data_9G91
# 
_entry.id   9G91 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9G91         pdb_00009g91 10.2210/pdb9g91/pdb 
WWPDB D_1292139031 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G91 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sergei.strelkov@kuleuven.be 
_pdbx_contact_author.name_first         Strelkov 
_pdbx_contact_author.name_last          Sergei 
_pdbx_contact_author.name_mi            V. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7189-4652 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vantieghem, T.' 1 0000-0002-1452-9584 
'Osipov, E.M.'   2 0000-0003-3101-2867 
'Strelkov, S.V.' 3 0000-0001-7189-4652 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            280 
_citation.language                  ? 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vantieghem, T.'   1  ? 
primary 'Aslam, N.A.'      2  ? 
primary 'Osipov, E.M.'     3  ? 
primary 'Akele, M.'        4  ? 
primary 'Van Belle, S.'    5  ? 
primary 'Beelen, S.'       6  ? 
primary 'Drexler, M.'      7  ? 
primary 'Paulovcakova, T.' 8  ? 
primary 'Lux, V.'          9  ? 
primary 'Fearon, D.'       10 ? 
primary 'Douangamath, A.'  11 ? 
primary 'von Delft, F.'    12 ? 
primary 'Christ, F.'       13 ? 
primary 'Veverka, V.'      14 ? 
primary 'Verwilst, P.'     15 ? 
primary 'Van Aerschot, A.' 16 ? 
primary 'Debyser, Z.'      17 ? 
primary 'Strelkov, S.V.'   18 ? 
# 
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 'Hepatoma-derived growth factor-related protein 2'        10698.171 2   ? C64S ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                            62.068    1   ? ?    ? ? 
3 non-polymer syn '[3-[(5-bromanylpyridin-3-yl)methylamino]phenyl]methanol' 293.159   2   ? ?    ? ? 
4 non-polymer nat 'SULFATE ION'                                             96.063    7   ? ?    ? ? 
5 water       nat water                                                     18.015    246 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL                                            EDO   
3 '[3-[(5-bromanylpyridin-3-yl)methylamino]phenyl]methanol' A1II3 
4 'SULFATE ION'                                             SO4   
5 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  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER 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                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_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                   ? 
# 
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 
A1II3 non-polymer         . '[3-[(5-bromanylpyridin-3-yl)methylamino]phenyl]methanol' ?                 'C13 H13 Br N2 O' 293.159 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL                                            'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE                                                 ?                 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                           ?                 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                   ?                 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                 ?                 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                     ?                 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                ?                 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                   ?                 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                    ?                 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                ?                 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                             ?                 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                   ?                 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                    ?                 'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION'                                             ?                 'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE                                                 ?                 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                ?                 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                  ?                 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                    ?                 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  ?  ?   ?   B . n 
B 1 3  PRO 3  2  ?  ?   ?   B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 29 ALA ALA B . n 
B 1 31 ASP 31 30 30 ASP ASP B . n 
B 1 32 GLY 32 31 31 GLY GLY B . n 
B 1 33 ALA 33 32 32 ALA ALA B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1II3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1II3 
_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 
C 2 EDO   1   101 102 EDO   EDO A . 
D 3 A1II3 1   102 103 A1II3 C43 A . 
E 4 SO4   1   103 2   SO4   SO4 A . 
F 4 SO4   1   104 6   SO4   SO4 A . 
G 3 A1II3 1   101 101 A1II3 C43 B . 
H 4 SO4   1   102 1   SO4   SO4 B . 
I 4 SO4   1   103 3   SO4   SO4 B . 
J 4 SO4   1   104 4   SO4   SO4 B . 
K 4 SO4   1   105 5   SO4   SO4 B . 
L 4 SO4   1   106 7   SO4   SO4 B . 
M 5 HOH   1   201 482 HOH   HOH A . 
M 5 HOH   2   202 200 HOH   HOH A . 
M 5 HOH   3   203 193 HOH   HOH A . 
M 5 HOH   4   204 442 HOH   HOH A . 
M 5 HOH   5   205 366 HOH   HOH A . 
M 5 HOH   6   206 141 HOH   HOH A . 
M 5 HOH   7   207 74  HOH   HOH A . 
M 5 HOH   8   208 5   HOH   HOH A . 
M 5 HOH   9   209 51  HOH   HOH A . 
M 5 HOH   10  210 230 HOH   HOH A . 
M 5 HOH   11  211 73  HOH   HOH A . 
M 5 HOH   12  212 97  HOH   HOH A . 
M 5 HOH   13  213 99  HOH   HOH A . 
M 5 HOH   14  214 121 HOH   HOH A . 
M 5 HOH   15  215 54  HOH   HOH A . 
M 5 HOH   16  216 116 HOH   HOH A . 
M 5 HOH   17  217 30  HOH   HOH A . 
M 5 HOH   18  218 126 HOH   HOH A . 
M 5 HOH   19  219 1   HOH   HOH A . 
M 5 HOH   20  220 14  HOH   HOH A . 
M 5 HOH   21  221 59  HOH   HOH A . 
M 5 HOH   22  222 2   HOH   HOH A . 
M 5 HOH   23  223 547 HOH   HOH A . 
M 5 HOH   24  224 17  HOH   HOH A . 
M 5 HOH   25  225 55  HOH   HOH A . 
M 5 HOH   26  226 261 HOH   HOH A . 
M 5 HOH   27  227 64  HOH   HOH A . 
M 5 HOH   28  228 204 HOH   HOH A . 
M 5 HOH   29  229 23  HOH   HOH A . 
M 5 HOH   30  230 101 HOH   HOH A . 
M 5 HOH   31  231 66  HOH   HOH A . 
M 5 HOH   32  232 76  HOH   HOH A . 
M 5 HOH   33  233 26  HOH   HOH A . 
M 5 HOH   34  234 8   HOH   HOH A . 
M 5 HOH   35  235 43  HOH   HOH A . 
M 5 HOH   36  236 53  HOH   HOH A . 
M 5 HOH   37  237 49  HOH   HOH A . 
M 5 HOH   38  238 16  HOH   HOH A . 
M 5 HOH   39  239 77  HOH   HOH A . 
M 5 HOH   40  240 85  HOH   HOH A . 
M 5 HOH   41  241 46  HOH   HOH A . 
M 5 HOH   42  242 50  HOH   HOH A . 
M 5 HOH   43  243 75  HOH   HOH A . 
M 5 HOH   44  244 103 HOH   HOH A . 
M 5 HOH   45  245 27  HOH   HOH A . 
M 5 HOH   46  246 390 HOH   HOH A . 
M 5 HOH   47  247 110 HOH   HOH A . 
M 5 HOH   48  248 82  HOH   HOH A . 
M 5 HOH   49  249 93  HOH   HOH A . 
M 5 HOH   50  250 83  HOH   HOH A . 
M 5 HOH   51  251 162 HOH   HOH A . 
M 5 HOH   52  252 29  HOH   HOH A . 
M 5 HOH   53  253 84  HOH   HOH A . 
M 5 HOH   54  254 159 HOH   HOH A . 
M 5 HOH   55  255 56  HOH   HOH A . 
M 5 HOH   56  256 176 HOH   HOH A . 
M 5 HOH   57  257 171 HOH   HOH A . 
M 5 HOH   58  258 114 HOH   HOH A . 
M 5 HOH   59  259 238 HOH   HOH A . 
M 5 HOH   60  260 9   HOH   HOH A . 
M 5 HOH   61  261 86  HOH   HOH A . 
M 5 HOH   62  262 81  HOH   HOH A . 
M 5 HOH   63  263 34  HOH   HOH A . 
M 5 HOH   64  264 24  HOH   HOH A . 
M 5 HOH   65  265 22  HOH   HOH A . 
M 5 HOH   66  266 40  HOH   HOH A . 
M 5 HOH   67  267 118 HOH   HOH A . 
M 5 HOH   68  268 52  HOH   HOH A . 
M 5 HOH   69  269 19  HOH   HOH A . 
M 5 HOH   70  270 166 HOH   HOH A . 
M 5 HOH   71  271 216 HOH   HOH A . 
M 5 HOH   72  272 142 HOH   HOH A . 
M 5 HOH   73  273 94  HOH   HOH A . 
M 5 HOH   74  274 4   HOH   HOH A . 
M 5 HOH   75  275 11  HOH   HOH A . 
M 5 HOH   76  276 42  HOH   HOH A . 
M 5 HOH   77  277 212 HOH   HOH A . 
M 5 HOH   78  278 106 HOH   HOH A . 
M 5 HOH   79  279 68  HOH   HOH A . 
M 5 HOH   80  280 112 HOH   HOH A . 
M 5 HOH   81  281 260 HOH   HOH A . 
M 5 HOH   82  282 15  HOH   HOH A . 
M 5 HOH   83  283 79  HOH   HOH A . 
M 5 HOH   84  284 170 HOH   HOH A . 
M 5 HOH   85  285 555 HOH   HOH A . 
M 5 HOH   86  286 274 HOH   HOH A . 
M 5 HOH   87  287 129 HOH   HOH A . 
M 5 HOH   88  288 462 HOH   HOH A . 
M 5 HOH   89  289 556 HOH   HOH A . 
M 5 HOH   90  290 231 HOH   HOH A . 
M 5 HOH   91  291 113 HOH   HOH A . 
M 5 HOH   92  292 115 HOH   HOH A . 
M 5 HOH   93  293 250 HOH   HOH A . 
M 5 HOH   94  294 541 HOH   HOH A . 
M 5 HOH   95  295 484 HOH   HOH A . 
M 5 HOH   96  296 251 HOH   HOH A . 
M 5 HOH   97  297 161 HOH   HOH A . 
M 5 HOH   98  298 36  HOH   HOH A . 
M 5 HOH   99  299 558 HOH   HOH A . 
M 5 HOH   100 300 249 HOH   HOH A . 
M 5 HOH   101 301 268 HOH   HOH A . 
M 5 HOH   102 302 535 HOH   HOH A . 
M 5 HOH   103 303 95  HOH   HOH A . 
M 5 HOH   104 304 220 HOH   HOH A . 
M 5 HOH   105 305 37  HOH   HOH A . 
M 5 HOH   106 306 322 HOH   HOH A . 
M 5 HOH   107 307 188 HOH   HOH A . 
M 5 HOH   108 308 244 HOH   HOH A . 
M 5 HOH   109 309 538 HOH   HOH A . 
M 5 HOH   110 310 534 HOH   HOH A . 
M 5 HOH   111 311 518 HOH   HOH A . 
M 5 HOH   112 312 536 HOH   HOH A . 
M 5 HOH   113 313 417 HOH   HOH A . 
M 5 HOH   114 314 120 HOH   HOH A . 
M 5 HOH   115 315 222 HOH   HOH A . 
M 5 HOH   116 316 67  HOH   HOH A . 
M 5 HOH   117 317 147 HOH   HOH A . 
M 5 HOH   118 318 465 HOH   HOH A . 
M 5 HOH   119 319 108 HOH   HOH A . 
M 5 HOH   120 320 306 HOH   HOH A . 
M 5 HOH   121 321 179 HOH   HOH A . 
M 5 HOH   122 322 184 HOH   HOH A . 
M 5 HOH   123 323 242 HOH   HOH A . 
M 5 HOH   124 324 90  HOH   HOH A . 
M 5 HOH   125 325 164 HOH   HOH A . 
M 5 HOH   126 326 136 HOH   HOH A . 
M 5 HOH   127 327 553 HOH   HOH A . 
M 5 HOH   128 328 252 HOH   HOH A . 
N 5 HOH   1   201 510 HOH   HOH B . 
N 5 HOH   2   202 33  HOH   HOH B . 
N 5 HOH   3   203 149 HOH   HOH B . 
N 5 HOH   4   204 28  HOH   HOH B . 
N 5 HOH   5   205 228 HOH   HOH B . 
N 5 HOH   6   206 3   HOH   HOH B . 
N 5 HOH   7   207 154 HOH   HOH B . 
N 5 HOH   8   208 140 HOH   HOH B . 
N 5 HOH   9   209 100 HOH   HOH B . 
N 5 HOH   10  210 158 HOH   HOH B . 
N 5 HOH   11  211 47  HOH   HOH B . 
N 5 HOH   12  212 21  HOH   HOH B . 
N 5 HOH   13  213 96  HOH   HOH B . 
N 5 HOH   14  214 102 HOH   HOH B . 
N 5 HOH   15  215 31  HOH   HOH B . 
N 5 HOH   16  216 548 HOH   HOH B . 
N 5 HOH   17  217 111 HOH   HOH B . 
N 5 HOH   18  218 57  HOH   HOH B . 
N 5 HOH   19  219 6   HOH   HOH B . 
N 5 HOH   20  220 60  HOH   HOH B . 
N 5 HOH   21  221 557 HOH   HOH B . 
N 5 HOH   22  222 32  HOH   HOH B . 
N 5 HOH   23  223 552 HOH   HOH B . 
N 5 HOH   24  224 13  HOH   HOH B . 
N 5 HOH   25  225 12  HOH   HOH B . 
N 5 HOH   26  226 123 HOH   HOH B . 
N 5 HOH   27  227 45  HOH   HOH B . 
N 5 HOH   28  228 72  HOH   HOH B . 
N 5 HOH   29  229 78  HOH   HOH B . 
N 5 HOH   30  230 199 HOH   HOH B . 
N 5 HOH   31  231 128 HOH   HOH B . 
N 5 HOH   32  232 105 HOH   HOH B . 
N 5 HOH   33  233 48  HOH   HOH B . 
N 5 HOH   34  234 470 HOH   HOH B . 
N 5 HOH   35  235 229 HOH   HOH B . 
N 5 HOH   36  236 10  HOH   HOH B . 
N 5 HOH   37  237 247 HOH   HOH B . 
N 5 HOH   38  238 133 HOH   HOH B . 
N 5 HOH   39  239 234 HOH   HOH B . 
N 5 HOH   40  240 144 HOH   HOH B . 
N 5 HOH   41  241 243 HOH   HOH B . 
N 5 HOH   42  242 540 HOH   HOH B . 
N 5 HOH   43  243 65  HOH   HOH B . 
N 5 HOH   44  244 138 HOH   HOH B . 
N 5 HOH   45  245 18  HOH   HOH B . 
N 5 HOH   46  246 139 HOH   HOH B . 
N 5 HOH   47  247 148 HOH   HOH B . 
N 5 HOH   48  248 91  HOH   HOH B . 
N 5 HOH   49  249 235 HOH   HOH B . 
N 5 HOH   50  250 165 HOH   HOH B . 
N 5 HOH   51  251 25  HOH   HOH B . 
N 5 HOH   52  252 545 HOH   HOH B . 
N 5 HOH   53  253 62  HOH   HOH B . 
N 5 HOH   54  254 71  HOH   HOH B . 
N 5 HOH   55  255 87  HOH   HOH B . 
N 5 HOH   56  256 209 HOH   HOH B . 
N 5 HOH   57  257 107 HOH   HOH B . 
N 5 HOH   58  258 20  HOH   HOH B . 
N 5 HOH   59  259 44  HOH   HOH B . 
N 5 HOH   60  260 70  HOH   HOH B . 
N 5 HOH   61  261 203 HOH   HOH B . 
N 5 HOH   62  262 155 HOH   HOH B . 
N 5 HOH   63  263 198 HOH   HOH B . 
N 5 HOH   64  264 63  HOH   HOH B . 
N 5 HOH   65  265 58  HOH   HOH B . 
N 5 HOH   66  266 544 HOH   HOH B . 
N 5 HOH   67  267 80  HOH   HOH B . 
N 5 HOH   68  268 88  HOH   HOH B . 
N 5 HOH   69  269 124 HOH   HOH B . 
N 5 HOH   70  270 41  HOH   HOH B . 
N 5 HOH   71  271 332 HOH   HOH B . 
N 5 HOH   72  272 89  HOH   HOH B . 
N 5 HOH   73  273 543 HOH   HOH B . 
N 5 HOH   74  274 407 HOH   HOH B . 
N 5 HOH   75  275 181 HOH   HOH B . 
N 5 HOH   76  276 539 HOH   HOH B . 
N 5 HOH   77  277 456 HOH   HOH B . 
N 5 HOH   78  278 197 HOH   HOH B . 
N 5 HOH   79  279 117 HOH   HOH B . 
N 5 HOH   80  280 187 HOH   HOH B . 
N 5 HOH   81  281 163 HOH   HOH B . 
N 5 HOH   82  282 477 HOH   HOH B . 
N 5 HOH   83  283 554 HOH   HOH B . 
N 5 HOH   84  284 466 HOH   HOH B . 
N 5 HOH   85  285 218 HOH   HOH B . 
N 5 HOH   86  286 130 HOH   HOH B . 
N 5 HOH   87  287 7   HOH   HOH B . 
N 5 HOH   88  288 549 HOH   HOH B . 
N 5 HOH   89  289 551 HOH   HOH B . 
N 5 HOH   90  290 546 HOH   HOH B . 
N 5 HOH   91  291 98  HOH   HOH B . 
N 5 HOH   92  292 191 HOH   HOH B . 
N 5 HOH   93  293 256 HOH   HOH B . 
N 5 HOH   94  294 39  HOH   HOH B . 
N 5 HOH   95  295 424 HOH   HOH B . 
N 5 HOH   96  296 293 HOH   HOH B . 
N 5 HOH   97  297 131 HOH   HOH B . 
N 5 HOH   98  298 537 HOH   HOH B . 
N 5 HOH   99  299 236 HOH   HOH B . 
N 5 HOH   100 300 119 HOH   HOH B . 
N 5 HOH   101 301 372 HOH   HOH B . 
N 5 HOH   102 302 160 HOH   HOH B . 
N 5 HOH   103 303 190 HOH   HOH B . 
N 5 HOH   104 304 35  HOH   HOH B . 
N 5 HOH   105 305 550 HOH   HOH B . 
N 5 HOH   106 306 219 HOH   HOH B . 
N 5 HOH   107 307 480 HOH   HOH B . 
N 5 HOH   108 308 340 HOH   HOH B . 
N 5 HOH   109 309 185 HOH   HOH B . 
N 5 HOH   110 310 286 HOH   HOH B . 
N 5 HOH   111 311 362 HOH   HOH B . 
N 5 HOH   112 312 152 HOH   HOH B . 
N 5 HOH   113 313 122 HOH   HOH B . 
N 5 HOH   114 314 174 HOH   HOH B . 
N 5 HOH   115 315 233 HOH   HOH B . 
N 5 HOH   116 316 514 HOH   HOH B . 
N 5 HOH   117 317 542 HOH   HOH B . 
N 5 HOH   118 318 312 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 1  ? CG  ? A MET 2  CG  
2  1 Y 1 A MET 1  ? SD  ? A MET 2  SD  
3  1 Y 1 A MET 1  ? CE  ? A MET 2  CE  
4  1 Y 1 A LYS 16 ? CD  ? A LYS 17 CD  
5  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
6  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
7  1 Y 1 A LYS 34 ? CE  ? A LYS 35 CE  
8  1 Y 1 A LYS 34 ? NZ  ? A LYS 35 NZ  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 B ASP 30 ? CG  ? B ASP 31 CG  
12 1 Y 1 B ASP 30 ? OD1 ? B ASP 31 OD1 
13 1 Y 1 B ASP 30 ? OD2 ? B ASP 31 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .                    2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .                    4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.21.1_5286: ???)' 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.84 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G91 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.056 
_cell.length_a_esd                 ? 
_cell.length_b                     41.663 
_cell.length_b_esd                 ? 
_cell.length_c                     72.179 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9G91 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G91 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.67 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.00 
_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    
;28% PEG MME 2000
0.15 M ammonium sulfate
0.1 M sodium acetate pH 4.6
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-03 
_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   0.976253 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976253 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G91 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               70.37 
_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                                     21823 
_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                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.91 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.145 
_reflns.pdbx_Rpim_I_all                                0.067 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       100197 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.129 
_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                                    1.78 
_reflns_shell.d_res_low                                     1.88 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           14148 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3148 
_reflns_shell.percent_possible_obs                          100.0 
_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                               4.5 
_reflns_shell.pdbx_chi_squared                              0.78 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.3 
_reflns_shell.pdbx_Rrim_I_all                               1.115 
_reflns_shell.pdbx_Rpim_I_all                               0.520 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.611 
_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                                  0.981 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G91 
_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                            1.78 
_refine.ls_d_res_low                             36.55 
_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                     21787 
_refine.ls_number_reflns_R_free                  1021 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 4.69 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1746 
_refine.ls_R_factor_R_free                       0.2056 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1730 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.53 
_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                            0.21 
_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                       1.78 
_refine_hist.d_res_low                        36.55 
_refine_hist.number_atoms_solvent             246 
_refine_hist.number_atoms_total               1803 
_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        1484 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         73 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 1633 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.593  ? 2221 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.269 ? 614  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 196  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 299  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.78 1.88  . . 145 2918 100.00 . . . . 0.2696 . . . . . . . . . . . 0.3317 
'X-RAY DIFFRACTION' 1.88 1.99  . . 153 2953 100.00 . . . . 0.2184 . . . . . . . . . . . 0.2219 
'X-RAY DIFFRACTION' 1.99 2.15  . . 127 2950 100.00 . . . . 0.1906 . . . . . . . . . . . 0.2387 
'X-RAY DIFFRACTION' 2.15 2.36  . . 144 2962 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.36 2.70  . . 144 2961 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.71 3.41  . . 160 2971 100.00 . . . . 0.1614 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 3.41 36.55 . . 148 3051 99.00  . . . . 0.1437 . . . . . . . . . . . 0.1670 
# 
_struct.entry_id                     9G91 
_struct.title                        'Crystal structure of HRP-2 PWWP domain in complex with compound 43' 
_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        9G91 
_struct_keywords.text            'Inhibitor, GENE REGULATION' 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
# 
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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
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 9G91 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 9G91 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
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 9G91 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 9G91 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 9G91 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 9G91 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,M     
2 1 B,G,H,I,J,K,L,N 
# 
_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 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 ASP B 28 ? GLY B 32 ? ASP B 27 GLY B 31 5 ? 5  
HELX_P HELX_P5 AA5 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P6 AA6 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P7 AA7 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 50 ? LEU A 54 ? GLU A 49 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
# 
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 ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
# 
_pdbx_entry_details.entry_id                   9G91 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD1 B ASP 62  ? ? O B HOH 201 ? ? 2.10 
2  1 O   A HOH 274 ? ? O B HOH 287 ? ? 2.12 
3  1 O   B HOH 208 ? ? O B HOH 299 ? ? 2.13 
4  1 O   B HOH 278 ? ? O B HOH 285 ? ? 2.15 
5  1 O   A HOH 284 ? ? O B HOH 265 ? ? 2.17 
6  1 O   A HOH 242 ? ? O B HOH 287 ? ? 2.17 
7  1 O   B HOH 306 ? ? O B HOH 315 ? ? 2.18 
8  1 O   A HOH 245 ? ? O A HOH 320 ? ? 2.18 
9  1 O   A HOH 304 ? ? O A HOH 323 ? ? 2.18 
10 1 O   B HOH 285 ? ? O B HOH 310 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     226 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     281 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_455 
_pdbx_validate_symm_contact.dist              2.15 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     87 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -153.51 
_pdbx_validate_torsion.psi             69.76 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 317 ? M HOH . 
2 1 A HOH 326 ? M HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 327 ? 6.01 . 
2 1 O ? A HOH 328 ? 6.81 . 
# 
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 GLY 0 ? A GLY 1 
2 1 Y 1 B GLY 0 ? B GLY 1 
3 1 Y 1 B MET 1 ? B MET 2 
4 1 Y 1 B PRO 2 ? B PRO 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1II3 N1   N  Y N 1   
A1II3 C2   C  Y N 2   
A1II3 C4   C  N N 3   
A1II3 C5   C  Y N 4   
A1II3 C6   C  Y N 5   
A1II3 C7   C  Y N 6   
A1II3 C8   C  Y N 7   
A1II3 C    C  N N 8   
A1II3 C1   C  Y N 9   
A1II3 C10  C  Y N 10  
A1II3 C11  C  Y N 11  
A1II3 C12  C  Y N 12  
A1II3 C3   C  Y N 13  
A1II3 C9   C  Y N 14  
A1II3 N    N  N N 15  
A1II3 O    O  N N 16  
A1II3 BR   BR N N 17  
A1II3 H1   H  N N 18  
A1II3 H2   H  N N 19  
A1II3 H3   H  N N 20  
A1II3 H4   H  N N 21  
A1II3 H5   H  N N 22  
A1II3 H6   H  N N 23  
A1II3 H7   H  N N 24  
A1II3 H8   H  N N 25  
A1II3 H9   H  N N 26  
A1II3 H10  H  N N 27  
A1II3 H11  H  N N 28  
A1II3 H12  H  N N 29  
A1II3 H13  H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CYS   N    N  N N 104 
CYS   CA   C  N R 105 
CYS   C    C  N N 106 
CYS   O    O  N N 107 
CYS   CB   C  N N 108 
CYS   SG   S  N N 109 
CYS   OXT  O  N N 110 
CYS   H    H  N N 111 
CYS   H2   H  N N 112 
CYS   HA   H  N N 113 
CYS   HB2  H  N N 114 
CYS   HB3  H  N N 115 
CYS   HG   H  N N 116 
CYS   HXT  H  N N 117 
EDO   C1   C  N N 118 
EDO   O1   O  N N 119 
EDO   C2   C  N N 120 
EDO   O2   O  N N 121 
EDO   H11  H  N N 122 
EDO   H12  H  N N 123 
EDO   HO1  H  N N 124 
EDO   H21  H  N N 125 
EDO   H22  H  N N 126 
EDO   HO2  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
HIS   N    N  N N 177 
HIS   CA   C  N S 178 
HIS   C    C  N N 179 
HIS   O    O  N N 180 
HIS   CB   C  N N 181 
HIS   CG   C  Y N 182 
HIS   ND1  N  Y N 183 
HIS   CD2  C  Y N 184 
HIS   CE1  C  Y N 185 
HIS   NE2  N  Y N 186 
HIS   OXT  O  N N 187 
HIS   H    H  N N 188 
HIS   H2   H  N N 189 
HIS   HA   H  N N 190 
HIS   HB2  H  N N 191 
HIS   HB3  H  N N 192 
HIS   HD1  H  N N 193 
HIS   HD2  H  N N 194 
HIS   HE1  H  N N 195 
HIS   HE2  H  N N 196 
HIS   HXT  H  N N 197 
HOH   O    O  N N 198 
HOH   H1   H  N N 199 
HOH   H2   H  N N 200 
ILE   N    N  N N 201 
ILE   CA   C  N S 202 
ILE   C    C  N N 203 
ILE   O    O  N N 204 
ILE   CB   C  N S 205 
ILE   CG1  C  N N 206 
ILE   CG2  C  N N 207 
ILE   CD1  C  N N 208 
ILE   OXT  O  N N 209 
ILE   H    H  N N 210 
ILE   H2   H  N N 211 
ILE   HA   H  N N 212 
ILE   HB   H  N N 213 
ILE   HG12 H  N N 214 
ILE   HG13 H  N N 215 
ILE   HG21 H  N N 216 
ILE   HG22 H  N N 217 
ILE   HG23 H  N N 218 
ILE   HD11 H  N N 219 
ILE   HD12 H  N N 220 
ILE   HD13 H  N N 221 
ILE   HXT  H  N N 222 
LEU   N    N  N N 223 
LEU   CA   C  N S 224 
LEU   C    C  N N 225 
LEU   O    O  N N 226 
LEU   CB   C  N N 227 
LEU   CG   C  N N 228 
LEU   CD1  C  N N 229 
LEU   CD2  C  N N 230 
LEU   OXT  O  N N 231 
LEU   H    H  N N 232 
LEU   H2   H  N N 233 
LEU   HA   H  N N 234 
LEU   HB2  H  N N 235 
LEU   HB3  H  N N 236 
LEU   HG   H  N N 237 
LEU   HD11 H  N N 238 
LEU   HD12 H  N N 239 
LEU   HD13 H  N N 240 
LEU   HD21 H  N N 241 
LEU   HD22 H  N N 242 
LEU   HD23 H  N N 243 
LEU   HXT  H  N N 244 
LYS   N    N  N N 245 
LYS   CA   C  N S 246 
LYS   C    C  N N 247 
LYS   O    O  N N 248 
LYS   CB   C  N N 249 
LYS   CG   C  N N 250 
LYS   CD   C  N N 251 
LYS   CE   C  N N 252 
LYS   NZ   N  N N 253 
LYS   OXT  O  N N 254 
LYS   H    H  N N 255 
LYS   H2   H  N N 256 
LYS   HA   H  N N 257 
LYS   HB2  H  N N 258 
LYS   HB3  H  N N 259 
LYS   HG2  H  N N 260 
LYS   HG3  H  N N 261 
LYS   HD2  H  N N 262 
LYS   HD3  H  N N 263 
LYS   HE2  H  N N 264 
LYS   HE3  H  N N 265 
LYS   HZ1  H  N N 266 
LYS   HZ2  H  N N 267 
LYS   HZ3  H  N N 268 
LYS   HXT  H  N N 269 
MET   N    N  N N 270 
MET   CA   C  N S 271 
MET   C    C  N N 272 
MET   O    O  N N 273 
MET   CB   C  N N 274 
MET   CG   C  N N 275 
MET   SD   S  N N 276 
MET   CE   C  N N 277 
MET   OXT  O  N N 278 
MET   H    H  N N 279 
MET   H2   H  N N 280 
MET   HA   H  N N 281 
MET   HB2  H  N N 282 
MET   HB3  H  N N 283 
MET   HG2  H  N N 284 
MET   HG3  H  N N 285 
MET   HE1  H  N N 286 
MET   HE2  H  N N 287 
MET   HE3  H  N N 288 
MET   HXT  H  N N 289 
PHE   N    N  N N 290 
PHE   CA   C  N S 291 
PHE   C    C  N N 292 
PHE   O    O  N N 293 
PHE   CB   C  N N 294 
PHE   CG   C  Y N 295 
PHE   CD1  C  Y N 296 
PHE   CD2  C  Y N 297 
PHE   CE1  C  Y N 298 
PHE   CE2  C  Y N 299 
PHE   CZ   C  Y N 300 
PHE   OXT  O  N N 301 
PHE   H    H  N N 302 
PHE   H2   H  N N 303 
PHE   HA   H  N N 304 
PHE   HB2  H  N N 305 
PHE   HB3  H  N N 306 
PHE   HD1  H  N N 307 
PHE   HD2  H  N N 308 
PHE   HE1  H  N N 309 
PHE   HE2  H  N N 310 
PHE   HZ   H  N N 311 
PHE   HXT  H  N N 312 
PRO   N    N  N N 313 
PRO   CA   C  N S 314 
PRO   C    C  N N 315 
PRO   O    O  N N 316 
PRO   CB   C  N N 317 
PRO   CG   C  N N 318 
PRO   CD   C  N N 319 
PRO   OXT  O  N N 320 
PRO   H    H  N N 321 
PRO   HA   H  N N 322 
PRO   HB2  H  N N 323 
PRO   HB3  H  N N 324 
PRO   HG2  H  N N 325 
PRO   HG3  H  N N 326 
PRO   HD2  H  N N 327 
PRO   HD3  H  N N 328 
PRO   HXT  H  N N 329 
SER   N    N  N N 330 
SER   CA   C  N S 331 
SER   C    C  N N 332 
SER   O    O  N N 333 
SER   CB   C  N N 334 
SER   OG   O  N N 335 
SER   OXT  O  N N 336 
SER   H    H  N N 337 
SER   H2   H  N N 338 
SER   HA   H  N N 339 
SER   HB2  H  N N 340 
SER   HB3  H  N N 341 
SER   HG   H  N N 342 
SER   HXT  H  N N 343 
SO4   S    S  N N 344 
SO4   O1   O  N N 345 
SO4   O2   O  N N 346 
SO4   O3   O  N N 347 
SO4   O4   O  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
# 
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 
A1II3 C12 C11  doub Y N 1   
A1II3 C12 C1   sing Y N 2   
A1II3 C   O    sing N N 3   
A1II3 C   C1   sing N N 4   
A1II3 C11 C10  sing Y N 5   
A1II3 C1  C2   doub Y N 6   
A1II3 C10 C3   doub Y N 7   
A1II3 C2  C3   sing Y N 8   
A1II3 BR  C8   sing N N 9   
A1II3 C3  N    sing N N 10  
A1II3 C7  C8   doub Y N 11  
A1II3 C7  N1   sing Y N 12  
A1II3 C8  C9   sing Y N 13  
A1II3 N1  C6   doub Y N 14  
A1II3 C9  C5   doub Y N 15  
A1II3 C6  C5   sing Y N 16  
A1II3 N   C4   sing N N 17  
A1II3 C5  C4   sing N N 18  
A1II3 C2  H1   sing N N 19  
A1II3 C4  H2   sing N N 20  
A1II3 C4  H3   sing N N 21  
A1II3 C6  H4   sing N N 22  
A1II3 C7  H5   sing N N 23  
A1II3 C   H6   sing N N 24  
A1II3 C   H7   sing N N 25  
A1II3 C10 H8   sing N N 26  
A1II3 C11 H9   sing N N 27  
A1II3 C12 H10  sing N N 28  
A1II3 C9  H11  sing N N 29  
A1II3 N   H12  sing N N 30  
A1II3 O   H13  sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
EDO   C1  O1   sing N N 114 
EDO   C1  C2   sing N N 115 
EDO   C1  H11  sing N N 116 
EDO   C1  H12  sing N N 117 
EDO   O1  HO1  sing N N 118 
EDO   C2  O2   sing N N 119 
EDO   C2  H21  sing N N 120 
EDO   C2  H22  sing N N 121 
EDO   O2  HO2  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
SO4   S   O1   doub N N 330 
SO4   S   O2   doub N N 331 
SO4   S   O3   sing N N 332 
SO4   S   O4   sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3QBY 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G91 
_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]   0.012811 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002920 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024002 
_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]   0.014210 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
BR 
C  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET   A 1 2  ? -28.686 -12.581 -10.701 1.00 57.32  ? 1   MET   A N   1 
ATOM   2    C  CA  . MET   A 1 2  ? -27.686 -13.631 -10.870 1.00 41.82  ? 1   MET   A CA  1 
ATOM   3    C  C   . MET   A 1 2  ? -26.341 -13.200 -10.299 1.00 31.86  ? 1   MET   A C   1 
ATOM   4    O  O   . MET   A 1 2  ? -25.891 -12.077 -10.534 1.00 35.51  ? 1   MET   A O   1 
ATOM   5    C  CB  . MET   A 1 2  ? -27.535 -14.002 -12.347 1.00 51.67  ? 1   MET   A CB  1 
ATOM   6    N  N   . PRO   A 1 3  ? -25.701 -14.091 -9.548  1.00 27.31  ? 2   PRO   A N   1 
ATOM   7    C  CA  . PRO   A 1 3  ? -24.405 -13.760 -8.952  1.00 17.88  ? 2   PRO   A CA  1 
ATOM   8    C  C   . PRO   A 1 3  ? -23.315 -13.695 -10.006 1.00 20.59  ? 2   PRO   A C   1 
ATOM   9    O  O   . PRO   A 1 3  ? -23.433 -14.239 -11.105 1.00 21.87  ? 2   PRO   A O   1 
ATOM   10   C  CB  . PRO   A 1 3  ? -24.149 -14.917 -7.978  1.00 25.35  ? 2   PRO   A CB  1 
ATOM   11   C  CG  . PRO   A 1 3  ? -25.458 -15.646 -7.872  1.00 25.92  ? 2   PRO   A CG  1 
ATOM   12   C  CD  . PRO   A 1 3  ? -26.151 -15.437 -9.168  1.00 23.78  ? 2   PRO   A CD  1 
ATOM   13   N  N   . HIS   A 1 4  ? -22.224 -13.037 -9.636  1.00 18.52  ? 3   HIS   A N   1 
ATOM   14   C  CA  . HIS   A 1 4  ? -21.039 -12.950 -10.472 1.00 16.06  ? 3   HIS   A CA  1 
ATOM   15   C  C   . HIS   A 1 4  ? -19.837 -13.344 -9.631  1.00 17.17  ? 3   HIS   A C   1 
ATOM   16   O  O   . HIS   A 1 4  ? -19.937 -13.523 -8.414  1.00 17.50  ? 3   HIS   A O   1 
ATOM   17   C  CB  . HIS   A 1 4  ? -20.857 -11.532 -11.048 1.00 18.76  ? 3   HIS   A CB  1 
ATOM   18   C  CG  . HIS   A 1 4  ? -22.073 -11.008 -11.747 1.00 23.98  ? 3   HIS   A CG  1 
ATOM   19   N  ND1 . HIS   A 1 4  ? -22.371 -11.320 -13.057 1.00 27.16  ? 3   HIS   A ND1 1 
ATOM   20   C  CD2 . HIS   A 1 4  ? -23.074 -10.203 -11.315 1.00 35.45  ? 3   HIS   A CD2 1 
ATOM   21   C  CE1 . HIS   A 1 4  ? -23.502 -10.729 -13.402 1.00 35.04  ? 3   HIS   A CE1 1 
ATOM   22   N  NE2 . HIS   A 1 4  ? -23.949 -10.046 -12.363 1.00 33.08  ? 3   HIS   A NE2 1 
ATOM   23   N  N   . ALA   A 1 5  ? -18.693 -13.497 -10.291 1.00 14.23  ? 4   ALA   A N   1 
ATOM   24   C  CA  . ALA   A 1 5  ? -17.451 -13.644 -9.552  1.00 14.87  ? 4   ALA   A CA  1 
ATOM   25   C  C   . ALA   A 1 5  ? -17.234 -12.426 -8.661  1.00 17.89  ? 4   ALA   A C   1 
ATOM   26   O  O   . ALA   A 1 5  ? -17.695 -11.321 -8.958  1.00 14.66  ? 4   ALA   A O   1 
ATOM   27   C  CB  . ALA   A 1 5  ? -16.275 -13.816 -10.509 1.00 21.06  ? 4   ALA   A CB  1 
ATOM   28   N  N   . PHE   A 1 6  ? -16.534 -12.635 -7.553  1.00 14.98  ? 5   PHE   A N   1 
ATOM   29   C  CA  . PHE   A 1 6  ? -16.310 -11.543 -6.621  1.00 12.01  ? 5   PHE   A CA  1 
ATOM   30   C  C   . PHE   A 1 6  ? -15.466 -10.456 -7.269  1.00 17.39  ? 5   PHE   A C   1 
ATOM   31   O  O   . PHE   A 1 6  ? -14.558 -10.733 -8.056  1.00 20.04  ? 5   PHE   A O   1 
ATOM   32   C  CB  . PHE   A 1 6  ? -15.639 -12.050 -5.351  1.00 17.20  ? 5   PHE   A CB  1 
ATOM   33   C  CG  . PHE   A 1 6  ? -16.571 -12.795 -4.449  1.00 12.87  ? 5   PHE   A CG  1 
ATOM   34   C  CD1 . PHE   A 1 6  ? -17.550 -12.117 -3.743  1.00 13.08  ? 5   PHE   A CD1 1 
ATOM   35   C  CD2 . PHE   A 1 6  ? -16.488 -14.178 -4.323  1.00 20.61  ? 5   PHE   A CD2 1 
ATOM   36   C  CE1 . PHE   A 1 6  ? -18.423 -12.794 -2.914  1.00 15.06  ? 5   PHE   A CE1 1 
ATOM   37   C  CE2 . PHE   A 1 6  ? -17.357 -14.861 -3.495  1.00 18.16  ? 5   PHE   A CE2 1 
ATOM   38   C  CZ  . PHE   A 1 6  ? -18.325 -14.174 -2.789  1.00 16.83  ? 5   PHE   A CZ  1 
ATOM   39   N  N   . LYS   A 1 7  ? -15.781 -9.216  -6.939  1.00 14.65  ? 6   LYS   A N   1 
ATOM   40   C  CA  . LYS   A 1 7  ? -15.082 -8.053  -7.457  1.00 14.32  ? 6   LYS   A CA  1 
ATOM   41   C  C   . LYS   A 1 7  ? -14.828 -7.091  -6.308  1.00 15.02  ? 6   LYS   A C   1 
ATOM   42   O  O   . LYS   A 1 7  ? -15.498 -7.165  -5.271  1.00 14.17  ? 6   LYS   A O   1 
ATOM   43   C  CB  . LYS   A 1 7  ? -15.896 -7.380  -8.572  1.00 24.11  ? 6   LYS   A CB  1 
ATOM   44   C  CG  . LYS   A 1 7  ? -17.249 -6.860  -8.144  1.00 28.14  ? 6   LYS   A CG  1 
ATOM   45   C  CD  . LYS   A 1 7  ? -17.960 -6.183  -9.312  1.00 50.04  ? 6   LYS   A CD  1 
ATOM   46   C  CE  . LYS   A 1 7  ? -19.146 -5.349  -8.842  1.00 36.17  ? 6   LYS   A CE  1 
ATOM   47   N  NZ  . LYS   A 1 7  ? -20.041 -6.135  -7.938  1.00 48.24  ? 6   LYS   A NZ  1 
ATOM   48   N  N   . PRO   A 1 8  ? -13.842 -6.205  -6.443  1.00 18.78  ? 7   PRO   A N   1 
ATOM   49   C  CA  . PRO   A 1 8  ? -13.577 -5.219  -5.386  1.00 15.83  ? 7   PRO   A CA  1 
ATOM   50   C  C   . PRO   A 1 8  ? -14.832 -4.449  -5.003  1.00 16.17  ? 7   PRO   A C   1 
ATOM   51   O  O   . PRO   A 1 8  ? -15.593 -3.998  -5.860  1.00 16.12  ? 7   PRO   A O   1 
ATOM   52   C  CB  . PRO   A 1 8  ? -12.523 -4.306  -6.019  1.00 20.08  ? 7   PRO   A CB  1 
ATOM   53   C  CG  . PRO   A 1 8  ? -11.810 -5.198  -6.984  1.00 17.04  ? 7   PRO   A CG  1 
ATOM   54   C  CD  . PRO   A 1 8  ? -12.846 -6.133  -7.530  1.00 17.55  ? 7   PRO   A CD  1 
ATOM   55   N  N   . GLY   A 1 9  ? -15.052 -4.314  -3.697  1.00 14.35  ? 8   GLY   A N   1 
ATOM   56   C  CA  . GLY   A 1 9  ? -16.230 -3.667  -3.168  1.00 15.70  ? 8   GLY   A CA  1 
ATOM   57   C  C   . GLY   A 1 9  ? -17.311 -4.616  -2.684  1.00 18.40  ? 8   GLY   A C   1 
ATOM   58   O  O   . GLY   A 1 9  ? -18.153 -4.209  -1.874  1.00 15.85  ? 8   GLY   A O   1 
ATOM   59   N  N   . ASP   A 1 10 ? -17.316 -5.861  -3.158  1.00 13.75  ? 9   ASP   A N   1 
ATOM   60   C  CA  . ASP   A 1 10 ? -18.324 -6.816  -2.712  1.00 11.03  ? 9   ASP   A CA  1 
ATOM   61   C  C   . ASP   A 1 10 ? -18.203 -7.049  -1.214  1.00 8.61   ? 9   ASP   A C   1 
ATOM   62   O  O   . ASP   A 1 10 ? -17.096 -7.156  -0.677  1.00 12.46  ? 9   ASP   A O   1 
ATOM   63   C  CB  . ASP   A 1 10 ? -18.171 -8.146  -3.453  1.00 13.51  ? 9   ASP   A CB  1 
ATOM   64   C  CG  . ASP   A 1 10 ? -18.680 -8.081  -4.880  1.00 22.18  ? 9   ASP   A CG  1 
ATOM   65   O  OD1 . ASP   A 1 10 ? -19.345 -7.086  -5.240  1.00 18.58  ? 9   ASP   A OD1 1 
ATOM   66   O  OD2 . ASP   A 1 10 ? -18.410 -9.031  -5.639  1.00 17.43  ? 9   ASP   A OD2 1 
ATOM   67   N  N   . LEU   A 1 11 ? -19.351 -7.150  -0.542  1.00 10.82  ? 10  LEU   A N   1 
ATOM   68   C  CA  . LEU   A 1 11 ? -19.407 -7.312  0.902   1.00 16.92  ? 10  LEU   A CA  1 
ATOM   69   C  C   . LEU   A 1 11 ? -19.774 -8.747  1.246   1.00 14.38  ? 10  LEU   A C   1 
ATOM   70   O  O   . LEU   A 1 11 ? -20.674 -9.336  0.628   1.00 10.54  ? 10  LEU   A O   1 
ATOM   71   C  CB  . LEU   A 1 11 ? -20.423 -6.349  1.522   1.00 11.35  ? 10  LEU   A CB  1 
ATOM   72   C  CG  . LEU   A 1 11 ? -20.210 -4.881  1.136   1.00 6.83   ? 10  LEU   A CG  1 
ATOM   73   C  CD1 . LEU   A 1 11 ? -21.239 -3.996  1.839   1.00 10.34  ? 10  LEU   A CD1 1 
ATOM   74   C  CD2 . LEU   A 1 11 ? -18.781 -4.446  1.466   1.00 9.54   ? 10  LEU   A CD2 1 
ATOM   75   N  N   . VAL   A 1 12 ? -19.071 -9.308  2.233   1.00 9.90   ? 11  VAL   A N   1 
ATOM   76   C  CA  . VAL   A 1 12 ? -19.204 -10.716 2.593   1.00 14.44  ? 11  VAL   A CA  1 
ATOM   77   C  C   . VAL   A 1 12 ? -19.072 -10.883 4.100   1.00 11.97  ? 11  VAL   A C   1 
ATOM   78   O  O   . VAL   A 1 12 ? -18.698 -9.964  4.830   1.00 11.77  ? 11  VAL   A O   1 
ATOM   79   C  CB  . VAL   A 1 12 ? -18.149 -11.610 1.900   1.00 12.85  ? 11  VAL   A CB  1 
ATOM   80   C  CG1 . VAL   A 1 12 ? -18.274 -11.538 0.385   1.00 13.82  ? 11  VAL   A CG1 1 
ATOM   81   C  CG2 . VAL   A 1 12 ? -16.736 -11.226 2.358   1.00 9.73   ? 11  VAL   A CG2 1 
ATOM   82   N  N   . PHE   A 1 13 ? -19.407 -12.082 4.558   1.00 10.76  ? 12  PHE   A N   1 
ATOM   83   C  CA  . PHE   A 1 13 ? -18.820 -12.645 5.762   1.00 11.59  ? 12  PHE   A CA  1 
ATOM   84   C  C   . PHE   A 1 13 ? -17.761 -13.643 5.311   1.00 13.32  ? 12  PHE   A C   1 
ATOM   85   O  O   . PHE   A 1 13 ? -18.020 -14.469 4.426   1.00 11.76  ? 12  PHE   A O   1 
ATOM   86   C  CB  . PHE   A 1 13 ? -19.876 -13.322 6.640   1.00 11.66  ? 12  PHE   A CB  1 
ATOM   87   C  CG  . PHE   A 1 13 ? -20.791 -12.355 7.344   1.00 12.44  ? 12  PHE   A CG  1 
ATOM   88   C  CD1 . PHE   A 1 13 ? -21.978 -11.950 6.754   1.00 16.73  ? 12  PHE   A CD1 1 
ATOM   89   C  CD2 . PHE   A 1 13 ? -20.462 -11.857 8.596   1.00 14.38  ? 12  PHE   A CD2 1 
ATOM   90   C  CE1 . PHE   A 1 13 ? -22.833 -11.053 7.398   1.00 21.67  ? 12  PHE   A CE1 1 
ATOM   91   C  CE2 . PHE   A 1 13 ? -21.305 -10.956 9.252   1.00 16.74  ? 12  PHE   A CE2 1 
ATOM   92   C  CZ  . PHE   A 1 13 ? -22.493 -10.554 8.649   1.00 15.97  ? 12  PHE   A CZ  1 
ATOM   93   N  N   . ALA   A 1 14 ? -16.572 -13.555 5.898   1.00 11.54  ? 13  ALA   A N   1 
ATOM   94   C  CA  . ALA   A 1 14 ? -15.445 -14.405 5.537   1.00 11.95  ? 13  ALA   A CA  1 
ATOM   95   C  C   . ALA   A 1 14 ? -15.097 -15.315 6.706   1.00 11.75  ? 13  ALA   A C   1 
ATOM   96   O  O   . ALA   A 1 14 ? -15.021 -14.855 7.853   1.00 16.63  ? 13  ALA   A O   1 
ATOM   97   C  CB  . ALA   A 1 14 ? -14.234 -13.552 5.149   1.00 12.71  ? 13  ALA   A CB  1 
ATOM   98   N  N   . LYS   A 1 15 ? -14.883 -16.598 6.415   1.00 14.26  ? 14  LYS   A N   1 
ATOM   99   C  CA  . LYS   A 1 15 ? -14.632 -17.606 7.439   1.00 13.17  ? 14  LYS   A CA  1 
ATOM   100  C  C   . LYS   A 1 15 ? -13.167 -18.013 7.437   1.00 15.97  ? 14  LYS   A C   1 
ATOM   101  O  O   . LYS   A 1 15 ? -12.619 -18.381 6.392   1.00 14.94  ? 14  LYS   A O   1 
ATOM   102  C  CB  . LYS   A 1 15 ? -15.505 -18.844 7.225   1.00 15.24  ? 14  LYS   A CB  1 
ATOM   103  C  CG  . LYS   A 1 15 ? -15.373 -19.879 8.334   1.00 13.92  ? 14  LYS   A CG  1 
ATOM   104  C  CD  . LYS   A 1 15 ? -15.887 -19.330 9.664   1.00 18.01  ? 14  LYS   A CD  1 
ATOM   105  C  CE  . LYS   A 1 15 ? -15.881 -20.401 10.764  1.00 24.32  ? 14  LYS   A CE  1 
ATOM   106  N  NZ  . LYS   A 1 15 ? -14.507 -20.676 11.277  1.00 27.43  ? 14  LYS   A NZ  1 
ATOM   107  N  N   . MET   A 1 16 ? -12.540 -17.945 8.609   1.00 16.69  ? 15  MET   A N   1 
ATOM   108  C  CA  . MET   A 1 16 ? -11.224 -18.521 8.829   1.00 23.09  ? 15  MET   A CA  1 
ATOM   109  C  C   . MET   A 1 16 ? -11.281 -19.397 10.072  1.00 22.64  ? 15  MET   A C   1 
ATOM   110  O  O   . MET   A 1 16 ? -12.069 -19.146 10.987  1.00 20.38  ? 15  MET   A O   1 
ATOM   111  C  CB  . MET   A 1 16 ? -10.149 -17.442 8.985   1.00 21.43  ? 15  MET   A CB  1 
ATOM   112  C  CG  . MET   A 1 16 ? -10.018 -16.531 7.781   1.00 24.31  ? 15  MET   A CG  1 
ATOM   113  S  SD  . MET   A 1 16 ? -8.375  -15.788 7.676   1.00 27.13  ? 15  MET   A SD  1 
ATOM   114  C  CE  . MET   A 1 16 ? -8.404  -14.785 9.151   1.00 18.79  ? 15  MET   A CE  1 
ATOM   115  N  N   . LYS   A 1 17 ? -10.439 -20.428 10.095  1.00 23.11  ? 16  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 17 ? -10.468 -21.395 11.187  1.00 20.30  ? 16  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 17 ? -10.178 -20.715 12.522  1.00 18.32  ? 16  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 17 ? -9.211  -19.963 12.653  1.00 18.86  ? 16  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 17 ? -9.453  -22.510 10.926  1.00 24.53  ? 16  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 17 ? -9.493  -23.628 11.959  1.00 32.35  ? 16  LYS   A CG  1 
ATOM   121  N  N   . GLY   A 1 18 ? -11.024 -20.977 13.514  1.00 19.06  ? 17  GLY   A N   1 
ATOM   122  C  CA  . GLY   A 1 18 ? -10.854 -20.405 14.833  1.00 26.58  ? 17  GLY   A CA  1 
ATOM   123  C  C   . GLY   A 1 18 ? -11.521 -19.063 15.051  1.00 36.60  ? 17  GLY   A C   1 
ATOM   124  O  O   . GLY   A 1 18 ? -11.393 -18.496 16.147  1.00 28.02  ? 17  GLY   A O   1 
ATOM   125  N  N   . TYR   A 1 19 ? -12.231 -18.539 14.056  1.00 19.42  ? 18  TYR   A N   1 
ATOM   126  C  CA  . TYR   A 1 19 ? -12.908 -17.258 14.162  1.00 16.24  ? 18  TYR   A CA  1 
ATOM   127  C  C   . TYR   A 1 19 ? -14.338 -17.388 13.666  1.00 19.78  ? 18  TYR   A C   1 
ATOM   128  O  O   . TYR   A 1 19 ? -14.614 -18.188 12.768  1.00 17.83  ? 18  TYR   A O   1 
ATOM   129  C  CB  . TYR   A 1 19 ? -12.191 -16.179 13.340  1.00 18.40  ? 18  TYR   A CB  1 
ATOM   130  C  CG  . TYR   A 1 19 ? -10.762 -15.932 13.753  1.00 21.11  ? 18  TYR   A CG  1 
ATOM   131  C  CD1 . TYR   A 1 19 ? -10.451 -14.991 14.732  1.00 17.02  ? 18  TYR   A CD1 1 
ATOM   132  C  CD2 . TYR   A 1 19 ? -9.720  -16.637 13.164  1.00 21.46  ? 18  TYR   A CD2 1 
ATOM   133  C  CE1 . TYR   A 1 19 ? -9.138  -14.761 15.110  1.00 17.18  ? 18  TYR   A CE1 1 
ATOM   134  C  CE2 . TYR   A 1 19 ? -8.408  -16.413 13.535  1.00 22.48  ? 18  TYR   A CE2 1 
ATOM   135  C  CZ  . TYR   A 1 19 ? -8.123  -15.478 14.508  1.00 21.58  ? 18  TYR   A CZ  1 
ATOM   136  O  OH  . TYR   A 1 19 ? -6.816  -15.254 14.879  1.00 30.11  ? 18  TYR   A OH  1 
ATOM   137  N  N   . PRO   A 1 20 ? -15.264 -16.601 14.214  1.00 17.38  ? 19  PRO   A N   1 
ATOM   138  C  CA  . PRO   A 1 20 ? -16.615 -16.569 13.648  1.00 13.19  ? 19  PRO   A CA  1 
ATOM   139  C  C   . PRO   A 1 20 ? -16.581 -15.993 12.242  1.00 14.30  ? 19  PRO   A C   1 
ATOM   140  O  O   . PRO   A 1 20 ? -15.655 -15.267 11.872  1.00 17.24  ? 19  PRO   A O   1 
ATOM   141  C  CB  . PRO   A 1 20 ? -17.385 -15.652 14.608  1.00 18.23  ? 19  PRO   A CB  1 
ATOM   142  C  CG  . PRO   A 1 20 ? -16.320 -14.760 15.184  1.00 18.96  ? 19  PRO   A CG  1 
ATOM   143  C  CD  . PRO   A 1 20 ? -15.100 -15.633 15.315  1.00 16.85  ? 19  PRO   A CD  1 
ATOM   144  N  N   . HIS   A 1 21 ? -17.601 -16.337 11.451  1.00 14.20  ? 20  HIS   A N   1 
ATOM   145  C  CA  . HIS   A 1 21 ? -17.793 -15.689 10.155  1.00 15.80  ? 20  HIS   A CA  1 
ATOM   146  C  C   . HIS   A 1 21 ? -17.757 -14.175 10.328  1.00 13.50  ? 20  HIS   A C   1 
ATOM   147  O  O   . HIS   A 1 21 ? -18.539 -13.616 11.104  1.00 13.60  ? 20  HIS   A O   1 
ATOM   148  C  CB  . HIS   A 1 21 ? -19.125 -16.126 9.536   1.00 15.08  ? 20  HIS   A CB  1 
ATOM   149  C  CG  . HIS   A 1 21 ? -19.196 -17.590 9.210   1.00 15.91  ? 20  HIS   A CG  1 
ATOM   150  N  ND1 . HIS   A 1 21 ? -19.351 -18.564 10.176  1.00 19.33  ? 20  HIS   A ND1 1 
ATOM   151  C  CD2 . HIS   A 1 21 ? -19.159 -18.241 8.023   1.00 23.62  ? 20  HIS   A CD2 1 
ATOM   152  C  CE1 . HIS   A 1 21 ? -19.389 -19.752 9.598   1.00 26.08  ? 20  HIS   A CE1 1 
ATOM   153  N  NE2 . HIS   A 1 21 ? -19.275 -19.585 8.292   1.00 24.37  ? 20  HIS   A NE2 1 
ATOM   154  N  N   . TRP   A 1 22 ? -16.838 -13.518 9.614   1.00 8.63   ? 21  TRP   A N   1 
ATOM   155  C  CA  . TRP   A 1 22 ? -16.405 -12.171 9.962   1.00 10.67  ? 21  TRP   A CA  1 
ATOM   156  C  C   . TRP   A 1 22 ? -16.790 -11.178 8.874   1.00 12.34  ? 21  TRP   A C   1 
ATOM   157  O  O   . TRP   A 1 22 ? -16.553 -11.446 7.690   1.00 11.95  ? 21  TRP   A O   1 
ATOM   158  C  CB  . TRP   A 1 22 ? -14.875 -12.138 10.183  1.00 11.24  ? 21  TRP   A CB  1 
ATOM   159  C  CG  . TRP   A 1 22 ? -14.408 -11.005 11.057  1.00 12.25  ? 21  TRP   A CG  1 
ATOM   160  C  CD1 . TRP   A 1 22 ? -14.254 -9.693  10.694  1.00 9.82   ? 21  TRP   A CD1 1 
ATOM   161  C  CD2 . TRP   A 1 22 ? -14.041 -11.081 12.442  1.00 14.23  ? 21  TRP   A CD2 1 
ATOM   162  N  NE1 . TRP   A 1 22 ? -13.814 -8.957  11.764  1.00 11.80  ? 21  TRP   A NE1 1 
ATOM   163  C  CE2 . TRP   A 1 22 ? -13.683 -9.781  12.851  1.00 11.55  ? 21  TRP   A CE2 1 
ATOM   164  C  CE3 . TRP   A 1 22 ? -13.989 -12.123 13.377  1.00 14.34  ? 21  TRP   A CE3 1 
ATOM   165  C  CZ2 . TRP   A 1 22 ? -13.268 -9.494  14.158  1.00 13.51  ? 21  TRP   A CZ2 1 
ATOM   166  C  CZ3 . TRP   A 1 22 ? -13.578 -11.837 14.673  1.00 13.33  ? 21  TRP   A CZ3 1 
ATOM   167  C  CH2 . TRP   A 1 22 ? -13.226 -10.532 15.050  1.00 13.33  ? 21  TRP   A CH2 1 
ATOM   168  N  N   . PRO   A 1 23 ? -17.350 -10.019 9.230   1.00 11.85  ? 22  PRO   A N   1 
ATOM   169  C  CA  . PRO   A 1 23 ? -17.713 -9.023  8.210   1.00 11.84  ? 22  PRO   A CA  1 
ATOM   170  C  C   . PRO   A 1 23 ? -16.476 -8.507  7.483   1.00 10.33  ? 22  PRO   A C   1 
ATOM   171  O  O   . PRO   A 1 23 ? -15.469 -8.158  8.103   1.00 9.36   ? 22  PRO   A O   1 
ATOM   172  C  CB  . PRO   A 1 23 ? -18.404 -7.919  9.021   1.00 12.89  ? 22  PRO   A CB  1 
ATOM   173  C  CG  . PRO   A 1 23 ? -17.877 -8.091  10.429  1.00 15.18  ? 22  PRO   A CG  1 
ATOM   174  C  CD  . PRO   A 1 23 ? -17.702 -9.581  10.591  1.00 10.61  ? 22  PRO   A CD  1 
ATOM   175  N  N   . ALA   A 1 24 ? -16.560 -8.462  6.154   1.00 7.48   ? 23  ALA   A N   1 
ATOM   176  C  CA  . ALA   A 1 24 ? -15.382 -8.185  5.344   1.00 11.18  ? 23  ALA   A CA  1 
ATOM   177  C  C   . ALA   A 1 24 ? -15.801 -7.689  3.964   1.00 8.96   ? 23  ALA   A C   1 
ATOM   178  O  O   . ALA   A 1 24 ? -16.976 -7.734  3.587   1.00 11.47  ? 23  ALA   A O   1 
ATOM   179  C  CB  . ALA   A 1 24 ? -14.498 -9.435  5.227   1.00 12.06  ? 23  ALA   A CB  1 
ATOM   180  N  N   . ARG   A 1 25 ? -14.814 -7.213  3.208   1.00 8.85   ? 24  ARG   A N   1 
ATOM   181  C  CA  . ARG   A 1 25 ? -15.050 -6.814  1.828   1.00 9.86   ? 24  ARG   A CA  1 
ATOM   182  C  C   . ARG   A 1 25 ? -13.925 -7.327  0.942   1.00 11.05  ? 24  ARG   A C   1 
ATOM   183  O  O   . ARG   A 1 25 ? -12.801 -7.548  1.400   1.00 11.59  ? 24  ARG   A O   1 
ATOM   184  C  CB  . ARG   A 1 25 ? -15.175 -5.287  1.678   1.00 11.17  ? 24  ARG   A CB  1 
ATOM   185  C  CG  . ARG   A 1 25 ? -13.880 -4.532  1.888   1.00 9.82   ? 24  ARG   A CG  1 
ATOM   186  C  CD  . ARG   A 1 25 ? -14.095 -3.019  1.891   1.00 12.14  ? 24  ARG   A CD  1 
ATOM   187  N  NE  . ARG   A 1 25 ? -12.834 -2.298  1.994   1.00 12.01  ? 24  ARG   A NE  1 
ATOM   188  C  CZ  . ARG   A 1 25 ? -12.723 -1.054  2.439   1.00 17.13  ? 24  ARG   A CZ  1 
ATOM   189  N  NH1 . ARG   A 1 25 ? -13.779 -0.373  2.849   1.00 13.37  ? 24  ARG   A NH1 1 
ATOM   190  N  NH2 . ARG   A 1 25 ? -11.522 -0.480  2.476   1.00 16.50  ? 24  ARG   A NH2 1 
ATOM   191  N  N   . ILE   A 1 26 ? -14.249 -7.520  -0.335  1.00 9.59   ? 25  ILE   A N   1 
ATOM   192  C  CA  . ILE   A 1 26 ? -13.237 -7.793  -1.352  1.00 9.52   ? 25  ILE   A CA  1 
ATOM   193  C  C   . ILE   A 1 26 ? -12.484 -6.499  -1.648  1.00 14.92  ? 25  ILE   A C   1 
ATOM   194  O  O   . ILE   A 1 26 ? -13.088 -5.482  -2.009  1.00 15.00  ? 25  ILE   A O   1 
ATOM   195  C  CB  . ILE   A 1 26 ? -13.876 -8.354  -2.632  1.00 12.85  ? 25  ILE   A CB  1 
ATOM   196  C  CG1 . ILE   A 1 26 ? -14.866 -9.488  -2.331  1.00 18.59  ? 25  ILE   A CG1 1 
ATOM   197  C  CG2 . ILE   A 1 26 ? -12.788 -8.791  -3.630  1.00 13.72  ? 25  ILE   A CG2 1 
ATOM   198  C  CD1 . ILE   A 1 26 ? -14.237 -10.741 -1.790  1.00 17.19  ? 25  ILE   A CD1 1 
ATOM   199  N  N   . ASP   A 1 27 ? -11.161 -6.531  -1.504  1.00 12.59  ? 26  ASP   A N   1 
ATOM   200  C  CA  . ASP   A 1 27 ? -10.334 -5.357  -1.749  1.00 17.01  ? 26  ASP   A CA  1 
ATOM   201  C  C   . ASP   A 1 27 ? -9.712  -5.408  -3.143  1.00 19.14  ? 26  ASP   A C   1 
ATOM   202  O  O   . ASP   A 1 27 ? -9.758  -6.421  -3.846  1.00 18.88  ? 26  ASP   A O   1 
ATOM   203  C  CB  . ASP   A 1 27 ? -9.232  -5.233  -0.689  1.00 17.05  ? 26  ASP   A CB  1 
ATOM   204  C  CG  . ASP   A 1 27 ? -9.528  -4.163  0.350   1.00 19.61  ? 26  ASP   A CG  1 
ATOM   205  O  OD1 . ASP   A 1 27 ? -10.657 -3.616  0.367   1.00 17.28  ? 26  ASP   A OD1 1 
ATOM   206  O  OD2 . ASP   A 1 27 ? -8.619  -3.867  1.156   1.00 15.05  ? 26  ASP   A OD2 1 
ATOM   207  N  N   . ASP   A 1 28 ? -9.143  -4.277  -3.541  1.00 16.01  ? 27  ASP   A N   1 
ATOM   208  C  CA  . ASP   A 1 28 ? -8.319  -4.208  -4.733  1.00 29.52  ? 27  ASP   A CA  1 
ATOM   209  C  C   . ASP   A 1 28 ? -6.900  -4.670  -4.418  1.00 23.86  ? 27  ASP   A C   1 
ATOM   210  O  O   . ASP   A 1 28 ? -6.476  -4.711  -3.261  1.00 32.22  ? 27  ASP   A O   1 
ATOM   211  C  CB  . ASP   A 1 28 ? -8.287  -2.779  -5.276  1.00 23.90  ? 27  ASP   A CB  1 
ATOM   212  C  CG  . ASP   A 1 28 ? -9.400  -2.504  -6.258  1.00 35.96  ? 27  ASP   A CG  1 
ATOM   213  O  OD1 . ASP   A 1 28 ? -9.394  -3.111  -7.349  1.00 43.69  ? 27  ASP   A OD1 1 
ATOM   214  O  OD2 . ASP   A 1 28 ? -10.277 -1.672  -5.937  1.00 54.53  ? 27  ASP   A OD2 1 
ATOM   215  N  N   . ILE   A 1 29 ? -6.161  -5.017  -5.467  1.00 27.47  ? 28  ILE   A N   1 
ATOM   216  C  CA  . ILE   A 1 29 ? -4.724  -5.237  -5.366  1.00 27.97  ? 28  ILE   A CA  1 
ATOM   217  C  C   . ILE   A 1 29 ? -4.032  -3.990  -5.895  1.00 38.55  ? 28  ILE   A C   1 
ATOM   218  O  O   . ILE   A 1 29 ? -4.233  -3.608  -7.054  1.00 32.43  ? 28  ILE   A O   1 
ATOM   219  C  CB  . ILE   A 1 29 ? -4.278  -6.485  -6.141  1.00 29.68  ? 28  ILE   A CB  1 
ATOM   220  C  CG1 . ILE   A 1 29 ? -4.907  -7.744  -5.541  1.00 28.98  ? 28  ILE   A CG1 1 
ATOM   221  C  CG2 . ILE   A 1 29 ? -2.760  -6.599  -6.124  1.00 35.67  ? 28  ILE   A CG2 1 
ATOM   222  C  CD1 . ILE   A 1 29 ? -4.246  -8.208  -4.248  1.00 32.09  ? 28  ILE   A CD1 1 
ATOM   223  N  N   . ALA   A 1 30 ? -3.235  -3.348  -5.046  1.00 35.05  ? 29  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 30 ? -2.486  -2.176  -5.471  1.00 40.30  ? 29  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 30 ? -1.452  -2.556  -6.529  1.00 51.84  ? 29  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 30 ? -1.067  -3.720  -6.674  1.00 38.34  ? 29  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 30 ? -1.801  -1.518  -4.274  1.00 36.12  ? 29  ALA   A CB  1 
ATOM   228  N  N   . ASP   A 1 31 ? -1.013  -1.552  -7.286  1.00 45.62  ? 30  ASP   A N   1 
ATOM   229  C  CA  . ASP   A 1 31 ? 0.021   -1.773  -8.288  1.00 42.68  ? 30  ASP   A CA  1 
ATOM   230  C  C   . ASP   A 1 31 ? 1.293   -2.291  -7.632  1.00 34.91  ? 30  ASP   A C   1 
ATOM   231  O  O   . ASP   A 1 31 ? 1.798   -1.700  -6.673  1.00 38.32  ? 30  ASP   A O   1 
ATOM   232  C  CB  . ASP   A 1 31 ? 0.315   -0.477  -9.046  1.00 48.25  ? 30  ASP   A CB  1 
ATOM   233  C  CG  . ASP   A 1 31 ? -0.682  -0.208  -10.156 1.00 69.69  ? 30  ASP   A CG  1 
ATOM   234  O  OD1 . ASP   A 1 31 ? -1.336  -1.168  -10.619 1.00 64.20  ? 30  ASP   A OD1 1 
ATOM   235  O  OD2 . ASP   A 1 31 ? -0.800  0.965   -10.574 1.00 72.26  ? 30  ASP   A OD2 1 
ATOM   236  N  N   . GLY   A 1 32 ? 1.802   -3.410  -8.143  1.00 36.37  ? 31  GLY   A N   1 
ATOM   237  C  CA  . GLY   A 1 32 ? 3.047   -3.963  -7.654  1.00 39.42  ? 31  GLY   A CA  1 
ATOM   238  C  C   . GLY   A 1 32 ? 2.979   -4.647  -6.307  1.00 41.25  ? 31  GLY   A C   1 
ATOM   239  O  O   . GLY   A 1 32 ? 4.017   -5.115  -5.823  1.00 33.14  ? 31  GLY   A O   1 
ATOM   240  N  N   . ALA   A 1 33 ? 1.807   -4.716  -5.679  1.00 26.61  ? 32  ALA   A N   1 
ATOM   241  C  CA  . ALA   A 1 33 ? 1.661   -5.454  -4.435  1.00 28.09  ? 32  ALA   A CA  1 
ATOM   242  C  C   . ALA   A 1 33 ? 1.532   -6.948  -4.724  1.00 17.95  ? 32  ALA   A C   1 
ATOM   243  O  O   . ALA   A 1 33 ? 1.315   -7.372  -5.863  1.00 21.10  ? 32  ALA   A O   1 
ATOM   244  C  CB  . ALA   A 1 33 ? 0.451   -4.950  -3.647  1.00 22.04  ? 32  ALA   A CB  1 
ATOM   245  N  N   A VAL   A 1 34 ? 1.653   -7.751  -3.661  0.28 17.14  ? 33  VAL   A N   1 
ATOM   246  N  N   B VAL   A 1 34 ? 1.695   -7.757  -3.677  0.72 17.29  ? 33  VAL   A N   1 
ATOM   247  C  CA  A VAL   A 1 34 ? 1.524   -9.197  -3.799  0.28 18.06  ? 33  VAL   A CA  1 
ATOM   248  C  CA  B VAL   A 1 34 ? 1.631   -9.202  -3.847  0.72 17.95  ? 33  VAL   A CA  1 
ATOM   249  C  C   A VAL   A 1 34 ? 0.137   -9.543  -4.317  0.28 15.38  ? 33  VAL   A C   1 
ATOM   250  C  C   B VAL   A 1 34 ? 0.211   -9.596  -4.232  0.72 15.13  ? 33  VAL   A C   1 
ATOM   251  O  O   A VAL   A 1 34 ? -0.877  -8.999  -3.859  0.28 19.31  ? 33  VAL   A O   1 
ATOM   252  O  O   B VAL   A 1 34 ? -0.768  -9.123  -3.638  0.72 19.04  ? 33  VAL   A O   1 
ATOM   253  C  CB  A VAL   A 1 34 ? 1.784   -9.908  -2.460  0.28 15.43  ? 33  VAL   A CB  1 
ATOM   254  C  CB  B VAL   A 1 34 ? 2.100   -9.918  -2.571  0.72 14.61  ? 33  VAL   A CB  1 
ATOM   255  C  CG1 A VAL   A 1 34 ? 1.791   -11.419 -2.655  0.28 20.41  ? 33  VAL   A CG1 1 
ATOM   256  C  CG1 B VAL   A 1 34 ? 1.324   -9.426  -1.350  0.72 17.36  ? 33  VAL   A CG1 1 
ATOM   257  C  CG2 A VAL   A 1 34 ? 3.081   -9.445  -1.848  0.28 20.07  ? 33  VAL   A CG2 1 
ATOM   258  C  CG2 B VAL   A 1 34 ? 1.976   -11.425 -2.726  0.72 19.52  ? 33  VAL   A CG2 1 
ATOM   259  N  N   . LYS   A 1 35 ? 0.090   -10.449 -5.263  1.00 19.15  ? 34  LYS   A N   1 
ATOM   260  C  CA  . LYS   A 1 35 ? -1.192  -10.909 -5.764  1.00 17.55  ? 34  LYS   A CA  1 
ATOM   261  C  C   . LYS   A 1 35 ? -1.599  -12.199 -5.059  1.00 18.47  ? 34  LYS   A C   1 
ATOM   262  O  O   . LYS   A 1 35 ? -0.741  -12.949 -4.586  1.00 16.41  ? 34  LYS   A O   1 
ATOM   263  C  CB  . LYS   A 1 35 ? -1.116  -11.140 -7.277  1.00 22.22  ? 34  LYS   A CB  1 
ATOM   264  C  CG  . LYS   A 1 35 ? -0.852  -9.866  -8.068  1.00 29.23  ? 34  LYS   A CG  1 
ATOM   265  C  CD  . LYS   A 1 35 ? -0.792  -10.142 -9.564  1.00 34.92  ? 34  LYS   A CD  1 
ATOM   266  N  N   . PRO   A 1 36 ? -2.896  -12.480 -4.955  1.00 15.81  ? 35  PRO   A N   1 
ATOM   267  C  CA  . PRO   A 1 36 ? -3.336  -13.694 -4.260  1.00 14.32  ? 35  PRO   A CA  1 
ATOM   268  C  C   . PRO   A 1 36 ? -2.934  -14.936 -5.032  1.00 20.10  ? 35  PRO   A C   1 
ATOM   269  O  O   . PRO   A 1 36 ? -2.659  -14.862 -6.238  1.00 18.76  ? 35  PRO   A O   1 
ATOM   270  C  CB  . PRO   A 1 36 ? -4.867  -13.554 -4.216  1.00 12.62  ? 35  PRO   A CB  1 
ATOM   271  C  CG  . PRO   A 1 36 ? -5.184  -12.172 -4.702  1.00 16.52  ? 35  PRO   A CG  1 
ATOM   272  C  CD  . PRO   A 1 36 ? -4.024  -11.727 -5.530  1.00 22.37  ? 35  PRO   A CD  1 
ATOM   273  N  N   . PRO   A 1 37 ? -2.905  -16.093 -4.379  1.00 17.22  ? 36  PRO   A N   1 
ATOM   274  C  CA  . PRO   A 1 37 ? -2.767  -17.366 -5.109  1.00 22.04  ? 36  PRO   A CA  1 
ATOM   275  C  C   . PRO   A 1 37 ? -3.926  -17.568 -6.071  1.00 35.77  ? 36  PRO   A C   1 
ATOM   276  O  O   . PRO   A 1 37 ? -4.916  -16.818 -6.027  1.00 19.06  ? 36  PRO   A O   1 
ATOM   277  C  CB  . PRO   A 1 37 ? -2.783  -18.415 -3.985  1.00 23.10  ? 36  PRO   A CB  1 
ATOM   278  C  CG  . PRO   A 1 37 ? -2.311  -17.677 -2.773  1.00 27.37  ? 36  PRO   A CG  1 
ATOM   279  C  CD  . PRO   A 1 37 ? -2.852  -16.281 -2.919  1.00 18.43  ? 36  PRO   A CD  1 
ATOM   280  N  N   . PRO   A 1 38 ? -3.847  -18.564 -6.956  1.00 29.79  ? 37  PRO   A N   1 
ATOM   281  C  CA  . PRO   A 1 38 ? -4.944  -18.796 -7.905  1.00 27.14  ? 37  PRO   A CA  1 
ATOM   282  C  C   . PRO   A 1 38 ? -6.291  -18.936 -7.205  1.00 18.35  ? 37  PRO   A C   1 
ATOM   283  O  O   . PRO   A 1 38 ? -6.422  -19.644 -6.202  1.00 19.96  ? 37  PRO   A O   1 
ATOM   284  C  CB  . PRO   A 1 38 ? -4.534  -20.098 -8.604  1.00 24.59  ? 37  PRO   A CB  1 
ATOM   285  C  CG  . PRO   A 1 38 ? -3.048  -20.105 -8.527  1.00 25.54  ? 37  PRO   A CG  1 
ATOM   286  C  CD  . PRO   A 1 38 ? -2.697  -19.454 -7.215  1.00 34.36  ? 37  PRO   A CD  1 
ATOM   287  N  N   . ASN   A 1 39 ? -7.291  -18.230 -7.742  1.00 17.15  ? 38  ASN   A N   1 
ATOM   288  C  CA  . ASN   A 1 39 ? -8.671  -18.261 -7.249  1.00 18.03  ? 38  ASN   A CA  1 
ATOM   289  C  C   . ASN   A 1 39 ? -8.773  -17.861 -5.780  1.00 17.39  ? 38  ASN   A C   1 
ATOM   290  O  O   . ASN   A 1 39 ? -9.622  -18.377 -5.042  1.00 19.86  ? 38  ASN   A O   1 
ATOM   291  C  CB  . ASN   A 1 39 ? -9.323  -19.627 -7.470  1.00 19.66  ? 38  ASN   A CB  1 
ATOM   292  C  CG  . ASN   A 1 39 ? -10.846 -19.546 -7.500  1.00 31.41  ? 38  ASN   A CG  1 
ATOM   293  O  OD1 . ASN   A 1 39 ? -11.416 -18.530 -7.905  1.00 34.83  ? 38  ASN   A OD1 1 
ATOM   294  N  ND2 . ASN   A 1 39 ? -11.508 -20.609 -7.063  1.00 21.87  ? 38  ASN   A ND2 1 
ATOM   295  N  N   . LYS   A 1 40 ? -7.926  -16.936 -5.337  1.00 15.15  ? 39  LYS   A N   1 
ATOM   296  C  CA  . LYS   A 1 40 ? -8.094  -16.325 -4.028  1.00 15.11  ? 39  LYS   A CA  1 
ATOM   297  C  C   . LYS   A 1 40 ? -8.186  -14.814 -4.181  1.00 15.43  ? 39  LYS   A C   1 
ATOM   298  O  O   . LYS   A 1 40 ? -7.845  -14.247 -5.226  1.00 13.79  ? 39  LYS   A O   1 
ATOM   299  C  CB  . LYS   A 1 40 ? -6.962  -16.711 -3.063  1.00 10.36  ? 39  LYS   A CB  1 
ATOM   300  C  CG  . LYS   A 1 40 ? -7.031  -18.184 -2.656  1.00 14.77  ? 39  LYS   A CG  1 
ATOM   301  C  CD  . LYS   A 1 40 ? -6.092  -18.530 -1.518  1.00 22.01  ? 39  LYS   A CD  1 
ATOM   302  C  CE  . LYS   A 1 40 ? -6.193  -20.027 -1.208  1.00 26.22  ? 39  LYS   A CE  1 
ATOM   303  N  NZ  . LYS   A 1 40 ? -5.404  -20.425 -0.013  1.00 24.50  ? 39  LYS   A NZ  1 
ATOM   304  N  N   . TYR   A 1 41 ? -8.677  -14.173 -3.128  1.00 11.64  ? 40  TYR   A N   1 
ATOM   305  C  CA  . TYR   A 1 41 ? -9.016  -12.761 -3.166  1.00 12.25  ? 40  TYR   A CA  1 
ATOM   306  C  C   . TYR   A 1 41 ? -8.462  -12.057 -1.940  1.00 9.96   ? 40  TYR   A C   1 
ATOM   307  O  O   . TYR   A 1 41 ? -8.370  -12.652 -0.859  1.00 12.23  ? 40  TYR   A O   1 
ATOM   308  C  CB  . TYR   A 1 41 ? -10.545 -12.558 -3.219  1.00 15.39  ? 40  TYR   A CB  1 
ATOM   309  C  CG  . TYR   A 1 41 ? -11.133 -13.031 -4.524  1.00 18.50  ? 40  TYR   A CG  1 
ATOM   310  C  CD1 . TYR   A 1 41 ? -11.475 -14.371 -4.715  1.00 17.03  ? 40  TYR   A CD1 1 
ATOM   311  C  CD2 . TYR   A 1 41 ? -11.305 -12.152 -5.582  1.00 19.35  ? 40  TYR   A CD2 1 
ATOM   312  C  CE1 . TYR   A 1 41 ? -11.991 -14.812 -5.929  1.00 17.13  ? 40  TYR   A CE1 1 
ATOM   313  C  CE2 . TYR   A 1 41 ? -11.822 -12.577 -6.788  1.00 22.43  ? 40  TYR   A CE2 1 
ATOM   314  C  CZ  . TYR   A 1 41 ? -12.160 -13.904 -6.959  1.00 26.38  ? 40  TYR   A CZ  1 
ATOM   315  O  OH  . TYR   A 1 41 ? -12.668 -14.320 -8.169  1.00 35.17  ? 40  TYR   A OH  1 
ATOM   316  N  N   . PRO   A 1 42 ? -8.096  -10.781 -2.074  1.00 11.23  ? 41  PRO   A N   1 
ATOM   317  C  CA  . PRO   A 1 42 ? -7.717  -9.999  -0.893  1.00 11.39  ? 41  PRO   A CA  1 
ATOM   318  C  C   . PRO   A 1 42 ? -8.969  -9.670  -0.098  1.00 12.40  ? 41  PRO   A C   1 
ATOM   319  O  O   . PRO   A 1 42 ? -9.868  -8.988  -0.596  1.00 13.15  ? 41  PRO   A O   1 
ATOM   320  C  CB  . PRO   A 1 42 ? -7.077  -8.740  -1.488  1.00 14.22  ? 41  PRO   A CB  1 
ATOM   321  C  CG  . PRO   A 1 42 ? -7.691  -8.610  -2.837  1.00 18.34  ? 41  PRO   A CG  1 
ATOM   322  C  CD  . PRO   A 1 42 ? -7.997  -9.997  -3.320  1.00 16.30  ? 41  PRO   A CD  1 
ATOM   323  N  N   . ILE   A 1 43 ? -9.030  -10.166 1.134   1.00 10.83  ? 42  ILE   A N   1 
ATOM   324  C  CA  . ILE   A 1 43 ? -10.184 -9.992  2.010   1.00 10.54  ? 42  ILE   A CA  1 
ATOM   325  C  C   . ILE   A 1 43 ? -9.796  -9.015  3.109   1.00 10.44  ? 42  ILE   A C   1 
ATOM   326  O  O   . ILE   A 1 43 ? -8.932  -9.316  3.941   1.00 17.35  ? 42  ILE   A O   1 
ATOM   327  C  CB  . ILE   A 1 43 ? -10.647 -11.327 2.618   1.00 9.72   ? 42  ILE   A CB  1 
ATOM   328  C  CG1 . ILE   A 1 43 ? -10.883 -12.371 1.528   1.00 10.75  ? 42  ILE   A CG1 1 
ATOM   329  C  CG2 . ILE   A 1 43 ? -11.891 -11.123 3.482   1.00 13.96  ? 42  ILE   A CG2 1 
ATOM   330  C  CD1 . ILE   A 1 43 ? -11.814 -11.920 0.435   1.00 14.53  ? 42  ILE   A CD1 1 
ATOM   331  N  N   . PHE   A 1 44 ? -10.440 -7.853  3.124   1.00 11.37  ? 43  PHE   A N   1 
ATOM   332  C  CA  . PHE   A 1 44 ? -10.228 -6.867  4.177   1.00 11.20  ? 43  PHE   A CA  1 
ATOM   333  C  C   . PHE   A 1 44 ? -11.281 -7.068  5.260   1.00 13.50  ? 43  PHE   A C   1 
ATOM   334  O  O   . PHE   A 1 44 ? -12.481 -6.948  4.990   1.00 12.23  ? 43  PHE   A O   1 
ATOM   335  C  CB  . PHE   A 1 44 ? -10.305 -5.449  3.615   1.00 10.74  ? 43  PHE   A CB  1 
ATOM   336  C  CG  . PHE   A 1 44 ? -10.125 -4.378  4.650   1.00 10.99  ? 43  PHE   A CG  1 
ATOM   337  C  CD1 . PHE   A 1 44 ? -8.859  -4.055  5.110   1.00 19.14  ? 43  PHE   A CD1 1 
ATOM   338  C  CD2 . PHE   A 1 44 ? -11.222 -3.700  5.170   1.00 15.67  ? 43  PHE   A CD2 1 
ATOM   339  C  CE1 . PHE   A 1 44 ? -8.684  -3.063  6.068   1.00 17.76  ? 43  PHE   A CE1 1 
ATOM   340  C  CE2 . PHE   A 1 44 ? -11.057 -2.702  6.131   1.00 15.38  ? 43  PHE   A CE2 1 
ATOM   341  C  CZ  . PHE   A 1 44 ? -9.780  -2.386  6.578   1.00 14.96  ? 43  PHE   A CZ  1 
ATOM   342  N  N   . PHE   A 1 45 ? -10.833 -7.370  6.475   1.00 8.65   ? 44  PHE   A N   1 
ATOM   343  C  CA  . PHE   A 1 45 ? -11.735 -7.630  7.591   1.00 10.20  ? 44  PHE   A CA  1 
ATOM   344  C  C   . PHE   A 1 45 ? -12.068 -6.316  8.283   1.00 14.67  ? 44  PHE   A C   1 
ATOM   345  O  O   . PHE   A 1 45 ? -11.170 -5.614  8.761   1.00 15.12  ? 44  PHE   A O   1 
ATOM   346  C  CB  . PHE   A 1 45 ? -11.117 -8.610  8.585   1.00 13.45  ? 44  PHE   A CB  1 
ATOM   347  C  CG  . PHE   A 1 45 ? -10.895 -9.984  8.018   1.00 10.39  ? 44  PHE   A CG  1 
ATOM   348  C  CD1 . PHE   A 1 45 ? -11.918 -10.911 7.994   1.00 15.90  ? 44  PHE   A CD1 1 
ATOM   349  C  CD2 . PHE   A 1 45 ? -9.661  -10.341 7.499   1.00 21.72  ? 44  PHE   A CD2 1 
ATOM   350  C  CE1 . PHE   A 1 45 ? -11.714 -12.188 7.468   1.00 16.47  ? 44  PHE   A CE1 1 
ATOM   351  C  CE2 . PHE   A 1 45 ? -9.452  -11.613 6.973   1.00 22.22  ? 44  PHE   A CE2 1 
ATOM   352  C  CZ  . PHE   A 1 45 ? -10.483 -12.530 6.956   1.00 15.79  ? 44  PHE   A CZ  1 
ATOM   353  N  N   . PHE   A 1 46 ? -13.355 -5.987  8.340   1.00 12.58  ? 45  PHE   A N   1 
ATOM   354  C  CA  . PHE   A 1 46 ? -13.780 -4.804  9.073   1.00 10.22  ? 45  PHE   A CA  1 
ATOM   355  C  C   . PHE   A 1 46 ? -13.514 -4.994  10.567  1.00 14.10  ? 45  PHE   A C   1 
ATOM   356  O  O   . PHE   A 1 46 ? -13.458 -6.120  11.080  1.00 13.80  ? 45  PHE   A O   1 
ATOM   357  C  CB  . PHE   A 1 46 ? -15.267 -4.526  8.836   1.00 10.21  ? 45  PHE   A CB  1 
ATOM   358  C  CG  . PHE   A 1 46 ? -15.615 -4.147  7.419   1.00 12.52  ? 45  PHE   A CG  1 
ATOM   359  C  CD1 . PHE   A 1 46 ? -15.235 -2.914  6.900   1.00 10.51  ? 45  PHE   A CD1 1 
ATOM   360  C  CD2 . PHE   A 1 46 ? -16.359 -5.014  6.617   1.00 11.85  ? 45  PHE   A CD2 1 
ATOM   361  C  CE1 . PHE   A 1 46 ? -15.564 -2.550  5.602   1.00 11.94  ? 45  PHE   A CE1 1 
ATOM   362  C  CE2 . PHE   A 1 46 ? -16.691 -4.664  5.320   1.00 11.14  ? 45  PHE   A CE2 1 
ATOM   363  C  CZ  . PHE   A 1 46 ? -16.296 -3.429  4.806   1.00 9.16   ? 45  PHE   A CZ  1 
ATOM   364  N  N   . GLY   A 1 47 ? -13.347 -3.873  11.267  1.00 10.60  ? 46  GLY   A N   1 
ATOM   365  C  CA  . GLY   A 1 47 ? -13.108 -3.880  12.701  1.00 15.77  ? 46  GLY   A CA  1 
ATOM   366  C  C   . GLY   A 1 47 ? -11.641 -4.035  13.051  1.00 13.06  ? 46  GLY   A C   1 
ATOM   367  O  O   . GLY   A 1 47 ? -11.034 -3.152  13.670  1.00 18.58  ? 46  GLY   A O   1 
ATOM   368  N  N   . THR   A 1 48 ? -11.057 -5.163  12.653  1.00 12.95  ? 47  THR   A N   1 
ATOM   369  C  CA  . THR   A 1 48 ? -9.638  -5.404  12.876  1.00 10.99  ? 47  THR   A CA  1 
ATOM   370  C  C   . THR   A 1 48 ? -8.775  -4.738  11.823  1.00 13.28  ? 47  THR   A C   1 
ATOM   371  O  O   . THR   A 1 48 ? -7.608  -4.437  12.093  1.00 14.85  ? 47  THR   A O   1 
ATOM   372  C  CB  . THR   A 1 48 ? -9.345  -6.903  12.873  1.00 9.62   ? 47  THR   A CB  1 
ATOM   373  O  OG1 . THR   A 1 48 ? -9.697  -7.440  11.589  1.00 14.29  ? 47  THR   A OG1 1 
ATOM   374  C  CG2 . THR   A 1 48 ? -10.135 -7.617  13.962  1.00 14.13  ? 47  THR   A CG2 1 
ATOM   375  N  N   . HIS   A 1 49 ? -9.323  -4.526  10.624  1.00 12.96  ? 48  HIS   A N   1 
ATOM   376  C  CA  . HIS   A 1 49 ? -8.623  -3.851  9.531   1.00 16.57  ? 48  HIS   A CA  1 
ATOM   377  C  C   . HIS   A 1 49 ? -7.368  -4.620  9.132   1.00 24.90  ? 48  HIS   A C   1 
ATOM   378  O  O   . HIS   A 1 49 ? -6.301  -4.043  8.918   1.00 21.21  ? 48  HIS   A O   1 
ATOM   379  C  CB  . HIS   A 1 49 ? -8.297  -2.397  9.893   1.00 14.02  ? 48  HIS   A CB  1 
ATOM   380  C  CG  . HIS   A 1 49 ? -9.466  -1.641  10.448  1.00 17.48  ? 48  HIS   A CG  1 
ATOM   381  N  ND1 . HIS   A 1 49 ? -9.340  -0.710  11.457  1.00 23.90  ? 48  HIS   A ND1 1 
ATOM   382  C  CD2 . HIS   A 1 49 ? -10.784 -1.685  10.138  1.00 14.88  ? 48  HIS   A CD2 1 
ATOM   383  C  CE1 . HIS   A 1 49 ? -10.531 -0.212  11.744  1.00 28.34  ? 48  HIS   A CE1 1 
ATOM   384  N  NE2 . HIS   A 1 49 ? -11.424 -0.786  10.957  1.00 18.25  ? 48  HIS   A NE2 1 
ATOM   385  N  N   . GLU   A 1 50 ? -7.497  -5.940  9.045   1.00 16.01  ? 49  GLU   A N   1 
ATOM   386  C  CA  . GLU   A 1 50 ? -6.445  -6.808  8.540   1.00 17.74  ? 49  GLU   A CA  1 
ATOM   387  C  C   . GLU   A 1 50 ? -6.892  -7.438  7.226   1.00 15.75  ? 49  GLU   A C   1 
ATOM   388  O  O   . GLU   A 1 50 ? -8.082  -7.474  6.904   1.00 15.88  ? 49  GLU   A O   1 
ATOM   389  C  CB  . GLU   A 1 50 ? -6.093  -7.890  9.566   1.00 18.03  ? 49  GLU   A CB  1 
ATOM   390  C  CG  . GLU   A 1 50 ? -5.751  -7.324  10.935  1.00 19.76  ? 49  GLU   A CG  1 
ATOM   391  C  CD  . GLU   A 1 50 ? -5.347  -8.387  11.938  1.00 39.24  ? 49  GLU   A CD  1 
ATOM   392  O  OE1 . GLU   A 1 50 ? -4.962  -9.499  11.518  1.00 48.39  ? 49  GLU   A OE1 1 
ATOM   393  O  OE2 . GLU   A 1 50 ? -5.413  -8.107  13.153  1.00 44.29  ? 49  GLU   A OE2 1 
ATOM   394  N  N   . THR   A 1 51 ? -5.922  -7.930  6.457   1.00 15.24  ? 50  THR   A N   1 
ATOM   395  C  CA  . THR   A 1 51 ? -6.200  -8.497  5.144   1.00 12.75  ? 50  THR   A CA  1 
ATOM   396  C  C   . THR   A 1 51 ? -5.649  -9.911  5.055   1.00 14.70  ? 50  THR   A C   1 
ATOM   397  O  O   . THR   A 1 51 ? -4.544  -10.184 5.530   1.00 17.15  ? 50  THR   A O   1 
ATOM   398  C  CB  . THR   A 1 51 ? -5.602  -7.635  4.015   1.00 13.86  ? 50  THR   A CB  1 
ATOM   399  O  OG1 . THR   A 1 51 ? -5.965  -6.269  4.225   1.00 19.18  ? 50  THR   A OG1 1 
ATOM   400  C  CG2 . THR   A 1 51 ? -6.145  -8.072  2.657   1.00 20.74  ? 50  THR   A CG2 1 
ATOM   401  N  N   . ALA   A 1 52 ? -6.429  -10.807 4.451   1.00 11.61  ? 51  ALA   A N   1 
ATOM   402  C  CA  . ALA   A 1 52 ? -5.980  -12.167 4.178   1.00 13.40  ? 51  ALA   A CA  1 
ATOM   403  C  C   . ALA   A 1 52 ? -6.390  -12.550 2.764   1.00 19.01  ? 51  ALA   A C   1 
ATOM   404  O  O   . ALA   A 1 52 ? -7.302  -11.959 2.182   1.00 18.52  ? 51  ALA   A O   1 
ATOM   405  C  CB  . ALA   A 1 52 ? -6.549  -13.172 5.188   1.00 18.00  ? 51  ALA   A CB  1 
ATOM   406  N  N   . PHE   A 1 53 ? -5.684  -13.530 2.205   1.00 14.60  ? 52  PHE   A N   1 
ATOM   407  C  CA  . PHE   A 1 53 ? -6.053  -14.125 0.925   1.00 10.83  ? 52  PHE   A CA  1 
ATOM   408  C  C   . PHE   A 1 53 ? -6.945  -15.333 1.195   1.00 14.09  ? 52  PHE   A C   1 
ATOM   409  O  O   . PHE   A 1 53 ? -6.516  -16.279 1.864   1.00 14.19  ? 52  PHE   A O   1 
ATOM   410  C  CB  . PHE   A 1 53 ? -4.813  -14.563 0.146   1.00 10.67  ? 52  PHE   A CB  1 
ATOM   411  C  CG  . PHE   A 1 53 ? -3.983  -13.431 -0.406  1.00 12.72  ? 52  PHE   A CG  1 
ATOM   412  C  CD1 . PHE   A 1 53 ? -4.563  -12.224 -0.757  1.00 13.35  ? 52  PHE   A CD1 1 
ATOM   413  C  CD2 . PHE   A 1 53 ? -2.619  -13.592 -0.591  1.00 18.58  ? 52  PHE   A CD2 1 
ATOM   414  C  CE1 . PHE   A 1 53 ? -3.797  -11.195 -1.288  1.00 18.70  ? 52  PHE   A CE1 1 
ATOM   415  C  CE2 . PHE   A 1 53 ? -1.841  -12.563 -1.112  1.00 15.38  ? 52  PHE   A CE2 1 
ATOM   416  C  CZ  . PHE   A 1 53 ? -2.434  -11.366 -1.461  1.00 14.29  ? 52  PHE   A CZ  1 
ATOM   417  N  N   . LEU   A 1 54 ? -8.177  -15.305 0.683   1.00 11.85  ? 53  LEU   A N   1 
ATOM   418  C  CA  . LEU   A 1 54 ? -9.114  -16.409 0.854   1.00 15.00  ? 53  LEU   A CA  1 
ATOM   419  C  C   . LEU   A 1 54 ? -9.800  -16.730 -0.466  1.00 12.37  ? 53  LEU   A C   1 
ATOM   420  O  O   . LEU   A 1 54 ? -9.952  -15.870 -1.337  1.00 14.45  ? 53  LEU   A O   1 
ATOM   421  C  CB  . LEU   A 1 54 ? -10.183 -16.093 1.912   1.00 13.06  ? 53  LEU   A CB  1 
ATOM   422  C  CG  . LEU   A 1 54 ? -9.719  -15.867 3.349   1.00 13.40  ? 53  LEU   A CG  1 
ATOM   423  C  CD1 . LEU   A 1 54 ? -10.902 -15.429 4.212   1.00 15.18  ? 53  LEU   A CD1 1 
ATOM   424  C  CD2 . LEU   A 1 54 ? -9.082  -17.131 3.913   1.00 19.69  ? 53  LEU   A CD2 1 
ATOM   425  N  N   . GLY   A 1 55 ? -10.232 -17.987 -0.591  1.00 13.76  ? 54  GLY   A N   1 
ATOM   426  C  CA  . GLY   A 1 55 ? -10.968 -18.436 -1.750  1.00 16.93  ? 54  GLY   A CA  1 
ATOM   427  C  C   . GLY   A 1 55 ? -12.467 -18.367 -1.541  1.00 16.12  ? 54  GLY   A C   1 
ATOM   428  O  O   . GLY   A 1 55 ? -12.956 -18.221 -0.416  1.00 13.50  ? 54  GLY   A O   1 
ATOM   429  N  N   . PRO   A 1 56 ? -13.225 -18.468 -2.637  1.00 13.82  ? 55  PRO   A N   1 
ATOM   430  C  CA  . PRO   A 1 56 ? -14.688 -18.302 -2.548  1.00 17.66  ? 55  PRO   A CA  1 
ATOM   431  C  C   . PRO   A 1 56 ? -15.389 -19.266 -1.604  1.00 13.93  ? 55  PRO   A C   1 
ATOM   432  O  O   . PRO   A 1 56 ? -16.460 -18.923 -1.085  1.00 10.95  ? 55  PRO   A O   1 
ATOM   433  C  CB  . PRO   A 1 56 ? -15.144 -18.517 -3.996  1.00 13.77  ? 55  PRO   A CB  1 
ATOM   434  C  CG  . PRO   A 1 56 ? -13.963 -18.056 -4.822  1.00 13.41  ? 55  PRO   A CG  1 
ATOM   435  C  CD  . PRO   A 1 56 ? -12.753 -18.506 -4.036  1.00 16.92  ? 55  PRO   A CD  1 
ATOM   436  N  N   . LYS   A 1 57 ? -14.848 -20.466 -1.377  1.00 14.83  ? 56  LYS   A N   1 
ATOM   437  C  CA  . LYS   A 1 57 ? -15.508 -21.393 -0.458  1.00 12.19  ? 56  LYS   A CA  1 
ATOM   438  C  C   . LYS   A 1 57 ? -15.655 -20.811 0.944   1.00 11.52  ? 56  LYS   A C   1 
ATOM   439  O  O   . LYS   A 1 57 ? -16.523 -21.258 1.706   1.00 11.96  ? 56  LYS   A O   1 
ATOM   440  C  CB  . LYS   A 1 57 ? -14.737 -22.713 -0.392  1.00 20.43  ? 56  LYS   A CB  1 
ATOM   441  C  CG  . LYS   A 1 57 ? -13.343 -22.576 0.208   1.00 18.68  ? 56  LYS   A CG  1 
ATOM   442  C  CD  . LYS   A 1 57 ? -12.681 -23.935 0.391   1.00 35.96  ? 56  LYS   A CD  1 
ATOM   443  C  CE  . LYS   A 1 57 ? -11.601 -23.882 1.468   1.00 35.08  ? 56  LYS   A CE  1 
ATOM   444  N  NZ  . LYS   A 1 57 ? -12.198 -23.812 2.838   1.00 46.79  ? 56  LYS   A NZ  1 
ATOM   445  N  N   . ASP   A 1 58 ? -14.850 -19.807 1.291   1.00 12.76  ? 57  ASP   A N   1 
ATOM   446  C  CA  . ASP   A 1 58 ? -14.895 -19.183 2.606   1.00 19.45  ? 57  ASP   A CA  1 
ATOM   447  C  C   . ASP   A 1 58 ? -15.575 -17.814 2.605   1.00 11.32  ? 57  ASP   A C   1 
ATOM   448  O  O   . ASP   A 1 58 ? -15.545 -17.124 3.630   1.00 12.51  ? 57  ASP   A O   1 
ATOM   449  C  CB  . ASP   A 1 58 ? -13.474 -19.072 3.169   1.00 16.23  ? 57  ASP   A CB  1 
ATOM   450  C  CG  . ASP   A 1 58 ? -12.875 -20.440 3.497   1.00 22.79  ? 57  ASP   A CG  1 
ATOM   451  O  OD1 . ASP   A 1 58 ? -13.620 -21.307 4.001   1.00 19.75  ? 57  ASP   A OD1 1 
ATOM   452  O  OD2 . ASP   A 1 58 ? -11.671 -20.654 3.245   1.00 19.44  ? 57  ASP   A OD2 1 
ATOM   453  N  N   . LEU   A 1 59 ? -16.224 -17.424 1.506   1.00 11.19  ? 58  LEU   A N   1 
ATOM   454  C  CA  . LEU   A 1 59 ? -16.797 -16.088 1.356   1.00 11.81  ? 58  LEU   A CA  1 
ATOM   455  C  C   . LEU   A 1 59 ? -18.308 -16.187 1.190   1.00 14.00  ? 58  LEU   A C   1 
ATOM   456  O  O   . LEU   A 1 59 ? -18.790 -16.790 0.229   1.00 9.98   ? 58  LEU   A O   1 
ATOM   457  C  CB  . LEU   A 1 59 ? -16.176 -15.365 0.156   1.00 12.64  ? 58  LEU   A CB  1 
ATOM   458  C  CG  . LEU   A 1 59 ? -14.651 -15.356 0.157   1.00 12.56  ? 58  LEU   A CG  1 
ATOM   459  C  CD1 . LEU   A 1 59 ? -14.134 -14.696 -1.106  1.00 10.15  ? 58  LEU   A CD1 1 
ATOM   460  C  CD2 . LEU   A 1 59 ? -14.115 -14.646 1.405   1.00 9.58   ? 58  LEU   A CD2 1 
ATOM   461  N  N   . PHE   A 1 60 ? -19.050 -15.575 2.111   1.00 9.88   ? 59  PHE   A N   1 
ATOM   462  C  CA  . PHE   A 1 60 ? -20.508 -15.662 2.122   1.00 11.85  ? 59  PHE   A CA  1 
ATOM   463  C  C   . PHE   A 1 60 ? -21.105 -14.293 1.831   1.00 15.99  ? 59  PHE   A C   1 
ATOM   464  O  O   . PHE   A 1 60 ? -20.936 -13.370 2.642   1.00 14.54  ? 59  PHE   A O   1 
ATOM   465  C  CB  . PHE   A 1 60 ? -20.998 -16.186 3.476   1.00 11.86  ? 59  PHE   A CB  1 
ATOM   466  C  CG  . PHE   A 1 60 ? -20.523 -17.583 3.783   1.00 11.23  ? 59  PHE   A CG  1 
ATOM   467  C  CD1 . PHE   A 1 60 ? -19.212 -17.809 4.200   1.00 11.52  ? 59  PHE   A CD1 1 
ATOM   468  C  CD2 . PHE   A 1 60 ? -21.374 -18.659 3.642   1.00 15.61  ? 59  PHE   A CD2 1 
ATOM   469  C  CE1 . PHE   A 1 60 ? -18.757 -19.093 4.463   1.00 17.58  ? 59  PHE   A CE1 1 
ATOM   470  C  CE2 . PHE   A 1 60 ? -20.935 -19.944 3.902   1.00 16.83  ? 59  PHE   A CE2 1 
ATOM   471  C  CZ  . PHE   A 1 60 ? -19.625 -20.163 4.321   1.00 22.98  ? 59  PHE   A CZ  1 
ATOM   472  N  N   . PRO   A 1 61 ? -21.795 -14.110 0.703   1.00 14.75  ? 60  PRO   A N   1 
ATOM   473  C  CA  . PRO   A 1 61 ? -22.323 -12.784 0.356   1.00 16.43  ? 60  PRO   A CA  1 
ATOM   474  C  C   . PRO   A 1 61 ? -23.168 -12.193 1.476   1.00 17.99  ? 60  PRO   A C   1 
ATOM   475  O  O   . PRO   A 1 61 ? -23.949 -12.887 2.134   1.00 17.33  ? 60  PRO   A O   1 
ATOM   476  C  CB  . PRO   A 1 61 ? -23.150 -13.057 -0.903  1.00 15.26  ? 60  PRO   A CB  1 
ATOM   477  C  CG  . PRO   A 1 61 ? -22.430 -14.205 -1.556  1.00 20.35  ? 60  PRO   A CG  1 
ATOM   478  C  CD  . PRO   A 1 61 ? -21.958 -15.077 -0.400  1.00 22.63  ? 60  PRO   A CD  1 
ATOM   479  N  N   . TYR   A 1 62 ? -22.997 -10.886 1.682   1.00 15.90  ? 61  TYR   A N   1 
ATOM   480  C  CA  . TYR   A 1 62 ? -23.431 -10.255 2.926   1.00 15.08  ? 61  TYR   A CA  1 
ATOM   481  C  C   . TYR   A 1 62 ? -24.947 -10.267 3.075   1.00 16.46  ? 61  TYR   A C   1 
ATOM   482  O  O   . TYR   A 1 62 ? -25.469 -10.643 4.130   1.00 19.92  ? 61  TYR   A O   1 
ATOM   483  C  CB  . TYR   A 1 62 ? -22.901 -8.824  2.993   1.00 14.75  ? 61  TYR   A CB  1 
ATOM   484  C  CG  . TYR   A 1 62 ? -23.473 -8.025  4.141   1.00 13.60  ? 61  TYR   A CG  1 
ATOM   485  C  CD1 . TYR   A 1 62 ? -23.061 -8.258  5.445   1.00 18.67  ? 61  TYR   A CD1 1 
ATOM   486  C  CD2 . TYR   A 1 62 ? -24.421 -7.039  3.919   1.00 19.38  ? 61  TYR   A CD2 1 
ATOM   487  C  CE1 . TYR   A 1 62 ? -23.581 -7.527  6.499   1.00 25.82  ? 61  TYR   A CE1 1 
ATOM   488  C  CE2 . TYR   A 1 62 ? -24.945 -6.305  4.966   1.00 17.19  ? 61  TYR   A CE2 1 
ATOM   489  C  CZ  . TYR   A 1 62 ? -24.518 -6.554  6.251   1.00 20.62  ? 61  TYR   A CZ  1 
ATOM   490  O  OH  . TYR   A 1 62 ? -25.036 -5.826  7.300   1.00 28.58  ? 61  TYR   A OH  1 
ATOM   491  N  N   . ASP   A 1 63 ? -25.671 -9.842  2.037   1.00 23.43  ? 62  ASP   A N   1 
ATOM   492  C  CA  . ASP   A 1 63 ? -27.125 -9.723  2.148   1.00 24.79  ? 62  ASP   A CA  1 
ATOM   493  C  C   . ASP   A 1 63 ? -27.776 -11.066 2.460   1.00 17.78  ? 62  ASP   A C   1 
ATOM   494  O  O   . ASP   A 1 63 ? -28.675 -11.145 3.306   1.00 25.82  ? 62  ASP   A O   1 
ATOM   495  C  CB  . ASP   A 1 63 ? -27.707 -9.130  0.864   1.00 22.77  ? 62  ASP   A CB  1 
ATOM   496  C  CG  . ASP   A 1 63 ? -27.717 -7.614  0.880   1.00 47.03  ? 62  ASP   A CG  1 
ATOM   497  O  OD1 . ASP   A 1 63 ? -27.341 -7.027  1.918   1.00 46.83  ? 62  ASP   A OD1 1 
ATOM   498  O  OD2 . ASP   A 1 63 ? -28.105 -7.007  -0.143  1.00 56.41  ? 62  ASP   A OD2 1 
ATOM   499  N  N   . LYS   A 1 64 ? -27.323 -12.135 1.807   1.00 21.53  ? 63  LYS   A N   1 
ATOM   500  C  CA  . LYS   A 1 64 ? -27.927 -13.448 2.025   1.00 20.40  ? 63  LYS   A CA  1 
ATOM   501  C  C   . LYS   A 1 64 ? -27.609 -14.013 3.408   1.00 21.72  ? 63  LYS   A C   1 
ATOM   502  O  O   . LYS   A 1 64 ? -28.413 -14.772 3.963   1.00 20.61  ? 63  LYS   A O   1 
ATOM   503  C  CB  . LYS   A 1 64 ? -27.448 -14.420 0.939   1.00 20.61  ? 63  LYS   A CB  1 
ATOM   504  C  CG  . LYS   A 1 64 ? -27.960 -15.847 1.095   1.00 33.48  ? 63  LYS   A CG  1 
ATOM   505  C  CD  . LYS   A 1 64 ? -27.252 -16.804 0.145   1.00 24.34  ? 63  LYS   A CD  1 
ATOM   506  C  CE  . LYS   A 1 64 ? -27.735 -18.239 0.322   1.00 38.64  ? 63  LYS   A CE  1 
ATOM   507  N  NZ  . LYS   A 1 64 ? -29.164 -18.422 -0.033  1.00 32.85  ? 63  LYS   A NZ  1 
ATOM   508  N  N   . SER   A 1 65 ? -26.467 -13.641 3.993   1.00 22.32  ? 64  SER   A N   1 
ATOM   509  C  CA  A SER   A 1 65 ? -25.951 -14.294 5.188   0.53 17.51  ? 64  SER   A CA  1 
ATOM   510  C  CA  B SER   A 1 65 ? -25.967 -14.300 5.191   0.47 17.47  ? 64  SER   A CA  1 
ATOM   511  C  C   . SER   A 1 65 ? -26.039 -13.452 6.454   1.00 17.41  ? 64  SER   A C   1 
ATOM   512  O  O   . SER   A 1 65 ? -25.711 -13.960 7.534   1.00 18.06  ? 64  SER   A O   1 
ATOM   513  C  CB  A SER   A 1 65 ? -24.484 -14.698 4.973   0.53 17.42  ? 64  SER   A CB  1 
ATOM   514  C  CB  B SER   A 1 65 ? -24.512 -14.743 4.977   0.47 17.49  ? 64  SER   A CB  1 
ATOM   515  O  OG  A SER   A 1 65 ? -24.330 -15.467 3.795   0.53 15.69  ? 64  SER   A OG  1 
ATOM   516  O  OG  B SER   A 1 65 ? -23.690 -13.637 4.650   0.47 20.80  ? 64  SER   A OG  1 
ATOM   517  N  N   . LYS   A 1 66 ? -26.465 -12.187 6.362   1.00 16.88  ? 65  LYS   A N   1 
ATOM   518  C  CA  . LYS   A 1 66 ? -26.382 -11.300 7.523   1.00 17.65  ? 65  LYS   A CA  1 
ATOM   519  C  C   . LYS   A 1 66 ? -27.301 -11.732 8.665   1.00 27.87  ? 65  LYS   A C   1 
ATOM   520  O  O   . LYS   A 1 66 ? -26.957 -11.536 9.837   1.00 22.17  ? 65  LYS   A O   1 
ATOM   521  C  CB  . LYS   A 1 66 ? -26.684 -9.858  7.108   1.00 22.99  ? 65  LYS   A CB  1 
ATOM   522  C  CG  . LYS   A 1 66 ? -28.083 -9.636  6.577   1.00 33.97  ? 65  LYS   A CG  1 
ATOM   523  C  CD  . LYS   A 1 66 ? -28.191 -8.277  5.914   1.00 34.09  ? 65  LYS   A CD  1 
ATOM   524  C  CE  . LYS   A 1 66 ? -29.611 -7.995  5.451   1.00 43.52  ? 65  LYS   A CE  1 
ATOM   525  N  NZ  . LYS   A 1 66 ? -29.688 -6.721  4.681   1.00 44.98  ? 65  LYS   A NZ  1 
ATOM   526  N  N   . ASP   A 1 67 ? -28.459 -12.320 8.357   1.00 26.21  ? 66  ASP   A N   1 
ATOM   527  C  CA  . ASP   A 1 67 ? -29.348 -12.790 9.417   1.00 25.12  ? 66  ASP   A CA  1 
ATOM   528  C  C   . ASP   A 1 67 ? -28.684 -13.869 10.262  1.00 26.13  ? 66  ASP   A C   1 
ATOM   529  O  O   . ASP   A 1 67 ? -28.908 -13.946 11.476  1.00 29.06  ? 66  ASP   A O   1 
ATOM   530  C  CB  . ASP   A 1 67 ? -30.649 -13.313 8.808   1.00 45.02  ? 66  ASP   A CB  1 
ATOM   531  C  CG  . ASP   A 1 67 ? -31.731 -12.254 8.739   1.00 57.53  ? 66  ASP   A CG  1 
ATOM   532  O  OD1 . ASP   A 1 67 ? -32.876 -12.549 9.137   1.00 76.51  ? 66  ASP   A OD1 1 
ATOM   533  O  OD2 . ASP   A 1 67 ? -31.431 -11.119 8.312   1.00 68.32  ? 66  ASP   A OD2 1 
ATOM   534  N  N   . LYS   A 1 68 ? -27.856 -14.705 9.640   1.00 21.10  ? 67  LYS   A N   1 
ATOM   535  C  CA  . LYS   A 1 68 ? -27.247 -15.821 10.347  1.00 17.70  ? 67  LYS   A CA  1 
ATOM   536  C  C   . LYS   A 1 68 ? -25.968 -15.411 11.066  1.00 20.86  ? 67  LYS   A C   1 
ATOM   537  O  O   . LYS   A 1 68 ? -25.730 -15.834 12.202  1.00 21.94  ? 67  LYS   A O   1 
ATOM   538  C  CB  . LYS   A 1 68 ? -26.963 -16.951 9.358   1.00 27.30  ? 67  LYS   A CB  1 
ATOM   539  C  CG  . LYS   A 1 68 ? -26.455 -18.228 9.982   1.00 24.88  ? 67  LYS   A CG  1 
ATOM   540  C  CD  . LYS   A 1 68 ? -26.350 -19.306 8.917   1.00 34.17  ? 67  LYS   A CD  1 
ATOM   541  C  CE  . LYS   A 1 68 ? -26.401 -20.697 9.514   1.00 46.66  ? 67  LYS   A CE  1 
ATOM   542  N  NZ  . LYS   A 1 68 ? -27.030 -21.656 8.557   1.00 53.42  ? 67  LYS   A NZ  1 
ATOM   543  N  N   . TYR   A 1 69 ? -25.138 -14.587 10.426  1.00 18.13  ? 68  TYR   A N   1 
ATOM   544  C  CA  . TYR   A 1 69 ? -23.795 -14.292 10.907  1.00 15.77  ? 68  TYR   A CA  1 
ATOM   545  C  C   . TYR   A 1 69 ? -23.648 -12.911 11.540  1.00 17.52  ? 68  TYR   A C   1 
ATOM   546  O  O   . TYR   A 1 69 ? -22.586 -12.620 12.101  1.00 17.15  ? 68  TYR   A O   1 
ATOM   547  C  CB  . TYR   A 1 69 ? -22.793 -14.420 9.751   1.00 14.48  ? 68  TYR   A CB  1 
ATOM   548  C  CG  . TYR   A 1 69 ? -22.703 -15.812 9.163   1.00 17.13  ? 68  TYR   A CG  1 
ATOM   549  C  CD1 . TYR   A 1 69 ? -22.726 -16.937 9.978   1.00 16.12  ? 68  TYR   A CD1 1 
ATOM   550  C  CD2 . TYR   A 1 69 ? -22.592 -15.999 7.791   1.00 17.84  ? 68  TYR   A CD2 1 
ATOM   551  C  CE1 . TYR   A 1 69 ? -22.631 -18.214 9.443   1.00 20.96  ? 68  TYR   A CE1 1 
ATOM   552  C  CE2 . TYR   A 1 69 ? -22.504 -17.277 7.245   1.00 24.19  ? 68  TYR   A CE2 1 
ATOM   553  C  CZ  . TYR   A 1 69 ? -22.524 -18.378 8.077   1.00 19.39  ? 68  TYR   A CZ  1 
ATOM   554  O  OH  . TYR   A 1 69 ? -22.434 -19.648 7.544   1.00 23.25  ? 68  TYR   A OH  1 
ATOM   555  N  N   . GLY   A 1 70 ? -24.672 -12.066 11.485  1.00 21.46  ? 69  GLY   A N   1 
ATOM   556  C  CA  . GLY   A 1 70 ? -24.520 -10.685 11.914  1.00 15.34  ? 69  GLY   A CA  1 
ATOM   557  C  C   . GLY   A 1 70 ? -24.735 -10.416 13.392  1.00 16.23  ? 69  GLY   A C   1 
ATOM   558  O  O   . GLY   A 1 70 ? -24.958 -9.265  13.779  1.00 21.86  ? 69  GLY   A O   1 
ATOM   559  N  N   . LYS   A 1 71 ? -24.663 -11.446 14.237  1.00 18.05  ? 70  LYS   A N   1 
ATOM   560  C  CA  . LYS   A 1 71 ? -24.942 -11.172 15.645  1.00 21.29  ? 70  LYS   A CA  1 
ATOM   561  C  C   . LYS   A 1 71 ? -23.687 -10.656 16.351  1.00 17.56  ? 70  LYS   A C   1 
ATOM   562  O  O   . LYS   A 1 71 ? -22.586 -11.137 16.083  1.00 17.11  ? 70  LYS   A O   1 
ATOM   563  C  CB  . LYS   A 1 71 ? -25.451 -12.427 16.359  1.00 20.01  ? 70  LYS   A CB  1 
ATOM   564  C  CG  . LYS   A 1 71 ? -26.658 -13.080 15.707  1.00 39.97  ? 70  LYS   A CG  1 
ATOM   565  C  CD  . LYS   A 1 71 ? -27.697 -12.059 15.263  1.00 50.40  ? 70  LYS   A CD  1 
ATOM   566  C  CE  . LYS   A 1 71 ? -28.812 -12.732 14.474  1.00 58.34  ? 70  LYS   A CE  1 
ATOM   567  N  NZ  . LYS   A 1 71 ? -29.605 -11.753 13.678  1.00 56.17  ? 70  LYS   A NZ  1 
ATOM   568  N  N   . PRO   A 1 72 ? -23.828 -9.675  17.244  1.00 14.61  ? 71  PRO   A N   1 
ATOM   569  C  CA  . PRO   A 1 72 ? -22.677 -9.228  18.038  1.00 13.83  ? 71  PRO   A CA  1 
ATOM   570  C  C   . PRO   A 1 72 ? -22.078 -10.372 18.841  1.00 16.67  ? 71  PRO   A C   1 
ATOM   571  O  O   . PRO   A 1 72 ? -22.760 -11.338 19.186  1.00 21.04  ? 71  PRO   A O   1 
ATOM   572  C  CB  . PRO   A 1 72 ? -23.275 -8.155  18.959  1.00 16.91  ? 71  PRO   A CB  1 
ATOM   573  C  CG  . PRO   A 1 72 ? -24.470 -7.642  18.217  1.00 19.44  ? 71  PRO   A CG  1 
ATOM   574  C  CD  . PRO   A 1 72 ? -25.018 -8.833  17.460  1.00 11.19  ? 71  PRO   A CD  1 
ATOM   575  N  N   . ASN   A 1 73 ? -20.780 -10.263 19.126  1.00 17.75  ? 72  ASN   A N   1 
ATOM   576  C  CA  . ASN   A 1 73 ? -20.109 -11.227 19.988  1.00 25.21  ? 72  ASN   A CA  1 
ATOM   577  C  C   . ASN   A 1 73 ? -18.919 -10.548 20.656  1.00 24.45  ? 72  ASN   A C   1 
ATOM   578  O  O   . ASN   A 1 73 ? -18.664 -9.358  20.460  1.00 16.43  ? 72  ASN   A O   1 
ATOM   579  C  CB  . ASN   A 1 73 ? -19.712 -12.494 19.211  1.00 14.77  ? 72  ASN   A CB  1 
ATOM   580  C  CG  . ASN   A 1 73 ? -18.679 -12.240 18.127  1.00 17.69  ? 72  ASN   A CG  1 
ATOM   581  O  OD1 . ASN   A 1 73 ? -17.620 -11.656 18.369  1.00 19.68  ? 72  ASN   A OD1 1 
ATOM   582  N  ND2 . ASN   A 1 73 ? -18.975 -12.710 16.923  1.00 18.67  ? 72  ASN   A ND2 1 
ATOM   583  N  N   . LYS   A 1 74 ? -18.186 -11.320 21.462  1.00 15.53  ? 73  LYS   A N   1 
ATOM   584  C  CA  . LYS   A 1 74 ? -17.145 -10.752 22.311  1.00 14.89  ? 73  LYS   A CA  1 
ATOM   585  C  C   . LYS   A 1 74 ? -15.785 -10.650 21.630  1.00 16.86  ? 73  LYS   A C   1 
ATOM   586  O  O   . LYS   A 1 74 ? -14.885 -10.001 22.181  1.00 19.77  ? 73  LYS   A O   1 
ATOM   587  C  CB  . LYS   A 1 74 ? -17.014 -11.575 23.600  1.00 23.80  ? 73  LYS   A CB  1 
ATOM   588  C  CG  . LYS   A 1 74 ? -16.519 -12.994 23.400  1.00 23.78  ? 73  LYS   A CG  1 
ATOM   589  C  CD  . LYS   A 1 74 ? -16.536 -13.771 24.715  1.00 36.68  ? 73  LYS   A CD  1 
ATOM   590  N  N   . ARG   A 1 75 ? -15.612 -11.252 20.456  1.00 18.78  ? 74  ARG   A N   1 
ATOM   591  C  CA  . ARG   A 1 75 ? -14.304 -11.255 19.812  1.00 18.58  ? 74  ARG   A CA  1 
ATOM   592  C  C   . ARG   A 1 75 ? -13.837 -9.831  19.519  1.00 22.16  ? 74  ARG   A C   1 
ATOM   593  O  O   . ARG   A 1 75 ? -14.619 -8.981  19.088  1.00 15.17  ? 74  ARG   A O   1 
ATOM   594  C  CB  . ARG   A 1 75 ? -14.360 -12.072 18.522  1.00 18.97  ? 74  ARG   A CB  1 
ATOM   595  C  CG  . ARG   A 1 75 ? -14.886 -13.494 18.717  1.00 19.30  ? 74  ARG   A CG  1 
ATOM   596  C  CD  . ARG   A 1 75 ? -13.984 -14.299 19.637  1.00 30.05  ? 74  ARG   A CD  1 
ATOM   597  N  NE  . ARG   A 1 75 ? -12.724 -14.638 18.989  1.00 46.36  ? 74  ARG   A NE  1 
ATOM   598  C  CZ  . ARG   A 1 75 ? -12.479 -15.791 18.379  1.00 32.45  ? 74  ARG   A CZ  1 
ATOM   599  N  NH1 . ARG   A 1 75 ? -13.378 -16.762 18.346  1.00 35.62  ? 74  ARG   A NH1 1 
ATOM   600  N  NH2 . ARG   A 1 75 ? -11.300 -15.976 17.793  1.00 28.37  ? 74  ARG   A NH2 1 
ATOM   601  N  N   . LYS   A 1 76 ? -12.549 -9.576  19.752  1.00 20.25  ? 75  LYS   A N   1 
ATOM   602  C  CA  . LYS   A 1 76 ? -12.010 -8.231  19.600  1.00 20.27  ? 75  LYS   A CA  1 
ATOM   603  C  C   . LYS   A 1 76 ? -12.192 -7.732  18.173  1.00 17.25  ? 75  LYS   A C   1 
ATOM   604  O  O   . LYS   A 1 76 ? -11.802 -8.399  17.213  1.00 15.30  ? 75  LYS   A O   1 
ATOM   605  C  CB  . LYS   A 1 76 ? -10.528 -8.200  19.979  1.00 19.37  ? 75  LYS   A CB  1 
ATOM   606  C  CG  . LYS   A 1 76 ? -9.939  -6.797  19.949  1.00 37.63  ? 75  LYS   A CG  1 
ATOM   607  C  CD  . LYS   A 1 76 ? -8.461  -6.769  20.305  1.00 50.29  ? 75  LYS   A CD  1 
ATOM   608  C  CE  . LYS   A 1 76 ? -8.100  -5.447  20.975  1.00 62.43  ? 75  LYS   A CE  1 
ATOM   609  N  NZ  . LYS   A 1 76 ? -6.630  -5.243  21.110  1.00 55.06  ? 75  LYS   A NZ  1 
ATOM   610  N  N   . GLY   A 1 77 ? -12.787 -6.547  18.039  1.00 19.85  ? 76  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 77 ? -13.004 -5.942  16.747  1.00 18.06  ? 76  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 77 ? -14.269 -6.366  16.032  1.00 12.45  ? 76  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 77 ? -14.639 -5.723  15.041  1.00 15.00  ? 76  GLY   A O   1 
ATOM   614  N  N   . PHE   A 1 78 ? -14.963 -7.409  16.501  1.00 13.10  ? 77  PHE   A N   1 
ATOM   615  C  CA  . PHE   A 1 78 ? -16.100 -7.923  15.742  1.00 12.72  ? 77  PHE   A CA  1 
ATOM   616  C  C   . PHE   A 1 78 ? -17.236 -6.910  15.675  1.00 13.08  ? 77  PHE   A C   1 
ATOM   617  O  O   . PHE   A 1 78 ? -17.774 -6.644  14.595  1.00 10.13  ? 77  PHE   A O   1 
ATOM   618  C  CB  . PHE   A 1 78 ? -16.607 -9.237  16.340  1.00 13.35  ? 77  PHE   A CB  1 
ATOM   619  C  CG  . PHE   A 1 78 ? -17.571 -9.964  15.448  1.00 15.53  ? 77  PHE   A CG  1 
ATOM   620  C  CD1 . PHE   A 1 78 ? -17.111 -10.886 14.515  1.00 13.68  ? 77  PHE   A CD1 1 
ATOM   621  C  CD2 . PHE   A 1 78 ? -18.935 -9.713  15.525  1.00 15.47  ? 77  PHE   A CD2 1 
ATOM   622  C  CE1 . PHE   A 1 78 ? -18.001 -11.556 13.682  1.00 9.99   ? 77  PHE   A CE1 1 
ATOM   623  C  CE2 . PHE   A 1 78 ? -19.829 -10.371 14.696  1.00 18.43  ? 77  PHE   A CE2 1 
ATOM   624  C  CZ  . PHE   A 1 78 ? -19.355 -11.300 13.770  1.00 19.79  ? 77  PHE   A CZ  1 
ATOM   625  N  N   . ASN   A 1 79 ? -17.655 -6.371  16.825  1.00 14.66  ? 78  ASN   A N   1 
ATOM   626  C  CA  . ASN   A 1 79 ? -18.793 -5.455  16.825  1.00 12.28  ? 78  ASN   A CA  1 
ATOM   627  C  C   . ASN   A 1 79 ? -18.495 -4.193  16.025  1.00 8.54   ? 78  ASN   A C   1 
ATOM   628  O  O   . ASN   A 1 79 ? -19.370 -3.677  15.322  1.00 11.48  ? 78  ASN   A O   1 
ATOM   629  C  CB  . ASN   A 1 79 ? -19.193 -5.105  18.258  1.00 12.78  ? 78  ASN   A CB  1 
ATOM   630  C  CG  . ASN   A 1 79 ? -19.847 -6.279  18.980  1.00 15.02  ? 78  ASN   A CG  1 
ATOM   631  O  OD1 . ASN   A 1 79 ? -20.154 -7.301  18.366  1.00 13.51  ? 78  ASN   A OD1 1 
ATOM   632  N  ND2 . ASN   A 1 79 ? -20.083 -6.128  20.285  1.00 12.73  ? 78  ASN   A ND2 1 
ATOM   633  N  N   . GLU   A 1 80 ? -17.266 -3.681  16.111  1.00 10.10  ? 79  GLU   A N   1 
ATOM   634  C  CA  . GLU   A 1 80 ? -16.898 -2.553  15.259  1.00 13.36  ? 79  GLU   A CA  1 
ATOM   635  C  C   . GLU   A 1 80 ? -16.943 -2.954  13.791  1.00 15.89  ? 79  GLU   A C   1 
ATOM   636  O  O   . GLU   A 1 80 ? -17.355 -2.162  12.934  1.00 10.15  ? 79  GLU   A O   1 
ATOM   637  C  CB  . GLU   A 1 80 ? -15.512 -2.025  15.635  1.00 13.77  ? 79  GLU   A CB  1 
ATOM   638  C  CG  . GLU   A 1 80 ? -14.896 -1.047  14.610  1.00 28.30  ? 79  GLU   A CG  1 
ATOM   639  C  CD  . GLU   A 1 80 ? -15.580 0.311   14.558  1.00 42.75  ? 79  GLU   A CD  1 
ATOM   640  O  OE1 . GLU   A 1 80 ? -15.299 1.080   13.601  1.00 32.48  ? 79  GLU   A OE1 1 
ATOM   641  O  OE2 . GLU   A 1 80 ? -16.382 0.617   15.472  1.00 26.80  ? 79  GLU   A OE2 1 
ATOM   642  N  N   . GLY   A 1 81 ? -16.538 -4.190  13.482  1.00 11.39  ? 80  GLY   A N   1 
ATOM   643  C  CA  . GLY   A 1 81 ? -16.668 -4.679  12.116  1.00 9.17   ? 80  GLY   A CA  1 
ATOM   644  C  C   . GLY   A 1 81 ? -18.110 -4.715  11.642  1.00 12.03  ? 80  GLY   A C   1 
ATOM   645  O  O   . GLY   A 1 81 ? -18.409 -4.342  10.503  1.00 10.91  ? 80  GLY   A O   1 
ATOM   646  N  N   . LEU   A 1 82 ? -19.022 -5.186  12.498  1.00 9.19   ? 81  LEU   A N   1 
ATOM   647  C  CA  . LEU   A 1 82 ? -20.442 -5.148  12.147  1.00 9.42   ? 81  LEU   A CA  1 
ATOM   648  C  C   . LEU   A 1 82 ? -20.891 -3.723  11.857  1.00 15.39  ? 81  LEU   A C   1 
ATOM   649  O  O   . LEU   A 1 82 ? -21.651 -3.478  10.909  1.00 11.55  ? 81  LEU   A O   1 
ATOM   650  C  CB  . LEU   A 1 82 ? -21.289 -5.737  13.275  1.00 6.68   ? 81  LEU   A CB  1 
ATOM   651  C  CG  . LEU   A 1 82 ? -21.242 -7.244  13.525  1.00 20.35  ? 81  LEU   A CG  1 
ATOM   652  C  CD1 . LEU   A 1 82 ? -22.112 -7.580  14.736  1.00 20.54  ? 81  LEU   A CD1 1 
ATOM   653  C  CD2 . LEU   A 1 82 ? -21.706 -8.009  12.296  1.00 15.69  ? 81  LEU   A CD2 1 
ATOM   654  N  N   . TRP   A 1 83 ? -20.441 -2.771  12.673  1.00 9.79   ? 82  TRP   A N   1 
ATOM   655  C  CA  . TRP   A 1 83 ? -20.816 -1.381  12.449  1.00 8.98   ? 82  TRP   A CA  1 
ATOM   656  C  C   . TRP   A 1 83 ? -20.279 -0.874  11.115  1.00 11.81  ? 82  TRP   A C   1 
ATOM   657  O  O   . TRP   A 1 83 ? -20.997 -0.203  10.363  1.00 13.69  ? 82  TRP   A O   1 
ATOM   658  C  CB  . TRP   A 1 83 ? -20.316 -0.500  13.593  1.00 12.91  ? 82  TRP   A CB  1 
ATOM   659  C  CG  . TRP   A 1 83 ? -20.670 0.935   13.376  1.00 12.52  ? 82  TRP   A CG  1 
ATOM   660  C  CD1 . TRP   A 1 83 ? -21.795 1.577   13.809  1.00 13.47  ? 82  TRP   A CD1 1 
ATOM   661  C  CD2 . TRP   A 1 83 ? -19.914 1.902   12.638  1.00 11.75  ? 82  TRP   A CD2 1 
ATOM   662  N  NE1 . TRP   A 1 83 ? -21.782 2.889   13.392  1.00 12.02  ? 82  TRP   A NE1 1 
ATOM   663  C  CE2 . TRP   A 1 83 ? -20.637 3.112   12.670  1.00 14.99  ? 82  TRP   A CE2 1 
ATOM   664  C  CE3 . TRP   A 1 83 ? -18.695 1.861   11.950  1.00 16.28  ? 82  TRP   A CE3 1 
ATOM   665  C  CZ2 . TRP   A 1 83 ? -20.179 4.274   12.047  1.00 18.00  ? 82  TRP   A CZ2 1 
ATOM   666  C  CZ3 . TRP   A 1 83 ? -18.243 3.019   11.329  1.00 18.98  ? 82  TRP   A CZ3 1 
ATOM   667  C  CH2 . TRP   A 1 83 ? -18.984 4.206   11.384  1.00 18.67  ? 82  TRP   A CH2 1 
ATOM   668  N  N   . GLU   A 1 84 ? -19.023 -1.199  10.798  1.00 12.01  ? 83  GLU   A N   1 
ATOM   669  C  CA  . GLU   A 1 84 ? -18.416 -0.696  9.567   1.00 15.35  ? 83  GLU   A CA  1 
ATOM   670  C  C   . GLU   A 1 84 ? -19.122 -1.249  8.336   1.00 8.54   ? 83  GLU   A C   1 
ATOM   671  O  O   . GLU   A 1 84 ? -19.412 -0.508  7.390   1.00 10.76  ? 83  GLU   A O   1 
ATOM   672  C  CB  . GLU   A 1 84 ? -16.922 -1.035  9.535   1.00 8.92   ? 83  GLU   A CB  1 
ATOM   673  C  CG  . GLU   A 1 84 ? -16.118 -0.233  10.566  1.00 11.31  ? 83  GLU   A CG  1 
ATOM   674  C  CD  . GLU   A 1 84 ? -14.672 -0.680  10.686  1.00 11.27  ? 83  GLU   A CD  1 
ATOM   675  O  OE1 . GLU   A 1 84 ? -14.257 -1.573  9.924   1.00 16.46  ? 83  GLU   A OE1 1 
ATOM   676  O  OE2 . GLU   A 1 84 ? -13.945 -0.135  11.549  1.00 13.91  ? 83  GLU   A OE2 1 
ATOM   677  N  N   . ILE   A 1 85 ? -19.415 -2.551  8.323   1.00 10.14  ? 84  ILE   A N   1 
ATOM   678  C  CA  . ILE   A 1 85 ? -20.026 -3.110  7.118   1.00 14.53  ? 84  ILE   A CA  1 
ATOM   679  C  C   . ILE   A 1 85 ? -21.442 -2.576  6.936   1.00 11.60  ? 84  ILE   A C   1 
ATOM   680  O  O   . ILE   A 1 85 ? -21.913 -2.425  5.800   1.00 13.79  ? 84  ILE   A O   1 
ATOM   681  C  CB  . ILE   A 1 85 ? -19.991 -4.653  7.140   1.00 10.79  ? 84  ILE   A CB  1 
ATOM   682  C  CG1 . ILE   A 1 85 ? -20.202 -5.209  5.728   1.00 11.31  ? 84  ILE   A CG1 1 
ATOM   683  C  CG2 . ILE   A 1 85 ? -21.040 -5.236  8.108   1.00 10.81  ? 84  ILE   A CG2 1 
ATOM   684  C  CD1 . ILE   A 1 85 ? -19.887 -6.718  5.615   1.00 10.83  ? 84  ILE   A CD1 1 
ATOM   685  N  N   . GLN   A 1 86 ? -22.134 -2.248  8.035   1.00 11.89  ? 85  GLN   A N   1 
ATOM   686  C  CA  . GLN   A 1 86 ? -23.497 -1.731  7.932   1.00 13.68  ? 85  GLN   A CA  1 
ATOM   687  C  C   . GLN   A 1 86 ? -23.542 -0.234  7.657   1.00 17.96  ? 85  GLN   A C   1 
ATOM   688  O  O   . GLN   A 1 86 ? -24.518 0.251   7.072   1.00 15.92  ? 85  GLN   A O   1 
ATOM   689  C  CB  . GLN   A 1 86 ? -24.274 -2.012  9.225   1.00 10.70  ? 85  GLN   A CB  1 
ATOM   690  C  CG  . GLN   A 1 86 ? -24.514 -3.485  9.517   1.00 17.93  ? 85  GLN   A CG  1 
ATOM   691  C  CD  . GLN   A 1 86 ? -25.245 -3.688  10.836  1.00 31.99  ? 85  GLN   A CD  1 
ATOM   692  O  OE1 . GLN   A 1 86 ? -25.024 -4.673  11.542  1.00 46.91  ? 85  GLN   A OE1 1 
ATOM   693  N  NE2 . GLN   A 1 86 ? -26.118 -2.750  11.174  1.00 27.10  ? 85  GLN   A NE2 1 
ATOM   694  N  N   . ASN   A 1 87 ? -22.526 0.516   8.078   1.00 11.36  ? 86  ASN   A N   1 
ATOM   695  C  CA  . ASN   A 1 87 ? -22.630 1.971   8.063   1.00 10.78  ? 86  ASN   A CA  1 
ATOM   696  C  C   . ASN   A 1 87 ? -21.711 2.661   7.068   1.00 14.01  ? 86  ASN   A C   1 
ATOM   697  O  O   . ASN   A 1 87 ? -22.093 3.700   6.524   1.00 13.12  ? 86  ASN   A O   1 
ATOM   698  C  CB  . ASN   A 1 87 ? -22.369 2.538   9.461   1.00 13.93  ? 86  ASN   A CB  1 
ATOM   699  C  CG  . ASN   A 1 87 ? -23.503 2.233   10.418  1.00 18.39  ? 86  ASN   A CG  1 
ATOM   700  O  OD1 . ASN   A 1 87 ? -24.463 2.991   10.501  1.00 20.41  ? 86  ASN   A OD1 1 
ATOM   701  N  ND2 . ASN   A 1 87 ? -23.409 1.109   11.127  1.00 15.07  ? 86  ASN   A ND2 1 
ATOM   702  N  N   . ASN   A 1 88 ? -20.505 2.146   6.818   1.00 13.35  ? 87  ASN   A N   1 
ATOM   703  C  CA  . ASN   A 1 88 ? -19.607 2.749   5.828   1.00 11.07  ? 87  ASN   A CA  1 
ATOM   704  C  C   . ASN   A 1 88 ? -18.675 1.682   5.282   1.00 12.93  ? 87  ASN   A C   1 
ATOM   705  O  O   . ASN   A 1 88 ? -17.464 1.696   5.536   1.00 13.69  ? 87  ASN   A O   1 
ATOM   706  C  CB  . ASN   A 1 88 ? -18.825 3.916   6.431   1.00 14.61  ? 87  ASN   A CB  1 
ATOM   707  C  CG  . ASN   A 1 88 ? -18.424 4.937   5.388   1.00 14.77  ? 87  ASN   A CG  1 
ATOM   708  O  OD1 . ASN   A 1 88 ? -18.324 4.616   4.202   1.00 15.44  ? 87  ASN   A OD1 1 
ATOM   709  N  ND2 . ASN   A 1 88 ? -18.194 6.175   5.819   1.00 17.12  ? 87  ASN   A ND2 1 
ATOM   710  N  N   . PRO   A 1 89 ? -19.210 0.742   4.498   1.00 9.00   ? 88  PRO   A N   1 
ATOM   711  C  CA  . PRO   A 1 89 ? -18.396 -0.412  4.078   1.00 11.76  ? 88  PRO   A CA  1 
ATOM   712  C  C   . PRO   A 1 89 ? -17.354 -0.094  3.019   1.00 13.84  ? 88  PRO   A C   1 
ATOM   713  O  O   . PRO   A 1 89 ? -16.467 -0.928  2.788   1.00 11.38  ? 88  PRO   A O   1 
ATOM   714  C  CB  . PRO   A 1 89 ? -19.441 -1.398  3.541   1.00 9.87   ? 88  PRO   A CB  1 
ATOM   715  C  CG  . PRO   A 1 89 ? -20.572 -0.528  3.082   1.00 11.00  ? 88  PRO   A CG  1 
ATOM   716  C  CD  . PRO   A 1 89 ? -20.614 0.627   4.049   1.00 13.16  ? 88  PRO   A CD  1 
ATOM   717  N  N   . HIS   A 1 90 ? -17.444 1.052   2.344   1.00 10.82  ? 89  HIS   A N   1 
ATOM   718  C  CA  . HIS   A 1 90 ? -16.514 1.388   1.274   1.00 12.23  ? 89  HIS   A CA  1 
ATOM   719  C  C   . HIS   A 1 90 ? -15.559 2.510   1.652   1.00 15.47  ? 89  HIS   A C   1 
ATOM   720  O  O   . HIS   A 1 90 ? -14.869 3.045   0.777   1.00 13.58  ? 89  HIS   A O   1 
ATOM   721  C  CB  . HIS   A 1 90 ? -17.280 1.747   -0.000  1.00 10.79  ? 89  HIS   A CB  1 
ATOM   722  C  CG  . HIS   A 1 90 ? -18.219 0.673   -0.453  1.00 11.27  ? 89  HIS   A CG  1 
ATOM   723  N  ND1 . HIS   A 1 90 ? -17.794 -0.598  -0.784  1.00 10.32  ? 89  HIS   A ND1 1 
ATOM   724  C  CD2 . HIS   A 1 90 ? -19.563 0.678   -0.622  1.00 12.00  ? 89  HIS   A CD2 1 
ATOM   725  C  CE1 . HIS   A 1 90 ? -18.836 -1.328  -1.143  1.00 14.50  ? 89  HIS   A CE1 1 
ATOM   726  N  NE2 . HIS   A 1 90 ? -19.922 -0.578  -1.052  1.00 17.89  ? 89  HIS   A NE2 1 
ATOM   727  N  N   . ALA   A 1 91 ? -15.476 2.854   2.930   1.00 12.37  ? 90  ALA   A N   1 
ATOM   728  C  CA  . ALA   A 1 91 ? -14.601 3.923   3.374   1.00 13.51  ? 90  ALA   A CA  1 
ATOM   729  C  C   . ALA   A 1 91 ? -13.158 3.438   3.480   1.00 15.08  ? 90  ALA   A C   1 
ATOM   730  O  O   . ALA   A 1 91 ? -12.859 2.239   3.414   1.00 14.53  ? 90  ALA   A O   1 
ATOM   731  C  CB  . ALA   A 1 91 ? -15.074 4.468   4.723   1.00 14.13  ? 90  ALA   A CB  1 
ATOM   732  N  N   . SER   A 1 92 ? -12.254 4.397   3.657   1.00 17.33  ? 91  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 92 ? -10.842 4.107   3.866   1.00 16.57  ? 91  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 92 ? -10.599 3.893   5.357   1.00 16.21  ? 91  SER   A C   1 
ATOM   735  O  O   . SER   A 1 92 ? -10.880 4.780   6.167   1.00 17.42  ? 91  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 92 ? -9.974  5.248   3.330   1.00 21.01  ? 91  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 92 ? -8.616  5.044   3.652   1.00 39.21  ? 91  SER   A OG  1 
ATOM   738  N  N   . TYR   A 1 93 ? -10.084 2.720   5.717   1.00 17.04  ? 92  TYR   A N   1 
ATOM   739  C  CA  . TYR   A 1 93 ? -9.813  2.390   7.108   1.00 22.23  ? 92  TYR   A CA  1 
ATOM   740  C  C   . TYR   A 1 93 ? -8.328  2.287   7.418   1.00 28.64  ? 92  TYR   A C   1 
ATOM   741  O  O   . TYR   A 1 93 ? -7.965  2.034   8.571   1.00 41.25  ? 92  TYR   A O   1 
ATOM   742  C  CB  . TYR   A 1 93 ? -10.520 1.081   7.488   1.00 18.49  ? 92  TYR   A CB  1 
ATOM   743  C  CG  . TYR   A 1 93 ? -12.023 1.243   7.544   1.00 15.58  ? 92  TYR   A CG  1 
ATOM   744  C  CD1 . TYR   A 1 93 ? -12.636 1.739   8.682   1.00 15.18  ? 92  TYR   A CD1 1 
ATOM   745  C  CD2 . TYR   A 1 93 ? -12.822 0.918   6.452   1.00 13.76  ? 92  TYR   A CD2 1 
ATOM   746  C  CE1 . TYR   A 1 93 ? -14.010 1.899   8.745   1.00 13.09  ? 92  TYR   A CE1 1 
ATOM   747  C  CE2 . TYR   A 1 93 ? -14.207 1.078   6.505   1.00 13.31  ? 92  TYR   A CE2 1 
ATOM   748  C  CZ  . TYR   A 1 93 ? -14.789 1.574   7.656   1.00 16.73  ? 92  TYR   A CZ  1 
ATOM   749  O  OH  . TYR   A 1 93 ? -16.155 1.740   7.730   1.00 13.19  ? 92  TYR   A OH  1 
ATOM   750  N  N   . SER   A 1 94 ? -7.465  2.469   6.429   1.00 30.67  ? 93  SER   A N   1 
ATOM   751  C  CA  . SER   A 1 94 ? -6.027  2.479   6.663   1.00 44.61  ? 93  SER   A CA  1 
ATOM   752  C  C   . SER   A 1 94 ? -5.570  3.871   7.086   1.00 51.42  ? 93  SER   A C   1 
ATOM   753  O  O   . SER   A 1 94 ? -5.701  4.258   8.250   1.00 56.64  ? 93  SER   A O   1 
ATOM   754  C  CB  . SER   A 1 94 ? -5.276  2.033   5.409   1.00 43.95  ? 93  SER   A CB  1 
ATOM   755  O  OG  . SER   A 1 94 ? -5.516  2.923   4.333   1.00 59.06  ? 93  SER   A OG  1 
ATOM   756  O  OXT . SER   A 1 94 ? -5.063  4.640   6.270   1.00 65.24  ? 93  SER   A OXT 1 
ATOM   757  N  N   . HIS   B 1 4  ? -24.178 2.938   48.522  1.00 53.37  ? 3   HIS   B N   1 
ATOM   758  C  CA  . HIS   B 1 4  ? -23.916 3.472   47.191  1.00 52.47  ? 3   HIS   B CA  1 
ATOM   759  C  C   . HIS   B 1 4  ? -25.152 3.338   46.309  1.00 36.85  ? 3   HIS   B C   1 
ATOM   760  O  O   . HIS   B 1 4  ? -25.943 2.410   46.473  1.00 42.25  ? 3   HIS   B O   1 
ATOM   761  C  CB  . HIS   B 1 4  ? -22.724 2.760   46.547  1.00 50.36  ? 3   HIS   B CB  1 
ATOM   762  C  CG  . HIS   B 1 4  ? -21.502 2.726   47.410  1.00 67.07  ? 3   HIS   B CG  1 
ATOM   763  N  ND1 . HIS   B 1 4  ? -21.155 1.627   48.165  1.00 80.40  ? 3   HIS   B ND1 1 
ATOM   764  C  CD2 . HIS   B 1 4  ? -20.550 3.660   47.647  1.00 73.24  ? 3   HIS   B CD2 1 
ATOM   765  C  CE1 . HIS   B 1 4  ? -20.040 1.882   48.826  1.00 89.35  ? 3   HIS   B CE1 1 
ATOM   766  N  NE2 . HIS   B 1 4  ? -19.652 3.110   48.529  1.00 84.70  ? 3   HIS   B NE2 1 
ATOM   767  N  N   . ALA   B 1 5  ? -25.319 4.275   45.374  1.00 31.23  ? 4   ALA   B N   1 
ATOM   768  C  CA  . ALA   B 1 5  ? -26.480 4.242   44.493  1.00 40.69  ? 4   ALA   B CA  1 
ATOM   769  C  C   . ALA   B 1 5  ? -26.427 3.086   43.501  1.00 41.45  ? 4   ALA   B C   1 
ATOM   770  O  O   . ALA   B 1 5  ? -27.474 2.697   42.969  1.00 34.61  ? 4   ALA   B O   1 
ATOM   771  C  CB  . ALA   B 1 5  ? -26.611 5.567   43.739  1.00 33.54  ? 4   ALA   B CB  1 
ATOM   772  N  N   . PHE   B 1 6  ? -25.243 2.531   43.242  1.00 22.02  ? 5   PHE   B N   1 
ATOM   773  C  CA  . PHE   B 1 6  ? -25.081 1.455   42.278  1.00 19.61  ? 5   PHE   B CA  1 
ATOM   774  C  C   . PHE   B 1 6  ? -24.219 0.348   42.865  1.00 20.08  ? 5   PHE   B C   1 
ATOM   775  O  O   . PHE   B 1 6  ? -23.363 0.589   43.719  1.00 24.63  ? 5   PHE   B O   1 
ATOM   776  C  CB  . PHE   B 1 6  ? -24.446 1.950   40.969  1.00 24.57  ? 5   PHE   B CB  1 
ATOM   777  C  CG  . PHE   B 1 6  ? -25.318 2.886   40.191  1.00 21.14  ? 5   PHE   B CG  1 
ATOM   778  C  CD1 . PHE   B 1 6  ? -26.461 2.425   39.555  1.00 29.05  ? 5   PHE   B CD1 1 
ATOM   779  C  CD2 . PHE   B 1 6  ? -24.993 4.231   40.090  1.00 19.78  ? 5   PHE   B CD2 1 
ATOM   780  C  CE1 . PHE   B 1 6  ? -27.274 3.292   38.835  1.00 19.83  ? 5   PHE   B CE1 1 
ATOM   781  C  CE2 . PHE   B 1 6  ? -25.798 5.099   39.374  1.00 38.64  ? 5   PHE   B CE2 1 
ATOM   782  C  CZ  . PHE   B 1 6  ? -26.939 4.628   38.744  1.00 24.32  ? 5   PHE   B CZ  1 
ATOM   783  N  N   . LYS   B 1 7  ? -24.448 -0.864  42.384  1.00 18.60  ? 6   LYS   B N   1 
ATOM   784  C  CA  . LYS   B 1 7  ? -23.691 -2.050  42.743  1.00 19.79  ? 6   LYS   B CA  1 
ATOM   785  C  C   . LYS   B 1 7  ? -23.267 -2.751  41.463  1.00 20.15  ? 6   LYS   B C   1 
ATOM   786  O  O   . LYS   B 1 7  ? -23.894 -2.566  40.414  1.00 16.91  ? 6   LYS   B O   1 
ATOM   787  C  CB  . LYS   B 1 7  ? -24.528 -2.998  43.614  1.00 27.13  ? 6   LYS   B CB  1 
ATOM   788  C  CG  . LYS   B 1 7  ? -25.772 -3.524  42.924  1.00 21.17  ? 6   LYS   B CG  1 
ATOM   789  C  CD  . LYS   B 1 7  ? -26.577 -4.417  43.856  1.00 41.19  ? 6   LYS   B CD  1 
ATOM   790  C  CE  . LYS   B 1 7  ? -27.829 -4.934  43.171  1.00 31.22  ? 6   LYS   B CE  1 
ATOM   791  N  NZ  . LYS   B 1 7  ? -28.708 -3.819  42.715  1.00 26.92  ? 6   LYS   B NZ  1 
ATOM   792  N  N   . PRO   B 1 8  ? -22.201 -3.552  41.510  1.00 25.87  ? 7   PRO   B N   1 
ATOM   793  C  CA  . PRO   B 1 8  ? -21.779 -4.283  40.310  1.00 21.82  ? 7   PRO   B CA  1 
ATOM   794  C  C   . PRO   B 1 8  ? -22.934 -5.104  39.762  1.00 17.00  ? 7   PRO   B C   1 
ATOM   795  O  O   . PRO   B 1 8  ? -23.683 -5.729  40.514  1.00 14.69  ? 7   PRO   B O   1 
ATOM   796  C  CB  . PRO   B 1 8  ? -20.636 -5.171  40.816  1.00 22.84  ? 7   PRO   B CB  1 
ATOM   797  C  CG  . PRO   B 1 8  ? -20.134 -4.478  42.027  1.00 28.83  ? 7   PRO   B CG  1 
ATOM   798  C  CD  . PRO   B 1 8  ? -21.327 -3.838  42.661  1.00 26.47  ? 7   PRO   B CD  1 
ATOM   799  N  N   . GLY   B 1 9  ? -23.095 -5.068  38.440  1.00 19.02  ? 8   GLY   B N   1 
ATOM   800  C  CA  . GLY   B 1 9  ? -24.191 -5.729  37.774  1.00 15.44  ? 8   GLY   B CA  1 
ATOM   801  C  C   . GLY   B 1 9  ? -25.348 -4.824  37.404  1.00 13.31  ? 8   GLY   B C   1 
ATOM   802  O  O   . GLY   B 1 9  ? -26.137 -5.184  36.520  1.00 13.74  ? 8   GLY   B O   1 
ATOM   803  N  N   . ASP   B 1 10 ? -25.480 -3.671  38.060  1.00 15.73  ? 9   ASP   B N   1 
ATOM   804  C  CA  . ASP   B 1 10 ? -26.526 -2.727  37.692  1.00 11.51  ? 9   ASP   B CA  1 
ATOM   805  C  C   . ASP   B 1 10 ? -26.349 -2.286  36.245  1.00 13.92  ? 9   ASP   B C   1 
ATOM   806  O  O   . ASP   B 1 10 ? -25.233 -2.018  35.792  1.00 16.08  ? 9   ASP   B O   1 
ATOM   807  C  CB  . ASP   B 1 10 ? -26.490 -1.503  38.609  1.00 12.02  ? 9   ASP   B CB  1 
ATOM   808  C  CG  . ASP   B 1 10 ? -27.053 -1.778  39.993  1.00 21.34  ? 9   ASP   B CG  1 
ATOM   809  O  OD1 . ASP   B 1 10 ? -27.657 -2.853  40.211  1.00 18.56  ? 9   ASP   B OD1 1 
ATOM   810  O  OD2 . ASP   B 1 10 ? -26.895 -0.893  40.863  1.00 19.62  ? 9   ASP   B OD2 1 
ATOM   811  N  N   . LEU   B 1 11 ? -27.459 -2.213  35.521  1.00 13.04  ? 10  LEU   B N   1 
ATOM   812  C  CA  . LEU   B 1 11 ? -27.464 -1.735  34.147  1.00 14.57  ? 10  LEU   B CA  1 
ATOM   813  C  C   . LEU   B 1 11 ? -27.803 -0.254  34.132  1.00 15.95  ? 10  LEU   B C   1 
ATOM   814  O  O   . LEU   B 1 11 ? -28.669 0.202   34.888  1.00 15.64  ? 10  LEU   B O   1 
ATOM   815  C  CB  . LEU   B 1 11 ? -28.475 -2.507  33.300  1.00 11.70  ? 10  LEU   B CB  1 
ATOM   816  C  CG  . LEU   B 1 11 ? -28.241 -4.023  33.241  1.00 8.52   ? 10  LEU   B CG  1 
ATOM   817  C  CD1 . LEU   B 1 11 ? -29.227 -4.678  32.290  1.00 15.50  ? 10  LEU   B CD1 1 
ATOM   818  C  CD2 . LEU   B 1 11 ? -26.802 -4.321  32.823  1.00 13.59  ? 10  LEU   B CD2 1 
ATOM   819  N  N   . VAL   B 1 12 ? -27.113 0.496   33.272  1.00 12.78  ? 11  VAL   B N   1 
ATOM   820  C  CA  . VAL   B 1 12 ? -27.284 1.939   33.194  1.00 11.37  ? 11  VAL   B CA  1 
ATOM   821  C  C   . VAL   B 1 12 ? -27.179 2.381   31.740  1.00 18.43  ? 11  VAL   B C   1 
ATOM   822  O  O   . VAL   B 1 12 ? -26.779 1.621   30.853  1.00 12.81  ? 11  VAL   B O   1 
ATOM   823  C  CB  . VAL   B 1 12 ? -26.235 2.707   34.032  1.00 13.79  ? 11  VAL   B CB  1 
ATOM   824  C  CG1 . VAL   B 1 12 ? -26.324 2.353   35.515  1.00 16.80  ? 11  VAL   B CG1 1 
ATOM   825  C  CG2 . VAL   B 1 12 ? -24.826 2.444   33.487  1.00 14.21  ? 11  VAL   B CG2 1 
ATOM   826  N  N   . PHE   B 1 13 ? -27.533 3.641   31.511  1.00 12.05  ? 12  PHE   B N   1 
ATOM   827  C  CA  . PHE   B 1 13 ? -27.027 4.390   30.372  1.00 15.51  ? 12  PHE   B CA  1 
ATOM   828  C  C   . PHE   B 1 13 ? -26.000 5.368   30.913  1.00 16.82  ? 12  PHE   B C   1 
ATOM   829  O  O   . PHE   B 1 13 ? -26.286 6.114   31.857  1.00 15.84  ? 12  PHE   B O   1 
ATOM   830  C  CB  . PHE   B 1 13 ? -28.141 5.112   29.618  1.00 14.68  ? 12  PHE   B CB  1 
ATOM   831  C  CG  . PHE   B 1 13 ? -29.050 4.182   28.864  1.00 17.48  ? 12  PHE   B CG  1 
ATOM   832  C  CD1 . PHE   B 1 13 ? -30.208 3.689   29.454  1.00 18.87  ? 12  PHE   B CD1 1 
ATOM   833  C  CD2 . PHE   B 1 13 ? -28.737 3.791   27.570  1.00 16.01  ? 12  PHE   B CD2 1 
ATOM   834  C  CE1 . PHE   B 1 13 ? -31.034 2.827   28.772  1.00 22.58  ? 12  PHE   B CE1 1 
ATOM   835  C  CE2 . PHE   B 1 13 ? -29.556 2.925   26.876  1.00 16.14  ? 12  PHE   B CE2 1 
ATOM   836  C  CZ  . PHE   B 1 13 ? -30.712 2.441   27.475  1.00 18.33  ? 12  PHE   B CZ  1 
ATOM   837  N  N   . ALA   B 1 14 ? -24.798 5.325   30.351  1.00 13.59  ? 13  ALA   B N   1 
ATOM   838  C  CA  . ALA   B 1 14 ? -23.676 6.123   30.819  1.00 14.51  ? 13  ALA   B CA  1 
ATOM   839  C  C   . ALA   B 1 14 ? -23.394 7.218   29.807  1.00 14.78  ? 13  ALA   B C   1 
ATOM   840  O  O   . ALA   B 1 14 ? -23.304 6.946   28.603  1.00 12.69  ? 13  ALA   B O   1 
ATOM   841  C  CB  . ALA   B 1 14 ? -22.430 5.260   31.025  1.00 13.77  ? 13  ALA   B CB  1 
ATOM   842  N  N   . LYS   B 1 15 ? -23.252 8.447   30.301  1.00 13.87  ? 14  LYS   B N   1 
ATOM   843  C  CA  . LYS   B 1 15 ? -23.089 9.622   29.457  1.00 16.92  ? 14  LYS   B CA  1 
ATOM   844  C  C   . LYS   B 1 15 ? -21.661 10.137  29.536  1.00 22.17  ? 14  LYS   B C   1 
ATOM   845  O  O   . LYS   B 1 15 ? -21.148 10.395  30.629  1.00 17.77  ? 14  LYS   B O   1 
ATOM   846  C  CB  . LYS   B 1 15 ? -24.055 10.735  29.868  1.00 15.00  ? 14  LYS   B CB  1 
ATOM   847  C  CG  . LYS   B 1 15 ? -24.015 11.942  28.934  1.00 18.08  ? 14  LYS   B CG  1 
ATOM   848  C  CD  . LYS   B 1 15 ? -24.490 11.569  27.530  1.00 13.46  ? 14  LYS   B CD  1 
ATOM   849  C  CE  . LYS   B 1 15 ? -24.649 12.799  26.644  1.00 25.05  ? 14  LYS   B CE  1 
ATOM   850  N  NZ  . LYS   B 1 15 ? -23.340 13.319  26.164  1.00 21.24  ? 14  LYS   B NZ  1 
ATOM   851  N  N   . MET   B 1 16 ? -21.032 10.308  28.378  1.00 13.25  ? 15  MET   B N   1 
ATOM   852  C  CA  . MET   B 1 16 ? -19.738 10.963  28.289  1.00 17.53  ? 15  MET   B CA  1 
ATOM   853  C  C   . MET   B 1 16 ? -19.812 12.050  27.229  1.00 22.49  ? 15  MET   B C   1 
ATOM   854  O  O   . MET   B 1 16 ? -20.578 11.945  26.266  1.00 18.99  ? 15  MET   B O   1 
ATOM   855  C  CB  . MET   B 1 16 ? -18.621 9.970   27.961  1.00 16.56  ? 15  MET   B CB  1 
ATOM   856  C  CG  . MET   B 1 16 ? -18.470 8.884   29.016  1.00 20.91  ? 15  MET   B CG  1 
ATOM   857  S  SD  . MET   B 1 16 ? -16.853 8.110   28.999  1.00 28.00  ? 15  MET   B SD  1 
ATOM   858  C  CE  . MET   B 1 16 ? -16.865 7.397   27.358  1.00 18.26  ? 15  MET   B CE  1 
ATOM   859  N  N   . LYS   B 1 17 ? -19.020 13.102  27.430  1.00 22.16  ? 16  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 1 17 ? -19.036 14.244  26.525  1.00 19.67  ? 16  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 1 17 ? -18.707 13.802  25.105  1.00 16.48  ? 16  LYS   B C   1 
ATOM   862  O  O   . LYS   B 1 17 ? -17.696 13.139  24.866  1.00 19.86  ? 16  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 1 17 ? -18.041 15.304  27.006  1.00 31.86  ? 16  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 1 17 ? -17.987 16.554  26.145  1.00 40.01  ? 16  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 1 17 ? -19.349 17.225  26.033  1.00 57.08  ? 16  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 1 17 ? -19.426 18.498  26.860  1.00 67.10  ? 16  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 1 17 ? -20.339 19.493  26.227  1.00 55.76  ? 16  LYS   B NZ  1 
ATOM   868  N  N   . GLY   B 1 18 ? -19.583 14.150  24.165  1.00 21.94  ? 17  GLY   B N   1 
ATOM   869  C  CA  . GLY   B 1 18 ? -19.405 13.795  22.773  1.00 23.79  ? 17  GLY   B CA  1 
ATOM   870  C  C   . GLY   B 1 18 ? -20.058 12.498  22.349  1.00 27.29  ? 17  GLY   B C   1 
ATOM   871  O  O   . GLY   B 1 18 ? -19.949 12.128  21.174  1.00 22.85  ? 17  GLY   B O   1 
ATOM   872  N  N   . TYR   B 1 19 ? -20.730 11.800  23.258  1.00 18.75  ? 18  TYR   B N   1 
ATOM   873  C  CA  . TYR   B 1 19 ? -21.345 10.514  22.978  1.00 17.60  ? 18  TYR   B CA  1 
ATOM   874  C  C   . TYR   B 1 19 ? -22.780 10.495  23.478  1.00 18.62  ? 18  TYR   B C   1 
ATOM   875  O  O   . TYR   B 1 19 ? -23.101 11.141  24.480  1.00 16.38  ? 18  TYR   B O   1 
ATOM   876  C  CB  . TYR   B 1 19 ? -20.568 9.374   23.650  1.00 17.70  ? 18  TYR   B CB  1 
ATOM   877  C  CG  . TYR   B 1 19 ? -19.132 9.260   23.205  1.00 16.01  ? 18  TYR   B CG  1 
ATOM   878  C  CD1 . TYR   B 1 19 ? -18.794 8.556   22.053  1.00 16.70  ? 18  TYR   B CD1 1 
ATOM   879  C  CD2 . TYR   B 1 19 ? -18.113 9.855   23.934  1.00 20.36  ? 18  TYR   B CD2 1 
ATOM   880  C  CE1 . TYR   B 1 19 ? -17.475 8.450   21.644  1.00 22.44  ? 18  TYR   B CE1 1 
ATOM   881  C  CE2 . TYR   B 1 19 ? -16.793 9.756   23.529  1.00 17.11  ? 18  TYR   B CE2 1 
ATOM   882  C  CZ  . TYR   B 1 19 ? -16.483 9.054   22.385  1.00 25.29  ? 18  TYR   B CZ  1 
ATOM   883  O  OH  . TYR   B 1 19 ? -15.167 8.955   21.988  1.00 24.48  ? 18  TYR   B OH  1 
ATOM   884  N  N   . PRO   B 1 20 ? -23.659 9.750   22.816  1.00 14.68  ? 19  PRO   B N   1 
ATOM   885  C  CA  . PRO   B 1 20 ? -25.018 9.584   23.341  1.00 18.57  ? 19  PRO   B CA  1 
ATOM   886  C  C   . PRO   B 1 20 ? -25.005 8.750   24.613  1.00 14.80  ? 19  PRO   B C   1 
ATOM   887  O  O   . PRO   B 1 20 ? -24.042 8.044   24.917  1.00 14.17  ? 19  PRO   B O   1 
ATOM   888  C  CB  . PRO   B 1 20 ? -25.747 8.854   22.207  1.00 18.32  ? 19  PRO   B CB  1 
ATOM   889  C  CG  . PRO   B 1 20 ? -24.645 8.032   21.553  1.00 20.83  ? 19  PRO   B CG  1 
ATOM   890  C  CD  . PRO   B 1 20 ? -23.427 8.928   21.607  1.00 19.84  ? 19  PRO   B CD  1 
ATOM   891  N  N   . HIS   B 1 21 ? -26.092 8.856   25.374  1.00 11.05  ? 20  HIS   B N   1 
ATOM   892  C  CA  . HIS   B 1 21 ? -26.264 7.996   26.542  1.00 14.12  ? 20  HIS   B CA  1 
ATOM   893  C  C   . HIS   B 1 21 ? -26.130 6.541   26.122  1.00 10.60  ? 20  HIS   B C   1 
ATOM   894  O  O   . HIS   B 1 21 ? -26.867 6.069   25.252  1.00 15.60  ? 20  HIS   B O   1 
ATOM   895  C  CB  . HIS   B 1 21 ? -27.625 8.248   27.194  1.00 14.25  ? 20  HIS   B CB  1 
ATOM   896  C  CG  . HIS   B 1 21 ? -27.850 9.676   27.588  1.00 16.48  ? 20  HIS   B CG  1 
ATOM   897  N  ND1 . HIS   B 1 21 ? -28.047 10.680  26.664  1.00 17.83  ? 20  HIS   B ND1 1 
ATOM   898  C  CD2 . HIS   B 1 21 ? -27.911 10.268  28.806  1.00 16.88  ? 20  HIS   B CD2 1 
ATOM   899  C  CE1 . HIS   B 1 21 ? -28.218 11.829  27.294  1.00 21.31  ? 20  HIS   B CE1 1 
ATOM   900  N  NE2 . HIS   B 1 21 ? -28.140 11.607  28.594  1.00 18.25  ? 20  HIS   B NE2 1 
ATOM   901  N  N   . TRP   B 1 22 ? -25.173 5.838   26.726  1.00 10.06  ? 21  TRP   B N   1 
ATOM   902  C  CA  . TRP   B 1 22 ? -24.673 4.591   26.165  1.00 12.59  ? 21  TRP   B CA  1 
ATOM   903  C  C   . TRP   B 1 22 ? -25.038 3.399   27.034  1.00 14.05  ? 21  TRP   B C   1 
ATOM   904  O  O   . TRP   B 1 22 ? -24.802 3.435   28.250  1.00 13.71  ? 21  TRP   B O   1 
ATOM   905  C  CB  . TRP   B 1 22 ? -23.148 4.664   26.011  1.00 10.82  ? 21  TRP   B CB  1 
ATOM   906  C  CG  . TRP   B 1 22 ? -22.615 3.756   24.950  1.00 12.27  ? 21  TRP   B CG  1 
ATOM   907  C  CD1 . TRP   B 1 22 ? -22.382 2.408   25.058  1.00 12.31  ? 21  TRP   B CD1 1 
ATOM   908  C  CD2 . TRP   B 1 22 ? -22.250 4.122   23.615  1.00 11.61  ? 21  TRP   B CD2 1 
ATOM   909  N  NE1 . TRP   B 1 22 ? -21.895 1.922   23.871  1.00 12.65  ? 21  TRP   B NE1 1 
ATOM   910  C  CE2 . TRP   B 1 22 ? -21.804 2.952   22.969  1.00 13.57  ? 21  TRP   B CE2 1 
ATOM   911  C  CE3 . TRP   B 1 22 ? -22.261 5.328   22.902  1.00 12.58  ? 21  TRP   B CE3 1 
ATOM   912  C  CZ2 . TRP   B 1 22 ? -21.365 2.951   21.642  1.00 15.95  ? 21  TRP   B CZ2 1 
ATOM   913  C  CZ3 . TRP   B 1 22 ? -21.828 5.327   21.587  1.00 16.54  ? 21  TRP   B CZ3 1 
ATOM   914  C  CH2 . TRP   B 1 22 ? -21.384 4.143   20.971  1.00 17.52  ? 21  TRP   B CH2 1 
ATOM   915  N  N   . PRO   B 1 23 ? -25.563 2.319   26.452  1.00 12.65  ? 22  PRO   B N   1 
ATOM   916  C  CA  . PRO   B 1 23 ? -25.877 1.124   27.253  1.00 12.94  ? 22  PRO   B CA  1 
ATOM   917  C  C   . PRO   B 1 23 ? -24.624 0.557   27.907  1.00 13.27  ? 22  PRO   B C   1 
ATOM   918  O  O   . PRO   B 1 23 ? -23.617 0.302   27.245  1.00 12.07  ? 22  PRO   B O   1 
ATOM   919  C  CB  . PRO   B 1 23 ? -26.468 0.154   26.222  1.00 11.18  ? 22  PRO   B CB  1 
ATOM   920  C  CG  . PRO   B 1 23 ? -25.874 0.602   24.896  1.00 11.45  ? 22  PRO   B CG  1 
ATOM   921  C  CD  . PRO   B 1 23 ? -25.831 2.114   25.017  1.00 8.48   ? 22  PRO   B CD  1 
ATOM   922  N  N   . ALA   B 1 24 ? -24.700 0.326   29.214  1.00 11.00  ? 23  ALA   B N   1 
ATOM   923  C  CA  . ALA   B 1 24 ? -23.504 0.016   29.982  1.00 12.32  ? 23  ALA   B CA  1 
ATOM   924  C  C   . ALA   B 1 24 ? -23.909 -0.718  31.252  1.00 13.09  ? 23  ALA   B C   1 
ATOM   925  O  O   . ALA   B 1 24 ? -25.093 -0.864  31.557  1.00 11.33  ? 23  ALA   B O   1 
ATOM   926  C  CB  . ALA   B 1 24 ? -22.720 1.292   30.309  1.00 12.33  ? 23  ALA   B CB  1 
ATOM   927  N  N   . ARG   B 1 25 ? -22.905 -1.180  31.993  1.00 11.77  ? 24  ARG   B N   1 
ATOM   928  C  CA  . ARG   B 1 25 ? -23.144 -1.832  33.272  1.00 18.14  ? 24  ARG   B CA  1 
ATOM   929  C  C   . ARG   B 1 25 ? -22.058 -1.440  34.260  1.00 16.57  ? 24  ARG   B C   1 
ATOM   930  O  O   . ARG   B 1 25 ? -20.938 -1.094  33.874  1.00 16.13  ? 24  ARG   B O   1 
ATOM   931  C  CB  . ARG   B 1 25 ? -23.194 -3.366  33.137  1.00 11.86  ? 24  ARG   B CB  1 
ATOM   932  C  CG  . ARG   B 1 25 ? -21.857 -4.005  32.766  1.00 14.33  ? 24  ARG   B CG  1 
ATOM   933  C  CD  . ARG   B 1 25 ? -22.021 -5.498  32.531  1.00 13.28  ? 24  ARG   B CD  1 
ATOM   934  N  NE  . ARG   B 1 25 ? -20.738 -6.190  32.466  1.00 18.49  ? 24  ARG   B NE  1 
ATOM   935  C  CZ  . ARG   B 1 25 ? -20.569 -7.390  31.930  1.00 22.64  ? 24  ARG   B CZ  1 
ATOM   936  N  NH1 . ARG   B 1 25 ? -21.577 -8.042  31.370  1.00 13.90  ? 24  ARG   B NH1 1 
ATOM   937  N  NH2 . ARG   B 1 25 ? -19.358 -7.948  31.954  1.00 18.27  ? 24  ARG   B NH2 1 
ATOM   938  N  N   . ILE   B 1 26 ? -22.408 -1.484  35.543  1.00 13.94  ? 25  ILE   B N   1 
ATOM   939  C  CA  . ILE   B 1 26 ? -21.441 -1.294  36.621  1.00 14.49  ? 25  ILE   B CA  1 
ATOM   940  C  C   . ILE   B 1 26 ? -20.646 -2.583  36.779  1.00 19.13  ? 25  ILE   B C   1 
ATOM   941  O  O   . ILE   B 1 26 ? -21.221 -3.649  37.021  1.00 19.05  ? 25  ILE   B O   1 
ATOM   942  C  CB  . ILE   B 1 26 ? -22.143 -0.930  37.937  1.00 16.79  ? 25  ILE   B CB  1 
ATOM   943  C  CG1 . ILE   B 1 26 ? -23.212 0.144   37.715  1.00 22.25  ? 25  ILE   B CG1 1 
ATOM   944  C  CG2 . ILE   B 1 26 ? -21.128 -0.509  38.990  1.00 19.46  ? 25  ILE   B CG2 1 
ATOM   945  C  CD1 . ILE   B 1 26 ? -22.678 1.481   37.301  1.00 33.30  ? 25  ILE   B CD1 1 
ATOM   946  N  N   . ASP   B 1 27 ? -19.328 -2.489  36.647  1.00 14.79  ? 26  ASP   B N   1 
ATOM   947  C  CA  . ASP   B 1 27 ? -18.442 -3.615  36.903  1.00 20.58  ? 26  ASP   B CA  1 
ATOM   948  C  C   . ASP   B 1 27 ? -17.913 -3.552  38.332  1.00 30.06  ? 26  ASP   B C   1 
ATOM   949  O  O   . ASP   B 1 27 ? -18.118 -2.579  39.060  1.00 24.97  ? 26  ASP   B O   1 
ATOM   950  C  CB  . ASP   B 1 27 ? -17.290 -3.643  35.895  1.00 20.71  ? 26  ASP   B CB  1 
ATOM   951  C  CG  . ASP   B 1 27 ? -17.631 -4.439  34.647  1.00 32.55  ? 26  ASP   B CG  1 
ATOM   952  O  OD1 . ASP   B 1 27 ? -18.765 -4.954  34.565  1.00 26.21  ? 26  ASP   B OD1 1 
ATOM   953  O  OD2 . ASP   B 1 27 ? -16.767 -4.561  33.751  1.00 27.77  ? 26  ASP   B OD2 1 
ATOM   954  N  N   . ASP   B 1 28 ? -17.229 -4.619  38.736  1.00 24.37  ? 27  ASP   B N   1 
ATOM   955  C  CA  . ASP   B 1 28 ? -16.762 -4.737  40.111  1.00 35.38  ? 27  ASP   B CA  1 
ATOM   956  C  C   . ASP   B 1 28 ? -15.411 -4.048  40.257  1.00 43.68  ? 27  ASP   B C   1 
ATOM   957  O  O   . ASP   B 1 28 ? -14.467 -4.358  39.520  1.00 33.82  ? 27  ASP   B O   1 
ATOM   958  C  CB  . ASP   B 1 28 ? -16.671 -6.205  40.518  1.00 30.58  ? 27  ASP   B CB  1 
ATOM   959  C  CG  . ASP   B 1 28 ? -16.823 -6.400  42.012  1.00 37.04  ? 27  ASP   B CG  1 
ATOM   960  O  OD1 . ASP   B 1 28 ? -16.444 -5.485  42.780  1.00 36.76  ? 27  ASP   B OD1 1 
ATOM   961  O  OD2 . ASP   B 1 28 ? -17.328 -7.467  42.419  1.00 48.21  ? 27  ASP   B OD2 1 
ATOM   962  N  N   . ILE   B 1 29 ? -15.329 -3.105  41.203  1.00 47.06  ? 28  ILE   B N   1 
ATOM   963  C  CA  . ILE   B 1 29 ? -14.060 -2.443  41.508  1.00 43.87  ? 28  ILE   B CA  1 
ATOM   964  C  C   . ILE   B 1 29 ? -12.996 -3.476  41.846  1.00 48.50  ? 28  ILE   B C   1 
ATOM   965  O  O   . ILE   B 1 29 ? -11.844 -3.377  41.402  1.00 43.20  ? 28  ILE   B O   1 
ATOM   966  C  CB  . ILE   B 1 29 ? -14.247 -1.431  42.655  1.00 44.82  ? 28  ILE   B CB  1 
ATOM   967  C  CG1 . ILE   B 1 29 ? -15.026 -0.206  42.172  1.00 36.25  ? 28  ILE   B CG1 1 
ATOM   968  C  CG2 . ILE   B 1 29 ? -12.903 -1.023  43.244  1.00 45.85  ? 28  ILE   B CG2 1 
ATOM   969  C  CD1 . ILE   B 1 29 ? -15.367 0.769   43.271  1.00 47.81  ? 28  ILE   B CD1 1 
ATOM   970  N  N   . ALA   B 1 30 ? -13.373 -4.498  42.618  1.00 61.39  ? 29  ALA   B N   1 
ATOM   971  C  CA  . ALA   B 1 30 ? -12.440 -5.546  43.014  1.00 60.52  ? 29  ALA   B CA  1 
ATOM   972  C  C   . ALA   B 1 30 ? -11.908 -6.345  41.831  1.00 60.06  ? 29  ALA   B C   1 
ATOM   973  O  O   . ALA   B 1 30 ? -11.009 -7.171  42.022  1.00 73.24  ? 29  ALA   B O   1 
ATOM   974  C  CB  . ALA   B 1 30 ? -13.112 -6.487  44.017  1.00 43.19  ? 29  ALA   B CB  1 
ATOM   975  N  N   . ASP   B 1 31 ? -12.430 -6.123  40.624  1.00 49.64  ? 30  ASP   B N   1 
ATOM   976  C  CA  . ASP   B 1 31 ? -11.955 -6.831  39.443  1.00 55.68  ? 30  ASP   B CA  1 
ATOM   977  C  C   . ASP   B 1 31 ? -10.820 -6.107  38.735  1.00 60.39  ? 30  ASP   B C   1 
ATOM   978  O  O   . ASP   B 1 31 ? -9.977  -6.761  38.110  1.00 73.95  ? 30  ASP   B O   1 
ATOM   979  C  CB  . ASP   B 1 31 ? -13.105 -7.046  38.453  1.00 65.67  ? 30  ASP   B CB  1 
ATOM   980  N  N   . GLY   B 1 32 ? -10.776 -4.782  38.817  1.00 55.79  ? 31  GLY   B N   1 
ATOM   981  C  CA  . GLY   B 1 32 ? -9.803  -3.988  38.082  1.00 65.02  ? 31  GLY   B CA  1 
ATOM   982  C  C   . GLY   B 1 32 ? -8.613  -3.608  38.945  1.00 61.53  ? 31  GLY   B C   1 
ATOM   983  O  O   . GLY   B 1 32 ? -8.762  -3.288  40.125  1.00 46.58  ? 31  GLY   B O   1 
ATOM   984  N  N   . ALA   B 1 33 ? -7.425  -3.644  38.334  1.00 43.01  ? 32  ALA   B N   1 
ATOM   985  C  CA  . ALA   B 1 33 ? -6.208  -3.259  39.042  1.00 32.08  ? 32  ALA   B CA  1 
ATOM   986  C  C   . ALA   B 1 33 ? -6.221  -1.771  39.375  1.00 28.07  ? 32  ALA   B C   1 
ATOM   987  O  O   . ALA   B 1 33 ? -6.049  -1.380  40.536  1.00 44.62  ? 32  ALA   B O   1 
ATOM   988  C  CB  . ALA   B 1 33 ? -4.978  -3.621  38.208  1.00 41.53  ? 32  ALA   B CB  1 
ATOM   989  N  N   . VAL   B 1 34 ? -6.416  -0.921  38.367  1.00 28.52  ? 33  VAL   B N   1 
ATOM   990  C  CA  . VAL   B 1 34 ? -6.599  0.502   38.626  1.00 23.30  ? 33  VAL   B CA  1 
ATOM   991  C  C   . VAL   B 1 34 ? -7.970  0.718   39.249  1.00 28.24  ? 33  VAL   B C   1 
ATOM   992  O  O   . VAL   B 1 34 ? -8.992  0.273   38.711  1.00 33.57  ? 33  VAL   B O   1 
ATOM   993  C  CB  . VAL   B 1 34 ? -6.442  1.322   37.337  1.00 29.24  ? 33  VAL   B CB  1 
ATOM   994  C  CG1 . VAL   B 1 34 ? -6.800  2.779   37.593  1.00 23.58  ? 33  VAL   B CG1 1 
ATOM   995  C  CG2 . VAL   B 1 34 ? -5.023  1.220   36.809  1.00 25.86  ? 33  VAL   B CG2 1 
ATOM   996  N  N   . LYS   B 1 35 ? -7.996  1.388   40.378  1.00 23.14  ? 34  LYS   B N   1 
ATOM   997  C  CA  . LYS   B 1 35 ? -9.217  1.689   41.102  1.00 21.95  ? 34  LYS   B CA  1 
ATOM   998  C  C   . LYS   B 1 35 ? -9.810  3.010   40.622  1.00 25.97  ? 34  LYS   B C   1 
ATOM   999  O  O   . LYS   B 1 35 ? -9.078  3.910   40.197  1.00 27.13  ? 34  LYS   B O   1 
ATOM   1000 C  CB  . LYS   B 1 35 ? -8.934  1.775   42.598  1.00 27.87  ? 34  LYS   B CB  1 
ATOM   1001 C  CG  . LYS   B 1 35 ? -8.144  0.603   43.153  1.00 31.18  ? 34  LYS   B CG  1 
ATOM   1002 C  CD  . LYS   B 1 35 ? -9.035  -0.587  43.446  1.00 40.16  ? 34  LYS   B CD  1 
ATOM   1003 C  CE  . LYS   B 1 35 ? -8.340  -1.537  44.404  1.00 54.45  ? 34  LYS   B CE  1 
ATOM   1004 N  NZ  . LYS   B 1 35 ? -7.725  -0.778  45.536  1.00 51.69  ? 34  LYS   B NZ  1 
ATOM   1005 N  N   . PRO   B 1 36 ? -11.137 3.154   40.672  1.00 33.00  ? 35  PRO   B N   1 
ATOM   1006 C  CA  . PRO   B 1 36 ? -11.740 4.421   40.265  1.00 21.57  ? 35  PRO   B CA  1 
ATOM   1007 C  C   . PRO   B 1 36 ? -11.370 5.525   41.233  1.00 23.63  ? 35  PRO   B C   1 
ATOM   1008 O  O   . PRO   B 1 36 ? -11.099 5.267   42.420  1.00 27.41  ? 35  PRO   B O   1 
ATOM   1009 C  CB  . PRO   B 1 36 ? -13.253 4.123   40.309  1.00 24.88  ? 35  PRO   B CB  1 
ATOM   1010 C  CG  . PRO   B 1 36 ? -13.370 2.627   40.324  1.00 23.87  ? 35  PRO   B CG  1 
ATOM   1011 C  CD  . PRO   B 1 36 ? -12.146 2.147   41.043  1.00 34.17  ? 35  PRO   B CD  1 
ATOM   1012 N  N   . PRO   B 1 37 ? -11.349 6.775   40.781  1.00 25.74  ? 36  PRO   B N   1 
ATOM   1013 C  CA  . PRO   B 1 37 ? -11.223 7.901   41.709  1.00 27.50  ? 36  PRO   B CA  1 
ATOM   1014 C  C   . PRO   B 1 37 ? -12.368 7.883   42.706  1.00 45.35  ? 36  PRO   B C   1 
ATOM   1015 O  O   . PRO   B 1 37 ? -13.372 7.188   42.485  1.00 26.19  ? 36  PRO   B O   1 
ATOM   1016 C  CB  . PRO   B 1 37 ? -11.296 9.130   40.787  1.00 37.66  ? 36  PRO   B CB  1 
ATOM   1017 C  CG  . PRO   B 1 37 ? -10.917 8.621   39.438  1.00 36.58  ? 36  PRO   B CG  1 
ATOM   1018 C  CD  . PRO   B 1 37 ? -11.437 7.216   39.380  1.00 23.67  ? 36  PRO   B CD  1 
ATOM   1019 N  N   . PRO   B 1 38 ? -12.256 8.611   43.819  1.00 42.94  ? 37  PRO   B N   1 
ATOM   1020 C  CA  . PRO   B 1 38 ? -13.322 8.571   44.828  1.00 43.00  ? 37  PRO   B CA  1 
ATOM   1021 C  C   . PRO   B 1 38 ? -14.682 8.889   44.221  1.00 30.13  ? 37  PRO   B C   1 
ATOM   1022 O  O   . PRO   B 1 38 ? -14.813 9.775   43.373  1.00 42.00  ? 37  PRO   B O   1 
ATOM   1023 C  CB  . PRO   B 1 38 ? -12.891 9.639   45.839  1.00 46.19  ? 37  PRO   B CB  1 
ATOM   1024 C  CG  . PRO   B 1 38 ? -11.411 9.716   45.693  1.00 42.87  ? 37  PRO   B CG  1 
ATOM   1025 C  CD  . PRO   B 1 38 ? -11.133 9.471   44.237  1.00 44.62  ? 37  PRO   B CD  1 
ATOM   1026 N  N   . ASN   B 1 39 ? -15.691 8.127   44.642  1.00 27.53  ? 38  ASN   B N   1 
ATOM   1027 C  CA  . ASN   B 1 39 ? -17.085 8.323   44.246  1.00 31.28  ? 38  ASN   B CA  1 
ATOM   1028 C  C   . ASN   B 1 39 ? -17.318 8.081   42.756  1.00 32.07  ? 38  ASN   B C   1 
ATOM   1029 O  O   . ASN   B 1 39 ? -18.296 8.578   42.189  1.00 25.41  ? 38  ASN   B O   1 
ATOM   1030 C  CB  . ASN   B 1 39 ? -17.582 9.720   44.636  1.00 35.21  ? 38  ASN   B CB  1 
ATOM   1031 C  CG  . ASN   B 1 39 ? -17.437 9.993   46.120  1.00 57.36  ? 38  ASN   B CG  1 
ATOM   1032 O  OD1 . ASN   B 1 39 ? -17.639 9.105   46.950  1.00 51.55  ? 38  ASN   B OD1 1 
ATOM   1033 N  ND2 . ASN   B 1 39 ? -17.078 11.226  46.463  1.00 65.59  ? 38  ASN   B ND2 1 
ATOM   1034 N  N   . LYS   B 1 40 ? -16.444 7.322   42.100  1.00 28.45  ? 39  LYS   B N   1 
ATOM   1035 C  CA  . LYS   B 1 40 ? -16.645 6.944   40.711  1.00 16.62  ? 39  LYS   B CA  1 
ATOM   1036 C  C   . LYS   B 1 40 ? -16.741 5.427   40.601  1.00 23.71  ? 39  LYS   B C   1 
ATOM   1037 O  O   . LYS   B 1 40 ? -16.357 4.689   41.516  1.00 20.14  ? 39  LYS   B O   1 
ATOM   1038 C  CB  . LYS   B 1 40 ? -15.524 7.493   39.813  1.00 17.95  ? 39  LYS   B CB  1 
ATOM   1039 C  CG  . LYS   B 1 40 ? -15.532 9.019   39.730  1.00 25.09  ? 39  LYS   B CG  1 
ATOM   1040 C  CD  . LYS   B 1 40 ? -14.773 9.540   38.527  1.00 22.58  ? 39  LYS   B CD  1 
ATOM   1041 C  CE  . LYS   B 1 40 ? -14.969 11.044  38.391  1.00 31.76  ? 39  LYS   B CE  1 
ATOM   1042 N  NZ  . LYS   B 1 40 ? -14.194 11.627  37.259  1.00 40.96  ? 39  LYS   B NZ  1 
ATOM   1043 N  N   . TYR   B 1 41 ? -17.280 4.969   39.470  1.00 18.09  ? 40  TYR   B N   1 
ATOM   1044 C  CA  . TYR   B 1 41 ? -17.542 3.560   39.239  1.00 15.35  ? 40  TYR   B CA  1 
ATOM   1045 C  C   . TYR   B 1 41 ? -16.806 3.071   38.000  1.00 13.19  ? 40  TYR   B C   1 
ATOM   1046 O  O   . TYR   B 1 41 ? -16.580 3.843   37.065  1.00 20.78  ? 40  TYR   B O   1 
ATOM   1047 C  CB  . TYR   B 1 41 ? -19.041 3.293   39.038  1.00 16.87  ? 40  TYR   B CB  1 
ATOM   1048 C  CG  . TYR   B 1 41 ? -19.933 3.596   40.221  1.00 18.41  ? 40  TYR   B CG  1 
ATOM   1049 C  CD1 . TYR   B 1 41 ? -20.486 4.858   40.390  1.00 24.55  ? 40  TYR   B CD1 1 
ATOM   1050 C  CD2 . TYR   B 1 41 ? -20.251 2.607   41.144  1.00 28.76  ? 40  TYR   B CD2 1 
ATOM   1051 C  CE1 . TYR   B 1 41 ? -21.318 5.139   41.465  1.00 31.75  ? 40  TYR   B CE1 1 
ATOM   1052 C  CE2 . TYR   B 1 41 ? -21.083 2.873   42.223  1.00 29.19  ? 40  TYR   B CE2 1 
ATOM   1053 C  CZ  . TYR   B 1 41 ? -21.616 4.139   42.378  1.00 29.68  ? 40  TYR   B CZ  1 
ATOM   1054 O  OH  . TYR   B 1 41 ? -22.444 4.411   43.446  1.00 32.34  ? 40  TYR   B OH  1 
ATOM   1055 N  N   . PRO   B 1 42 ? -16.450 1.785   37.948  1.00 17.92  ? 41  PRO   B N   1 
ATOM   1056 C  CA  . PRO   B 1 42 ? -15.983 1.192   36.687  1.00 15.75  ? 41  PRO   B CA  1 
ATOM   1057 C  C   . PRO   B 1 42 ? -17.178 0.879   35.797  1.00 18.27  ? 41  PRO   B C   1 
ATOM   1058 O  O   . PRO   B 1 42 ? -18.088 0.151   36.199  1.00 18.70  ? 41  PRO   B O   1 
ATOM   1059 C  CB  . PRO   B 1 42 ? -15.261 -0.087  37.138  1.00 16.33  ? 41  PRO   B CB  1 
ATOM   1060 C  CG  . PRO   B 1 42 ? -15.517 -0.220  38.629  1.00 20.68  ? 41  PRO   B CG  1 
ATOM   1061 C  CD  . PRO   B 1 42 ? -16.566 0.775   39.010  1.00 26.14  ? 41  PRO   B CD  1 
ATOM   1062 N  N   . ILE   B 1 43 ? -17.181 1.438   34.590  1.00 12.53  ? 42  ILE   B N   1 
ATOM   1063 C  CA  . ILE   B 1 43 ? -18.314 1.342   33.677  1.00 14.70  ? 42  ILE   B CA  1 
ATOM   1064 C  C   . ILE   B 1 43 ? -17.872 0.560   32.453  1.00 19.51  ? 42  ILE   B C   1 
ATOM   1065 O  O   . ILE   B 1 43 ? -16.933 0.969   31.761  1.00 20.29  ? 42  ILE   B O   1 
ATOM   1066 C  CB  . ILE   B 1 43 ? -18.837 2.724   33.257  1.00 17.33  ? 42  ILE   B CB  1 
ATOM   1067 C  CG1 . ILE   B 1 43 ? -19.186 3.562   34.485  1.00 15.53  ? 42  ILE   B CG1 1 
ATOM   1068 C  CG2 . ILE   B 1 43 ? -20.043 2.560   32.334  1.00 13.74  ? 42  ILE   B CG2 1 
ATOM   1069 C  CD1 . ILE   B 1 43 ? -20.229 2.925   35.374  1.00 15.99  ? 42  ILE   B CD1 1 
ATOM   1070 N  N   . PHE   B 1 44 ? -18.558 -0.544  32.173  1.00 12.91  ? 43  PHE   B N   1 
ATOM   1071 C  CA  . PHE   B 1 44 ? -18.316 -1.336  30.975  1.00 9.46   ? 43  PHE   B CA  1 
ATOM   1072 C  C   . PHE   B 1 44 ? -19.365 -0.991  29.927  1.00 11.24  ? 43  PHE   B C   1 
ATOM   1073 O  O   . PHE   B 1 44 ? -20.567 -1.130  30.181  1.00 12.24  ? 43  PHE   B O   1 
ATOM   1074 C  CB  . PHE   B 1 44 ? -18.357 -2.826  31.303  1.00 11.62  ? 43  PHE   B CB  1 
ATOM   1075 C  CG  . PHE   B 1 44 ? -18.168 -3.716  30.112  1.00 15.27  ? 43  PHE   B CG  1 
ATOM   1076 C  CD1 . PHE   B 1 44 ? -16.901 -3.928  29.592  1.00 13.43  ? 43  PHE   B CD1 1 
ATOM   1077 C  CD2 . PHE   B 1 44 ? -19.252 -4.357  29.528  1.00 18.76  ? 43  PHE   B CD2 1 
ATOM   1078 C  CE1 . PHE   B 1 44 ? -16.709 -4.761  28.500  1.00 22.38  ? 43  PHE   B CE1 1 
ATOM   1079 C  CE2 . PHE   B 1 44 ? -19.074 -5.194  28.428  1.00 14.24  ? 43  PHE   B CE2 1 
ATOM   1080 C  CZ  . PHE   B 1 44 ? -17.797 -5.395  27.915  1.00 14.05  ? 43  PHE   B CZ  1 
ATOM   1081 N  N   . PHE   B 1 45 ? -18.914 -0.562  28.748  1.00 12.60  ? 44  PHE   B N   1 
ATOM   1082 C  CA  . PHE   B 1 45 ? -19.812 -0.133  27.679  1.00 13.75  ? 44  PHE   B CA  1 
ATOM   1083 C  C   . PHE   B 1 45 ? -20.113 -1.310  26.760  1.00 12.40  ? 44  PHE   B C   1 
ATOM   1084 O  O   . PHE   B 1 45 ? -19.191 -1.930  26.218  1.00 10.84  ? 44  PHE   B O   1 
ATOM   1085 C  CB  . PHE   B 1 45 ? -19.198 1.013   26.876  1.00 12.24  ? 44  PHE   B CB  1 
ATOM   1086 C  CG  . PHE   B 1 45 ? -19.065 2.284   27.656  1.00 10.35  ? 44  PHE   B CG  1 
ATOM   1087 C  CD1 . PHE   B 1 45 ? -20.140 3.149   27.778  1.00 13.26  ? 44  PHE   B CD1 1 
ATOM   1088 C  CD2 . PHE   B 1 45 ? -17.876 2.602   28.293  1.00 19.06  ? 44  PHE   B CD2 1 
ATOM   1089 C  CE1 . PHE   B 1 45 ? -20.032 4.328   28.517  1.00 15.75  ? 44  PHE   B CE1 1 
ATOM   1090 C  CE2 . PHE   B 1 45 ? -17.761 3.782   29.033  1.00 22.14  ? 44  PHE   B CE2 1 
ATOM   1091 C  CZ  . PHE   B 1 45 ? -18.847 4.638   29.145  1.00 15.85  ? 44  PHE   B CZ  1 
ATOM   1092 N  N   . PHE   B 1 46 ? -21.397 -1.608  26.579  1.00 12.76  ? 45  PHE   B N   1 
ATOM   1093 C  CA  . PHE   B 1 46 ? -21.785 -2.663  25.654  1.00 9.91   ? 45  PHE   B CA  1 
ATOM   1094 C  C   . PHE   B 1 46 ? -21.497 -2.227  24.224  1.00 10.56  ? 45  PHE   B C   1 
ATOM   1095 O  O   . PHE   B 1 46 ? -21.439 -1.032  23.914  1.00 10.57  ? 45  PHE   B O   1 
ATOM   1096 C  CB  . PHE   B 1 46 ? -23.264 -3.001  25.812  1.00 9.74   ? 45  PHE   B CB  1 
ATOM   1097 C  CG  . PHE   B 1 46 ? -23.591 -3.670  27.116  1.00 12.41  ? 45  PHE   B CG  1 
ATOM   1098 C  CD1 . PHE   B 1 46 ? -23.219 -4.986  27.340  1.00 13.51  ? 45  PHE   B CD1 1 
ATOM   1099 C  CD2 . PHE   B 1 46 ? -24.273 -2.984  28.111  1.00 10.71  ? 45  PHE   B CD2 1 
ATOM   1100 C  CE1 . PHE   B 1 46 ? -23.529 -5.620  28.552  1.00 11.79  ? 45  PHE   B CE1 1 
ATOM   1101 C  CE2 . PHE   B 1 46 ? -24.578 -3.605  29.319  1.00 13.65  ? 45  PHE   B CE2 1 
ATOM   1102 C  CZ  . PHE   B 1 46 ? -24.209 -4.923  29.537  1.00 15.13  ? 45  PHE   B CZ  1 
ATOM   1103 N  N   . GLY   B 1 47 ? -21.290 -3.212  23.354  1.00 9.97   ? 46  GLY   B N   1 
ATOM   1104 C  CA  . GLY   B 1 47 ? -20.950 -2.935  21.973  1.00 12.22  ? 46  GLY   B CA  1 
ATOM   1105 C  C   . GLY   B 1 47 ? -19.464 -2.732  21.774  1.00 21.41  ? 46  GLY   B C   1 
ATOM   1106 O  O   . GLY   B 1 47 ? -18.796 -3.569  21.162  1.00 14.75  ? 46  GLY   B O   1 
ATOM   1107 N  N   . THR   B 1 48 ? -18.933 -1.625  22.299  1.00 11.14  ? 47  THR   B N   1 
ATOM   1108 C  CA  . THR   B 1 48 ? -17.510 -1.328  22.162  1.00 11.48  ? 47  THR   B CA  1 
ATOM   1109 C  C   . THR   B 1 48 ? -16.656 -2.121  23.145  1.00 16.64  ? 47  THR   B C   1 
ATOM   1110 O  O   . THR   B 1 48 ? -15.471 -2.344  22.884  1.00 14.92  ? 47  THR   B O   1 
ATOM   1111 C  CB  . THR   B 1 48 ? -17.259 0.166   22.380  1.00 16.87  ? 47  THR   B CB  1 
ATOM   1112 O  OG1 . THR   B 1 48 ? -17.599 0.494   23.731  1.00 16.06  ? 47  THR   B OG1 1 
ATOM   1113 C  CG2 . THR   B 1 48 ? -18.105 1.004   21.434  1.00 17.27  ? 47  THR   B CG2 1 
ATOM   1114 N  N   . HIS   B 1 49 ? -17.228 -2.517  24.284  1.00 14.57  ? 48  HIS   B N   1 
ATOM   1115 C  CA  . HIS   B 1 49 ? -16.532 -3.304  25.305  1.00 19.93  ? 48  HIS   B CA  1 
ATOM   1116 C  C   . HIS   B 1 49 ? -15.375 -2.537  25.938  1.00 17.52  ? 48  HIS   B C   1 
ATOM   1117 O  O   . HIS   B 1 49 ? -14.422 -3.131  26.448  1.00 21.87  ? 48  HIS   B O   1 
ATOM   1118 C  CB  . HIS   B 1 49 ? -16.059 -4.648  24.742  1.00 13.90  ? 48  HIS   B CB  1 
ATOM   1119 C  CG  . HIS   B 1 49 ? -17.159 -5.439  24.111  1.00 16.37  ? 48  HIS   B CG  1 
ATOM   1120 N  ND1 . HIS   B 1 49 ? -16.925 -6.464  23.223  1.00 16.85  ? 48  HIS   B ND1 1 
ATOM   1121 C  CD2 . HIS   B 1 49 ? -18.505 -5.346  24.233  1.00 14.65  ? 48  HIS   B CD2 1 
ATOM   1122 C  CE1 . HIS   B 1 49 ? -18.078 -6.975  22.830  1.00 14.65  ? 48  HIS   B CE1 1 
ATOM   1123 N  NE2 . HIS   B 1 49 ? -19.053 -6.313  23.427  1.00 15.49  ? 48  HIS   B NE2 1 
ATOM   1124 N  N   . GLU   B 1 50 ? -15.454 -1.215  25.935  1.00 13.35  ? 49  GLU   B N   1 
ATOM   1125 C  CA  A GLU   B 1 50 ? -14.465 -0.429  26.645  0.57 16.13  ? 49  GLU   B CA  1 
ATOM   1126 C  CA  B GLU   B 1 50 ? -14.492 -0.376  26.631  0.43 16.01  ? 49  GLU   B CA  1 
ATOM   1127 C  C   . GLU   B 1 50 ? -14.941 -0.146  28.068  1.00 20.98  ? 49  GLU   B C   1 
ATOM   1128 O  O   . GLU   B 1 50 ? -16.109 -0.336  28.412  1.00 16.06  ? 49  GLU   B O   1 
ATOM   1129 C  CB  A GLU   B 1 50 ? -14.177 0.857   25.876  0.57 18.12  ? 49  GLU   B CB  1 
ATOM   1130 C  CB  B GLU   B 1 50 ? -14.329 0.971   25.925  0.43 17.05  ? 49  GLU   B CB  1 
ATOM   1131 C  CG  A GLU   B 1 50 ? -13.935 0.586   24.393  0.57 27.97  ? 49  GLU   B CG  1 
ATOM   1132 C  CG  B GLU   B 1 50 ? -13.806 0.883   24.501  0.43 26.86  ? 49  GLU   B CG  1 
ATOM   1133 C  CD  A GLU   B 1 50 ? -13.408 1.785   23.647  0.57 25.94  ? 49  GLU   B CD  1 
ATOM   1134 C  CD  B GLU   B 1 50 ? -12.558 0.034   24.392  0.43 25.47  ? 49  GLU   B CD  1 
ATOM   1135 O  OE1 A GLU   B 1 50 ? -12.830 2.679   24.299  0.57 34.39  ? 49  GLU   B OE1 1 
ATOM   1136 O  OE1 B GLU   B 1 50 ? -12.663 -1.122  23.930  0.43 44.51  ? 49  GLU   B OE1 1 
ATOM   1137 O  OE2 A GLU   B 1 50 ? -13.568 1.830   22.409  0.57 24.17  ? 49  GLU   B OE2 1 
ATOM   1138 O  OE2 B GLU   B 1 50 ? -11.472 0.516   24.779  0.43 25.80  ? 49  GLU   B OE2 1 
ATOM   1139 N  N   . THR   B 1 51 ? -14.000 0.284   28.907  1.00 20.22  ? 50  THR   B N   1 
ATOM   1140 C  CA  . THR   B 1 51 ? -14.285 0.570   30.306  1.00 15.81  ? 50  THR   B CA  1 
ATOM   1141 C  C   . THR   B 1 51 ? -13.765 1.955   30.659  1.00 17.58  ? 50  THR   B C   1 
ATOM   1142 O  O   . THR   B 1 51 ? -12.677 2.349   30.223  1.00 23.16  ? 50  THR   B O   1 
ATOM   1143 C  CB  . THR   B 1 51 ? -13.662 -0.484  31.240  1.00 16.93  ? 50  THR   B CB  1 
ATOM   1144 O  OG1 . THR   B 1 51 ? -14.115 -1.794  30.871  1.00 22.90  ? 50  THR   B OG1 1 
ATOM   1145 C  CG2 . THR   B 1 51 ? -14.079 -0.236  32.680  1.00 30.05  ? 50  THR   B CG2 1 
ATOM   1146 N  N   . ALA   B 1 52 ? -14.544 2.692   31.451  1.00 16.45  ? 51  ALA   B N   1 
ATOM   1147 C  CA  . ALA   B 1 52 ? -14.155 4.015   31.914  1.00 18.66  ? 51  ALA   B CA  1 
ATOM   1148 C  C   . ALA   B 1 52 ? -14.606 4.183   33.357  1.00 17.54  ? 51  ALA   B C   1 
ATOM   1149 O  O   . ALA   B 1 52 ? -15.343 3.356   33.899  1.00 17.24  ? 51  ALA   B O   1 
ATOM   1150 C  CB  . ALA   B 1 52 ? -14.751 5.120   31.032  1.00 23.63  ? 51  ALA   B CB  1 
ATOM   1151 N  N   . PHE   B 1 53 ? -14.156 5.270   33.979  1.00 15.75  ? 52  PHE   B N   1 
ATOM   1152 C  CA  . PHE   B 1 53 ? -14.532 5.612   35.346  1.00 15.66  ? 52  PHE   B CA  1 
ATOM   1153 C  C   . PHE   B 1 53 ? -15.496 6.790   35.296  1.00 17.06  ? 52  PHE   B C   1 
ATOM   1154 O  O   . PHE   B 1 53 ? -15.155 7.850   34.757  1.00 17.35  ? 52  PHE   B O   1 
ATOM   1155 C  CB  . PHE   B 1 53 ? -13.303 5.957   36.191  1.00 13.98  ? 52  PHE   B CB  1 
ATOM   1156 C  CG  . PHE   B 1 53 ? -12.375 4.795   36.428  1.00 17.28  ? 52  PHE   B CG  1 
ATOM   1157 C  CD1 . PHE   B 1 53 ? -12.871 3.543   36.737  1.00 24.29  ? 52  PHE   B CD1 1 
ATOM   1158 C  CD2 . PHE   B 1 53 ? -11.003 4.963   36.342  1.00 24.39  ? 52  PHE   B CD2 1 
ATOM   1159 C  CE1 . PHE   B 1 53 ? -12.017 2.478   36.960  1.00 30.79  ? 52  PHE   B CE1 1 
ATOM   1160 C  CE2 . PHE   B 1 53 ? -10.147 3.904   36.563  1.00 29.39  ? 52  PHE   B CE2 1 
ATOM   1161 C  CZ  . PHE   B 1 53 ? -10.654 2.659   36.870  1.00 25.51  ? 52  PHE   B CZ  1 
ATOM   1162 N  N   . LEU   B 1 54 ? -16.699 6.603   35.841  1.00 12.81  ? 53  LEU   B N   1 
ATOM   1163 C  CA  . LEU   B 1 54 ? -17.725 7.634   35.823  1.00 15.70  ? 53  LEU   B CA  1 
ATOM   1164 C  C   . LEU   B 1 54 ? -18.397 7.729   37.183  1.00 17.55  ? 53  LEU   B C   1 
ATOM   1165 O  O   . LEU   B 1 54 ? -18.519 6.735   37.908  1.00 18.85  ? 53  LEU   B O   1 
ATOM   1166 C  CB  . LEU   B 1 54 ? -18.790 7.363   34.746  1.00 13.18  ? 53  LEU   B CB  1 
ATOM   1167 C  CG  . LEU   B 1 54 ? -18.316 7.416   33.290  1.00 14.08  ? 53  LEU   B CG  1 
ATOM   1168 C  CD1 . LEU   B 1 54 ? -19.469 7.086   32.359  1.00 16.49  ? 53  LEU   B CD1 1 
ATOM   1169 C  CD2 . LEU   B 1 54 ? -17.735 8.786   32.968  1.00 21.88  ? 53  LEU   B CD2 1 
ATOM   1170 N  N   . GLY   B 1 55 ? -18.833 8.942   37.517  1.00 15.71  ? 54  GLY   B N   1 
ATOM   1171 C  CA  . GLY   B 1 55 ? -19.559 9.186   38.743  1.00 14.66  ? 54  GLY   B CA  1 
ATOM   1172 C  C   . GLY   B 1 55 ? -21.053 9.282   38.503  1.00 25.64  ? 54  GLY   B C   1 
ATOM   1173 O  O   . GLY   B 1 55 ? -21.521 9.283   37.357  1.00 15.33  ? 54  GLY   B O   1 
ATOM   1174 N  N   . PRO   B 1 56 ? -21.828 9.385   39.589  1.00 19.21  ? 55  PRO   B N   1 
ATOM   1175 C  CA  . PRO   B 1 56 ? -23.297 9.359   39.469  1.00 16.16  ? 55  PRO   B CA  1 
ATOM   1176 C  C   . PRO   B 1 56 ? -23.878 10.387  38.510  1.00 12.92  ? 55  PRO   B C   1 
ATOM   1177 O  O   . PRO   B 1 56 ? -24.915 10.116  37.890  1.00 15.14  ? 55  PRO   B O   1 
ATOM   1178 C  CB  . PRO   B 1 56 ? -23.762 9.615   40.912  1.00 21.57  ? 55  PRO   B CB  1 
ATOM   1179 C  CG  . PRO   B 1 56 ? -22.643 9.138   41.758  1.00 20.58  ? 55  PRO   B CG  1 
ATOM   1180 C  CD  . PRO   B 1 56 ? -21.386 9.443   40.993  1.00 23.53  ? 55  PRO   B CD  1 
ATOM   1181 N  N   . LYS   B 1 57 ? -23.241 11.551  38.344  1.00 15.86  ? 56  LYS   B N   1 
ATOM   1182 C  CA  . LYS   B 1 57 ? -23.808 12.566  37.461  1.00 15.00  ? 56  LYS   B CA  1 
ATOM   1183 C  C   . LYS   B 1 57 ? -23.941 12.077  36.025  1.00 17.83  ? 56  LYS   B C   1 
ATOM   1184 O  O   . LYS   B 1 57 ? -24.745 12.628  35.265  1.00 16.41  ? 56  LYS   B O   1 
ATOM   1185 C  CB  . LYS   B 1 57 ? -22.962 13.841  37.497  1.00 21.12  ? 56  LYS   B CB  1 
ATOM   1186 C  CG  . LYS   B 1 57 ? -21.565 13.678  36.903  1.00 23.13  ? 56  LYS   B CG  1 
ATOM   1187 C  CD  . LYS   B 1 57 ? -20.808 15.002  36.890  1.00 25.94  ? 56  LYS   B CD  1 
ATOM   1188 C  CE  . LYS   B 1 57 ? -19.446 14.846  36.239  1.00 37.34  ? 56  LYS   B CE  1 
ATOM   1189 N  NZ  . LYS   B 1 57 ? -18.866 16.159  35.847  1.00 38.18  ? 56  LYS   B NZ  1 
ATOM   1190 N  N   . ASP   B 1 58 ? -23.187 11.047  35.640  1.00 18.70  ? 57  ASP   B N   1 
ATOM   1191 C  CA  . ASP   B 1 58 ? -23.205 10.535  34.278  1.00 15.61  ? 57  ASP   B CA  1 
ATOM   1192 C  C   . ASP   B 1 58 ? -23.915 9.189   34.147  1.00 15.98  ? 57  ASP   B C   1 
ATOM   1193 O  O   . ASP   B 1 58 ? -23.842 8.571   33.081  1.00 19.04  ? 57  ASP   B O   1 
ATOM   1194 C  CB  . ASP   B 1 58 ? -21.771 10.419  33.751  1.00 16.09  ? 57  ASP   B CB  1 
ATOM   1195 C  CG  . ASP   B 1 58 ? -21.113 11.774  33.547  1.00 24.14  ? 57  ASP   B CG  1 
ATOM   1196 O  OD1 . ASP   B 1 58 ? -21.784 12.690  33.027  1.00 21.24  ? 57  ASP   B OD1 1 
ATOM   1197 O  OD2 . ASP   B 1 58 ? -19.927 11.921  33.912  1.00 31.48  ? 57  ASP   B OD2 1 
ATOM   1198 N  N   . LEU   B 1 59 ? -24.608 8.720   35.187  1.00 12.09  ? 58  LEU   B N   1 
ATOM   1199 C  CA  . LEU   B 1 59 ? -25.156 7.365   35.208  1.00 12.19  ? 58  LEU   B CA  1 
ATOM   1200 C  C   . LEU   B 1 59 ? -26.667 7.421   35.382  1.00 13.69  ? 58  LEU   B C   1 
ATOM   1201 O  O   . LEU   B 1 59 ? -27.167 7.947   36.385  1.00 16.08  ? 58  LEU   B O   1 
ATOM   1202 C  CB  . LEU   B 1 59 ? -24.504 6.533   36.317  1.00 8.67   ? 58  LEU   B CB  1 
ATOM   1203 C  CG  . LEU   B 1 59 ? -22.979 6.458   36.216  1.00 13.36  ? 58  LEU   B CG  1 
ATOM   1204 C  CD1 . LEU   B 1 59 ? -22.398 5.741   37.418  1.00 16.02  ? 58  LEU   B CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 59 ? -22.554 5.784   34.909  1.00 17.65  ? 58  LEU   B CD2 1 
ATOM   1206 N  N   . PHE   B 1 60 ? -27.389 6.887   34.398  1.00 14.20  ? 59  PHE   B N   1 
ATOM   1207 C  CA  . PHE   B 1 60 ? -28.846 6.858   34.382  1.00 11.10  ? 59  PHE   B CA  1 
ATOM   1208 C  C   . PHE   B 1 60 ? -29.333 5.430   34.565  1.00 16.69  ? 59  PHE   B C   1 
ATOM   1209 O  O   . PHE   B 1 60 ? -29.009 4.567   33.736  1.00 16.60  ? 59  PHE   B O   1 
ATOM   1210 C  CB  . PHE   B 1 60 ? -29.370 7.430   33.068  1.00 17.19  ? 59  PHE   B CB  1 
ATOM   1211 C  CG  . PHE   B 1 60 ? -29.022 8.881   32.858  1.00 18.32  ? 59  PHE   B CG  1 
ATOM   1212 C  CD1 . PHE   B 1 60 ? -27.734 9.259   32.486  1.00 16.82  ? 59  PHE   B CD1 1 
ATOM   1213 C  CD2 . PHE   B 1 60 ? -29.981 9.862   33.027  1.00 19.27  ? 59  PHE   B CD2 1 
ATOM   1214 C  CE1 . PHE   B 1 60 ? -27.412 10.606  32.296  1.00 14.97  ? 59  PHE   B CE1 1 
ATOM   1215 C  CE2 . PHE   B 1 60 ? -29.671 11.211  32.827  1.00 21.19  ? 59  PHE   B CE2 1 
ATOM   1216 C  CZ  . PHE   B 1 60 ? -28.387 11.576  32.465  1.00 15.73  ? 59  PHE   B CZ  1 
ATOM   1217 N  N   . PRO   B 1 61 ? -30.121 5.139   35.600  1.00 15.07  ? 60  PRO   B N   1 
ATOM   1218 C  CA  . PRO   B 1 61 ? -30.621 3.769   35.792  1.00 18.73  ? 60  PRO   B CA  1 
ATOM   1219 C  C   . PRO   B 1 61 ? -31.351 3.261   34.554  1.00 13.37  ? 60  PRO   B C   1 
ATOM   1220 O  O   . PRO   B 1 61 ? -32.130 3.981   33.925  1.00 16.52  ? 60  PRO   B O   1 
ATOM   1221 C  CB  . PRO   B 1 61 ? -31.562 3.902   36.995  1.00 18.24  ? 60  PRO   B CB  1 
ATOM   1222 C  CG  . PRO   B 1 61 ? -31.018 5.079   37.756  1.00 20.94  ? 60  PRO   B CG  1 
ATOM   1223 C  CD  . PRO   B 1 61 ? -30.499 6.034   36.706  1.00 22.14  ? 60  PRO   B CD  1 
ATOM   1224 N  N   . TYR   B 1 62 ? -31.092 1.996   34.215  1.00 15.89  ? 61  TYR   B N   1 
ATOM   1225 C  CA  . TYR   B 1 62 ? -31.481 1.468   32.909  1.00 14.70  ? 61  TYR   B CA  1 
ATOM   1226 C  C   . TYR   B 1 62 ? -32.994 1.440   32.728  1.00 16.88  ? 61  TYR   B C   1 
ATOM   1227 O  O   . TYR   B 1 62 ? -33.509 1.878   31.693  1.00 17.53  ? 61  TYR   B O   1 
ATOM   1228 C  CB  . TYR   B 1 62 ? -30.898 0.066   32.721  1.00 16.78  ? 61  TYR   B CB  1 
ATOM   1229 C  CG  . TYR   B 1 62 ? -31.380 -0.636  31.477  1.00 14.28  ? 61  TYR   B CG  1 
ATOM   1230 C  CD1 . TYR   B 1 62 ? -30.898 -0.278  30.223  1.00 16.46  ? 61  TYR   B CD1 1 
ATOM   1231 C  CD2 . TYR   B 1 62 ? -32.316 -1.663  31.554  1.00 21.62  ? 61  TYR   B CD2 1 
ATOM   1232 C  CE1 . TYR   B 1 62 ? -31.337 -0.919  29.078  1.00 27.23  ? 61  TYR   B CE1 1 
ATOM   1233 C  CE2 . TYR   B 1 62 ? -32.759 -2.315  30.415  1.00 33.30  ? 61  TYR   B CE2 1 
ATOM   1234 C  CZ  . TYR   B 1 62 ? -32.264 -1.937  29.180  1.00 31.52  ? 61  TYR   B CZ  1 
ATOM   1235 O  OH  . TYR   B 1 62 ? -32.701 -2.576  28.041  1.00 35.27  ? 61  TYR   B OH  1 
ATOM   1236 N  N   . ASP   B 1 63 ? -33.722 0.907   33.714  1.00 19.00  ? 62  ASP   B N   1 
ATOM   1237 C  CA  . ASP   B 1 63 ? -35.148 0.641   33.528  1.00 19.73  ? 62  ASP   B CA  1 
ATOM   1238 C  C   . ASP   B 1 63 ? -35.922 1.923   33.237  1.00 29.66  ? 62  ASP   B C   1 
ATOM   1239 O  O   . ASP   B 1 63 ? -36.712 1.983   32.287  1.00 23.71  ? 62  ASP   B O   1 
ATOM   1240 C  CB  . ASP   B 1 63 ? -35.720 -0.064  34.762  1.00 22.18  ? 62  ASP   B CB  1 
ATOM   1241 C  CG  . ASP   B 1 63 ? -35.432 -1.557  34.770  1.00 38.94  ? 62  ASP   B CG  1 
ATOM   1242 O  OD1 . ASP   B 1 63 ? -35.323 -2.144  33.677  1.00 39.67  ? 62  ASP   B OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 63 ? -35.326 -2.142  35.871  1.00 50.11  ? 62  ASP   B OD2 1 
ATOM   1244 N  N   . LYS   B 1 64 ? -35.699 2.968   34.038  1.00 20.10  ? 63  LYS   B N   1 
ATOM   1245 C  CA  . LYS   B 1 64 ? -36.476 4.192   33.879  1.00 19.24  ? 63  LYS   B CA  1 
ATOM   1246 C  C   . LYS   B 1 64 ? -36.085 4.993   32.640  1.00 23.06  ? 63  LYS   B C   1 
ATOM   1247 O  O   . LYS   B 1 64 ? -36.862 5.848   32.210  1.00 22.44  ? 63  LYS   B O   1 
ATOM   1248 C  CB  . LYS   B 1 64 ? -36.331 5.074   35.121  1.00 25.80  ? 63  LYS   B CB  1 
ATOM   1249 C  CG  . LYS   B 1 64 ? -36.972 4.511   36.393  1.00 32.35  ? 63  LYS   B CG  1 
ATOM   1250 C  CD  . LYS   B 1 64 ? -38.483 4.387   36.271  1.00 42.51  ? 63  LYS   B CD  1 
ATOM   1251 C  CE  . LYS   B 1 64 ? -39.150 4.399   37.645  1.00 42.23  ? 63  LYS   B CE  1 
ATOM   1252 N  NZ  . LYS   B 1 64 ? -38.517 3.432   38.589  1.00 48.28  ? 63  LYS   B NZ  1 
ATOM   1253 N  N   . SER   B 1 65 ? -34.915 4.738   32.051  1.00 15.43  ? 64  SER   B N   1 
ATOM   1254 C  CA  . SER   B 1 65 ? -34.413 5.555   30.954  1.00 16.75  ? 64  SER   B CA  1 
ATOM   1255 C  C   . SER   B 1 65 ? -34.345 4.830   29.616  1.00 21.44  ? 64  SER   B C   1 
ATOM   1256 O  O   . SER   B 1 65 ? -33.958 5.450   28.620  1.00 18.93  ? 64  SER   B O   1 
ATOM   1257 C  CB  . SER   B 1 65 ? -33.020 6.098   31.299  1.00 21.20  ? 64  SER   B CB  1 
ATOM   1258 O  OG  . SER   B 1 65 ? -33.104 7.162   32.236  1.00 32.82  ? 64  SER   B OG  1 
ATOM   1259 N  N   . LYS   B 1 66 ? -34.707 3.544   29.557  1.00 14.97  ? 65  LYS   B N   1 
ATOM   1260 C  CA  . LYS   B 1 66 ? -34.479 2.787   28.328  1.00 23.19  ? 65  LYS   B CA  1 
ATOM   1261 C  C   . LYS   B 1 66 ? -35.409 3.221   27.203  1.00 20.92  ? 65  LYS   B C   1 
ATOM   1262 O  O   . LYS   B 1 66 ? -35.028 3.145   26.030  1.00 25.17  ? 65  LYS   B O   1 
ATOM   1263 C  CB  . LYS   B 1 66 ? -34.621 1.287   28.584  1.00 21.06  ? 65  LYS   B CB  1 
ATOM   1264 C  CG  . LYS   B 1 66 ? -35.972 0.852   29.107  1.00 26.67  ? 65  LYS   B CG  1 
ATOM   1265 C  CD  . LYS   B 1 66 ? -36.178 -0.634  28.863  1.00 39.13  ? 65  LYS   B CD  1 
ATOM   1266 C  CE  . LYS   B 1 66 ? -37.200 -1.219  29.824  1.00 31.28  ? 65  LYS   B CE  1 
ATOM   1267 N  NZ  . LYS   B 1 66 ? -38.336 -0.289  30.085  1.00 49.73  ? 65  LYS   B NZ  1 
ATOM   1268 N  N   . ASP   B 1 67 ? -36.620 3.679   27.525  1.00 22.16  ? 66  ASP   B N   1 
ATOM   1269 C  CA  . ASP   B 1 67 ? -37.517 4.136   26.467  1.00 25.31  ? 66  ASP   B CA  1 
ATOM   1270 C  C   . ASP   B 1 67 ? -36.962 5.371   25.770  1.00 29.58  ? 66  ASP   B C   1 
ATOM   1271 O  O   . ASP   B 1 67 ? -37.102 5.518   24.551  1.00 28.67  ? 66  ASP   B O   1 
ATOM   1272 C  CB  . ASP   B 1 67 ? -38.910 4.412   27.035  1.00 33.26  ? 66  ASP   B CB  1 
ATOM   1273 C  CG  . ASP   B 1 67 ? -39.686 3.138   27.321  1.00 53.73  ? 66  ASP   B CG  1 
ATOM   1274 O  OD1 . ASP   B 1 67 ? -39.470 2.134   26.606  1.00 52.79  ? 66  ASP   B OD1 1 
ATOM   1275 O  OD2 . ASP   B 1 67 ? -40.514 3.138   28.257  1.00 68.12  ? 66  ASP   B OD2 1 
ATOM   1276 N  N   . LYS   B 1 68 ? -36.314 6.260   26.521  1.00 21.98  ? 67  LYS   B N   1 
ATOM   1277 C  CA  . LYS   B 1 68 ? -35.755 7.470   25.929  1.00 23.81  ? 67  LYS   B CA  1 
ATOM   1278 C  C   . LYS   B 1 68 ? -34.418 7.196   25.248  1.00 29.34  ? 67  LYS   B C   1 
ATOM   1279 O  O   . LYS   B 1 68 ? -34.183 7.646   24.120  1.00 23.65  ? 67  LYS   B O   1 
ATOM   1280 C  CB  . LYS   B 1 68 ? -35.599 8.547   27.006  1.00 21.01  ? 67  LYS   B CB  1 
ATOM   1281 C  CG  . LYS   B 1 68 ? -35.144 9.910   26.489  1.00 30.77  ? 67  LYS   B CG  1 
ATOM   1282 C  CD  . LYS   B 1 68 ? -35.346 10.992  27.549  1.00 48.30  ? 67  LYS   B CD  1 
ATOM   1283 C  CE  . LYS   B 1 68 ? -34.760 12.331  27.106  1.00 39.90  ? 67  LYS   B CE  1 
ATOM   1284 N  NZ  . LYS   B 1 68 ? -35.342 12.805  25.817  1.00 41.94  ? 67  LYS   B NZ  1 
ATOM   1285 N  N   . TYR   B 1 69 ? -33.531 6.453   25.913  1.00 19.36  ? 68  TYR   B N   1 
ATOM   1286 C  CA  . TYR   B 1 69 ? -32.153 6.316   25.461  1.00 15.42  ? 68  TYR   B CA  1 
ATOM   1287 C  C   . TYR   B 1 69 ? -31.874 5.019   24.709  1.00 15.60  ? 68  TYR   B C   1 
ATOM   1288 O  O   . TYR   B 1 69 ? -30.806 4.902   24.099  1.00 17.89  ? 68  TYR   B O   1 
ATOM   1289 C  CB  . TYR   B 1 69 ? -31.198 6.418   26.658  1.00 18.11  ? 68  TYR   B CB  1 
ATOM   1290 C  CG  . TYR   B 1 69 ? -31.216 7.775   27.328  1.00 19.72  ? 68  TYR   B CG  1 
ATOM   1291 C  CD1 . TYR   B 1 69 ? -31.375 8.941   26.579  1.00 18.39  ? 68  TYR   B CD1 1 
ATOM   1292 C  CD2 . TYR   B 1 69 ? -31.092 7.894   28.708  1.00 21.15  ? 68  TYR   B CD2 1 
ATOM   1293 C  CE1 . TYR   B 1 69 ? -31.397 10.189  27.191  1.00 17.04  ? 68  TYR   B CE1 1 
ATOM   1294 C  CE2 . TYR   B 1 69 ? -31.112 9.139   29.327  1.00 16.86  ? 68  TYR   B CE2 1 
ATOM   1295 C  CZ  . TYR   B 1 69 ? -31.264 10.278  28.564  1.00 21.49  ? 68  TYR   B CZ  1 
ATOM   1296 O  OH  . TYR   B 1 69 ? -31.285 11.510  29.180  1.00 22.16  ? 68  TYR   B OH  1 
ATOM   1297 N  N   . GLY   B 1 70 ? -32.788 4.053   24.738  1.00 19.66  ? 69  GLY   B N   1 
ATOM   1298 C  CA  . GLY   B 1 70 ? -32.551 2.774   24.092  1.00 17.07  ? 69  GLY   B CA  1 
ATOM   1299 C  C   . GLY   B 1 70 ? -32.939 2.722   22.629  1.00 20.57  ? 69  GLY   B C   1 
ATOM   1300 O  O   . GLY   B 1 70 ? -33.246 1.649   22.103  1.00 35.14  ? 69  GLY   B O   1 
ATOM   1301 N  N   . LYS   B 1 71 ? -32.925 3.868   21.958  1.00 17.28  ? 70  LYS   B N   1 
ATOM   1302 C  CA  . LYS   B 1 71 ? -33.280 3.945   20.548  1.00 18.21  ? 70  LYS   B CA  1 
ATOM   1303 C  C   . LYS   B 1 71 ? -32.026 3.823   19.690  1.00 18.63  ? 70  LYS   B C   1 
ATOM   1304 O  O   . LYS   B 1 71 ? -30.965 4.319   20.073  1.00 18.75  ? 70  LYS   B O   1 
ATOM   1305 C  CB  . LYS   B 1 71 ? -33.986 5.262   20.236  1.00 27.17  ? 70  LYS   B CB  1 
ATOM   1306 C  CG  . LYS   B 1 71 ? -35.338 5.420   20.928  1.00 30.61  ? 70  LYS   B CG  1 
ATOM   1307 C  CD  . LYS   B 1 71 ? -35.855 6.850   20.810  1.00 42.85  ? 70  LYS   B CD  1 
ATOM   1308 C  CE  . LYS   B 1 71 ? -37.209 7.020   21.494  1.00 45.53  ? 70  LYS   B CE  1 
ATOM   1309 N  NZ  . LYS   B 1 71 ? -38.350 6.819   20.553  1.00 57.54  ? 70  LYS   B NZ  1 
ATOM   1310 N  N   . PRO   B 1 72 ? -32.118 3.156   18.542  1.00 21.25  ? 71  PRO   B N   1 
ATOM   1311 C  CA  . PRO   B 1 72 ? -30.927 2.973   17.702  1.00 19.87  ? 71  PRO   B CA  1 
ATOM   1312 C  C   . PRO   B 1 72 ? -30.393 4.297   17.170  1.00 29.49  ? 71  PRO   B C   1 
ATOM   1313 O  O   . PRO   B 1 72 ? -31.134 5.268   16.992  1.00 22.21  ? 71  PRO   B O   1 
ATOM   1314 C  CB  . PRO   B 1 72 ? -31.433 2.081   16.560  1.00 23.65  ? 71  PRO   B CB  1 
ATOM   1315 C  CG  . PRO   B 1 72 ? -32.653 1.417   17.101  1.00 28.94  ? 71  PRO   B CG  1 
ATOM   1316 C  CD  . PRO   B 1 72 ? -33.281 2.418   18.022  1.00 21.28  ? 71  PRO   B CD  1 
ATOM   1317 N  N   . ASN   B 1 73 ? -29.083 4.327   16.921  1.00 16.82  ? 72  ASN   B N   1 
ATOM   1318 C  CA  . ASN   B 1 73 ? -28.446 5.447   16.240  1.00 15.71  ? 72  ASN   B CA  1 
ATOM   1319 C  C   . ASN   B 1 73 ? -27.239 4.919   15.473  1.00 19.34  ? 72  ASN   B C   1 
ATOM   1320 O  O   . ASN   B 1 73 ? -26.926 3.728   15.524  1.00 18.66  ? 72  ASN   B O   1 
ATOM   1321 C  CB  . ASN   B 1 73 ? -28.054 6.564   17.217  1.00 16.68  ? 72  ASN   B CB  1 
ATOM   1322 C  CG  . ASN   B 1 73 ? -27.009 6.133   18.241  1.00 19.34  ? 72  ASN   B CG  1 
ATOM   1323 O  OD1 . ASN   B 1 73 ? -25.911 5.690   17.896  1.00 17.60  ? 72  ASN   B OD1 1 
ATOM   1324 N  ND2 . ASN   B 1 73 ? -27.334 6.322   19.517  1.00 17.19  ? 72  ASN   B ND2 1 
ATOM   1325 N  N   . LYS   B 1 74 ? -26.546 5.824   14.774  1.00 16.27  ? 73  LYS   B N   1 
ATOM   1326 C  CA  . LYS   B 1 74 ? -25.473 5.455   13.854  1.00 15.03  ? 73  LYS   B CA  1 
ATOM   1327 C  C   . LYS   B 1 74 ? -24.081 5.563   14.464  1.00 13.80  ? 73  LYS   B C   1 
ATOM   1328 O  O   . LYS   B 1 74 ? -23.090 5.450   13.736  1.00 14.38  ? 73  LYS   B O   1 
ATOM   1329 C  CB  . LYS   B 1 74 ? -25.538 6.319   12.593  1.00 26.81  ? 73  LYS   B CB  1 
ATOM   1330 C  CG  . LYS   B 1 74 ? -26.862 6.271   11.856  1.00 30.89  ? 73  LYS   B CG  1 
ATOM   1331 C  CD  . LYS   B 1 74 ? -27.331 4.850   11.643  1.00 29.13  ? 73  LYS   B CD  1 
ATOM   1332 C  CE  . LYS   B 1 74 ? -28.602 4.818   10.812  1.00 35.35  ? 73  LYS   B CE  1 
ATOM   1333 N  NZ  . LYS   B 1 74 ? -29.205 3.457   10.771  1.00 38.64  ? 73  LYS   B NZ  1 
ATOM   1334 N  N   . ARG   B 1 75 ? -23.974 5.789   15.768  1.00 14.48  ? 74  ARG   B N   1 
ATOM   1335 C  CA  . ARG   B 1 75 ? -22.661 5.915   16.383  1.00 13.07  ? 74  ARG   B CA  1 
ATOM   1336 C  C   . ARG   B 1 75 ? -21.975 4.555   16.443  1.00 18.49  ? 74  ARG   B C   1 
ATOM   1337 O  O   . ARG   B 1 75 ? -22.627 3.514   16.554  1.00 13.75  ? 74  ARG   B O   1 
ATOM   1338 C  CB  . ARG   B 1 75 ? -22.778 6.514   17.781  1.00 14.15  ? 74  ARG   B CB  1 
ATOM   1339 C  CG  . ARG   B 1 75 ? -23.425 7.904   17.796  1.00 13.54  ? 74  ARG   B CG  1 
ATOM   1340 C  CD  . ARG   B 1 75 ? -22.619 8.909   16.965  1.00 19.46  ? 74  ARG   B CD  1 
ATOM   1341 N  NE  . ARG   B 1 75 ? -21.269 9.083   17.491  1.00 22.37  ? 74  ARG   B NE  1 
ATOM   1342 C  CZ  . ARG   B 1 75 ? -20.940 9.957   18.433  1.00 25.12  ? 74  ARG   B CZ  1 
ATOM   1343 N  NH1 . ARG   B 1 75 ? -21.833 10.787  18.948  1.00 17.31  ? 74  ARG   B NH1 1 
ATOM   1344 N  NH2 . ARG   B 1 75 ? -19.685 9.999   18.870  1.00 20.47  ? 74  ARG   B NH2 1 
ATOM   1345 N  N   . LYS   B 1 76 ? -20.643 4.580   16.388  1.00 14.54  ? 75  LYS   B N   1 
ATOM   1346 C  CA  . LYS   B 1 76 ? -19.860 3.353   16.256  1.00 14.51  ? 75  LYS   B CA  1 
ATOM   1347 C  C   . LYS   B 1 76 ? -20.130 2.392   17.405  1.00 11.67  ? 75  LYS   B C   1 
ATOM   1348 O  O   . LYS   B 1 76 ? -19.875 2.716   18.570  1.00 15.64  ? 75  LYS   B O   1 
ATOM   1349 C  CB  . LYS   B 1 76 ? -18.368 3.682   16.202  1.00 20.50  ? 75  LYS   B CB  1 
ATOM   1350 C  CG  . LYS   B 1 76 ? -17.880 4.270   14.900  1.00 33.74  ? 75  LYS   B CG  1 
ATOM   1351 C  CD  . LYS   B 1 76 ? -16.367 4.139   14.830  1.00 24.22  ? 75  LYS   B CD  1 
ATOM   1352 C  CE  . LYS   B 1 76 ? -15.793 4.767   13.578  1.00 41.34  ? 75  LYS   B CE  1 
ATOM   1353 N  NZ  . LYS   B 1 76 ? -15.709 6.247   13.682  1.00 33.54  ? 75  LYS   B NZ  1 
ATOM   1354 N  N   . GLY   B 1 77 ? -20.626 1.197   17.072  1.00 11.88  ? 76  GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 1 77 ? -20.860 0.164   18.055  1.00 17.83  ? 76  GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 1 77 ? -22.119 0.314   18.882  1.00 21.25  ? 76  GLY   B C   1 
ATOM   1357 O  O   . GLY   B 1 77 ? -22.417 -0.584  19.681  1.00 13.86  ? 76  GLY   B O   1 
ATOM   1358 N  N   . PHE   B 1 78 ? -22.879 1.403   18.710  1.00 12.58  ? 77  PHE   B N   1 
ATOM   1359 C  CA  . PHE   B 1 78 ? -24.006 1.672   19.604  1.00 14.49  ? 77  PHE   B CA  1 
ATOM   1360 C  C   . PHE   B 1 78 ? -25.111 0.634   19.443  1.00 14.76  ? 77  PHE   B C   1 
ATOM   1361 O  O   . PHE   B 1 78 ? -25.601 0.079   20.434  1.00 14.69  ? 77  PHE   B O   1 
ATOM   1362 C  CB  . PHE   B 1 78 ? -24.560 3.079   19.359  1.00 12.70  ? 77  PHE   B CB  1 
ATOM   1363 C  CG  . PHE   B 1 78 ? -25.625 3.489   20.348  1.00 15.23  ? 77  PHE   B CG  1 
ATOM   1364 C  CD1 . PHE   B 1 78 ? -26.965 3.193   20.116  1.00 14.77  ? 77  PHE   B CD1 1 
ATOM   1365 C  CD2 . PHE   B 1 78 ? -25.281 4.162   21.510  1.00 13.68  ? 77  PHE   B CD2 1 
ATOM   1366 C  CE1 . PHE   B 1 78 ? -27.947 3.560   21.031  1.00 16.01  ? 77  PHE   B CE1 1 
ATOM   1367 C  CE2 . PHE   B 1 78 ? -26.257 4.538   22.434  1.00 13.75  ? 77  PHE   B CE2 1 
ATOM   1368 C  CZ  . PHE   B 1 78 ? -27.592 4.233   22.192  1.00 14.69  ? 77  PHE   B CZ  1 
ATOM   1369 N  N   . ASN   B 1 79 ? -25.543 0.379   18.203  1.00 9.46   ? 78  ASN   B N   1 
ATOM   1370 C  CA  . ASN   B 1 79 ? -26.618 -0.589  18.004  1.00 13.89  ? 78  ASN   B CA  1 
ATOM   1371 C  C   . ASN   B 1 79 ? -26.188 -1.986  18.421  1.00 13.57  ? 78  ASN   B C   1 
ATOM   1372 O  O   . ASN   B 1 79 ? -27.013 -2.773  18.899  1.00 13.72  ? 78  ASN   B O   1 
ATOM   1373 C  CB  . ASN   B 1 79 ? -27.084 -0.586  16.550  1.00 15.63  ? 78  ASN   B CB  1 
ATOM   1374 C  CG  . ASN   B 1 79 ? -27.875 0.660   16.199  1.00 28.02  ? 78  ASN   B CG  1 
ATOM   1375 O  OD1 . ASN   B 1 79 ? -28.192 1.469   17.074  1.00 16.76  ? 78  ASN   B OD1 1 
ATOM   1376 N  ND2 . ASN   B 1 79 ? -28.216 0.812   14.924  1.00 16.04  ? 78  ASN   B ND2 1 
ATOM   1377 N  N   . GLU   B 1 80 ? -24.906 -2.310  18.244  1.00 14.82  ? 79  GLU   B N   1 
ATOM   1378 C  CA  . GLU   B 1 80 ? -24.380 -3.559  18.783  1.00 11.00  ? 79  GLU   B CA  1 
ATOM   1379 C  C   . GLU   B 1 80 ? -24.513 -3.594  20.301  1.00 14.77  ? 79  GLU   B C   1 
ATOM   1380 O  O   . GLU   B 1 80 ? -24.841 -4.639  20.881  1.00 12.47  ? 79  GLU   B O   1 
ATOM   1381 C  CB  . GLU   B 1 80 ? -22.923 -3.737  18.363  1.00 12.84  ? 79  GLU   B CB  1 
ATOM   1382 C  CG  . GLU   B 1 80 ? -22.721 -4.049  16.869  1.00 14.52  ? 79  GLU   B CG  1 
ATOM   1383 C  CD  . GLU   B 1 80 ? -23.014 -2.878  15.948  1.00 16.89  ? 79  GLU   B CD  1 
ATOM   1384 O  OE1 . GLU   B 1 80 ? -22.843 -1.712  16.367  1.00 14.76  ? 79  GLU   B OE1 1 
ATOM   1385 O  OE2 . GLU   B 1 80 ? -23.411 -3.121  14.786  1.00 19.11  ? 79  GLU   B OE2 1 
ATOM   1386 N  N   . GLY   B 1 81 ? -24.287 -2.455  20.961  1.00 10.62  ? 80  GLY   B N   1 
ATOM   1387 C  CA  . GLY   B 1 81 ? -24.431 -2.412  22.408  1.00 11.49  ? 80  GLY   B CA  1 
ATOM   1388 C  C   . GLY   B 1 81 ? -25.871 -2.549  22.863  1.00 13.78  ? 80  GLY   B C   1 
ATOM   1389 O  O   . GLY   B 1 81 ? -26.148 -3.192  23.879  1.00 15.01  ? 80  GLY   B O   1 
ATOM   1390 N  N   . LEU   B 1 82 ? -26.801 -1.926  22.135  1.00 13.89  ? 81  LEU   B N   1 
ATOM   1391 C  CA  . LEU   B 1 82 ? -28.221 -2.100  22.422  1.00 13.45  ? 81  LEU   B CA  1 
ATOM   1392 C  C   . LEU   B 1 82 ? -28.611 -3.570  22.380  1.00 15.39  ? 81  LEU   B C   1 
ATOM   1393 O  O   . LEU   B 1 82 ? -29.341 -4.061  23.247  1.00 12.60  ? 81  LEU   B O   1 
ATOM   1394 C  CB  . LEU   B 1 82 ? -29.059 -1.311  21.419  1.00 16.87  ? 81  LEU   B CB  1 
ATOM   1395 C  CG  . LEU   B 1 82 ? -29.095 0.205   21.573  1.00 24.97  ? 81  LEU   B CG  1 
ATOM   1396 C  CD1 . LEU   B 1 82 ? -30.105 0.800   20.595  1.00 20.57  ? 81  LEU   B CD1 1 
ATOM   1397 C  CD2 . LEU   B 1 82 ? -29.439 0.569   23.003  1.00 18.56  ? 81  LEU   B CD2 1 
ATOM   1398 N  N   . TRP   B 1 83 ? -28.150 -4.281  21.352  1.00 12.66  ? 82  TRP   B N   1 
ATOM   1399 C  CA  . TRP   B 1 83 ? -28.440 -5.702  21.244  1.00 20.36  ? 82  TRP   B CA  1 
ATOM   1400 C  C   . TRP   B 1 83 ? -27.892 -6.466  22.444  1.00 16.58  ? 82  TRP   B C   1 
ATOM   1401 O  O   . TRP   B 1 83 ? -28.569 -7.345  22.990  1.00 16.85  ? 82  TRP   B O   1 
ATOM   1402 C  CB  . TRP   B 1 83 ? -27.856 -6.232  19.933  1.00 19.05  ? 82  TRP   B CB  1 
ATOM   1403 C  CG  . TRP   B 1 83 ? -28.268 -7.632  19.590  1.00 15.91  ? 82  TRP   B CG  1 
ATOM   1404 C  CD1 . TRP   B 1 83 ? -29.324 -8.008  18.811  1.00 18.80  ? 82  TRP   B CD1 1 
ATOM   1405 C  CD2 . TRP   B 1 83 ? -27.624 -8.838  20.007  1.00 13.92  ? 82  TRP   B CD2 1 
ATOM   1406 N  NE1 . TRP   B 1 83 ? -29.376 -9.380  18.717  1.00 30.98  ? 82  TRP   B NE1 1 
ATOM   1407 C  CE2 . TRP   B 1 83 ? -28.343 -9.912  19.443  1.00 20.49  ? 82  TRP   B CE2 1 
ATOM   1408 C  CE3 . TRP   B 1 83 ? -26.508 -9.115  20.801  1.00 18.60  ? 82  TRP   B CE3 1 
ATOM   1409 C  CZ2 . TRP   B 1 83 ? -27.982 -11.241 19.648  1.00 23.28  ? 82  TRP   B CZ2 1 
ATOM   1410 C  CZ3 . TRP   B 1 83 ? -26.147 -10.436 21.001  1.00 25.10  ? 82  TRP   B CZ3 1 
ATOM   1411 C  CH2 . TRP   B 1 83 ? -26.883 -11.483 20.427  1.00 25.88  ? 82  TRP   B CH2 1 
ATOM   1412 N  N   . GLU   B 1 84 ? -26.677 -6.120  22.888  1.00 15.11  ? 83  GLU   B N   1 
ATOM   1413 C  CA  . GLU   B 1 84 ? -26.029 -6.871  23.962  1.00 14.36  ? 83  GLU   B CA  1 
ATOM   1414 C  C   . GLU   B 1 84 ? -26.685 -6.614  25.314  1.00 13.28  ? 83  GLU   B C   1 
ATOM   1415 O  O   . GLU   B 1 84 ? -26.847 -7.543  26.115  1.00 15.71  ? 83  GLU   B O   1 
ATOM   1416 C  CB  . GLU   B 1 84 ? -24.537 -6.529  24.016  1.00 15.47  ? 83  GLU   B CB  1 
ATOM   1417 C  CG  . GLU   B 1 84 ? -23.745 -7.051  22.814  1.00 14.35  ? 83  GLU   B CG  1 
ATOM   1418 C  CD  . GLU   B 1 84 ? -22.245 -6.826  22.953  1.00 17.02  ? 83  GLU   B CD  1 
ATOM   1419 O  OE1 . GLU   B 1 84 ? -21.844 -5.876  23.663  1.00 16.33  ? 83  GLU   B OE1 1 
ATOM   1420 O  OE2 . GLU   B 1 84 ? -21.469 -7.604  22.357  1.00 16.31  ? 83  GLU   B OE2 1 
ATOM   1421 N  N   . ILE   B 1 85 ? -27.067 -5.368  25.598  1.00 11.90  ? 84  ILE   B N   1 
ATOM   1422 C  CA  . ILE   B 1 85 ? -27.711 -5.106  26.882  1.00 11.06  ? 84  ILE   B CA  1 
ATOM   1423 C  C   . ILE   B 1 85 ? -29.073 -5.794  26.943  1.00 21.47  ? 84  ILE   B C   1 
ATOM   1424 O  O   . ILE   B 1 85 ? -29.543 -6.175  28.027  1.00 15.09  ? 84  ILE   B O   1 
ATOM   1425 C  CB  . ILE   B 1 85 ? -27.813 -3.588  27.143  1.00 10.30  ? 84  ILE   B CB  1 
ATOM   1426 C  CG1 . ILE   B 1 85 ? -28.042 -3.321  28.638  1.00 11.90  ? 84  ILE   B CG1 1 
ATOM   1427 C  CG2 . ILE   B 1 85 ? -28.927 -2.956  26.307  1.00 11.14  ? 84  ILE   B CG2 1 
ATOM   1428 C  CD1 . ILE   B 1 85 ? -27.837 -1.860  29.037  1.00 13.86  ? 84  ILE   B CD1 1 
ATOM   1429 N  N   . GLN   B 1 86 ? -29.713 -5.995  25.789  1.00 14.60  ? 85  GLN   B N   1 
ATOM   1430 C  CA  . GLN   B 1 86 ? -31.015 -6.652  25.768  1.00 22.53  ? 85  GLN   B CA  1 
ATOM   1431 C  C   . GLN   B 1 86 ? -30.894 -8.172  25.808  1.00 17.04  ? 85  GLN   B C   1 
ATOM   1432 O  O   . GLN   B 1 86 ? -31.771 -8.847  26.359  1.00 20.87  ? 85  GLN   B O   1 
ATOM   1433 C  CB  . GLN   B 1 86 ? -31.800 -6.214  24.527  1.00 17.67  ? 85  GLN   B CB  1 
ATOM   1434 C  CG  . GLN   B 1 86 ? -32.410 -4.826  24.653  1.00 29.97  ? 85  GLN   B CG  1 
ATOM   1435 C  CD  . GLN   B 1 86 ? -32.495 -4.088  23.331  1.00 44.00  ? 85  GLN   B CD  1 
ATOM   1436 O  OE1 . GLN   B 1 86 ? -32.772 -4.682  22.288  1.00 40.70  ? 85  GLN   B OE1 1 
ATOM   1437 N  NE2 . GLN   B 1 86 ? -32.246 -2.781  23.368  1.00 34.93  ? 85  GLN   B NE2 1 
ATOM   1438 N  N   . ASN   B 1 87 ? -29.818 -8.728  25.261  1.00 18.67  ? 86  ASN   B N   1 
ATOM   1439 C  CA  . ASN   B 1 87 ? -29.698 -10.172 25.100  1.00 22.46  ? 86  ASN   B CA  1 
ATOM   1440 C  C   . ASN   B 1 87 ? -28.649 -10.815 25.992  1.00 26.91  ? 86  ASN   B C   1 
ATOM   1441 O  O   . ASN   B 1 87 ? -28.880 -11.916 26.498  1.00 24.46  ? 86  ASN   B O   1 
ATOM   1442 C  CB  . ASN   B 1 87 ? -29.399 -10.510 23.637  1.00 28.36  ? 86  ASN   B CB  1 
ATOM   1443 C  CG  . ASN   B 1 87 ? -30.590 -10.251 22.730  1.00 30.70  ? 86  ASN   B CG  1 
ATOM   1444 O  OD1 . ASN   B 1 87 ? -31.526 -11.050 22.677  1.00 37.12  ? 86  ASN   B OD1 1 
ATOM   1445 N  ND2 . ASN   B 1 87 ? -30.563 -9.132  22.017  1.00 19.92  ? 86  ASN   B ND2 1 
ATOM   1446 N  N   . ASN   B 1 88 ? -27.493 -10.178 26.193  1.00 16.96  ? 87  ASN   B N   1 
ATOM   1447 C  CA  . ASN   B 1 88 ? -26.453 -10.770 27.031  1.00 29.41  ? 87  ASN   B CA  1 
ATOM   1448 C  C   . ASN   B 1 88 ? -25.882 -9.760  28.020  1.00 17.82  ? 87  ASN   B C   1 
ATOM   1449 O  O   . ASN   B 1 88 ? -24.663 -9.560  28.048  1.00 17.28  ? 87  ASN   B O   1 
ATOM   1450 C  CB  . ASN   B 1 88 ? -25.309 -11.324 26.176  1.00 30.66  ? 87  ASN   B CB  1 
ATOM   1451 C  CG  . ASN   B 1 88 ? -25.726 -12.501 25.316  1.00 34.86  ? 87  ASN   B CG  1 
ATOM   1452 O  OD1 . ASN   B 1 88 ? -26.249 -12.323 24.215  1.00 35.17  ? 87  ASN   B OD1 1 
ATOM   1453 N  ND2 . ASN   B 1 88 ? -25.484 -13.711 25.807  1.00 53.42  ? 87  ASN   B ND2 1 
ATOM   1454 N  N   . PRO   B 1 89 ? -26.705 -9.114  28.854  1.00 14.13  ? 88  PRO   B N   1 
ATOM   1455 C  CA  . PRO   B 1 89 ? -26.167 -8.028  29.694  1.00 14.33  ? 88  PRO   B CA  1 
ATOM   1456 C  C   . PRO   B 1 89 ? -25.180 -8.489  30.754  1.00 18.85  ? 88  PRO   B C   1 
ATOM   1457 O  O   . PRO   B 1 89 ? -24.347 -7.682  31.187  1.00 15.09  ? 88  PRO   B O   1 
ATOM   1458 C  CB  . PRO   B 1 89 ? -27.423 -7.415  30.333  1.00 11.83  ? 88  PRO   B CB  1 
ATOM   1459 C  CG  . PRO   B 1 89 ? -28.409 -8.566  30.363  1.00 13.65  ? 88  PRO   B CG  1 
ATOM   1460 C  CD  . PRO   B 1 89 ? -28.139 -9.357  29.113  1.00 13.26  ? 88  PRO   B CD  1 
ATOM   1461 N  N   . HIS   B 1 90 ? -25.235 -9.747  31.197  1.00 14.16  ? 89  HIS   B N   1 
ATOM   1462 C  CA  . HIS   B 1 90 ? -24.354 -10.220 32.259  1.00 9.96   ? 89  HIS   B CA  1 
ATOM   1463 C  C   . HIS   B 1 90 ? -23.382 -11.281 31.768  1.00 17.87  ? 89  HIS   B C   1 
ATOM   1464 O  O   . HIS   B 1 90 ? -22.841 -12.046 32.571  1.00 18.57  ? 89  HIS   B O   1 
ATOM   1465 C  CB  . HIS   B 1 90 ? -25.192 -10.721 33.436  1.00 10.58  ? 89  HIS   B CB  1 
ATOM   1466 C  CG  . HIS   B 1 90 ? -26.070 -9.651  34.010  1.00 12.22  ? 89  HIS   B CG  1 
ATOM   1467 N  ND1 . HIS   B 1 90 ? -25.562 -8.465  34.496  1.00 16.76  ? 89  HIS   B ND1 1 
ATOM   1468 C  CD2 . HIS   B 1 90 ? -27.416 -9.565  34.135  1.00 13.55  ? 89  HIS   B CD2 1 
ATOM   1469 C  CE1 . HIS   B 1 90 ? -26.556 -7.703  34.914  1.00 17.38  ? 89  HIS   B CE1 1 
ATOM   1470 N  NE2 . HIS   B 1 90 ? -27.691 -8.346  34.708  1.00 17.98  ? 89  HIS   B NE2 1 
ATOM   1471 N  N   . ALA   B 1 91 ? -23.143 -11.326 30.464  1.00 14.37  ? 90  ALA   B N   1 
ATOM   1472 C  CA  . ALA   B 1 91 ? -22.130 -12.202 29.908  1.00 16.22  ? 90  ALA   B CA  1 
ATOM   1473 C  C   . ALA   B 1 91 ? -20.733 -11.758 30.335  1.00 15.65  ? 90  ALA   B C   1 
ATOM   1474 O  O   . ALA   B 1 91 ? -20.489 -10.599 30.688  1.00 17.29  ? 90  ALA   B O   1 
ATOM   1475 C  CB  . ALA   B 1 91 ? -22.225 -12.222 28.380  1.00 20.68  ? 90  ALA   B CB  1 
ATOM   1476 N  N   . SER   B 1 92 ? -19.811 -12.711 30.315  1.00 22.51  ? 91  SER   B N   1 
ATOM   1477 C  CA  . SER   B 1 92 ? -18.396 -12.396 30.412  1.00 19.81  ? 91  SER   B CA  1 
ATOM   1478 C  C   . SER   B 1 92 ? -17.891 -12.005 29.029  1.00 22.66  ? 91  SER   B C   1 
ATOM   1479 O  O   . SER   B 1 92 ? -18.097 -12.735 28.055  1.00 24.01  ? 91  SER   B O   1 
ATOM   1480 C  CB  . SER   B 1 92 ? -17.618 -13.596 30.952  1.00 33.41  ? 91  SER   B CB  1 
ATOM   1481 O  OG  . SER   B 1 92 ? -16.224 -13.431 30.766  1.00 47.88  ? 91  SER   B OG  1 
ATOM   1482 N  N   . TYR   B 1 93 ? -17.252 -10.842 28.937  1.00 25.40  ? 92  TYR   B N   1 
ATOM   1483 C  CA  . TYR   B 1 93 ? -16.724 -10.359 27.669  1.00 23.61  ? 92  TYR   B CA  1 
ATOM   1484 C  C   . TYR   B 1 93 ? -15.207 -10.421 27.598  1.00 28.03  ? 92  TYR   B C   1 
ATOM   1485 O  O   . TYR   B 1 93 ? -14.630 -9.983  26.596  1.00 44.53  ? 92  TYR   B O   1 
ATOM   1486 C  CB  . TYR   B 1 93 ? -17.208 -8.927  27.406  1.00 17.74  ? 92  TYR   B CB  1 
ATOM   1487 C  CG  . TYR   B 1 93 ? -18.680 -8.866  27.064  1.00 25.95  ? 92  TYR   B CG  1 
ATOM   1488 C  CD1 . TYR   B 1 93 ? -19.107 -8.922  25.745  1.00 21.58  ? 92  TYR   B CD1 1 
ATOM   1489 C  CD2 . TYR   B 1 93 ? -19.642 -8.778  28.064  1.00 19.50  ? 92  TYR   B CD2 1 
ATOM   1490 C  CE1 . TYR   B 1 93 ? -20.459 -8.883  25.426  1.00 19.01  ? 92  TYR   B CE1 1 
ATOM   1491 C  CE2 . TYR   B 1 93 ? -20.994 -8.736  27.756  1.00 16.50  ? 92  TYR   B CE2 1 
ATOM   1492 C  CZ  . TYR   B 1 93 ? -21.397 -8.790  26.436  1.00 22.55  ? 92  TYR   B CZ  1 
ATOM   1493 O  OH  . TYR   B 1 93 ? -22.743 -8.750  26.126  1.00 21.40  ? 92  TYR   B OH  1 
ATOM   1494 N  N   . SER   B 1 94 ? -14.551 -10.956 28.623  1.00 43.64  ? 93  SER   B N   1 
ATOM   1495 C  CA  . SER   B 1 94 ? -13.097 -11.086 28.645  1.00 34.66  ? 93  SER   B CA  1 
ATOM   1496 C  C   . SER   B 1 94 ? -12.641 -12.277 27.806  1.00 54.30  ? 93  SER   B C   1 
ATOM   1497 O  O   . SER   B 1 94 ? -13.417 -13.197 27.527  1.00 42.06  ? 93  SER   B O   1 
ATOM   1498 C  CB  . SER   B 1 94 ? -12.597 -11.236 30.083  1.00 48.02  ? 93  SER   B CB  1 
ATOM   1499 O  OG  . SER   B 1 94 ? -13.065 -12.445 30.655  1.00 48.77  ? 93  SER   B OG  1 
ATOM   1500 O  OXT . SER   B 1 94 ? -11.483 -12.346 27.390  1.00 60.18  ? 93  SER   B OXT 1 
HETATM 1501 C  C1  . EDO   C 2 .  ? -8.508  -0.178  4.138   1.00 26.99  ? 101 EDO   A C1  1 
HETATM 1502 O  O1  . EDO   C 2 .  ? -9.040  1.032   3.654   1.00 19.47  ? 101 EDO   A O1  1 
HETATM 1503 C  C2  . EDO   C 2 .  ? -7.876  -0.966  3.015   1.00 24.03  ? 101 EDO   A C2  1 
HETATM 1504 O  O2  . EDO   C 2 .  ? -8.863  -1.399  2.099   1.00 20.68  ? 101 EDO   A O2  1 
HETATM 1505 N  N1  . A1II3 D 3 .  ? -9.654  -10.151 11.695  0.82 14.23  ? 102 A1II3 A N1  1 
HETATM 1506 C  C2  . A1II3 D 3 .  ? -5.125  -14.441 10.417  0.82 32.03  ? 102 A1II3 A C2  1 
HETATM 1507 C  C4  . A1II3 D 3 .  ? -6.833  -12.305 13.002  0.82 18.65  ? 102 A1II3 A C4  1 
HETATM 1508 C  C5  . A1II3 D 3 .  ? -8.170  -11.902 12.425  0.82 15.79  ? 102 A1II3 A C5  1 
HETATM 1509 C  C6  . A1II3 D 3 .  ? -8.502  -10.573 12.234  0.82 25.54  ? 102 A1II3 A C6  1 
HETATM 1510 C  C7  . A1II3 D 3 .  ? -10.540 -11.077 11.320  0.82 14.38  ? 102 A1II3 A C7  1 
HETATM 1511 C  C8  . A1II3 D 3 .  ? -10.289 -12.423 11.474  0.82 22.44  ? 102 A1II3 A C8  1 
HETATM 1512 C  C   . A1II3 D 3 .  ? -3.995  -15.581 8.480   0.82 35.40  ? 102 A1II3 A C   1 
HETATM 1513 C  C1  . A1II3 D 3 .  ? -4.672  -14.388 9.102   0.82 24.92  ? 102 A1II3 A C1  1 
HETATM 1514 C  C10 . A1II3 D 3 .  ? -5.916  -12.176 10.264  0.82 33.39  ? 102 A1II3 A C10 1 
HETATM 1515 C  C11 . A1II3 D 3 .  ? -5.467  -12.119 8.956   0.82 23.14  ? 102 A1II3 A C11 1 
HETATM 1516 C  C12 . A1II3 D 3 .  ? -4.850  -13.217 8.380   0.82 26.25  ? 102 A1II3 A C12 1 
HETATM 1517 C  C3  . A1II3 D 3 .  ? -5.746  -13.341 11.003  0.82 24.69  ? 102 A1II3 A C3  1 
HETATM 1518 C  C9  . A1II3 D 3 .  ? -9.102  -12.851 12.028  0.82 16.16  ? 102 A1II3 A C9  1 
HETATM 1519 N  N   . A1II3 D 3 .  ? -6.207  -13.419 12.307  0.82 19.09  ? 102 A1II3 A N   1 
HETATM 1520 O  O   . A1II3 D 3 .  ? -4.466  -16.807 9.014   0.82 51.87  ? 102 A1II3 A O   1 
HETATM 1521 BR BR  . A1II3 D 3 .  ? -11.560 -13.711 10.896  0.82 22.67  ? 102 A1II3 A BR  1 
HETATM 1522 S  S   . SO4   E 4 .  ? -13.891 -22.838 13.960  1.00 66.73  ? 103 SO4   A S   1 
HETATM 1523 O  O1  . SO4   E 4 .  ? -12.937 -22.576 12.838  1.00 45.13  ? 103 SO4   A O1  1 
HETATM 1524 O  O2  . SO4   E 4 .  ? -15.152 -22.058 13.731  1.00 63.75  ? 103 SO4   A O2  1 
HETATM 1525 O  O3  . SO4   E 4 .  ? -14.203 -24.303 14.011  1.00 54.32  ? 103 SO4   A O3  1 
HETATM 1526 O  O4  . SO4   E 4 .  ? -13.274 -22.417 15.260  1.00 73.33  ? 103 SO4   A O4  1 
HETATM 1527 S  S   . SO4   F 4 .  ? -7.032  3.253   1.541   1.00 68.13  ? 104 SO4   A S   1 
HETATM 1528 O  O1  . SO4   F 4 .  ? -6.330  2.192   0.747   1.00 75.57  ? 104 SO4   A O1  1 
HETATM 1529 O  O2  . SO4   F 4 .  ? -8.232  3.734   0.786   1.00 64.23  ? 104 SO4   A O2  1 
HETATM 1530 O  O3  . SO4   F 4 .  ? -7.465  2.684   2.857   1.00 55.10  ? 104 SO4   A O3  1 
HETATM 1531 O  O4  . SO4   F 4 .  ? -6.100  4.405   1.773   1.00 57.50  ? 104 SO4   A O4  1 
HETATM 1532 N  N1  . A1II3 G 3 .  ? -17.823 3.166   24.000  0.76 10.22  ? 101 A1II3 B N1  1 
HETATM 1533 C  C2  . A1II3 G 3 .  ? -13.453 7.270   26.071  0.76 35.62  ? 101 A1II3 B C2  1 
HETATM 1534 C  C4  . A1II3 G 3 .  ? -15.067 5.599   23.113  0.76 19.35  ? 101 A1II3 B C4  1 
HETATM 1535 C  C5  . A1II3 G 3 .  ? -16.390 5.061   23.608  0.76 24.12  ? 101 A1II3 B C5  1 
HETATM 1536 C  C6  . A1II3 G 3 .  ? -16.687 3.711   23.546  0.76 25.76  ? 101 A1II3 B C6  1 
HETATM 1537 C  C7  . A1II3 G 3 .  ? -18.728 3.981   24.549  0.76 9.69   ? 101 A1II3 B C7  1 
HETATM 1538 C  C8  . A1II3 G 3 .  ? -18.514 5.338   24.651  0.76 13.42  ? 101 A1II3 B C8  1 
HETATM 1539 C  C   . A1II3 G 3 .  ? -12.405 8.076   28.210  0.76 37.66  ? 101 A1II3 B C   1 
HETATM 1540 C  C1  . A1II3 G 3 .  ? -12.987 6.984   27.350  0.76 33.50  ? 101 A1II3 B C1  1 
HETATM 1541 C  C10 . A1II3 G 3 .  ? -14.078 4.972   25.754  0.76 32.08  ? 101 A1II3 B C10 1 
HETATM 1542 C  C11 . A1II3 G 3 .  ? -13.615 4.682   27.025  0.76 21.67  ? 101 A1II3 B C11 1 
HETATM 1543 C  C12 . A1II3 G 3 .  ? -13.074 5.680   27.817  0.76 29.30  ? 101 A1II3 B C12 1 
HETATM 1544 C  C3  . A1II3 G 3 .  ? -13.999 6.273   25.269  0.76 30.15  ? 101 A1II3 B C3  1 
HETATM 1545 C  C9  . A1II3 G 3 .  ? -17.343 5.893   24.182  0.76 26.23  ? 101 A1II3 B C9  1 
HETATM 1546 N  N   . A1II3 G 3 .  ? -14.463 6.582   23.998  0.76 21.81  ? 101 A1II3 B N   1 
HETATM 1547 O  O   . A1II3 G 3 .  ? -12.635 9.364   27.662  0.76 54.14  ? 101 A1II3 B O   1 
HETATM 1548 BR BR  . A1II3 G 3 .  ? -19.817 6.458   25.464  0.76 19.76  ? 101 A1II3 B BR  1 
HETATM 1549 S  S   . SO4   H 4 .  ? -18.480 7.850   15.617  1.00 35.86  ? 102 SO4   B S   1 
HETATM 1550 O  O1  . SO4   H 4 .  ? -17.145 7.256   15.943  1.00 41.11  ? 102 SO4   B O1  1 
HETATM 1551 O  O2  . SO4   H 4 .  ? -18.763 7.682   14.153  1.00 29.67  ? 102 SO4   B O2  1 
HETATM 1552 O  O3  . SO4   H 4 .  ? -19.547 7.154   16.411  1.00 23.47  ? 102 SO4   B O3  1 
HETATM 1553 O  O4  . SO4   H 4 .  ? -18.470 9.310   15.965  1.00 41.64  ? 102 SO4   B O4  1 
HETATM 1554 S  S   . SO4   I 4 .  ? -22.886 15.895  23.778  1.00 56.03  ? 103 SO4   B S   1 
HETATM 1555 O  O1  . SO4   I 4 .  ? -22.462 14.988  22.662  1.00 53.43  ? 103 SO4   B O1  1 
HETATM 1556 O  O2  . SO4   I 4 .  ? -24.243 15.484  24.272  1.00 60.79  ? 103 SO4   B O2  1 
HETATM 1557 O  O3  . SO4   I 4 .  ? -21.900 15.794  24.899  1.00 39.01  ? 103 SO4   B O3  1 
HETATM 1558 O  O4  . SO4   I 4 .  ? -22.941 17.308  23.280  1.00 68.18  ? 103 SO4   B O4  1 
HETATM 1559 S  S   . SO4   J 4 .  ? -20.514 -16.443 30.340  1.00 55.44  ? 104 SO4   B S   1 
HETATM 1560 O  O1  . SO4   J 4 .  ? -19.191 -17.011 29.920  1.00 69.64  ? 104 SO4   B O1  1 
HETATM 1561 O  O2  . SO4   J 4 .  ? -20.831 -15.244 29.504  1.00 31.97  ? 104 SO4   B O2  1 
HETATM 1562 O  O3  . SO4   J 4 .  ? -21.575 -17.487 30.152  1.00 62.98  ? 104 SO4   B O3  1 
HETATM 1563 O  O4  . SO4   J 4 .  ? -20.455 -16.046 31.785  1.00 36.37  ? 104 SO4   B O4  1 
HETATM 1564 S  S   . SO4   K 4 .  ? -23.144 15.659  28.957  1.00 65.53  ? 105 SO4   B S   1 
HETATM 1565 O  O1  . SO4   K 4 .  ? -22.081 14.686  28.532  1.00 26.61  ? 105 SO4   B O1  1 
HETATM 1566 O  O2  . SO4   K 4 .  ? -24.159 15.790  27.864  1.00 56.47  ? 105 SO4   B O2  1 
HETATM 1567 O  O3  . SO4   K 4 .  ? -23.814 15.160  30.205  1.00 45.41  ? 105 SO4   B O3  1 
HETATM 1568 O  O4  . SO4   K 4 .  ? -22.525 16.998  29.220  1.00 77.58  ? 105 SO4   B O4  1 
HETATM 1569 S  S   . SO4   L 4 .  ? -15.904 15.234  38.423  1.00 103.28 ? 106 SO4   B S   1 
HETATM 1570 O  O1  . SO4   L 4 .  ? -14.668 14.659  39.045  1.00 72.22  ? 106 SO4   B O1  1 
HETATM 1571 O  O2  . SO4   L 4 .  ? -16.029 14.745  37.011  1.00 66.52  ? 106 SO4   B O2  1 
HETATM 1572 O  O3  . SO4   L 4 .  ? -17.103 14.801  39.211  1.00 64.63  ? 106 SO4   B O3  1 
HETATM 1573 O  O4  . SO4   L 4 .  ? -15.814 16.732  38.429  1.00 72.47  ? 106 SO4   B O4  1 
HETATM 1574 O  O   . HOH   M 5 .  ? -10.284 -2.195  -9.146  1.00 56.62  ? 201 HOH   A O   1 
HETATM 1575 O  O   . HOH   M 5 .  ? -7.826  -4.603  -8.037  1.00 44.90  ? 202 HOH   A O   1 
HETATM 1576 O  O   . HOH   M 5 .  ? -5.950  -9.080  15.154  1.00 48.66  ? 203 HOH   A O   1 
HETATM 1577 O  O   . HOH   M 5 .  ? -3.618  -14.132 -8.241  1.00 46.26  ? 204 HOH   A O   1 
HETATM 1578 O  O   . HOH   M 5 .  ? -17.919 -4.675  -6.023  1.00 42.99  ? 205 HOH   A O   1 
HETATM 1579 O  O   . HOH   M 5 .  ? -19.649 -9.556  -7.721  1.00 32.82  ? 206 HOH   A O   1 
HETATM 1580 O  O   . HOH   M 5 .  ? -11.725 -1.398  15.293  1.00 38.92  ? 207 HOH   A O   1 
HETATM 1581 O  O   . HOH   M 5 .  ? -23.526 5.551   7.401   1.00 16.98  ? 208 HOH   A O   1 
HETATM 1582 O  O   . HOH   M 5 .  ? -13.213 -16.854 -8.405  1.00 23.03  ? 209 HOH   A O   1 
HETATM 1583 O  O   . HOH   M 5 .  ? -21.123 -7.906  -9.365  1.00 42.23  ? 210 HOH   A O   1 
HETATM 1584 O  O   . HOH   M 5 .  ? -7.087  -16.843 -9.848  1.00 38.18  ? 211 HOH   A O   1 
HETATM 1585 O  O   . HOH   M 5 .  ? -25.301 -7.060  12.552  1.00 30.96  ? 212 HOH   A O   1 
HETATM 1586 O  O   . HOH   M 5 .  ? -8.898  -0.124  -0.115  1.00 35.03  ? 213 HOH   A O   1 
HETATM 1587 O  O   . HOH   M 5 .  ? -13.319 -12.133 -9.806  1.00 38.85  ? 214 HOH   A O   1 
HETATM 1588 O  O   . HOH   M 5 .  ? -6.164  -4.553  1.570   1.00 31.31  ? 215 HOH   A O   1 
HETATM 1589 O  O   . HOH   M 5 .  ? -25.365 -17.857 3.912   1.00 38.34  ? 216 HOH   A O   1 
HETATM 1590 O  O   . HOH   M 5 .  ? -21.589 -13.520 15.643  1.00 24.29  ? 217 HOH   A O   1 
HETATM 1591 O  O   . HOH   M 5 .  ? -6.269  -13.476 16.732  1.00 41.68  ? 218 HOH   A O   1 
HETATM 1592 O  O   . HOH   M 5 .  ? -19.552 3.093   2.403   1.00 13.51  ? 219 HOH   A O   1 
HETATM 1593 O  O   . HOH   M 5 .  ? -20.450 -14.488 12.735  1.00 16.97  ? 220 HOH   A O   1 
HETATM 1594 O  O   . HOH   M 5 .  ? 3.184   -7.906  -7.681  1.00 22.90  ? 221 HOH   A O   1 
HETATM 1595 O  O   . HOH   M 5 .  ? -13.697 -15.810 10.149  1.00 15.91  ? 222 HOH   A O   1 
HETATM 1596 O  O   . HOH   M 5 .  ? -27.954 -2.871  9.247   1.00 44.72  ? 223 HOH   A O   1 
HETATM 1597 O  O   . HOH   M 5 .  ? -9.791  -19.977 1.433   1.00 21.69  ? 224 HOH   A O   1 
HETATM 1598 O  O   . HOH   M 5 .  ? -2.370  -11.317 6.669   1.00 22.95  ? 225 HOH   A O   1 
HETATM 1599 O  O   . HOH   M 5 .  ? -12.725 -0.722  -5.272  1.00 37.82  ? 226 HOH   A O   1 
HETATM 1600 O  O   . HOH   M 5 .  ? -15.353 -3.378  -8.504  1.00 31.35  ? 227 HOH   A O   1 
HETATM 1601 O  O   . HOH   M 5 .  ? -13.497 2.713   12.363  1.00 47.06  ? 228 HOH   A O   1 
HETATM 1602 O  O   . HOH   M 5 .  ? -16.214 -21.889 4.704   1.00 30.40  ? 229 HOH   A O   1 
HETATM 1603 O  O   . HOH   M 5 .  ? -4.860  -21.366 -4.720  1.00 36.25  ? 230 HOH   A O   1 
HETATM 1604 O  O   . HOH   M 5 .  ? -21.778 -9.869  -1.845  1.00 28.43  ? 231 HOH   A O   1 
HETATM 1605 O  O   . HOH   M 5 .  ? -7.863  -14.816 -7.929  1.00 29.90  ? 232 HOH   A O   1 
HETATM 1606 O  O   . HOH   M 5 .  ? -1.347  -7.276  -1.652  1.00 21.29  ? 233 HOH   A O   1 
HETATM 1607 O  O   . HOH   M 5 .  ? -16.910 -7.440  19.372  1.00 13.84  ? 234 HOH   A O   1 
HETATM 1608 O  O   . HOH   M 5 .  ? -18.730 -21.899 6.842   1.00 35.25  ? 235 HOH   A O   1 
HETATM 1609 O  O   . HOH   M 5 .  ? -22.093 -21.946 9.106   1.00 36.36  ? 236 HOH   A O   1 
HETATM 1610 O  O   . HOH   M 5 .  ? -6.812  -0.201  12.573  1.00 36.76  ? 237 HOH   A O   1 
HETATM 1611 O  O   . HOH   M 5 .  ? -17.555 -9.800  -11.322 1.00 41.27  ? 238 HOH   A O   1 
HETATM 1612 O  O   . HOH   M 5 .  ? -15.005 -0.803  -1.148  1.00 15.11  ? 239 HOH   A O   1 
HETATM 1613 O  O   . HOH   M 5 .  ? -2.787  -4.541  -2.528  1.00 30.19  ? 240 HOH   A O   1 
HETATM 1614 O  O   . HOH   M 5 .  ? -13.012 -21.707 -3.126  1.00 19.19  ? 241 HOH   A O   1 
HETATM 1615 O  O   . HOH   M 5 .  ? -13.606 -5.280  20.432  1.00 26.69  ? 242 HOH   A O   1 
HETATM 1616 O  O   . HOH   M 5 .  ? -13.210 -22.211 9.278   1.00 28.73  ? 243 HOH   A O   1 
HETATM 1617 O  O   . HOH   M 5 .  ? -6.167  -5.473  14.310  1.00 36.85  ? 244 HOH   A O   1 
HETATM 1618 O  O   . HOH   M 5 .  ? -24.588 -8.951  -0.444  1.00 26.37  ? 245 HOH   A O   1 
HETATM 1619 O  O   . HOH   M 5 .  ? -27.131 -3.400  13.758  1.00 42.84  ? 246 HOH   A O   1 
HETATM 1620 O  O   . HOH   M 5 .  ? -13.981 1.563   -1.496  1.00 23.41  ? 247 HOH   A O   1 
HETATM 1621 O  O   . HOH   M 5 .  ? -13.147 -2.675  -1.464  1.00 18.26  ? 248 HOH   A O   1 
HETATM 1622 O  O   . HOH   M 5 .  ? -8.886  -20.875 7.731   1.00 33.01  ? 249 HOH   A O   1 
HETATM 1623 O  O   . HOH   M 5 .  ? -4.930  -5.294  -0.911  1.00 31.01  ? 250 HOH   A O   1 
HETATM 1624 O  O   . HOH   M 5 .  ? -8.866  -1.879  -1.983  1.00 45.56  ? 251 HOH   A O   1 
HETATM 1625 O  O   . HOH   M 5 .  ? -21.881 -6.623  -1.819  1.00 30.39  ? 252 HOH   A O   1 
HETATM 1626 O  O   . HOH   M 5 .  ? -29.920 -12.266 5.659   1.00 29.31  ? 253 HOH   A O   1 
HETATM 1627 O  O   . HOH   M 5 .  ? -9.157  -8.149  -6.113  1.00 34.33  ? 254 HOH   A O   1 
HETATM 1628 O  O   . HOH   M 5 .  ? -28.808 -15.454 6.768   1.00 26.11  ? 255 HOH   A O   1 
HETATM 1629 O  O   . HOH   M 5 .  ? -10.302 -13.101 18.450  1.00 46.09  ? 256 HOH   A O   1 
HETATM 1630 O  O   . HOH   M 5 .  ? 0.079   -6.138  -8.204  1.00 39.34  ? 257 HOH   A O   1 
HETATM 1631 O  O   . HOH   M 5 .  ? -10.068 -22.895 -5.909  1.00 37.81  ? 258 HOH   A O   1 
HETATM 1632 O  O   . HOH   M 5 .  ? -16.023 0.657   18.393  1.00 40.30  ? 259 HOH   A O   1 
HETATM 1633 O  O   . HOH   M 5 .  ? -3.453  -14.627 3.786   1.00 27.37  ? 260 HOH   A O   1 
HETATM 1634 O  O   . HOH   M 5 .  ? 2.622   -6.165  -1.366  1.00 36.20  ? 261 HOH   A O   1 
HETATM 1635 O  O   . HOH   M 5 .  ? 0.608   -15.052 -2.957  1.00 25.51  ? 262 HOH   A O   1 
HETATM 1636 O  O   . HOH   M 5 .  ? -9.583  -21.077 -3.769  1.00 35.49  ? 263 HOH   A O   1 
HETATM 1637 O  O   . HOH   M 5 .  ? -25.254 0.865   13.466  1.00 24.11  ? 264 HOH   A O   1 
HETATM 1638 O  O   . HOH   M 5 .  ? -24.052 -14.426 14.251  1.00 30.23  ? 265 HOH   A O   1 
HETATM 1639 O  O   . HOH   M 5 .  ? -13.303 7.202   3.426   1.00 25.16  ? 266 HOH   A O   1 
HETATM 1640 O  O   . HOH   M 5 .  ? -29.718 -18.297 2.924   1.00 39.41  ? 267 HOH   A O   1 
HETATM 1641 O  O   . HOH   M 5 .  ? -9.863  -10.641 16.645  1.00 35.78  ? 268 HOH   A O   1 
HETATM 1642 O  O   . HOH   M 5 .  ? -22.207 -11.404 -7.086  1.00 26.63  ? 269 HOH   A O   1 
HETATM 1643 O  O   . HOH   M 5 .  ? -7.989  -11.823 -7.060  1.00 43.24  ? 270 HOH   A O   1 
HETATM 1644 O  O   . HOH   M 5 .  ? -7.029  -19.091 10.710  1.00 52.97  ? 271 HOH   A O   1 
HETATM 1645 O  O   . HOH   M 5 .  ? -17.230 8.778   4.554   1.00 31.70  ? 272 HOH   A O   1 
HETATM 1646 O  O   . HOH   M 5 .  ? 1.919   -13.602 -5.943  1.00 43.89  ? 273 HOH   A O   1 
HETATM 1647 O  O   . HOH   M 5 .  ? -15.155 -4.189  18.304  1.00 19.03  ? 274 HOH   A O   1 
HETATM 1648 O  O   . HOH   M 5 .  ? -24.568 -2.176  4.228   1.00 38.79  ? 275 HOH   A O   1 
HETATM 1649 O  O   . HOH   M 5 .  ? -9.755  -20.339 5.680   1.00 46.54  ? 276 HOH   A O   1 
HETATM 1650 O  O   . HOH   M 5 .  ? -19.596 -14.025 22.100  1.00 41.29  ? 277 HOH   A O   1 
HETATM 1651 O  O   . HOH   M 5 .  ? -26.346 -11.775 -1.138  1.00 29.41  ? 278 HOH   A O   1 
HETATM 1652 O  O   . HOH   M 5 .  ? -20.261 -4.174  -4.514  1.00 44.12  ? 279 HOH   A O   1 
HETATM 1653 O  O   . HOH   M 5 .  ? -27.569 -4.125  6.509   1.00 28.80  ? 280 HOH   A O   1 
HETATM 1654 O  O   . HOH   M 5 .  ? -24.267 -20.866 5.261   1.00 45.03  ? 281 HOH   A O   1 
HETATM 1655 O  O   . HOH   M 5 .  ? -21.124 -3.312  -2.531  1.00 23.76  ? 282 HOH   A O   1 
HETATM 1656 O  O   . HOH   M 5 .  ? -10.616 -11.897 20.726  1.00 25.86  ? 283 HOH   A O   1 
HETATM 1657 O  O   . HOH   M 5 .  ? -27.800 -0.112  10.536  1.00 49.53  ? 284 HOH   A O   1 
HETATM 1658 O  O   . HOH   M 5 .  ? -26.242 -7.819  -12.358 1.00 48.30  ? 285 HOH   A O   1 
HETATM 1659 O  O   . HOH   M 5 .  ? 0.284   -15.631 -7.328  1.00 45.04  ? 286 HOH   A O   1 
HETATM 1660 O  O   . HOH   M 5 .  ? -2.700  -10.007 9.203   1.00 44.17  ? 287 HOH   A O   1 
HETATM 1661 O  O   . HOH   M 5 .  ? -5.005  -16.958 4.708   1.00 45.85  ? 288 HOH   A O   1 
HETATM 1662 O  O   . HOH   M 5 .  ? -3.638  -17.930 1.442   1.00 42.34  ? 289 HOH   A O   1 
HETATM 1663 O  O   . HOH   M 5 .  ? -18.597 -2.522  -5.705  1.00 34.72  ? 290 HOH   A O   1 
HETATM 1664 O  O   . HOH   M 5 .  ? -7.528  -1.679  14.152  1.00 44.17  ? 291 HOH   A O   1 
HETATM 1665 O  O   . HOH   M 5 .  ? -28.044 -18.113 4.449   1.00 40.15  ? 292 HOH   A O   1 
HETATM 1666 O  O   . HOH   M 5 .  ? -15.487 -19.345 16.206  1.00 38.39  ? 293 HOH   A O   1 
HETATM 1667 O  O   . HOH   M 5 .  ? -5.936  -23.436 1.503   1.00 47.06  ? 294 HOH   A O   1 
HETATM 1668 O  O   . HOH   M 5 .  ? -5.729  -14.894 -8.788  1.00 51.49  ? 295 HOH   A O   1 
HETATM 1669 O  O   . HOH   M 5 .  ? -8.230  -17.605 17.531  1.00 36.39  ? 296 HOH   A O   1 
HETATM 1670 O  O   . HOH   M 5 .  ? -11.111 -1.394  -2.352  1.00 44.63  ? 297 HOH   A O   1 
HETATM 1671 O  O   . HOH   M 5 .  ? -24.516 -6.564  -0.213  1.00 37.55  ? 298 HOH   A O   1 
HETATM 1672 O  O   . HOH   M 5 .  ? -7.167  -23.511 -0.473  1.00 41.07  ? 299 HOH   A O   1 
HETATM 1673 O  O   . HOH   M 5 .  ? -12.049 -21.993 7.191   1.00 38.92  ? 300 HOH   A O   1 
HETATM 1674 O  O   . HOH   M 5 .  ? 3.035   -6.542  -9.624  1.00 55.10  ? 301 HOH   A O   1 
HETATM 1675 O  O   . HOH   M 5 .  ? -5.715  -0.996  6.898   1.00 45.36  ? 302 HOH   A O   1 
HETATM 1676 O  O   . HOH   M 5 .  ? -28.899 -11.815 -1.823  1.00 42.76  ? 303 HOH   A O   1 
HETATM 1677 O  O   . HOH   M 5 .  ? -9.477  -4.549  17.132  1.00 39.68  ? 304 HOH   A O   1 
HETATM 1678 O  O   . HOH   M 5 .  ? -15.542 -25.647 1.645   1.00 38.98  ? 305 HOH   A O   1 
HETATM 1679 O  O   . HOH   M 5 .  ? -8.350  -7.060  -8.119  1.00 47.63  ? 306 HOH   A O   1 
HETATM 1680 O  O   . HOH   M 5 .  ? -10.948 -9.253  -7.112  1.00 41.37  ? 307 HOH   A O   1 
HETATM 1681 O  O   . HOH   M 5 .  ? -17.375 -16.373 18.608  1.00 41.71  ? 308 HOH   A O   1 
HETATM 1682 O  O   . HOH   M 5 .  ? -5.777  -1.392  -1.025  1.00 51.53  ? 309 HOH   A O   1 
HETATM 1683 O  O   . HOH   M 5 .  ? -20.705 -2.613  -9.883  1.00 51.69  ? 310 HOH   A O   1 
HETATM 1684 O  O   . HOH   M 5 .  ? -18.824 -22.756 11.995  1.00 46.73  ? 311 HOH   A O   1 
HETATM 1685 O  O   . HOH   M 5 .  ? 4.547   -2.042  -3.100  1.00 50.17  ? 312 HOH   A O   1 
HETATM 1686 O  O   . HOH   M 5 .  ? -9.173  -22.076 -0.546  1.00 38.70  ? 313 HOH   A O   1 
HETATM 1687 O  O   . HOH   M 5 .  ? -19.844 -8.200  -11.996 1.00 37.97  ? 314 HOH   A O   1 
HETATM 1688 O  O   . HOH   M 5 .  ? -19.593 -16.646 18.171  1.00 34.11  ? 315 HOH   A O   1 
HETATM 1689 O  O   . HOH   M 5 .  ? -12.837 -2.328  17.748  1.00 35.26  ? 316 HOH   A O   1 
HETATM 1690 O  O   . HOH   M 5 .  ? -0.000  -6.356  -0.000  0.25 27.02  ? 317 HOH   A O   1 
HETATM 1691 O  O   . HOH   M 5 .  ? -4.507  -12.181 -9.099  1.00 44.49  ? 318 HOH   A O   1 
HETATM 1692 O  O   . HOH   M 5 .  ? -21.800 -21.744 11.848  1.00 37.98  ? 319 HOH   A O   1 
HETATM 1693 O  O   . HOH   M 5 .  ? -25.436 -9.658  -2.325  1.00 41.33  ? 320 HOH   A O   1 
HETATM 1694 O  O   . HOH   M 5 .  ? -31.180 -16.807 7.735   1.00 42.80  ? 321 HOH   A O   1 
HETATM 1695 O  O   . HOH   M 5 .  ? -14.658 8.725   4.669   1.00 41.62  ? 322 HOH   A O   1 
HETATM 1696 O  O   . HOH   M 5 .  ? -7.654  -5.548  16.468  1.00 45.23  ? 323 HOH   A O   1 
HETATM 1697 O  O   . HOH   M 5 .  ? -3.701  -7.419  -0.555  1.00 32.07  ? 324 HOH   A O   1 
HETATM 1698 O  O   . HOH   M 5 .  ? -6.857  -9.763  -6.966  1.00 41.49  ? 325 HOH   A O   1 
HETATM 1699 O  O   . HOH   M 5 .  ? -0.000  -15.941 -0.000  0.48 19.54  ? 326 HOH   A O   1 
HETATM 1700 O  O   . HOH   M 5 .  ? -31.564 -16.901 16.092  1.00 57.06  ? 327 HOH   A O   1 
HETATM 1701 O  O   . HOH   M 5 .  ? -7.171  -19.418 21.970  1.00 45.75  ? 328 HOH   A O   1 
HETATM 1702 O  O   . HOH   N 5 .  ? -36.329 -3.072  32.084  1.00 58.46  ? 201 HOH   B O   1 
HETATM 1703 O  O   . HOH   N 5 .  ? -20.800 7.658   13.257  1.00 25.03  ? 202 HOH   B O   1 
HETATM 1704 O  O   . HOH   N 5 .  ? -14.665 -14.563 28.803  1.00 51.12  ? 203 HOH   B O   1 
HETATM 1705 O  O   . HOH   N 5 .  ? -32.990 6.458   34.576  1.00 27.04  ? 204 HOH   B O   1 
HETATM 1706 O  O   . HOH   N 5 .  ? -25.344 -13.884 28.252  1.00 43.14  ? 205 HOH   B O   1 
HETATM 1707 O  O   . HOH   N 5 .  ? -22.089 8.236   26.425  1.00 13.73  ? 206 HOH   B O   1 
HETATM 1708 O  O   . HOH   N 5 .  ? -19.086 -14.905 27.315  1.00 44.16  ? 207 HOH   B O   1 
HETATM 1709 O  O   . HOH   N 5 .  ? -16.903 -6.864  32.736  1.00 31.84  ? 208 HOH   B O   1 
HETATM 1710 O  O   . HOH   N 5 .  ? -14.431 -3.765  33.186  1.00 37.76  ? 209 HOH   B O   1 
HETATM 1711 O  O   . HOH   N 5 .  ? -18.351 12.620  38.877  1.00 38.79  ? 210 HOH   B O   1 
HETATM 1712 O  O   . HOH   N 5 .  ? -31.511 13.611  27.737  1.00 25.78  ? 211 HOH   B O   1 
HETATM 1713 O  O   . HOH   N 5 .  ? -24.104 -1.219  13.207  1.00 27.49  ? 212 HOH   B O   1 
HETATM 1714 O  O   . HOH   N 5 .  ? -20.855 13.722  30.573  1.00 30.35  ? 213 HOH   B O   1 
HETATM 1715 O  O   . HOH   N 5 .  ? -28.422 -0.695  42.950  1.00 33.43  ? 214 HOH   B O   1 
HETATM 1716 O  O   . HOH   N 5 .  ? -10.403 2.428   28.960  1.00 25.14  ? 215 HOH   B O   1 
HETATM 1717 O  O   . HOH   N 5 .  ? -15.766 11.346  35.197  1.00 48.70  ? 216 HOH   B O   1 
HETATM 1718 O  O   . HOH   N 5 .  ? -12.981 -3.106  28.914  1.00 27.00  ? 217 HOH   B O   1 
HETATM 1719 O  O   . HOH   N 5 .  ? -22.054 -10.156 22.343  1.00 30.14  ? 218 HOH   B O   1 
HETATM 1720 O  O   . HOH   N 5 .  ? -24.953 2.024   15.824  1.00 13.39  ? 219 HOH   B O   1 
HETATM 1721 O  O   . HOH   N 5 .  ? -20.945 -13.992 33.348  1.00 21.59  ? 220 HOH   B O   1 
HETATM 1722 O  O   . HOH   N 5 .  ? -14.589 7.365   19.975  1.00 40.66  ? 221 HOH   B O   1 
HETATM 1723 O  O   . HOH   N 5 .  ? -15.751 12.080  26.293  1.00 37.36  ? 222 HOH   B O   1 
HETATM 1724 O  O   . HOH   N 5 .  ? -18.925 16.436  40.193  1.00 43.71  ? 223 HOH   B O   1 
HETATM 1725 O  O   . HOH   N 5 .  ? -28.945 6.976   23.903  1.00 14.07  ? 224 HOH   B O   1 
HETATM 1726 O  O   . HOH   N 5 .  ? -30.039 6.732   20.666  1.00 23.47  ? 225 HOH   B O   1 
HETATM 1727 O  O   . HOH   N 5 .  ? -14.108 6.898   15.708  1.00 36.13  ? 226 HOH   B O   1 
HETATM 1728 O  O   . HOH   N 5 .  ? -21.218 12.467  39.823  1.00 28.28  ? 227 HOH   B O   1 
HETATM 1729 O  O   . HOH   N 5 .  ? -13.581 11.967  42.473  1.00 46.06  ? 228 HOH   B O   1 
HETATM 1730 O  O   . HOH   N 5 .  ? -16.604 -9.445  31.126  1.00 28.52  ? 229 HOH   B O   1 
HETATM 1731 O  O   . HOH   N 5 .  ? -18.115 12.912  32.195  1.00 39.57  ? 230 HOH   B O   1 
HETATM 1732 O  O   . HOH   N 5 .  ? -10.582 2.622   26.193  1.00 50.87  ? 231 HOH   B O   1 
HETATM 1733 O  O   . HOH   N 5 .  ? -33.201 11.737  31.064  1.00 44.84  ? 232 HOH   B O   1 
HETATM 1734 O  O   . HOH   N 5 .  ? -30.109 0.342   37.171  1.00 21.88  ? 233 HOH   B O   1 
HETATM 1735 O  O   . HOH   N 5 .  ? -34.719 15.144  24.610  1.00 52.63  ? 234 HOH   B O   1 
HETATM 1736 O  O   . HOH   N 5 .  ? -27.027 8.463   39.056  1.00 33.80  ? 235 HOH   B O   1 
HETATM 1737 O  O   . HOH   N 5 .  ? -29.858 2.848   13.360  1.00 25.00  ? 236 HOH   B O   1 
HETATM 1738 O  O   . HOH   N 5 .  ? -8.142  6.314   39.275  1.00 54.39  ? 237 HOH   B O   1 
HETATM 1739 O  O   . HOH   N 5 .  ? -33.787 5.766   16.521  1.00 46.55  ? 238 HOH   B O   1 
HETATM 1740 O  O   . HOH   N 5 .  ? -24.539 11.161  18.728  1.00 46.24  ? 239 HOH   B O   1 
HETATM 1741 O  O   . HOH   N 5 .  ? -24.427 13.569  32.357  1.00 34.43  ? 240 HOH   B O   1 
HETATM 1742 O  O   . HOH   N 5 .  ? -16.781 6.240   18.483  1.00 40.80  ? 241 HOH   B O   1 
HETATM 1743 O  O   . HOH   N 5 .  ? -29.391 -2.585  45.091  1.00 49.76  ? 242 HOH   B O   1 
HETATM 1744 O  O   . HOH   N 5 .  ? -13.851 -0.933  21.144  1.00 27.19  ? 243 HOH   B O   1 
HETATM 1745 O  O   . HOH   N 5 .  ? -28.462 13.961  30.025  1.00 22.95  ? 244 HOH   B O   1 
HETATM 1746 O  O   . HOH   N 5 .  ? -14.379 -7.267  22.463  1.00 22.24  ? 245 HOH   B O   1 
HETATM 1747 O  O   . HOH   N 5 .  ? -28.765 -6.092  36.677  1.00 25.17  ? 246 HOH   B O   1 
HETATM 1748 O  O   . HOH   N 5 .  ? -28.023 -1.446  13.279  1.00 40.53  ? 247 HOH   B O   1 
HETATM 1749 O  O   . HOH   N 5 .  ? -31.855 -6.651  29.546  1.00 32.27  ? 248 HOH   B O   1 
HETATM 1750 O  O   . HOH   N 5 .  ? -23.618 6.888   44.071  1.00 46.11  ? 249 HOH   B O   1 
HETATM 1751 O  O   . HOH   N 5 .  ? -38.180 3.330   30.301  1.00 36.86  ? 250 HOH   B O   1 
HETATM 1752 O  O   . HOH   N 5 .  ? -18.098 11.189  35.921  1.00 21.90  ? 251 HOH   B O   1 
HETATM 1753 O  O   . HOH   N 5 .  ? -20.091 11.333  14.850  1.00 41.73  ? 252 HOH   B O   1 
HETATM 1754 O  O   . HOH   N 5 .  ? -12.074 6.695   32.672  1.00 24.68  ? 253 HOH   B O   1 
HETATM 1755 O  O   . HOH   N 5 .  ? -20.902 -6.345  35.847  1.00 28.46  ? 254 HOH   B O   1 
HETATM 1756 O  O   . HOH   N 5 .  ? -37.378 6.370   29.449  1.00 29.42  ? 255 HOH   B O   1 
HETATM 1757 O  O   . HOH   N 5 .  ? -34.650 2.337   36.633  1.00 21.60  ? 256 HOH   B O   1 
HETATM 1758 O  O   . HOH   N 5 .  ? -34.196 9.777   31.783  1.00 35.93  ? 257 HOH   B O   1 
HETATM 1759 O  O   . HOH   N 5 .  ? -29.890 -3.347  36.570  1.00 21.87  ? 258 HOH   B O   1 
HETATM 1760 O  O   . HOH   N 5 .  ? -22.713 -8.214  34.927  1.00 16.71  ? 259 HOH   B O   1 
HETATM 1761 O  O   . HOH   N 5 .  ? -4.720  0.060   42.683  1.00 26.63  ? 260 HOH   B O   1 
HETATM 1762 O  O   . HOH   N 5 .  ? -18.780 6.843   19.226  1.00 51.27  ? 261 HOH   B O   1 
HETATM 1763 O  O   . HOH   N 5 .  ? -28.437 -5.513  39.234  1.00 36.32  ? 262 HOH   B O   1 
HETATM 1764 O  O   . HOH   N 5 .  ? -17.585 12.901  29.993  1.00 29.90  ? 263 HOH   B O   1 
HETATM 1765 O  O   . HOH   N 5 .  ? -32.623 -0.865  25.645  1.00 33.14  ? 264 HOH   B O   1 
HETATM 1766 O  O   . HOH   N 5 .  ? -27.105 1.597   11.677  1.00 32.80  ? 265 HOH   B O   1 
HETATM 1767 O  O   . HOH   N 5 .  ? -21.494 15.635  32.975  1.00 54.20  ? 266 HOH   B O   1 
HETATM 1768 O  O   . HOH   N 5 .  ? -28.912 10.044  23.891  1.00 20.13  ? 267 HOH   B O   1 
HETATM 1769 O  O   . HOH   N 5 .  ? -23.658 12.687  21.181  1.00 30.93  ? 268 HOH   B O   1 
HETATM 1770 O  O   . HOH   N 5 .  ? -32.802 -7.597  20.620  1.00 47.16  ? 269 HOH   B O   1 
HETATM 1771 O  O   . HOH   N 5 .  ? -32.697 0.249   36.521  1.00 23.52  ? 270 HOH   B O   1 
HETATM 1772 O  O   . HOH   N 5 .  ? -40.346 4.535   30.977  1.00 44.85  ? 271 HOH   B O   1 
HETATM 1773 O  O   . HOH   N 5 .  ? -10.322 -1.067  36.256  1.00 37.02  ? 272 HOH   B O   1 
HETATM 1774 O  O   . HOH   N 5 .  ? -29.931 -9.084  15.683  1.00 48.64  ? 273 HOH   B O   1 
HETATM 1775 O  O   . HOH   N 5 .  ? -30.434 -2.444  38.895  1.00 43.39  ? 274 HOH   B O   1 
HETATM 1776 O  O   . HOH   N 5 .  ? -18.035 4.741   20.039  1.00 32.83  ? 275 HOH   B O   1 
HETATM 1777 O  O   . HOH   N 5 .  ? -24.079 6.948   46.361  1.00 44.98  ? 276 HOH   B O   1 
HETATM 1778 O  O   . HOH   N 5 .  ? -24.539 -18.374 29.854  1.00 46.16  ? 277 HOH   B O   1 
HETATM 1779 O  O   . HOH   N 5 .  ? -26.509 8.925   15.140  1.00 29.02  ? 278 HOH   B O   1 
HETATM 1780 O  O   . HOH   N 5 .  ? -26.162 -12.478 29.966  1.00 34.51  ? 279 HOH   B O   1 
HETATM 1781 O  O   . HOH   N 5 .  ? -15.624 9.784   17.353  1.00 41.06  ? 280 HOH   B O   1 
HETATM 1782 O  O   . HOH   N 5 .  ? -35.498 0.108   24.922  1.00 39.59  ? 281 HOH   B O   1 
HETATM 1783 O  O   . HOH   N 5 .  ? -18.399 -7.467  36.663  1.00 39.92  ? 282 HOH   B O   1 
HETATM 1784 O  O   . HOH   N 5 .  ? -18.306 -3.852  44.980  1.00 49.83  ? 283 HOH   B O   1 
HETATM 1785 O  O   . HOH   N 5 .  ? -29.649 0.529   39.490  1.00 49.86  ? 284 HOH   B O   1 
HETATM 1786 O  O   . HOH   N 5 .  ? -28.404 8.605   14.174  1.00 37.14  ? 285 HOH   B O   1 
HETATM 1787 O  O   . HOH   N 5 .  ? -31.430 0.954   11.352  1.00 49.08  ? 286 HOH   B O   1 
HETATM 1788 O  O   . HOH   N 5 .  ? -15.662 -4.594  20.320  1.00 38.58  ? 287 HOH   B O   1 
HETATM 1789 O  O   . HOH   N 5 .  ? -13.555 -9.336  40.580  1.00 54.66  ? 288 HOH   B O   1 
HETATM 1790 O  O   . HOH   N 5 .  ? -30.274 -2.844  17.852  1.00 41.66  ? 289 HOH   B O   1 
HETATM 1791 O  O   . HOH   N 5 .  ? -7.864  6.153   43.149  1.00 45.02  ? 290 HOH   B O   1 
HETATM 1792 O  O   . HOH   N 5 .  ? -21.754 -10.559 35.494  1.00 38.85  ? 291 HOH   B O   1 
HETATM 1793 O  O   . HOH   N 5 .  ? -17.817 11.861  41.148  1.00 42.95  ? 292 HOH   B O   1 
HETATM 1794 O  O   . HOH   N 5 .  ? -26.245 -5.139  15.001  1.00 38.09  ? 293 HOH   B O   1 
HETATM 1795 O  O   . HOH   N 5 .  ? -30.885 5.314   13.474  1.00 39.82  ? 294 HOH   B O   1 
HETATM 1796 O  O   . HOH   N 5 .  ? -27.384 13.707  24.410  1.00 45.58  ? 295 HOH   B O   1 
HETATM 1797 O  O   . HOH   N 5 .  ? -28.103 -3.959  15.653  1.00 38.78  ? 296 HOH   B O   1 
HETATM 1798 O  O   . HOH   N 5 .  ? -36.699 9.457   32.711  1.00 43.90  ? 297 HOH   B O   1 
HETATM 1799 O  O   . HOH   N 5 .  ? -13.972 9.220   31.576  1.00 50.19  ? 298 HOH   B O   1 
HETATM 1800 O  O   . HOH   N 5 .  ? -15.883 -7.373  30.932  1.00 42.72  ? 299 HOH   B O   1 
HETATM 1801 O  O   . HOH   N 5 .  ? -31.981 -3.661  35.746  1.00 34.98  ? 300 HOH   B O   1 
HETATM 1802 O  O   . HOH   N 5 .  ? -20.366 -7.478  37.890  1.00 47.92  ? 301 HOH   B O   1 
HETATM 1803 O  O   . HOH   N 5 .  ? -19.729 -11.069 34.566  1.00 49.96  ? 302 HOH   B O   1 
HETATM 1804 O  O   . HOH   N 5 .  ? -16.497 -8.296  34.684  1.00 47.27  ? 303 HOH   B O   1 
HETATM 1805 O  O   . HOH   N 5 .  ? -22.255 9.661   13.733  1.00 31.72  ? 304 HOH   B O   1 
HETATM 1806 O  O   . HOH   N 5 .  ? -20.508 -12.964 24.959  1.00 48.22  ? 305 HOH   B O   1 
HETATM 1807 O  O   . HOH   N 5 .  ? -26.585 9.990   18.307  1.00 32.28  ? 306 HOH   B O   1 
HETATM 1808 O  O   . HOH   N 5 .  ? -15.260 3.055   19.040  1.00 45.01  ? 307 HOH   B O   1 
HETATM 1809 O  O   . HOH   N 5 .  ? -27.715 11.728  22.775  1.00 50.42  ? 308 HOH   B O   1 
HETATM 1810 O  O   . HOH   N 5 .  ? -31.925 11.377  23.808  1.00 36.67  ? 309 HOH   B O   1 
HETATM 1811 O  O   . HOH   N 5 .  ? -30.286 7.647   13.605  1.00 52.27  ? 310 HOH   B O   1 
HETATM 1812 O  O   . HOH   N 5 .  ? -7.351  8.157   40.556  1.00 52.93  ? 311 HOH   B O   1 
HETATM 1813 O  O   . HOH   N 5 .  ? -31.412 -1.964  14.441  1.00 47.72  ? 312 HOH   B O   1 
HETATM 1814 O  O   . HOH   N 5 .  ? -32.277 0.131   13.494  1.00 49.66  ? 313 HOH   B O   1 
HETATM 1815 O  O   . HOH   N 5 .  ? -31.073 13.822  25.046  1.00 44.13  ? 314 HOH   B O   1 
HETATM 1816 O  O   . HOH   N 5 .  ? -28.022 10.925  19.649  1.00 38.40  ? 315 HOH   B O   1 
HETATM 1817 O  O   . HOH   N 5 .  ? -21.110 -3.287  46.208  1.00 48.73  ? 316 HOH   B O   1 
HETATM 1818 O  O   . HOH   N 5 .  ? -8.626  7.297   36.555  1.00 54.11  ? 317 HOH   B O   1 
HETATM 1819 O  O   . HOH   N 5 .  ? -9.219  9.662   31.415  1.00 43.43  ? 318 HOH   B O   1 
# 
