15848 0.05851  -0.04774 -0.01723 5   VAL B CB  
447  C  CG1 . VAL B 5  ? 0.32119 0.20084 0.18457 0.06048  -0.02091 -0.05101 5   VAL B CG1 
448  C  CG2 . VAL B 5  ? 0.35374 0.24340 0.15722 0.06832  -0.05793 -0.00121 5   VAL B CG2 
449  N  N   . ILE B 6  ? 0.24947 0.18988 0.16311 0.02089  -0.02013 0.01420  6   ILE B N   
450  C  CA  . ILE B 6  ? 0.22450 0.17852 0.16035 0.02338  -0.00406 -0.00380 6   ILE B CA  
451  C  C   . ILE B 6  ? 0.21985 0.18209 0.13956 0.01927  0.01540  0.00567  6   ILE B C   
452  O  O   . ILE B 6  ? 0.23549 0.19054 0.12868 0.02821  0.02873  -0.01501 6   ILE B O   
453  C  CB  . ILE B 6  ? 0.23363 0.17467 0.19293 0.00560  -0.00441 -0.00801 6   ILE B CB  
454  C  CG1 . ILE B 6  ? 0.24418 0.17574 0.21385 -0.01085 -0.03453 -0.01080 6   ILE B CG1 
455  C  CG2 . ILE B 6  ? 0.23611 0.21546 0.20223 0.02040  -0.01244 0.00358  6   ILE B CG2 
456  C  CD1 . ILE B 6  ? 0.26378 0.18191 0.21910 -0.01461 -0.03594 -0.01476 6   ILE B CD1 
457  N  N   . ARG B 7  ? 0.20149 0.17241 0.15024 -0.00152 -0.01103 0.01054  7   ARG B N   
458  C  CA  . ARG B 7  ? 0.17819 0.17867 0.15433 0.00290  -0.01617 0.00482  7   ARG B CA  
459  C  C   . ARG B 7  ? 0.18802 0.22829 0.16567 0.00778  -0.02440 0.00067  7   ARG B C   
460  O  O   . ARG B 7  ? 0.16983 0.26365 0.16614 -0.00515 -0.01740 0.02704  7   ARG B O   
461  C  CB  . ARG B 7  ? 0.16053 0.20470 0.16701 0.00347  -0.00894 0.00242  7   ARG B CB  
462  C  CG  . ARG B 7  ? 0.16956 0.22214 0.17474 0.00090  -0.00185 -0.01848 7   ARG B CG  
463  C  CD  . ARG B 7  ? 0.18488 0.24931 0.18564 -0.01073 0.02261  -0.00741 7   ARG B CD  
464  N  NE  . ARG B 7  ? 0.19648 0.26774 0.16915 -0.02512 0.01747  0.01704  7   ARG B NE  
465  C  CZ  . ARG B 7  ? 0.15631 0.27021 0.15849 -0.00548 0.00330  0.02638  7   ARG B CZ  
466  N  NH1 . ARG B 7  ? 0.17263 0.27890 0.20845 -0.00025 -0.00362 0.02463  7   ARG B NH1 
467  N  NH2 . ARG B 7  ? 0.15546 0.28976 0.18052 -0.01972 -0.00026 0.02859  7   ARG B NH2 
468  N  N   . CYS B 8  ? 0.17967 0.23391 0.18405 0.00639  -0.01996 0.01793  8   CYS B N   
469  C  CA  . CYS B 8  ? 0.17827 0.22965 0.20381 0.00637  -0.03402 0.01520  8   CYS B CA  
470  C  C   . CYS B 8  ? 0.19031 0.23263 0.22440 -0.01806 -0.04942 0.01712  8   CYS B C   
471  O  O   . CYS B 8  ? 0.20950 0.24630 0.23011 -0.01360 -0.02990 0.00960  8   CYS B O   
472  C  CB  . CYS B 8  ? 0.18512 0.21709 0.19054 -0.00765 -0.03494 0.02016  8   CYS B CB  
473  S  SG  . CYS B 8  ? 0.20153 0.22036 0.20519 -0.00646 -0.04689 0.01874  8   CYS B SG  
474  N  N   . ILE B 9  ? 0.21673 0.22845 0.23858 -0.02540 -0.06141 0.03656  9   ILE B N   
475  C  CA  . ILE B 9  ? 0.23064 0.25469 0.26499 -0.01360 -0.05447 0.03455  9   ILE B CA  
476  C  C   . ILE B 9  ? 0.22061 0.24222 0.28494 -0.00513 -0.05784 0.03315  9   ILE B C   
477  O  O   . ILE B 9  ? 0.24869 0.22911 0.31487 -0.00505 -0.05348 0.01359  9   ILE B O   
478  C  CB  . ILE B 9  ? 0.24623 0.28217 0.25058 -0.02963 -0.06583 0.05497  9   ILE B CB  
479  C  CG1 . ILE B 9  ? 0.25108 0.27545 0.26785 -0.03898 -0.06591 0.07242  9   ILE B CG1 
480  C  CG2 . ILE B 9  ? 0.25304 0.27592 0.25990 -0.02932 -0.06304 0.06245  9   ILE B CG2 
481  C  CD1 . ILE B 9  ? 0.27258 0.28961 0.27830 -0.03256 -0.05460 0.07630  9   ILE B CD1 
482  N  N   . CYS B 10 ? 0.19792 0.25826 0.27065 -0.00372 -0.06308 0.01482  10  CYS B N   
483  C  CA  . CYS B 10 ? 0.20071 0.25092 0.28831 0.01356  -0.05061 -0.02434 10  CYS B CA  
484  C  C   . CYS B 10 ? 0.20654 0.25790 0.29415 0.02332  -0.04284 -0.04317 10  CYS B C   
485  O  O   . CYS B 10 ? 0.18903 0.27509 0.33219 0.03288  -0.01408 -0.04459 10  CYS B O   
486  C  CB  . CYS B 10 ? 0.19557 0.23311 0.30608 0.01762  -0.03840 -0.02003 10  CYS B CB  
487  S  SG  . CYS B 10 ? 0.17808 0.24364 0.26404 0.00291  -0.03172 -0.00600 10  CYS B SG  
488  N  N   . GLY B 11 ? 0.21423 0.24380 0.25167 -0.00831 -0.04485 -0.01044 11  GLY B N   
489  C  CA  . GLY B 11 ? 0.20529 0.26617 0.26442 -0.03722 -0.01212 -0.02091 11  GLY B CA  
490  C  C   . GLY B 11 ? 0.22137 0.26278 0.25113 -0.03148 -0.01350 -0.03595 11  GLY B C   
491  O  O   . GLY B 11 ? 0.25562 0.28400 0.25684 -0.03452 -0.00537 -0.04393 11  GLY B O   
492  N  N   . LEU B 12 ? 0.18971 0.23538 0.26172 0.00025  -0.02425 -0.00896 12  LEU B N   
493  C  CA  . LEU B 12 ? 0.19238 0.26182 0.26141 0.00364  -0.02056 -0.02585 12  LEU B CA  
494  C  C   . LEU B 12 ? 0.20000 0.25734 0.24563 -0.00974 0.00478  -0.03926 12  LEU B C   
495  O  O   . LEU B 12 ? 0.19218 0.26022 0.24019 -0.02493 0.01539  -0.02648 12  LEU B O   
496  C  CB  . LEU B 12 ? 0.20111 0.31644 0.28676 0.01039  -0.03403 -0.03648 12  LEU B CB  
497  C  CG  . LEU B 12 ? 0.20526 0.34666 0.27979 0.02838  -0.02624 -0.05620 12  LEU B CG  
498  C  CD1 . LEU B 12 ? 0.20100 0.35824 0.29632 0.02792  -0.03660 -0.08472 12  LEU B CD1 
499  C  CD2 . LEU B 12 ? 0.20957 0.36366 0.27279 0.05072  -0.00608 -0.04405 12  LEU B CD2 
500  N  N   . TYR B 13 ? 0.21960 0.26278 0.24017 -0.01534 -0.01692 -0.00857 13  TYR B N   
501  C  CA  . TYR B 13 ? 0.23643 0.26254 0.21089 -0.04223 -0.02017 0.00167  13  TYR B CA  
502  C  C   . TYR B 13 ? 0.24205 0.27511 0.22494 -0.05468 0.00213  -0.01968 13  TYR B C   
503  O  O   . TYR B 13 ? 0.23864 0.29449 0.20365 -0.06628 -0.01149 0.01660  13  TYR B O   
504  C  CB  . TYR B 13 ? 0.26190 0.26356 0.18654 -0.00373 -0.01385 -0.00885 13  TYR B CB  
505  C  CG  . TYR B 13 ? 0.24503 0.23643 0.19478 -0.01585 0.00015  -0.00650 13  TYR B CG  
506  C  CD1 . TYR B 13 ? 0.25008 0.23707 0.21530 -0.02652 0.00070  0.02580  13  TYR B CD1 
507  C  CD2 . TYR B 13 ? 0.23227 0.23931 0.17675 -0.00883 -0.00329 0.00482  13  TYR B CD2 
508  C  CE1 . TYR B 13 ? 0.24872 0.22560 0.22434 -0.01239 -0.00992 0.01639  13  TYR B CE1 
509  C  CE2 . TYR B 13 ? 0.26521 0.23954 0.17518 0.00200  -0.02571 0.01005  13  TYR B CE2 
510  C  CZ  . TYR B 13 ? 0.26026 0.23980 0.22038 0.00560  -0.01502 0.04293  13  TYR B CZ  
511  O  OH  . TYR B 13 ? 0.26920 0.26124 0.26314 0.05266  0.02557  0.05620  13  TYR B OH  
512  N  N   . LYS B 14 ? 0.24742 0.28236 0.26116 -0.05817 0.03627  -0.05182 14  LYS B N   
513  C  CA  . LYS B 14 ? 0.27013 0.29707 0.26636 -0.05911 0.03598  -0.05839 14  LYS B CA  
514  C  C   . LYS B 14 ? 0.27595 0.27164 0.21104 -0.07639 0.01723  -0.01610 14  LYS B C   
515  O  O   . LYS B 14 ? 0.27828 0.28190 0.23425 -0.07155 0.01424  0.02572  14  LYS B O   
516  C  CB  . LYS B 14 ? 0.29373 0.34626 0.30902 -0.03329 0.02602  -0.06582 14  LYS B CB  
517  C  CG  . LYS B 14 ? 0.30450 0.38026 0.34917 -0.00505 0.04201  -0.04927 14  LYS B CG  
518  C  CD  . LYS B 14 ? 0.31602 0.41258 0.37167 0.02043  0.05898  -0.04489 14  LYS B CD  
519  C  CE  . LYS B 14 ? 0.32909 0.42810 0.37645 0.03021  0.06120  -0.04071 14  LYS B CE  
520  N  NZ  . LYS B 14 ? 0.32945 0.43417 0.37532 0.03688  0.05877  -0.04328 14  LYS B NZ  
521  N  N   . ASP B 15 ? 0.30595 0.23952 0.20626 -0.07283 -0.00129 -0.01850 15  ASP B N   
522  C  CA  . ASP B 15 ? 0.34111 0.25983 0.24428 -0.05985 -0.02469 -0.02559 15  ASP B CA  
523  C  C   . ASP B 15 ? 0.33906 0.30380 0.24974 -0.05736 -0.03639 -0.02064 15  ASP B C   
524  O  O   . ASP B 15 ? 0.33807 0.33297 0.24577 -0.06019 -0.01784 -0.00613 15  ASP B O   
525  C  CB  . ASP B 15 ? 0.36992 0.25133 0.28010 -0.06134 -0.03549 0.00150  15  ASP B CB  
526  C  CG  . ASP B 15 ? 0.38918 0.23969 0.32358 -0.05660 -0.04269 -0.01128 15  ASP B CG  
527  O  OD1 . ASP B 15 ? 0.40056 0.22015 0.31945 -0.04542 -0.05685 -0.02270 15  ASP B OD1 
528  O  OD2 . ASP B 15 ? 0.39620 0.24677 0.35304 -0.06194 -0.03738 -0.00101 15  ASP B OD2 
529  N  N   . GLU B 16 ? 0.32544 0.30358 0.25553 -0.01878 -0.05149 -0.02318 16  GLU B N   
530  C  CA  . GLU B 16 ? 0.33049 0.32881 0.27812 0.01282  -0.06185 -0.03718 16  GLU B CA  
531  C  C   . GLU B 16 ? 0.31523 0.30504 0.25664 -0.01368 -0.06822 -0.04245 16  GLU B C   
532  O  O   . GLU B 16 ? 0.29421 0.26874 0.26624 -0.04672 -0.08323 -0.02847 16  GLU B O   
533  C  CB  . GLU B 16 ? 0.34366 0.36487 0.29972 0.03704  -0.07236 -0.04520 16  GLU B CB  
534  C  CG  . GLU B 16 ? 0.35641 0.39694 0.32082 0.04816  -0.06841 -0.04748 16  GLU B CG  
535  C  CD  . GLU B 16 ? 0.36503 0.43049 0.34379 0.04741  -0.06205 -0.06051 16  GLU B CD  
536  O  OE1 . GLU B 16 ? 0.36444 0.44085 0.34736 0.04810  -0.04056 -0.07920 16  GLU B OE1 
537  O  OE2 . GLU B 16 ? 0.37096 0.44405 0.36013 0.04053  -0.06669 -0.05023 16  GLU B OE2 
538  N  N   . GLY B 17 ? 0.32075 0.31281 0.23789 -0.01750 -0.05418 -0.04735 17  GLY B N   
539  C  CA  . GLY B 17 ? 0.31671 0.31519 0.23808 -0.02833 -0.05237 -0.02354 17  GLY B CA  
540  C  C   . GLY B 17 ? 0.29147 0.29558 0.21277 -0.02511 -0.05544 -0.04687 17  GLY B C   
541  O  O   . GLY B 17 ? 0.29728 0.28941 0.21498 -0.03048 -0.03984 -0.02761 17  GLY B O   
542  N  N   . LEU B 18 ? 0.28907 0.29682 0.17739 -0.01464 -0.03669 -0.07135 18  LEU B N   
543  C  CA  . LEU B 18 ? 0.29011 0.32811 0.17718 0.03404  -0.02369 -0.06996 18  LEU B CA  
544  C  C   . LEU B 18 ? 0.26868 0.31692 0.17891 0.05440  -0.03381 -0.04890 18  LEU B C   
545  O  O   . LEU B 18 ? 0.25788 0.31972 0.18151 0.04574  -0.03365 -0.01124 18  LEU B O   
546  C  CB  . LEU B 18 ? 0.31958 0.37570 0.22459 0.04529  -0.01545 -0.03362 18  LEU B CB  
547  C  CG  . LEU B 18 ? 0.32665 0.37590 0.22595 0.04155  0.00299  -0.00761 18  LEU B CG  
548  C  CD1 . LEU B 18 ? 0.32862 0.37506 0.26632 0.04834  -0.01389 -0.02607 18  LEU B CD1 
549  C  CD2 . LEU B 18 ? 0.34078 0.38212 0.18366 0.03506  0.02883  0.00271  18  LEU B CD2 
550  N  N   . MET B 19 ? 0.30087 0.32023 0.14985 0.05475  -0.04619 -0.04730 19  MET B N   
551  C  CA  . MET B 19 ? 0.28769 0.30616 0.14509 0.05207  -0.02694 -0.02618 19  MET B CA  
552  C  C   . MET B 19 ? 0.27612 0.29763 0.13933 0.07414  0.00017  -0.02958 19  MET B C   
553  O  O   . MET B 19 ? 0.30236 0.28043 0.15850 0.08274  -0.00067 -0.04950 19  MET B O   
554  C  CB  . MET B 19 ? 0.29199 0.28448 0.15359 0.04190  -0.00620 -0.01505 19  MET B CB  
555  C  CG  . MET B 19 ? 0.28752 0.26728 0.17503 0.03676  -0.00529 -0.00433 19  MET B CG  
556  S  SD  . MET B 19 ? 0.30715 0.23845 0.16841 0.02248  -0.00344 -0.00648 19  MET B SD  
557  C  CE  . MET B 19 ? 0.31430 0.26338 0.18101 0.01863  -0.05404 -0.01899 19  MET B CE  
558  N  N   . ILE B 20 ? 0.26002 0.33000 0.15845 0.05979  -0.00814 -0.00165 20  ILE B N   
559  C  CA  . ILE B 20 ? 0.24246 0.35910 0.11103 0.04985  -0.00260 0.00903  20  ILE B CA  
560  C  C   . ILE B 20 ? 0.23705 0.35887 0.11330 0.07309  -0.00903 -0.01187 20  ILE B C   
561  O  O   . ILE B 20 ? 0.22672 0.34313 0.14063 0.06005  0.00824  0.00328  20  ILE B O   
562  C  CB  . ILE B 20 ? 0.23503 0.39277 0.14196 0.03111  0.00712  0.00456  20  ILE B CB  
563  C  CG1 . ILE B 20 ? 0.23491 0.44473 0.12876 0.00871  0.01964  0.00062  20  ILE B CG1 
564  C  CG2 . ILE B 20 ? 0.23841 0.38083 0.19678 0.01660  -0.02179 0.01965  20  ILE B CG2 
565  C  CD1 . ILE B 20 ? 0.25019 0.45888 0.11726 -0.00602 0.01690  0.00972  20  ILE B CD1 
566  N  N   . GLN B 21 ? 0.26265 0.38944 0.12048 0.10302  -0.02787 -0.02244 21  GLN B N   
567  C  CA  . GLN B 21 ? 0.26333 0.41830 0.13107 0.12100  -0.01936 -0.01600 21  GLN B CA  
568  C  C   . GLN B 21 ? 0.24122 0.46570 0.12576 0.09015  -0.00389 -0.01960 21  GLN B C   
569  O  O   . GLN B 21 ? 0.22668 0.47237 0.13457 0.08893  0.00330  -0.01043 21  GLN B O   
570  C  CB  . GLN B 21 ? 0.30484 0.40583 0.14490 0.14506  -0.02394 -0.02702 21  GLN B CB  
571  C  CG  . GLN B 21 ? 0.33711 0.40505 0.16693 0.14488  -0.04339 -0.02917 21  GLN B CG  
572  C  CD  . GLN B 21 ? 0.36899 0.38846 0.20851 0.15346  -0.01209 -0.03648 21  GLN B CD  
573  O  OE1 . GLN B 21 ? 0.37735 0.35725 0.21046 0.18560  -0.01856 -0.06297 21  GLN B OE1 
574  N  NE2 . GLN B 21 ? 0.37492 0.39063 0.21895 0.13758  -0.01281 -0.03285 21  GLN B NE2 
575  N  N   . CYS B 22 ? 0.21800 0.50259 0.13517 0.08595  0.01035  -0.01482 22  CYS B N   
576  C  CA  . CYS B 22 ? 0.20688 0.54173 0.17111 0.08694  0.02841  -0.03342 22  CYS B CA  
577  C  C   . CYS B 22 ? 0.23636 0.55340 0.16666 0.11641  0.02065  -0.03123 22  CYS B C   
578  O  O   . CYS B 22 ? 0.24025 0.55309 0.16330 0.12251  0.00707  -0.04585 22  CYS B O   
579  C  CB  . CYS B 22 ? 0.18361 0.57157 0.17135 0.07045  0.01981  -0.02764 22  CYS B CB  
580  S  SG  . CYS B 22 ? 0.18927 0.61552 0.17139 0.05996  -0.00530 -0.00085 22  CYS B SG  
581  N  N   . ASP B 23 ? 0.24281 0.59076 0.19001 0.12262  0.01736  -0.05818 23  ASP B N   
582  C  CA  . ASP B 23 ? 0.25614 0.59839 0.19068 0.14054  -0.00070 -0.07583 23  ASP B CA  
583  C  C   . ASP B 23 ? 0.26130 0.60728 0.19101 0.15022  -0.01847 -0.07747 23  ASP B C   
584  O  O   . ASP B 23 ? 0.26781 0.61927 0.22396 0.16404  -0.04939 -0.09928 23  ASP B O   
585  C  CB  . ASP B 23 ? 0.27316 0.62892 0.19106 0.13682  0.00409  -0.06861 23  ASP B CB  
586  C  CG  . ASP B 23 ? 0.26619 0.64658 0.21914 0.14520  0.00547  -0.08046 23  ASP B CG  
587  O  OD1 . ASP B 23 ? 0.27057 0.64573 0.23389 0.14901  0.01645  -0.08475 23  ASP B OD1 
588  O  OD2 . ASP B 23 ? 0.25586 0.66431 0.23254 0.15588  -0.01392 -0.05934 23  ASP B OD2 
589  N  N   . LYS B 24 ? 0.24259 0.59712 0.22015 0.12690  -0.00595 -0.03828 24  LYS B N   
590  C  CA  . LYS B 24 ? 0.25514 0.57347 0.21669 0.10480  -0.01313 -0.03936 24  LYS B CA  
591  C  C   . LYS B 24 ? 0.23813 0.56899 0.20111 0.11817  0.01245  -0.03740 24  LYS B C   
592  O  O   . LYS B 24 ? 0.22360 0.58922 0.19828 0.13010  0.01819  -0.00152 24  LYS B O   
593  C  CB  . LYS B 24 ? 0.27560 0.55782 0.25569 0.09453  0.01431  -0.05983 24  LYS B CB  
594  C  CG  . LYS B 24 ? 0.26139 0.54600 0.30984 0.10099  -0.00170 -0.07847 24  LYS B CG  
595  C  CD  . LYS B 24 ? 0.27314 0.53726 0.36990 0.09356  -0.01061 -0.09419 24  LYS B CD  
596  C  CE  . LYS B 24 ? 0.28844 0.53719 0.39078 0.07092  -0.03679 -0.10649 24  LYS B CE  
597  N  NZ  . LYS B 24 ? 0.28947 0.53473 0.40322 0.06594  -0.05960 -0.11339 24  LYS B NZ  
598  N  N   . CYS B 25 ? 0.22740 0.54405 0.18712 0.11806  0.00292  -0.04798 25  CYS B N   
599  C  CA  . CYS B 25 ? 0.23556 0.52013 0.17197 0.13128  -0.01607 -0.04077 25  CYS B CA  
600  C  C   . CYS B 25 ? 0.23785 0.50892 0.16567 0.14549  -0.01148 -0.00534 25  CYS B C   
601  O  O   . CYS B 25 ? 0.25275 0.51114 0.18371 0.14666  0.01055  -0.01663 25  CYS B O   
602  C  CB  . CYS B 25 ? 0.21281 0.52244 0.15981 0.12110  -0.00899 -0.01827 25  CYS B CB  
603  S  SG  . CYS B 25 ? 0.18783 0.52846 0.17715 0.09204  -0.01240 -0.00002 25  CYS B SG  
604  N  N   . MET B 26 ? 0.23700 0.49921 0.18996 0.13664  -0.01996 -0.01071 26  MET B N   
605  C  CA  . MET B 26 ? 0.26360 0.46530 0.19645 0.14304  -0.03327 -0.01072 26  MET B CA  
606  C  C   . MET B 26 ? 0.26239 0.40677 0.17192 0.11412  -0.01116 -0.03089 26  MET B C   
607  O  O   . MET B 26 ? 0.29263 0.40537 0.16891 0.11643  -0.01390 -0.05372 26  MET B O   
608  C  CB  . MET B 26 ? 0.27408 0.49813 0.23459 0.18018  -0.03587 -0.01756 26  MET B CB  
609  C  CG  . MET B 26 ? 0.29208 0.51759 0.27416 0.20524  -0.00706 -0.02281 26  MET B CG  
610  S  SD  . MET B 26 ? 0.32415 0.53435 0.31457 0.21554  0.02533  -0.04278 26  MET B SD  
611  C  CE  . MET B 26 ? 0.31708 0.54437 0.31386 0.19707  0.01597  -0.05627 26  MET B CE  
612  N  N   . VAL B 27 ? 0.23861 0.37136 0.16198 0.09620  -0.01113 -0.02810 27  VAL B N   
613  C  CA  . VAL B 27 ? 0.21293 0.33981 0.15990 0.07379  -0.02641 -0.01278 27  VAL B CA  
614  C  C   . VAL B 27 ? 0.21049 0.32112 0.15588 0.05938  -0.01041 -0.01310 27  VAL B C   
615  O  O   . VAL B 27 ? 0.22466 0.37145 0.16948 0.05102  0.00958  -0.01371 27  VAL B O   
616  C  CB  . VAL B 27 ? 0.21374 0.33136 0.16167 0.05557  -0.01267 -0.00764 27  VAL B CB  
617  C  CG1 . VAL B 27 ? 0.21295 0.34856 0.15644 0.04017  -0.02820 0.00668  27  VAL B CG1 
618  C  CG2 . VAL B 27 ? 0.19519 0.34142 0.18749 0.02875  0.00465  0.01214  27  VAL B CG2 
619  N  N   . TRP B 28 ? 0.20451 0.28700 0.14510 0.02933  -0.00294 -0.00957 28  TRP B N   
620  C  CA  . TRP B 28 ? 0.20931 0.25707 0.15258 0.03511  -0.00864 -0.00265 28  TRP B CA  
621  C  C   . TRP B 28 ? 0.20076 0.22598 0.13123 0.03283  -0.03234 -0.00466 28  TRP B C   
622  O  O   . TRP B 28 ? 0.21036 0.20991 0.14090 0.01425  -0.03435 -0.00402 28  TRP B O   
623  C  CB  . TRP B 28 ? 0.26316 0.24825 0.18186 0.04068  -0.02063 -0.00630 28  TRP B CB  
624  C  CG  . TRP B 28 ? 0.29598 0.25407 0.15829 0.07206  -0.02558 -0.00265 28  TRP B CG  
625  C  CD1 . TRP B 28 ? 0.31390 0.24707 0.17741 0.06851  -0.03106 -0.00300 28  TRP B CD1 
626  C  CD2 . TRP B 28 ? 0.32787 0.27009 0.14908 0.07407  -0.03139 -0.03062 28  TRP B CD2 
627  N  NE1 . TRP B 28 ? 0.32820 0.24235 0.18330 0.08028  -0.02666 -0.01898 28  TRP B NE1 
628  C  CE2 . TRP B 28 ? 0.33120 0.26110 0.17034 0.07881  -0.02050 -0.03857 28  TRP B CE2 
629  C  CE3 . TRP B 28 ? 0.32463 0.27662 0.15911 0.06770  -0.02566 -0.04909 28  TRP B CE3 
630  C  CZ2 . TRP B 28 ? 0.33752 0.26500 0.17889 0.09050  -0.03107 -0.05936 28  TRP B CZ2 
631  C  CZ3 . TRP B 28 ? 0.33112 0.28925 0.16674 0.07850  -0.02022 -0.04895 28  TRP B CZ3 
632  C  CH2 . TRP B 28 ? 0.32245 0.28312 0.17355 0.09444  -0.02019 -0.05999 28  TRP B CH2 
633  N  N   . GLN B 29 ? 0.18879 0.21652 0.12607 0.04598  -0.02029 0.01314  29  GLN B N   
634  C  CA  . GLN B 29 ? 0.21188 0.21964 0.15678 0.01892  -0.02922 0.01187  29  GLN B CA  
635  C  C   . GLN B 29 ? 0.22152 0.23525 0.14637 0.02567  -0.02331 0.00017  29  GLN B C   
636  O  O   . GLN B 29 ? 0.23286 0.24048 0.16241 0.03635  -0.01778 0.00852  29  GLN B O   
637  C  CB  . GLN B 29 ? 0.20780 0.25894 0.17171 -0.01110 -0.02814 0.02074  29  GLN B CB  
638  C  CG  . GLN B 29 ? 0.19881 0.28680 0.17592 -0.01022 -0.03386 0.03851  29  GLN B CG  
639  C  CD  . GLN B 29 ? 0.14459 0.31553 0.15515 -0.00167 -0.01541 0.04587  29  GLN B CD  
640  O  OE1 . GLN B 29 ? 0.17816 0.36715 0.17123 0.00706  -0.00033 0.04406  29  GLN B OE1 
641  N  NE2 . GLN B 29 ? 0.14620 0.31723 0.17359 0.02018  -0.01562 0.01934  29  GLN B NE2 
642  N  N   . HIS B 30 ? 0.21107 0.24765 0.15062 0.01652  -0.02322 0.01219  30  HIS B N   
643  C  CA  . HIS B 30 ? 0.21771 0.27395 0.16727 0.01530  -0.03789 0.01872  30  HIS B CA  
644  C  C   . HIS B 30 ? 0.20620 0.29056 0.17720 -0.00059 -0.03676 0.02293  30  HIS B C   
645  O  O   . HIS B 30 ? 0.18445 0.25251 0.18510 -0.01910 -0.04789 0.02065  30  HIS B O   
646  C  CB  . HIS B 30 ? 0.20438 0.26048 0.17260 0.00998  -0.01846 -0.00555 30  HIS B CB  
647  C  CG  . HIS B 30 ? 0.20094 0.25120 0.17461 0.00693  -0.00983 0.00837  30  HIS B CG  
648  N  ND1 . HIS B 30 ? 0.18356 0.23428 0.18533 0.01597  -0.00998 0.00098  30  HIS B ND1 
649  C  CD2 . HIS B 30 ? 0.21419 0.24374 0.17277 -0.01708 -0.01157 0.01716  30  HIS B CD2 
650  C  CE1 . HIS B 30 ? 0.20473 0.23554 0.18495 -0.00074 -0.00690 -0.00050 30  HIS B CE1 
651  N  NE2 . HIS B 30 ? 0.22071 0.24107 0.17976 -0.00516 -0.00082 -0.01580 30  HIS B NE2 
652  N  N   . CYS B 31 ? 0.20979 0.33716 0.17453 0.02862  -0.02898 0.01659  31  CYS B N   
653  C  CA  . CYS B 31 ? 0.24314 0.37048 0.16026 0.04827  -0.02206 0.01133  31  CYS B CA  
654  C  C   . CYS B 31 ? 0.24345 0.36848 0.17081 0.03503  -0.02996 0.04401  31  CYS B C   
655  O  O   . CYS B 31 ? 0.25505 0.38175 0.18210 0.01706  -0.02506 0.06828  31  CYS B O   
656  C  CB  . CYS B 31 ? 0.25603 0.39538 0.16079 0.06700  -0.02051 -0.00371 31  CYS B CB  
657  S  SG  . CYS B 31 ? 0.24129 0.41258 0.16082 0.07001  -0.03500 -0.03344 31  CYS B SG  
658  N  N   . ASP B 32 ? 0.24408 0.36362 0.18563 0.02684  -0.06089 0.03724  32  ASP B N   
659  C  CA  . ASP B 32 ? 0.23897 0.35037 0.21780 0.02205  -0.04777 0.03863  32  ASP B CA  
660  C  C   . ASP B 32 ? 0.24659 0.33039 0.22672 0.00429  -0.06106 0.07056  32  ASP B C   
661  O  O   . ASP B 32 ? 0.27910 0.31833 0.23664 -0.01246 -0.07713 0.09045  32  ASP B O   
662  C  CB  . ASP B 32 ? 0.21778 0.35201 0.25341 0.02304  -0.04856 -0.00623 32  ASP B CB  
663  C  CG  . ASP B 32 ? 0.22586 0.35429 0.26244 0.03335  -0.05990 -0.02540 32  ASP B CG  
664  O  OD1 . ASP B 32 ? 0.24405 0.35803 0.24283 0.03836  -0.06051 -0.05357 32  ASP B OD1 
665  O  OD2 . ASP B 32 ? 0.22154 0.35974 0.29292 0.03313  -0.07519 -0.01298 32  ASP B OD2 
666  N  N   . CYS B 33 ? 0.22388 0.31525 0.22724 -0.00413 -0.07551 0.06701  33  CYS B N   
667  C  CA  . CYS B 33 ? 0.22637 0.31316 0.24412 -0.02638 -0.07315 0.07051  33  CYS B CA  
668  C  C   . CYS B 33 ? 0.21715 0.33455 0.26934 -0.03761 -0.07198 0.09077  33  CYS B C   
669  O  O   . CYS B 33 ? 0.21142 0.31977 0.29713 -0.03702 -0.09591 0.11162  33  CYS B O   
670  C  CB  . CYS B 33 ? 0.22741 0.29578 0.24266 -0.00811 -0.06249 0.04598  33  CYS B CB  
671  S  SG  . CYS B 33 ? 0.21391 0.26278 0.25629 0.00712  -0.07607 0.01725  33  CYS B SG  
672  N  N   . MET B 34 ? 0.23536 0.37199 0.26549 -0.04712 -0.05747 0.08962  34  MET B N   
673  C  CA  . MET B 34 ? 0.23796 0.41537 0.24875 -0.03993 -0.05463 0.13172  34  MET B CA  
674  C  C   . MET B 34 ? 0.27260 0.46584 0.26136 -0.03698 -0.08679 0.16132  34  MET B C   
675  O  O   . MET B 34 ? 0.29367 0.47438 0.26297 -0.05291 -0.07209 0.17980  34  MET B O   
676  C  CB  . MET B 34 ? 0.21859 0.40617 0.23298 -0.01434 -0.03440 0.10951  34  MET B CB  
677  C  CG  . MET B 34 ? 0.20329 0.38468 0.22520 -0.01297 -0.02983 0.09234  34  MET B CG  
678  S  SD  . MET B 34 ? 0.19702 0.34335 0.25535 -0.02806 -0.04855 0.08865  34  MET B SD  
679  C  CE  . MET B 34 ? 0.20328 0.33657 0.28783 -0.05195 -0.04090 0.07451  34  MET B CE  
680  N  N   . GLY B 35 ? 0.29519 0.50731 0.27490 -0.04596 -0.09013 0.17346  35  GLY B N   
681  C  CA  . GLY B 35 ? 0.32991 0.53913 0.26470 -0.04302 -0.08887 0.16915  35  GLY B CA  
682  C  C   . GLY B 35 ? 0.34819 0.57330 0.25071 -0.04233 -0.06409 0.17289  35  GLY B C   
683  O  O   . GLY B 35 ? 0.36030 0.57978 0.25184 -0.04393 -0.04288 0.18258  35  GLY B O   
684  N  N   . VAL B 36 ? 0.35880 0.59613 0.26414 -0.02242 -0.07961 0.13942  36  VAL B N   
685  C  CA  . VAL B 36 ? 0.36704 0.61097 0.24731 -0.02791 -0.04845 0.08227  36  VAL B CA  
686  C  C   . VAL B 36 ? 0.38289 0.61265 0.26222 -0.01371 -0.07599 0.01744  36  VAL B C   
687  O  O   . VAL B 36 ? 0.38887 0.60206 0.22334 -0.01343 -0.06218 0.00493  36  VAL B O   
688  C  CB  . VAL B 36 ? 0.35471 0.60910 0.25380 -0.05786 -0.06548 0.09586  36  VAL B CB  
689  C  CG1 . VAL B 36 ? 0.35154 0.60328 0.25562 -0.07599 -0.10672 0.09798  36  VAL B CG1 
690  C  CG2 . VAL B 36 ? 0.35017 0.60740 0.24954 -0.06864 -0.06108 0.09205  36  VAL B CG2 
691  N  N   . ASN B 37 ? 0.40266 0.62039 0.33097 0.00315  -0.09237 -0.00681 37  ASN B N   
692  C  CA  . ASN B 37 ? 0.43547 0.63157 0.36861 0.01539  -0.09247 -0.04764 37  ASN B CA  
693  C  C   . ASN B 37 ? 0.44909 0.62252 0.33947 0.01829  -0.05142 -0.05052 37  ASN B C   
694  O  O   . ASN B 37 ? 0.44819 0.63628 0.30159 0.02723  -0.03370 -0.06249 37  ASN B O   
695  C  CB  . ASN B 37 ? 0.45051 0.65052 0.42478 0.01408  -0.11670 -0.06322 37  ASN B CB  
696  C  CG  . ASN B 37 ? 0.46820 0.66625 0.46141 0.01166  -0.14138 -0.07373 37  ASN B CG  
697  O  OD1 . ASN B 37 ? 0.48986 0.67112 0.47527 0.00238  -0.13975 -0.08732 37  ASN B OD1 
698  N  ND2 . ASN B 37 ? 0.46711 0.67239 0.47783 0.01358  -0.15526 -0.07468 37  ASN B ND2 
699  N  N   . SER B 38 ? 0.45694 0.60261 0.33943 0.02739  -0.01694 -0.01068 38  SER B N   
700  C  CA  . SER B 38 ? 0.46061 0.58238 0.31533 0.02999  0.00714  0.00264  38  SER B CA  
701  C  C   . SER B 38 ? 0.45337 0.56401 0.31045 0.03490  0.03180  0.03978  38  SER B C   
702  O  O   . SER B 38 ? 0.46405 0.55418 0.29075 0.02638  0.05312  0.05194  38  SER B O   
703  C  CB  . SER B 38 ? 0.46146 0.58254 0.30629 0.02200  -0.00997 -0.02896 38  SER B CB  
704  O  OG  . SER B 38 ? 0.46160 0.58050 0.29965 0.01421  -0.02693 -0.04393 38  SER B OG  
705  N  N   . ASP B 39 ? 0.43846 0.55701 0.32126 0.04629  0.03774  0.06266  39  ASP B N   
706  C  CA  . ASP B 39 ? 0.43301 0.55531 0.32416 0.06324  0.03749  0.07353  39  ASP B CA  
707  C  C   . ASP B 39 ? 0.42014 0.56120 0.30397 0.08635  0.02530  0.05616  39  ASP B C   
708  O  O   . ASP B 39 ? 0.41271 0.55064 0.33629 0.08745  0.02617  0.06051  39  ASP B O   
709  C  CB  . ASP B 39 ? 0.42999 0.55219 0.34402 0.05485  0.03173  0.07783  39  ASP B CB  
710  C  CG  . ASP B 39 ? 0.43273 0.55676 0.37020 0.04328  0.03780  0.08098  39  ASP B CG  
711  O  OD1 . ASP B 39 ? 0.43523 0.55850 0.38585 0.03926  0.04076  0.07969  39  ASP B OD1 
712  O  OD2 . ASP B 39 ? 0.43193 0.56134 0.38241 0.03406  0.03978  0.07627  39  ASP B OD2 
713  N  N   . VAL B 40 ? 0.41505 0.58244 0.24546 0.10313  0.02502  0.05815  40  VAL B N   
714  C  CA  . VAL B 40 ? 0.40190 0.61170 0.20752 0.09464  0.03286  0.01216  40  VAL B CA  
715  C  C   . VAL B 40 ? 0.39942 0.62803 0.19940 0.10086  0.04466  0.04844  40  VAL B C   
716  O  O   . VAL B 40 ? 0.39316 0.62545 0.22652 0.09879  0.04889  0.10441  40  VAL B O   
717  C  CB  . VAL B 40 ? 0.41204 0.62726 0.20656 0.09187  0.03073  -0.00976 40  VAL B CB  
718  C  CG1 . VAL B 40 ? 0.42112 0.62216 0.24174 0.09583  0.02145  -0.02412 40  VAL B CG1 
719  C  CG2 . VAL B 40 ? 0.40410 0.64013 0.21035 0.08525  0.03873  0.00152  40  VAL B CG2 
720  N  N   . GLU B 41 ? 0.40148 0.64164 0.18077 0.10459  0.04794  0.01830  41  GLU B N   
721  C  CA  . GLU B 41 ? 0.40154 0.65869 0.19036 0.11399  0.05578  0.01213  41  GLU B CA  
722  C  C   . GLU B 41 ? 0.37860 0.66971 0.18882 0.11450  0.04657  0.01769  41  GLU B C   
723  O  O   . GLU B 41 ? 0.38290 0.68036 0.22277 0.12621  0.02772  0.02997  41  GLU B O   
724  C  CB  . GLU B 41 ? 0.42227 0.66865 0.20562 0.11473  0.06099  0.01559  41  GLU B CB  
725  C  CG  . GLU B 41 ? 0.42371 0.67183 0.24528 0.12835  0.06657  0.02269  41  GLU B CG  
726  C  CD  . GLU B 41 ? 0.43145 0.67418 0.26993 0.13654  0.07803  0.02272  41  GLU B CD  
727  O  OE1 . GLU B 41 ? 0.43717 0.67465 0.27906 0.12938  0.07099  0.02689  41  GLU B OE1 
728  O  OE2 . GLU B 41 ? 0.43331 0.67437 0.29012 0.14048  0.06380  0.02481  41  GLU B OE2 
729  N  N   . HIS B 42 ? 0.35914 0.67881 0.18720 0.11193  0.03672  0.00057  42  HIS B N   
730  C  CA  . HIS B 42 ? 0.35632 0.70136 0.20494 0.12881  0.02107  -0.03943 42  HIS B CA  
731  C  C   . HIS B 42 ? 0.31679 0.66476 0.18418 0.11218  0.01664  -0.04058 42  HIS B C   
732  O  O   . HIS B 42 ? 0.33783 0.67915 0.18038 0.11258  0.01152  -0.01491 42  HIS B O   
733  C  CB  . HIS B 42 ? 0.36857 0.72660 0.24897 0.15011  0.03014  -0.06545 42  HIS B CB  
734  C  CG  . HIS B 42 ? 0.38453 0.75914 0.29510 0.16079  0.03494  -0.07264 42  HIS B CG  
735  N  ND1 . HIS B 42 ? 0.38784 0.76520 0.30261 0.16799  0.04993  -0.07353 42  HIS B ND1 
736  C  CD2 . HIS B 42 ? 0.38778 0.77013 0.30165 0.16965  0.06346  -0.07440 42  HIS B CD2 
737  C  CE1 . HIS B 42 ? 0.38827 0.77085 0.31399 0.17284  0.06734  -0.06807 42  HIS B CE1 
738  N  NE2 . HIS B 42 ? 0.38754 0.77114 0.31721 0.17885  0.07258  -0.07013 42  HIS B NE2 
739  N  N   . TYR B 43 ? 0.28345 0.64758 0.17729 0.09688  0.01072  -0.04544 43  TYR B N   
740  C  CA  . TYR B 43 ? 0.24627 0.62048 0.15862 0.06604  -0.00051 -0.01537 43  TYR B CA  
741  C  C   . TYR B 43 ? 0.22362 0.61554 0.15681 0.06356  0.00424  -0.00354 43  TYR B C   
742  O  O   . TYR B 43 ? 0.20152 0.62875 0.16227 0.08721  -0.00541 -0.01101 43  TYR B O   
743  C  CB  . TYR B 43 ? 0.23607 0.60213 0.16014 0.06323  -0.00742 -0.02783 43  TYR B CB  
744  C  CG  . TYR B 43 ? 0.22057 0.57072 0.16062 0.04898  0.00066  0.00126  43  TYR B CG  
745  C  CD1 . TYR B 43 ? 0.22810 0.55287 0.14464 0.03698  0.00379  0.00801  43  TYR B CD1 
746  C  CD2 . TYR B 43 ? 0.20921 0.54141 0.14451 0.03563  0.00443  -0.01157 43  TYR B CD2 
747  C  CE1 . TYR B 43 ? 0.21921 0.53815 0.15963 0.03222  0.00157  0.03322  43  TYR B CE1 
748  C  CE2 . TYR B 43 ? 0.19926 0.52482 0.15527 0.02375  -0.01068 0.00409  43  TYR B CE2 
749  C  CZ  . TYR B 43 ? 0.19365 0.52244 0.15757 0.02994  -0.01071 0.03131  43  TYR B CZ  
750  O  OH  . TYR B 43 ? 0.16745 0.51071 0.15724 0.04154  -0.00144 0.04409  43  TYR B OH  
751  N  N   . LEU B 44 ? 0.21819 0.61742 0.15799 0.03657  0.01035  -0.01494 44  LEU B N   
752  C  CA  . LEU B 44 ? 0.19582 0.59898 0.17082 0.02418  0.00975  0.00344  44  LEU B CA  
753  C  C   . LEU B 44 ? 0.17190 0.58367 0.17062 -0.00007 -0.00911 0.01797  44  LEU B C   
754  O  O   . LEU B 44 ? 0.15664 0.59957 0.15862 -0.00409 -0.00358 0.04962  44  LEU B O   
755  C  CB  . LEU B 44 ? 0.19519 0.60501 0.18546 0.01750  0.02624  0.01339  44  LEU B CB  
756  C  CG  . LEU B 44 ? 0.20855 0.60923 0.20151 0.02219  0.05207  0.01152  44  LEU B CG  
757  C  CD1 . LEU B 44 ? 0.22660 0.60712 0.19932 0.00929  0.05941  0.01290  44  LEU B CD1 
758  C  CD2 . LEU B 44 ? 0.20291 0.62098 0.20552 0.03531  0.04654  -0.00344 44  LEU B CD2 
759  N  N   . CYS B 45 ? 0.16873 0.55025 0.17707 0.01185  0.00812  0.01736  45  CYS B N   
760  C  CA  . CYS B 45 ? 0.17106 0.51879 0.17976 -0.00630 -0.00436 0.03889  45  CYS B CA  
761  C  C   . CYS B 45 ? 0.17314 0.49819 0.18312 -0.01901 0.01521  0.08828  45  CYS B C   
762  O  O   . CYS B 45 ? 0.19223 0.52798 0.19495 -0.03193 0.00417  0.09697  45  CYS B O   
763  C  CB  . CYS B 45 ? 0.16360 0.50796 0.15642 0.00065  -0.03081 0.02795  45  CYS B CB  
764  S  SG  . CYS B 45 ? 0.16300 0.48815 0.16250 0.03447  -0.00290 0.02759  45  CYS B SG  
765  N  N   . GLU B 46 ? 0.20162 0.44992 0.19360 -0.01353 -0.02105 0.10185  46  GLU B N   
766  C  CA  . GLU B 46 ? 0.20458 0.43525 0.23424 -0.02563 -0.01392 0.09521  46  GLU B CA  
767  C  C   . GLU B 46 ? 0.19541 0.45081 0.23336 -0.03673 -0.03681 0.09169  46  GLU B C   
768  O  O   . GLU B 46 ? 0.19885 0.44851 0.23350 -0.02967 -0.03926 0.07075  46  GLU B O   
769  C  CB  . GLU B 46 ? 0.20427 0.39883 0.24868 -0.03085 -0.00356 0.11207  46  GLU B CB  
770  C  CG  . GLU B 46 ? 0.21788 0.37810 0.23620 -0.03109 0.02320  0.14126  46  GLU B CG  
771  C  CD  . GLU B 46 ? 0.19928 0.37354 0.23528 -0.01249 0.04662  0.12620  46  GLU B CD  
772  O  OE1 . GLU B 46 ? 0.17524 0.39773 0.22362 -0.00844 0.02804  0.09597  46  GLU B OE1 
773  O  OE2 . GLU B 46 ? 0.21573 0.36088 0.23591 0.01853  0.04765  0.14443  46  GLU B OE2 
774  N  N   . GLN B 47 ? 0.17929 0.47012 0.21051 -0.05258 -0.03161 0.09217  47  GLN B N   
775  C  CA  . GLN B 47 ? 0.18856 0.48792 0.22213 -0.05062 -0.00387 0.08712  47  GLN B CA  
776  C  C   . GLN B 47 ? 0.18246 0.53304 0.20921 -0.04279 -0.01675 0.05669  47  GLN B C   
777  O  O   . GLN B 47 ? 0.17801 0.53243 0.20704 -0.06144 -0.01433 0.00852  47  GLN B O   
778  C  CB  . GLN B 47 ? 0.21057 0.48053 0.21758 -0.03026 -0.00840 0.08184  47  GLN B CB  
779  C  CG  . GLN B 47 ? 0.22708 0.47314 0.24270 -0.01100 0.00527  0.08436  47  GLN B CG  
780  C  CD  . GLN B 47 ? 0.23795 0.48465 0.27383 -0.01444 0.00647  0.08433  47  GLN B CD  
781  O  OE1 . GLN B 47 ? 0.25631 0.47545 0.27993 -0.02689 0.00672  0.09212  47  GLN B OE1 
782  N  NE2 . GLN B 47 ? 0.24760 0.48632 0.28887 0.00957  -0.00368 0.07758  47  GLN B NE2 
783  N  N   . CYS B 48 ? 0.18902 0.56561 0.19575 -0.02547 -0.00990 0.06183  48  CYS B N   
784  C  CA  . CYS B 48 ? 0.19129 0.60611 0.21614 -0.02780 0.00180  0.07173  48  CYS B CA  
785  C  C   . CYS B 48 ? 0.16869 0.61047 0.19640 -0.06316 -0.00556 0.08026  48  CYS B C   
786  O  O   . CYS B 48 ? 0.18025 0.58415 0.25530 -0.10011 -0.01590 0.08267  48  CYS B O   
787  C  CB  . CYS B 48 ? 0.18453 0.63495 0.19447 -0.01244 0.00171  0.04542  48  CYS B CB  
788  S  SG  . CYS B 48 ? 0.18522 0.66405 0.19702 0.04247  -0.01317 -0.02390 48  CYS B SG  
789  N  N   . ASP B 49 ? 0.20986 0.62136 0.19208 -0.07967 -0.01808 0.10971  49  ASP B N   
790  C  CA  . ASP B 49 ? 0.26235 0.61783 0.23386 -0.09733 -0.01276 0.12788  49  ASP B CA  
791  C  C   . ASP B 49 ? 0.28149 0.61369 0.28106 -0.11789 -0.02524 0.12884  49  ASP B C   
792  O  O   . ASP B 49 ? 0.28251 0.62320 0.28745 -0.12470 -0.03518 0.16144  49  ASP B O   
793  C  CB  . ASP B 49 ? 0.28830 0.62795 0.24009 -0.09795 -0.00451 0.13750  49  ASP B CB  
794  C  CG  . ASP B 49 ? 0.32288 0.63643 0.25347 -0.08412 0.02126  0.12745  49  ASP B CG  
795  O  OD1 . ASP B 49 ? 0.31343 0.63746 0.26244 -0.07374 0.05563  0.11709  49  ASP B OD1 
796  O  OD2 . ASP B 49 ? 0.35690 0.64271 0.21912 -0.09009 0.01110  0.11603  49  ASP B OD2 
797  N  N   . PRO B 50 ? 0.27242 0.58687 0.29757 -0.14153 -0.02478 0.12178  50  PRO B N   
798  C  CA  . PRO B 50 ? 0.28927 0.56328 0.31233 -0.13015 -0.03369 0.10640  50  PRO B CA  
799  C  C   . PRO B 50 ? 0.29189 0.54826 0.30615 -0.12310 -0.04408 0.11955  50  PRO B C   
800  O  O   . PRO B 50 ? 0.26836 0.55153 0.28894 -0.12535 -0.03781 0.13235  50  PRO B O   
801  C  CB  . PRO B 50 ? 0.28753 0.56582 0.33110 -0.13076 -0.01862 0.10461  50  PRO B CB  
802  C  CG  . PRO B 50 ? 0.28360 0.57460 0.32714 -0.14227 -0.01995 0.09647  50  PRO B CG  
803  C  CD  . PRO B 50 ? 0.28701 0.58427 0.30414 -0.14385 -0.01820 0.10760  50  PRO B CD  
804  N  N   . ARG B 51 ? 0.31390 0.52675 0.30615 -0.11962 -0.05660 0.13185  51  ARG B N   
805  C  CA  . ARG B 51 ? 0.34440 0.50919 0.34515 -0.11969 -0.05897 0.14720  51  ARG B CA  
806  C  C   . ARG B 51 ? 0.36219 0.50191 0.41018 -0.12364 -0.07274 0.17148  51  ARG B C   
807  O  O   . ARG B 51 ? 0.34730 0.49133 0.39385 -0.13178 -0.06983 0.18238  51  ARG B O   
808  C  CB  . ARG B 51 ? 0.33712 0.50499 0.32836 -0.11300 -0.02944 0.12029  51  ARG B CB  
809  C  CG  . ARG B 51 ? 0.31475 0.50597 0.27848 -0.10397 -0.02219 0.11210  51  ARG B CG  
810  C  CD  . ARG B 51 ? 0.29694 0.50658 0.24555 -0.09747 -0.01922 0.09543  51  ARG B CD  
811  N  NE  . ARG B 51 ? 0.25164 0.51287 0.21625 -0.08608 -0.02112 0.10305  51  ARG B NE  
812  C  CZ  . ARG B 51 ? 0.22171 0.52333 0.20959 -0.07508 -0.02699 0.10876  51  ARG B CZ  
813  N  NH1 . ARG B 51 ? 0.20835 0.54524 0.24846 -0.06856 -0.03556 0.08172  51  ARG B NH1 
814  N  NH2 . ARG B 51 ? 0.22006 0.53271 0.21756 -0.07311 -0.00633 0.08640  51  ARG B NH2 
815  N  N   . PRO B 52 ? 0.38886 0.51069 0.49786 -0.11728 -0.08636 0.18610  52  PRO B N   
816  C  CA  . PRO B 52 ? 0.41231 0.51675 0.55135 -0.11167 -0.10002 0.18860  52  PRO B CA  
817  C  C   . PRO B 52 ? 0.42668 0.51842 0.59761 -0.11554 -0.10832 0.18964  52  PRO B C   
818  O  O   . PRO B 52 ? 0.42986 0.52134 0.61140 -0.11815 -0.10802 0.17151  52  PRO B O   
819  C  CB  . PRO B 52 ? 0.40510 0.52268 0.53860 -0.11013 -0.08930 0.19949  52  PRO B CB  
820  C  CG  . PRO B 52 ? 0.39826 0.52213 0.52294 -0.10665 -0.08514 0.20632  52  PRO B CG  
821  C  CD  . PRO B 52 ? 0.39753 0.51777 0.50802 -0.10574 -0.07988 0.20315  52  PRO B CD  
822  N  N   . VAL B 53 ? 0.44713 0.51605 0.61897 -0.10865 -0.11674 0.20621  53  VAL B N   
823  C  CA  . VAL B 53 ? 0.46350 0.52186 0.64208 -0.10465 -0.11976 0.20912  53  VAL B CA  
824  C  C   . VAL B 53 ? 0.46494 0.53220 0.64892 -0.10872 -0.13696 0.21612  53  VAL B C   
825  O  O   . VAL B 53 ? 0.47413 0.54426 0.65161 -0.09837 -0.14908 0.20608  53  VAL B O   
826  C  CB  . VAL B 53 ? 0.47497 0.51533 0.65351 -0.09483 -0.10421 0.20690  53  VAL B CB  
827  C  CG1 . VAL B 53 ? 0.48031 0.50778 0.65665 -0.09239 -0.09583 0.21142  53  VAL B CG1 
828  C  CG2 . VAL B 53 ? 0.47201 0.50988 0.65837 -0.09808 -0.10067 0.20360  53  VAL B CG2 
829  N  N   . ALA C 1  ? 0.46788 0.55322 0.30255 0.16751  0.13969  -0.01460 1   ALA P N   
830  C  CA  . ALA C 1  ? 0.47158 0.55814 0.30429 0.16483  0.11599  -0.00777 1   ALA P CA  
831  C  C   . ALA C 1  ? 0.47632 0.54831 0.28385 0.16082  0.06838  -0.02570 1   ALA P C   
832  O  O   . ALA C 1  ? 0.48841 0.56627 0.27741 0.13869  0.04717  -0.03852 1   ALA P O   
833  C  CB  . ALA C 1  ? 0.47355 0.55695 0.30681 0.16083  0.11684  0.00874  1   ALA P CB  
834  N  N   . ARG C 2  ? 0.46639 0.51425 0.27160 0.17866  0.04201  -0.04023 2   ARG P N   
835  C  CA  . ARG C 2  ? 0.46210 0.49835 0.23142 0.18169  0.01778  -0.03462 2   ARG P CA  
836  C  C   . ARG C 2  ? 0.44470 0.46060 0.18251 0.18117  0.00011  -0.05909 2   ARG P C   
837  O  O   . ARG C 2  ? 0.42709 0.46778 0.17060 0.16909  -0.00333 -0.05773 2   ARG P O   
838  C  CB  . ARG C 2  ? 0.48633 0.52149 0.24447 0.16203  0.00784  -0.00389 2   ARG P CB  
839  C  CG  . ARG C 2  ? 0.51719 0.52403 0.28662 0.15563  -0.00393 0.00601  2   ARG P CG  
840  C  CD  . ARG C 2  ? 0.54493 0.52935 0.31597 0.14020  -0.01515 0.00267  2   ARG P CD  
841  N  NE  . ARG C 2  ? 0.56573 0.53133 0.34538 0.12875  -0.02581 -0.00125 2   ARG P NE  
842  C  CZ  . ARG C 2  ? 0.57167 0.52877 0.36674 0.12738  -0.03369 -0.00574 2   ARG P CZ  
843  N  NH1 . ARG C 2  ? 0.57345 0.52886 0.37468 0.13222  -0.03797 -0.01839 2   ARG P NH1 
844  N  NH2 . ARG C 2  ? 0.57363 0.52797 0.37346 0.12268  -0.03167 -0.00095 2   ARG P NH2 
845  N  N   . THR C 3  ? 0.45118 0.43442 0.18404 0.16670  0.00313  -0.05393 3   THR P N   
846  C  CA  . THR C 3  ? 0.48088 0.41101 0.18358 0.13191  -0.02097 -0.07088 3   THR P CA  
847  C  C   . THR C 3  ? 0.47946 0.36805 0.20076 0.11524  -0.00346 -0.09790 3   THR P C   
848  O  O   . THR C 3  ? 0.48228 0.35348 0.23490 0.11369  -0.00810 -0.10407 3   THR P O   
849  C  CB  . THR C 3  ? 0.49722 0.43059 0.16626 0.11711  -0.01720 -0.07028 3   THR P CB  
850  O  OG1 . THR C 3  ? 0.51331 0.43948 0.18419 0.10974  -0.02217 -0.09615 3   THR P OG1 
851  C  CG2 . THR C 3  ? 0.49799 0.43217 0.16188 0.11337  -0.01383 -0.05890 3   THR P CG2 
852  N  N   . M3L C 4  ? 0.49501 0.34890 0.22611 0.07185  -0.01877 -0.09598 4   M3L P N   
853  C  CA  . M3L C 4  ? 0.51330 0.32828 0.25774 0.04866  -0.03480 -0.10374 4   M3L P CA  
854  C  CB  . M3L C 4  ? 0.50905 0.29960 0.25253 0.03837  -0.03288 -0.09472 4   M3L P CB  
855  C  CG  . M3L C 4  ? 0.50086 0.29957 0.22286 0.02778  -0.03791 -0.07160 4   M3L P CG  
856  C  CD  . M3L C 4  ? 0.49096 0.30630 0.23252 0.04130  -0.01647 -0.03796 4   M3L P CD  
857  C  CE  . M3L C 4  ? 0.48949 0.30918 0.21690 0.02442  -0.01148 -0.00994 4   M3L P CE  
858  N  NZ  . M3L C 4  ? 0.49669 0.29515 0.21227 0.01383  -0.02166 -0.01267 4   M3L P NZ  
859  C  C   . M3L C 4  ? 0.53573 0.33544 0.27105 0.03612  -0.07794 -0.08929 4   M3L P C   
860  O  O   . M3L C 4  ? 0.53948 0.34023 0.26419 0.04341  -0.10319 -0.06943 4   M3L P O   
861  C  CM1 . M3L C 4  ? 0.49434 0.31767 0.23194 0.00574  -0.02879 -0.03796 4   M3L P CM1 
862  C  CM2 . M3L C 4  ? 0.49314 0.31759 0.22672 0.01005  -0.04438 -0.01102 4   M3L P CM2 
863  C  CM3 . M3L C 4  ? 0.52100 0.29042 0.18977 0.02084  -0.00833 -0.02901 4   M3L P CM3 
864  N  N   . GLN C 5  ? 0.56042 0.35201 0.31332 0.00708  -0.07373 -0.07787 5   GLN P N   
865  C  CA  . GLN C 5  ? 0.58356 0.36294 0.36122 -0.02907 -0.07294 -0.06176 5   GLN P CA  
866  C  C   . GLN C 5  ? 0.60226 0.37778 0.37306 -0.04208 -0.05423 -0.07358 5   GLN P C   
867  O  O   . GLN C 5  ? 0.60812 0.35914 0.36515 -0.03332 -0.05106 -0.07758 5   GLN P O   
868  C  CB  . GLN C 5  ? 0.59120 0.35883 0.41716 -0.05846 -0.08233 -0.02438 5   GLN P CB  
869  C  CG  . GLN C 5  ? 0.59836 0.35825 0.46487 -0.07920 -0.09965 -0.01042 5   GLN P CG  
870  C  CD  . GLN C 5  ? 0.59494 0.36097 0.50391 -0.08968 -0.11952 0.01298  5   GLN P CD  
871  O  OE1 . GLN C 5  ? 0.59416 0.35399 0.52462 -0.09419 -0.11431 0.01201  5   GLN P OE1 
872  N  NE2 . GLN C 5  ? 0.59446 0.36213 0.50723 -0.09699 -0.13447 0.02267  5   GLN P NE2 
873  N  N   . THR C 6  ? 0.61429 0.41358 0.40447 -0.05450 -0.03240 -0.04672 6   THR P N   
874  C  CA  . THR C 6  ? 0.61305 0.44281 0.41161 -0.06777 -0.02785 -0.04535 6   THR P CA  
875  C  C   . THR C 6  ? 0.61809 0.47993 0.42151 -0.07707 0.00328  -0.05948 6   THR P C   
876  O  O   . THR C 6  ? 0.62201 0.47496 0.43126 -0.07808 0.00480  -0.04874 6   THR P O   
877  C  CB  . THR C 6  ? 0.60526 0.43636 0.41382 -0.07173 -0.05511 -0.03503 6   THR P CB  
878  O  OG1 . THR C 6  ? 0.60165 0.42775 0.41933 -0.07563 -0.07970 -0.03585 6   THR P OG1 
879  C  CG2 . THR C 6  ? 0.60277 0.43506 0.40660 -0.07404 -0.05692 -0.02687 6   THR P CG2 
880  N  N   . ALA C 7  ? 0.62050 0.52121 0.42030 -0.08705 0.03130  -0.08117 7   ALA P N   
881  C  CA  . ALA C 7  ? 0.62902 0.55560 0.43141 -0.08372 0.06720  -0.09706 7   ALA P CA  
882  C  C   . ALA C 7  ? 0.62888 0.56907 0.44447 -0.07933 0.09894  -0.11213 7   ALA P C   
883  O  O   . ALA C 7  ? 0.62920 0.57187 0.45011 -0.07966 0.10948  -0.11299 7   ALA P O   
884  C  CB  . ALA C 7  ? 0.62965 0.55852 0.42104 -0.08142 0.07361  -0.10328 7   ALA P CB  
885  N  N   . ARG C 8  ? 0.62324 0.57396 0.45734 -0.07417 0.11579  -0.12005 8   ARG P N   
886  C  CA  . ARG C 8  ? 0.61621 0.58066 0.47598 -0.05759 0.13065  -0.12241 8   ARG P CA  
887  C  C   . ARG C 8  ? 0.61642 0.60461 0.49487 -0.03996 0.13187  -0.12480 8   ARG P C   
888  O  O   . ARG C 8  ? 0.62634 0.60924 0.50000 -0.04220 0.13610  -0.12402 8   ARG P O   
889  C  CB  . ARG C 8  ? 0.60630 0.56345 0.45881 -0.05588 0.13950  -0.11280 8   ARG P CB  
890  C  CG  . ARG C 8  ? 0.59479 0.54372 0.43792 -0.04677 0.14005  -0.10113 8   ARG P CG  
891  C  CD  . ARG C 8  ? 0.57504 0.52769 0.41112 -0.03463 0.15126  -0.10499 8   ARG P CD  
892  N  NE  . ARG C 8  ? 0.55600 0.51608 0.39558 -0.02738 0.16238  -0.10037 8   ARG P NE  
893  C  CZ  . ARG C 8  ? 0.54278 0.50906 0.36204 -0.00838 0.17836  -0.10796 8   ARG P CZ  
894  N  NH1 . ARG C 8  ? 0.52997 0.50845 0.37423 0.00104  0.17753  -0.10266 8   ARG P NH1 
895  N  NH2 . ARG C 8  ? 0.54882 0.50548 0.33892 -0.00308 0.16861  -0.12141 8   ARG P NH2 
896  N  N   . LYS C 9  ? 0.60118 0.62032 0.49850 -0.01952 0.12960  -0.13414 9   LYS P N   
897  C  CA  . LYS C 9  ? 0.56899 0.63272 0.50598 -0.00569 0.13925  -0.12513 9   LYS P CA  
898  C  C   . LYS C 9  ? 0.53890 0.62338 0.47027 0.01726  0.14968  -0.13150 9   LYS P C   
899  O  O   . LYS C 9  ? 0.53628 0.62582 0.46561 0.00176  0.14106  -0.13458 9   LYS P O   
900  C  CB  . LYS C 9  ? 0.57345 0.65042 0.52636 -0.01332 0.13361  -0.11181 9   LYS P CB  
901  C  CG  . LYS C 9  ? 0.58042 0.66597 0.53511 -0.02177 0.12188  -0.10180 9   LYS P CG  
902  C  CD  . LYS C 9  ? 0.58517 0.67673 0.54073 -0.03199 0.11025  -0.09243 9   LYS P CD  
903  C  CE  . LYS C 9  ? 0.58669 0.68227 0.54521 -0.03711 0.10714  -0.08084 9   LYS P CE  
904  N  NZ  . LYS C 9  ? 0.59239 0.68497 0.55447 -0.03680 0.10510  -0.07030 9   LYS P NZ  
905  N  N   . SER C 10 ? 0.51337 0.60989 0.43760 0.06057  0.16573  -0.13049 10  SER P N   
906  C  CA  . SER C 10 ? 0.50048 0.59554 0.41570 0.08977  0.12927  -0.10141 10  SER P CA  
907  C  C   . SER C 10 ? 0.46354 0.58413 0.40104 0.11554  0.11638  -0.07370 10  SER P C   
908  O  O   . SER C 10 ? 0.46109 0.58966 0.43003 0.11878  0.10899  -0.06804 10  SER P O   
909  C  CB  . SER C 10 ? 0.50723 0.59312 0.40934 0.08760  0.11108  -0.07542 10  SER P CB  
910  O  OG  . SER C 10 ? 0.51340 0.59278 0.40209 0.07628  0.10570  -0.05381 10  SER P OG  
911  N  N   . THR C 11 ? 0.42390 0.57377 0.36038 0.12041  0.11087  -0.02905 11  THR P N   
912  C  CA  . THR C 11 ? 0.38627 0.56738 0.35014 0.12749  0.10630  -0.00417 11  THR P CA  
913  C  C   . THR C 11 ? 0.38434 0.54421 0.35380 0.13974  0.07156  0.01952  11  THR P C   
914  O  O   . THR C 11 ? 0.39928 0.52149 0.31445 0.15556  0.05193  -0.00484 11  THR P O   
915  C  CB  . THR C 11 ? 0.38059 0.57945 0.34248 0.11911  0.11120  0.01596  11  THR P CB  
916  O  OG1 . THR C 11 ? 0.36055 0.58013 0.32845 0.12462  0.09116  0.00641  11  THR P OG1 
917  C  CG2 . THR C 11 ? 0.38318 0.58681 0.34338 0.10353  0.13133  0.03026  11  THR P CG2 
918  N  N   . GLY C 12 ? 0.37316 0.54983 0.38702 0.12662  0.05296  0.06153  12  GLY P N   
919  C  CA  . GLY C 12 ? 0.37011 0.56560 0.42650 0.10479  0.05032  0.08665  12  GLY P CA  
920  C  C   . GLY C 12 ? 0.37219 0.57559 0.45512 0.08950  0.04919  0.10968  12  GLY P C   
921  O  O   . GLY C 12 ? 0.37529 0.57938 0.47285 0.08431  0.04621  0.11939  12  GLY P O   
922  N  N   . ALA D 1  ? 0.58146 0.51414 0.27493 0.18102  -0.03743 0.11663  1   ALA T N   
923  C  CA  . ALA D 1  ? 0.58049 0.51654 0.27569 0.17456  -0.02622 0.09053  1   ALA T CA  
924  C  C   . ALA D 1  ? 0.57119 0.50918 0.26546 0.17006  -0.04205 0.05498  1   ALA T C   
925  O  O   . ALA D 1  ? 0.59621 0.51663 0.25888 0.14029  -0.04833 0.02496  1   ALA T O   
926  C  CB  . ALA D 1  ? 0.58907 0.52977 0.28860 0.16714  -0.01343 0.09449  1   ALA T CB  
927  N  N   . ARG D 2  ? 0.53038 0.48737 0.25795 0.18695  -0.05508 0.04462  2   ARG T N   
928  C  CA  . ARG D 2  ? 0.50209 0.48242 0.22480 0.19593  -0.04717 0.01929  2   ARG T CA  
929  C  C   . ARG D 2  ? 0.45494 0.45848 0.18379 0.18616  -0.06315 -0.00156 2   ARG T C   
930  O  O   . ARG D 2  ? 0.45650 0.43704 0.17443 0.18001  -0.05300 0.00409  2   ARG T O   
931  C  CB  . ARG D 2  ? 0.52057 0.50786 0.25715 0.18793  -0.02136 0.01195  2   ARG T CB  
932  C  CG  . ARG D 2  ? 0.52849 0.54074 0.30055 0.18512  -0.01008 -0.00390 2   ARG T CG  
933  C  CD  . ARG D 2  ? 0.53656 0.56528 0.33488 0.17213  -0.01199 -0.01729 2   ARG T CD  
934  N  NE  . ARG D 2  ? 0.53636 0.57807 0.36942 0.16980  -0.00661 -0.03068 2   ARG T NE  
935  C  CZ  . ARG D 2  ? 0.53663 0.58215 0.39948 0.16657  -0.00393 -0.03241 2   ARG T CZ  
936  N  NH1 . ARG D 2  ? 0.54264 0.58470 0.41102 0.16707  -0.00399 -0.03735 2   ARG T NH1 
937  N  NH2 . ARG D 2  ? 0.53357 0.58125 0.40939 0.16478  -0.00202 -0.03034 2   ARG T NH2 
938  N  N   . THR D 3  ? 0.43377 0.46203 0.18107 0.17165  -0.05114 -0.01318 3   THR T N   
939  C  CA  . THR D 3  ? 0.40095 0.48841 0.17214 0.12989  -0.07328 -0.03357 3   THR T CA  
940  C  C   . THR D 3  ? 0.35668 0.49794 0.20675 0.11353  -0.08748 -0.02223 3   THR T C   
941  O  O   . THR D 3  ? 0.33750 0.50490 0.24364 0.11620  -0.08293 -0.02794 3   THR T O   
942  C  CB  . THR D 3  ? 0.40873 0.49309 0.16328 0.10587  -0.07097 -0.03483 3   THR T CB  
943  O  OG1 . THR D 3  ? 0.41536 0.49925 0.18580 0.09285  -0.10528 -0.03498 3   THR T OG1 
944  C  CG2 . THR D 3  ? 0.39797 0.48378 0.15569 0.11041  -0.06027 -0.01970 3   THR T CG2 
945  N  N   . M3L D 4  ? 0.34637 0.51403 0.23347 0.06951  -0.08145 -0.02921 4   M3L T N   
946  C  CA  . M3L D 4  ? 0.31460 0.53274 0.26234 0.04453  -0.09825 -0.03874 4   M3L T CA  
947  C  CB  . M3L D 4  ? 0.28632 0.54126 0.26498 0.03617  -0.07011 -0.03528 4   M3L T CB  
948  C  CG  . M3L D 4  ? 0.28548 0.53720 0.21987 0.02249  -0.05157 -0.02970 4   M3L T CG  
949  C  CD  . M3L D 4  ? 0.28493 0.53665 0.22371 0.02560  -0.03010 -0.01276 4   M3L T CD  
950  C  CE  . M3L D 4  ? 0.29004 0.54028 0.21679 0.00745  -0.00899 -0.02453 4   M3L T CE  
951  N  NZ  . M3L D 4  ? 0.26797 0.54799 0.21162 -0.00779 -0.00367 -0.03276 4   M3L T NZ  
952  C  C   . M3L D 4  ? 0.31766 0.55236 0.28277 0.02563  -0.09096 -0.06538 4   M3L T C   
953  O  O   . M3L D 4  ? 0.32635 0.55964 0.27930 0.03059  -0.07516 -0.09410 4   M3L T O   
954  C  CM1 . M3L D 4  ? 0.29310 0.54954 0.22669 -0.00348 -0.01460 -0.04598 4   M3L T CM1 
955  C  CM2 . M3L D 4  ? 0.28636 0.54767 0.23055 -0.01789 -0.01025 -0.05031 4   M3L T CM2 
956  C  CM3 . M3L D 4  ? 0.25267 0.56020 0.18591 -0.01460 -0.02627 -0.03660 4   M3L T CM3 
957  N  N   . GLN D 5  ? 0.33226 0.56586 0.31447 -0.00511 -0.09414 -0.05580 5   GLN T N   
958  C  CA  . GLN D 5  ? 0.34038 0.57420 0.35061 -0.04094 -0.08420 -0.05968 5   GLN T CA  
959  C  C   . GLN D 5  ? 0.35287 0.59103 0.36138 -0.05324 -0.08875 -0.03787 5   GLN T C   
960  O  O   . GLN D 5  ? 0.33735 0.59671 0.34904 -0.05443 -0.09534 -0.02976 5   GLN T O   
961  C  CB  . GLN D 5  ? 0.34764 0.57200 0.39969 -0.05927 -0.04359 -0.06858 5   GLN T CB  
962  C  CG  . GLN D 5  ? 0.34909 0.57668 0.44319 -0.07414 -0.02994 -0.07653 5   GLN T CG  
963  C  CD  . GLN D 5  ? 0.34837 0.57169 0.46737 -0.07989 -0.00653 -0.08725 5   GLN T CD  
964  O  OE1 . GLN D 5  ? 0.35563 0.57179 0.47180 -0.08837 -0.00670 -0.10812 5   GLN T OE1 
965  N  NE2 . GLN D 5  ? 0.34311 0.57038 0.48389 -0.07820 0.00140  -0.07324 5   GLN T NE2 
966  N  N   . THR D 6  ? 0.38078 0.60101 0.38281 -0.05309 -0.06673 -0.03083 6   THR T N   
967  C  CA  . THR D 6  ? 0.41447 0.60606 0.40964 -0.04866 -0.06238 -0.03550 6   THR T CA  
968  C  C   . THR D 6  ? 0.45513 0.60435 0.42656 -0.04404 -0.07499 -0.00684 6   THR T C   
969  O  O   . THR D 6  ? 0.45226 0.61226 0.43699 -0.04726 -0.06855 -0.00301 6   THR T O   
970  C  CB  . THR D 6  ? 0.40451 0.60858 0.41497 -0.04523 -0.04958 -0.06670 6   THR T CB  
971  O  OG1 . THR D 6  ? 0.39413 0.60787 0.41010 -0.04506 -0.03743 -0.09680 6   THR T OG1 
972  C  CG2 . THR D 6  ? 0.40004 0.60813 0.41307 -0.04555 -0.04731 -0.07151 6   THR T CG2 
973  N  N   . ALA D 7  ? 0.49675 0.59075 0.43139 -0.03958 -0.08430 0.01734  7   ALA T N   
974  C  CA  . ALA D 7  ? 0.52526 0.57814 0.45296 -0.02944 -0.09523 0.04354  7   ALA T CA  
975  C  C   . ALA D 7  ? 0.53638 0.55925 0.48883 -0.02288 -0.10207 0.06806  7   ALA T C   
976  O  O   . ALA D 7  ? 0.53722 0.55868 0.48012 -0.02064 -0.10047 0.08130  7   ALA T O   
977  C  CB  . ALA D 7  ? 0.52874 0.58166 0.43844 -0.02318 -0.10017 0.05105  7   ALA T CB  
998  N  N   . SER D 10 ? 0.83393 0.83846 0.81741 0.05327  -0.19573 0.15914  10  SER T N   
999  C  CA  . SER D 10 ? 0.69141 0.69916 0.66410 0.05113  -0.18741 0.14905  10  SER T CA  
1000 C  C   . SER D 10 ? 0.60726 0.61622 0.59637 0.05307  -0.19132 0.14484  10  SER T C   
1001 O  O   . SER D 10 ? 0.60485 0.61661 0.60438 0.04964  -0.18621 0.14157  10  SER T O   
1002 C  CB  . SER D 10 ? 0.64733 0.65054 0.59508 0.04161  -0.16425 0.14088  10  SER T CB  
1003 O  OG  . SER D 10 ? 0.62530 0.62271 0.55946 0.03279  -0.14673 0.13835  10  SER T OG  
1015 ZN ZN  . ZN  E .  ? 0.59507 0.18441 0.18212 0.06439  0.00711  -0.00143 101 ZN  A ZN  
1016 ZN ZN  . ZN  F .  ? 0.22103 0.17796 0.21548 -0.00410 0.00772  -0.04717 102 ZN  A ZN  
1017 ZN ZN  . ZN  G .  ? 0.18693 0.22306 0.21621 -0.00530 -0.04448 0.00561  101 ZN  B ZN  
1018 ZN ZN  . ZN  H .  ? 0.18642 0.59714 0.18390 0.06720  -0.00199 0.00340  102 ZN  B ZN  
# 
