data_9G94
# 
_entry.id   9G94 
# 
_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   9G94         pdb_00009g94 10.2210/pdb9g94/pdb 
WWPDB D_1292140582 ?            ?                   
# 
_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                        9G94 
_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         Sergei 
_pdbx_contact_author.name_last          Strelkov 
_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 
'Osipov, E.M.'   1 0000-0003-3101-2867 
'Vantieghem, T.' 2 0000-0002-1452-9584 
'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' 10714.236 3   ? ? ? ? 
2 non-polymer syn '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine'        224.057   3   ? ? ? ? 
3 non-polymer nat 'SULFATE ION'                                      96.063    5   ? ? ? ? 
4 water       nat water                                              18.015    211 ? ? ? ? 
# 
_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       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine' A1D73 
3 'SULFATE ION'                               SO4   
4 water                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  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 CYS 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 
A1D73 non-polymer         . '4-(4-bromanyl-1~{H}-pyrazol-3-yl)pyridine' ? 'C8 H6 Br N3'    224.057 
ALA   'L-peptide linking' y ALANINE                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                             ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                    ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                   ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                      ? 'C6 H15 N2 O2 1' 147.195 
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 CYS 65 64 64 CYS CYS 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  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO 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 CYS 65 64 64 CYS CYS 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 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 30 ASP ASP C . n 
C 1 32 GLY 32 31 31 GLY GLY C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 CYS 65 64 64 CYS CYS C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D73 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D73 
_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 
D 2 A1D73 1  101 101 A1D73 C32 A . 
E 3 SO4   1  102 95  SO4   SO4 A . 
F 3 SO4   1  103 96  SO4   SO4 A . 
G 2 A1D73 1  101 101 A1D73 C32 B . 
H 3 SO4   1  102 1   SO4   SO4 B . 
I 3 SO4   1  103 3   SO4   SO4 B . 
J 2 A1D73 1  101 101 A1D73 C32 C . 
K 3 SO4   1  102 2   SO4   SO4 C . 
L 4 HOH   1  201 139 HOH   HOH A . 
L 4 HOH   2  202 66  HOH   HOH A . 
L 4 HOH   3  203 174 HOH   HOH A . 
L 4 HOH   4  204 141 HOH   HOH A . 
L 4 HOH   5  205 54  HOH   HOH A . 
L 4 HOH   6  206 181 HOH   HOH A . 
L 4 HOH   7  207 200 HOH   HOH A . 
L 4 HOH   8  208 128 HOH   HOH A . 
L 4 HOH   9  209 157 HOH   HOH A . 
L 4 HOH   10 210 67  HOH   HOH A . 
L 4 HOH   11 211 188 HOH   HOH A . 
L 4 HOH   12 212 25  HOH   HOH A . 
L 4 HOH   13 213 145 HOH   HOH A . 
L 4 HOH   14 214 33  HOH   HOH A . 
L 4 HOH   15 215 86  HOH   HOH A . 
L 4 HOH   16 216 75  HOH   HOH A . 
L 4 HOH   17 217 6   HOH   HOH A . 
L 4 HOH   18 218 36  HOH   HOH A . 
L 4 HOH   19 219 199 HOH   HOH A . 
L 4 HOH   20 220 10  HOH   HOH A . 
L 4 HOH   21 221 85  HOH   HOH A . 
L 4 HOH   22 222 191 HOH   HOH A . 
L 4 HOH   23 223 20  HOH   HOH A . 
L 4 HOH   24 224 7   HOH   HOH A . 
L 4 HOH   25 225 68  HOH   HOH A . 
L 4 HOH   26 226 120 HOH   HOH A . 
L 4 HOH   27 227 118 HOH   HOH A . 
L 4 HOH   28 228 77  HOH   HOH A . 
L 4 HOH   29 229 45  HOH   HOH A . 
L 4 HOH   30 230 82  HOH   HOH A . 
L 4 HOH   31 231 1   HOH   HOH A . 
L 4 HOH   32 232 167 HOH   HOH A . 
L 4 HOH   33 233 140 HOH   HOH A . 
L 4 HOH   34 234 2   HOH   HOH A . 
L 4 HOH   35 235 49  HOH   HOH A . 
L 4 HOH   36 236 11  HOH   HOH A . 
L 4 HOH   37 237 107 HOH   HOH A . 
L 4 HOH   38 238 30  HOH   HOH A . 
L 4 HOH   39 239 73  HOH   HOH A . 
L 4 HOH   40 240 35  HOH   HOH A . 
L 4 HOH   41 241 126 HOH   HOH A . 
L 4 HOH   42 242 71  HOH   HOH A . 
L 4 HOH   43 243 111 HOH   HOH A . 
L 4 HOH   44 244 129 HOH   HOH A . 
L 4 HOH   45 245 18  HOH   HOH A . 
L 4 HOH   46 246 112 HOH   HOH A . 
L 4 HOH   47 247 103 HOH   HOH A . 
L 4 HOH   48 248 26  HOH   HOH A . 
L 4 HOH   49 249 132 HOH   HOH A . 
L 4 HOH   50 250 13  HOH   HOH A . 
L 4 HOH   51 251 143 HOH   HOH A . 
L 4 HOH   52 252 24  HOH   HOH A . 
L 4 HOH   53 253 34  HOH   HOH A . 
L 4 HOH   54 254 17  HOH   HOH A . 
L 4 HOH   55 255 27  HOH   HOH A . 
L 4 HOH   56 256 207 HOH   HOH A . 
L 4 HOH   57 257 179 HOH   HOH A . 
L 4 HOH   58 258 28  HOH   HOH A . 
L 4 HOH   59 259 202 HOH   HOH A . 
L 4 HOH   60 260 29  HOH   HOH A . 
L 4 HOH   61 261 193 HOH   HOH A . 
L 4 HOH   62 262 59  HOH   HOH A . 
L 4 HOH   63 263 62  HOH   HOH A . 
L 4 HOH   64 264 138 HOH   HOH A . 
L 4 HOH   65 265 117 HOH   HOH A . 
L 4 HOH   66 266 40  HOH   HOH A . 
L 4 HOH   67 267 106 HOH   HOH A . 
L 4 HOH   68 268 47  HOH   HOH A . 
L 4 HOH   69 269 8   HOH   HOH A . 
L 4 HOH   70 270 211 HOH   HOH A . 
L 4 HOH   71 271 144 HOH   HOH A . 
L 4 HOH   72 272 84  HOH   HOH A . 
L 4 HOH   73 273 15  HOH   HOH A . 
L 4 HOH   74 274 19  HOH   HOH A . 
L 4 HOH   75 275 180 HOH   HOH A . 
L 4 HOH   76 276 206 HOH   HOH A . 
L 4 HOH   77 277 87  HOH   HOH A . 
L 4 HOH   78 278 104 HOH   HOH A . 
L 4 HOH   79 279 98  HOH   HOH A . 
L 4 HOH   80 280 53  HOH   HOH A . 
L 4 HOH   81 281 52  HOH   HOH A . 
L 4 HOH   82 282 209 HOH   HOH A . 
L 4 HOH   83 283 150 HOH   HOH A . 
L 4 HOH   84 284 65  HOH   HOH A . 
L 4 HOH   85 285 156 HOH   HOH A . 
L 4 HOH   86 286 204 HOH   HOH A . 
L 4 HOH   87 287 165 HOH   HOH A . 
L 4 HOH   88 288 173 HOH   HOH A . 
L 4 HOH   89 289 149 HOH   HOH A . 
L 4 HOH   90 290 130 HOH   HOH A . 
L 4 HOH   91 291 192 HOH   HOH A . 
L 4 HOH   92 292 31  HOH   HOH A . 
L 4 HOH   93 293 198 HOH   HOH A . 
L 4 HOH   94 294 102 HOH   HOH A . 
L 4 HOH   95 295 95  HOH   HOH A . 
M 4 HOH   1  201 135 HOH   HOH B . 
M 4 HOH   2  202 155 HOH   HOH B . 
M 4 HOH   3  203 171 HOH   HOH B . 
M 4 HOH   4  204 148 HOH   HOH B . 
M 4 HOH   5  205 76  HOH   HOH B . 
M 4 HOH   6  206 69  HOH   HOH B . 
M 4 HOH   7  207 166 HOH   HOH B . 
M 4 HOH   8  208 214 HOH   HOH B . 
M 4 HOH   9  209 9   HOH   HOH B . 
M 4 HOH   10 210 16  HOH   HOH B . 
M 4 HOH   11 211 196 HOH   HOH B . 
M 4 HOH   12 212 56  HOH   HOH B . 
M 4 HOH   13 213 121 HOH   HOH B . 
M 4 HOH   14 214 113 HOH   HOH B . 
M 4 HOH   15 215 63  HOH   HOH B . 
M 4 HOH   16 216 101 HOH   HOH B . 
M 4 HOH   17 217 109 HOH   HOH B . 
M 4 HOH   18 218 90  HOH   HOH B . 
M 4 HOH   19 219 5   HOH   HOH B . 
M 4 HOH   20 220 182 HOH   HOH B . 
M 4 HOH   21 221 61  HOH   HOH B . 
M 4 HOH   22 222 4   HOH   HOH B . 
M 4 HOH   23 223 48  HOH   HOH B . 
M 4 HOH   24 224 12  HOH   HOH B . 
M 4 HOH   25 225 74  HOH   HOH B . 
M 4 HOH   26 226 208 HOH   HOH B . 
M 4 HOH   27 227 116 HOH   HOH B . 
M 4 HOH   28 228 194 HOH   HOH B . 
M 4 HOH   29 229 60  HOH   HOH B . 
M 4 HOH   30 230 21  HOH   HOH B . 
M 4 HOH   31 231 97  HOH   HOH B . 
M 4 HOH   32 232 205 HOH   HOH B . 
M 4 HOH   33 233 177 HOH   HOH B . 
M 4 HOH   34 234 88  HOH   HOH B . 
M 4 HOH   35 235 94  HOH   HOH B . 
M 4 HOH   36 236 50  HOH   HOH B . 
M 4 HOH   37 237 175 HOH   HOH B . 
M 4 HOH   38 238 44  HOH   HOH B . 
M 4 HOH   39 239 134 HOH   HOH B . 
M 4 HOH   40 240 32  HOH   HOH B . 
M 4 HOH   41 241 58  HOH   HOH B . 
M 4 HOH   42 242 78  HOH   HOH B . 
M 4 HOH   43 243 38  HOH   HOH B . 
M 4 HOH   44 244 91  HOH   HOH B . 
M 4 HOH   45 245 168 HOH   HOH B . 
M 4 HOH   46 246 22  HOH   HOH B . 
M 4 HOH   47 247 169 HOH   HOH B . 
M 4 HOH   48 248 210 HOH   HOH B . 
M 4 HOH   49 249 195 HOH   HOH B . 
M 4 HOH   50 250 163 HOH   HOH B . 
M 4 HOH   51 251 81  HOH   HOH B . 
M 4 HOH   52 252 127 HOH   HOH B . 
M 4 HOH   53 253 197 HOH   HOH B . 
M 4 HOH   54 254 185 HOH   HOH B . 
M 4 HOH   55 255 201 HOH   HOH B . 
M 4 HOH   56 256 152 HOH   HOH B . 
M 4 HOH   57 257 186 HOH   HOH B . 
M 4 HOH   58 258 178 HOH   HOH B . 
M 4 HOH   59 259 83  HOH   HOH B . 
N 4 HOH   1  201 158 HOH   HOH C . 
N 4 HOH   2  202 176 HOH   HOH C . 
N 4 HOH   3  203 133 HOH   HOH C . 
N 4 HOH   4  204 114 HOH   HOH C . 
N 4 HOH   5  205 105 HOH   HOH C . 
N 4 HOH   6  206 136 HOH   HOH C . 
N 4 HOH   7  207 147 HOH   HOH C . 
N 4 HOH   8  208 108 HOH   HOH C . 
N 4 HOH   9  209 96  HOH   HOH C . 
N 4 HOH   10 210 89  HOH   HOH C . 
N 4 HOH   11 211 79  HOH   HOH C . 
N 4 HOH   12 212 99  HOH   HOH C . 
N 4 HOH   13 213 14  HOH   HOH C . 
N 4 HOH   14 214 187 HOH   HOH C . 
N 4 HOH   15 215 213 HOH   HOH C . 
N 4 HOH   16 216 154 HOH   HOH C . 
N 4 HOH   17 217 42  HOH   HOH C . 
N 4 HOH   18 218 183 HOH   HOH C . 
N 4 HOH   19 219 23  HOH   HOH C . 
N 4 HOH   20 220 3   HOH   HOH C . 
N 4 HOH   21 221 115 HOH   HOH C . 
N 4 HOH   22 222 70  HOH   HOH C . 
N 4 HOH   23 223 122 HOH   HOH C . 
N 4 HOH   24 224 110 HOH   HOH C . 
N 4 HOH   25 225 39  HOH   HOH C . 
N 4 HOH   26 226 41  HOH   HOH C . 
N 4 HOH   27 227 151 HOH   HOH C . 
N 4 HOH   28 228 142 HOH   HOH C . 
N 4 HOH   29 229 100 HOH   HOH C . 
N 4 HOH   30 230 119 HOH   HOH C . 
N 4 HOH   31 231 159 HOH   HOH C . 
N 4 HOH   32 232 131 HOH   HOH C . 
N 4 HOH   33 233 92  HOH   HOH C . 
N 4 HOH   34 234 123 HOH   HOH C . 
N 4 HOH   35 235 124 HOH   HOH C . 
N 4 HOH   36 236 51  HOH   HOH C . 
N 4 HOH   37 237 64  HOH   HOH C . 
N 4 HOH   38 238 203 HOH   HOH C . 
N 4 HOH   39 239 37  HOH   HOH C . 
N 4 HOH   40 240 43  HOH   HOH C . 
N 4 HOH   41 241 125 HOH   HOH C . 
N 4 HOH   42 242 160 HOH   HOH C . 
N 4 HOH   43 243 93  HOH   HOH C . 
N 4 HOH   44 244 146 HOH   HOH C . 
N 4 HOH   45 245 57  HOH   HOH C . 
N 4 HOH   46 246 189 HOH   HOH C . 
N 4 HOH   47 247 46  HOH   HOH C . 
N 4 HOH   48 248 80  HOH   HOH C . 
N 4 HOH   49 249 55  HOH   HOH C . 
N 4 HOH   50 250 184 HOH   HOH C . 
N 4 HOH   51 251 164 HOH   HOH C . 
N 4 HOH   52 252 212 HOH   HOH C . 
N 4 HOH   53 253 137 HOH   HOH C . 
N 4 HOH   54 254 153 HOH   HOH C . 
N 4 HOH   55 255 72  HOH   HOH C . 
N 4 HOH   56 256 172 HOH   HOH C . 
N 4 HOH   57 257 190 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 73 ? CG  ? A LYS 74 CG  
2  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
3  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
4  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
5  1 Y 1 B ASP 66 ? CG  ? B ASP 67 CG  
6  1 Y 1 B ASP 66 ? OD1 ? B ASP 67 OD1 
7  1 Y 1 B ASP 66 ? OD2 ? B ASP 67 OD2 
8  1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
9  1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
10 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
11 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
12 1 Y 1 B GLU 79 ? CG  ? B GLU 80 CG  
13 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
14 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
15 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
16 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
17 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
18 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
19 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
20 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
21 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
22 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
23 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
24 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
25 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
26 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
27 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
28 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
29 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
30 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
31 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
32 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
# 
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                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G94 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.426 
_cell.length_a_esd                 ? 
_cell.length_b                     41.930 
_cell.length_b_esd                 ? 
_cell.length_c                     157.431 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9G94 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G94 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.17 
_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    
;2.2 M ammonium sulfate
0.2 M ammonium iodide
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-07-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000000 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G94 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.73 
_reflns.d_resolution_low                               40.52 
_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                                     29757 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.79 
_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                                0.122 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       393065 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.117 
_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                                    1.73 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           57213 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4245 
_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                               13.5 
_reflns_shell.pdbx_chi_squared                              0.52 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.1 
_reflns_shell.pdbx_Rrim_I_all                               2.308 
_reflns_shell.pdbx_Rpim_I_all                               0.621 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.643 
_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                                  2.221 
_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                                 9G94 
_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                            1.73 
_refine.ls_d_res_low                             40.52 
_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                     29688 
_refine.ls_number_reflns_R_free                  1477 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2075 
_refine.ls_R_factor_R_free                       0.2553 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2051 
_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                          1.34 
_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                 25.26 
_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                            0.25 
_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                       1.73 
_refine_hist.d_res_low                        40.52 
_refine_hist.number_atoms_solvent             211 
_refine_hist.number_atoms_total               2484 
_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        2212 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         61 
_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' ? 0.003  ? 2379 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.588  ? 3233 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.644 ? 890  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 290  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 434  ? 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' 1.73 1.78  . . 147 2476 100.00 . . . . 0.3255 . . . . . . . . . . . 0.3618 
'X-RAY DIFFRACTION' 1.78 1.85  . . 148 2499 100.00 . . . . 0.2722 . . . . . . . . . . . 0.3291 
'X-RAY DIFFRACTION' 1.85 1.92  . . 164 2486 100.00 . . . . 0.2514 . . . . . . . . . . . 0.2778 
'X-RAY DIFFRACTION' 1.92 2.01  . . 126 2537 100.00 . . . . 0.2366 . . . . . . . . . . . 0.3137 
'X-RAY DIFFRACTION' 2.01 2.11  . . 121 2545 100.00 . . . . 0.2295 . . . . . . . . . . . 0.2868 
'X-RAY DIFFRACTION' 2.11 2.25  . . 126 2527 100.00 . . . . 0.2174 . . . . . . . . . . . 0.3017 
'X-RAY DIFFRACTION' 2.25 2.42  . . 103 2596 100.00 . . . . 0.2130 . . . . . . . . . . . 0.2800 
'X-RAY DIFFRACTION' 2.42 2.66  . . 158 2546 100.00 . . . . 0.2200 . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 2.66 3.05  . . 114 2592 100.00 . . . . 0.2155 . . . . . . . . . . . 0.2929 
'X-RAY DIFFRACTION' 3.05 3.84  . . 138 2630 100.00 . . . . 0.1903 . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 3.84 40.52 . . 132 2777 100.00 . . . . 0.1810 . . . . . . . . . . . 0.2089 
# 
_struct.entry_id                     9G94 
_struct.title                        'Crystal structure of HRP-2 PWWP domain in complex with compound 32' 
_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        9G94 
_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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
_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 9G94 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 9G94 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 9G94 C 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 9G94 GLY A 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 1 
2 9G94 GLY B 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 2 
3 9G94 GLY C 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 3 
# 
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 
3 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,D,E,F,L 
2 1 B,G,H,I,M 
3 1 C,J,K,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 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 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 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 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 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 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 ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
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 ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   9G94 
_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 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NH2 
_pdbx_validate_symm_contact.auth_asym_id_1    C 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     74 
_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    N03 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    A1D73 
_pdbx_validate_symm_contact.auth_seq_id_2     101 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_535 
_pdbx_validate_symm_contact.dist              1.36 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -154.35 65.58   
2 1 ASP B 30 ? ? -55.74  105.44  
3 1 ASN B 87 ? ? -160.36 65.85   
4 1 ASN C 87 ? ? -148.90 59.65   
5 1 ALA C 90 ? ? -78.34  -167.15 
# 
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 C GLY 0  ? C GLY 1  
4 1 Y 1 C MET 1  ? C MET 2  
5 1 Y 1 C PRO 2  ? C PRO 3  
6 1 Y 1 C SER 93 ? C SER 94 
# 
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 
A1D73 C01  C  Y N 1   
A1D73 C02  C  Y N 2   
A1D73 C04  C  Y N 3   
A1D73 C05  C  Y N 4   
A1D73 C06  C  Y N 5   
A1D73 C07  C  Y N 6   
A1D73 C08  C  Y N 7   
A1D73 C09  C  Y N 8   
A1D73 N03  N  Y N 9   
A1D73 N10  N  Y N 10  
A1D73 N11  N  Y N 11  
A1D73 BR12 BR N N 12  
A1D73 H1   H  N N 13  
A1D73 H2   H  N N 14  
A1D73 H3   H  N N 15  
A1D73 H4   H  N N 16  
A1D73 H5   H  N N 17  
A1D73 H6   H  N N 18  
ALA   N    N  N N 19  
ALA   CA   C  N S 20  
ALA   C    C  N N 21  
ALA   O    O  N N 22  
ALA   CB   C  N N 23  
ALA   OXT  O  N N 24  
ALA   H    H  N N 25  
ALA   H2   H  N N 26  
ALA   HA   H  N N 27  
ALA   HB1  H  N N 28  
ALA   HB2  H  N N 29  
ALA   HB3  H  N N 30  
ALA   HXT  H  N N 31  
ARG   N    N  N N 32  
ARG   CA   C  N S 33  
ARG   C    C  N N 34  
ARG   O    O  N N 35  
ARG   CB   C  N N 36  
ARG   CG   C  N N 37  
ARG   CD   C  N N 38  
ARG   NE   N  N N 39  
ARG   CZ   C  N N 40  
ARG   NH1  N  N N 41  
ARG   NH2  N  N N 42  
ARG   OXT  O  N N 43  
ARG   H    H  N N 44  
ARG   H2   H  N N 45  
ARG   HA   H  N N 46  
ARG   HB2  H  N N 47  
ARG   HB3  H  N N 48  
ARG   HG2  H  N N 49  
ARG   HG3  H  N N 50  
ARG   HD2  H  N N 51  
ARG   HD3  H  N N 52  
ARG   HE   H  N N 53  
ARG   HH11 H  N N 54  
ARG   HH12 H  N N 55  
ARG   HH21 H  N N 56  
ARG   HH22 H  N N 57  
ARG   HXT  H  N N 58  
ASN   N    N  N N 59  
ASN   CA   C  N S 60  
ASN   C    C  N N 61  
ASN   O    O  N N 62  
ASN   CB   C  N N 63  
ASN   CG   C  N N 64  
ASN   OD1  O  N N 65  
ASN   ND2  N  N N 66  
ASN   OXT  O  N N 67  
ASN   H    H  N N 68  
ASN   H2   H  N N 69  
ASN   HA   H  N N 70  
ASN   HB2  H  N N 71  
ASN   HB3  H  N N 72  
ASN   HD21 H  N N 73  
ASN   HD22 H  N N 74  
ASN   HXT  H  N N 75  
ASP   N    N  N N 76  
ASP   CA   C  N S 77  
ASP   C    C  N N 78  
ASP   O    O  N N 79  
ASP   CB   C  N N 80  
ASP   CG   C  N N 81  
ASP   OD1  O  N N 82  
ASP   OD2  O  N N 83  
ASP   OXT  O  N N 84  
ASP   H    H  N N 85  
ASP   H2   H  N N 86  
ASP   HA   H  N N 87  
ASP   HB2  H  N N 88  
ASP   HB3  H  N N 89  
ASP   HD2  H  N N 90  
ASP   HXT  H  N N 91  
CYS   N    N  N N 92  
CYS   CA   C  N R 93  
CYS   C    C  N N 94  
CYS   O    O  N N 95  
CYS   CB   C  N N 96  
CYS   SG   S  N N 97  
CYS   OXT  O  N N 98  
CYS   H    H  N N 99  
CYS   H2   H  N N 100 
CYS   HA   H  N N 101 
CYS   HB2  H  N N 102 
CYS   HB3  H  N N 103 
CYS   HG   H  N N 104 
CYS   HXT  H  N N 105 
GLN   N    N  N N 106 
GLN   CA   C  N S 107 
GLN   C    C  N N 108 
GLN   O    O  N N 109 
GLN   CB   C  N N 110 
GLN   CG   C  N N 111 
GLN   CD   C  N N 112 
GLN   OE1  O  N N 113 
GLN   NE2  N  N N 114 
GLN   OXT  O  N N 115 
GLN   H    H  N N 116 
GLN   H2   H  N N 117 
GLN   HA   H  N N 118 
GLN   HB2  H  N N 119 
GLN   HB3  H  N N 120 
GLN   HG2  H  N N 121 
GLN   HG3  H  N N 122 
GLN   HE21 H  N N 123 
GLN   HE22 H  N N 124 
GLN   HXT  H  N N 125 
GLU   N    N  N N 126 
GLU   CA   C  N S 127 
GLU   C    C  N N 128 
GLU   O    O  N N 129 
GLU   CB   C  N N 130 
GLU   CG   C  N N 131 
GLU   CD   C  N N 132 
GLU   OE1  O  N N 133 
GLU   OE2  O  N N 134 
GLU   OXT  O  N N 135 
GLU   H    H  N N 136 
GLU   H2   H  N N 137 
GLU   HA   H  N N 138 
GLU   HB2  H  N N 139 
GLU   HB3  H  N N 140 
GLU   HG2  H  N N 141 
GLU   HG3  H  N N 142 
GLU   HE2  H  N N 143 
GLU   HXT  H  N N 144 
GLY   N    N  N N 145 
GLY   CA   C  N N 146 
GLY   C    C  N N 147 
GLY   O    O  N N 148 
GLY   OXT  O  N N 149 
GLY   H    H  N N 150 
GLY   H2   H  N N 151 
GLY   HA2  H  N N 152 
GLY   HA3  H  N N 153 
GLY   HXT  H  N N 154 
HIS   N    N  N N 155 
HIS   CA   C  N S 156 
HIS   C    C  N N 157 
HIS   O    O  N N 158 
HIS   CB   C  N N 159 
HIS   CG   C  Y N 160 
HIS   ND1  N  Y N 161 
HIS   CD2  C  Y N 162 
HIS   CE1  C  Y N 163 
HIS   NE2  N  Y N 164 
HIS   OXT  O  N N 165 
HIS   H    H  N N 166 
HIS   H2   H  N N 167 
HIS   HA   H  N N 168 
HIS   HB2  H  N N 169 
HIS   HB3  H  N N 170 
HIS   HD1  H  N N 171 
HIS   HD2  H  N N 172 
HIS   HE1  H  N N 173 
HIS   HE2  H  N N 174 
HIS   HXT  H  N N 175 
HOH   O    O  N N 176 
HOH   H1   H  N N 177 
HOH   H2   H  N N 178 
ILE   N    N  N N 179 
ILE   CA   C  N S 180 
ILE   C    C  N N 181 
ILE   O    O  N N 182 
ILE   CB   C  N S 183 
ILE   CG1  C  N N 184 
ILE   CG2  C  N N 185 
ILE   CD1  C  N N 186 
ILE   OXT  O  N N 187 
ILE   H    H  N N 188 
ILE   H2   H  N N 189 
ILE   HA   H  N N 190 
ILE   HB   H  N N 191 
ILE   HG12 H  N N 192 
ILE   HG13 H  N N 193 
ILE   HG21 H  N N 194 
ILE   HG22 H  N N 195 
ILE   HG23 H  N N 196 
ILE   HD11 H  N N 197 
ILE   HD12 H  N N 198 
ILE   HD13 H  N N 199 
ILE   HXT  H  N N 200 
LEU   N    N  N N 201 
LEU   CA   C  N S 202 
LEU   C    C  N N 203 
LEU   O    O  N N 204 
LEU   CB   C  N N 205 
LEU   CG   C  N N 206 
LEU   CD1  C  N N 207 
LEU   CD2  C  N N 208 
LEU   OXT  O  N N 209 
LEU   H    H  N N 210 
LEU   H2   H  N N 211 
LEU   HA   H  N N 212 
LEU   HB2  H  N N 213 
LEU   HB3  H  N N 214 
LEU   HG   H  N N 215 
LEU   HD11 H  N N 216 
LEU   HD12 H  N N 217 
LEU   HD13 H  N N 218 
LEU   HD21 H  N N 219 
LEU   HD22 H  N N 220 
LEU   HD23 H  N N 221 
LEU   HXT  H  N N 222 
LYS   N    N  N N 223 
LYS   CA   C  N S 224 
LYS   C    C  N N 225 
LYS   O    O  N N 226 
LYS   CB   C  N N 227 
LYS   CG   C  N N 228 
LYS   CD   C  N N 229 
LYS   CE   C  N N 230 
LYS   NZ   N  N N 231 
LYS   OXT  O  N N 232 
LYS   H    H  N N 233 
LYS   H2   H  N N 234 
LYS   HA   H  N N 235 
LYS   HB2  H  N N 236 
LYS   HB3  H  N N 237 
LYS   HG2  H  N N 238 
LYS   HG3  H  N N 239 
LYS   HD2  H  N N 240 
LYS   HD3  H  N N 241 
LYS   HE2  H  N N 242 
LYS   HE3  H  N N 243 
LYS   HZ1  H  N N 244 
LYS   HZ2  H  N N 245 
LYS   HZ3  H  N N 246 
LYS   HXT  H  N N 247 
MET   N    N  N N 248 
MET   CA   C  N S 249 
MET   C    C  N N 250 
MET   O    O  N N 251 
MET   CB   C  N N 252 
MET   CG   C  N N 253 
MET   SD   S  N N 254 
MET   CE   C  N N 255 
MET   OXT  O  N N 256 
MET   H    H  N N 257 
MET   H2   H  N N 258 
MET   HA   H  N N 259 
MET   HB2  H  N N 260 
MET   HB3  H  N N 261 
MET   HG2  H  N N 262 
MET   HG3  H  N N 263 
MET   HE1  H  N N 264 
MET   HE2  H  N N 265 
MET   HE3  H  N N 266 
MET   HXT  H  N N 267 
PHE   N    N  N N 268 
PHE   CA   C  N S 269 
PHE   C    C  N N 270 
PHE   O    O  N N 271 
PHE   CB   C  N N 272 
PHE   CG   C  Y N 273 
PHE   CD1  C  Y N 274 
PHE   CD2  C  Y N 275 
PHE   CE1  C  Y N 276 
PHE   CE2  C  Y N 277 
PHE   CZ   C  Y N 278 
PHE   OXT  O  N N 279 
PHE   H    H  N N 280 
PHE   H2   H  N N 281 
PHE   HA   H  N N 282 
PHE   HB2  H  N N 283 
PHE   HB3  H  N N 284 
PHE   HD1  H  N N 285 
PHE   HD2  H  N N 286 
PHE   HE1  H  N N 287 
PHE   HE2  H  N N 288 
PHE   HZ   H  N N 289 
PHE   HXT  H  N N 290 
PRO   N    N  N N 291 
PRO   CA   C  N S 292 
PRO   C    C  N N 293 
PRO   O    O  N N 294 
PRO   CB   C  N N 295 
PRO   CG   C  N N 296 
PRO   CD   C  N N 297 
PRO   OXT  O  N N 298 
PRO   H    H  N N 299 
PRO   HA   H  N N 300 
PRO   HB2  H  N N 301 
PRO   HB3  H  N N 302 
PRO   HG2  H  N N 303 
PRO   HG3  H  N N 304 
PRO   HD2  H  N N 305 
PRO   HD3  H  N N 306 
PRO   HXT  H  N N 307 
SER   N    N  N N 308 
SER   CA   C  N S 309 
SER   C    C  N N 310 
SER   O    O  N N 311 
SER   CB   C  N N 312 
SER   OG   O  N N 313 
SER   OXT  O  N N 314 
SER   H    H  N N 315 
SER   H2   H  N N 316 
SER   HA   H  N N 317 
SER   HB2  H  N N 318 
SER   HB3  H  N N 319 
SER   HG   H  N N 320 
SER   HXT  H  N N 321 
SO4   S    S  N N 322 
SO4   O1   O  N N 323 
SO4   O2   O  N N 324 
SO4   O3   O  N N 325 
SO4   O4   O  N N 326 
THR   N    N  N N 327 
THR   CA   C  N S 328 
THR   C    C  N N 329 
THR   O    O  N N 330 
THR   CB   C  N R 331 
THR   OG1  O  N N 332 
THR   CG2  C  N N 333 
THR   OXT  O  N N 334 
THR   H    H  N N 335 
THR   H2   H  N N 336 
THR   HA   H  N N 337 
THR   HB   H  N N 338 
THR   HG1  H  N N 339 
THR   HG21 H  N N 340 
THR   HG22 H  N N 341 
THR   HG23 H  N N 342 
THR   HXT  H  N N 343 
TRP   N    N  N N 344 
TRP   CA   C  N S 345 
TRP   C    C  N N 346 
TRP   O    O  N N 347 
TRP   CB   C  N N 348 
TRP   CG   C  Y N 349 
TRP   CD1  C  Y N 350 
TRP   CD2  C  Y N 351 
TRP   NE1  N  Y N 352 
TRP   CE2  C  Y N 353 
TRP   CE3  C  Y N 354 
TRP   CZ2  C  Y N 355 
TRP   CZ3  C  Y N 356 
TRP   CH2  C  Y N 357 
TRP   OXT  O  N N 358 
TRP   H    H  N N 359 
TRP   H2   H  N N 360 
TRP   HA   H  N N 361 
TRP   HB2  H  N N 362 
TRP   HB3  H  N N 363 
TRP   HD1  H  N N 364 
TRP   HE1  H  N N 365 
TRP   HE3  H  N N 366 
TRP   HZ2  H  N N 367 
TRP   HZ3  H  N N 368 
TRP   HH2  H  N N 369 
TRP   HXT  H  N N 370 
TYR   N    N  N N 371 
TYR   CA   C  N S 372 
TYR   C    C  N N 373 
TYR   O    O  N N 374 
TYR   CB   C  N N 375 
TYR   CG   C  Y N 376 
TYR   CD1  C  Y N 377 
TYR   CD2  C  Y N 378 
TYR   CE1  C  Y N 379 
TYR   CE2  C  Y N 380 
TYR   CZ   C  Y N 381 
TYR   OH   O  N N 382 
TYR   OXT  O  N N 383 
TYR   H    H  N N 384 
TYR   H2   H  N N 385 
TYR   HA   H  N N 386 
TYR   HB2  H  N N 387 
TYR   HB3  H  N N 388 
TYR   HD1  H  N N 389 
TYR   HD2  H  N N 390 
TYR   HE1  H  N N 391 
TYR   HE2  H  N N 392 
TYR   HH   H  N N 393 
TYR   HXT  H  N N 394 
VAL   N    N  N N 395 
VAL   CA   C  N S 396 
VAL   C    C  N N 397 
VAL   O    O  N N 398 
VAL   CB   C  N N 399 
VAL   CG1  C  N N 400 
VAL   CG2  C  N N 401 
VAL   OXT  O  N N 402 
VAL   H    H  N N 403 
VAL   H2   H  N N 404 
VAL   HA   H  N N 405 
VAL   HB   H  N N 406 
VAL   HG11 H  N N 407 
VAL   HG12 H  N N 408 
VAL   HG13 H  N N 409 
VAL   HG21 H  N N 410 
VAL   HG22 H  N N 411 
VAL   HG23 H  N N 412 
VAL   HXT  H  N N 413 
# 
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 
A1D73 C09  N10  sing Y N 1   
A1D73 C09  C08  doub Y N 2   
A1D73 BR12 C08  sing N N 3   
A1D73 N10  N11  sing Y N 4   
A1D73 C08  C07  sing Y N 5   
A1D73 N11  C07  doub Y N 6   
A1D73 C07  C06  sing N N 7   
A1D73 C05  C06  doub Y N 8   
A1D73 C05  C04  sing Y N 9   
A1D73 C06  C01  sing Y N 10  
A1D73 C04  N03  doub Y N 11  
A1D73 C01  C02  doub Y N 12  
A1D73 N03  C02  sing Y N 13  
A1D73 C01  H1   sing N N 14  
A1D73 C02  H2   sing N N 15  
A1D73 C04  H3   sing N N 16  
A1D73 C05  H4   sing N N 17  
A1D73 C09  H5   sing N N 18  
A1D73 N10  H6   sing N N 19  
ALA   N    CA   sing N N 20  
ALA   N    H    sing N N 21  
ALA   N    H2   sing N N 22  
ALA   CA   C    sing N N 23  
ALA   CA   CB   sing N N 24  
ALA   CA   HA   sing N N 25  
ALA   C    O    doub N N 26  
ALA   C    OXT  sing N N 27  
ALA   CB   HB1  sing N N 28  
ALA   CB   HB2  sing N N 29  
ALA   CB   HB3  sing N N 30  
ALA   OXT  HXT  sing N N 31  
ARG   N    CA   sing N N 32  
ARG   N    H    sing N N 33  
ARG   N    H2   sing N N 34  
ARG   CA   C    sing N N 35  
ARG   CA   CB   sing N N 36  
ARG   CA   HA   sing N N 37  
ARG   C    O    doub N N 38  
ARG   C    OXT  sing N N 39  
ARG   CB   CG   sing N N 40  
ARG   CB   HB2  sing N N 41  
ARG   CB   HB3  sing N N 42  
ARG   CG   CD   sing N N 43  
ARG   CG   HG2  sing N N 44  
ARG   CG   HG3  sing N N 45  
ARG   CD   NE   sing N N 46  
ARG   CD   HD2  sing N N 47  
ARG   CD   HD3  sing N N 48  
ARG   NE   CZ   sing N N 49  
ARG   NE   HE   sing N N 50  
ARG   CZ   NH1  sing N N 51  
ARG   CZ   NH2  doub N N 52  
ARG   NH1  HH11 sing N N 53  
ARG   NH1  HH12 sing N N 54  
ARG   NH2  HH21 sing N N 55  
ARG   NH2  HH22 sing N N 56  
ARG   OXT  HXT  sing N N 57  
ASN   N    CA   sing N N 58  
ASN   N    H    sing N N 59  
ASN   N    H2   sing N N 60  
ASN   CA   C    sing N N 61  
ASN   CA   CB   sing N N 62  
ASN   CA   HA   sing N N 63  
ASN   C    O    doub N N 64  
ASN   C    OXT  sing N N 65  
ASN   CB   CG   sing N N 66  
ASN   CB   HB2  sing N N 67  
ASN   CB   HB3  sing N N 68  
ASN   CG   OD1  doub N N 69  
ASN   CG   ND2  sing N N 70  
ASN   ND2  HD21 sing N N 71  
ASN   ND2  HD22 sing N N 72  
ASN   OXT  HXT  sing N N 73  
ASP   N    CA   sing N N 74  
ASP   N    H    sing N N 75  
ASP   N    H2   sing N N 76  
ASP   CA   C    sing N N 77  
ASP   CA   CB   sing N N 78  
ASP   CA   HA   sing N N 79  
ASP   C    O    doub N N 80  
ASP   C    OXT  sing N N 81  
ASP   CB   CG   sing N N 82  
ASP   CB   HB2  sing N N 83  
ASP   CB   HB3  sing N N 84  
ASP   CG   OD1  doub N N 85  
ASP   CG   OD2  sing N N 86  
ASP   OD2  HD2  sing N N 87  
ASP   OXT  HXT  sing N N 88  
CYS   N    CA   sing N N 89  
CYS   N    H    sing N N 90  
CYS   N    H2   sing N N 91  
CYS   CA   C    sing N N 92  
CYS   CA   CB   sing N N 93  
CYS   CA   HA   sing N N 94  
CYS   C    O    doub N N 95  
CYS   C    OXT  sing N N 96  
CYS   CB   SG   sing N N 97  
CYS   CB   HB2  sing N N 98  
CYS   CB   HB3  sing N N 99  
CYS   SG   HG   sing N N 100 
CYS   OXT  HXT  sing N N 101 
GLN   N    CA   sing N N 102 
GLN   N    H    sing N N 103 
GLN   N    H2   sing N N 104 
GLN   CA   C    sing N N 105 
GLN   CA   CB   sing N N 106 
GLN   CA   HA   sing N N 107 
GLN   C    O    doub N N 108 
GLN   C    OXT  sing N N 109 
GLN   CB   CG   sing N N 110 
GLN   CB   HB2  sing N N 111 
GLN   CB   HB3  sing N N 112 
GLN   CG   CD   sing N N 113 
GLN   CG   HG2  sing N N 114 
GLN   CG   HG3  sing N N 115 
GLN   CD   OE1  doub N N 116 
GLN   CD   NE2  sing N N 117 
GLN   NE2  HE21 sing N N 118 
GLN   NE2  HE22 sing N N 119 
GLN   OXT  HXT  sing N N 120 
GLU   N    CA   sing N N 121 
GLU   N    H    sing N N 122 
GLU   N    H2   sing N N 123 
GLU   CA   C    sing N N 124 
GLU   CA   CB   sing N N 125 
GLU   CA   HA   sing N N 126 
GLU   C    O    doub N N 127 
GLU   C    OXT  sing N N 128 
GLU   CB   CG   sing N N 129 
GLU   CB   HB2  sing N N 130 
GLU   CB   HB3  sing N N 131 
GLU   CG   CD   sing N N 132 
GLU   CG   HG2  sing N N 133 
GLU   CG   HG3  sing N N 134 
GLU   CD   OE1  doub N N 135 
GLU   CD   OE2  sing N N 136 
GLU   OE2  HE2  sing N N 137 
GLU   OXT  HXT  sing N N 138 
GLY   N    CA   sing N N 139 
GLY   N    H    sing N N 140 
GLY   N    H2   sing N N 141 
GLY   CA   C    sing N N 142 
GLY   CA   HA2  sing N N 143 
GLY   CA   HA3  sing N N 144 
GLY   C    O    doub N N 145 
GLY   C    OXT  sing N N 146 
GLY   OXT  HXT  sing N N 147 
HIS   N    CA   sing N N 148 
HIS   N    H    sing N N 149 
HIS   N    H2   sing N N 150 
HIS   CA   C    sing N N 151 
HIS   CA   CB   sing N N 152 
HIS   CA   HA   sing N N 153 
HIS   C    O    doub N N 154 
HIS   C    OXT  sing N N 155 
HIS   CB   CG   sing N N 156 
HIS   CB   HB2  sing N N 157 
HIS   CB   HB3  sing N N 158 
HIS   CG   ND1  sing Y N 159 
HIS   CG   CD2  doub Y N 160 
HIS   ND1  CE1  doub Y N 161 
HIS   ND1  HD1  sing N N 162 
HIS   CD2  NE2  sing Y N 163 
HIS   CD2  HD2  sing N N 164 
HIS   CE1  NE2  sing Y N 165 
HIS   CE1  HE1  sing N N 166 
HIS   NE2  HE2  sing N N 167 
HIS   OXT  HXT  sing N N 168 
HOH   O    H1   sing N N 169 
HOH   O    H2   sing N N 170 
ILE   N    CA   sing N N 171 
ILE   N    H    sing N N 172 
ILE   N    H2   sing N N 173 
ILE   CA   C    sing N N 174 
ILE   CA   CB   sing N N 175 
ILE   CA   HA   sing N N 176 
ILE   C    O    doub N N 177 
ILE   C    OXT  sing N N 178 
ILE   CB   CG1  sing N N 179 
ILE   CB   CG2  sing N N 180 
ILE   CB   HB   sing N N 181 
ILE   CG1  CD1  sing N N 182 
ILE   CG1  HG12 sing N N 183 
ILE   CG1  HG13 sing N N 184 
ILE   CG2  HG21 sing N N 185 
ILE   CG2  HG22 sing N N 186 
ILE   CG2  HG23 sing N N 187 
ILE   CD1  HD11 sing N N 188 
ILE   CD1  HD12 sing N N 189 
ILE   CD1  HD13 sing N N 190 
ILE   OXT  HXT  sing N N 191 
LEU   N    CA   sing N N 192 
LEU   N    H    sing N N 193 
LEU   N    H2   sing N N 194 
LEU   CA   C    sing N N 195 
LEU   CA   CB   sing N N 196 
LEU   CA   HA   sing N N 197 
LEU   C    O    doub N N 198 
LEU   C    OXT  sing N N 199 
LEU   CB   CG   sing N N 200 
LEU   CB   HB2  sing N N 201 
LEU   CB   HB3  sing N N 202 
LEU   CG   CD1  sing N N 203 
LEU   CG   CD2  sing N N 204 
LEU   CG   HG   sing N N 205 
LEU   CD1  HD11 sing N N 206 
LEU   CD1  HD12 sing N N 207 
LEU   CD1  HD13 sing N N 208 
LEU   CD2  HD21 sing N N 209 
LEU   CD2  HD22 sing N N 210 
LEU   CD2  HD23 sing N N 211 
LEU   OXT  HXT  sing N N 212 
LYS   N    CA   sing N N 213 
LYS   N    H    sing N N 214 
LYS   N    H2   sing N N 215 
LYS   CA   C    sing N N 216 
LYS   CA   CB   sing N N 217 
LYS   CA   HA   sing N N 218 
LYS   C    O    doub N N 219 
LYS   C    OXT  sing N N 220 
LYS   CB   CG   sing N N 221 
LYS   CB   HB2  sing N N 222 
LYS   CB   HB3  sing N N 223 
LYS   CG   CD   sing N N 224 
LYS   CG   HG2  sing N N 225 
LYS   CG   HG3  sing N N 226 
LYS   CD   CE   sing N N 227 
LYS   CD   HD2  sing N N 228 
LYS   CD   HD3  sing N N 229 
LYS   CE   NZ   sing N N 230 
LYS   CE   HE2  sing N N 231 
LYS   CE   HE3  sing N N 232 
LYS   NZ   HZ1  sing N N 233 
LYS   NZ   HZ2  sing N N 234 
LYS   NZ   HZ3  sing N N 235 
LYS   OXT  HXT  sing N N 236 
MET   N    CA   sing N N 237 
MET   N    H    sing N N 238 
MET   N    H2   sing N N 239 
MET   CA   C    sing N N 240 
MET   CA   CB   sing N N 241 
MET   CA   HA   sing N N 242 
MET   C    O    doub N N 243 
MET   C    OXT  sing N N 244 
MET   CB   CG   sing N N 245 
MET   CB   HB2  sing N N 246 
MET   CB   HB3  sing N N 247 
MET   CG   SD   sing N N 248 
MET   CG   HG2  sing N N 249 
MET   CG   HG3  sing N N 250 
MET   SD   CE   sing N N 251 
MET   CE   HE1  sing N N 252 
MET   CE   HE2  sing N N 253 
MET   CE   HE3  sing N N 254 
MET   OXT  HXT  sing N N 255 
PHE   N    CA   sing N N 256 
PHE   N    H    sing N N 257 
PHE   N    H2   sing N N 258 
PHE   CA   C    sing N N 259 
PHE   CA   CB   sing N N 260 
PHE   CA   HA   sing N N 261 
PHE   C    O    doub N N 262 
PHE   C    OXT  sing N N 263 
PHE   CB   CG   sing N N 264 
PHE   CB   HB2  sing N N 265 
PHE   CB   HB3  sing N N 266 
PHE   CG   CD1  doub Y N 267 
PHE   CG   CD2  sing Y N 268 
PHE   CD1  CE1  sing Y N 269 
PHE   CD1  HD1  sing N N 270 
PHE   CD2  CE2  doub Y N 271 
PHE   CD2  HD2  sing N N 272 
PHE   CE1  CZ   doub Y N 273 
PHE   CE1  HE1  sing N N 274 
PHE   CE2  CZ   sing Y N 275 
PHE   CE2  HE2  sing N N 276 
PHE   CZ   HZ   sing N N 277 
PHE   OXT  HXT  sing N N 278 
PRO   N    CA   sing N N 279 
PRO   N    CD   sing N N 280 
PRO   N    H    sing N N 281 
PRO   CA   C    sing N N 282 
PRO   CA   CB   sing N N 283 
PRO   CA   HA   sing N N 284 
PRO   C    O    doub N N 285 
PRO   C    OXT  sing N N 286 
PRO   CB   CG   sing N N 287 
PRO   CB   HB2  sing N N 288 
PRO   CB   HB3  sing N N 289 
PRO   CG   CD   sing N N 290 
PRO   CG   HG2  sing N N 291 
PRO   CG   HG3  sing N N 292 
PRO   CD   HD2  sing N N 293 
PRO   CD   HD3  sing N N 294 
PRO   OXT  HXT  sing N N 295 
SER   N    CA   sing N N 296 
SER   N    H    sing N N 297 
SER   N    H2   sing N N 298 
SER   CA   C    sing N N 299 
SER   CA   CB   sing N N 300 
SER   CA   HA   sing N N 301 
SER   C    O    doub N N 302 
SER   C    OXT  sing N N 303 
SER   CB   OG   sing N N 304 
SER   CB   HB2  sing N N 305 
SER   CB   HB3  sing N N 306 
SER   OG   HG   sing N N 307 
SER   OXT  HXT  sing N N 308 
SO4   S    O1   doub N N 309 
SO4   S    O2   doub N N 310 
SO4   S    O3   sing N N 311 
SO4   S    O4   sing N N 312 
THR   N    CA   sing N N 313 
THR   N    H    sing N N 314 
THR   N    H2   sing N N 315 
THR   CA   C    sing N N 316 
THR   CA   CB   sing N N 317 
THR   CA   HA   sing N N 318 
THR   C    O    doub N N 319 
THR   C    OXT  sing N N 320 
THR   CB   OG1  sing N N 321 
THR   CB   CG2  sing N N 322 
THR   CB   HB   sing N N 323 
THR   OG1  HG1  sing N N 324 
THR   CG2  HG21 sing N N 325 
THR   CG2  HG22 sing N N 326 
THR   CG2  HG23 sing N N 327 
THR   OXT  HXT  sing N N 328 
TRP   N    CA   sing N N 329 
TRP   N    H    sing N N 330 
TRP   N    H2   sing N N 331 
TRP   CA   C    sing N N 332 
TRP   CA   CB   sing N N 333 
TRP   CA   HA   sing N N 334 
TRP   C    O    doub N N 335 
TRP   C    OXT  sing N N 336 
TRP   CB   CG   sing N N 337 
TRP   CB   HB2  sing N N 338 
TRP   CB   HB3  sing N N 339 
TRP   CG   CD1  doub Y N 340 
TRP   CG   CD2  sing Y N 341 
TRP   CD1  NE1  sing Y N 342 
TRP   CD1  HD1  sing N N 343 
TRP   CD2  CE2  doub Y N 344 
TRP   CD2  CE3  sing Y N 345 
TRP   NE1  CE2  sing Y N 346 
TRP   NE1  HE1  sing N N 347 
TRP   CE2  CZ2  sing Y N 348 
TRP   CE3  CZ3  doub Y N 349 
TRP   CE3  HE3  sing N N 350 
TRP   CZ2  CH2  doub Y N 351 
TRP   CZ2  HZ2  sing N N 352 
TRP   CZ3  CH2  sing Y N 353 
TRP   CZ3  HZ3  sing N N 354 
TRP   CH2  HH2  sing N N 355 
TRP   OXT  HXT  sing N N 356 
TYR   N    CA   sing N N 357 
TYR   N    H    sing N N 358 
TYR   N    H2   sing N N 359 
TYR   CA   C    sing N N 360 
TYR   CA   CB   sing N N 361 
TYR   CA   HA   sing N N 362 
TYR   C    O    doub N N 363 
TYR   C    OXT  sing N N 364 
TYR   CB   CG   sing N N 365 
TYR   CB   HB2  sing N N 366 
TYR   CB   HB3  sing N N 367 
TYR   CG   CD1  doub Y N 368 
TYR   CG   CD2  sing Y N 369 
TYR   CD1  CE1  sing Y N 370 
TYR   CD1  HD1  sing N N 371 
TYR   CD2  CE2  doub Y N 372 
TYR   CD2  HD2  sing N N 373 
TYR   CE1  CZ   doub Y N 374 
TYR   CE1  HE1  sing N N 375 
TYR   CE2  CZ   sing Y N 376 
TYR   CE2  HE2  sing N N 377 
TYR   CZ   OH   sing N N 378 
TYR   OH   HH   sing N N 379 
TYR   OXT  HXT  sing N N 380 
VAL   N    CA   sing N N 381 
VAL   N    H    sing N N 382 
VAL   N    H2   sing N N 383 
VAL   CA   C    sing N N 384 
VAL   CA   CB   sing N N 385 
VAL   CA   HA   sing N N 386 
VAL   C    O    doub N N 387 
VAL   C    OXT  sing N N 388 
VAL   CB   CG1  sing N N 389 
VAL   CB   CG2  sing N N 390 
VAL   CB   HB   sing N N 391 
VAL   CG1  HG11 sing N N 392 
VAL   CG1  HG12 sing N N 393 
VAL   CG1  HG13 sing N N 394 
VAL   CG2  HG21 sing N N 395 
VAL   CG2  HG22 sing N N 396 
VAL   CG2  HG23 sing N N 397 
VAL   OXT  HXT  sing N N 398 
# 
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 1SC24N   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                    9G94 
_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]   0.024139 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023849 
_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]   0.006352 
_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  ? 1.238   3.703   2.702   1.00 57.69 ? 1   MET   A N    1 
ATOM   2    C  CA   . MET   A 1 2  ? -0.010  3.383   2.018   1.00 51.32 ? 1   MET   A CA   1 
ATOM   3    C  C    . MET   A 1 2  ? 0.279   2.412   0.871   1.00 49.47 ? 1   MET   A C    1 
ATOM   4    O  O    . MET   A 1 2  ? 1.252   2.589   0.136   1.00 46.13 ? 1   MET   A O    1 
ATOM   5    C  CB   . MET   A 1 2  ? -0.692  4.666   1.523   1.00 56.24 ? 1   MET   A CB   1 
ATOM   6    C  CG   . MET   A 1 2  ? -2.171  4.539   1.123   1.00 50.57 ? 1   MET   A CG   1 
ATOM   7    S  SD   . MET   A 1 2  ? -3.372  4.139   2.428   1.00 60.80 ? 1   MET   A SD   1 
ATOM   8    C  CE   . MET   A 1 2  ? -2.555  4.728   3.912   1.00 49.05 ? 1   MET   A CE   1 
ATOM   9    N  N    . PRO   A 1 3  ? -0.557  1.379   0.743   1.00 43.86 ? 2   PRO   A N    1 
ATOM   10   C  CA   . PRO   A 1 3  ? -0.222  0.254   -0.140  1.00 38.99 ? 2   PRO   A CA   1 
ATOM   11   C  C    . PRO   A 1 3  ? -0.077  0.654   -1.601  1.00 38.16 ? 2   PRO   A C    1 
ATOM   12   O  O    . PRO   A 1 3  ? -0.866  1.432   -2.140  1.00 33.99 ? 2   PRO   A O    1 
ATOM   13   C  CB   . PRO   A 1 3  ? -1.402  -0.705  0.053   1.00 33.11 ? 2   PRO   A CB   1 
ATOM   14   C  CG   . PRO   A 1 3  ? -1.895  -0.401  1.432   1.00 45.77 ? 2   PRO   A CG   1 
ATOM   15   C  CD   . PRO   A 1 3  ? -1.726  1.083   1.589   1.00 44.45 ? 2   PRO   A CD   1 
ATOM   16   N  N    . HIS   A 1 4  ? 0.940   0.085   -2.239  1.00 35.39 ? 3   HIS   A N    1 
ATOM   17   C  CA   . HIS   A 1 4  ? 1.124   0.145   -3.675  1.00 34.60 ? 3   HIS   A CA   1 
ATOM   18   C  C    . HIS   A 1 4  ? 0.636   -1.163  -4.290  1.00 36.25 ? 3   HIS   A C    1 
ATOM   19   O  O    . HIS   A 1 4  ? 0.166   -2.070  -3.597  1.00 33.81 ? 3   HIS   A O    1 
ATOM   20   C  CB   . HIS   A 1 4  ? 2.596   0.398   -4.017  1.00 37.34 ? 3   HIS   A CB   1 
ATOM   21   C  CG   . HIS   A 1 4  ? 3.121   1.710   -3.520  1.00 43.98 ? 3   HIS   A CG   1 
ATOM   22   N  ND1  . HIS   A 1 4  ? 2.889   2.173   -2.242  1.00 59.75 ? 3   HIS   A ND1  1 
ATOM   23   C  CD2  . HIS   A 1 4  ? 3.876   2.654   -4.130  1.00 59.15 ? 3   HIS   A CD2  1 
ATOM   24   C  CE1  . HIS   A 1 4  ? 3.472   3.349   -2.089  1.00 56.54 ? 3   HIS   A CE1  1 
ATOM   25   N  NE2  . HIS   A 1 4  ? 4.079   3.663   -3.220  1.00 52.37 ? 3   HIS   A NE2  1 
ATOM   26   N  N    . ALA   A 1 5  ? 0.747   -1.263  -5.611  1.00 30.93 ? 4   ALA   A N    1 
ATOM   27   C  CA   . ALA   A 1 5  ? 0.506   -2.538  -6.261  1.00 26.74 ? 4   ALA   A CA   1 
ATOM   28   C  C    . ALA   A 1 5  ? 1.620   -3.517  -5.904  1.00 28.41 ? 4   ALA   A C    1 
ATOM   29   O  O    . ALA   A 1 5  ? 2.698   -3.132  -5.439  1.00 27.58 ? 4   ALA   A O    1 
ATOM   30   C  CB   . ALA   A 1 5  ? 0.414   -2.364  -7.777  1.00 35.91 ? 4   ALA   A CB   1 
ATOM   31   N  N    . PHE   A 1 6  ? 1.346   -4.800  -6.109  1.00 26.70 ? 5   PHE   A N    1 
ATOM   32   C  CA   . PHE   A 1 6  ? 2.359   -5.813  -5.848  1.00 28.80 ? 5   PHE   A CA   1 
ATOM   33   C  C    . PHE   A 1 6  ? 3.506   -5.691  -6.842  1.00 29.76 ? 5   PHE   A C    1 
ATOM   34   O  O    . PHE   A 1 6  ? 3.302   -5.367  -8.015  1.00 28.43 ? 5   PHE   A O    1 
ATOM   35   C  CB   . PHE   A 1 6  ? 1.753   -7.211  -5.913  1.00 29.79 ? 5   PHE   A CB   1 
ATOM   36   C  CG   . PHE   A 1 6  ? 0.984   -7.589  -4.677  1.00 26.64 ? 5   PHE   A CG   1 
ATOM   37   C  CD1  . PHE   A 1 6  ? 1.641   -7.780  -3.470  1.00 28.82 ? 5   PHE   A CD1  1 
ATOM   38   C  CD2  . PHE   A 1 6  ? -0.388  -7.755  -4.719  1.00 26.80 ? 5   PHE   A CD2  1 
ATOM   39   C  CE1  . PHE   A 1 6  ? 0.943   -8.125  -2.324  1.00 28.01 ? 5   PHE   A CE1  1 
ATOM   40   C  CE2  . PHE   A 1 6  ? -1.092  -8.106  -3.569  1.00 24.74 ? 5   PHE   A CE2  1 
ATOM   41   C  CZ   . PHE   A 1 6  ? -0.423  -8.289  -2.375  1.00 25.30 ? 5   PHE   A CZ   1 
ATOM   42   N  N    . LYS   A 1 7  ? 4.716   -5.948  -6.366  1.00 26.44 ? 6   LYS   A N    1 
ATOM   43   C  CA   . LYS   A 1 7  ? 5.915   -5.851  -7.182  1.00 24.48 ? 6   LYS   A CA   1 
ATOM   44   C  C    . LYS   A 1 7  ? 6.814   -7.037  -6.877  1.00 25.66 ? 6   LYS   A C    1 
ATOM   45   O  O    . LYS   A 1 7  ? 6.722   -7.634  -5.798  1.00 24.97 ? 6   LYS   A O    1 
ATOM   46   C  CB   . LYS   A 1 7  ? 6.662   -4.535  -6.922  1.00 25.92 ? 6   LYS   A CB   1 
ATOM   47   C  CG   . LYS   A 1 7  ? 7.223   -4.409  -5.517  1.00 25.16 ? 6   LYS   A CG   1 
ATOM   48   C  CD   . LYS   A 1 7  ? 7.870   -3.047  -5.302  1.00 36.47 ? 6   LYS   A CD   1 
ATOM   49   C  CE   . LYS   A 1 7  ? 8.395   -2.905  -3.883  1.00 32.19 ? 6   LYS   A CE   1 
ATOM   50   N  NZ   . LYS   A 1 7  ? 7.304   -3.073  -2.886  1.00 37.63 ? 6   LYS   A NZ   1 
ATOM   51   N  N    . PRO   A 1 8  ? 7.683   -7.414  -7.814  1.00 25.03 ? 7   PRO   A N    1 
ATOM   52   C  CA   . PRO   A 1 8  ? 8.616   -8.516  -7.556  1.00 26.25 ? 7   PRO   A CA   1 
ATOM   53   C  C    . PRO   A 1 8  ? 9.413   -8.276  -6.281  1.00 23.03 ? 7   PRO   A C    1 
ATOM   54   O  O    . PRO   A 1 8  ? 9.900   -7.171  -6.027  1.00 26.17 ? 7   PRO   A O    1 
ATOM   55   C  CB   . PRO   A 1 8  ? 9.517   -8.513  -8.796  1.00 25.63 ? 7   PRO   A CB   1 
ATOM   56   C  CG   . PRO   A 1 8  ? 8.670   -7.919  -9.864  1.00 33.14 ? 7   PRO   A CG   1 
ATOM   57   C  CD   . PRO   A 1 8  ? 7.790   -6.908  -9.196  1.00 27.13 ? 7   PRO   A CD   1 
ATOM   58   N  N    . GLY   A 1 9  ? 9.513   -9.322  -5.461  1.00 23.68 ? 8   GLY   A N    1 
ATOM   59   C  CA   . GLY   A 1 9  ? 10.187  -9.257  -4.187  1.00 19.94 ? 8   GLY   A CA   1 
ATOM   60   C  C    . GLY   A 1 9  ? 9.265   -9.127  -2.992  1.00 22.96 ? 8   GLY   A C    1 
ATOM   61   O  O    . GLY   A 1 9  ? 9.692   -9.414  -1.865  1.00 23.82 ? 8   GLY   A O    1 
ATOM   62   N  N    . ASP   A 1 10 ? 8.023   -8.690  -3.202  1.00 20.87 ? 9   ASP   A N    1 
ATOM   63   C  CA   . ASP   A 1 10 ? 7.065   -8.618  -2.105  1.00 19.87 ? 9   ASP   A CA   1 
ATOM   64   C  C    . ASP   A 1 10 ? 6.857   -9.999  -1.497  1.00 20.20 ? 9   ASP   A C    1 
ATOM   65   O  O    . ASP   A 1 10 ? 6.738   -10.997 -2.210  1.00 20.18 ? 9   ASP   A O    1 
ATOM   66   C  CB   . ASP   A 1 10 ? 5.726   -8.063  -2.594  1.00 20.85 ? 9   ASP   A CB   1 
ATOM   67   C  CG   . ASP   A 1 10 ? 5.761   -6.567  -2.828  1.00 25.62 ? 9   ASP   A CG   1 
ATOM   68   O  OD1  . ASP   A 1 10 ? 6.737   -5.907  -2.405  1.00 26.73 ? 9   ASP   A OD1  1 
ATOM   69   O  OD2  . ASP   A 1 10 ? 4.802   -6.050  -3.433  1.00 27.39 ? 9   ASP   A OD2  1 
ATOM   70   N  N    . LEU   A 1 11 ? 6.810   -10.053 -0.171  1.00 18.95 ? 10  LEU   A N    1 
ATOM   71   C  CA   . LEU   A 1 11 ? 6.614   -11.306 0.541   1.00 19.15 ? 10  LEU   A CA   1 
ATOM   72   C  C    . LEU   A 1 11 ? 5.160   -11.416 0.971   1.00 18.92 ? 10  LEU   A C    1 
ATOM   73   O  O    . LEU   A 1 11 ? 4.568   -10.445 1.453   1.00 23.11 ? 10  LEU   A O    1 
ATOM   74   C  CB   . LEU   A 1 11 ? 7.535   -11.398 1.757   1.00 17.69 ? 10  LEU   A CB   1 
ATOM   75   C  CG   . LEU   A 1 11 ? 9.010   -11.162 1.437   1.00 21.53 ? 10  LEU   A CG   1 
ATOM   76   C  CD1  . LEU   A 1 11 ? 9.862   -11.311 2.690   1.00 21.91 ? 10  LEU   A CD1  1 
ATOM   77   C  CD2  . LEU   A 1 11 ? 9.463   -12.119 0.343   1.00 20.06 ? 10  LEU   A CD2  1 
ATOM   78   N  N    . VAL   A 1 12 ? 4.588   -12.604 0.783   1.00 17.17 ? 11  VAL   A N    1 
ATOM   79   C  CA   . VAL   A 1 12 ? 3.162   -12.818 0.963   1.00 19.29 ? 11  VAL   A CA   1 
ATOM   80   C  C    . VAL   A 1 12 ? 2.919   -14.182 1.587   1.00 19.92 ? 11  VAL   A C    1 
ATOM   81   O  O    . VAL   A 1 12 ? 3.796   -15.046 1.625   1.00 21.11 ? 11  VAL   A O    1 
ATOM   82   C  CB   . VAL   A 1 12 ? 2.391   -12.734 -0.375  1.00 19.07 ? 11  VAL   A CB   1 
ATOM   83   C  CG1  . VAL   A 1 12 ? 2.515   -11.347 -0.979  1.00 21.95 ? 11  VAL   A CG1  1 
ATOM   84   C  CG2  . VAL   A 1 12 ? 2.906   -13.807 -1.347  1.00 19.83 ? 11  VAL   A CG2  1 
ATOM   85   N  N    . PHE   A 1 13 ? 1.705   -14.359 2.088   1.00 20.93 ? 12  PHE   A N    1 
ATOM   86   C  CA   . PHE   A 1 13 ? 1.084   -15.670 2.148   1.00 18.21 ? 12  PHE   A CA   1 
ATOM   87   C  C    . PHE   A 1 13 ? 0.140   -15.768 0.960   1.00 21.68 ? 12  PHE   A C    1 
ATOM   88   O  O    . PHE   A 1 13 ? -0.650  -14.852 0.720   1.00 22.41 ? 12  PHE   A O    1 
ATOM   89   C  CB   . PHE   A 1 13 ? 0.334   -15.882 3.462   1.00 24.18 ? 12  PHE   A CB   1 
ATOM   90   C  CG   . PHE   A 1 13 ? 1.240   -16.019 4.647   1.00 22.30 ? 12  PHE   A CG   1 
ATOM   91   C  CD1  . PHE   A 1 13 ? 1.773   -17.252 4.981   1.00 22.91 ? 12  PHE   A CD1  1 
ATOM   92   C  CD2  . PHE   A 1 13 ? 1.585   -14.914 5.399   1.00 23.30 ? 12  PHE   A CD2  1 
ATOM   93   C  CE1  . PHE   A 1 13 ? 2.623   -17.386 6.062   1.00 29.69 ? 12  PHE   A CE1  1 
ATOM   94   C  CE2  . PHE   A 1 13 ? 2.436   -15.041 6.486   1.00 27.56 ? 12  PHE   A CE2  1 
ATOM   95   C  CZ   . PHE   A 1 13 ? 2.958   -16.283 6.812   1.00 28.89 ? 12  PHE   A CZ   1 
ATOM   96   N  N    . ALA   A 1 14 ? 0.251   -16.852 0.198   1.00 20.46 ? 13  ALA   A N    1 
ATOM   97   C  CA   . ALA   A 1 14 ? -0.546  -17.047 -1.005  1.00 20.44 ? 13  ALA   A CA   1 
ATOM   98   C  C    . ALA   A 1 14 ? -1.510  -18.202 -0.787  1.00 22.46 ? 13  ALA   A C    1 
ATOM   99   O  O    . ALA   A 1 14 ? -1.105  -19.276 -0.327  1.00 24.42 ? 13  ALA   A O    1 
ATOM   100  C  CB   . ALA   A 1 14 ? 0.348   -17.320 -2.215  1.00 18.51 ? 13  ALA   A CB   1 
ATOM   101  N  N    . LYS   A 1 15 ? -2.776  -17.991 -1.132  1.00 23.06 ? 14  LYS   A N    1 
ATOM   102  C  CA   . LYS   A 1 15 ? -3.815  -18.979 -0.880  1.00 20.56 ? 14  LYS   A CA   1 
ATOM   103  C  C    . LYS   A 1 15 ? -4.123  -19.742 -2.159  1.00 25.11 ? 14  LYS   A C    1 
ATOM   104  O  O    . LYS   A 1 15 ? -4.426  -19.139 -3.193  1.00 27.05 ? 14  LYS   A O    1 
ATOM   105  C  CB   . LYS   A 1 15 ? -5.086  -18.322 -0.337  1.00 25.42 ? 14  LYS   A CB   1 
ATOM   106  C  CG   . LYS   A 1 15 ? -6.165  -19.322 0.075   1.00 33.48 ? 14  LYS   A CG   1 
ATOM   107  C  CD   . LYS   A 1 15 ? -5.673  -20.231 1.197   1.00 30.62 ? 14  LYS   A CD   1 
ATOM   108  C  CE   . LYS   A 1 15 ? -6.775  -21.161 1.701   1.00 31.98 ? 14  LYS   A CE   1 
ATOM   109  N  NZ   . LYS   A 1 15 ? -7.119  -22.230 0.718   1.00 33.00 ? 14  LYS   A NZ   1 
ATOM   110  N  N    . MET   A 1 16 ? -4.034  -21.067 -2.080  1.00 24.35 ? 15  MET   A N    1 
ATOM   111  C  CA   . MET   A 1 16 ? -4.404  -21.973 -3.153  1.00 30.62 ? 15  MET   A CA   1 
ATOM   112  C  C    . MET   A 1 16 ? -5.459  -22.938 -2.634  1.00 31.70 ? 15  MET   A C    1 
ATOM   113  O  O    . MET   A 1 16 ? -5.442  -23.315 -1.461  1.00 27.37 ? 15  MET   A O    1 
ATOM   114  C  CB   . MET   A 1 16 ? -3.188  -22.745 -3.649  1.00 30.41 ? 15  MET   A CB   1 
ATOM   115  C  CG   . MET   A 1 16 ? -2.069  -21.846 -4.099  1.00 31.42 ? 15  MET   A CG   1 
ATOM   116  S  SD   . MET   A 1 16 ? -2.203  -21.543 -5.854  1.00 36.60 ? 15  MET   A SD   1 
ATOM   117  C  CE   . MET   A 1 16 ? -1.863  -23.166 -6.517  1.00 42.91 ? 15  MET   A CE   1 
ATOM   118  N  N    . LYS   A 1 17 ? -6.383  -23.321 -3.514  1.00 31.00 ? 16  LYS   A N    1 
ATOM   119  C  CA   . LYS   A 1 17 ? -7.433  -24.257 -3.130  1.00 31.71 ? 16  LYS   A CA   1 
ATOM   120  C  C    . LYS   A 1 17 ? -6.818  -25.533 -2.569  1.00 28.95 ? 16  LYS   A C    1 
ATOM   121  O  O    . LYS   A 1 17 ? -5.883  -26.090 -3.150  1.00 30.91 ? 16  LYS   A O    1 
ATOM   122  C  CB   . LYS   A 1 17 ? -8.317  -24.574 -4.337  1.00 37.98 ? 16  LYS   A CB   1 
ATOM   123  C  CG   . LYS   A 1 17 ? -9.356  -25.657 -4.099  1.00 34.62 ? 16  LYS   A CG   1 
ATOM   124  C  CD   . LYS   A 1 17 ? -10.023 -26.045 -5.409  1.00 41.61 ? 16  LYS   A CD   1 
ATOM   125  C  CE   . LYS   A 1 17 ? -10.918 -27.261 -5.247  1.00 47.26 ? 16  LYS   A CE   1 
ATOM   126  N  NZ   . LYS   A 1 17 ? -11.461 -27.719 -6.558  1.00 51.35 ? 16  LYS   A NZ   1 
ATOM   127  N  N    . GLY   A 1 18 ? -7.320  -25.977 -1.417  1.00 29.75 ? 17  GLY   A N    1 
ATOM   128  C  CA   . GLY   A 1 18 ? -6.839  -27.190 -0.788  1.00 33.14 ? 17  GLY   A CA   1 
ATOM   129  C  C    . GLY   A 1 18 ? -5.547  -27.056 -0.013  1.00 41.99 ? 17  GLY   A C    1 
ATOM   130  O  O    . GLY   A 1 18 ? -5.069  -28.059 0.536   1.00 37.96 ? 17  GLY   A O    1 
ATOM   131  N  N    . TYR   A 1 19 ? -4.966  -25.863 0.054   1.00 33.18 ? 18  TYR   A N    1 
ATOM   132  C  CA   . TYR   A 1 19 ? -3.752  -25.620 0.815   1.00 27.12 ? 18  TYR   A CA   1 
ATOM   133  C  C    . TYR   A 1 19 ? -3.979  -24.499 1.816   1.00 29.83 ? 18  TYR   A C    1 
ATOM   134  O  O    . TYR   A 1 19 ? -4.755  -23.577 1.556   1.00 28.35 ? 18  TYR   A O    1 
ATOM   135  C  CB   . TYR   A 1 19 ? -2.586  -25.223 -0.098  1.00 29.92 ? 18  TYR   A CB   1 
ATOM   136  C  CG   . TYR   A 1 19 ? -2.139  -26.277 -1.077  1.00 36.77 ? 18  TYR   A CG   1 
ATOM   137  C  CD1  . TYR   A 1 19 ? -1.176  -27.215 -0.726  1.00 47.47 ? 18  TYR   A CD1  1 
ATOM   138  C  CD2  . TYR   A 1 19 ? -2.655  -26.316 -2.364  1.00 39.08 ? 18  TYR   A CD2  1 
ATOM   139  C  CE1  . TYR   A 1 19 ? -0.753  -28.175 -1.625  1.00 42.83 ? 18  TYR   A CE1  1 
ATOM   140  C  CE2  . TYR   A 1 19 ? -2.237  -27.270 -3.270  1.00 39.79 ? 18  TYR   A CE2  1 
ATOM   141  C  CZ   . TYR   A 1 19 ? -1.287  -28.196 -2.897  1.00 48.97 ? 18  TYR   A CZ   1 
ATOM   142  O  OH   . TYR   A 1 19 ? -0.876  -29.147 -3.804  1.00 54.81 ? 18  TYR   A OH   1 
ATOM   143  N  N    . PRO   A 1 20 ? -3.298  -24.538 2.956   1.00 29.14 ? 19  PRO   A N    1 
ATOM   144  C  CA   . PRO   A 1 20 ? -3.298  -23.376 3.847   1.00 24.65 ? 19  PRO   A CA   1 
ATOM   145  C  C    . PRO   A 1 20 ? -2.571  -22.213 3.190   1.00 27.77 ? 19  PRO   A C    1 
ATOM   146  O  O    . PRO   A 1 20 ? -1.796  -22.393 2.248   1.00 25.02 ? 19  PRO   A O    1 
ATOM   147  C  CB   . PRO   A 1 20 ? -2.539  -23.877 5.078   1.00 30.66 ? 19  PRO   A CB   1 
ATOM   148  C  CG   . PRO   A 1 20 ? -1.616  -24.905 4.526   1.00 29.97 ? 19  PRO   A CG   1 
ATOM   149  C  CD   . PRO   A 1 20 ? -2.380  -25.590 3.427   1.00 35.14 ? 19  PRO   A CD   1 
ATOM   150  N  N    . HIS   A 1 21 ? -2.842  -21.009 3.694   1.00 27.58 ? 20  HIS   A N    1 
ATOM   151  C  CA   . HIS   A 1 21 ? -2.102  -19.832 3.249   1.00 26.95 ? 20  HIS   A CA   1 
ATOM   152  C  C    . HIS   A 1 21 ? -0.610  -20.091 3.398   1.00 25.20 ? 20  HIS   A C    1 
ATOM   153  O  O    . HIS   A 1 21 ? -0.137  -20.465 4.474   1.00 26.01 ? 20  HIS   A O    1 
ATOM   154  C  CB   . HIS   A 1 21 ? -2.521  -18.600 4.052   1.00 27.83 ? 20  HIS   A CB   1 
ATOM   155  C  CG   . HIS   A 1 21 ? -3.963  -18.232 3.886   1.00 33.81 ? 20  HIS   A CG   1 
ATOM   156  N  ND1  . HIS   A 1 21 ? -4.985  -18.940 4.483   1.00 32.33 ? 20  HIS   A ND1  1 
ATOM   157  C  CD2  . HIS   A 1 21 ? -4.555  -17.232 3.189   1.00 28.41 ? 20  HIS   A CD2  1 
ATOM   158  C  CE1  . HIS   A 1 21 ? -6.144  -18.389 4.166   1.00 35.26 ? 20  HIS   A CE1  1 
ATOM   159  N  NE2  . HIS   A 1 21 ? -5.911  -17.354 3.378   1.00 34.12 ? 20  HIS   A NE2  1 
ATOM   160  N  N    . TRP   A 1 22 ? 0.125   -19.919 2.301   1.00 25.01 ? 21  TRP   A N    1 
ATOM   161  C  CA   . TRP   A 1 22 ? 1.453   -20.489 2.152   1.00 21.12 ? 21  TRP   A CA   1 
ATOM   162  C  C    . TRP   A 1 22 ? 2.499   -19.393 1.999   1.00 23.33 ? 21  TRP   A C    1 
ATOM   163  O  O    . TRP   A 1 22 ? 2.301   -18.464 1.203   1.00 22.25 ? 21  TRP   A O    1 
ATOM   164  C  CB   . TRP   A 1 22 ? 1.497   -21.412 0.927   1.00 24.23 ? 21  TRP   A CB   1 
ATOM   165  C  CG   . TRP   A 1 22 ? 2.570   -22.437 0.981   1.00 22.57 ? 21  TRP   A CG   1 
ATOM   166  C  CD1  . TRP   A 1 22 ? 3.889   -22.268 0.672   1.00 22.24 ? 21  TRP   A CD1  1 
ATOM   167  C  CD2  . TRP   A 1 22 ? 2.417   -23.813 1.356   1.00 22.09 ? 21  TRP   A CD2  1 
ATOM   168  N  NE1  . TRP   A 1 22 ? 4.567   -23.457 0.831   1.00 23.95 ? 21  TRP   A NE1  1 
ATOM   169  C  CE2  . TRP   A 1 22 ? 3.685   -24.418 1.256   1.00 24.58 ? 21  TRP   A CE2  1 
ATOM   170  C  CE3  . TRP   A 1 22 ? 1.329   -24.590 1.770   1.00 31.36 ? 21  TRP   A CE3  1 
ATOM   171  C  CZ2  . TRP   A 1 22 ? 3.896   -25.766 1.552   1.00 27.75 ? 21  TRP   A CZ2  1 
ATOM   172  C  CZ3  . TRP   A 1 22 ? 1.540   -25.929 2.066   1.00 29.23 ? 21  TRP   A CZ3  1 
ATOM   173  C  CH2  . TRP   A 1 22 ? 2.814   -26.501 1.956   1.00 33.88 ? 21  TRP   A CH2  1 
ATOM   174  N  N    . PRO   A 1 23 ? 3.618   -19.464 2.721   1.00 20.16 ? 22  PRO   A N    1 
ATOM   175  C  CA   . PRO   A 1 23 ? 4.667   -18.446 2.565   1.00 20.74 ? 22  PRO   A CA   1 
ATOM   176  C  C    . PRO   A 1 23 ? 5.174   -18.420 1.131   1.00 18.08 ? 22  PRO   A C    1 
ATOM   177  O  O    . PRO   A 1 23 ? 5.516   -19.455 0.562   1.00 20.56 ? 22  PRO   A O    1 
ATOM   178  C  CB   . PRO   A 1 23 ? 5.757   -18.910 3.541   1.00 19.87 ? 22  PRO   A CB   1 
ATOM   179  C  CG   . PRO   A 1 23 ? 5.525   -20.395 3.675   1.00 20.30 ? 22  PRO   A CG   1 
ATOM   180  C  CD   . PRO   A 1 23 ? 4.029   -20.541 3.637   1.00 22.45 ? 22  PRO   A CD   1 
ATOM   181  N  N    . ALA   A 1 24 ? 5.234   -17.225 0.552   1.00 17.83 ? 23  ALA   A N    1 
ATOM   182  C  CA   . ALA   A 1 24 ? 5.554   -17.108 -0.866  1.00 18.20 ? 23  ALA   A CA   1 
ATOM   183  C  C    . ALA   A 1 24 ? 6.131   -15.727 -1.143  1.00 19.91 ? 23  ALA   A C    1 
ATOM   184  O  O    . ALA   A 1 24 ? 6.155   -14.857 -0.275  1.00 20.90 ? 23  ALA   A O    1 
ATOM   185  C  CB   . ALA   A 1 24 ? 4.316   -17.363 -1.729  1.00 21.15 ? 23  ALA   A CB   1 
ATOM   186  N  N    . ARG   A 1 25 ? 6.590   -15.534 -2.380  1.00 19.95 ? 24  ARG   A N    1 
ATOM   187  C  CA   . ARG   A 1 25 ? 7.051   -14.226 -2.819  1.00 19.89 ? 24  ARG   A CA   1 
ATOM   188  C  C    . ARG   A 1 25 ? 6.547   -13.974 -4.231  1.00 18.57 ? 24  ARG   A C    1 
ATOM   189  O  O    . ARG   A 1 25 ? 6.270   -14.909 -4.987  1.00 19.28 ? 24  ARG   A O    1 
ATOM   190  C  CB   . ARG   A 1 25 ? 8.581   -14.118 -2.781  1.00 18.08 ? 24  ARG   A CB   1 
ATOM   191  C  CG   . ARG   A 1 25 ? 9.273   -14.970 -3.834  1.00 22.37 ? 24  ARG   A CG   1 
ATOM   192  C  CD   . ARG   A 1 25 ? 10.794  -14.907 -3.710  1.00 19.82 ? 24  ARG   A CD   1 
ATOM   193  N  NE   . ARG   A 1 25 ? 11.458  -15.654 -4.776  1.00 21.81 ? 24  ARG   A NE   1 
ATOM   194  C  CZ   . ARG   A 1 25 ? 12.699  -16.119 -4.711  1.00 25.47 ? 24  ARG   A CZ   1 
ATOM   195  N  NH1  . ARG   A 1 25 ? 13.434  -15.978 -3.617  1.00 22.43 ? 24  ARG   A NH1  1 
ATOM   196  N  NH2  . ARG   A 1 25 ? 13.214  -16.745 -5.769  1.00 24.81 ? 24  ARG   A NH2  1 
ATOM   197  N  N    . ILE   A 1 26 ? 6.410   -12.693 -4.568  1.00 16.62 ? 25  ILE   A N    1 
ATOM   198  C  CA   . ILE   A 1 26 ? 6.196   -12.284 -5.953  1.00 18.62 ? 25  ILE   A CA   1 
ATOM   199  C  C    . ILE   A 1 26 ? 7.513   -12.452 -6.694  1.00 21.56 ? 25  ILE   A C    1 
ATOM   200  O  O    . ILE   A 1 26 ? 8.513   -11.809 -6.356  1.00 21.08 ? 25  ILE   A O    1 
ATOM   201  C  CB   . ILE   A 1 26 ? 5.715   -10.829 -6.041  1.00 21.19 ? 25  ILE   A CB   1 
ATOM   202  C  CG1  . ILE   A 1 26 ? 4.549   -10.561 -5.085  1.00 27.53 ? 25  ILE   A CG1  1 
ATOM   203  C  CG2  . ILE   A 1 26 ? 5.352   -10.481 -7.488  1.00 22.72 ? 25  ILE   A CG2  1 
ATOM   204  C  CD1  . ILE   A 1 26 ? 3.266   -11.216 -5.477  1.00 31.11 ? 25  ILE   A CD1  1 
ATOM   205  N  N    . ASP   A 1 27 ? 7.521   -13.308 -7.706  1.00 23.16 ? 26  ASP   A N    1 
ATOM   206  C  CA   . ASP   A 1 27 ? 8.768   -13.572 -8.396  1.00 26.56 ? 26  ASP   A CA   1 
ATOM   207  C  C    . ASP   A 1 27 ? 9.038   -12.511 -9.453  1.00 29.36 ? 26  ASP   A C    1 
ATOM   208  O  O    . ASP   A 1 27 ? 8.141   -11.791 -9.899  1.00 26.17 ? 26  ASP   A O    1 
ATOM   209  C  CB   . ASP   A 1 27 ? 8.745   -14.953 -9.049  1.00 26.36 ? 26  ASP   A CB   1 
ATOM   210  C  CG   . ASP   A 1 27 ? 9.794   -15.880 -8.480  1.00 30.39 ? 26  ASP   A CG   1 
ATOM   211  O  OD1  . ASP   A 1 27 ? 10.489  -15.479 -7.523  1.00 35.39 ? 26  ASP   A OD1  1 
ATOM   212  O  OD2  . ASP   A 1 27 ? 9.931   -17.008 -8.992  1.00 30.80 ? 26  ASP   A OD2  1 
ATOM   213  N  N    . ASP   A 1 28 ? 10.307  -12.402 -9.825  1.00 32.36 ? 27  ASP   A N    1 
ATOM   214  C  CA   . ASP   A 1 28 ? 10.655  -11.743 -11.067 1.00 32.64 ? 27  ASP   A CA   1 
ATOM   215  C  C    . ASP   A 1 28 ? 10.401  -12.698 -12.225 1.00 31.18 ? 27  ASP   A C    1 
ATOM   216  O  O    . ASP   A 1 28 ? 10.301  -13.916 -12.050 1.00 33.34 ? 27  ASP   A O    1 
ATOM   217  C  CB   . ASP   A 1 28 ? 12.120  -11.306 -11.061 1.00 47.85 ? 27  ASP   A CB   1 
ATOM   218  C  CG   . ASP   A 1 28 ? 12.291  -9.824  -10.788 1.00 57.21 ? 27  ASP   A CG   1 
ATOM   219  O  OD1  . ASP   A 1 28 ? 11.649  -9.006  -11.483 1.00 54.46 ? 27  ASP   A OD1  1 
ATOM   220  O  OD2  . ASP   A 1 28 ? 13.075  -9.480  -9.878  1.00 63.39 ? 27  ASP   A OD2  1 
ATOM   221  N  N    . ILE   A 1 29 ? 10.284  -12.134 -13.417 1.00 32.86 ? 28  ILE   A N    1 
ATOM   222  C  CA   . ILE   A 1 29 ? 10.188  -12.913 -14.644 1.00 33.34 ? 28  ILE   A CA   1 
ATOM   223  C  C    . ILE   A 1 29 ? 11.521  -12.779 -15.358 1.00 31.97 ? 28  ILE   A C    1 
ATOM   224  O  O    . ILE   A 1 29 ? 11.909  -11.673 -15.749 1.00 31.70 ? 28  ILE   A O    1 
ATOM   225  C  CB   . ILE   A 1 29 ? 9.032   -12.437 -15.533 1.00 34.71 ? 28  ILE   A CB   1 
ATOM   226  C  CG1  . ILE   A 1 29 ? 7.720   -12.476 -14.753 1.00 31.94 ? 28  ILE   A CG1  1 
ATOM   227  C  CG2  . ILE   A 1 29 ? 8.938   -13.298 -16.788 1.00 28.68 ? 28  ILE   A CG2  1 
ATOM   228  C  CD1  . ILE   A 1 29 ? 6.719   -11.453 -15.217 1.00 39.69 ? 28  ILE   A CD1  1 
ATOM   229  N  N    . ALA   A 1 30 ? 12.233  -13.893 -15.497 1.00 36.14 ? 29  ALA   A N    1 
ATOM   230  C  CA   . ALA   A 1 30 ? 13.525  -13.872 -16.164 1.00 31.86 ? 29  ALA   A CA   1 
ATOM   231  C  C    . ALA   A 1 30 ? 13.353  -13.567 -17.646 1.00 35.16 ? 29  ALA   A C    1 
ATOM   232  O  O    . ALA   A 1 30 ? 12.302  -13.825 -18.239 1.00 31.88 ? 29  ALA   A O    1 
ATOM   233  C  CB   . ALA   A 1 30 ? 14.243  -15.210 -15.989 1.00 36.62 ? 29  ALA   A CB   1 
ATOM   234  N  N    . ASP   A 1 31 ? 14.397  -12.992 -18.238 1.00 29.47 ? 30  ASP   A N    1 
ATOM   235  C  CA   . ASP   A 1 31 ? 14.423  -12.812 -19.682 1.00 33.31 ? 30  ASP   A CA   1 
ATOM   236  C  C    . ASP   A 1 31 ? 14.161  -14.140 -20.379 1.00 22.85 ? 30  ASP   A C    1 
ATOM   237  O  O    . ASP   A 1 31 ? 14.738  -15.169 -20.019 1.00 33.33 ? 30  ASP   A O    1 
ATOM   238  C  CB   . ASP   A 1 31 ? 15.775  -12.244 -20.119 1.00 34.01 ? 30  ASP   A CB   1 
ATOM   239  C  CG   . ASP   A 1 31 ? 15.873  -10.742 -19.925 1.00 38.63 ? 30  ASP   A CG   1 
ATOM   240  O  OD1  . ASP   A 1 31 ? 14.823  -10.073 -19.822 1.00 42.17 ? 30  ASP   A OD1  1 
ATOM   241  O  OD2  . ASP   A 1 31 ? 17.009  -10.224 -19.890 1.00 44.78 ? 30  ASP   A OD2  1 
ATOM   242  N  N    . GLY   A 1 32 ? 13.279  -14.115 -21.377 1.00 30.08 ? 31  GLY   A N    1 
ATOM   243  C  CA   . GLY   A 1 32 ? 12.943  -15.311 -22.117 1.00 34.84 ? 31  GLY   A CA   1 
ATOM   244  C  C    . GLY   A 1 32 ? 12.087  -16.315 -21.379 1.00 37.29 ? 31  GLY   A C    1 
ATOM   245  O  O    . GLY   A 1 32 ? 11.775  -17.367 -21.947 1.00 34.52 ? 31  GLY   A O    1 
ATOM   246  N  N    . ALA   A 1 33 ? 11.697  -16.036 -20.139 1.00 29.41 ? 32  ALA   A N    1 
ATOM   247  C  CA   . ALA   A 1 33 ? 10.864  -16.960 -19.387 1.00 30.10 ? 32  ALA   A CA   1 
ATOM   248  C  C    . ALA   A 1 33 ? 9.385   -16.717 -19.672 1.00 28.97 ? 32  ALA   A C    1 
ATOM   249  O  O    . ALA   A 1 33 ? 8.982   -15.657 -20.160 1.00 31.67 ? 32  ALA   A O    1 
ATOM   250  C  CB   . ALA   A 1 33 ? 11.134  -16.836 -17.886 1.00 36.26 ? 32  ALA   A CB   1 
ATOM   251  N  N    . VAL   A 1 34 ? 8.574   -17.729 -19.353 1.00 32.23 ? 33  VAL   A N    1 
ATOM   252  C  CA   . VAL   A 1 34 ? 7.135   -17.644 -19.577 1.00 29.47 ? 33  VAL   A CA   1 
ATOM   253  C  C    . VAL   A 1 34 ? 6.535   -16.572 -18.681 1.00 28.37 ? 33  VAL   A C    1 
ATOM   254  O  O    . VAL   A 1 34 ? 6.765   -16.552 -17.465 1.00 31.10 ? 33  VAL   A O    1 
ATOM   255  C  CB   . VAL   A 1 34 ? 6.482   -19.010 -19.321 1.00 26.52 ? 33  VAL   A CB   1 
ATOM   256  C  CG1  . VAL   A 1 34 ? 4.968   -18.892 -19.356 1.00 34.93 ? 33  VAL   A CG1  1 
ATOM   257  C  CG2  . VAL   A 1 34 ? 6.973   -20.037 -20.339 1.00 30.14 ? 33  VAL   A CG2  1 
ATOM   258  N  N    . LYS   A 1 35 ? 5.731   -15.646 -19.299 1.00 28.20 ? 34  LYS   A N    1 
ATOM   259  C  CA   . LYS   A 1 35 ? 5.066   -14.561 -18.593 1.00 32.05 ? 34  LYS   A CA   1 
ATOM   260  C  C    . LYS   A 1 35 ? 3.718   -15.017 -18.038 1.00 31.97 ? 34  LYS   A C    1 
ATOM   261  O  O    . LYS   A 1 35 ? 3.085   -15.922 -18.590 1.00 30.23 ? 34  LYS   A O    1 
ATOM   262  C  CB   . LYS   A 1 35 ? 4.855   -13.369 -19.525 1.00 35.26 ? 34  LYS   A CB   1 
ATOM   263  C  CG   . LYS   A 1 35 ? 6.146   -12.710 -19.987 1.00 30.31 ? 34  LYS   A CG   1 
ATOM   264  C  CD   . LYS   A 1 35 ? 5.870   -11.519 -20.891 1.00 35.46 ? 34  LYS   A CD   1 
ATOM   265  C  CE   . LYS   A 1 35 ? 5.180   -11.948 -22.175 1.00 41.09 ? 34  LYS   A CE   1 
ATOM   266  N  NZ   . LYS   A 1 35 ? 5.044   -10.815 -23.129 1.00 42.42 ? 34  LYS   A NZ   1 
ATOM   267  N  N    . PRO   A 1 36 ? 3.249   -14.404 -16.955 1.00 31.72 ? 35  PRO   A N    1 
ATOM   268  C  CA   . PRO   A 1 36 ? 1.943   -14.770 -16.400 1.00 36.16 ? 35  PRO   A CA   1 
ATOM   269  C  C    . PRO   A 1 36 ? 0.818   -14.223 -17.258 1.00 34.61 ? 35  PRO   A C    1 
ATOM   270  O  O    . PRO   A 1 36 ? 1.033   -13.314 -18.073 1.00 37.15 ? 35  PRO   A O    1 
ATOM   271  C  CB   . PRO   A 1 36 ? 1.947   -14.107 -15.011 1.00 29.06 ? 35  PRO   A CB   1 
ATOM   272  C  CG   . PRO   A 1 36 ? 3.337   -13.580 -14.806 1.00 39.15 ? 35  PRO   A CG   1 
ATOM   273  C  CD   . PRO   A 1 36 ? 3.902   -13.355 -16.161 1.00 37.27 ? 35  PRO   A CD   1 
ATOM   274  N  N    . PRO   A 1 37 ? -0.398  -14.740 -17.098 1.00 39.57 ? 36  PRO   A N    1 
ATOM   275  C  CA   . PRO   A 1 37 ? -1.556  -14.134 -17.763 1.00 37.84 ? 36  PRO   A CA   1 
ATOM   276  C  C    . PRO   A 1 37 ? -1.765  -12.713 -17.273 1.00 45.41 ? 36  PRO   A C    1 
ATOM   277  O  O    . PRO   A 1 37 ? -1.211  -12.324 -16.232 1.00 30.85 ? 36  PRO   A O    1 
ATOM   278  C  CB   . PRO   A 1 37 ? -2.724  -15.046 -17.346 1.00 40.30 ? 36  PRO   A CB   1 
ATOM   279  C  CG   . PRO   A 1 37 ? -2.089  -16.313 -16.876 1.00 39.94 ? 36  PRO   A CG   1 
ATOM   280  C  CD   . PRO   A 1 37 ? -0.774  -15.913 -16.290 1.00 33.98 ? 36  PRO   A CD   1 
ATOM   281  N  N    . PRO   A 1 38 ? -2.542  -11.902 -17.994 1.00 34.92 ? 37  PRO   A N    1 
ATOM   282  C  CA   . PRO   A 1 38 ? -2.823  -10.544 -17.514 1.00 40.65 ? 37  PRO   A CA   1 
ATOM   283  C  C    . PRO   A 1 38 ? -3.483  -10.562 -16.144 1.00 34.38 ? 37  PRO   A C    1 
ATOM   284  O  O    . PRO   A 1 38 ? -4.250  -11.468 -15.808 1.00 39.01 ? 37  PRO   A O    1 
ATOM   285  C  CB   . PRO   A 1 38 ? -3.763  -9.971  -18.585 1.00 45.87 ? 37  PRO   A CB   1 
ATOM   286  C  CG   . PRO   A 1 38 ? -4.278  -11.166 -19.337 1.00 37.65 ? 37  PRO   A CG   1 
ATOM   287  C  CD   . PRO   A 1 38 ? -3.170  -12.166 -19.299 1.00 44.51 ? 37  PRO   A CD   1 
ATOM   288  N  N    . ASN   A 1 39 ? -3.147  -9.555  -15.340 1.00 32.71 ? 38  ASN   A N    1 
ATOM   289  C  CA   . ASN   A 1 39 ? -3.650  -9.366  -13.983 1.00 36.98 ? 38  ASN   A CA   1 
ATOM   290  C  C    . ASN   A 1 39 ? -3.242  -10.486 -13.036 1.00 35.60 ? 38  ASN   A C    1 
ATOM   291  O  O    . ASN   A 1 39 ? -3.814  -10.609 -11.947 1.00 36.92 ? 38  ASN   A O    1 
ATOM   292  C  CB   . ASN   A 1 39 ? -5.176  -9.205  -13.972 1.00 40.06 ? 38  ASN   A CB   1 
ATOM   293  C  CG   . ASN   A 1 39 ? -5.651  -8.129  -14.927 1.00 45.41 ? 38  ASN   A CG   1 
ATOM   294  O  OD1  . ASN   A 1 39 ? -5.950  -8.400  -16.089 1.00 51.08 ? 38  ASN   A OD1  1 
ATOM   295  N  ND2  . ASN   A 1 39 ? -5.715  -6.897  -14.440 1.00 45.66 ? 38  ASN   A ND2  1 
ATOM   296  N  N    . LYS   A 1 40 ? -2.278  -11.317 -13.418 1.00 29.18 ? 39  LYS   A N    1 
ATOM   297  C  CA   . LYS   A 1 40 ? -1.757  -12.352 -12.539 1.00 27.52 ? 39  LYS   A CA   1 
ATOM   298  C  C    . LYS   A 1 40 ? -0.274  -12.115 -12.294 1.00 26.13 ? 39  LYS   A C    1 
ATOM   299  O  O    . LYS   A 1 40 ? 0.419   -11.473 -13.091 1.00 30.24 ? 39  LYS   A O    1 
ATOM   300  C  CB   . LYS   A 1 40 ? -1.974  -13.755 -13.119 1.00 30.48 ? 39  LYS   A CB   1 
ATOM   301  C  CG   . LYS   A 1 40 ? -3.434  -14.126 -13.349 1.00 40.01 ? 39  LYS   A CG   1 
ATOM   302  C  CD   . LYS   A 1 40 ? -4.285  -13.856 -12.116 1.00 34.15 ? 39  LYS   A CD   1 
ATOM   303  C  CE   . LYS   A 1 40 ? -5.747  -14.244 -12.352 1.00 43.71 ? 39  LYS   A CE   1 
ATOM   304  N  NZ   . LYS   A 1 40 ? -5.917  -15.715 -12.501 1.00 49.52 ? 39  LYS   A NZ   1 
ATOM   305  N  N    . TYR   A 1 41 ? 0.201   -12.637 -11.166 1.00 21.03 ? 40  TYR   A N    1 
ATOM   306  C  CA   . TYR   A 1 41 ? 1.584   -12.533 -10.735 1.00 21.70 ? 40  TYR   A CA   1 
ATOM   307  C  C    . TYR   A 1 41 ? 2.219   -13.911 -10.645 1.00 24.50 ? 40  TYR   A C    1 
ATOM   308  O  O    . TYR   A 1 41 ? 1.548   -14.885 -10.298 1.00 23.88 ? 40  TYR   A O    1 
ATOM   309  C  CB   . TYR   A 1 41 ? 1.685   -11.850 -9.364  1.00 20.72 ? 40  TYR   A CB   1 
ATOM   310  C  CG   . TYR   A 1 41 ? 1.163   -10.447 -9.406  1.00 24.22 ? 40  TYR   A CG   1 
ATOM   311  C  CD1  . TYR   A 1 41 ? -0.191  -10.187 -9.230  1.00 27.55 ? 40  TYR   A CD1  1 
ATOM   312  C  CD2  . TYR   A 1 41 ? 2.011   -9.383  -9.660  1.00 31.57 ? 40  TYR   A CD2  1 
ATOM   313  C  CE1  . TYR   A 1 41 ? -0.679  -8.900  -9.293  1.00 30.27 ? 40  TYR   A CE1  1 
ATOM   314  C  CE2  . TYR   A 1 41 ? 1.533   -8.097  -9.719  1.00 27.82 ? 40  TYR   A CE2  1 
ATOM   315  C  CZ   . TYR   A 1 41 ? 0.187   -7.860  -9.535  1.00 29.65 ? 40  TYR   A CZ   1 
ATOM   316  O  OH   . TYR   A 1 41 ? -0.294  -6.576  -9.604  1.00 31.67 ? 40  TYR   A OH   1 
ATOM   317  N  N    . PRO   A 1 42 ? 3.514   -14.027 -10.949 1.00 20.90 ? 41  PRO   A N    1 
ATOM   318  C  CA   . PRO   A 1 42 ? 4.205   -15.304 -10.744 1.00 22.60 ? 41  PRO   A CA   1 
ATOM   319  C  C    . PRO   A 1 42 ? 4.533   -15.443 -9.265  1.00 23.50 ? 41  PRO   A C    1 
ATOM   320  O  O    . PRO   A 1 42 ? 5.269   -14.627 -8.706  1.00 22.47 ? 41  PRO   A O    1 
ATOM   321  C  CB   . PRO   A 1 42 ? 5.468   -15.163 -11.603 1.00 22.63 ? 41  PRO   A CB   1 
ATOM   322  C  CG   . PRO   A 1 42 ? 5.731   -13.703 -11.629 1.00 21.27 ? 41  PRO   A CG   1 
ATOM   323  C  CD   . PRO   A 1 42 ? 4.417   -12.983 -11.462 1.00 28.22 ? 41  PRO   A CD   1 
ATOM   324  N  N    . ILE   A 1 43 ? 3.949   -16.448 -8.622  1.00 19.77 ? 42  ILE   A N    1 
ATOM   325  C  CA   . ILE   A 1 43 ? 4.104   -16.649 -7.185  1.00 19.56 ? 42  ILE   A CA   1 
ATOM   326  C  C    . ILE   A 1 43 ? 5.051   -17.814 -6.971  1.00 27.70 ? 42  ILE   A C    1 
ATOM   327  O  O    . ILE   A 1 43 ? 4.781   -18.931 -7.424  1.00 25.21 ? 42  ILE   A O    1 
ATOM   328  C  CB   . ILE   A 1 43 ? 2.755   -16.917 -6.504  1.00 20.86 ? 42  ILE   A CB   1 
ATOM   329  C  CG1  . ILE   A 1 43 ? 1.777   -15.801 -6.844  1.00 20.22 ? 42  ILE   A CG1  1 
ATOM   330  C  CG2  . ILE   A 1 43 ? 2.938   -17.034 -4.986  1.00 20.17 ? 42  ILE   A CG2  1 
ATOM   331  C  CD1  . ILE   A 1 43 ? 2.294   -14.432 -6.483  1.00 23.62 ? 42  ILE   A CD1  1 
ATOM   332  N  N    . PHE   A 1 44 ? 6.150   -17.562 -6.272  1.00 18.80 ? 43  PHE   A N    1 
ATOM   333  C  CA   . PHE   A 1 44 ? 7.093   -18.606 -5.899  1.00 21.05 ? 43  PHE   A CA   1 
ATOM   334  C  C    . PHE   A 1 44 ? 6.783   -19.034 -4.472  1.00 22.83 ? 43  PHE   A C    1 
ATOM   335  O  O    . PHE   A 1 44 ? 6.813   -18.208 -3.558  1.00 21.86 ? 43  PHE   A O    1 
ATOM   336  C  CB   . PHE   A 1 44 ? 8.534   -18.111 -6.010  1.00 21.35 ? 43  PHE   A CB   1 
ATOM   337  C  CG   . PHE   A 1 44 ? 9.555   -19.108 -5.543  1.00 23.78 ? 43  PHE   A CG   1 
ATOM   338  C  CD1  . PHE   A 1 44 ? 9.984   -20.125 -6.385  1.00 25.46 ? 43  PHE   A CD1  1 
ATOM   339  C  CD2  . PHE   A 1 44 ? 10.096  -19.026 -4.268  1.00 26.80 ? 43  PHE   A CD2  1 
ATOM   340  C  CE1  . PHE   A 1 44 ? 10.929  -21.046 -5.963  1.00 28.67 ? 43  PHE   A CE1  1 
ATOM   341  C  CE2  . PHE   A 1 44 ? 11.040  -19.950 -3.843  1.00 28.31 ? 43  PHE   A CE2  1 
ATOM   342  C  CZ   . PHE   A 1 44 ? 11.456  -20.956 -4.693  1.00 27.11 ? 43  PHE   A CZ   1 
ATOM   343  N  N    . PHE   A 1 45 ? 6.478   -20.316 -4.283  1.00 19.49 ? 44  PHE   A N    1 
ATOM   344  C  CA   . PHE   A 1 45 ? 6.093   -20.832 -2.975  1.00 21.02 ? 44  PHE   A CA   1 
ATOM   345  C  C    . PHE   A 1 45 ? 7.336   -21.350 -2.266  1.00 20.70 ? 44  PHE   A C    1 
ATOM   346  O  O    . PHE   A 1 45 ? 8.016   -22.248 -2.774  1.00 23.12 ? 44  PHE   A O    1 
ATOM   347  C  CB   . PHE   A 1 45 ? 5.046   -21.940 -3.115  1.00 23.72 ? 44  PHE   A CB   1 
ATOM   348  C  CG   . PHE   A 1 45 ? 3.705   -21.451 -3.574  1.00 26.50 ? 44  PHE   A CG   1 
ATOM   349  C  CD1  . PHE   A 1 45 ? 3.414   -21.344 -4.923  1.00 26.64 ? 44  PHE   A CD1  1 
ATOM   350  C  CD2  . PHE   A 1 45 ? 2.734   -21.087 -2.657  1.00 28.07 ? 44  PHE   A CD2  1 
ATOM   351  C  CE1  . PHE   A 1 45 ? 2.181   -20.882 -5.344  1.00 28.70 ? 44  PHE   A CE1  1 
ATOM   352  C  CE2  . PHE   A 1 45 ? 1.498   -20.625 -3.076  1.00 25.27 ? 44  PHE   A CE2  1 
ATOM   353  C  CZ   . PHE   A 1 45 ? 1.224   -20.525 -4.418  1.00 28.56 ? 44  PHE   A CZ   1 
ATOM   354  N  N    . PHE   A 1 46 ? 7.638   -20.789 -1.100  1.00 20.14 ? 45  PHE   A N    1 
ATOM   355  C  CA   . PHE   A 1 46 ? 8.782   -21.271 -0.343  1.00 21.37 ? 45  PHE   A CA   1 
ATOM   356  C  C    . PHE   A 1 46 ? 8.551   -22.702 0.136   1.00 22.30 ? 45  PHE   A C    1 
ATOM   357  O  O    . PHE   A 1 46 ? 7.415   -23.144 0.323   1.00 24.25 ? 45  PHE   A O    1 
ATOM   358  C  CB   . PHE   A 1 46 ? 9.057   -20.364 0.853   1.00 22.12 ? 45  PHE   A CB   1 
ATOM   359  C  CG   . PHE   A 1 46 ? 9.491   -18.978 0.474   1.00 24.52 ? 45  PHE   A CG   1 
ATOM   360  C  CD1  . PHE   A 1 46 ? 10.732  -18.767 -0.102  1.00 21.84 ? 45  PHE   A CD1  1 
ATOM   361  C  CD2  . PHE   A 1 46 ? 8.665   -17.887 0.699   1.00 20.23 ? 45  PHE   A CD2  1 
ATOM   362  C  CE1  . PHE   A 1 46 ? 11.146  -17.487 -0.453  1.00 22.04 ? 45  PHE   A CE1  1 
ATOM   363  C  CE2  . PHE   A 1 46 ? 9.075   -16.603 0.353   1.00 22.17 ? 45  PHE   A CE2  1 
ATOM   364  C  CZ   . PHE   A 1 46 ? 10.321  -16.406 -0.225  1.00 22.83 ? 45  PHE   A CZ   1 
ATOM   365  N  N    . GLY   A 1 47 ? 9.647   -23.423 0.342   1.00 22.78 ? 46  GLY   A N    1 
ATOM   366  C  CA   . GLY   A 1 47 ? 9.566   -24.807 0.768   1.00 24.25 ? 46  GLY   A CA   1 
ATOM   367  C  C    . GLY   A 1 47 ? 9.402   -25.767 -0.394  1.00 29.67 ? 46  GLY   A C    1 
ATOM   368  O  O    . GLY   A 1 47 ? 10.311  -26.546 -0.696  1.00 33.13 ? 46  GLY   A O    1 
ATOM   369  N  N    . THR   A 1 48 ? 8.251   -25.722 -1.064  1.00 27.91 ? 47  THR   A N    1 
ATOM   370  C  CA   . THR   A 1 48 ? 8.043   -26.572 -2.229  1.00 30.20 ? 47  THR   A CA   1 
ATOM   371  C  C    . THR   A 1 48 ? 8.770   -26.061 -3.464  1.00 29.69 ? 47  THR   A C    1 
ATOM   372  O  O    . THR   A 1 48 ? 9.034   -26.850 -4.382  1.00 26.64 ? 47  THR   A O    1 
ATOM   373  C  CB   . THR   A 1 48 ? 6.554   -26.689 -2.537  1.00 30.83 ? 47  THR   A CB   1 
ATOM   374  O  OG1  . THR   A 1 48 ? 6.050   -25.402 -2.926  1.00 28.52 ? 47  THR   A OG1  1 
ATOM   375  C  CG2  . THR   A 1 48 ? 5.802   -27.176 -1.309  1.00 35.50 ? 47  THR   A CG2  1 
ATOM   376  N  N    . HIS   A 1 49 ? 9.079   -24.764 -3.509  1.00 24.40 ? 48  HIS   A N    1 
ATOM   377  C  CA   . HIS   A 1 49 ? 9.767   -24.123 -4.625  1.00 24.33 ? 48  HIS   A CA   1 
ATOM   378  C  C    . HIS   A 1 49 ? 8.993   -24.254 -5.933  1.00 24.99 ? 48  HIS   A C    1 
ATOM   379  O  O    . HIS   A 1 49 ? 9.577   -24.171 -7.016  1.00 30.27 ? 48  HIS   A O    1 
ATOM   380  C  CB   . HIS   A 1 49 ? 11.191  -24.663 -4.785  1.00 28.97 ? 48  HIS   A CB   1 
ATOM   381  C  CG   . HIS   A 1 49 ? 11.967  -24.691 -3.505  1.00 28.95 ? 48  HIS   A CG   1 
ATOM   382  N  ND1  . HIS   A 1 49 ? 12.860  -25.694 -3.196  1.00 32.22 ? 48  HIS   A ND1  1 
ATOM   383  C  CD2  . HIS   A 1 49 ? 11.977  -23.839 -2.453  1.00 27.15 ? 48  HIS   A CD2  1 
ATOM   384  C  CE1  . HIS   A 1 49 ? 13.389  -25.458 -2.008  1.00 45.58 ? 48  HIS   A CE1  1 
ATOM   385  N  NE2  . HIS   A 1 49 ? 12.871  -24.337 -1.536  1.00 32.84 ? 48  HIS   A NE2  1 
ATOM   386  N  N    . GLU   A 1 50 ? 7.682   -24.448 -5.845  1.00 29.51 ? 49  GLU   A N    1 
ATOM   387  C  CA   . GLU   A 1 50 ? 6.809   -24.456 -7.006  1.00 32.40 ? 49  GLU   A CA   1 
ATOM   388  C  C    . GLU   A 1 50 ? 6.334   -23.039 -7.306  1.00 28.29 ? 49  GLU   A C    1 
ATOM   389  O  O    . GLU   A 1 50 ? 6.388   -22.146 -6.458  1.00 27.07 ? 49  GLU   A O    1 
ATOM   390  C  CB   . GLU   A 1 50 ? 5.615   -25.385 -6.773  1.00 29.81 ? 49  GLU   A CB   1 
ATOM   391  C  CG   . GLU   A 1 50 ? 6.018   -26.838 -6.530  1.00 40.03 ? 49  GLU   A CG   1 
ATOM   392  C  CD   . GLU   A 1 50 ? 4.868   -27.706 -6.054  1.00 46.89 ? 49  GLU   A CD   1 
ATOM   393  O  OE1  . GLU   A 1 50 ? 3.699   -27.351 -6.314  1.00 46.53 ? 49  GLU   A OE1  1 
ATOM   394  O  OE2  . GLU   A 1 50 ? 5.137   -28.746 -5.412  1.00 49.08 ? 49  GLU   A OE2  1 
ATOM   395  N  N    . THR   A 1 51 ? 5.884   -22.835 -8.539  1.00 26.77 ? 50  THR   A N    1 
ATOM   396  C  CA   . THR   A 1 51 ? 5.374   -21.548 -8.985  1.00 23.49 ? 50  THR   A CA   1 
ATOM   397  C  C    . THR   A 1 51 ? 3.929   -21.707 -9.436  1.00 29.40 ? 50  THR   A C    1 
ATOM   398  O  O    . THR   A 1 51 ? 3.574   -22.711 -10.059 1.00 32.76 ? 50  THR   A O    1 
ATOM   399  C  CB   . THR   A 1 51 ? 6.222   -20.975 -10.139 1.00 30.74 ? 50  THR   A CB   1 
ATOM   400  O  OG1  . THR   A 1 51 ? 7.541   -20.670 -9.667  1.00 31.37 ? 50  THR   A OG1  1 
ATOM   401  C  CG2  . THR   A 1 51 ? 5.594   -19.711 -10.712 1.00 33.52 ? 50  THR   A CG2  1 
ATOM   402  N  N    . ALA   A 1 52 ? 3.097   -20.724 -9.100  1.00 25.36 ? 51  ALA   A N    1 
ATOM   403  C  CA   . ALA   A 1 52 ? 1.753   -20.625 -9.644  1.00 22.85 ? 51  ALA   A CA   1 
ATOM   404  C  C    . ALA   A 1 52 ? 1.464   -19.173 -9.993  1.00 30.32 ? 51  ALA   A C    1 
ATOM   405  O  O    . ALA   A 1 52 ? 2.113   -18.250 -9.493  1.00 28.21 ? 51  ALA   A O    1 
ATOM   406  C  CB   . ALA   A 1 52 ? 0.697   -21.155 -8.666  1.00 30.59 ? 51  ALA   A CB   1 
ATOM   407  N  N    . PHE   A 1 53 ? 0.476   -18.977 -10.861 1.00 21.35 ? 52  PHE   A N    1 
ATOM   408  C  CA   . PHE   A 1 53 ? 0.039   -17.647 -11.271 1.00 20.33 ? 52  PHE   A CA   1 
ATOM   409  C  C    . PHE   A 1 53 ? -1.214  -17.284 -10.486 1.00 26.11 ? 52  PHE   A C    1 
ATOM   410  O  O    . PHE   A 1 53 ? -2.216  -18.001 -10.553 1.00 31.29 ? 52  PHE   A O    1 
ATOM   411  C  CB   . PHE   A 1 53 ? -0.243  -17.608 -12.773 1.00 28.89 ? 52  PHE   A CB   1 
ATOM   412  C  CG   . PHE   A 1 53 ? 0.966   -17.865 -13.623 1.00 30.35 ? 52  PHE   A CG   1 
ATOM   413  C  CD1  . PHE   A 1 53 ? 2.135   -17.152 -13.420 1.00 28.14 ? 52  PHE   A CD1  1 
ATOM   414  C  CD2  . PHE   A 1 53 ? 0.932   -18.820 -14.629 1.00 32.75 ? 52  PHE   A CD2  1 
ATOM   415  C  CE1  . PHE   A 1 53 ? 3.251   -17.384 -14.206 1.00 42.87 ? 52  PHE   A CE1  1 
ATOM   416  C  CE2  . PHE   A 1 53 ? 2.046   -19.055 -15.418 1.00 33.82 ? 52  PHE   A CE2  1 
ATOM   417  C  CZ   . PHE   A 1 53 ? 3.205   -18.340 -15.205 1.00 33.01 ? 52  PHE   A CZ   1 
ATOM   418  N  N    . LEU   A 1 54 ? -1.164  -16.174 -9.751  1.00 22.92 ? 53  LEU   A N    1 
ATOM   419  C  CA   . LEU   A 1 54 ? -2.260  -15.811 -8.867  1.00 22.68 ? 53  LEU   A CA   1 
ATOM   420  C  C    . LEU   A 1 54 ? -2.565  -14.328 -8.987  1.00 21.94 ? 53  LEU   A C    1 
ATOM   421  O  O    . LEU   A 1 54 ? -1.686  -13.519 -9.298  1.00 24.62 ? 53  LEU   A O    1 
ATOM   422  C  CB   . LEU   A 1 54 ? -1.944  -16.133 -7.398  1.00 21.11 ? 53  LEU   A CB   1 
ATOM   423  C  CG   . LEU   A 1 54 ? -1.874  -17.602 -6.993  1.00 23.84 ? 53  LEU   A CG   1 
ATOM   424  C  CD1  . LEU   A 1 54 ? -1.557  -17.712 -5.511  1.00 23.69 ? 53  LEU   A CD1  1 
ATOM   425  C  CD2  . LEU   A 1 54 ? -3.180  -18.302 -7.314  1.00 32.43 ? 53  LEU   A CD2  1 
ATOM   426  N  N    . GLY   A 1 55 ? -3.823  -13.981 -8.724  1.00 21.13 ? 54  GLY   A N    1 
ATOM   427  C  CA   . GLY   A 1 55 ? -4.237  -12.603 -8.633  1.00 22.47 ? 54  GLY   A CA   1 
ATOM   428  C  C    . GLY   A 1 55 ? -4.205  -12.120 -7.196  1.00 22.51 ? 54  GLY   A C    1 
ATOM   429  O  O    . GLY   A 1 55 ? -4.089  -12.911 -6.255  1.00 23.89 ? 54  GLY   A O    1 
ATOM   430  N  N    . PRO   A 1 56 ? -4.312  -10.805 -7.001  1.00 20.80 ? 55  PRO   A N    1 
ATOM   431  C  CA   . PRO   A 1 56 ? -4.178  -10.246 -5.644  1.00 21.61 ? 55  PRO   A CA   1 
ATOM   432  C  C    . PRO   A 1 56 ? -5.199  -10.766 -4.646  1.00 24.64 ? 55  PRO   A C    1 
ATOM   433  O  O    . PRO   A 1 56 ? -4.941  -10.693 -3.438  1.00 21.44 ? 55  PRO   A O    1 
ATOM   434  C  CB   . PRO   A 1 56 ? -4.338  -8.739  -5.875  1.00 22.00 ? 55  PRO   A CB   1 
ATOM   435  C  CG   . PRO   A 1 56 ? -3.877  -8.540  -7.279  1.00 29.02 ? 55  PRO   A CG   1 
ATOM   436  C  CD   . PRO   A 1 56 ? -4.357  -9.750  -8.025  1.00 24.05 ? 55  PRO   A CD   1 
ATOM   437  N  N    . LYS   A 1 57 ? -6.343  -11.292 -5.096  1.00 24.17 ? 56  LYS   A N    1 
ATOM   438  C  CA   . LYS   A 1 57 ? -7.329  -11.802 -4.144  1.00 24.04 ? 56  LYS   A CA   1 
ATOM   439  C  C    . LYS   A 1 57 ? -6.764  -12.927 -3.288  1.00 24.56 ? 56  LYS   A C    1 
ATOM   440  O  O    . LYS   A 1 57 ? -7.268  -13.172 -2.185  1.00 24.82 ? 56  LYS   A O    1 
ATOM   441  C  CB   . LYS   A 1 57 ? -8.586  -12.291 -4.873  1.00 28.47 ? 56  LYS   A CB   1 
ATOM   442  C  CG   . LYS   A 1 57 ? -8.448  -13.654 -5.533  1.00 29.55 ? 56  LYS   A CG   1 
ATOM   443  C  CD   . LYS   A 1 57 ? -9.685  -13.991 -6.366  1.00 37.05 ? 56  LYS   A CD   1 
ATOM   444  C  CE   . LYS   A 1 57 ? -9.600  -15.396 -6.945  1.00 33.42 ? 56  LYS   A CE   1 
ATOM   445  N  NZ   . LYS   A 1 57 ? -9.624  -16.457 -5.899  1.00 40.98 ? 56  LYS   A NZ   1 
ATOM   446  N  N    . ASP   A 1 58 ? -5.718  -13.601 -3.761  1.00 21.46 ? 57  ASP   A N    1 
ATOM   447  C  CA   . ASP   A 1 58 ? -5.120  -14.723 -3.057  1.00 20.84 ? 57  ASP   A CA   1 
ATOM   448  C  C    . ASP   A 1 58 ? -3.768  -14.383 -2.444  1.00 21.09 ? 57  ASP   A C    1 
ATOM   449  O  O    . ASP   A 1 58 ? -3.046  -15.293 -2.035  1.00 25.94 ? 57  ASP   A O    1 
ATOM   450  C  CB   . ASP   A 1 58 ? -4.988  -15.918 -4.008  1.00 24.16 ? 57  ASP   A CB   1 
ATOM   451  C  CG   . ASP   A 1 58 ? -6.335  -16.527 -4.355  1.00 31.85 ? 57  ASP   A CG   1 
ATOM   452  O  OD1  . ASP   A 1 58 ? -7.199  -16.597 -3.456  1.00 30.25 ? 57  ASP   A OD1  1 
ATOM   453  O  OD2  . ASP   A 1 58 ? -6.540  -16.922 -5.519  1.00 29.98 ? 57  ASP   A OD2  1 
ATOM   454  N  N    . LEU   A 1 59 ? -3.413  -13.099 -2.363  1.00 21.35 ? 58  LEU   A N    1 
ATOM   455  C  CA   . LEU   A 1 59 ? -2.101  -12.660 -1.893  1.00 18.57 ? 58  LEU   A CA   1 
ATOM   456  C  C    . LEU   A 1 59 ? -2.273  -11.811 -0.641  1.00 19.72 ? 58  LEU   A C    1 
ATOM   457  O  O    . LEU   A 1 59 ? -2.905  -10.749 -0.686  1.00 21.04 ? 58  LEU   A O    1 
ATOM   458  C  CB   . LEU   A 1 59 ? -1.368  -11.869 -2.986  1.00 19.54 ? 58  LEU   A CB   1 
ATOM   459  C  CG   . LEU   A 1 59 ? -1.225  -12.622 -4.309  1.00 22.01 ? 58  LEU   A CG   1 
ATOM   460  C  CD1  . LEU   A 1 59 ? -0.548  -11.767 -5.364  1.00 23.05 ? 58  LEU   A CD1  1 
ATOM   461  C  CD2  . LEU   A 1 59 ? -0.457  -13.910 -4.102  1.00 20.97 ? 58  LEU   A CD2  1 
ATOM   462  N  N    . PHE   A 1 60 ? -1.700  -12.271 0.470   1.00 20.34 ? 59  PHE   A N    1 
ATOM   463  C  CA   . PHE   A 1 60 ? -1.796  -11.589 1.755   1.00 21.37 ? 59  PHE   A CA   1 
ATOM   464  C  C    . PHE   A 1 60 ? -0.422  -11.107 2.190   1.00 19.76 ? 59  PHE   A C    1 
ATOM   465  O  O    . PHE   A 1 60 ? 0.513   -11.912 2.218   1.00 25.41 ? 59  PHE   A O    1 
ATOM   466  C  CB   . PHE   A 1 60 ? -2.376  -12.540 2.812   1.00 24.64 ? 59  PHE   A CB   1 
ATOM   467  C  CG   . PHE   A 1 60 ? -3.771  -13.006 2.506   1.00 24.51 ? 59  PHE   A CG   1 
ATOM   468  C  CD1  . PHE   A 1 60 ? -4.004  -13.960 1.525   1.00 22.26 ? 59  PHE   A CD1  1 
ATOM   469  C  CD2  . PHE   A 1 60 ? -4.852  -12.482 3.198   1.00 23.70 ? 59  PHE   A CD2  1 
ATOM   470  C  CE1  . PHE   A 1 60 ? -5.293  -14.384 1.236   1.00 30.99 ? 59  PHE   A CE1  1 
ATOM   471  C  CE2  . PHE   A 1 60 ? -6.141  -12.905 2.919   1.00 24.21 ? 59  PHE   A CE2  1 
ATOM   472  C  CZ   . PHE   A 1 60 ? -6.362  -13.851 1.938   1.00 24.40 ? 59  PHE   A CZ   1 
ATOM   473  N  N    . PRO   A 1 61 ? -0.250  -9.834  2.544   1.00 25.97 ? 60  PRO   A N    1 
ATOM   474  C  CA   . PRO   A 1 61 ? 1.088   -9.349  2.912   1.00 24.66 ? 60  PRO   A CA   1 
ATOM   475  C  C    . PRO   A 1 61 ? 1.671   -10.112 4.095   1.00 24.61 ? 60  PRO   A C    1 
ATOM   476  O  O    . PRO   A 1 61 ? 0.981   -10.410 5.072   1.00 28.02 ? 60  PRO   A O    1 
ATOM   477  C  CB   . PRO   A 1 61 ? 0.849   -7.873  3.255   1.00 32.35 ? 60  PRO   A CB   1 
ATOM   478  C  CG   . PRO   A 1 61 ? -0.615  -7.788  3.579   1.00 37.93 ? 60  PRO   A CG   1 
ATOM   479  C  CD   . PRO   A 1 61 ? -1.267  -8.772  2.654   1.00 32.35 ? 60  PRO   A CD   1 
ATOM   480  N  N    . TYR   A 1 62 ? 2.965   -10.431 3.989   1.00 24.08 ? 61  TYR   A N    1 
ATOM   481  C  CA   . TYR   A 1 62 ? 3.591   -11.322 4.962   1.00 23.74 ? 61  TYR   A CA   1 
ATOM   482  C  C    . TYR   A 1 62 ? 3.663   -10.683 6.341   1.00 26.08 ? 61  TYR   A C    1 
ATOM   483  O  O    . TYR   A 1 62 ? 3.377   -11.340 7.349   1.00 30.20 ? 61  TYR   A O    1 
ATOM   484  C  CB   . TYR   A 1 62 ? 4.991   -11.722 4.489   1.00 27.03 ? 61  TYR   A CB   1 
ATOM   485  C  CG   . TYR   A 1 62 ? 5.803   -12.484 5.521   1.00 21.87 ? 61  TYR   A CG   1 
ATOM   486  C  CD1  . TYR   A 1 62 ? 5.513   -13.806 5.826   1.00 28.17 ? 61  TYR   A CD1  1 
ATOM   487  C  CD2  . TYR   A 1 62 ? 6.873   -11.882 6.169   1.00 29.21 ? 61  TYR   A CD2  1 
ATOM   488  C  CE1  . TYR   A 1 62 ? 6.257   -14.510 6.764   1.00 26.97 ? 61  TYR   A CE1  1 
ATOM   489  C  CE2  . TYR   A 1 62 ? 7.624   -12.575 7.106   1.00 25.56 ? 61  TYR   A CE2  1 
ATOM   490  C  CZ   . TYR   A 1 62 ? 7.312   -13.886 7.399   1.00 26.35 ? 61  TYR   A CZ   1 
ATOM   491  O  OH   . TYR   A 1 62 ? 8.053   -14.581 8.329   1.00 28.50 ? 61  TYR   A OH   1 
ATOM   492  N  N    . ASP   A 1 63 ? 4.043   -9.408  6.411   1.00 27.69 ? 62  ASP   A N    1 
ATOM   493  C  CA   . ASP   A 1 63 ? 4.209   -8.781  7.719   1.00 32.22 ? 62  ASP   A CA   1 
ATOM   494  C  C    . ASP   A 1 63 ? 2.872   -8.634  8.435   1.00 30.79 ? 62  ASP   A C    1 
ATOM   495  O  O    . ASP   A 1 63 ? 2.785   -8.848  9.649   1.00 39.65 ? 62  ASP   A O    1 
ATOM   496  C  CB   . ASP   A 1 63 ? 4.914   -7.431  7.578   1.00 27.71 ? 62  ASP   A CB   1 
ATOM   497  C  CG   . ASP   A 1 63 ? 4.208   -6.478  6.620   1.00 42.80 ? 62  ASP   A CG   1 
ATOM   498  O  OD1  . ASP   A 1 63 ? 3.089   -6.779  6.145   1.00 40.66 ? 62  ASP   A OD1  1 
ATOM   499  O  OD2  . ASP   A 1 63 ? 4.792   -5.411  6.335   1.00 52.87 ? 62  ASP   A OD2  1 
ATOM   500  N  N    . LYS   A 1 64 ? 1.815   -8.303  7.694   1.00 33.32 ? 63  LYS   A N    1 
ATOM   501  C  CA   . LYS   A 1 64 ? 0.508   -8.109  8.313   1.00 37.91 ? 63  LYS   A CA   1 
ATOM   502  C  C    . LYS   A 1 64 ? -0.104  -9.419  8.798   1.00 32.27 ? 63  LYS   A C    1 
ATOM   503  O  O    . LYS   A 1 64 ? -0.809  -9.431  9.814   1.00 30.81 ? 63  LYS   A O    1 
ATOM   504  C  CB   . LYS   A 1 64 ? -0.427  -7.418  7.317   1.00 36.47 ? 63  LYS   A CB   1 
ATOM   505  C  CG   . LYS   A 1 64 ? -1.882  -7.267  7.755   1.00 35.20 ? 63  LYS   A CG   1 
ATOM   506  C  CD   . LYS   A 1 64 ? -2.710  -6.625  6.640   1.00 34.66 ? 63  LYS   A CD   1 
ATOM   507  C  CE   . LYS   A 1 64 ? -4.193  -6.603  6.978   1.00 46.09 ? 63  LYS   A CE   1 
ATOM   508  N  NZ   . LYS   A 1 64 ? -4.471  -5.867  8.241   1.00 42.74 ? 63  LYS   A NZ   1 
ATOM   509  N  N    . CYS   A 1 65 ? 0.161   -10.532 8.115   1.00 30.74 ? 64  CYS   A N    1 
ATOM   510  C  CA   A CYS   A 1 65 ? -0.574  -11.768 8.353   0.75 29.32 ? 64  CYS   A CA   1 
ATOM   511  C  CA   B CYS   A 1 65 ? -0.572  -11.771 8.346   0.25 29.42 ? 64  CYS   A CA   1 
ATOM   512  C  C    . CYS   A 1 65 ? 0.283   -12.891 8.925   1.00 29.41 ? 64  CYS   A C    1 
ATOM   513  O  O    . CYS   A 1 65 ? -0.200  -14.023 9.041   1.00 32.25 ? 64  CYS   A O    1 
ATOM   514  C  CB   A CYS   A 1 65 ? -1.237  -12.227 7.054   0.75 27.04 ? 64  CYS   A CB   1 
ATOM   515  C  CB   B CYS   A 1 65 ? -1.220  -12.247 7.044   0.25 27.18 ? 64  CYS   A CB   1 
ATOM   516  S  SG   A CYS   A 1 65 ? -2.255  -10.951 6.292   0.75 33.94 ? 64  CYS   A SG   1 
ATOM   517  S  SG   B CYS   A 1 65 ? -2.603  -11.238 6.491   0.25 33.00 ? 64  CYS   A SG   1 
ATOM   518  N  N    . LYS   A 1 66 ? 1.536   -12.616 9.299   1.00 27.69 ? 65  LYS   A N    1 
ATOM   519  C  CA   . LYS   A 1 66 ? 2.390   -13.707 9.765   1.00 37.16 ? 65  LYS   A CA   1 
ATOM   520  C  C    . LYS   A 1 66 ? 1.932   -14.263 11.106  1.00 32.28 ? 65  LYS   A C    1 
ATOM   521  O  O    . LYS   A 1 66 ? 2.070   -15.468 11.350  1.00 31.75 ? 65  LYS   A O    1 
ATOM   522  C  CB   . LYS   A 1 66 ? 3.850   -13.263 9.838   1.00 34.41 ? 65  LYS   A CB   1 
ATOM   523  C  CG   . LYS   A 1 66 ? 4.117   -12.007 10.629  1.00 41.13 ? 65  LYS   A CG   1 
ATOM   524  C  CD   . LYS   A 1 66 ? 5.605   -11.710 10.614  1.00 52.22 ? 65  LYS   A CD   1 
ATOM   525  C  CE   . LYS   A 1 66 ? 5.918   -10.356 11.219  1.00 49.11 ? 65  LYS   A CE   1 
ATOM   526  N  NZ   . LYS   A 1 66 ? 7.365   -10.041 11.069  1.00 62.37 ? 65  LYS   A NZ   1 
ATOM   527  N  N    A ASP   A 1 67 ? 1.390   -13.412 11.981  0.48 33.16 ? 66  ASP   A N    1 
ATOM   528  N  N    B ASP   A 1 67 ? 1.384   -13.422 11.986  0.52 33.16 ? 66  ASP   A N    1 
ATOM   529  C  CA   A ASP   A 1 67 ? 0.856   -13.904 13.248  0.48 37.14 ? 66  ASP   A CA   1 
ATOM   530  C  CA   B ASP   A 1 67 ? 0.881   -13.939 13.255  0.52 37.12 ? 66  ASP   A CA   1 
ATOM   531  C  C    A ASP   A 1 67 ? -0.269  -14.901 13.015  0.48 36.54 ? 66  ASP   A C    1 
ATOM   532  C  C    B ASP   A 1 67 ? -0.309  -14.869 13.052  0.52 36.53 ? 66  ASP   A C    1 
ATOM   533  O  O    A ASP   A 1 67 ? -0.406  -15.881 13.756  0.48 40.30 ? 66  ASP   A O    1 
ATOM   534  O  O    B ASP   A 1 67 ? -0.531  -15.773 13.864  0.52 40.86 ? 66  ASP   A O    1 
ATOM   535  C  CB   A ASP   A 1 67 ? 0.366   -12.735 14.106  0.48 37.61 ? 66  ASP   A CB   1 
ATOM   536  C  CB   B ASP   A 1 67 ? 0.509   -12.786 14.188  0.52 37.57 ? 66  ASP   A CB   1 
ATOM   537  C  CG   A ASP   A 1 67 ? -0.821  -12.005 13.491  0.48 40.75 ? 66  ASP   A CG   1 
ATOM   538  C  CG   B ASP   A 1 67 ? 1.677   -12.322 15.039  0.52 44.72 ? 66  ASP   A CG   1 
ATOM   539  O  OD1  A ASP   A 1 67 ? -0.930  -11.963 12.248  0.48 40.54 ? 66  ASP   A OD1  1 
ATOM   540  O  OD1  B ASP   A 1 67 ? 2.325   -13.176 15.680  0.52 48.55 ? 66  ASP   A OD1  1 
ATOM   541  O  OD2  A ASP   A 1 67 ? -1.651  -11.468 14.261  0.48 42.82 ? 66  ASP   A OD2  1 
ATOM   542  O  OD2  B ASP   A 1 67 ? 1.951   -11.103 15.064  0.52 43.88 ? 66  ASP   A OD2  1 
ATOM   543  N  N    . LYS   A 1 68 ? -1.073  -14.675 11.977  1.00 30.24 ? 67  LYS   A N    1 
ATOM   544  C  CA   . LYS   A 1 68 ? -2.211  -15.542 11.702  1.00 30.68 ? 67  LYS   A CA   1 
ATOM   545  C  C    . LYS   A 1 68 ? -1.792  -16.803 10.951  1.00 33.49 ? 67  LYS   A C    1 
ATOM   546  O  O    . LYS   A 1 68 ? -2.207  -17.913 11.305  1.00 31.66 ? 67  LYS   A O    1 
ATOM   547  C  CB   . LYS   A 1 68 ? -3.257  -14.762 10.904  1.00 33.73 ? 67  LYS   A CB   1 
ATOM   548  C  CG   . LYS   A 1 68 ? -4.549  -15.505 10.636  1.00 35.42 ? 67  LYS   A CG   1 
ATOM   549  C  CD   . LYS   A 1 68 ? -5.566  -14.588 9.973   1.00 48.13 ? 67  LYS   A CD   1 
ATOM   550  C  CE   . LYS   A 1 68 ? -6.917  -15.268 9.818   1.00 56.05 ? 67  LYS   A CE   1 
ATOM   551  N  NZ   . LYS   A 1 68 ? -7.926  -14.350 9.219   1.00 49.40 ? 67  LYS   A NZ   1 
ATOM   552  N  N    . TYR   A 1 69 ? -0.958  -16.654 9.918   1.00 27.81 ? 68  TYR   A N    1 
ATOM   553  C  CA   . TYR   A 1 69 ? -0.684  -17.729 8.975   1.00 24.87 ? 68  TYR   A CA   1 
ATOM   554  C  C    . TYR   A 1 69 ? 0.690   -18.365 9.131   1.00 28.17 ? 68  TYR   A C    1 
ATOM   555  O  O    . TYR   A 1 69 ? 0.947   -19.391 8.490   1.00 30.96 ? 68  TYR   A O    1 
ATOM   556  C  CB   . TYR   A 1 69 ? -0.818  -17.214 7.531   1.00 25.73 ? 68  TYR   A CB   1 
ATOM   557  C  CG   . TYR   A 1 69 ? -2.208  -16.754 7.149   1.00 24.45 ? 68  TYR   A CG   1 
ATOM   558  C  CD1  . TYR   A 1 69 ? -3.334  -17.452 7.564   1.00 30.77 ? 68  TYR   A CD1  1 
ATOM   559  C  CD2  . TYR   A 1 69 ? -2.390  -15.616 6.372   1.00 26.29 ? 68  TYR   A CD2  1 
ATOM   560  C  CE1  . TYR   A 1 69 ? -4.607  -17.031 7.213   1.00 29.28 ? 68  TYR   A CE1  1 
ATOM   561  C  CE2  . TYR   A 1 69 ? -3.654  -15.186 6.020   1.00 30.35 ? 68  TYR   A CE2  1 
ATOM   562  C  CZ   . TYR   A 1 69 ? -4.759  -15.897 6.443   1.00 31.74 ? 68  TYR   A CZ   1 
ATOM   563  O  OH   . TYR   A 1 69 ? -6.016  -15.469 6.089   1.00 33.23 ? 68  TYR   A OH   1 
ATOM   564  N  N    . GLY   A 1 70 ? 1.574   -17.798 9.949   1.00 27.83 ? 69  GLY   A N    1 
ATOM   565  C  CA   . GLY   A 1 70 ? 2.951   -18.251 9.991   1.00 28.84 ? 69  GLY   A CA   1 
ATOM   566  C  C    . GLY   A 1 70 ? 3.279   -19.252 11.082  1.00 33.00 ? 69  GLY   A C    1 
ATOM   567  O  O    . GLY   A 1 70 ? 4.368   -19.204 11.659  1.00 36.68 ? 69  GLY   A O    1 
ATOM   568  N  N    . LYS   A 1 71 ? 2.361   -20.157 11.369  1.00 32.02 ? 70  LYS   A N    1 
ATOM   569  C  CA   . LYS   A 1 71 ? 2.600   -21.196 12.359  1.00 34.98 ? 70  LYS   A CA   1 
ATOM   570  C  C    . LYS   A 1 71 ? 2.952   -22.508 11.669  1.00 32.01 ? 70  LYS   A C    1 
ATOM   571  O  O    . LYS   A 1 71 ? 2.540   -22.743 10.531  1.00 31.42 ? 70  LYS   A O    1 
ATOM   572  C  CB   . LYS   A 1 71 ? 1.365   -21.403 13.241  1.00 33.18 ? 70  LYS   A CB   1 
ATOM   573  C  CG   . LYS   A 1 71 ? 0.869   -20.142 13.927  1.00 39.62 ? 70  LYS   A CG   1 
ATOM   574  C  CD   . LYS   A 1 71 ? 1.923   -19.560 14.854  1.00 51.58 ? 70  LYS   A CD   1 
ATOM   575  C  CE   . LYS   A 1 71 ? 1.414   -18.306 15.550  1.00 47.17 ? 70  LYS   A CE   1 
ATOM   576  N  NZ   . LYS   A 1 71 ? 2.460   -17.688 16.411  1.00 51.41 ? 70  LYS   A NZ   1 
ATOM   577  N  N    . PRO   A 1 72 ? 3.717   -23.380 12.326  1.00 31.21 ? 71  PRO   A N    1 
ATOM   578  C  CA   . PRO   A 1 72 ? 4.069   -24.662 11.707  1.00 30.73 ? 71  PRO   A CA   1 
ATOM   579  C  C    . PRO   A 1 72 ? 2.843   -25.450 11.268  1.00 31.88 ? 71  PRO   A C    1 
ATOM   580  O  O    . PRO   A 1 72 ? 1.782   -25.405 11.895  1.00 38.48 ? 71  PRO   A O    1 
ATOM   581  C  CB   . PRO   A 1 72 ? 4.833   -25.389 12.817  1.00 34.85 ? 71  PRO   A CB   1 
ATOM   582  C  CG   . PRO   A 1 72 ? 5.462   -24.284 13.584  1.00 39.15 ? 71  PRO   A CG   1 
ATOM   583  C  CD   . PRO   A 1 72 ? 4.468   -23.151 13.572  1.00 35.41 ? 71  PRO   A CD   1 
ATOM   584  N  N    . ASN   A 1 73 ? 3.007   -26.171 10.164  1.00 33.44 ? 72  ASN   A N    1 
ATOM   585  C  CA   . ASN   A 1 73 ? 1.934   -26.927 9.540   1.00 40.91 ? 72  ASN   A CA   1 
ATOM   586  C  C    . ASN   A 1 73 ? 2.505   -28.246 9.042   1.00 44.76 ? 72  ASN   A C    1 
ATOM   587  O  O    . ASN   A 1 73 ? 3.681   -28.329 8.677   1.00 42.92 ? 72  ASN   A O    1 
ATOM   588  C  CB   . ASN   A 1 73 ? 1.303   -26.138 8.382   1.00 43.87 ? 72  ASN   A CB   1 
ATOM   589  C  CG   . ASN   A 1 73 ? -0.007  -26.728 7.914   1.00 46.97 ? 72  ASN   A CG   1 
ATOM   590  O  OD1  . ASN   A 1 73 ? -0.029  -27.713 7.182   1.00 45.68 ? 72  ASN   A OD1  1 
ATOM   591  N  ND2  . ASN   A 1 73 ? -1.112  -26.118 8.328   1.00 56.31 ? 72  ASN   A ND2  1 
ATOM   592  N  N    . LYS   A 1 74 ? 1.663   -29.280 9.029   1.00 40.79 ? 73  LYS   A N    1 
ATOM   593  C  CA   . LYS   A 1 74 ? 2.128   -30.612 8.663   1.00 38.42 ? 73  LYS   A CA   1 
ATOM   594  C  C    . LYS   A 1 74 ? 2.330   -30.792 7.163   1.00 36.50 ? 73  LYS   A C    1 
ATOM   595  O  O    . LYS   A 1 74 ? 2.954   -31.779 6.761   1.00 41.79 ? 73  LYS   A O    1 
ATOM   596  C  CB   . LYS   A 1 74 ? 1.144   -31.667 9.176   1.00 42.48 ? 73  LYS   A CB   1 
ATOM   597  N  N    . ARG   A 1 75 ? 1.833   -29.879 6.331   1.00 38.08 ? 74  ARG   A N    1 
ATOM   598  C  CA   . ARG   A 1 75 ? 1.901   -30.079 4.890   1.00 37.97 ? 74  ARG   A CA   1 
ATOM   599  C  C    . ARG   A 1 75 ? 3.347   -30.100 4.405   1.00 34.23 ? 74  ARG   A C    1 
ATOM   600  O  O    . ARG   A 1 75 ? 4.220   -29.411 4.939   1.00 34.30 ? 74  ARG   A O    1 
ATOM   601  C  CB   . ARG   A 1 75 ? 1.113   -28.990 4.162   1.00 40.45 ? 74  ARG   A CB   1 
ATOM   602  C  CG   . ARG   A 1 75 ? -0.384  -29.035 4.437   1.00 43.91 ? 74  ARG   A CG   1 
ATOM   603  C  CD   . ARG   A 1 75 ? -1.012  -30.337 3.960   1.00 36.88 ? 74  ARG   A CD   1 
ATOM   604  N  NE   . ARG   A 1 75 ? -1.338  -30.301 2.540   1.00 49.36 ? 74  ARG   A NE   1 
ATOM   605  C  CZ   . ARG   A 1 75 ? -2.439  -29.755 2.040   1.00 42.17 ? 74  ARG   A CZ   1 
ATOM   606  N  NH1  . ARG   A 1 75 ? -3.343  -29.185 2.818   1.00 42.02 ? 74  ARG   A NH1  1 
ATOM   607  N  NH2  . ARG   A 1 75 ? -2.636  -29.781 0.725   1.00 52.54 ? 74  ARG   A NH2  1 
ATOM   608  N  N    . LYS   A 1 76 ? 3.589   -30.913 3.379   1.00 32.89 ? 75  LYS   A N    1 
ATOM   609  C  CA   . LYS   A 1 76 ? 4.935   -31.116 2.858   1.00 31.40 ? 75  LYS   A CA   1 
ATOM   610  C  C    . LYS   A 1 76 ? 5.535   -29.799 2.386   1.00 35.40 ? 75  LYS   A C    1 
ATOM   611  O  O    . LYS   A 1 76 ? 4.962   -29.116 1.533   1.00 33.51 ? 75  LYS   A O    1 
ATOM   612  C  CB   . LYS   A 1 76 ? 4.898   -32.125 1.712   1.00 38.89 ? 75  LYS   A CB   1 
ATOM   613  C  CG   . LYS   A 1 76 ? 6.244   -32.386 1.058   1.00 39.82 ? 75  LYS   A CG   1 
ATOM   614  C  CD   . LYS   A 1 76 ? 6.113   -33.381 -0.087  1.00 43.63 ? 75  LYS   A CD   1 
ATOM   615  C  CE   . LYS   A 1 76 ? 7.448   -33.602 -0.782  1.00 52.37 ? 75  LYS   A CE   1 
ATOM   616  N  NZ   . LYS   A 1 76 ? 8.487   -34.105 0.158   1.00 52.24 ? 75  LYS   A NZ   1 
ATOM   617  N  N    . GLY   A 1 77 ? 6.687   -29.442 2.949   1.00 33.55 ? 76  GLY   A N    1 
ATOM   618  C  CA   . GLY   A 1 77 ? 7.398   -28.248 2.552   1.00 27.90 ? 76  GLY   A CA   1 
ATOM   619  C  C    . GLY   A 1 77 ? 7.020   -26.990 3.301   1.00 27.94 ? 76  GLY   A C    1 
ATOM   620  O  O    . GLY   A 1 77 ? 7.716   -25.978 3.157   1.00 31.19 ? 76  GLY   A O    1 
ATOM   621  N  N    . PHE   A 1 78 ? 5.956   -27.015 4.107   1.00 26.38 ? 77  PHE   A N    1 
ATOM   622  C  CA   . PHE   A 1 78 ? 5.470   -25.781 4.719   1.00 27.47 ? 77  PHE   A CA   1 
ATOM   623  C  C    . PHE   A 1 78 ? 6.477   -25.214 5.712   1.00 28.12 ? 77  PHE   A C    1 
ATOM   624  O  O    . PHE   A 1 78 ? 6.769   -24.014 5.693   1.00 25.89 ? 77  PHE   A O    1 
ATOM   625  C  CB   . PHE   A 1 78 ? 4.121   -26.017 5.401   1.00 31.25 ? 77  PHE   A CB   1 
ATOM   626  C  CG   . PHE   A 1 78 ? 3.418   -24.749 5.807   1.00 31.89 ? 77  PHE   A CG   1 
ATOM   627  C  CD1  . PHE   A 1 78 ? 3.716   -24.126 7.010   1.00 29.00 ? 77  PHE   A CD1  1 
ATOM   628  C  CD2  . PHE   A 1 78 ? 2.465   -24.174 4.980   1.00 25.44 ? 77  PHE   A CD2  1 
ATOM   629  C  CE1  . PHE   A 1 78 ? 3.073   -22.959 7.385   1.00 32.94 ? 77  PHE   A CE1  1 
ATOM   630  C  CE2  . PHE   A 1 78 ? 1.818   -23.004 5.355   1.00 23.51 ? 77  PHE   A CE2  1 
ATOM   631  C  CZ   . PHE   A 1 78 ? 2.124   -22.397 6.553   1.00 27.81 ? 77  PHE   A CZ   1 
ATOM   632  N  N    . ASN   A 1 79 ? 7.000   -26.058 6.605   1.00 27.94 ? 78  ASN   A N    1 
ATOM   633  C  CA   . ASN   A 1 79 ? 7.898   -25.568 7.646   1.00 26.36 ? 78  ASN   A CA   1 
ATOM   634  C  C    . ASN   A 1 79 ? 9.242   -25.155 7.072   1.00 25.35 ? 78  ASN   A C    1 
ATOM   635  O  O    . ASN   A 1 79 ? 9.842   -24.179 7.543   1.00 23.78 ? 78  ASN   A O    1 
ATOM   636  C  CB   . ASN   A 1 79 ? 8.070   -26.633 8.729   1.00 29.29 ? 78  ASN   A CB   1 
ATOM   637  C  CG   . ASN   A 1 79 ? 6.776   -26.916 9.459   1.00 33.39 ? 78  ASN   A CG   1 
ATOM   638  O  OD1  . ASN   A 1 79 ? 5.881   -26.075 9.491   1.00 28.52 ? 78  ASN   A OD1  1 
ATOM   639  N  ND2  . ASN   A 1 79 ? 6.665   -28.108 10.045  1.00 29.07 ? 78  ASN   A ND2  1 
ATOM   640  N  N    . GLU   A 1 80 ? 9.724   -25.871 6.054   1.00 24.81 ? 79  GLU   A N    1 
ATOM   641  C  CA   . GLU   A 1 80 ? 10.868  -25.379 5.299   1.00 24.10 ? 79  GLU   A CA   1 
ATOM   642  C  C    . GLU   A 1 80 ? 10.569  -24.006 4.711   1.00 23.44 ? 79  GLU   A C    1 
ATOM   643  O  O    . GLU   A 1 80 ? 11.400  -23.095 4.790   1.00 22.70 ? 79  GLU   A O    1 
ATOM   644  C  CB   . GLU   A 1 80 ? 11.246  -26.368 4.196   1.00 27.92 ? 79  GLU   A CB   1 
ATOM   645  C  CG   . GLU   A 1 80 ? 12.371  -25.879 3.294   1.00 27.76 ? 79  GLU   A CG   1 
ATOM   646  C  CD   . GLU   A 1 80 ? 12.999  -26.991 2.474   1.00 40.57 ? 79  GLU   A CD   1 
ATOM   647  O  OE1  . GLU   A 1 80 ? 12.382  -28.074 2.365   1.00 42.13 ? 79  GLU   A OE1  1 
ATOM   648  O  OE2  . GLU   A 1 80 ? 14.116  -26.787 1.950   1.00 39.58 ? 79  GLU   A OE2  1 
ATOM   649  N  N    . GLY   A 1 81 ? 9.373   -23.832 4.141   1.00 25.76 ? 80  GLY   A N    1 
ATOM   650  C  CA   . GLY   A 1 81 ? 9.001   -22.534 3.600   1.00 23.15 ? 80  GLY   A CA   1 
ATOM   651  C  C    . GLY   A 1 81 ? 8.949   -21.438 4.644   1.00 22.01 ? 80  GLY   A C    1 
ATOM   652  O  O    . GLY   A 1 81 ? 9.274   -20.281 4.359   1.00 21.26 ? 80  GLY   A O    1 
ATOM   653  N  N    . LEU   A 1 82 ? 8.528   -21.772 5.864   1.00 20.44 ? 81  LEU   A N    1 
ATOM   654  C  CA   . LEU   A 1 82 ? 8.536   -20.766 6.919   1.00 22.03 ? 81  LEU   A CA   1 
ATOM   655  C  C    . LEU   A 1 82 ? 9.956   -20.292 7.203   1.00 22.31 ? 81  LEU   A C    1 
ATOM   656  O  O    . LEU   A 1 82 ? 10.190  -19.099 7.429   1.00 20.67 ? 81  LEU   A O    1 
ATOM   657  C  CB   . LEU   A 1 82 ? 7.883   -21.321 8.185   1.00 25.83 ? 81  LEU   A CB   1 
ATOM   658  C  CG   . LEU   A 1 82 ? 6.366   -21.521 8.166   1.00 26.34 ? 81  LEU   A CG   1 
ATOM   659  C  CD1  . LEU   A 1 82 ? 5.901   -22.070 9.508   1.00 29.01 ? 81  LEU   A CD1  1 
ATOM   660  C  CD2  . LEU   A 1 82 ? 5.648   -20.216 7.852   1.00 28.68 ? 81  LEU   A CD2  1 
ATOM   661  N  N    . TRP   A 1 83 ? 10.926  -21.211 7.172   1.00 23.48 ? 82  TRP   A N    1 
ATOM   662  C  CA   . TRP   A 1 83 ? 12.309  -20.807 7.407   1.00 23.09 ? 82  TRP   A CA   1 
ATOM   663  C  C    . TRP   A 1 83 ? 12.808  -19.916 6.281   1.00 22.23 ? 82  TRP   A C    1 
ATOM   664  O  O    . TRP   A 1 83 ? 13.484  -18.912 6.528   1.00 21.27 ? 82  TRP   A O    1 
ATOM   665  C  CB   . TRP   A 1 83 ? 13.218  -22.029 7.553   1.00 22.67 ? 82  TRP   A CB   1 
ATOM   666  C  CG   . TRP   A 1 83 ? 14.667  -21.655 7.781   1.00 22.23 ? 82  TRP   A CG   1 
ATOM   667  C  CD1  . TRP   A 1 83 ? 15.297  -21.520 8.984   1.00 24.45 ? 82  TRP   A CD1  1 
ATOM   668  C  CD2  . TRP   A 1 83 ? 15.650  -21.361 6.780   1.00 23.95 ? 82  TRP   A CD2  1 
ATOM   669  N  NE1  . TRP   A 1 83 ? 16.605  -21.166 8.796   1.00 25.24 ? 82  TRP   A NE1  1 
ATOM   670  C  CE2  . TRP   A 1 83 ? 16.848  -21.057 7.452   1.00 26.48 ? 82  TRP   A CE2  1 
ATOM   671  C  CE3  . TRP   A 1 83 ? 15.630  -21.318 5.381   1.00 24.75 ? 82  TRP   A CE3  1 
ATOM   672  C  CZ2  . TRP   A 1 83 ? 18.020  -20.722 6.775   1.00 27.87 ? 82  TRP   A CZ2  1 
ATOM   673  C  CZ3  . TRP   A 1 83 ? 16.796  -20.988 4.708   1.00 26.26 ? 82  TRP   A CZ3  1 
ATOM   674  C  CH2  . TRP   A 1 83 ? 17.975  -20.692 5.407   1.00 26.43 ? 82  TRP   A CH2  1 
ATOM   675  N  N    . GLU   A 1 84 ? 12.468  -20.262 5.040   1.00 23.26 ? 83  GLU   A N    1 
ATOM   676  C  CA   . GLU   A 1 84 ? 12.979  -19.513 3.899   1.00 19.23 ? 83  GLU   A CA   1 
ATOM   677  C  C    . GLU   A 1 84 ? 12.462  -18.084 3.910   1.00 21.43 ? 83  GLU   A C    1 
ATOM   678  O  O    . GLU   A 1 84 ? 13.232  -17.133 3.734   1.00 22.29 ? 83  GLU   A O    1 
ATOM   679  C  CB   . GLU   A 1 84 ? 12.601  -20.219 2.598   1.00 18.63 ? 83  GLU   A CB   1 
ATOM   680  C  CG   . GLU   A 1 84 ? 13.228  -21.608 2.472   1.00 23.60 ? 83  GLU   A CG   1 
ATOM   681  C  CD   . GLU   A 1 84 ? 12.812  -22.334 1.204   1.00 29.34 ? 83  GLU   A CD   1 
ATOM   682  O  OE1  . GLU   A 1 84 ? 11.927  -21.821 0.491   1.00 27.60 ? 83  GLU   A OE1  1 
ATOM   683  O  OE2  . GLU   A 1 84 ? 13.367  -23.418 0.918   1.00 28.52 ? 83  GLU   A OE2  1 
ATOM   684  N  N    . ILE   A 1 85 ? 11.160  -17.907 4.143   1.00 20.12 ? 84  ILE   A N    1 
ATOM   685  C  CA   . ILE   A 1 85 ? 10.591  -16.569 4.049   1.00 17.62 ? 84  ILE   A CA   1 
ATOM   686  C  C    . ILE   A 1 85 ? 11.118  -15.682 5.165   1.00 21.11 ? 84  ILE   A C    1 
ATOM   687  O  O    . ILE   A 1 85 ? 11.225  -14.460 4.996   1.00 23.21 ? 84  ILE   A O    1 
ATOM   688  C  CB   . ILE   A 1 85 ? 9.053   -16.632 4.053   1.00 19.04 ? 84  ILE   A CB   1 
ATOM   689  C  CG1  . ILE   A 1 85 ? 8.463   -15.290 3.614   1.00 18.95 ? 84  ILE   A CG1  1 
ATOM   690  C  CG2  . ILE   A 1 85 ? 8.527   -17.026 5.431   1.00 18.29 ? 84  ILE   A CG2  1 
ATOM   691  C  CD1  . ILE   A 1 85 ? 7.041   -15.406 3.061   1.00 22.46 ? 84  ILE   A CD1  1 
ATOM   692  N  N    . GLN   A 1 86 ? 11.486  -16.274 6.306   1.00 21.06 ? 85  GLN   A N    1 
ATOM   693  C  CA   . GLN   A 1 86 ? 11.994  -15.491 7.425   1.00 21.97 ? 85  GLN   A CA   1 
ATOM   694  C  C    . GLN   A 1 86 ? 13.495  -15.244 7.322   1.00 25.81 ? 85  GLN   A C    1 
ATOM   695  O  O    . GLN   A 1 86 ? 13.973  -14.188 7.753   1.00 26.74 ? 85  GLN   A O    1 
ATOM   696  C  CB   . GLN   A 1 86 ? 11.661  -16.203 8.742   1.00 21.95 ? 85  GLN   A CB   1 
ATOM   697  C  CG   . GLN   A 1 86 ? 12.099  -15.458 9.994   1.00 31.41 ? 85  GLN   A CG   1 
ATOM   698  C  CD   . GLN   A 1 86 ? 11.484  -16.041 11.259  1.00 41.26 ? 85  GLN   A CD   1 
ATOM   699  O  OE1  . GLN   A 1 86 ? 11.214  -17.242 11.338  1.00 42.44 ? 85  GLN   A OE1  1 
ATOM   700  N  NE2  . GLN   A 1 86 ? 11.251  -15.188 12.249  1.00 49.10 ? 85  GLN   A NE2  1 
ATOM   701  N  N    . ASN   A 1 87 ? 14.251  -16.185 6.747   1.00 23.15 ? 86  ASN   A N    1 
ATOM   702  C  CA   . ASN   A 1 87 ? 15.704  -16.138 6.834   1.00 20.97 ? 86  ASN   A CA   1 
ATOM   703  C  C    . ASN   A 1 87 ? 16.431  -15.907 5.516   1.00 22.81 ? 86  ASN   A C    1 
ATOM   704  O  O    . ASN   A 1 87 ? 17.553  -15.392 5.545   1.00 26.84 ? 86  ASN   A O    1 
ATOM   705  C  CB   . ASN   A 1 87 ? 16.224  -17.425 7.487   1.00 24.40 ? 86  ASN   A CB   1 
ATOM   706  C  CG   . ASN   A 1 87 ? 15.768  -17.548 8.919   1.00 27.33 ? 86  ASN   A CG   1 
ATOM   707  O  OD1  . ASN   A 1 87 ? 16.225  -16.808 9.786   1.00 32.50 ? 86  ASN   A OD1  1 
ATOM   708  N  ND2  . ASN   A 1 87 ? 14.833  -18.456 9.171   1.00 30.11 ? 86  ASN   A ND2  1 
ATOM   709  N  N    . ASN   A 1 88 ? 15.842  -16.258 4.368   1.00 19.45 ? 87  ASN   A N    1 
ATOM   710  C  CA   . ASN   A 1 88 ? 16.473  -15.880 3.104   1.00 21.07 ? 87  ASN   A CA   1 
ATOM   711  C  C    . ASN   A 1 88 ? 15.430  -15.782 1.996   1.00 20.23 ? 87  ASN   A C    1 
ATOM   712  O  O    . ASN   A 1 88 ? 15.460  -16.561 1.032   1.00 23.09 ? 87  ASN   A O    1 
ATOM   713  C  CB   . ASN   A 1 88 ? 17.575  -16.866 2.714   1.00 27.85 ? 87  ASN   A CB   1 
ATOM   714  C  CG   . ASN   A 1 88 ? 18.668  -16.210 1.893   1.00 28.28 ? 87  ASN   A CG   1 
ATOM   715  O  OD1  . ASN   A 1 88 ? 18.447  -15.174 1.267   1.00 23.72 ? 87  ASN   A OD1  1 
ATOM   716  N  ND2  . ASN   A 1 88 ? 19.859  -16.803 1.900   1.00 29.32 ? 87  ASN   A ND2  1 
ATOM   717  N  N    . PRO   A 1 89 ? 14.501  -14.829 2.091   1.00 20.71 ? 88  PRO   A N    1 
ATOM   718  C  CA   . PRO   A 1 89 ? 13.356  -14.836 1.172   1.00 21.20 ? 88  PRO   A CA   1 
ATOM   719  C  C    . PRO   A 1 89 ? 13.703  -14.442 -0.250  1.00 22.86 ? 88  PRO   A C    1 
ATOM   720  O  O    . PRO   A 1 89 ? 12.907  -14.715 -1.155  1.00 21.71 ? 88  PRO   A O    1 
ATOM   721  C  CB   . PRO   A 1 89 ? 12.390  -13.831 1.813   1.00 20.67 ? 88  PRO   A CB   1 
ATOM   722  C  CG   . PRO   A 1 89 ? 13.289  -12.879 2.553   1.00 22.28 ? 88  PRO   A CG   1 
ATOM   723  C  CD   . PRO   A 1 89 ? 14.405  -13.745 3.087   1.00 19.04 ? 88  PRO   A CD   1 
ATOM   724  N  N    . HIS   A 1 90 ? 14.852  -13.813 -0.490  1.00 20.76 ? 89  HIS   A N    1 
ATOM   725  C  CA   . HIS   A 1 90 ? 15.180  -13.303 -1.816  1.00 17.68 ? 89  HIS   A CA   1 
ATOM   726  C  C    . HIS   A 1 90 ? 16.254  -14.130 -2.503  1.00 21.75 ? 89  HIS   A C    1 
ATOM   727  O  O    . HIS   A 1 90 ? 16.764  -13.726 -3.551  1.00 22.03 ? 89  HIS   A O    1 
ATOM   728  C  CB   . HIS   A 1 90 ? 15.603  -11.834 -1.715  1.00 20.89 ? 89  HIS   A CB   1 
ATOM   729  C  CG   . HIS   A 1 90 ? 14.552  -10.958 -1.109  1.00 20.95 ? 89  HIS   A CG   1 
ATOM   730  N  ND1  . HIS   A 1 90 ? 13.314  -10.773 -1.690  1.00 21.63 ? 89  HIS   A ND1  1 
ATOM   731  C  CD2  . HIS   A 1 90 ? 14.540  -10.239 0.039   1.00 19.24 ? 89  HIS   A CD2  1 
ATOM   732  C  CE1  . HIS   A 1 90 ? 12.592  -9.966  -0.932  1.00 23.34 ? 89  HIS   A CE1  1 
ATOM   733  N  NE2  . HIS   A 1 90 ? 13.310  -9.632  0.125   1.00 21.40 ? 89  HIS   A NE2  1 
ATOM   734  N  N    . ALA   A 1 91 ? 16.586  -15.292 -1.956  1.00 22.99 ? 90  ALA   A N    1 
ATOM   735  C  CA   . ALA   A 1 91 ? 17.653  -16.094 -2.520  1.00 21.00 ? 90  ALA   A CA   1 
ATOM   736  C  C    . ALA   A 1 91 ? 17.150  -16.877 -3.729  1.00 28.56 ? 90  ALA   A C    1 
ATOM   737  O  O    . ALA   A 1 91 ? 15.949  -17.005 -3.969  1.00 26.39 ? 90  ALA   A O    1 
ATOM   738  C  CB   . ALA   A 1 91 ? 18.219  -17.041 -1.466  1.00 25.41 ? 90  ALA   A CB   1 
ATOM   739  N  N    . SER   A 1 92 ? 18.097  -17.399 -4.502  1.00 27.43 ? 91  SER   A N    1 
ATOM   740  C  CA   . SER   A 1 92 ? 17.794  -18.282 -5.621  1.00 28.27 ? 91  SER   A CA   1 
ATOM   741  C  C    . SER   A 1 92 ? 17.649  -19.708 -5.103  1.00 33.30 ? 91  SER   A C    1 
ATOM   742  O  O    . SER   A 1 92 ? 18.598  -20.272 -4.549  1.00 40.30 ? 91  SER   A O    1 
ATOM   743  C  CB   . SER   A 1 92 ? 18.893  -18.198 -6.677  1.00 39.14 ? 91  SER   A CB   1 
ATOM   744  O  OG   . SER   A 1 92 ? 18.981  -19.409 -7.405  1.00 48.16 ? 91  SER   A OG   1 
ATOM   745  N  N    . TYR   A 1 93 ? 16.463  -20.288 -5.273  1.00 30.69 ? 92  TYR   A N    1 
ATOM   746  C  CA   . TYR   A 1 93 ? 16.178  -21.625 -4.769  1.00 29.21 ? 92  TYR   A CA   1 
ATOM   747  C  C    . TYR   A 1 93 ? 16.149  -22.677 -5.869  1.00 41.10 ? 92  TYR   A C    1 
ATOM   748  O  O    . TYR   A 1 93 ? 15.672  -23.792 -5.635  1.00 43.90 ? 92  TYR   A O    1 
ATOM   749  C  CB   . TYR   A 1 93 ? 14.859  -21.626 -3.991  1.00 37.15 ? 92  TYR   A CB   1 
ATOM   750  C  CG   . TYR   A 1 93 ? 14.994  -20.986 -2.631  1.00 31.73 ? 92  TYR   A CG   1 
ATOM   751  C  CD1  . TYR   A 1 93 ? 15.420  -21.724 -1.537  1.00 33.13 ? 92  TYR   A CD1  1 
ATOM   752  C  CD2  . TYR   A 1 93 ? 14.725  -19.637 -2.448  1.00 33.12 ? 92  TYR   A CD2  1 
ATOM   753  C  CE1  . TYR   A 1 93 ? 15.562  -21.143 -0.299  1.00 34.33 ? 92  TYR   A CE1  1 
ATOM   754  C  CE2  . TYR   A 1 93 ? 14.863  -19.045 -1.212  1.00 28.84 ? 92  TYR   A CE2  1 
ATOM   755  C  CZ   . TYR   A 1 93 ? 15.281  -19.802 -0.142  1.00 32.10 ? 92  TYR   A CZ   1 
ATOM   756  O  OH   . TYR   A 1 93 ? 15.425  -19.220 1.091   1.00 31.13 ? 92  TYR   A OH   1 
ATOM   757  N  N    . SER   A 1 94 ? 16.661  -22.355 -7.049  1.00 50.53 ? 93  SER   A N    1 
ATOM   758  C  CA   . SER   A 1 94 ? 16.708  -23.303 -8.154  1.00 57.65 ? 93  SER   A CA   1 
ATOM   759  C  C    . SER   A 1 94 ? 17.620  -24.485 -7.831  1.00 60.88 ? 93  SER   A C    1 
ATOM   760  O  O    . SER   A 1 94 ? 18.579  -24.355 -7.068  1.00 67.74 ? 93  SER   A O    1 
ATOM   761  C  CB   . SER   A 1 94 ? 17.183  -22.608 -9.431  1.00 56.76 ? 93  SER   A CB   1 
ATOM   762  O  OG   . SER   A 1 94 ? 16.447  -21.420 -9.665  1.00 58.49 ? 93  SER   A OG   1 
ATOM   763  N  N    . MET   B 1 2  ? 38.377  -10.554 -41.728 1.00 56.67 ? 1   MET   B N    1 
ATOM   764  C  CA   . MET   B 1 2  ? 38.140  -11.560 -42.759 1.00 55.51 ? 1   MET   B CA   1 
ATOM   765  C  C    . MET   B 1 2  ? 36.660  -11.931 -42.808 1.00 48.94 ? 1   MET   B C    1 
ATOM   766  O  O    . MET   B 1 2  ? 36.077  -12.305 -41.790 1.00 59.05 ? 1   MET   B O    1 
ATOM   767  C  CB   . MET   B 1 2  ? 38.999  -12.804 -42.502 1.00 50.63 ? 1   MET   B CB   1 
ATOM   768  C  CG   . MET   B 1 2  ? 39.021  -13.827 -43.636 1.00 54.85 ? 1   MET   B CG   1 
ATOM   769  S  SD   . MET   B 1 2  ? 40.072  -13.390 -45.047 1.00 60.34 ? 1   MET   B SD   1 
ATOM   770  C  CE   . MET   B 1 2  ? 41.264  -12.300 -44.270 1.00 60.32 ? 1   MET   B CE   1 
ATOM   771  N  N    . PRO   B 1 3  ? 36.051  -11.813 -43.986 1.00 42.26 ? 2   PRO   B N    1 
ATOM   772  C  CA   . PRO   B 1 3  ? 34.615  -12.096 -44.101 1.00 42.92 ? 2   PRO   B CA   1 
ATOM   773  C  C    . PRO   B 1 3  ? 34.313  -13.560 -43.830 1.00 42.36 ? 2   PRO   B C    1 
ATOM   774  O  O    . PRO   B 1 3  ? 35.042  -14.456 -44.260 1.00 43.82 ? 2   PRO   B O    1 
ATOM   775  C  CB   . PRO   B 1 3  ? 34.290  -11.721 -45.553 1.00 41.30 ? 2   PRO   B CB   1 
ATOM   776  C  CG   . PRO   B 1 3  ? 35.417  -10.840 -45.988 1.00 47.70 ? 2   PRO   B CG   1 
ATOM   777  C  CD   . PRO   B 1 3  ? 36.622  -11.332 -45.253 1.00 40.44 ? 2   PRO   B CD   1 
ATOM   778  N  N    . HIS   B 1 4  ? 33.224  -13.792 -43.111 1.00 38.32 ? 3   HIS   B N    1 
ATOM   779  C  CA   . HIS   B 1 4  ? 32.754  -15.130 -42.792 1.00 42.48 ? 3   HIS   B CA   1 
ATOM   780  C  C    . HIS   B 1 4  ? 31.365  -15.327 -43.390 1.00 42.17 ? 3   HIS   B C    1 
ATOM   781  O  O    . HIS   B 1 4  ? 30.824  -14.445 -44.064 1.00 41.91 ? 3   HIS   B O    1 
ATOM   782  C  CB   . HIS   B 1 4  ? 32.746  -15.356 -41.278 1.00 42.04 ? 3   HIS   B CB   1 
ATOM   783  C  CG   . HIS   B 1 4  ? 34.071  -15.114 -40.626 1.00 50.68 ? 3   HIS   B CG   1 
ATOM   784  N  ND1  . HIS   B 1 4  ? 35.130  -15.989 -40.746 1.00 54.68 ? 3   HIS   B ND1  1 
ATOM   785  C  CD2  . HIS   B 1 4  ? 34.511  -14.095 -39.850 1.00 51.99 ? 3   HIS   B CD2  1 
ATOM   786  C  CE1  . HIS   B 1 4  ? 36.164  -15.519 -40.072 1.00 58.00 ? 3   HIS   B CE1  1 
ATOM   787  N  NE2  . HIS   B 1 4  ? 35.815  -14.372 -39.518 1.00 56.87 ? 3   HIS   B NE2  1 
ATOM   788  N  N    . ALA   B 1 5  ? 30.792  -16.508 -43.145 1.00 41.73 ? 4   ALA   B N    1 
ATOM   789  C  CA   . ALA   B 1 5  ? 29.441  -16.781 -43.624 1.00 42.16 ? 4   ALA   B CA   1 
ATOM   790  C  C    . ALA   B 1 5  ? 28.455  -15.758 -43.080 1.00 38.01 ? 4   ALA   B C    1 
ATOM   791  O  O    . ALA   B 1 5  ? 27.608  -15.243 -43.820 1.00 39.26 ? 4   ALA   B O    1 
ATOM   792  C  CB   . ALA   B 1 5  ? 29.017  -18.194 -43.227 1.00 34.30 ? 4   ALA   B CB   1 
ATOM   793  N  N    . PHE   B 1 6  ? 28.552  -15.454 -41.790 1.00 39.67 ? 5   PHE   B N    1 
ATOM   794  C  CA   . PHE   B 1 6  ? 27.749  -14.419 -41.155 1.00 39.11 ? 5   PHE   B CA   1 
ATOM   795  C  C    . PHE   B 1 6  ? 28.595  -13.167 -40.964 1.00 35.34 ? 5   PHE   B C    1 
ATOM   796  O  O    . PHE   B 1 6  ? 29.717  -13.241 -40.455 1.00 42.18 ? 5   PHE   B O    1 
ATOM   797  C  CB   . PHE   B 1 6  ? 27.206  -14.895 -39.808 1.00 35.44 ? 5   PHE   B CB   1 
ATOM   798  C  CG   . PHE   B 1 6  ? 26.216  -16.017 -39.918 1.00 31.29 ? 5   PHE   B CG   1 
ATOM   799  C  CD1  . PHE   B 1 6  ? 26.641  -17.332 -39.922 1.00 36.53 ? 5   PHE   B CD1  1 
ATOM   800  C  CD2  . PHE   B 1 6  ? 24.859  -15.756 -40.027 1.00 32.70 ? 5   PHE   B CD2  1 
ATOM   801  C  CE1  . PHE   B 1 6  ? 25.731  -18.368 -40.031 1.00 34.21 ? 5   PHE   B CE1  1 
ATOM   802  C  CE2  . PHE   B 1 6  ? 23.945  -16.789 -40.132 1.00 31.96 ? 5   PHE   B CE2  1 
ATOM   803  C  CZ   . PHE   B 1 6  ? 24.382  -18.097 -40.133 1.00 31.11 ? 5   PHE   B CZ   1 
ATOM   804  N  N    . LYS   B 1 7  ? 28.055  -12.027 -41.371 1.00 36.15 ? 6   LYS   B N    1 
ATOM   805  C  CA   . LYS   B 1 7  ? 28.766  -10.776 -41.181 1.00 36.17 ? 6   LYS   B CA   1 
ATOM   806  C  C    . LYS   B 1 7  ? 28.052  -9.906  -40.150 1.00 37.74 ? 6   LYS   B C    1 
ATOM   807  O  O    . LYS   B 1 7  ? 26.836  -10.023 -39.968 1.00 33.00 ? 6   LYS   B O    1 
ATOM   808  C  CB   . LYS   B 1 7  ? 28.892  -10.003 -42.500 1.00 37.98 ? 6   LYS   B CB   1 
ATOM   809  C  CG   . LYS   B 1 7  ? 27.582  -9.781  -43.231 1.00 41.69 ? 6   LYS   B CG   1 
ATOM   810  C  CD   . LYS   B 1 7  ? 27.826  -9.222  -44.629 1.00 41.95 ? 6   LYS   B CD   1 
ATOM   811  C  CE   . LYS   B 1 7  ? 26.531  -9.140  -45.421 1.00 41.34 ? 6   LYS   B CE   1 
ATOM   812  N  NZ   . LYS   B 1 7  ? 25.816  -10.448 -45.435 1.00 50.57 ? 6   LYS   B NZ   1 
ATOM   813  N  N    . PRO   B 1 8  ? 28.782  -9.035  -39.454 1.00 39.50 ? 7   PRO   B N    1 
ATOM   814  C  CA   . PRO   B 1 8  ? 28.141  -8.139  -38.485 1.00 31.38 ? 7   PRO   B CA   1 
ATOM   815  C  C    . PRO   B 1 8  ? 26.977  -7.389  -39.110 1.00 35.43 ? 7   PRO   B C    1 
ATOM   816  O  O    . PRO   B 1 8  ? 27.098  -6.798  -40.188 1.00 38.39 ? 7   PRO   B O    1 
ATOM   817  C  CB   . PRO   B 1 8  ? 29.275  -7.193  -38.082 1.00 39.19 ? 7   PRO   B CB   1 
ATOM   818  C  CG   . PRO   B 1 8  ? 30.504  -8.001  -38.266 1.00 42.59 ? 7   PRO   B CG   1 
ATOM   819  C  CD   . PRO   B 1 8  ? 30.248  -8.885  -39.455 1.00 42.12 ? 7   PRO   B CD   1 
ATOM   820  N  N    . GLY   B 1 9  ? 25.830  -7.437  -38.436 1.00 27.88 ? 8   GLY   B N    1 
ATOM   821  C  CA   . GLY   B 1 9  ? 24.613  -6.844  -38.929 1.00 28.42 ? 8   GLY   B CA   1 
ATOM   822  C  C    . GLY   B 1 9  ? 23.643  -7.824  -39.555 1.00 28.06 ? 8   GLY   B C    1 
ATOM   823  O  O    . GLY   B 1 9  ? 22.478  -7.467  -39.769 1.00 32.78 ? 8   GLY   B O    1 
ATOM   824  N  N    . ASP   B 1 10 ? 24.095  -9.039  -39.871 1.00 27.56 ? 9   ASP   B N    1 
ATOM   825  C  CA   . ASP   B 1 10 ? 23.181  -10.059 -40.364 1.00 31.70 ? 9   ASP   B CA   1 
ATOM   826  C  C    . ASP   B 1 10 ? 22.089  -10.318 -39.337 1.00 25.22 ? 9   ASP   B C    1 
ATOM   827  O  O    . ASP   B 1 10 ? 22.350  -10.383 -38.136 1.00 25.57 ? 9   ASP   B O    1 
ATOM   828  C  CB   . ASP   B 1 10 ? 23.925  -11.362 -40.664 1.00 30.21 ? 9   ASP   B CB   1 
ATOM   829  C  CG   . ASP   B 1 10 ? 24.620  -11.346 -42.012 1.00 41.76 ? 9   ASP   B CG   1 
ATOM   830  O  OD1  . ASP   B 1 10 ? 25.598  -12.105 -42.182 1.00 40.81 ? 9   ASP   B OD1  1 
ATOM   831  O  OD2  . ASP   B 1 10 ? 24.192  -10.581 -42.900 1.00 41.12 ? 9   ASP   B OD2  1 
ATOM   832  N  N    . LEU   B 1 11 ? 20.859  -10.441 -39.816 1.00 25.73 ? 10  LEU   B N    1 
ATOM   833  C  CA   . LEU   B 1 11 ? 19.711  -10.711 -38.965 1.00 24.48 ? 10  LEU   B CA   1 
ATOM   834  C  C    . LEU   B 1 11 ? 19.400  -12.199 -39.001 1.00 23.69 ? 10  LEU   B C    1 
ATOM   835  O  O    . LEU   B 1 11 ? 19.403  -12.817 -40.069 1.00 27.99 ? 10  LEU   B O    1 
ATOM   836  C  CB   . LEU   B 1 11 ? 18.497  -9.906  -39.418 1.00 23.43 ? 10  LEU   B CB   1 
ATOM   837  C  CG   . LEU   B 1 11 ? 18.768  -8.398  -39.489 1.00 24.12 ? 10  LEU   B CG   1 
ATOM   838  C  CD1  . LEU   B 1 11 ? 17.492  -7.639  -39.799 1.00 30.19 ? 10  LEU   B CD1  1 
ATOM   839  C  CD2  . LEU   B 1 11 ? 19.396  -7.918  -38.185 1.00 27.05 ? 10  LEU   B CD2  1 
ATOM   840  N  N    . VAL   B 1 12 ? 19.144  -12.775 -37.828 1.00 23.61 ? 11  VAL   B N    1 
ATOM   841  C  CA   . VAL   B 1 12 ? 18.976  -14.217 -37.682 1.00 20.74 ? 11  VAL   B CA   1 
ATOM   842  C  C    . VAL   B 1 12 ? 17.921  -14.498 -36.623 1.00 29.30 ? 11  VAL   B C    1 
ATOM   843  O  O    . VAL   B 1 12 ? 17.520  -13.620 -35.857 1.00 23.60 ? 11  VAL   B O    1 
ATOM   844  C  CB   . VAL   B 1 12 ? 20.284  -14.930 -37.274 1.00 19.15 ? 11  VAL   B CB   1 
ATOM   845  C  CG1  . VAL   B 1 12 ? 21.386  -14.688 -38.294 1.00 23.91 ? 11  VAL   B CG1  1 
ATOM   846  C  CG2  . VAL   B 1 12 ? 20.717  -14.509 -35.855 1.00 22.80 ? 11  VAL   B CG2  1 
ATOM   847  N  N    . PHE   B 1 13 ? 17.471  -15.746 -36.583 1.00 26.44 ? 12  PHE   B N    1 
ATOM   848  C  CA   . PHE   B 1 13 ? 16.935  -16.325 -35.364 1.00 25.73 ? 12  PHE   B CA   1 
ATOM   849  C  C    . PHE   B 1 13 ? 18.020  -17.200 -34.763 1.00 27.35 ? 12  PHE   B C    1 
ATOM   850  O  O    . PHE   B 1 13 ? 18.685  -17.955 -35.480 1.00 26.38 ? 12  PHE   B O    1 
ATOM   851  C  CB   . PHE   B 1 13 ? 15.669  -17.139 -35.631 1.00 26.02 ? 12  PHE   B CB   1 
ATOM   852  C  CG   . PHE   B 1 13 ? 14.472  -16.299 -35.961 1.00 26.44 ? 12  PHE   B CG   1 
ATOM   853  C  CD1  . PHE   B 1 13 ? 13.622  -15.861 -34.968 1.00 25.07 ? 12  PHE   B CD1  1 
ATOM   854  C  CD2  . PHE   B 1 13 ? 14.194  -15.952 -37.269 1.00 31.84 ? 12  PHE   B CD2  1 
ATOM   855  C  CE1  . PHE   B 1 13 ? 12.515  -15.088 -35.275 1.00 29.27 ? 12  PHE   B CE1  1 
ATOM   856  C  CE2  . PHE   B 1 13 ? 13.091  -15.185 -37.579 1.00 34.89 ? 12  PHE   B CE2  1 
ATOM   857  C  CZ   . PHE   B 1 13 ? 12.252  -14.752 -36.582 1.00 32.72 ? 12  PHE   B CZ   1 
ATOM   858  N  N    . ALA   B 1 14 ? 18.217  -17.075 -33.453 1.00 23.99 ? 13  ALA   B N    1 
ATOM   859  C  CA   . ALA   B 1 14 ? 19.256  -17.794 -32.733 1.00 24.31 ? 13  ALA   B CA   1 
ATOM   860  C  C    . ALA   B 1 14 ? 18.606  -18.737 -31.734 1.00 24.75 ? 13  ALA   B C    1 
ATOM   861  O  O    . ALA   B 1 14 ? 17.711  -18.330 -30.985 1.00 23.07 ? 13  ALA   B O    1 
ATOM   862  C  CB   . ALA   B 1 14 ? 20.195  -16.828 -32.009 1.00 23.60 ? 13  ALA   B CB   1 
ATOM   863  N  N    . LYS   B 1 15 ? 19.064  -19.982 -31.716 1.00 25.10 ? 14  LYS   B N    1 
ATOM   864  C  CA   . LYS   B 1 15 ? 18.463  -21.019 -30.891 1.00 24.62 ? 14  LYS   B CA   1 
ATOM   865  C  C    . LYS   B 1 15 ? 19.325  -21.281 -29.666 1.00 29.76 ? 14  LYS   B C    1 
ATOM   866  O  O    . LYS   B 1 15 ? 20.527  -21.540 -29.786 1.00 31.24 ? 14  LYS   B O    1 
ATOM   867  C  CB   . LYS   B 1 15 ? 18.280  -22.314 -31.684 1.00 29.85 ? 14  LYS   B CB   1 
ATOM   868  C  CG   . LYS   B 1 15 ? 17.529  -23.404 -30.903 1.00 26.67 ? 14  LYS   B CG   1 
ATOM   869  C  CD   . LYS   B 1 15 ? 16.044  -23.058 -30.763 1.00 33.80 ? 14  LYS   B CD   1 
ATOM   870  C  CE   . LYS   B 1 15 ? 15.259  -24.172 -30.072 1.00 28.39 ? 14  LYS   B CE   1 
ATOM   871  N  NZ   . LYS   B 1 15 ? 15.695  -24.333 -28.660 1.00 27.12 ? 14  LYS   B NZ   1 
ATOM   872  N  N    . MET   B 1 16 ? 18.705  -21.206 -28.494 1.00 32.16 ? 15  MET   B N    1 
ATOM   873  C  CA   . MET   B 1 16 ? 19.308  -21.609 -27.234 1.00 33.90 ? 15  MET   B CA   1 
ATOM   874  C  C    . MET   B 1 16 ? 18.436  -22.697 -26.626 1.00 28.99 ? 15  MET   B C    1 
ATOM   875  O  O    . MET   B 1 16 ? 17.206  -22.619 -26.692 1.00 32.83 ? 15  MET   B O    1 
ATOM   876  C  CB   . MET   B 1 16 ? 19.425  -20.423 -26.271 1.00 34.63 ? 15  MET   B CB   1 
ATOM   877  C  CG   . MET   B 1 16 ? 20.189  -19.241 -26.836 1.00 39.01 ? 15  MET   B CG   1 
ATOM   878  S  SD   . MET   B 1 16 ? 21.958  -19.375 -26.549 1.00 55.29 ? 15  MET   B SD   1 
ATOM   879  C  CE   . MET   B 1 16 ? 22.127  -18.403 -25.064 1.00 40.17 ? 15  MET   B CE   1 
ATOM   880  N  N    . LYS   B 1 17 ? 19.068  -23.720 -26.056 1.00 33.48 ? 16  LYS   B N    1 
ATOM   881  C  CA   . LYS   B 1 17 ? 18.303  -24.806 -25.456 1.00 34.87 ? 16  LYS   B CA   1 
ATOM   882  C  C    . LYS   B 1 17 ? 17.352  -24.253 -24.401 1.00 33.38 ? 16  LYS   B C    1 
ATOM   883  O  O    . LYS   B 1 17 ? 17.736  -23.419 -23.577 1.00 33.26 ? 16  LYS   B O    1 
ATOM   884  C  CB   . LYS   B 1 17 ? 19.235  -25.846 -24.840 1.00 42.34 ? 16  LYS   B CB   1 
ATOM   885  C  CG   . LYS   B 1 17 ? 18.500  -27.069 -24.311 1.00 45.22 ? 16  LYS   B CG   1 
ATOM   886  C  CD   . LYS   B 1 17 ? 19.434  -28.015 -23.573 1.00 52.70 ? 16  LYS   B CD   1 
ATOM   887  C  CE   . LYS   B 1 17 ? 18.654  -29.101 -22.842 1.00 54.96 ? 16  LYS   B CE   1 
ATOM   888  N  NZ   . LYS   B 1 17 ? 18.697  -28.924 -21.362 1.00 64.10 ? 16  LYS   B NZ   1 
ATOM   889  N  N    . GLY   B 1 18 ? 16.098  -24.697 -24.451 1.00 36.27 ? 17  GLY   B N    1 
ATOM   890  C  CA   . GLY   B 1 18 ? 15.078  -24.206 -23.549 1.00 34.37 ? 17  GLY   B CA   1 
ATOM   891  C  C    . GLY   B 1 18 ? 14.405  -22.916 -23.969 1.00 37.79 ? 17  GLY   B C    1 
ATOM   892  O  O    . GLY   B 1 18 ? 13.569  -22.402 -23.217 1.00 32.07 ? 17  GLY   B O    1 
ATOM   893  N  N    . TYR   B 1 19 ? 14.740  -22.371 -25.136 1.00 33.29 ? 18  TYR   B N    1 
ATOM   894  C  CA   . TYR   B 1 19 ? 14.141  -21.142 -25.627 1.00 26.01 ? 18  TYR   B CA   1 
ATOM   895  C  C    . TYR   B 1 19 ? 13.763  -21.310 -27.088 1.00 27.72 ? 18  TYR   B C    1 
ATOM   896  O  O    . TYR   B 1 19 ? 14.446  -22.019 -27.831 1.00 31.20 ? 18  TYR   B O    1 
ATOM   897  C  CB   . TYR   B 1 19 ? 15.103  -19.952 -25.490 1.00 27.08 ? 18  TYR   B CB   1 
ATOM   898  C  CG   . TYR   B 1 19 ? 15.535  -19.709 -24.068 1.00 28.27 ? 18  TYR   B CG   1 
ATOM   899  C  CD1  . TYR   B 1 19 ? 16.603  -20.406 -23.519 1.00 33.53 ? 18  TYR   B CD1  1 
ATOM   900  C  CD2  . TYR   B 1 19 ? 14.865  -18.797 -23.269 1.00 31.61 ? 18  TYR   B CD2  1 
ATOM   901  C  CE1  . TYR   B 1 19 ? 16.990  -20.201 -22.209 1.00 44.22 ? 18  TYR   B CE1  1 
ATOM   902  C  CE2  . TYR   B 1 19 ? 15.248  -18.579 -21.960 1.00 35.17 ? 18  TYR   B CE2  1 
ATOM   903  C  CZ   . TYR   B 1 19 ? 16.312  -19.281 -21.436 1.00 40.26 ? 18  TYR   B CZ   1 
ATOM   904  O  OH   . TYR   B 1 19 ? 16.699  -19.071 -20.134 1.00 44.43 ? 18  TYR   B OH   1 
ATOM   905  N  N    . PRO   B 1 20 ? 12.688  -20.665 -27.528 1.00 26.79 ? 19  PRO   B N    1 
ATOM   906  C  CA   . PRO   B 1 20 ? 12.361  -20.679 -28.955 1.00 24.32 ? 19  PRO   B CA   1 
ATOM   907  C  C    . PRO   B 1 20 ? 13.437  -19.961 -29.749 1.00 27.22 ? 19  PRO   B C    1 
ATOM   908  O  O    . PRO   B 1 20 ? 14.223  -19.178 -29.211 1.00 26.05 ? 19  PRO   B O    1 
ATOM   909  C  CB   . PRO   B 1 20 ? 11.026  -19.936 -29.024 1.00 25.56 ? 19  PRO   B CB   1 
ATOM   910  C  CG   . PRO   B 1 20 ? 11.015  -19.070 -27.789 1.00 27.31 ? 19  PRO   B CG   1 
ATOM   911  C  CD   . PRO   B 1 20 ? 11.730  -19.873 -26.743 1.00 25.01 ? 19  PRO   B CD   1 
ATOM   912  N  N    . HIS   B 1 21 ? 13.486  -20.266 -31.046 1.00 24.46 ? 20  HIS   B N    1 
ATOM   913  C  CA   . HIS   B 1 21 ? 14.341  -19.512 -31.952 1.00 24.99 ? 20  HIS   B CA   1 
ATOM   914  C  C    . HIS   B 1 21 ? 14.062  -18.027 -31.784 1.00 21.50 ? 20  HIS   B C    1 
ATOM   915  O  O    . HIS   B 1 21 ? 12.913  -17.587 -31.861 1.00 23.17 ? 20  HIS   B O    1 
ATOM   916  C  CB   . HIS   B 1 21 ? 14.093  -19.945 -33.398 1.00 23.68 ? 20  HIS   B CB   1 
ATOM   917  C  CG   . HIS   B 1 21 ? 14.268  -21.416 -33.626 1.00 26.85 ? 20  HIS   B CG   1 
ATOM   918  N  ND1  . HIS   B 1 21 ? 13.358  -22.353 -33.183 1.00 26.84 ? 20  HIS   B ND1  1 
ATOM   919  C  CD2  . HIS   B 1 21 ? 15.250  -22.111 -34.247 1.00 30.07 ? 20  HIS   B CD2  1 
ATOM   920  C  CE1  . HIS   B 1 21 ? 13.771  -23.561 -33.524 1.00 29.21 ? 20  HIS   B CE1  1 
ATOM   921  N  NE2  . HIS   B 1 21 ? 14.916  -23.442 -34.172 1.00 26.43 ? 20  HIS   B NE2  1 
ATOM   922  N  N    . TRP   B 1 22 ? 15.114  -17.259 -31.534 1.00 23.80 ? 21  TRP   B N    1 
ATOM   923  C  CA   . TRP   B 1 22 ? 14.948  -15.922 -30.991 1.00 16.83 ? 21  TRP   B CA   1 
ATOM   924  C  C    . TRP   B 1 22 ? 15.472  -14.873 -31.963 1.00 23.25 ? 21  TRP   B C    1 
ATOM   925  O  O    . TRP   B 1 22 ? 16.599  -15.011 -32.457 1.00 25.42 ? 21  TRP   B O    1 
ATOM   926  C  CB   . TRP   B 1 22 ? 15.684  -15.802 -29.647 1.00 23.39 ? 21  TRP   B CB   1 
ATOM   927  C  CG   . TRP   B 1 22 ? 15.156  -14.702 -28.805 1.00 28.53 ? 21  TRP   B CG   1 
ATOM   928  C  CD1  . TRP   B 1 22 ? 15.436  -13.369 -28.921 1.00 28.85 ? 21  TRP   B CD1  1 
ATOM   929  C  CD2  . TRP   B 1 22 ? 14.242  -14.828 -27.709 1.00 27.04 ? 21  TRP   B CD2  1 
ATOM   930  N  NE1  . TRP   B 1 22 ? 14.748  -12.658 -27.963 1.00 23.43 ? 21  TRP   B NE1  1 
ATOM   931  C  CE2  . TRP   B 1 22 ? 14.012  -13.531 -27.205 1.00 27.63 ? 21  TRP   B CE2  1 
ATOM   932  C  CE3  . TRP   B 1 22 ? 13.597  -15.912 -27.104 1.00 29.12 ? 21  TRP   B CE3  1 
ATOM   933  C  CZ2  . TRP   B 1 22 ? 13.165  -13.291 -26.126 1.00 24.98 ? 21  TRP   B CZ2  1 
ATOM   934  C  CZ3  . TRP   B 1 22 ? 12.756  -15.670 -26.031 1.00 30.69 ? 21  TRP   B CZ3  1 
ATOM   935  C  CH2  . TRP   B 1 22 ? 12.545  -14.370 -25.558 1.00 26.68 ? 21  TRP   B CH2  1 
ATOM   936  N  N    . PRO   B 1 23 ? 14.703  -13.820 -32.256 1.00 22.93 ? 22  PRO   B N    1 
ATOM   937  C  CA   . PRO   B 1 23 ? 15.204  -12.772 -33.157 1.00 24.28 ? 22  PRO   B CA   1 
ATOM   938  C  C    . PRO   B 1 23 ? 16.490  -12.180 -32.607 1.00 22.77 ? 22  PRO   B C    1 
ATOM   939  O  O    . PRO   B 1 23 ? 16.593  -11.864 -31.421 1.00 22.39 ? 22  PRO   B O    1 
ATOM   940  C  CB   . PRO   B 1 23 ? 14.062  -11.748 -33.186 1.00 26.14 ? 22  PRO   B CB   1 
ATOM   941  C  CG   . PRO   B 1 23 ? 13.305  -11.988 -31.889 1.00 25.00 ? 22  PRO   B CG   1 
ATOM   942  C  CD   . PRO   B 1 23 ? 13.387  -13.477 -31.689 1.00 23.10 ? 22  PRO   B CD   1 
ATOM   943  N  N    . ALA   B 1 24 ? 17.492  -12.071 -33.470 1.00 23.29 ? 23  ALA   B N    1 
ATOM   944  C  CA   . ALA   B 1 24 ? 18.821  -11.702 -33.011 1.00 22.76 ? 23  ALA   B CA   1 
ATOM   945  C  C    . ALA   B 1 24 ? 19.599  -11.132 -34.187 1.00 20.34 ? 23  ALA   B C    1 
ATOM   946  O  O    . ALA   B 1 24 ? 19.141  -11.155 -35.330 1.00 24.39 ? 23  ALA   B O    1 
ATOM   947  C  CB   . ALA   B 1 24 ? 19.544  -12.902 -32.390 1.00 24.03 ? 23  ALA   B CB   1 
ATOM   948  N  N    . ARG   B 1 25 ? 20.781  -10.606 -33.885 1.00 24.68 ? 24  ARG   B N    1 
ATOM   949  C  CA   . ARG   B 1 25 ? 21.668  -10.089 -34.912 1.00 22.39 ? 24  ARG   B CA   1 
ATOM   950  C  C    . ARG   B 1 25 ? 23.087  -10.538 -34.614 1.00 27.04 ? 24  ARG   B C    1 
ATOM   951  O  O    . ARG   B 1 25 ? 23.443  -10.806 -33.462 1.00 25.39 ? 24  ARG   B O    1 
ATOM   952  C  CB   . ARG   B 1 25 ? 21.607  -8.559  -34.999 1.00 25.56 ? 24  ARG   B CB   1 
ATOM   953  C  CG   . ARG   B 1 25 ? 22.294  -7.861  -33.843 1.00 25.53 ? 24  ARG   B CG   1 
ATOM   954  C  CD   . ARG   B 1 25 ? 22.043  -6.358  -33.890 1.00 24.05 ? 24  ARG   B CD   1 
ATOM   955  N  NE   . ARG   B 1 25 ? 22.681  -5.672  -32.775 1.00 29.33 ? 24  ARG   B NE   1 
ATOM   956  C  CZ   . ARG   B 1 25 ? 22.374  -4.446  -32.373 1.00 26.15 ? 24  ARG   B CZ   1 
ATOM   957  N  NH1  . ARG   B 1 25 ? 21.404  -3.754  -32.946 1.00 28.60 ? 24  ARG   B NH1  1 
ATOM   958  N  NH2  . ARG   B 1 25 ? 23.053  -3.905  -31.366 1.00 31.49 ? 24  ARG   B NH2  1 
ATOM   959  N  N    . ILE   B 1 26 ? 23.888  -10.644 -35.670 1.00 24.51 ? 25  ILE   B N    1 
ATOM   960  C  CA   . ILE   B 1 26 ? 25.324  -10.843 -35.526 1.00 25.32 ? 25  ILE   B CA   1 
ATOM   961  C  C    . ILE   B 1 26 ? 25.932  -9.509  -35.120 1.00 30.03 ? 25  ILE   B C    1 
ATOM   962  O  O    . ILE   B 1 26 ? 25.773  -8.509  -35.826 1.00 29.69 ? 25  ILE   B O    1 
ATOM   963  C  CB   . ILE   B 1 26 ? 25.949  -11.356 -36.831 1.00 28.43 ? 25  ILE   B CB   1 
ATOM   964  C  CG1  . ILE   B 1 26 ? 25.229  -12.615 -37.308 1.00 30.07 ? 25  ILE   B CG1  1 
ATOM   965  C  CG2  . ILE   B 1 26 ? 27.432  -11.617 -36.632 1.00 30.97 ? 25  ILE   B CG2  1 
ATOM   966  C  CD1  . ILE   B 1 26 ? 25.313  -13.744 -36.333 1.00 26.91 ? 25  ILE   B CD1  1 
ATOM   967  N  N    . ASP   B 1 27 ? 26.620  -9.490  -33.983 1.00 28.79 ? 26  ASP   B N    1 
ATOM   968  C  CA   . ASP   B 1 27 ? 27.190  -8.260  -33.462 1.00 37.12 ? 26  ASP   B CA   1 
ATOM   969  C  C    . ASP   B 1 27 ? 28.606  -8.068  -33.994 1.00 42.47 ? 26  ASP   B C    1 
ATOM   970  O  O    . ASP   B 1 27 ? 29.169  -8.927  -34.676 1.00 36.77 ? 26  ASP   B O    1 
ATOM   971  C  CB   . ASP   B 1 27 ? 27.184  -8.270  -31.934 1.00 38.15 ? 26  ASP   B CB   1 
ATOM   972  C  CG   . ASP   B 1 27 ? 26.082  -7.409  -31.348 1.00 39.12 ? 26  ASP   B CG   1 
ATOM   973  O  OD1  . ASP   B 1 27 ? 25.275  -6.860  -32.129 1.00 33.97 ? 26  ASP   B OD1  1 
ATOM   974  O  OD2  . ASP   B 1 27 ? 26.024  -7.282  -30.107 1.00 37.14 ? 26  ASP   B OD2  1 
ATOM   975  N  N    . ASP   B 1 28 ? 29.187  -6.918  -33.674 1.00 53.21 ? 27  ASP   B N    1 
ATOM   976  C  CA   . ASP   B 1 28 ? 30.574  -6.627  -33.994 1.00 48.40 ? 27  ASP   B CA   1 
ATOM   977  C  C    . ASP   B 1 28 ? 31.485  -7.037  -32.847 1.00 59.40 ? 27  ASP   B C    1 
ATOM   978  O  O    . ASP   B 1 28 ? 31.080  -7.060  -31.680 1.00 56.67 ? 27  ASP   B O    1 
ATOM   979  C  CB   . ASP   B 1 28 ? 30.759  -5.139  -34.286 1.00 57.85 ? 27  ASP   B CB   1 
ATOM   980  C  CG   . ASP   B 1 28 ? 30.683  -4.825  -35.758 1.00 60.21 ? 27  ASP   B CG   1 
ATOM   981  O  OD1  . ASP   B 1 28 ? 31.516  -5.364  -36.520 1.00 60.70 ? 27  ASP   B OD1  1 
ATOM   982  O  OD2  . ASP   B 1 28 ? 29.785  -4.050  -36.149 1.00 60.65 ? 27  ASP   B OD2  1 
ATOM   983  N  N    . ILE   B 1 29 ? 32.726  -7.363  -33.194 1.00 58.40 ? 28  ILE   B N    1 
ATOM   984  C  CA   . ILE   B 1 29 ? 33.771  -7.606  -32.210 1.00 65.07 ? 28  ILE   B CA   1 
ATOM   985  C  C    . ILE   B 1 29 ? 34.477  -6.271  -31.998 1.00 81.92 ? 28  ILE   B C    1 
ATOM   986  O  O    . ILE   B 1 29 ? 35.368  -5.898  -32.763 1.00 83.56 ? 28  ILE   B O    1 
ATOM   987  C  CB   . ILE   B 1 29 ? 34.737  -8.703  -32.662 1.00 65.56 ? 28  ILE   B CB   1 
ATOM   988  C  CG1  . ILE   B 1 29 ? 33.960  -9.967  -33.041 1.00 65.26 ? 28  ILE   B CG1  1 
ATOM   989  C  CG2  . ILE   B 1 29 ? 35.757  -9.002  -31.569 1.00 67.42 ? 28  ILE   B CG2  1 
ATOM   990  C  CD1  . ILE   B 1 29 ? 34.814  -11.030 -33.692 1.00 69.65 ? 28  ILE   B CD1  1 
ATOM   991  N  N    . ALA   B 1 30 ? 34.056  -5.538  -30.969 1.00 79.40 ? 29  ALA   B N    1 
ATOM   992  C  CA   . ALA   B 1 30 ? 34.641  -4.233  -30.688 1.00 77.18 ? 29  ALA   B CA   1 
ATOM   993  C  C    . ALA   B 1 30 ? 36.138  -4.367  -30.446 1.00 81.24 ? 29  ALA   B C    1 
ATOM   994  O  O    . ALA   B 1 30 ? 36.578  -5.216  -29.666 1.00 89.79 ? 29  ALA   B O    1 
ATOM   995  C  CB   . ALA   B 1 30 ? 33.961  -3.597  -29.478 1.00 71.50 ? 29  ALA   B CB   1 
ATOM   996  N  N    . ASP   B 1 31 ? 36.919  -3.528  -31.131 1.00 86.97 ? 30  ASP   B N    1 
ATOM   997  C  CA   . ASP   B 1 31 ? 38.376  -3.594  -31.078 1.00 84.43 ? 30  ASP   B CA   1 
ATOM   998  C  C    . ASP   B 1 31 ? 38.890  -3.496  -29.647 1.00 79.22 ? 30  ASP   B C    1 
ATOM   999  O  O    . ASP   B 1 31 ? 38.889  -2.415  -29.048 1.00 77.60 ? 30  ASP   B O    1 
ATOM   1000 C  CB   . ASP   B 1 31 ? 38.990  -2.491  -31.943 1.00 81.00 ? 30  ASP   B CB   1 
ATOM   1001 C  CG   . ASP   B 1 31 ? 38.967  -2.831  -33.421 1.00 85.27 ? 30  ASP   B CG   1 
ATOM   1002 O  OD1  . ASP   B 1 31 ? 39.299  -3.984  -33.771 1.00 84.49 ? 30  ASP   B OD1  1 
ATOM   1003 O  OD2  . ASP   B 1 31 ? 38.612  -1.949  -34.232 1.00 80.98 ? 30  ASP   B OD2  1 
ATOM   1004 N  N    . GLY   B 1 32 ? 39.333  -4.624  -29.097 1.00 80.92 ? 31  GLY   B N    1 
ATOM   1005 C  CA   . GLY   B 1 32 ? 39.800  -4.677  -27.726 1.00 73.49 ? 31  GLY   B CA   1 
ATOM   1006 C  C    . GLY   B 1 32 ? 38.771  -5.259  -26.781 1.00 79.51 ? 31  GLY   B C    1 
ATOM   1007 O  O    . GLY   B 1 32 ? 38.510  -4.696  -25.713 1.00 85.59 ? 31  GLY   B O    1 
ATOM   1008 N  N    . ALA   B 1 33 ? 38.176  -6.390  -27.162 1.00 84.48 ? 32  ALA   B N    1 
ATOM   1009 C  CA   . ALA   B 1 33 ? 37.144  -7.035  -26.365 1.00 76.04 ? 32  ALA   B CA   1 
ATOM   1010 C  C    . ALA   B 1 33 ? 37.318  -8.546  -26.441 1.00 81.00 ? 32  ALA   B C    1 
ATOM   1011 O  O    . ALA   B 1 33 ? 38.108  -9.065  -27.234 1.00 70.06 ? 32  ALA   B O    1 
ATOM   1012 C  CB   . ALA   B 1 33 ? 35.739  -6.629  -26.830 1.00 71.39 ? 32  ALA   B CB   1 
ATOM   1013 N  N    . VAL   B 1 34 ? 36.562  -9.253  -25.600 1.00 79.59 ? 33  VAL   B N    1 
ATOM   1014 C  CA   . VAL   B 1 34 ? 36.611  -10.710 -25.535 1.00 71.04 ? 33  VAL   B CA   1 
ATOM   1015 C  C    . VAL   B 1 34 ? 36.139  -11.294 -26.859 1.00 77.32 ? 33  VAL   B C    1 
ATOM   1016 O  O    . VAL   B 1 34 ? 34.946  -11.247 -27.182 1.00 81.14 ? 33  VAL   B O    1 
ATOM   1017 C  CB   . VAL   B 1 34 ? 35.766  -11.248 -24.367 1.00 64.98 ? 33  VAL   B CB   1 
ATOM   1018 C  CG1  . VAL   B 1 34 ? 35.745  -12.767 -24.382 1.00 73.24 ? 33  VAL   B CG1  1 
ATOM   1019 C  CG2  . VAL   B 1 34 ? 36.302  -10.732 -23.041 1.00 73.97 ? 33  VAL   B CG2  1 
ATOM   1020 N  N    . LYS   B 1 35 ? 37.070  -11.845 -27.633 1.00 74.44 ? 34  LYS   B N    1 
ATOM   1021 C  CA   . LYS   B 1 35 ? 36.716  -12.436 -28.911 1.00 68.56 ? 34  LYS   B CA   1 
ATOM   1022 C  C    . LYS   B 1 35 ? 35.933  -13.733 -28.700 1.00 58.23 ? 34  LYS   B C    1 
ATOM   1023 O  O    . LYS   B 1 35 ? 36.089  -14.401 -27.676 1.00 56.95 ? 34  LYS   B O    1 
ATOM   1024 C  CB   . LYS   B 1 35 ? 37.970  -12.700 -29.742 1.00 61.13 ? 34  LYS   B CB   1 
ATOM   1025 C  CG   . LYS   B 1 35 ? 38.621  -11.434 -30.284 1.00 74.34 ? 34  LYS   B CG   1 
ATOM   1026 C  CD   . LYS   B 1 35 ? 39.740  -11.757 -31.261 1.00 73.69 ? 34  LYS   B CD   1 
ATOM   1027 C  CE   . LYS   B 1 35 ? 40.906  -12.445 -30.568 1.00 73.07 ? 34  LYS   B CE   1 
ATOM   1028 N  NZ   . LYS   B 1 35 ? 41.555  -11.560 -29.559 1.00 58.87 ? 34  LYS   B NZ   1 
ATOM   1029 N  N    . PRO   B 1 36 ? 35.071  -14.103 -29.653 1.00 53.18 ? 35  PRO   B N    1 
ATOM   1030 C  CA   . PRO   B 1 36 ? 34.282  -15.320 -29.481 1.00 50.14 ? 35  PRO   B CA   1 
ATOM   1031 C  C    . PRO   B 1 36 ? 35.165  -16.554 -29.525 1.00 44.39 ? 35  PRO   B C    1 
ATOM   1032 O  O    . PRO   B 1 36 ? 36.268  -16.527 -30.096 1.00 51.12 ? 35  PRO   B O    1 
ATOM   1033 C  CB   . PRO   B 1 36 ? 33.310  -15.281 -30.677 1.00 48.85 ? 35  PRO   B CB   1 
ATOM   1034 C  CG   . PRO   B 1 36 ? 33.984  -14.417 -31.684 1.00 56.88 ? 35  PRO   B CG   1 
ATOM   1035 C  CD   . PRO   B 1 36 ? 34.716  -13.383 -30.885 1.00 54.40 ? 35  PRO   B CD   1 
ATOM   1036 N  N    . PRO   B 1 37 ? 34.718  -17.659 -28.936 1.00 46.65 ? 36  PRO   B N    1 
ATOM   1037 C  CA   . PRO   B 1 37 ? 35.432  -18.929 -29.091 1.00 48.83 ? 36  PRO   B CA   1 
ATOM   1038 C  C    . PRO   B 1 37 ? 35.476  -19.333 -30.552 1.00 49.79 ? 36  PRO   B C    1 
ATOM   1039 O  O    . PRO   B 1 37 ? 34.736  -18.772 -31.374 1.00 48.81 ? 36  PRO   B O    1 
ATOM   1040 C  CB   . PRO   B 1 37 ? 34.588  -19.913 -28.262 1.00 48.00 ? 36  PRO   B CB   1 
ATOM   1041 C  CG   . PRO   B 1 37 ? 33.812  -19.055 -27.320 1.00 48.49 ? 36  PRO   B CG   1 
ATOM   1042 C  CD   . PRO   B 1 37 ? 33.544  -17.785 -28.059 1.00 47.46 ? 36  PRO   B CD   1 
ATOM   1043 N  N    . PRO   B 1 38 ? 36.332  -20.285 -30.922 1.00 55.22 ? 37  PRO   B N    1 
ATOM   1044 C  CA   . PRO   B 1 38 ? 36.394  -20.710 -32.326 1.00 53.83 ? 37  PRO   B CA   1 
ATOM   1045 C  C    . PRO   B 1 38 ? 35.028  -21.145 -32.843 1.00 50.05 ? 37  PRO   B C    1 
ATOM   1046 O  O    . PRO   B 1 38 ? 34.204  -21.687 -32.102 1.00 47.73 ? 37  PRO   B O    1 
ATOM   1047 C  CB   . PRO   B 1 38 ? 37.384  -21.879 -32.299 1.00 54.05 ? 37  PRO   B CB   1 
ATOM   1048 C  CG   . PRO   B 1 38 ? 38.235  -21.621 -31.101 1.00 46.33 ? 37  PRO   B CG   1 
ATOM   1049 C  CD   . PRO   B 1 38 ? 37.329  -20.984 -30.089 1.00 48.90 ? 37  PRO   B CD   1 
ATOM   1050 N  N    . ASN   B 1 39 ? 34.792  -20.878 -34.128 1.00 44.29 ? 38  ASN   B N    1 
ATOM   1051 C  CA   . ASN   B 1 39 ? 33.589  -21.229 -34.880 1.00 44.15 ? 38  ASN   B CA   1 
ATOM   1052 C  C    . ASN   B 1 39 ? 32.348  -20.451 -34.454 1.00 40.09 ? 38  ASN   B C    1 
ATOM   1053 O  O    . ASN   B 1 39 ? 31.276  -20.683 -35.022 1.00 39.05 ? 38  ASN   B O    1 
ATOM   1054 C  CB   . ASN   B 1 39 ? 33.256  -22.727 -34.796 1.00 42.94 ? 38  ASN   B CB   1 
ATOM   1055 C  CG   . ASN   B 1 39 ? 34.485  -23.606 -34.886 1.00 59.67 ? 38  ASN   B CG   1 
ATOM   1056 O  OD1  . ASN   B 1 39 ? 35.360  -23.385 -35.720 1.00 52.79 ? 38  ASN   B OD1  1 
ATOM   1057 N  ND2  . ASN   B 1 39 ? 34.561  -24.608 -34.016 1.00 57.59 ? 38  ASN   B ND2  1 
ATOM   1058 N  N    . LYS   B 1 40 ? 32.443  -19.538 -33.490 1.00 40.35 ? 39  LYS   B N    1 
ATOM   1059 C  CA   . LYS   B 1 40 ? 31.262  -18.911 -32.919 1.00 33.62 ? 39  LYS   B CA   1 
ATOM   1060 C  C    . LYS   B 1 40 ? 31.250  -17.413 -33.195 1.00 38.74 ? 39  LYS   B C    1 
ATOM   1061 O  O    . LYS   B 1 40 ? 32.282  -16.797 -33.475 1.00 39.81 ? 39  LYS   B O    1 
ATOM   1062 C  CB   . LYS   B 1 40 ? 31.177  -19.177 -31.410 1.00 37.64 ? 39  LYS   B CB   1 
ATOM   1063 C  CG   . LYS   B 1 40 ? 31.294  -20.655 -31.074 1.00 37.93 ? 39  LYS   B CG   1 
ATOM   1064 C  CD   . LYS   B 1 40 ? 30.521  -21.033 -29.824 1.00 39.47 ? 39  LYS   B CD   1 
ATOM   1065 C  CE   . LYS   B 1 40 ? 30.401  -22.548 -29.706 1.00 45.17 ? 39  LYS   B CE   1 
ATOM   1066 N  NZ   . LYS   B 1 40 ? 29.650  -22.966 -28.486 1.00 56.02 ? 39  LYS   B NZ   1 
ATOM   1067 N  N    . TYR   B 1 41 ? 30.052  -16.835 -33.115 1.00 29.91 ? 40  TYR   B N    1 
ATOM   1068 C  CA   . TYR   B 1 41 ? 29.783  -15.438 -33.415 1.00 30.96 ? 40  TYR   B CA   1 
ATOM   1069 C  C    . TYR   B 1 41 ? 29.214  -14.737 -32.191 1.00 36.58 ? 40  TYR   B C    1 
ATOM   1070 O  O    . TYR   B 1 41 ? 28.533  -15.366 -31.378 1.00 32.55 ? 40  TYR   B O    1 
ATOM   1071 C  CB   . TYR   B 1 41 ? 28.779  -15.293 -34.564 1.00 32.72 ? 40  TYR   B CB   1 
ATOM   1072 C  CG   . TYR   B 1 41 ? 29.280  -15.775 -35.901 1.00 32.28 ? 40  TYR   B CG   1 
ATOM   1073 C  CD1  . TYR   B 1 41 ? 29.982  -14.928 -36.745 1.00 33.87 ? 40  TYR   B CD1  1 
ATOM   1074 C  CD2  . TYR   B 1 41 ? 29.042  -17.075 -36.323 1.00 27.17 ? 40  TYR   B CD2  1 
ATOM   1075 C  CE1  . TYR   B 1 41 ? 30.444  -15.364 -37.979 1.00 38.47 ? 40  TYR   B CE1  1 
ATOM   1076 C  CE2  . TYR   B 1 41 ? 29.499  -17.522 -37.554 1.00 31.68 ? 40  TYR   B CE2  1 
ATOM   1077 C  CZ   . TYR   B 1 41 ? 30.199  -16.662 -38.378 1.00 36.69 ? 40  TYR   B CZ   1 
ATOM   1078 O  OH   . TYR   B 1 41 ? 30.654  -17.098 -39.604 1.00 39.08 ? 40  TYR   B OH   1 
ATOM   1079 N  N    . PRO   B 1 42 ? 29.449  -13.431 -32.046 1.00 34.93 ? 41  PRO   B N    1 
ATOM   1080 C  CA   . PRO   B 1 42 ? 28.757  -12.671 -30.994 1.00 26.94 ? 41  PRO   B CA   1 
ATOM   1081 C  C    . PRO   B 1 42 ? 27.321  -12.399 -31.415 1.00 31.03 ? 41  PRO   B C    1 
ATOM   1082 O  O    . PRO   B 1 42 ? 27.071  -11.809 -32.468 1.00 30.80 ? 41  PRO   B O    1 
ATOM   1083 C  CB   . PRO   B 1 42 ? 29.574  -11.376 -30.890 1.00 37.50 ? 41  PRO   B CB   1 
ATOM   1084 C  CG   . PRO   B 1 42 ? 30.372  -11.282 -32.164 1.00 32.91 ? 41  PRO   B CG   1 
ATOM   1085 C  CD   . PRO   B 1 42 ? 30.237  -12.563 -32.938 1.00 36.68 ? 41  PRO   B CD   1 
ATOM   1086 N  N    . ILE   B 1 43 ? 26.375  -12.843 -30.593 1.00 27.61 ? 42  ILE   B N    1 
ATOM   1087 C  CA   . ILE   B 1 43 ? 24.952  -12.706 -30.872 1.00 27.13 ? 42  ILE   B CA   1 
ATOM   1088 C  C    . ILE   B 1 43 ? 24.369  -11.665 -29.929 1.00 27.84 ? 42  ILE   B C    1 
ATOM   1089 O  O    . ILE   B 1 43 ? 24.713  -11.624 -28.745 1.00 31.82 ? 42  ILE   B O    1 
ATOM   1090 C  CB   . ILE   B 1 43 ? 24.217  -14.052 -30.714 1.00 25.23 ? 42  ILE   B CB   1 
ATOM   1091 C  CG1  . ILE   B 1 43 ? 24.920  -15.144 -31.519 1.00 27.43 ? 42  ILE   B CG1  1 
ATOM   1092 C  CG2  . ILE   B 1 43 ? 22.771  -13.921 -31.145 1.00 30.52 ? 42  ILE   B CG2  1 
ATOM   1093 C  CD1  . ILE   B 1 43 ? 25.053  -14.819 -32.971 1.00 26.94 ? 42  ILE   B CD1  1 
ATOM   1094 N  N    . PHE   B 1 44 ? 23.497  -10.814 -30.462 1.00 26.33 ? 43  PHE   B N    1 
ATOM   1095 C  CA   . PHE   B 1 44 ? 22.706  -9.885  -29.665 1.00 27.81 ? 43  PHE   B CA   1 
ATOM   1096 C  C    . PHE   B 1 44 ? 21.249  -10.278 -29.837 1.00 28.73 ? 43  PHE   B C    1 
ATOM   1097 O  O    . PHE   B 1 44 ? 20.732  -10.256 -30.958 1.00 23.49 ? 43  PHE   B O    1 
ATOM   1098 C  CB   . PHE   B 1 44 ? 22.944  -8.437  -30.103 1.00 26.69 ? 43  PHE   B CB   1 
ATOM   1099 C  CG   . PHE   B 1 44 ? 22.029  -7.433  -29.441 1.00 28.59 ? 43  PHE   B CG   1 
ATOM   1100 C  CD1  . PHE   B 1 44 ? 22.369  -6.863  -28.230 1.00 29.99 ? 43  PHE   B CD1  1 
ATOM   1101 C  CD2  . PHE   B 1 44 ? 20.841  -7.045  -30.048 1.00 29.24 ? 43  PHE   B CD2  1 
ATOM   1102 C  CE1  . PHE   B 1 44 ? 21.535  -5.928  -27.622 1.00 28.38 ? 43  PHE   B CE1  1 
ATOM   1103 C  CE2  . PHE   B 1 44 ? 20.005  -6.114  -29.448 1.00 32.02 ? 43  PHE   B CE2  1 
ATOM   1104 C  CZ   . PHE   B 1 44 ? 20.353  -5.556  -28.234 1.00 29.28 ? 43  PHE   B CZ   1 
ATOM   1105 N  N    . PHE   B 1 45 ? 20.600  -10.662 -28.740 1.00 26.80 ? 44  PHE   B N    1 
ATOM   1106 C  CA   . PHE   B 1 45 ? 19.199  -11.061 -28.765 1.00 25.21 ? 44  PHE   B CA   1 
ATOM   1107 C  C    . PHE   B 1 45 ? 18.327  -9.821  -28.641 1.00 22.53 ? 44  PHE   B C    1 
ATOM   1108 O  O    . PHE   B 1 45 ? 18.427  -9.087  -27.656 1.00 26.75 ? 44  PHE   B O    1 
ATOM   1109 C  CB   . PHE   B 1 45 ? 18.891  -12.041 -27.633 1.00 27.59 ? 44  PHE   B CB   1 
ATOM   1110 C  CG   . PHE   B 1 45 ? 19.617  -13.345 -27.752 1.00 22.44 ? 44  PHE   B CG   1 
ATOM   1111 C  CD1  . PHE   B 1 45 ? 19.062  -14.396 -28.457 1.00 26.84 ? 44  PHE   B CD1  1 
ATOM   1112 C  CD2  . PHE   B 1 45 ? 20.856  -13.520 -27.166 1.00 26.47 ? 44  PHE   B CD2  1 
ATOM   1113 C  CE1  . PHE   B 1 45 ? 19.729  -15.594 -28.575 1.00 29.16 ? 44  PHE   B CE1  1 
ATOM   1114 C  CE2  . PHE   B 1 45 ? 21.529  -14.720 -27.282 1.00 37.59 ? 44  PHE   B CE2  1 
ATOM   1115 C  CZ   . PHE   B 1 45 ? 20.963  -15.756 -27.989 1.00 31.16 ? 44  PHE   B CZ   1 
ATOM   1116 N  N    . PHE   B 1 46 ? 17.475  -9.589  -29.633 1.00 22.69 ? 45  PHE   B N    1 
ATOM   1117 C  CA   . PHE   B 1 46 ? 16.552  -8.472  -29.543 1.00 24.30 ? 45  PHE   B CA   1 
ATOM   1118 C  C    . PHE   B 1 46 ? 15.563  -8.696  -28.401 1.00 29.77 ? 45  PHE   B C    1 
ATOM   1119 O  O    . PHE   B 1 46 ? 15.326  -9.824  -27.960 1.00 27.94 ? 45  PHE   B O    1 
ATOM   1120 C  CB   . PHE   B 1 46 ? 15.810  -8.285  -30.860 1.00 21.16 ? 45  PHE   B CB   1 
ATOM   1121 C  CG   . PHE   B 1 46 ? 16.688  -7.820  -31.984 1.00 25.81 ? 45  PHE   B CG   1 
ATOM   1122 C  CD1  . PHE   B 1 46 ? 17.168  -6.521  -32.008 1.00 23.47 ? 45  PHE   B CD1  1 
ATOM   1123 C  CD2  . PHE   B 1 46 ? 17.028  -8.677  -33.020 1.00 26.15 ? 45  PHE   B CD2  1 
ATOM   1124 C  CE1  . PHE   B 1 46 ? 17.977  -6.081  -33.049 1.00 30.82 ? 45  PHE   B CE1  1 
ATOM   1125 C  CE2  . PHE   B 1 46 ? 17.839  -8.244  -34.064 1.00 26.10 ? 45  PHE   B CE2  1 
ATOM   1126 C  CZ   . PHE   B 1 46 ? 18.311  -6.946  -34.080 1.00 24.66 ? 45  PHE   B CZ   1 
ATOM   1127 N  N    . GLY   B 1 47 ? 14.996  -7.597  -27.912 1.00 27.77 ? 46  GLY   B N    1 
ATOM   1128 C  CA   . GLY   B 1 47 ? 14.021  -7.674  -26.838 1.00 30.58 ? 46  GLY   B CA   1 
ATOM   1129 C  C    . GLY   B 1 47 ? 14.649  -7.776  -25.464 1.00 32.15 ? 46  GLY   B C    1 
ATOM   1130 O  O    . GLY   B 1 47 ? 14.504  -6.870  -24.636 1.00 32.53 ? 46  GLY   B O    1 
ATOM   1131 N  N    . THR   B 1 48 ? 15.342  -8.885  -25.201 1.00 27.62 ? 47  THR   B N    1 
ATOM   1132 C  CA   . THR   B 1 48 ? 16.063  -9.024  -23.942 1.00 31.29 ? 47  THR   B CA   1 
ATOM   1133 C  C    . THR   B 1 48 ? 17.354  -8.220  -23.938 1.00 32.93 ? 47  THR   B C    1 
ATOM   1134 O  O    . THR   B 1 48 ? 17.826  -7.825  -22.867 1.00 30.58 ? 47  THR   B O    1 
ATOM   1135 C  CB   . THR   B 1 48 ? 16.389  -10.493 -23.668 1.00 31.57 ? 47  THR   B CB   1 
ATOM   1136 O  OG1  . THR   B 1 48 ? 17.274  -10.975 -24.687 1.00 28.73 ? 47  THR   B OG1  1 
ATOM   1137 C  CG2  . THR   B 1 48 ? 15.121  -11.333 -23.653 1.00 24.74 ? 47  THR   B CG2  1 
ATOM   1138 N  N    . HIS   B 1 49 ? 17.939  -7.991  -25.116 1.00 30.92 ? 48  HIS   B N    1 
ATOM   1139 C  CA   . HIS   B 1 49 ? 19.220  -7.306  -25.279 1.00 33.84 ? 48  HIS   B CA   1 
ATOM   1140 C  C    . HIS   B 1 49 ? 20.360  -8.058  -24.608 1.00 32.32 ? 48  HIS   B C    1 
ATOM   1141 O  O    . HIS   B 1 49 ? 21.416  -7.482  -24.340 1.00 36.40 ? 48  HIS   B O    1 
ATOM   1142 C  CB   . HIS   B 1 49 ? 19.150  -5.862  -24.773 1.00 30.54 ? 48  HIS   B CB   1 
ATOM   1143 C  CG   . HIS   B 1 49 ? 17.944  -5.122  -25.257 1.00 35.93 ? 48  HIS   B CG   1 
ATOM   1144 N  ND1  . HIS   B 1 49 ? 17.292  -4.179  -24.494 1.00 34.12 ? 48  HIS   B ND1  1 
ATOM   1145 C  CD2  . HIS   B 1 49 ? 17.259  -5.203  -26.423 1.00 31.35 ? 48  HIS   B CD2  1 
ATOM   1146 C  CE1  . HIS   B 1 49 ? 16.259  -3.707  -25.169 1.00 36.87 ? 48  HIS   B CE1  1 
ATOM   1147 N  NE2  . HIS   B 1 49 ? 16.217  -4.312  -26.344 1.00 35.62 ? 48  HIS   B NE2  1 
ATOM   1148 N  N    . GLU   B 1 50 ? 20.167  -9.344  -24.338 1.00 28.96 ? 49  GLU   B N    1 
ATOM   1149 C  CA   . GLU   B 1 50 ? 21.256  -10.161 -23.840 1.00 29.04 ? 49  GLU   B CA   1 
ATOM   1150 C  C    . GLU   B 1 50 ? 22.161  -10.573 -24.996 1.00 36.03 ? 49  GLU   B C    1 
ATOM   1151 O  O    . GLU   B 1 50 ? 21.818  -10.429 -26.171 1.00 31.15 ? 49  GLU   B O    1 
ATOM   1152 C  CB   . GLU   B 1 50 ? 20.712  -11.383 -23.104 1.00 42.02 ? 49  GLU   B CB   1 
ATOM   1153 C  CG   . GLU   B 1 50 ? 20.049  -11.026 -21.784 1.00 40.11 ? 49  GLU   B CG   1 
ATOM   1154 C  CD   . GLU   B 1 50 ? 19.535  -12.231 -21.030 1.00 48.65 ? 49  GLU   B CD   1 
ATOM   1155 O  OE1  . GLU   B 1 50 ? 19.495  -13.331 -21.616 1.00 44.05 ? 49  GLU   B OE1  1 
ATOM   1156 O  OE2  . GLU   B 1 50 ? 19.166  -12.075 -19.846 1.00 48.46 ? 49  GLU   B OE2  1 
ATOM   1157 N  N    . THR   B 1 51 ? 23.336  -11.086 -24.653 1.00 29.26 ? 50  THR   B N    1 
ATOM   1158 C  CA   . THR   B 1 51 ? 24.312  -11.504 -25.644 1.00 30.08 ? 50  THR   B CA   1 
ATOM   1159 C  C    . THR   B 1 51 ? 24.800  -12.906 -25.317 1.00 37.33 ? 50  THR   B C    1 
ATOM   1160 O  O    . THR   B 1 51 ? 24.743  -13.357 -24.170 1.00 34.56 ? 50  THR   B O    1 
ATOM   1161 C  CB   . THR   B 1 51 ? 25.508  -10.542 -25.714 1.00 34.02 ? 50  THR   B CB   1 
ATOM   1162 O  OG1  . THR   B 1 51 ? 26.014  -10.313 -24.393 1.00 44.74 ? 50  THR   B OG1  1 
ATOM   1163 C  CG2  . THR   B 1 51 ? 25.097  -9.216  -26.344 1.00 29.73 ? 50  THR   B CG2  1 
ATOM   1164 N  N    . ALA   B 1 52 ? 25.280  -13.593 -26.348 1.00 33.49 ? 51  ALA   B N    1 
ATOM   1165 C  CA   . ALA   B 1 52 ? 25.871  -14.913 -26.190 1.00 30.90 ? 51  ALA   B CA   1 
ATOM   1166 C  C    . ALA   B 1 52 ? 26.760  -15.181 -27.395 1.00 33.23 ? 51  ALA   B C    1 
ATOM   1167 O  O    . ALA   B 1 52 ? 26.731  -14.450 -28.388 1.00 33.23 ? 51  ALA   B O    1 
ATOM   1168 C  CB   . ALA   B 1 52 ? 24.799  -16.000 -26.045 1.00 33.10 ? 51  ALA   B CB   1 
ATOM   1169 N  N    . PHE   B 1 53 ? 27.562  -16.232 -27.287 1.00 30.84 ? 52  PHE   B N    1 
ATOM   1170 C  CA   . PHE   B 1 53 ? 28.344  -16.731 -28.408 1.00 33.40 ? 52  PHE   B CA   1 
ATOM   1171 C  C    . PHE   B 1 53 ? 27.691  -18.004 -28.930 1.00 38.54 ? 52  PHE   B C    1 
ATOM   1172 O  O    . PHE   B 1 53 ? 27.473  -18.954 -28.170 1.00 33.60 ? 52  PHE   B O    1 
ATOM   1173 C  CB   . PHE   B 1 53 ? 29.793  -17.001 -28.000 1.00 40.34 ? 52  PHE   B CB   1 
ATOM   1174 C  CG   . PHE   B 1 53 ? 30.547  -15.768 -27.592 1.00 37.41 ? 52  PHE   B CG   1 
ATOM   1175 C  CD1  . PHE   B 1 53 ? 30.714  -14.721 -28.478 1.00 40.47 ? 52  PHE   B CD1  1 
ATOM   1176 C  CD2  . PHE   B 1 53 ? 31.099  -15.663 -26.326 1.00 44.84 ? 52  PHE   B CD2  1 
ATOM   1177 C  CE1  . PHE   B 1 53 ? 31.408  -13.588 -28.112 1.00 41.94 ? 52  PHE   B CE1  1 
ATOM   1178 C  CE2  . PHE   B 1 53 ? 31.797  -14.530 -25.953 1.00 46.15 ? 52  PHE   B CE2  1 
ATOM   1179 C  CZ   . PHE   B 1 53 ? 31.951  -13.492 -26.848 1.00 47.89 ? 52  PHE   B CZ   1 
ATOM   1180 N  N    . LEU   B 1 54 ? 27.377  -18.019 -30.223 1.00 33.01 ? 53  LEU   B N    1 
ATOM   1181 C  CA   . LEU   B 1 54 ? 26.705  -19.149 -30.842 1.00 31.55 ? 53  LEU   B CA   1 
ATOM   1182 C  C    . LEU   B 1 54 ? 27.394  -19.518 -32.147 1.00 29.57 ? 53  LEU   B C    1 
ATOM   1183 O  O    . LEU   B 1 54 ? 27.974  -18.666 -32.827 1.00 30.47 ? 53  LEU   B O    1 
ATOM   1184 C  CB   . LEU   B 1 54 ? 25.225  -18.847 -31.109 1.00 26.82 ? 53  LEU   B CB   1 
ATOM   1185 C  CG   . LEU   B 1 54 ? 24.299  -18.813 -29.894 1.00 28.69 ? 53  LEU   B CG   1 
ATOM   1186 C  CD1  . LEU   B 1 54 ? 22.869  -18.613 -30.353 1.00 32.08 ? 53  LEU   B CD1  1 
ATOM   1187 C  CD2  . LEU   B 1 54 ? 24.440  -20.096 -29.091 1.00 37.82 ? 53  LEU   B CD2  1 
ATOM   1188 N  N    . GLY   B 1 55 ? 27.321  -20.802 -32.487 1.00 30.79 ? 54  GLY   B N    1 
ATOM   1189 C  CA   . GLY   B 1 55 ? 27.847  -21.296 -33.737 1.00 28.86 ? 54  GLY   B CA   1 
ATOM   1190 C  C    . GLY   B 1 55 ? 26.772  -21.397 -34.798 1.00 30.51 ? 54  GLY   B C    1 
ATOM   1191 O  O    . GLY   B 1 55 ? 25.577  -21.270 -34.520 1.00 27.34 ? 54  GLY   B O    1 
ATOM   1192 N  N    . PRO   B 1 56 ? 27.182  -21.645 -36.045 1.00 28.12 ? 55  PRO   B N    1 
ATOM   1193 C  CA   . PRO   B 1 56 ? 26.218  -21.602 -37.155 1.00 28.03 ? 55  PRO   B CA   1 
ATOM   1194 C  C    . PRO   B 1 56 ? 25.065  -22.583 -37.025 1.00 21.58 ? 55  PRO   B C    1 
ATOM   1195 O  O    . PRO   B 1 56 ? 23.982  -22.309 -37.555 1.00 26.45 ? 55  PRO   B O    1 
ATOM   1196 C  CB   . PRO   B 1 56 ? 27.088  -21.914 -38.381 1.00 31.91 ? 55  PRO   B CB   1 
ATOM   1197 C  CG   . PRO   B 1 56 ? 28.464  -21.523 -37.979 1.00 35.40 ? 55  PRO   B CG   1 
ATOM   1198 C  CD   . PRO   B 1 56 ? 28.565  -21.826 -36.517 1.00 33.36 ? 55  PRO   B CD   1 
ATOM   1199 N  N    . LYS   B 1 57 ? 25.246  -23.715 -36.338 1.00 25.90 ? 56  LYS   B N    1 
ATOM   1200 C  CA   . LYS   B 1 57 ? 24.160  -24.687 -36.270 1.00 30.35 ? 56  LYS   B CA   1 
ATOM   1201 C  C    . LYS   B 1 57 ? 22.943  -24.132 -35.543 1.00 30.93 ? 56  LYS   B C    1 
ATOM   1202 O  O    . LYS   B 1 57 ? 21.833  -24.638 -35.739 1.00 27.83 ? 56  LYS   B O    1 
ATOM   1203 C  CB   . LYS   B 1 57 ? 24.635  -25.987 -35.608 1.00 33.58 ? 56  LYS   B CB   1 
ATOM   1204 C  CG   . LYS   B 1 57 ? 24.867  -25.915 -34.110 1.00 31.86 ? 56  LYS   B CG   1 
ATOM   1205 C  CD   . LYS   B 1 57 ? 25.179  -27.307 -33.560 1.00 38.70 ? 56  LYS   B CD   1 
ATOM   1206 C  CE   . LYS   B 1 57 ? 25.437  -27.288 -32.062 1.00 45.54 ? 56  LYS   B CE   1 
ATOM   1207 N  NZ   . LYS   B 1 57 ? 24.242  -26.819 -31.303 1.00 44.28 ? 56  LYS   B NZ   1 
ATOM   1208 N  N    . ASP   B 1 58 ? 23.124  -23.083 -34.737 1.00 24.93 ? 57  ASP   B N    1 
ATOM   1209 C  CA   . ASP   B 1 58 ? 22.039  -22.450 -34.001 1.00 21.96 ? 57  ASP   B CA   1 
ATOM   1210 C  C    . ASP   B 1 58 ? 21.639  -21.104 -34.587 1.00 26.18 ? 57  ASP   B C    1 
ATOM   1211 O  O    . ASP   B 1 58 ? 20.879  -20.364 -33.951 1.00 25.57 ? 57  ASP   B O    1 
ATOM   1212 C  CB   . ASP   B 1 58 ? 22.430  -22.277 -32.531 1.00 29.10 ? 57  ASP   B CB   1 
ATOM   1213 C  CG   . ASP   B 1 58 ? 22.699  -23.600 -31.840 1.00 32.36 ? 57  ASP   B CG   1 
ATOM   1214 O  OD1  . ASP   B 1 58 ? 21.855  -24.515 -31.952 1.00 32.23 ? 57  ASP   B OD1  1 
ATOM   1215 O  OD2  . ASP   B 1 58 ? 23.758  -23.722 -31.189 1.00 32.71 ? 57  ASP   B OD2  1 
ATOM   1216 N  N    . LEU   B 1 59 ? 22.129  -20.766 -35.780 1.00 23.68 ? 58  LEU   B N    1 
ATOM   1217 C  CA   . LEU   B 1 59 ? 21.883  -19.469 -36.399 1.00 26.79 ? 58  LEU   B CA   1 
ATOM   1218 C  C    . LEU   B 1 59 ? 21.120  -19.685 -37.696 1.00 26.62 ? 58  LEU   B C    1 
ATOM   1219 O  O    . LEU   B 1 59 ? 21.583  -20.418 -38.579 1.00 27.98 ? 58  LEU   B O    1 
ATOM   1220 C  CB   . LEU   B 1 59 ? 23.199  -18.730 -36.647 1.00 27.68 ? 58  LEU   B CB   1 
ATOM   1221 C  CG   . LEU   B 1 59 ? 23.977  -18.443 -35.361 1.00 25.06 ? 58  LEU   B CG   1 
ATOM   1222 C  CD1  . LEU   B 1 59 ? 25.303  -17.765 -35.662 1.00 29.12 ? 58  LEU   B CD1  1 
ATOM   1223 C  CD2  . LEU   B 1 59 ? 23.131  -17.576 -34.430 1.00 32.29 ? 58  LEU   B CD2  1 
ATOM   1224 N  N    . PHE   B 1 60 ? 19.948  -19.063 -37.798 1.00 22.54 ? 59  PHE   B N    1 
ATOM   1225 C  CA   . PHE   B 1 60 ? 19.027  -19.243 -38.914 1.00 21.84 ? 59  PHE   B CA   1 
ATOM   1226 C  C    . PHE   B 1 60 ? 18.790  -17.899 -39.592 1.00 28.61 ? 59  PHE   B C    1 
ATOM   1227 O  O    . PHE   B 1 60 ? 18.261  -16.977 -38.947 1.00 25.27 ? 59  PHE   B O    1 
ATOM   1228 C  CB   . PHE   B 1 60 ? 17.700  -19.831 -38.419 1.00 25.12 ? 59  PHE   B CB   1 
ATOM   1229 C  CG   . PHE   B 1 60 ? 17.831  -21.194 -37.785 1.00 23.88 ? 59  PHE   B CG   1 
ATOM   1230 C  CD1  . PHE   B 1 60 ? 18.335  -21.335 -36.501 1.00 24.86 ? 59  PHE   B CD1  1 
ATOM   1231 C  CD2  . PHE   B 1 60 ? 17.429  -22.329 -38.469 1.00 33.20 ? 59  PHE   B CD2  1 
ATOM   1232 C  CE1  . PHE   B 1 60 ? 18.451  -22.589 -35.915 1.00 27.60 ? 59  PHE   B CE1  1 
ATOM   1233 C  CE2  . PHE   B 1 60 ? 17.538  -23.582 -37.891 1.00 30.68 ? 59  PHE   B CE2  1 
ATOM   1234 C  CZ   . PHE   B 1 60 ? 18.053  -23.713 -36.616 1.00 31.77 ? 59  PHE   B CZ   1 
ATOM   1235 N  N    . PRO   B 1 61 ? 19.147  -17.730 -40.865 1.00 28.03 ? 60  PRO   B N    1 
ATOM   1236 C  CA   . PRO   B 1 61 ? 18.965  -16.426 -41.522 1.00 28.02 ? 60  PRO   B CA   1 
ATOM   1237 C  C    . PRO   B 1 61 ? 17.527  -15.932 -41.429 1.00 27.60 ? 60  PRO   B C    1 
ATOM   1238 O  O    . PRO   B 1 61 ? 16.581  -16.662 -41.721 1.00 31.18 ? 60  PRO   B O    1 
ATOM   1239 C  CB   . PRO   B 1 61 ? 19.374  -16.706 -42.972 1.00 32.19 ? 60  PRO   B CB   1 
ATOM   1240 C  CG   . PRO   B 1 61 ? 20.321  -17.852 -42.882 1.00 37.84 ? 60  PRO   B CG   1 
ATOM   1241 C  CD   . PRO   B 1 61 ? 19.835  -18.703 -41.731 1.00 32.57 ? 60  PRO   B CD   1 
ATOM   1242 N  N    . TYR   B 1 62 ? 17.373  -14.663 -41.034 1.00 26.45 ? 61  TYR   B N    1 
ATOM   1243 C  CA   . TYR   B 1 62 ? 16.059  -14.136 -40.670 1.00 27.81 ? 61  TYR   B CA   1 
ATOM   1244 C  C    . TYR   B 1 62 ? 15.085  -14.169 -41.840 1.00 35.14 ? 61  TYR   B C    1 
ATOM   1245 O  O    . TYR   B 1 62 ? 13.944  -14.619 -41.694 1.00 34.81 ? 61  TYR   B O    1 
ATOM   1246 C  CB   . TYR   B 1 62 ? 16.197  -12.710 -40.139 1.00 30.90 ? 61  TYR   B CB   1 
ATOM   1247 C  CG   . TYR   B 1 62 ? 14.879  -11.996 -39.933 1.00 26.87 ? 61  TYR   B CG   1 
ATOM   1248 C  CD1  . TYR   B 1 62 ? 14.112  -12.223 -38.800 1.00 32.99 ? 61  TYR   B CD1  1 
ATOM   1249 C  CD2  . TYR   B 1 62 ? 14.407  -11.085 -40.872 1.00 39.63 ? 61  TYR   B CD2  1 
ATOM   1250 C  CE1  . TYR   B 1 62 ? 12.911  -11.570 -38.605 1.00 37.54 ? 61  TYR   B CE1  1 
ATOM   1251 C  CE2  . TYR   B 1 62 ? 13.208  -10.426 -40.689 1.00 37.32 ? 61  TYR   B CE2  1 
ATOM   1252 C  CZ   . TYR   B 1 62 ? 12.464  -10.670 -39.553 1.00 41.87 ? 61  TYR   B CZ   1 
ATOM   1253 O  OH   . TYR   B 1 62 ? 11.270  -10.011 -39.369 1.00 43.74 ? 61  TYR   B OH   1 
ATOM   1254 N  N    . ASP   B 1 63 ? 15.507  -13.673 -43.008 1.00 34.48 ? 62  ASP   B N    1 
ATOM   1255 C  CA   . ASP   B 1 63 ? 14.592  -13.596 -44.145 1.00 43.02 ? 62  ASP   B CA   1 
ATOM   1256 C  C    . ASP   B 1 63 ? 14.076  -14.973 -44.541 1.00 34.86 ? 62  ASP   B C    1 
ATOM   1257 O  O    . ASP   B 1 63 ? 12.897  -15.129 -44.876 1.00 43.54 ? 62  ASP   B O    1 
ATOM   1258 C  CB   . ASP   B 1 63 ? 15.273  -12.922 -45.337 1.00 41.57 ? 62  ASP   B CB   1 
ATOM   1259 C  CG   . ASP   B 1 63 ? 15.166  -11.411 -45.291 1.00 58.51 ? 62  ASP   B CG   1 
ATOM   1260 O  OD1  . ASP   B 1 63 ? 15.619  -10.752 -46.252 1.00 73.81 ? 62  ASP   B OD1  1 
ATOM   1261 O  OD2  . ASP   B 1 63 ? 14.639  -10.879 -44.290 1.00 56.79 ? 62  ASP   B OD2  1 
ATOM   1262 N  N    . LYS   B 1 64 ? 14.940  -15.988 -44.495 1.00 39.28 ? 63  LYS   B N    1 
ATOM   1263 C  CA   . LYS   B 1 64 ? 14.530  -17.324 -44.910 1.00 35.14 ? 63  LYS   B CA   1 
ATOM   1264 C  C    . LYS   B 1 64 ? 13.492  -17.916 -43.960 1.00 36.27 ? 63  LYS   B C    1 
ATOM   1265 O  O    . LYS   B 1 64 ? 12.538  -18.565 -44.404 1.00 34.96 ? 63  LYS   B O    1 
ATOM   1266 C  CB   . LYS   B 1 64 ? 15.754  -18.236 -45.008 1.00 40.99 ? 63  LYS   B CB   1 
ATOM   1267 C  CG   . LYS   B 1 64 ? 15.435  -19.695 -45.319 1.00 33.10 ? 63  LYS   B CG   1 
ATOM   1268 C  CD   . LYS   B 1 64 ? 16.709  -20.503 -45.550 1.00 36.32 ? 63  LYS   B CD   1 
ATOM   1269 C  CE   . LYS   B 1 64 ? 16.429  -22.003 -45.564 1.00 38.12 ? 63  LYS   B CE   1 
ATOM   1270 N  NZ   . LYS   B 1 64 ? 15.470  -22.401 -46.632 1.00 42.14 ? 63  LYS   B NZ   1 
ATOM   1271 N  N    . CYS   B 1 65 ? 13.646  -17.694 -42.655 1.00 36.10 ? 64  CYS   B N    1 
ATOM   1272 C  CA   . CYS   B 1 65 ? 12.880  -18.437 -41.662 1.00 34.89 ? 64  CYS   B CA   1 
ATOM   1273 C  C    . CYS   B 1 65 ? 11.918  -17.576 -40.851 1.00 34.12 ? 64  CYS   B C    1 
ATOM   1274 O  O    . CYS   B 1 65 ? 11.315  -18.084 -39.900 1.00 34.69 ? 64  CYS   B O    1 
ATOM   1275 C  CB   . CYS   B 1 65 ? 13.828  -19.172 -40.712 1.00 34.44 ? 64  CYS   B CB   1 
ATOM   1276 S  SG   A CYS   B 1 65 ? 15.277  -19.896 -41.500 0.70 36.68 ? 64  CYS   B SG   1 
ATOM   1277 S  SG   B CYS   B 1 65 ? 14.866  -18.097 -39.727 0.30 32.56 ? 64  CYS   B SG   1 
ATOM   1278 N  N    . LYS   B 1 66 ? 11.748  -16.297 -41.199 1.00 35.59 ? 65  LYS   B N    1 
ATOM   1279 C  CA   . LYS   B 1 66 ? 10.892  -15.426 -40.395 1.00 37.38 ? 65  LYS   B CA   1 
ATOM   1280 C  C    . LYS   B 1 66 ? 9.453   -15.929 -40.356 1.00 39.59 ? 65  LYS   B C    1 
ATOM   1281 O  O    . LYS   B 1 66 ? 8.775   -15.809 -39.328 1.00 40.80 ? 65  LYS   B O    1 
ATOM   1282 C  CB   . LYS   B 1 66 ? 10.934  -13.995 -40.933 1.00 39.98 ? 65  LYS   B CB   1 
ATOM   1283 C  CG   . LYS   B 1 66 ? 10.532  -13.878 -42.390 1.00 41.72 ? 65  LYS   B CG   1 
ATOM   1284 C  CD   . LYS   B 1 66 ? 9.788   -12.583 -42.655 1.00 62.89 ? 65  LYS   B CD   1 
ATOM   1285 C  CE   . LYS   B 1 66 ? 9.061   -12.635 -43.991 1.00 53.01 ? 65  LYS   B CE   1 
ATOM   1286 N  NZ   . LYS   B 1 66 ? 8.089   -13.766 -44.053 1.00 61.53 ? 65  LYS   B NZ   1 
ATOM   1287 N  N    . ASP   B 1 67 ? 8.965   -16.489 -41.465 1.00 36.59 ? 66  ASP   B N    1 
ATOM   1288 C  CA   . ASP   B 1 67 ? 7.600   -16.998 -41.495 1.00 42.15 ? 66  ASP   B CA   1 
ATOM   1289 C  C    . ASP   B 1 67 ? 7.417   -18.161 -40.530 1.00 46.52 ? 66  ASP   B C    1 
ATOM   1290 O  O    . ASP   B 1 67 ? 6.311   -18.379 -40.024 1.00 44.18 ? 66  ASP   B O    1 
ATOM   1291 C  CB   . ASP   B 1 67 ? 7.230   -17.419 -42.917 1.00 39.80 ? 66  ASP   B CB   1 
ATOM   1292 N  N    . LYS   B 1 68 ? 8.487   -18.904 -40.254 1.00 36.69 ? 67  LYS   B N    1 
ATOM   1293 C  CA   . LYS   B 1 68 ? 8.434   -20.072 -39.385 1.00 33.59 ? 67  LYS   B CA   1 
ATOM   1294 C  C    . LYS   B 1 68 ? 8.642   -19.712 -37.916 1.00 33.49 ? 67  LYS   B C    1 
ATOM   1295 O  O    . LYS   B 1 68 ? 7.874   -20.146 -37.054 1.00 35.76 ? 67  LYS   B O    1 
ATOM   1296 C  CB   . LYS   B 1 68 ? 9.486   -21.089 -39.836 1.00 36.90 ? 67  LYS   B CB   1 
ATOM   1297 C  CG   . LYS   B 1 68 ? 9.534   -22.361 -39.022 1.00 43.75 ? 67  LYS   B CG   1 
ATOM   1298 C  CD   . LYS   B 1 68 ? 10.752  -23.184 -39.413 1.00 53.69 ? 67  LYS   B CD   1 
ATOM   1299 C  CE   . LYS   B 1 68 ? 10.396  -24.636 -39.671 1.00 49.39 ? 67  LYS   B CE   1 
ATOM   1300 N  NZ   . LYS   B 1 68 ? 9.960   -25.363 -38.450 1.00 52.75 ? 67  LYS   B NZ   1 
ATOM   1301 N  N    . TYR   B 1 69 ? 9.671   -18.918 -37.619 1.00 28.76 ? 68  TYR   B N    1 
ATOM   1302 C  CA   . TYR   B 1 69 ? 10.062  -18.622 -36.245 1.00 23.46 ? 68  TYR   B CA   1 
ATOM   1303 C  C    . TYR   B 1 69 ? 9.575   -17.269 -35.744 1.00 32.58 ? 68  TYR   B C    1 
ATOM   1304 O  O    . TYR   B 1 69 ? 9.644   -17.016 -34.534 1.00 31.38 ? 68  TYR   B O    1 
ATOM   1305 C  CB   . TYR   B 1 69 ? 11.588  -18.674 -36.112 1.00 28.14 ? 68  TYR   B CB   1 
ATOM   1306 C  CG   . TYR   B 1 69 ? 12.203  -20.004 -36.482 1.00 27.25 ? 68  TYR   B CG   1 
ATOM   1307 C  CD1  . TYR   B 1 69 ? 11.686  -21.193 -35.989 1.00 28.38 ? 68  TYR   B CD1  1 
ATOM   1308 C  CD2  . TYR   B 1 69 ? 13.300  -20.068 -37.329 1.00 32.81 ? 68  TYR   B CD2  1 
ATOM   1309 C  CE1  . TYR   B 1 69 ? 12.252  -22.415 -36.325 1.00 37.85 ? 68  TYR   B CE1  1 
ATOM   1310 C  CE2  . TYR   B 1 69 ? 13.868  -21.281 -37.674 1.00 29.72 ? 68  TYR   B CE2  1 
ATOM   1311 C  CZ   . TYR   B 1 69 ? 13.341  -22.450 -37.171 1.00 37.40 ? 68  TYR   B CZ   1 
ATOM   1312 O  OH   . TYR   B 1 69 ? 13.912  -23.653 -37.517 1.00 33.13 ? 68  TYR   B OH   1 
ATOM   1313 N  N    . GLY   B 1 70 ? 9.106   -16.396 -36.628 1.00 30.97 ? 69  GLY   B N    1 
ATOM   1314 C  CA   . GLY   B 1 70 ? 8.782   -15.037 -36.235 1.00 33.03 ? 69  GLY   B CA   1 
ATOM   1315 C  C    . GLY   B 1 70 ? 7.353   -14.835 -35.778 1.00 41.62 ? 69  GLY   B C    1 
ATOM   1316 O  O    . GLY   B 1 70 ? 6.697   -13.869 -36.180 1.00 42.88 ? 69  GLY   B O    1 
ATOM   1317 N  N    . LYS   B 1 71 ? 6.862   -15.730 -34.933 1.00 35.50 ? 70  LYS   B N    1 
ATOM   1318 C  CA   . LYS   B 1 71 ? 5.508   -15.601 -34.427 1.00 40.85 ? 70  LYS   B CA   1 
ATOM   1319 C  C    . LYS   B 1 71 ? 5.521   -15.312 -32.931 1.00 42.63 ? 70  LYS   B C    1 
ATOM   1320 O  O    . LYS   B 1 71 ? 6.380   -15.832 -32.210 1.00 39.46 ? 70  LYS   B O    1 
ATOM   1321 C  CB   . LYS   B 1 71 ? 4.701   -16.875 -34.693 1.00 44.50 ? 70  LYS   B CB   1 
ATOM   1322 C  CG   . LYS   B 1 71 ? 4.631   -17.231 -36.169 1.00 51.84 ? 70  LYS   B CG   1 
ATOM   1323 C  CD   . LYS   B 1 71 ? 3.793   -18.469 -36.425 1.00 59.77 ? 70  LYS   B CD   1 
ATOM   1324 C  CE   . LYS   B 1 71 ? 3.877   -18.868 -37.890 1.00 54.59 ? 70  LYS   B CE   1 
ATOM   1325 N  NZ   . LYS   B 1 71 ? 3.770   -17.680 -38.781 1.00 56.27 ? 70  LYS   B NZ   1 
ATOM   1326 N  N    . PRO   B 1 72 ? 4.592   -14.491 -32.443 1.00 37.53 ? 71  PRO   B N    1 
ATOM   1327 C  CA   . PRO   B 1 72 ? 4.608   -14.122 -31.023 1.00 37.65 ? 71  PRO   B CA   1 
ATOM   1328 C  C    . PRO   B 1 72 ? 4.411   -15.330 -30.120 1.00 37.28 ? 71  PRO   B C    1 
ATOM   1329 O  O    . PRO   B 1 72 ? 3.796   -16.328 -30.501 1.00 36.45 ? 71  PRO   B O    1 
ATOM   1330 C  CB   . PRO   B 1 72 ? 3.439   -13.136 -30.899 1.00 37.22 ? 71  PRO   B CB   1 
ATOM   1331 C  CG   . PRO   B 1 72 ? 3.220   -12.626 -32.288 1.00 43.21 ? 71  PRO   B CG   1 
ATOM   1332 C  CD   . PRO   B 1 72 ? 3.543   -13.778 -33.189 1.00 41.99 ? 71  PRO   B CD   1 
ATOM   1333 N  N    . ASN   B 1 73 ? 4.955   -15.232 -28.909 1.00 34.93 ? 72  ASN   B N    1 
ATOM   1334 C  CA   . ASN   B 1 73 ? 4.787   -16.272 -27.902 1.00 38.68 ? 72  ASN   B CA   1 
ATOM   1335 C  C    . ASN   B 1 73 ? 4.736   -15.606 -26.530 1.00 34.23 ? 72  ASN   B C    1 
ATOM   1336 O  O    . ASN   B 1 73 ? 4.659   -14.379 -26.418 1.00 38.08 ? 72  ASN   B O    1 
ATOM   1337 C  CB   . ASN   B 1 73 ? 5.898   -17.326 -28.011 1.00 36.45 ? 72  ASN   B CB   1 
ATOM   1338 C  CG   . ASN   B 1 73 ? 7.289   -16.744 -27.813 1.00 30.03 ? 72  ASN   B CG   1 
ATOM   1339 O  OD1  . ASN   B 1 73 ? 7.531   -15.975 -26.887 1.00 32.02 ? 72  ASN   B OD1  1 
ATOM   1340 N  ND2  . ASN   B 1 73 ? 8.213   -17.112 -28.694 1.00 33.06 ? 72  ASN   B ND2  1 
ATOM   1341 N  N    . LYS   B 1 74 ? 4.806   -16.424 -25.482 1.00 38.08 ? 73  LYS   B N    1 
ATOM   1342 C  CA   . LYS   B 1 74 ? 4.639   -15.961 -24.113 1.00 44.39 ? 73  LYS   B CA   1 
ATOM   1343 C  C    . LYS   B 1 74 ? 5.964   -15.733 -23.389 1.00 37.45 ? 73  LYS   B C    1 
ATOM   1344 O  O    . LYS   B 1 74 ? 5.960   -15.521 -22.173 1.00 31.61 ? 73  LYS   B O    1 
ATOM   1345 C  CB   . LYS   B 1 74 ? 3.783   -16.959 -23.330 1.00 40.47 ? 73  LYS   B CB   1 
ATOM   1346 N  N    . ARG   B 1 75 ? 7.090   -15.766 -24.100 1.00 28.35 ? 74  ARG   B N    1 
ATOM   1347 C  CA   . ARG   B 1 75 ? 8.388   -15.588 -23.459 1.00 28.34 ? 74  ARG   B CA   1 
ATOM   1348 C  C    . ARG   B 1 75 ? 8.688   -14.105 -23.278 1.00 32.77 ? 74  ARG   B C    1 
ATOM   1349 O  O    . ARG   B 1 75 ? 8.489   -13.304 -24.197 1.00 31.25 ? 74  ARG   B O    1 
ATOM   1350 C  CB   . ARG   B 1 75 ? 9.492   -16.255 -24.281 1.00 27.45 ? 74  ARG   B CB   1 
ATOM   1351 C  CG   . ARG   B 1 75 ? 9.280   -17.743 -24.545 1.00 27.32 ? 74  ARG   B CG   1 
ATOM   1352 C  CD   . ARG   B 1 75 ? 9.155   -18.524 -23.252 1.00 31.87 ? 74  ARG   B CD   1 
ATOM   1353 N  NE   . ARG   B 1 75 ? 9.317   -19.959 -23.455 1.00 28.16 ? 74  ARG   B NE   1 
ATOM   1354 C  CZ   . ARG   B 1 75 ? 10.457  -20.615 -23.290 1.00 26.70 ? 74  ARG   B CZ   1 
ATOM   1355 N  NH1  . ARG   B 1 75 ? 11.562  -19.995 -22.911 1.00 29.51 ? 74  ARG   B NH1  1 
ATOM   1356 N  NH2  . ARG   B 1 75 ? 10.488  -21.926 -23.506 1.00 37.04 ? 74  ARG   B NH2  1 
ATOM   1357 N  N    . LYS   B 1 76 ? 9.174   -13.742 -22.092 1.00 28.30 ? 75  LYS   B N    1 
ATOM   1358 C  CA   . LYS   B 1 76 ? 9.453   -12.345 -21.792 1.00 26.57 ? 75  LYS   B CA   1 
ATOM   1359 C  C    . LYS   B 1 76 ? 10.537  -11.805 -22.712 1.00 23.00 ? 75  LYS   B C    1 
ATOM   1360 O  O    . LYS   B 1 76 ? 11.645  -12.347 -22.764 1.00 26.22 ? 75  LYS   B O    1 
ATOM   1361 C  CB   . LYS   B 1 76 ? 9.884   -12.187 -20.337 1.00 26.89 ? 75  LYS   B CB   1 
ATOM   1362 C  CG   . LYS   B 1 76 ? 10.365  -10.783 -20.008 1.00 29.51 ? 75  LYS   B CG   1 
ATOM   1363 C  CD   . LYS   B 1 76 ? 10.777  -10.668 -18.555 1.00 34.67 ? 75  LYS   B CD   1 
ATOM   1364 C  CE   . LYS   B 1 76 ? 11.172  -9.244  -18.206 1.00 35.40 ? 75  LYS   B CE   1 
ATOM   1365 N  NZ   . LYS   B 1 76 ? 11.553  -9.122  -16.769 1.00 44.68 ? 75  LYS   B NZ   1 
ATOM   1366 N  N    . GLY   B 1 77 ? 10.219  -10.727 -23.419 1.00 27.37 ? 76  GLY   B N    1 
ATOM   1367 C  CA   . GLY   B 1 77 ? 11.150  -10.084 -24.318 1.00 28.33 ? 76  GLY   B CA   1 
ATOM   1368 C  C    . GLY   B 1 77 ? 10.998  -10.478 -25.771 1.00 27.56 ? 76  GLY   B C    1 
ATOM   1369 O  O    . GLY   B 1 77 ? 11.580  -9.816  -26.638 1.00 28.74 ? 76  GLY   B O    1 
ATOM   1370 N  N    . PHE   B 1 78 ? 10.219  -11.519 -26.068 1.00 28.76 ? 77  PHE   B N    1 
ATOM   1371 C  CA   . PHE   B 1 78 ? 10.180  -12.038 -27.433 1.00 27.87 ? 77  PHE   B CA   1 
ATOM   1372 C  C    . PHE   B 1 78 ? 9.430   -11.099 -28.373 1.00 29.47 ? 77  PHE   B C    1 
ATOM   1373 O  O    . PHE   B 1 78 ? 9.917   -10.777 -29.464 1.00 27.37 ? 77  PHE   B O    1 
ATOM   1374 C  CB   . PHE   B 1 78 ? 9.547   -13.427 -27.450 1.00 29.24 ? 77  PHE   B CB   1 
ATOM   1375 C  CG   . PHE   B 1 78 ? 9.737   -14.153 -28.747 1.00 26.60 ? 77  PHE   B CG   1 
ATOM   1376 C  CD1  . PHE   B 1 78 ? 8.821   -14.014 -29.778 1.00 32.77 ? 77  PHE   B CD1  1 
ATOM   1377 C  CD2  . PHE   B 1 78 ? 10.838  -14.969 -28.937 1.00 26.19 ? 77  PHE   B CD2  1 
ATOM   1378 C  CE1  . PHE   B 1 78 ? 9.001   -14.682 -30.978 1.00 31.79 ? 77  PHE   B CE1  1 
ATOM   1379 C  CE2  . PHE   B 1 78 ? 11.021  -15.639 -30.133 1.00 26.75 ? 77  PHE   B CE2  1 
ATOM   1380 C  CZ   . PHE   B 1 78 ? 10.101  -15.493 -31.154 1.00 23.55 ? 77  PHE   B CZ   1 
ATOM   1381 N  N    . ASN   B 1 79 ? 8.232   -10.664 -27.981 1.00 30.05 ? 78  ASN   B N    1 
ATOM   1382 C  CA   . ASN   B 1 79 ? 7.451   -9.805  -28.866 1.00 32.37 ? 78  ASN   B CA   1 
ATOM   1383 C  C    . ASN   B 1 79 ? 8.121   -8.449  -29.058 1.00 31.73 ? 78  ASN   B C    1 
ATOM   1384 O  O    . ASN   B 1 79 ? 8.069   -7.876  -30.153 1.00 28.83 ? 78  ASN   B O    1 
ATOM   1385 C  CB   . ASN   B 1 79 ? 6.032   -9.644  -28.329 1.00 38.16 ? 78  ASN   B CB   1 
ATOM   1386 C  CG   . ASN   B 1 79 ? 5.265   -10.952 -28.328 1.00 47.14 ? 78  ASN   B CG   1 
ATOM   1387 O  OD1  . ASN   B 1 79 ? 5.693   -11.936 -28.935 1.00 46.79 ? 78  ASN   B OD1  1 
ATOM   1388 N  ND2  . ASN   B 1 79 ? 4.123   -10.970 -27.651 1.00 48.71 ? 78  ASN   B ND2  1 
ATOM   1389 N  N    . GLU   B 1 80 ? 8.760   -7.921  -28.013 1.00 31.45 ? 79  GLU   B N    1 
ATOM   1390 C  CA   . GLU   B 1 80 ? 9.566   -6.718  -28.188 1.00 34.59 ? 79  GLU   B CA   1 
ATOM   1391 C  C    . GLU   B 1 80 ? 10.711  -6.976  -29.158 1.00 27.63 ? 79  GLU   B C    1 
ATOM   1392 O  O    . GLU   B 1 80 ? 11.033  -6.124  -29.994 1.00 30.15 ? 79  GLU   B O    1 
ATOM   1393 C  CB   . GLU   B 1 80 ? 10.102  -6.234  -26.843 1.00 35.04 ? 79  GLU   B CB   1 
ATOM   1394 N  N    . GLY   B 1 81 ? 11.323  -8.160  -29.071 1.00 26.63 ? 80  GLY   B N    1 
ATOM   1395 C  CA   . GLY   B 1 81 ? 12.389  -8.502  -29.997 1.00 27.42 ? 80  GLY   B CA   1 
ATOM   1396 C  C    . GLY   B 1 81 ? 11.904  -8.585  -31.429 1.00 27.58 ? 80  GLY   B C    1 
ATOM   1397 O  O    . GLY   B 1 81 ? 12.600  -8.164  -32.357 1.00 27.74 ? 80  GLY   B O    1 
ATOM   1398 N  N    . LEU   B 1 82 ? 10.701  -9.126  -31.629 1.00 24.16 ? 81  LEU   B N    1 
ATOM   1399 C  CA   . LEU   B 1 82 ? 10.123  -9.143  -32.969 1.00 32.09 ? 81  LEU   B CA   1 
ATOM   1400 C  C    . LEU   B 1 82 ? 9.924   -7.727  -33.493 1.00 30.75 ? 81  LEU   B C    1 
ATOM   1401 O  O    . LEU   B 1 82 ? 10.133  -7.460  -34.683 1.00 29.15 ? 81  LEU   B O    1 
ATOM   1402 C  CB   . LEU   B 1 82 ? 8.799   -9.907  -32.966 1.00 31.53 ? 81  LEU   B CB   1 
ATOM   1403 C  CG   . LEU   B 1 82 ? 8.873   -11.425 -32.796 1.00 28.63 ? 81  LEU   B CG   1 
ATOM   1404 C  CD1  . LEU   B 1 82 ? 7.489   -12.038 -32.937 1.00 33.73 ? 81  LEU   B CD1  1 
ATOM   1405 C  CD2  . LEU   B 1 82 ? 9.837   -12.042 -33.801 1.00 26.16 ? 81  LEU   B CD2  1 
ATOM   1406 N  N    . TRP   B 1 83 ? 9.525   -6.803  -32.618 1.00 27.13 ? 82  TRP   B N    1 
ATOM   1407 C  CA   . TRP   B 1 83 ? 9.417   -5.411  -33.035 1.00 28.61 ? 82  TRP   B CA   1 
ATOM   1408 C  C    . TRP   B 1 83 ? 10.776  -4.848  -33.422 1.00 25.61 ? 82  TRP   B C    1 
ATOM   1409 O  O    . TRP   B 1 83 ? 10.903  -4.167  -34.443 1.00 32.81 ? 82  TRP   B O    1 
ATOM   1410 C  CB   . TRP   B 1 83 ? 8.800   -4.560  -31.927 1.00 28.59 ? 82  TRP   B CB   1 
ATOM   1411 C  CG   . TRP   B 1 83 ? 8.531   -3.155  -32.384 1.00 29.35 ? 82  TRP   B CG   1 
ATOM   1412 C  CD1  . TRP   B 1 83 ? 7.366   -2.674  -32.900 1.00 39.06 ? 82  TRP   B CD1  1 
ATOM   1413 C  CD2  . TRP   B 1 83 ? 9.458   -2.062  -32.397 1.00 37.50 ? 82  TRP   B CD2  1 
ATOM   1414 N  NE1  . TRP   B 1 83 ? 7.503   -1.344  -33.222 1.00 39.49 ? 82  TRP   B NE1  1 
ATOM   1415 C  CE2  . TRP   B 1 83 ? 8.778   -0.945  -32.922 1.00 31.83 ? 82  TRP   B CE2  1 
ATOM   1416 C  CE3  . TRP   B 1 83 ? 10.794  -1.917  -32.007 1.00 35.61 ? 82  TRP   B CE3  1 
ATOM   1417 C  CZ2  . TRP   B 1 83 ? 9.389   0.299   -33.071 1.00 43.15 ? 82  TRP   B CZ2  1 
ATOM   1418 C  CZ3  . TRP   B 1 83 ? 11.399  -0.680  -32.155 1.00 37.85 ? 82  TRP   B CZ3  1 
ATOM   1419 C  CH2  . TRP   B 1 83 ? 10.697  0.411   -32.681 1.00 38.77 ? 82  TRP   B CH2  1 
ATOM   1420 N  N    . GLU   B 1 84 ? 11.805  -5.132  -32.622 1.00 24.40 ? 83  GLU   B N    1 
ATOM   1421 C  CA   . GLU   B 1 84 ? 13.114  -4.528  -32.856 1.00 27.44 ? 83  GLU   B CA   1 
ATOM   1422 C  C    . GLU   B 1 84 ? 13.735  -5.019  -34.155 1.00 31.12 ? 83  GLU   B C    1 
ATOM   1423 O  O    . GLU   B 1 84 ? 14.285  -4.221  -34.925 1.00 26.35 ? 83  GLU   B O    1 
ATOM   1424 C  CB   . GLU   B 1 84 ? 14.043  -4.817  -31.682 1.00 26.83 ? 83  GLU   B CB   1 
ATOM   1425 C  CG   . GLU   B 1 84 ? 13.607  -4.136  -30.388 1.00 28.85 ? 83  GLU   B CG   1 
ATOM   1426 C  CD   . GLU   B 1 84 ? 14.499  -4.483  -29.216 1.00 30.89 ? 83  GLU   B CD   1 
ATOM   1427 O  OE1  . GLU   B 1 84 ? 15.384  -5.349  -29.378 1.00 26.56 ? 83  GLU   B OE1  1 
ATOM   1428 O  OE2  . GLU   B 1 84 ? 14.315  -3.893  -28.130 1.00 29.48 ? 83  GLU   B OE2  1 
ATOM   1429 N  N    . ILE   B 1 85 ? 13.673  -6.327  -34.414 1.00 25.77 ? 84  ILE   B N    1 
ATOM   1430 C  CA   . ILE   B 1 85 ? 14.311  -6.856  -35.620 1.00 23.34 ? 84  ILE   B CA   1 
ATOM   1431 C  C    . ILE   B 1 85 ? 13.611  -6.340  -36.873 1.00 27.34 ? 84  ILE   B C    1 
ATOM   1432 O  O    . ILE   B 1 85 ? 14.231  -6.233  -37.941 1.00 25.13 ? 84  ILE   B O    1 
ATOM   1433 C  CB   . ILE   B 1 85 ? 14.351  -8.397  -35.578 1.00 27.97 ? 84  ILE   B CB   1 
ATOM   1434 C  CG1  . ILE   B 1 85 ? 15.322  -8.941  -36.631 1.00 21.45 ? 84  ILE   B CG1  1 
ATOM   1435 C  CG2  . ILE   B 1 85 ? 12.959  -8.987  -35.786 1.00 25.55 ? 84  ILE   B CG2  1 
ATOM   1436 C  CD1  . ILE   B 1 85 ? 15.777  -10.368 -36.351 1.00 22.95 ? 84  ILE   B CD1  1 
ATOM   1437 N  N    . GLN   B 1 86 ? 12.328  -5.981  -36.766 1.00 24.28 ? 85  GLN   B N    1 
ATOM   1438 C  CA   . GLN   B 1 86 ? 11.598  -5.483  -37.927 1.00 25.62 ? 85  GLN   B CA   1 
ATOM   1439 C  C    . GLN   B 1 86 ? 11.788  -3.982  -38.125 1.00 32.29 ? 85  GLN   B C    1 
ATOM   1440 O  O    . GLN   B 1 86 ? 11.958  -3.524  -39.260 1.00 31.36 ? 85  GLN   B O    1 
ATOM   1441 C  CB   . GLN   B 1 86 ? 10.110  -5.804  -37.785 1.00 35.14 ? 85  GLN   B CB   1 
ATOM   1442 N  N    . ASN   B 1 87 ? 11.764  -3.202  -37.043 1.00 29.73 ? 86  ASN   B N    1 
ATOM   1443 C  CA   . ASN   B 1 87 ? 11.675  -1.747  -37.141 1.00 26.63 ? 86  ASN   B CA   1 
ATOM   1444 C  C    . ASN   B 1 87 ? 13.001  -1.021  -36.956 1.00 28.02 ? 86  ASN   B C    1 
ATOM   1445 O  O    . ASN   B 1 87 ? 13.154  0.095   -37.464 1.00 31.28 ? 86  ASN   B O    1 
ATOM   1446 C  CB   . ASN   B 1 87 ? 10.666  -1.222  -36.111 1.00 29.21 ? 86  ASN   B CB   1 
ATOM   1447 C  CG   . ASN   B 1 87 ? 9.254   -1.686  -36.404 1.00 42.41 ? 86  ASN   B CG   1 
ATOM   1448 O  OD1  . ASN   B 1 87 ? 8.795   -2.704  -35.882 1.00 40.18 ? 86  ASN   B OD1  1 
ATOM   1449 N  ND2  . ASN   B 1 87 ? 8.562   -0.947  -37.262 1.00 48.40 ? 86  ASN   B ND2  1 
ATOM   1450 N  N    . ASN   B 1 88 ? 13.955  -1.596  -36.229 1.00 25.40 ? 87  ASN   B N    1 
ATOM   1451 C  CA   . ASN   B 1 88 ? 15.246  -0.939  -36.047 1.00 28.44 ? 87  ASN   B CA   1 
ATOM   1452 C  C    . ASN   B 1 88 ? 16.295  -1.955  -35.620 1.00 26.84 ? 87  ASN   B C    1 
ATOM   1453 O  O    . ASN   B 1 88 ? 16.827  -1.875  -34.504 1.00 25.35 ? 87  ASN   B O    1 
ATOM   1454 C  CB   . ASN   B 1 88 ? 15.155  0.191   -35.016 1.00 33.09 ? 87  ASN   B CB   1 
ATOM   1455 C  CG   . ASN   B 1 88 ? 16.235  1.243   -35.213 1.00 30.98 ? 87  ASN   B CG   1 
ATOM   1456 O  OD1  . ASN   B 1 88 ? 17.246  0.996   -35.873 1.00 29.80 ? 87  ASN   B OD1  1 
ATOM   1457 N  ND2  . ASN   B 1 88 ? 16.024  2.424   -34.644 1.00 36.64 ? 87  ASN   B ND2  1 
ATOM   1458 N  N    . PRO   B 1 89 ? 16.635  -2.909  -36.491 1.00 27.94 ? 88  PRO   B N    1 
ATOM   1459 C  CA   . PRO   B 1 89 ? 17.530  -3.997  -36.076 1.00 25.77 ? 88  PRO   B CA   1 
ATOM   1460 C  C    . PRO   B 1 89 ? 18.955  -3.558  -35.813 1.00 25.69 ? 88  PRO   B C    1 
ATOM   1461 O  O    . PRO   B 1 89 ? 19.679  -4.279  -35.118 1.00 27.48 ? 88  PRO   B O    1 
ATOM   1462 C  CB   . PRO   B 1 89 ? 17.462  -4.975  -37.259 1.00 25.09 ? 88  PRO   B CB   1 
ATOM   1463 C  CG   . PRO   B 1 89 ? 17.138  -4.116  -38.432 1.00 26.06 ? 88  PRO   B CG   1 
ATOM   1464 C  CD   . PRO   B 1 89 ? 16.212  -3.050  -37.897 1.00 23.28 ? 88  PRO   B CD   1 
ATOM   1465 N  N    . HIS   B 1 90 ? 19.389  -2.412  -36.339 1.00 25.51 ? 89  HIS   B N    1 
ATOM   1466 C  CA   . HIS   B 1 90 ? 20.785  -2.006  -36.241 1.00 25.54 ? 89  HIS   B CA   1 
ATOM   1467 C  C    . HIS   B 1 90 ? 21.016  -0.897  -35.225 1.00 27.32 ? 89  HIS   B C    1 
ATOM   1468 O  O    . HIS   B 1 90 ? 22.121  -0.351  -35.166 1.00 27.45 ? 89  HIS   B O    1 
ATOM   1469 C  CB   . HIS   B 1 90 ? 21.300  -1.575  -37.617 1.00 24.66 ? 89  HIS   B CB   1 
ATOM   1470 C  CG   . HIS   B 1 90 ? 21.117  -2.622  -38.667 1.00 26.98 ? 89  HIS   B CG   1 
ATOM   1471 N  ND1  . HIS   B 1 90 ? 21.756  -3.843  -38.618 1.00 24.37 ? 89  HIS   B ND1  1 
ATOM   1472 C  CD2  . HIS   B 1 90 ? 20.347  -2.644  -39.781 1.00 27.53 ? 89  HIS   B CD2  1 
ATOM   1473 C  CE1  . HIS   B 1 90 ? 21.397  -4.567  -39.663 1.00 25.38 ? 89  HIS   B CE1  1 
ATOM   1474 N  NE2  . HIS   B 1 90 ? 20.544  -3.862  -40.384 1.00 26.51 ? 89  HIS   B NE2  1 
ATOM   1475 N  N    . ALA   B 1 91 ? 20.015  -0.574  -34.413 1.00 27.92 ? 90  ALA   B N    1 
ATOM   1476 C  CA   . ALA   B 1 91 ? 20.142  0.504   -33.446 1.00 31.58 ? 90  ALA   B CA   1 
ATOM   1477 C  C    . ALA   B 1 91 ? 21.041  0.105   -32.282 1.00 37.76 ? 90  ALA   B C    1 
ATOM   1478 O  O    . ALA   B 1 91 ? 21.346  -1.071  -32.061 1.00 30.38 ? 90  ALA   B O    1 
ATOM   1479 C  CB   . ALA   B 1 91 ? 18.770  0.911   -32.912 1.00 28.26 ? 90  ALA   B CB   1 
ATOM   1480 N  N    . SER   B 1 92 ? 21.465  1.118   -31.530 1.00 31.95 ? 91  SER   B N    1 
ATOM   1481 C  CA   . SER   B 1 92 ? 22.124  0.895   -30.254 1.00 36.60 ? 91  SER   B CA   1 
ATOM   1482 C  C    . SER   B 1 92 ? 21.060  0.688   -29.185 1.00 42.59 ? 91  SER   B C    1 
ATOM   1483 O  O    . SER   B 1 92 ? 20.164  1.521   -29.021 1.00 35.66 ? 91  SER   B O    1 
ATOM   1484 C  CB   . SER   B 1 92 ? 23.021  2.081   -29.896 1.00 42.19 ? 91  SER   B CB   1 
ATOM   1485 O  OG   . SER   B 1 92 ? 23.795  1.798   -28.741 1.00 58.19 ? 91  SER   B OG   1 
ATOM   1486 N  N    . TYR   B 1 93 ? 21.144  -0.436  -28.478 1.00 34.55 ? 92  TYR   B N    1 
ATOM   1487 C  CA   . TYR   B 1 93 ? 20.177  -0.778  -27.446 1.00 38.65 ? 92  TYR   B CA   1 
ATOM   1488 C  C    . TYR   B 1 93 ? 20.781  -0.790  -26.050 1.00 54.38 ? 92  TYR   B C    1 
ATOM   1489 O  O    . TYR   B 1 93 ? 20.053  -1.008  -25.075 1.00 53.36 ? 92  TYR   B O    1 
ATOM   1490 C  CB   . TYR   B 1 93 ? 19.532  -2.133  -27.764 1.00 34.19 ? 92  TYR   B CB   1 
ATOM   1491 C  CG   . TYR   B 1 93 ? 18.543  -2.052  -28.903 1.00 30.00 ? 92  TYR   B CG   1 
ATOM   1492 C  CD1  . TYR   B 1 93 ? 17.267  -1.554  -28.697 1.00 28.29 ? 92  TYR   B CD1  1 
ATOM   1493 C  CD2  . TYR   B 1 93 ? 18.890  -2.456  -30.189 1.00 27.03 ? 92  TYR   B CD2  1 
ATOM   1494 C  CE1  . TYR   B 1 93 ? 16.356  -1.464  -29.728 1.00 31.32 ? 92  TYR   B CE1  1 
ATOM   1495 C  CE2  . TYR   B 1 93 ? 17.982  -2.371  -31.233 1.00 26.19 ? 92  TYR   B CE2  1 
ATOM   1496 C  CZ   . TYR   B 1 93 ? 16.717  -1.874  -30.995 1.00 30.12 ? 92  TYR   B CZ   1 
ATOM   1497 O  OH   . TYR   B 1 93 ? 15.799  -1.781  -32.017 1.00 29.67 ? 92  TYR   B OH   1 
ATOM   1498 N  N    . SER   B 1 94 ? 22.080  -0.544  -25.926 1.00 57.31 ? 93  SER   B N    1 
ATOM   1499 C  CA   . SER   B 1 94 ? 22.727  -0.432  -24.627 1.00 66.34 ? 93  SER   B CA   1 
ATOM   1500 C  C    . SER   B 1 94 ? 22.428  0.922   -23.989 1.00 68.13 ? 93  SER   B C    1 
ATOM   1501 O  O    . SER   B 1 94 ? 21.712  1.747   -24.561 1.00 65.29 ? 93  SER   B O    1 
ATOM   1502 C  CB   . SER   B 1 94 ? 24.237  -0.633  -24.767 1.00 62.36 ? 93  SER   B CB   1 
ATOM   1503 O  OG   . SER   B 1 94 ? 24.769  0.212   -25.775 1.00 68.60 ? 93  SER   B OG   1 
ATOM   1504 N  N    . HIS   C 1 4  ? 32.039  -22.418 27.041  1.00 55.05 ? 3   HIS   C N    1 
ATOM   1505 C  CA   . HIS   C 1 4  ? 31.623  -22.283 28.433  1.00 49.83 ? 3   HIS   C CA   1 
ATOM   1506 C  C    . HIS   C 1 4  ? 30.502  -23.261 28.762  1.00 53.20 ? 3   HIS   C C    1 
ATOM   1507 O  O    . HIS   C 1 4  ? 29.761  -23.686 27.875  1.00 62.88 ? 3   HIS   C O    1 
ATOM   1508 C  CB   . HIS   C 1 4  ? 31.172  -20.849 28.722  1.00 61.01 ? 3   HIS   C CB   1 
ATOM   1509 N  N    . ALA   C 1 5  ? 30.384  -23.619 30.039  1.00 46.01 ? 4   ALA   C N    1 
ATOM   1510 C  CA   . ALA   C 1 5  ? 29.328  -24.525 30.468  1.00 50.90 ? 4   ALA   C CA   1 
ATOM   1511 C  C    . ALA   C 1 5  ? 27.962  -23.872 30.294  1.00 50.29 ? 4   ALA   C C    1 
ATOM   1512 O  O    . ALA   C 1 5  ? 27.800  -22.664 30.494  1.00 52.93 ? 4   ALA   C O    1 
ATOM   1513 C  CB   . ALA   C 1 5  ? 29.536  -24.939 31.926  1.00 46.42 ? 4   ALA   C CB   1 
ATOM   1514 N  N    . PHE   C 1 6  ? 26.978  -24.680 29.916  1.00 49.75 ? 5   PHE   C N    1 
ATOM   1515 C  CA   . PHE   C 1 6  ? 25.639  -24.193 29.627  1.00 41.61 ? 5   PHE   C CA   1 
ATOM   1516 C  C    . PHE   C 1 6  ? 24.771  -24.230 30.881  1.00 46.97 ? 5   PHE   C C    1 
ATOM   1517 O  O    . PHE   C 1 6  ? 25.117  -24.839 31.896  1.00 51.46 ? 5   PHE   C O    1 
ATOM   1518 C  CB   . PHE   C 1 6  ? 25.000  -25.025 28.511  1.00 37.81 ? 5   PHE   C CB   1 
ATOM   1519 C  CG   . PHE   C 1 6  ? 25.755  -24.981 27.210  1.00 42.42 ? 5   PHE   C CG   1 
ATOM   1520 C  CD1  . PHE   C 1 6  ? 26.786  -25.872 26.960  1.00 38.76 ? 5   PHE   C CD1  1 
ATOM   1521 C  CD2  . PHE   C 1 6  ? 25.429  -24.052 26.236  1.00 45.88 ? 5   PHE   C CD2  1 
ATOM   1522 C  CE1  . PHE   C 1 6  ? 27.483  -25.835 25.763  1.00 46.83 ? 5   PHE   C CE1  1 
ATOM   1523 C  CE2  . PHE   C 1 6  ? 26.122  -24.009 25.035  1.00 38.81 ? 5   PHE   C CE2  1 
ATOM   1524 C  CZ   . PHE   C 1 6  ? 27.149  -24.901 24.799  1.00 40.55 ? 5   PHE   C CZ   1 
ATOM   1525 N  N    . LYS   C 1 7  ? 23.626  -23.569 30.797  1.00 46.14 ? 6   LYS   C N    1 
ATOM   1526 C  CA   . LYS   C 1 7  ? 22.644  -23.498 31.866  1.00 47.98 ? 6   LYS   C CA   1 
ATOM   1527 C  C    . LYS   C 1 7  ? 21.270  -23.793 31.289  1.00 41.64 ? 6   LYS   C C    1 
ATOM   1528 O  O    . LYS   C 1 7  ? 21.056  -23.650 30.080  1.00 37.73 ? 6   LYS   C O    1 
ATOM   1529 C  CB   . LYS   C 1 7  ? 22.654  -22.113 32.534  1.00 47.88 ? 6   LYS   C CB   1 
ATOM   1530 C  CG   . LYS   C 1 7  ? 22.090  -20.990 31.675  1.00 47.08 ? 6   LYS   C CG   1 
ATOM   1531 C  CD   . LYS   C 1 7  ? 22.760  -19.661 32.002  1.00 58.04 ? 6   LYS   C CD   1 
ATOM   1532 C  CE   . LYS   C 1 7  ? 21.960  -18.476 31.472  1.00 59.28 ? 6   LYS   C CE   1 
ATOM   1533 N  NZ   . LYS   C 1 7  ? 21.814  -18.483 29.987  1.00 64.62 ? 6   LYS   C NZ   1 
ATOM   1534 N  N    . PRO   C 1 8  ? 20.321  -24.230 32.119  1.00 39.81 ? 7   PRO   C N    1 
ATOM   1535 C  CA   . PRO   C 1 8  ? 18.973  -24.512 31.612  1.00 44.39 ? 7   PRO   C CA   1 
ATOM   1536 C  C    . PRO   C 1 8  ? 18.386  -23.313 30.879  1.00 51.82 ? 7   PRO   C C    1 
ATOM   1537 O  O    . PRO   C 1 8  ? 18.488  -22.170 31.331  1.00 45.97 ? 7   PRO   C O    1 
ATOM   1538 C  CB   . PRO   C 1 8  ? 18.183  -24.844 32.881  1.00 51.06 ? 7   PRO   C CB   1 
ATOM   1539 C  CG   . PRO   C 1 8  ? 19.205  -25.395 33.808  1.00 48.87 ? 7   PRO   C CG   1 
ATOM   1540 C  CD   . PRO   C 1 8  ? 20.472  -24.632 33.530  1.00 43.12 ? 7   PRO   C CD   1 
ATOM   1541 N  N    . GLY   C 1 9  ? 17.784  -23.585 29.721  1.00 47.15 ? 8   GLY   C N    1 
ATOM   1542 C  CA   . GLY   C 1 9  ? 17.203  -22.568 28.878  1.00 44.09 ? 8   GLY   C CA   1 
ATOM   1543 C  C    . GLY   C 1 9  ? 18.079  -22.125 27.724  1.00 43.49 ? 8   GLY   C C    1 
ATOM   1544 O  O    . GLY   C 1 9  ? 17.561  -21.538 26.766  1.00 46.99 ? 8   GLY   C O    1 
ATOM   1545 N  N    . ASP   C 1 10 ? 19.384  -22.381 27.790  1.00 44.67 ? 9   ASP   C N    1 
ATOM   1546 C  CA   . ASP   C 1 10 ? 20.283  -21.985 26.714  1.00 36.33 ? 9   ASP   C CA   1 
ATOM   1547 C  C    . ASP   C 1 10 ? 19.908  -22.692 25.418  1.00 38.73 ? 9   ASP   C C    1 
ATOM   1548 O  O    . ASP   C 1 10 ? 19.593  -23.884 25.412  1.00 36.81 ? 9   ASP   C O    1 
ATOM   1549 C  CB   . ASP   C 1 10 ? 21.730  -22.310 27.083  1.00 45.28 ? 9   ASP   C CB   1 
ATOM   1550 C  CG   . ASP   C 1 10 ? 22.255  -21.445 28.211  1.00 55.32 ? 9   ASP   C CG   1 
ATOM   1551 O  OD1  . ASP   C 1 10 ? 21.576  -20.457 28.566  1.00 49.79 ? 9   ASP   C OD1  1 
ATOM   1552 O  OD2  . ASP   C 1 10 ? 23.344  -21.755 28.741  1.00 46.97 ? 9   ASP   C OD2  1 
ATOM   1553 N  N    . LEU   C 1 11 ? 19.943  -21.948 24.316  1.00 35.45 ? 10  LEU   C N    1 
ATOM   1554 C  CA   . LEU   C 1 11 ? 19.593  -22.482 23.006  1.00 36.42 ? 10  LEU   C CA   1 
ATOM   1555 C  C    . LEU   C 1 11 ? 20.849  -22.972 22.298  1.00 33.24 ? 10  LEU   C C    1 
ATOM   1556 O  O    . LEU   C 1 11 ? 21.867  -22.274 22.275  1.00 30.50 ? 10  LEU   C O    1 
ATOM   1557 C  CB   . LEU   C 1 11 ? 18.889  -21.418 22.166  1.00 36.22 ? 10  LEU   C CB   1 
ATOM   1558 C  CG   . LEU   C 1 11 ? 17.672  -20.799 22.848  1.00 31.94 ? 10  LEU   C CG   1 
ATOM   1559 C  CD1  . LEU   C 1 11 ? 17.056  -19.724 21.970  1.00 35.40 ? 10  LEU   C CD1  1 
ATOM   1560 C  CD2  . LEU   C 1 11 ? 16.656  -21.878 23.189  1.00 33.25 ? 10  LEU   C CD2  1 
ATOM   1561 N  N    . VAL   C 1 12 ? 20.781  -24.177 21.727  1.00 31.85 ? 11  VAL   C N    1 
ATOM   1562 C  CA   . VAL   C 1 12 ? 21.950  -24.836 21.160  1.00 31.28 ? 11  VAL   C CA   1 
ATOM   1563 C  C    . VAL   C 1 12 ? 21.557  -25.596 19.898  1.00 27.37 ? 11  VAL   C C    1 
ATOM   1564 O  O    . VAL   C 1 12 ? 20.378  -25.790 19.593  1.00 27.34 ? 11  VAL   C O    1 
ATOM   1565 C  CB   . VAL   C 1 12 ? 22.616  -25.817 22.155  1.00 36.81 ? 11  VAL   C CB   1 
ATOM   1566 C  CG1  . VAL   C 1 12 ? 23.073  -25.105 23.431  1.00 33.42 ? 11  VAL   C CG1  1 
ATOM   1567 C  CG2  . VAL   C 1 12 ? 21.665  -26.956 22.482  1.00 27.99 ? 11  VAL   C CG2  1 
ATOM   1568 N  N    . PHE   C 1 13 ? 22.579  -26.013 19.159  1.00 26.18 ? 12  PHE   C N    1 
ATOM   1569 C  CA   . PHE   C 1 13 ? 22.484  -27.132 18.234  1.00 24.78 ? 12  PHE   C CA   1 
ATOM   1570 C  C    . PHE   C 1 13 ? 23.148  -28.331 18.894  1.00 29.64 ? 12  PHE   C C    1 
ATOM   1571 O  O    . PHE   C 1 13 ? 24.262  -28.218 19.417  1.00 34.18 ? 12  PHE   C O    1 
ATOM   1572 C  CB   . PHE   C 1 13 ? 23.158  -26.819 16.898  1.00 33.34 ? 12  PHE   C CB   1 
ATOM   1573 C  CG   . PHE   C 1 13 ? 22.432  -25.794 16.083  1.00 31.14 ? 12  PHE   C CG   1 
ATOM   1574 C  CD1  . PHE   C 1 13 ? 21.393  -26.167 15.249  1.00 31.63 ? 12  PHE   C CD1  1 
ATOM   1575 C  CD2  . PHE   C 1 13 ? 22.783  -24.458 16.152  1.00 35.38 ? 12  PHE   C CD2  1 
ATOM   1576 C  CE1  . PHE   C 1 13 ? 20.717  -25.227 14.496  1.00 29.78 ? 12  PHE   C CE1  1 
ATOM   1577 C  CE2  . PHE   C 1 13 ? 22.109  -23.513 15.400  1.00 33.68 ? 12  PHE   C CE2  1 
ATOM   1578 C  CZ   . PHE   C 1 13 ? 21.074  -23.900 14.573  1.00 32.84 ? 12  PHE   C CZ   1 
ATOM   1579 N  N    . ALA   C 1 14 ? 22.455  -29.466 18.891  1.00 24.43 ? 13  ALA   C N    1 
ATOM   1580 C  CA   . ALA   C 1 14 ? 22.908  -30.670 19.571  1.00 23.03 ? 13  ALA   C CA   1 
ATOM   1581 C  C    . ALA   C 1 14 ? 23.196  -31.741 18.532  1.00 27.26 ? 13  ALA   C C    1 
ATOM   1582 O  O    . ALA   C 1 14 ? 22.379  -31.972 17.635  1.00 23.76 ? 13  ALA   C O    1 
ATOM   1583 C  CB   . ALA   C 1 14 ? 21.860  -31.158 20.571  1.00 24.99 ? 13  ALA   C CB   1 
ATOM   1584 N  N    . LYS   C 1 15 ? 24.356  -32.384 18.648  1.00 26.79 ? 14  LYS   C N    1 
ATOM   1585 C  CA   . LYS   C 1 15 ? 24.821  -33.360 17.669  1.00 29.14 ? 14  LYS   C CA   1 
ATOM   1586 C  C    . LYS   C 1 15 ? 24.775  -34.751 18.287  1.00 31.69 ? 14  LYS   C C    1 
ATOM   1587 O  O    . LYS   C 1 15 ? 25.525  -35.049 19.224  1.00 31.57 ? 14  LYS   C O    1 
ATOM   1588 C  CB   . LYS   C 1 15 ? 26.230  -33.025 17.189  1.00 29.70 ? 14  LYS   C CB   1 
ATOM   1589 C  CG   . LYS   C 1 15 ? 26.749  -33.968 16.115  1.00 34.25 ? 14  LYS   C CG   1 
ATOM   1590 C  CD   . LYS   C 1 15 ? 25.933  -33.857 14.832  1.00 32.54 ? 14  LYS   C CD   1 
ATOM   1591 C  CE   . LYS   C 1 15 ? 26.475  -34.789 13.746  1.00 34.17 ? 14  LYS   C CE   1 
ATOM   1592 N  NZ   . LYS   C 1 15 ? 26.157  -36.219 14.028  1.00 31.89 ? 14  LYS   C NZ   1 
ATOM   1593 N  N    . MET   C 1 16 ? 23.889  -35.592 17.765  1.00 24.78 ? 15  MET   C N    1 
ATOM   1594 C  CA   . MET   C 1 16 ? 23.833  -37.008 18.093  1.00 24.05 ? 15  MET   C CA   1 
ATOM   1595 C  C    . MET   C 1 16 ? 24.361  -37.809 16.911  1.00 29.70 ? 15  MET   C C    1 
ATOM   1596 O  O    . MET   C 1 16 ? 24.196  -37.413 15.756  1.00 28.46 ? 15  MET   C O    1 
ATOM   1597 C  CB   . MET   C 1 16 ? 22.399  -37.448 18.410  1.00 26.49 ? 15  MET   C CB   1 
ATOM   1598 C  CG   . MET   C 1 16 ? 21.717  -36.650 19.506  1.00 36.88 ? 15  MET   C CG   1 
ATOM   1599 S  SD   . MET   C 1 16 ? 22.226  -37.197 21.137  1.00 42.84 ? 15  MET   C SD   1 
ATOM   1600 C  CE   . MET   C 1 16 ? 21.737  -38.916 21.098  1.00 36.09 ? 15  MET   C CE   1 
ATOM   1601 N  N    . LYS   C 1 17 ? 25.004  -38.937 17.205  1.00 29.94 ? 16  LYS   C N    1 
ATOM   1602 C  CA   . LYS   C 1 17 ? 25.474  -39.815 16.142  1.00 31.83 ? 16  LYS   C CA   1 
ATOM   1603 C  C    . LYS   C 1 17 ? 24.295  -40.277 15.296  1.00 26.80 ? 16  LYS   C C    1 
ATOM   1604 O  O    . LYS   C 1 17 ? 23.294  -40.771 15.825  1.00 29.24 ? 16  LYS   C O    1 
ATOM   1605 C  CB   . LYS   C 1 17 ? 26.212  -41.018 16.735  1.00 28.98 ? 16  LYS   C CB   1 
ATOM   1606 C  CG   . LYS   C 1 17 ? 26.867  -41.927 15.693  1.00 31.06 ? 16  LYS   C CG   1 
ATOM   1607 C  CD   . LYS   C 1 17 ? 27.916  -41.171 14.889  1.00 35.47 ? 16  LYS   C CD   1 
ATOM   1608 C  CE   . LYS   C 1 17 ? 28.712  -42.112 14.001  1.00 46.91 ? 16  LYS   C CE   1 
ATOM   1609 N  NZ   . LYS   C 1 17 ? 29.807  -41.405 13.284  1.00 41.69 ? 16  LYS   C NZ   1 
ATOM   1610 N  N    . GLY   C 1 18 ? 24.410  -40.101 13.983  1.00 27.93 ? 17  GLY   C N    1 
ATOM   1611 C  CA   . GLY   C 1 18 ? 23.350  -40.454 13.060  1.00 30.67 ? 17  GLY   C CA   1 
ATOM   1612 C  C    . GLY   C 1 18 ? 22.342  -39.363 12.772  1.00 31.30 ? 17  GLY   C C    1 
ATOM   1613 O  O    . GLY   C 1 18 ? 21.332  -39.636 12.112  1.00 31.02 ? 17  GLY   C O    1 
ATOM   1614 N  N    . TYR   C 1 19 ? 22.578  -38.141 13.241  1.00 27.47 ? 18  TYR   C N    1 
ATOM   1615 C  CA   . TYR   C 1 19 ? 21.627  -37.049 13.102  1.00 24.30 ? 18  TYR   C CA   1 
ATOM   1616 C  C    . TYR   C 1 19 ? 22.363  -35.760 12.783  1.00 23.83 ? 18  TYR   C C    1 
ATOM   1617 O  O    . TYR   C 1 19 ? 23.486  -35.550 13.255  1.00 24.25 ? 18  TYR   C O    1 
ATOM   1618 C  CB   . TYR   C 1 19 ? 20.807  -36.850 14.387  1.00 26.66 ? 18  TYR   C CB   1 
ATOM   1619 C  CG   . TYR   C 1 19 ? 19.969  -38.045 14.738  1.00 27.20 ? 18  TYR   C CG   1 
ATOM   1620 C  CD1  . TYR   C 1 19 ? 20.505  -39.100 15.468  1.00 29.46 ? 18  TYR   C CD1  1 
ATOM   1621 C  CD2  . TYR   C 1 19 ? 18.649  -38.132 14.328  1.00 32.63 ? 18  TYR   C CD2  1 
ATOM   1622 C  CE1  . TYR   C 1 19 ? 19.747  -40.204 15.781  1.00 32.82 ? 18  TYR   C CE1  1 
ATOM   1623 C  CE2  . TYR   C 1 19 ? 17.878  -39.234 14.641  1.00 34.98 ? 18  TYR   C CE2  1 
ATOM   1624 C  CZ   . TYR   C 1 19 ? 18.434  -40.266 15.369  1.00 38.82 ? 18  TYR   C CZ   1 
ATOM   1625 O  OH   . TYR   C 1 19 ? 17.674  -41.369 15.683  1.00 46.75 ? 18  TYR   C OH   1 
ATOM   1626 N  N    . PRO   C 1 20 ? 21.754  -34.875 12.003  1.00 22.63 ? 19  PRO   C N    1 
ATOM   1627 C  CA   . PRO   C 1 20 ? 22.356  -33.561 11.781  1.00 23.96 ? 19  PRO   C CA   1 
ATOM   1628 C  C    . PRO   C 1 20 ? 22.338  -32.745 13.061  1.00 19.67 ? 19  PRO   C C    1 
ATOM   1629 O  O    . PRO   C 1 20 ? 21.603  -33.043 14.006  1.00 27.80 ? 19  PRO   C O    1 
ATOM   1630 C  CB   . PRO   C 1 20 ? 21.456  -32.935 10.714  1.00 29.65 ? 19  PRO   C CB   1 
ATOM   1631 C  CG   . PRO   C 1 20 ? 20.121  -33.579 10.951  1.00 27.01 ? 19  PRO   C CG   1 
ATOM   1632 C  CD   . PRO   C 1 20 ? 20.422  -34.990 11.382  1.00 23.83 ? 19  PRO   C CD   1 
ATOM   1633 N  N    . HIS   C 1 21 ? 23.169  -31.704 13.085  1.00 23.78 ? 20  HIS   C N    1 
ATOM   1634 C  CA   . HIS   C 1 21 ? 23.158  -30.772 14.208  1.00 20.72 ? 20  HIS   C CA   1 
ATOM   1635 C  C    . HIS   C 1 21 ? 21.755  -30.211 14.374  1.00 22.74 ? 20  HIS   C C    1 
ATOM   1636 O  O    . HIS   C 1 21 ? 21.213  -29.593 13.451  1.00 27.73 ? 20  HIS   C O    1 
ATOM   1637 C  CB   . HIS   C 1 21 ? 24.169  -29.652 13.981  1.00 27.28 ? 20  HIS   C CB   1 
ATOM   1638 C  CG   . HIS   C 1 21 ? 25.592  -30.113 14.010  1.00 31.76 ? 20  HIS   C CG   1 
ATOM   1639 N  ND1  . HIS   C 1 21 ? 26.178  -30.783 12.957  1.00 31.44 ? 20  HIS   C ND1  1 
ATOM   1640 C  CD2  . HIS   C 1 21 ? 26.542  -30.010 14.970  1.00 35.76 ? 20  HIS   C CD2  1 
ATOM   1641 C  CE1  . HIS   C 1 21 ? 27.432  -31.068 13.265  1.00 37.48 ? 20  HIS   C CE1  1 
ATOM   1642 N  NE2  . HIS   C 1 21 ? 27.677  -30.610 14.481  1.00 35.52 ? 20  HIS   C NE2  1 
ATOM   1643 N  N    . TRP   C 1 22 ? 21.155  -30.456 15.542  1.00 23.74 ? 21  TRP   C N    1 
ATOM   1644 C  CA   . TRP   C 1 22 ? 19.722  -30.298 15.720  1.00 25.93 ? 21  TRP   C CA   1 
ATOM   1645 C  C    . TRP   C 1 22 ? 19.394  -29.149 16.668  1.00 23.00 ? 21  TRP   C C    1 
ATOM   1646 O  O    . TRP   C 1 22 ? 19.976  -29.056 17.756  1.00 23.58 ? 21  TRP   C O    1 
ATOM   1647 C  CB   . TRP   C 1 22 ? 19.115  -31.586 16.275  1.00 25.73 ? 21  TRP   C CB   1 
ATOM   1648 C  CG   . TRP   C 1 22 ? 17.668  -31.741 15.974  1.00 25.02 ? 21  TRP   C CG   1 
ATOM   1649 C  CD1  . TRP   C 1 22 ? 16.627  -31.087 16.572  1.00 22.39 ? 21  TRP   C CD1  1 
ATOM   1650 C  CD2  . TRP   C 1 22 ? 17.089  -32.623 15.008  1.00 22.83 ? 21  TRP   C CD2  1 
ATOM   1651 N  NE1  . TRP   C 1 22 ? 15.433  -31.503 16.024  1.00 26.47 ? 21  TRP   C NE1  1 
ATOM   1652 C  CE2  . TRP   C 1 22 ? 15.693  -32.448 15.064  1.00 26.13 ? 21  TRP   C CE2  1 
ATOM   1653 C  CE3  . TRP   C 1 22 ? 17.618  -33.544 14.095  1.00 22.63 ? 21  TRP   C CE3  1 
ATOM   1654 C  CZ2  . TRP   C 1 22 ? 14.818  -33.161 14.244  1.00 27.37 ? 21  TRP   C CZ2  1 
ATOM   1655 C  CZ3  . TRP   C 1 22 ? 16.747  -34.252 13.283  1.00 23.75 ? 21  TRP   C CZ3  1 
ATOM   1656 C  CH2  . TRP   C 1 22 ? 15.364  -34.056 13.363  1.00 24.85 ? 21  TRP   C CH2  1 
ATOM   1657 N  N    . PRO   C 1 23 ? 18.441  -28.289 16.308  1.00 23.04 ? 22  PRO   C N    1 
ATOM   1658 C  CA   . PRO   C 1 23 ? 18.055  -27.198 17.213  1.00 22.42 ? 22  PRO   C CA   1 
ATOM   1659 C  C    . PRO   C 1 23 ? 17.489  -27.746 18.512  1.00 19.49 ? 22  PRO   C C    1 
ATOM   1660 O  O    . PRO   C 1 23 ? 16.599  -28.601 18.516  1.00 22.20 ? 22  PRO   C O    1 
ATOM   1661 C  CB   . PRO   C 1 23 ? 17.001  -26.424 16.411  1.00 28.92 ? 22  PRO   C CB   1 
ATOM   1662 C  CG   . PRO   C 1 23 ? 16.486  -27.417 15.410  1.00 22.64 ? 22  PRO   C CG   1 
ATOM   1663 C  CD   . PRO   C 1 23 ? 17.661  -28.270 15.058  1.00 24.99 ? 22  PRO   C CD   1 
ATOM   1664 N  N    . ALA   C 1 24 ? 18.018  -27.252 19.625  1.00 26.02 ? 23  ALA   C N    1 
ATOM   1665 C  CA   . ALA   C 1 24 ? 17.683  -27.821 20.921  1.00 25.22 ? 23  ALA   C CA   1 
ATOM   1666 C  C    . ALA   C 1 24 ? 17.899  -26.767 21.995  1.00 26.39 ? 23  ALA   C C    1 
ATOM   1667 O  O    . ALA   C 1 24 ? 18.408  -25.675 21.734  1.00 27.37 ? 23  ALA   C O    1 
ATOM   1668 C  CB   . ALA   C 1 24 ? 18.518  -29.074 21.204  1.00 26.56 ? 23  ALA   C CB   1 
ATOM   1669 N  N    . ARG   C 1 25 ? 17.500  -27.112 23.215  1.00 31.71 ? 24  ARG   C N    1 
ATOM   1670 C  CA   . ARG   C 1 25 ? 17.753  -26.263 24.367  1.00 29.95 ? 24  ARG   C CA   1 
ATOM   1671 C  C    . ARG   C 1 25 ? 18.219  -27.133 25.524  1.00 27.02 ? 24  ARG   C C    1 
ATOM   1672 O  O    . ARG   C 1 25 ? 17.925  -28.330 25.586  1.00 28.53 ? 24  ARG   C O    1 
ATOM   1673 C  CB   . ARG   C 1 25 ? 16.511  -25.459 24.774  1.00 30.43 ? 24  ARG   C CB   1 
ATOM   1674 C  CG   . ARG   C 1 25 ? 15.322  -26.303 25.208  1.00 35.91 ? 24  ARG   C CG   1 
ATOM   1675 C  CD   . ARG   C 1 25 ? 14.277  -25.447 25.922  1.00 39.00 ? 24  ARG   C CD   1 
ATOM   1676 N  NE   . ARG   C 1 25 ? 13.158  -26.248 26.402  1.00 44.90 ? 24  ARG   C NE   1 
ATOM   1677 C  CZ   . ARG   C 1 25 ? 11.884  -26.025 26.109  1.00 47.45 ? 24  ARG   C CZ   1 
ATOM   1678 N  NH1  . ARG   C 1 25 ? 11.514  -24.997 25.362  1.00 42.64 ? 24  ARG   C NH1  1 
ATOM   1679 N  NH2  . ARG   C 1 25 ? 10.955  -26.848 26.590  1.00 43.11 ? 24  ARG   C NH2  1 
ATOM   1680 N  N    . ILE   C 1 26 ? 18.955  -26.511 26.439  1.00 28.74 ? 25  ILE   C N    1 
ATOM   1681 C  CA   . ILE   C 1 26 ? 19.372  -27.172 27.670  1.00 33.55 ? 25  ILE   C CA   1 
ATOM   1682 C  C    . ILE   C 1 26 ? 18.180  -27.247 28.614  1.00 40.10 ? 25  ILE   C C    1 
ATOM   1683 O  O    . ILE   C 1 26 ? 17.507  -26.240 28.868  1.00 43.44 ? 25  ILE   C O    1 
ATOM   1684 C  CB   . ILE   C 1 26 ? 20.545  -26.423 28.322  1.00 33.94 ? 25  ILE   C CB   1 
ATOM   1685 C  CG1  . ILE   C 1 26 ? 21.694  -26.237 27.329  1.00 31.64 ? 25  ILE   C CG1  1 
ATOM   1686 C  CG2  . ILE   C 1 26 ? 21.028  -27.160 29.563  1.00 37.16 ? 25  ILE   C CG2  1 
ATOM   1687 C  CD1  . ILE   C 1 26 ? 22.406  -27.513 26.964  1.00 35.05 ? 25  ILE   C CD1  1 
ATOM   1688 N  N    . ASP   C 1 27 ? 17.904  -28.441 29.124  1.00 35.69 ? 26  ASP   C N    1 
ATOM   1689 C  CA   . ASP   C 1 27 ? 16.883  -28.612 30.143  1.00 43.05 ? 26  ASP   C CA   1 
ATOM   1690 C  C    . ASP   C 1 27 ? 17.515  -28.563 31.532  1.00 47.31 ? 26  ASP   C C    1 
ATOM   1691 O  O    . ASP   C 1 27 ? 18.737  -28.564 31.692  1.00 51.35 ? 26  ASP   C O    1 
ATOM   1692 C  CB   . ASP   C 1 27 ? 16.132  -29.931 29.946  1.00 39.26 ? 26  ASP   C CB   1 
ATOM   1693 C  CG   . ASP   C 1 27 ? 14.839  -29.760 29.170  1.00 53.90 ? 26  ASP   C CG   1 
ATOM   1694 O  OD1  . ASP   C 1 27 ? 14.633  -28.682 28.571  1.00 51.27 ? 26  ASP   C OD1  1 
ATOM   1695 O  OD2  . ASP   C 1 27 ? 14.023  -30.707 29.168  1.00 47.79 ? 26  ASP   C OD2  1 
ATOM   1696 N  N    . ASP   C 1 28 ? 16.660  -28.515 32.547  1.00 52.56 ? 27  ASP   C N    1 
ATOM   1697 C  CA   . ASP   C 1 28 ? 17.092  -28.596 33.932  1.00 54.06 ? 27  ASP   C CA   1 
ATOM   1698 C  C    . ASP   C 1 28 ? 16.747  -29.971 34.485  1.00 61.24 ? 27  ASP   C C    1 
ATOM   1699 O  O    . ASP   C 1 28 ? 15.781  -30.608 34.053  1.00 57.57 ? 27  ASP   C O    1 
ATOM   1700 C  CB   . ASP   C 1 28 ? 16.438  -27.503 34.785  1.00 66.22 ? 27  ASP   C CB   1 
ATOM   1701 C  CG   . ASP   C 1 28 ? 17.179  -27.257 36.090  1.00 71.17 ? 27  ASP   C CG   1 
ATOM   1702 O  OD1  . ASP   C 1 28 ? 18.114  -28.024 36.404  1.00 57.88 ? 27  ASP   C OD1  1 
ATOM   1703 O  OD2  . ASP   C 1 28 ? 16.829  -26.289 36.798  1.00 64.48 ? 27  ASP   C OD2  1 
ATOM   1704 N  N    . ILE   C 1 29 ? 17.551  -30.431 35.437  1.00 56.71 ? 28  ILE   C N    1 
ATOM   1705 C  CA   . ILE   C 1 29 ? 17.317  -31.709 36.098  1.00 62.58 ? 28  ILE   C CA   1 
ATOM   1706 C  C    . ILE   C 1 29 ? 16.365  -31.479 37.263  1.00 66.41 ? 28  ILE   C C    1 
ATOM   1707 O  O    . ILE   C 1 29 ? 16.665  -30.706 38.180  1.00 69.51 ? 28  ILE   C O    1 
ATOM   1708 C  CB   . ILE   C 1 29 ? 18.632  -32.343 36.575  1.00 62.59 ? 28  ILE   C CB   1 
ATOM   1709 C  CG1  . ILE   C 1 29 ? 19.394  -32.939 35.390  1.00 62.23 ? 28  ILE   C CG1  1 
ATOM   1710 C  CG2  . ILE   C 1 29 ? 18.362  -33.419 37.620  1.00 57.57 ? 28  ILE   C CG2  1 
ATOM   1711 C  CD1  . ILE   C 1 29 ? 18.652  -34.067 34.699  1.00 60.30 ? 28  ILE   C CD1  1 
ATOM   1712 N  N    . ALA   C 1 30 ? 15.209  -32.137 37.220  1.00 61.69 ? 29  ALA   C N    1 
ATOM   1713 C  CA   . ALA   C 1 30 ? 14.282  -32.083 38.340  1.00 61.32 ? 29  ALA   C CA   1 
ATOM   1714 C  C    . ALA   C 1 30 ? 14.900  -32.778 39.546  1.00 64.84 ? 29  ALA   C C    1 
ATOM   1715 O  O    . ALA   C 1 30 ? 15.389  -33.907 39.440  1.00 54.69 ? 29  ALA   C O    1 
ATOM   1716 C  CB   . ALA   C 1 30 ? 12.954  -32.738 37.966  1.00 54.45 ? 29  ALA   C CB   1 
ATOM   1717 N  N    . ASP   C 1 31 ? 14.901  -32.094 40.688  1.00 56.29 ? 30  ASP   C N    1 
ATOM   1718 C  CA   . ASP   C 1 31 ? 15.468  -32.672 41.899  1.00 62.87 ? 30  ASP   C CA   1 
ATOM   1719 C  C    . ASP   C 1 31 ? 14.714  -33.943 42.266  1.00 54.85 ? 30  ASP   C C    1 
ATOM   1720 O  O    . ASP   C 1 31 ? 13.492  -33.924 42.444  1.00 55.27 ? 30  ASP   C O    1 
ATOM   1721 C  CB   . ASP   C 1 31 ? 15.416  -31.662 43.045  1.00 57.54 ? 30  ASP   C CB   1 
ATOM   1722 C  CG   . ASP   C 1 31 ? 16.510  -31.889 44.072  1.00 64.90 ? 30  ASP   C CG   1 
ATOM   1723 O  OD1  . ASP   C 1 31 ? 17.674  -31.530 43.790  1.00 72.75 ? 30  ASP   C OD1  1 
ATOM   1724 O  OD2  . ASP   C 1 31 ? 16.209  -32.427 45.159  1.00 67.63 ? 30  ASP   C OD2  1 
ATOM   1725 N  N    . GLY   C 1 32 ? 15.443  -35.052 42.357  1.00 59.19 ? 31  GLY   C N    1 
ATOM   1726 C  CA   . GLY   C 1 32 ? 14.852  -36.351 42.587  1.00 61.77 ? 31  GLY   C CA   1 
ATOM   1727 C  C    . GLY   C 1 32 ? 14.766  -37.229 41.358  1.00 63.72 ? 31  GLY   C C    1 
ATOM   1728 O  O    . GLY   C 1 32 ? 14.548  -38.439 41.497  1.00 50.74 ? 31  GLY   C O    1 
ATOM   1729 N  N    . ALA   C 1 33 ? 14.926  -36.662 40.166  1.00 59.63 ? 32  ALA   C N    1 
ATOM   1730 C  CA   . ALA   C 1 33 ? 14.940  -37.452 38.947  1.00 55.81 ? 32  ALA   C CA   1 
ATOM   1731 C  C    . ALA   C 1 33 ? 16.295  -38.135 38.774  1.00 63.43 ? 32  ALA   C C    1 
ATOM   1732 O  O    . ALA   C 1 33 ? 17.255  -37.867 39.502  1.00 59.82 ? 32  ALA   C O    1 
ATOM   1733 C  CB   . ALA   C 1 33 ? 14.623  -36.577 37.735  1.00 56.19 ? 32  ALA   C CB   1 
ATOM   1734 N  N    . VAL   C 1 34 ? 16.365  -39.033 37.791  1.00 58.78 ? 33  VAL   C N    1 
ATOM   1735 C  CA   . VAL   C 1 34 ? 17.605  -39.753 37.524  1.00 68.22 ? 33  VAL   C CA   1 
ATOM   1736 C  C    . VAL   C 1 34 ? 18.664  -38.769 37.048  1.00 71.39 ? 33  VAL   C C    1 
ATOM   1737 O  O    . VAL   C 1 34 ? 18.412  -37.931 36.172  1.00 58.62 ? 33  VAL   C O    1 
ATOM   1738 C  CB   . VAL   C 1 34 ? 17.376  -40.871 36.495  1.00 68.34 ? 33  VAL   C CB   1 
ATOM   1739 C  CG1  . VAL   C 1 34 ? 18.705  -41.488 36.069  1.00 71.91 ? 33  VAL   C CG1  1 
ATOM   1740 C  CG2  . VAL   C 1 34 ? 16.454  -41.937 37.069  1.00 68.43 ? 33  VAL   C CG2  1 
ATOM   1741 N  N    . LYS   C 1 35 ? 19.853  -38.861 37.635  1.00 70.37 ? 34  LYS   C N    1 
ATOM   1742 C  CA   . LYS   C 1 35 ? 20.926  -37.954 37.274  1.00 68.10 ? 34  LYS   C CA   1 
ATOM   1743 C  C    . LYS   C 1 35 ? 21.490  -38.323 35.904  1.00 62.72 ? 34  LYS   C C    1 
ATOM   1744 O  O    . LYS   C 1 35 ? 21.512  -39.499 35.527  1.00 59.25 ? 34  LYS   C O    1 
ATOM   1745 C  CB   . LYS   C 1 35 ? 22.036  -37.990 38.323  1.00 70.00 ? 34  LYS   C CB   1 
ATOM   1746 C  CG   . LYS   C 1 35 ? 21.537  -37.834 39.749  1.00 71.56 ? 34  LYS   C CG   1 
ATOM   1747 C  CD   . LYS   C 1 35 ? 20.616  -36.632 39.881  1.00 69.53 ? 34  LYS   C CD   1 
ATOM   1748 C  CE   . LYS   C 1 35 ? 19.831  -36.681 41.181  1.00 71.42 ? 34  LYS   C CE   1 
ATOM   1749 N  NZ   . LYS   C 1 35 ? 18.738  -35.669 41.205  1.00 67.34 ? 34  LYS   C NZ   1 
ATOM   1750 N  N    . PRO   C 1 36 ? 21.940  -37.337 35.136  1.00 52.60 ? 35  PRO   C N    1 
ATOM   1751 C  CA   . PRO   C 1 36 ? 22.605  -37.632 33.867  1.00 51.79 ? 35  PRO   C CA   1 
ATOM   1752 C  C    . PRO   C 1 36 ? 23.914  -38.355 34.118  1.00 54.01 ? 35  PRO   C C    1 
ATOM   1753 O  O    . PRO   C 1 36 ? 24.433  -38.331 35.245  1.00 48.11 ? 35  PRO   C O    1 
ATOM   1754 C  CB   . PRO   C 1 36 ? 22.849  -36.241 33.258  1.00 54.09 ? 35  PRO   C CB   1 
ATOM   1755 C  CG   . PRO   C 1 36 ? 22.007  -35.292 34.059  1.00 52.16 ? 35  PRO   C CG   1 
ATOM   1756 C  CD   . PRO   C 1 36 ? 21.894  -35.893 35.417  1.00 55.86 ? 35  PRO   C CD   1 
ATOM   1757 N  N    . PRO   C 1 37 ? 24.473  -39.016 33.110  1.00 52.87 ? 36  PRO   C N    1 
ATOM   1758 C  CA   . PRO   C 1 37 ? 25.847  -39.506 33.227  1.00 50.78 ? 36  PRO   C CA   1 
ATOM   1759 C  C    . PRO   C 1 37 ? 26.785  -38.356 33.544  1.00 45.47 ? 36  PRO   C C    1 
ATOM   1760 O  O    . PRO   C 1 37 ? 26.453  -37.191 33.278  1.00 42.09 ? 36  PRO   C O    1 
ATOM   1761 C  CB   . PRO   C 1 37 ? 26.132  -40.100 31.839  1.00 46.09 ? 36  PRO   C CB   1 
ATOM   1762 C  CG   . PRO   C 1 37 ? 24.785  -40.467 31.310  1.00 48.47 ? 36  PRO   C CG   1 
ATOM   1763 C  CD   . PRO   C 1 37 ? 23.846  -39.418 31.839  1.00 47.48 ? 36  PRO   C CD   1 
ATOM   1764 N  N    . PRO   C 1 38 ? 27.945  -38.634 34.134  1.00 44.92 ? 37  PRO   C N    1 
ATOM   1765 C  CA   . PRO   C 1 38 ? 28.869  -37.551 34.493  1.00 49.82 ? 37  PRO   C CA   1 
ATOM   1766 C  C    . PRO   C 1 38 ? 29.188  -36.654 33.306  1.00 44.96 ? 37  PRO   C C    1 
ATOM   1767 O  O    . PRO   C 1 38 ? 29.458  -37.127 32.198  1.00 40.24 ? 37  PRO   C O    1 
ATOM   1768 C  CB   . PRO   C 1 38 ? 30.108  -38.302 34.988  1.00 51.40 ? 37  PRO   C CB   1 
ATOM   1769 C  CG   . PRO   C 1 38 ? 29.560  -39.583 35.525  1.00 48.89 ? 37  PRO   C CG   1 
ATOM   1770 C  CD   . PRO   C 1 38 ? 28.414  -39.945 34.620  1.00 47.76 ? 37  PRO   C CD   1 
ATOM   1771 N  N    . ASN   C 1 39 ? 29.118  -35.341 33.546  1.00 42.53 ? 38  ASN   C N    1 
ATOM   1772 C  CA   . ASN   C 1 39 ? 29.473  -34.315 32.564  1.00 38.77 ? 38  ASN   C CA   1 
ATOM   1773 C  C    . ASN   C 1 39 ? 28.552  -34.333 31.347  1.00 40.18 ? 38  ASN   C C    1 
ATOM   1774 O  O    . ASN   C 1 39 ? 28.979  -34.024 30.231  1.00 41.66 ? 38  ASN   C O    1 
ATOM   1775 C  CB   . ASN   C 1 39 ? 30.938  -34.444 32.132  1.00 41.39 ? 38  ASN   C CB   1 
ATOM   1776 C  CG   . ASN   C 1 39 ? 31.497  -33.150 31.570  1.00 47.41 ? 38  ASN   C CG   1 
ATOM   1777 O  OD1  . ASN   C 1 39 ? 31.051  -32.061 31.934  1.00 49.58 ? 38  ASN   C OD1  1 
ATOM   1778 N  ND2  . ASN   C 1 39 ? 32.470  -33.263 30.671  1.00 49.33 ? 38  ASN   C ND2  1 
ATOM   1779 N  N    . LYS   C 1 40 ? 27.282  -34.683 31.546  1.00 37.36 ? 39  LYS   C N    1 
ATOM   1780 C  CA   . LYS   C 1 40 ? 26.285  -34.656 30.484  1.00 39.25 ? 39  LYS   C CA   1 
ATOM   1781 C  C    . LYS   C 1 40 ? 25.166  -33.691 30.850  1.00 34.45 ? 39  LYS   C C    1 
ATOM   1782 O  O    . LYS   C 1 40 ? 24.811  -33.543 32.023  1.00 36.94 ? 39  LYS   C O    1 
ATOM   1783 C  CB   . LYS   C 1 40 ? 25.694  -36.047 30.229  1.00 34.82 ? 39  LYS   C CB   1 
ATOM   1784 C  CG   . LYS   C 1 40 ? 26.717  -37.098 29.833  1.00 38.96 ? 39  LYS   C CG   1 
ATOM   1785 C  CD   . LYS   C 1 40 ? 26.721  -37.338 28.334  1.00 44.55 ? 39  LYS   C CD   1 
ATOM   1786 C  CE   . LYS   C 1 40 ? 27.842  -38.290 27.931  1.00 45.79 ? 39  LYS   C CE   1 
ATOM   1787 N  NZ   . LYS   C 1 40 ? 29.178  -37.677 28.178  1.00 47.50 ? 39  LYS   C NZ   1 
ATOM   1788 N  N    . TYR   C 1 41 ? 24.594  -33.026 29.808  1.00 30.87 ? 40  TYR   C N    1 
ATOM   1789 C  CA   . TYR   C 1 41 ? 23.486  -32.088 29.924  1.00 34.14 ? 40  TYR   C CA   1 
ATOM   1790 C  C    . TYR   C 1 41 ? 22.176  -32.744 29.507  1.00 37.34 ? 40  TYR   C C    1 
ATOM   1791 O  O    . TYR   C 1 41 ? 22.151  -33.568 28.588  1.00 34.44 ? 40  TYR   C O    1 
ATOM   1792 C  CB   . TYR   C 1 41 ? 23.710  -30.860 29.035  1.00 30.65 ? 40  TYR   C CB   1 
ATOM   1793 C  CG   . TYR   C 1 41 ? 24.886  -29.990 29.409  1.00 35.32 ? 40  TYR   C CG   1 
ATOM   1794 C  CD1  . TYR   C 1 41 ? 26.151  -30.238 28.892  1.00 37.87 ? 40  TYR   C CD1  1 
ATOM   1795 C  CD2  . TYR   C 1 41 ? 24.724  -28.901 30.253  1.00 33.67 ? 40  TYR   C CD2  1 
ATOM   1796 C  CE1  . TYR   C 1 41 ? 27.226  -29.435 29.219  1.00 38.21 ? 40  TYR   C CE1  1 
ATOM   1797 C  CE2  . TYR   C 1 41 ? 25.792  -28.093 30.587  1.00 37.57 ? 40  TYR   C CE2  1 
ATOM   1798 C  CZ   . TYR   C 1 41 ? 27.040  -28.364 30.068  1.00 38.81 ? 40  TYR   C CZ   1 
ATOM   1799 O  OH   . TYR   C 1 41 ? 28.109  -27.563 30.396  1.00 49.30 ? 40  TYR   C OH   1 
ATOM   1800 N  N    . PRO   C 1 42 ? 21.061  -32.387 30.147  1.00 34.84 ? 41  PRO   C N    1 
ATOM   1801 C  CA   . PRO   C 1 42 ? 19.749  -32.819 29.645  1.00 30.10 ? 41  PRO   C CA   1 
ATOM   1802 C  C    . PRO   C 1 42 ? 19.356  -31.946 28.464  1.00 31.68 ? 41  PRO   C C    1 
ATOM   1803 O  O    . PRO   C 1 42 ? 19.316  -30.719 28.577  1.00 34.40 ? 41  PRO   C O    1 
ATOM   1804 C  CB   . PRO   C 1 42 ? 18.815  -32.603 30.845  1.00 33.23 ? 41  PRO   C CB   1 
ATOM   1805 C  CG   . PRO   C 1 42 ? 19.652  -31.937 31.918  1.00 43.34 ? 41  PRO   C CG   1 
ATOM   1806 C  CD   . PRO   C 1 42 ? 20.931  -31.484 31.299  1.00 39.31 ? 41  PRO   C CD   1 
ATOM   1807 N  N    . ILE   C 1 43 ? 19.080  -32.577 27.328  1.00 30.72 ? 42  ILE   C N    1 
ATOM   1808 C  CA   . ILE   C 1 43 ? 18.794  -31.873 26.083  1.00 28.71 ? 42  ILE   C CA   1 
ATOM   1809 C  C    . ILE   C 1 43 ? 17.333  -32.083 25.717  1.00 28.97 ? 42  ILE   C C    1 
ATOM   1810 O  O    . ILE   C 1 43 ? 16.792  -33.184 25.873  1.00 32.96 ? 42  ILE   C O    1 
ATOM   1811 C  CB   . ILE   C 1 43 ? 19.716  -32.350 24.943  1.00 29.58 ? 42  ILE   C CB   1 
ATOM   1812 C  CG1  . ILE   C 1 43 ? 21.181  -32.148 25.326  1.00 30.95 ? 42  ILE   C CG1  1 
ATOM   1813 C  CG2  . ILE   C 1 43 ? 19.410  -31.605 23.647  1.00 24.76 ? 42  ILE   C CG2  1 
ATOM   1814 C  CD1  . ILE   C 1 43 ? 21.528  -30.715 25.647  1.00 33.14 ? 42  ILE   C CD1  1 
ATOM   1815 N  N    . PHE   C 1 44 ? 16.695  -31.016 25.242  1.00 30.13 ? 43  PHE   C N    1 
ATOM   1816 C  CA   . PHE   C 1 44 ? 15.354  -31.070 24.674  1.00 30.23 ? 43  PHE   C CA   1 
ATOM   1817 C  C    . PHE   C 1 44 ? 15.455  -30.663 23.211  1.00 25.95 ? 43  PHE   C C    1 
ATOM   1818 O  O    . PHE   C 1 44 ? 15.898  -29.552 22.907  1.00 33.25 ? 43  PHE   C O    1 
ATOM   1819 C  CB   . PHE   C 1 44 ? 14.396  -30.145 25.430  1.00 35.03 ? 43  PHE   C CB   1 
ATOM   1820 C  CG   . PHE   C 1 44 ? 13.037  -30.023 24.794  1.00 29.83 ? 43  PHE   C CG   1 
ATOM   1821 C  CD1  . PHE   C 1 44 ? 12.036  -30.935 25.086  1.00 33.78 ? 43  PHE   C CD1  1 
ATOM   1822 C  CD2  . PHE   C 1 44 ? 12.759  -28.992 23.909  1.00 35.13 ? 43  PHE   C CD2  1 
ATOM   1823 C  CE1  . PHE   C 1 44 ? 10.784  -30.826 24.504  1.00 36.86 ? 43  PHE   C CE1  1 
ATOM   1824 C  CE2  . PHE   C 1 44 ? 11.511  -28.879 23.323  1.00 35.56 ? 43  PHE   C CE2  1 
ATOM   1825 C  CZ   . PHE   C 1 44 ? 10.521  -29.799 23.623  1.00 44.10 ? 43  PHE   C CZ   1 
ATOM   1826 N  N    . PHE   C 1 45 ? 15.044  -31.556 22.314  1.00 29.14 ? 44  PHE   C N    1 
ATOM   1827 C  CA   . PHE   C 1 45 ? 15.159  -31.324 20.879  1.00 27.11 ? 44  PHE   C CA   1 
ATOM   1828 C  C    . PHE   C 1 45 ? 13.897  -30.644 20.361  1.00 30.66 ? 44  PHE   C C    1 
ATOM   1829 O  O    . PHE   C 1 45 ? 12.795  -31.190 20.491  1.00 31.68 ? 44  PHE   C O    1 
ATOM   1830 C  CB   . PHE   C 1 45 ? 15.400  -32.642 20.143  1.00 27.22 ? 44  PHE   C CB   1 
ATOM   1831 C  CG   . PHE   C 1 45 ? 16.703  -33.301 20.494  1.00 27.40 ? 44  PHE   C CG   1 
ATOM   1832 C  CD1  . PHE   C 1 45 ? 17.885  -32.887 19.905  1.00 29.73 ? 44  PHE   C CD1  1 
ATOM   1833 C  CD2  . PHE   C 1 45 ? 16.743  -34.342 21.407  1.00 28.16 ? 44  PHE   C CD2  1 
ATOM   1834 C  CE1  . PHE   C 1 45 ? 19.086  -33.498 20.226  1.00 33.16 ? 44  PHE   C CE1  1 
ATOM   1835 C  CE2  . PHE   C 1 45 ? 17.939  -34.956 21.731  1.00 28.44 ? 44  PHE   C CE2  1 
ATOM   1836 C  CZ   . PHE   C 1 45 ? 19.110  -34.535 21.141  1.00 27.66 ? 44  PHE   C CZ   1 
ATOM   1837 N  N    . PHE   C 1 46 ? 14.058  -29.460 19.771  1.00 26.24 ? 45  PHE   C N    1 
ATOM   1838 C  CA   . PHE   C 1 46 ? 12.927  -28.796 19.133  1.00 25.85 ? 45  PHE   C CA   1 
ATOM   1839 C  C    . PHE   C 1 46 ? 12.419  -29.619 17.953  1.00 28.05 ? 45  PHE   C C    1 
ATOM   1840 O  O    . PHE   C 1 46 ? 13.153  -30.406 17.350  1.00 27.96 ? 45  PHE   C O    1 
ATOM   1841 C  CB   . PHE   C 1 46 ? 13.318  -27.395 18.663  1.00 30.14 ? 45  PHE   C CB   1 
ATOM   1842 C  CG   . PHE   C 1 46 ? 13.570  -26.422 19.782  1.00 28.58 ? 45  PHE   C CG   1 
ATOM   1843 C  CD1  . PHE   C 1 46 ? 12.527  -25.970 20.577  1.00 31.65 ? 45  PHE   C CD1  1 
ATOM   1844 C  CD2  . PHE   C 1 46 ? 14.842  -25.939 20.021  1.00 24.54 ? 45  PHE   C CD2  1 
ATOM   1845 C  CE1  . PHE   C 1 46 ? 12.756  -25.072 21.598  1.00 30.08 ? 45  PHE   C CE1  1 
ATOM   1846 C  CE2  . PHE   C 1 46 ? 15.076  -25.038 21.041  1.00 24.62 ? 45  PHE   C CE2  1 
ATOM   1847 C  CZ   . PHE   C 1 46 ? 14.033  -24.606 21.829  1.00 26.77 ? 45  PHE   C CZ   1 
ATOM   1848 N  N    . GLY   C 1 47 ? 11.142  -29.430 17.628  1.00 27.59 ? 46  GLY   C N    1 
ATOM   1849 C  CA   . GLY   C 1 47 ? 10.528  -30.150 16.531  1.00 31.55 ? 46  GLY   C CA   1 
ATOM   1850 C  C    . GLY   C 1 47 ? 10.023  -31.521 16.931  1.00 34.45 ? 46  GLY   C C    1 
ATOM   1851 O  O    . GLY   C 1 47 ? 8.821   -31.793 16.856  1.00 38.73 ? 46  GLY   C O    1 
ATOM   1852 N  N    . THR   C 1 48 ? 10.935  -32.400 17.353  1.00 32.87 ? 47  THR   C N    1 
ATOM   1853 C  CA   . THR   C 1 48 ? 10.544  -33.732 17.797  1.00 32.98 ? 47  THR   C CA   1 
ATOM   1854 C  C    . THR   C 1 48 ? 10.091  -33.753 19.248  1.00 34.82 ? 47  THR   C C    1 
ATOM   1855 O  O    . THR   C 1 48 ? 9.361   -34.671 19.640  1.00 35.51 ? 47  THR   C O    1 
ATOM   1856 C  CB   . THR   C 1 48 ? 11.704  -34.717 17.633  1.00 35.05 ? 47  THR   C CB   1 
ATOM   1857 O  OG1  . THR   C 1 48 ? 12.768  -34.340 18.515  1.00 33.66 ? 47  THR   C OG1  1 
ATOM   1858 C  CG2  . THR   C 1 48 ? 12.207  -34.720 16.202  1.00 33.11 ? 47  THR   C CG2  1 
ATOM   1859 N  N    . HIS   C 1 49 ? 10.515  -32.772 20.047  1.00 31.02 ? 48  HIS   C N    1 
ATOM   1860 C  CA   . HIS   C 1 49 ? 10.180  -32.697 21.470  1.00 37.11 ? 48  HIS   C CA   1 
ATOM   1861 C  C    . HIS   C 1 49 ? 10.703  -33.906 22.238  1.00 37.47 ? 48  HIS   C C    1 
ATOM   1862 O  O    . HIS   C 1 49 ? 10.163  -34.267 23.287  1.00 36.30 ? 48  HIS   C O    1 
ATOM   1863 C  CB   . HIS   C 1 49 ? 8.672   -32.538 21.682  1.00 37.85 ? 48  HIS   C CB   1 
ATOM   1864 C  CG   . HIS   C 1 49 ? 8.049   -31.496 20.806  1.00 47.47 ? 48  HIS   C CG   1 
ATOM   1865 N  ND1  . HIS   C 1 49 ? 8.613   -30.253 20.615  1.00 41.53 ? 48  HIS   C ND1  1 
ATOM   1866 C  CD2  . HIS   C 1 49 ? 6.923   -31.519 20.055  1.00 50.24 ? 48  HIS   C CD2  1 
ATOM   1867 C  CE1  . HIS   C 1 49 ? 7.854   -29.551 19.793  1.00 39.86 ? 48  HIS   C CE1  1 
ATOM   1868 N  NE2  . HIS   C 1 49 ? 6.823   -30.297 19.437  1.00 54.83 ? 48  HIS   C NE2  1 
ATOM   1869 N  N    . GLU   C 1 50 ? 11.755  -34.538 21.725  1.00 31.85 ? 49  GLU   C N    1 
ATOM   1870 C  CA   . GLU   C 1 50 ? 12.388  -35.657 22.405  1.00 34.13 ? 49  GLU   C CA   1 
ATOM   1871 C  C    . GLU   C 1 50 ? 13.511  -35.155 23.312  1.00 31.88 ? 49  GLU   C C    1 
ATOM   1872 O  O    . GLU   C 1 50 ? 13.844  -33.971 23.333  1.00 33.20 ? 49  GLU   C O    1 
ATOM   1873 C  CB   . GLU   C 1 50 ? 12.909  -36.670 21.389  1.00 32.84 ? 49  GLU   C CB   1 
ATOM   1874 C  CG   . GLU   C 1 50 ? 11.804  -37.285 20.540  1.00 34.00 ? 49  GLU   C CG   1 
ATOM   1875 C  CD   . GLU   C 1 50 ? 12.330  -38.168 19.431  1.00 40.19 ? 49  GLU   C CD   1 
ATOM   1876 O  OE1  . GLU   C 1 50 ? 13.565  -38.238 19.251  1.00 39.25 ? 49  GLU   C OE1  1 
ATOM   1877 O  OE2  . GLU   C 1 50 ? 11.504  -38.795 18.737  1.00 51.88 ? 49  GLU   C OE2  1 
ATOM   1878 N  N    . THR   C 1 51 ? 14.084  -36.073 24.088  1.00 37.47 ? 50  THR   C N    1 
ATOM   1879 C  CA   . THR   C 1 51 ? 15.112  -35.732 25.061  1.00 30.19 ? 50  THR   C CA   1 
ATOM   1880 C  C    . THR   C 1 51 ? 16.271  -36.714 24.968  1.00 30.92 ? 50  THR   C C    1 
ATOM   1881 O  O    . THR   C 1 51 ? 16.130  -37.835 24.470  1.00 32.45 ? 50  THR   C O    1 
ATOM   1882 C  CB   . THR   C 1 51 ? 14.563  -35.727 26.498  1.00 34.74 ? 50  THR   C CB   1 
ATOM   1883 O  OG1  . THR   C 1 51 ? 13.913  -36.976 26.767  1.00 34.93 ? 50  THR   C OG1  1 
ATOM   1884 C  CG2  . THR   C 1 51 ? 13.581  -34.582 26.701  1.00 37.98 ? 50  THR   C CG2  1 
ATOM   1885 N  N    . ALA   C 1 52 ? 17.425  -36.271 25.459  1.00 30.05 ? 51  ALA   C N    1 
ATOM   1886 C  CA   . ALA   C 1 52 ? 18.616  -37.106 25.559  1.00 32.06 ? 51  ALA   C CA   1 
ATOM   1887 C  C    . ALA   C 1 52 ? 19.614  -36.402 26.469  1.00 33.73 ? 51  ALA   C C    1 
ATOM   1888 O  O    . ALA   C 1 52 ? 19.405  -35.261 26.886  1.00 34.56 ? 51  ALA   C O    1 
ATOM   1889 C  CB   . ALA   C 1 52 ? 19.222  -37.386 24.180  1.00 32.83 ? 51  ALA   C CB   1 
ATOM   1890 N  N    . PHE   C 1 53 ? 20.710  -37.096 26.771  1.00 40.19 ? 52  PHE   C N    1 
ATOM   1891 C  CA   . PHE   C 1 53 ? 21.838  -36.534 27.503  1.00 31.72 ? 52  PHE   C CA   1 
ATOM   1892 C  C    . PHE   C 1 53 ? 23.022  -36.393 26.556  1.00 35.95 ? 52  PHE   C C    1 
ATOM   1893 O  O    . PHE   C 1 53 ? 23.331  -37.324 25.804  1.00 34.70 ? 52  PHE   C O    1 
ATOM   1894 C  CB   . PHE   C 1 53 ? 22.224  -37.417 28.695  1.00 34.80 ? 52  PHE   C CB   1 
ATOM   1895 C  CG   . PHE   C 1 53 ? 21.232  -37.393 29.821  1.00 34.66 ? 52  PHE   C CG   1 
ATOM   1896 C  CD1  . PHE   C 1 53 ? 20.767  -38.576 30.377  1.00 44.04 ? 52  PHE   C CD1  1 
ATOM   1897 C  CD2  . PHE   C 1 53 ? 20.778  -36.192 30.340  1.00 36.40 ? 52  PHE   C CD2  1 
ATOM   1898 C  CE1  . PHE   C 1 53 ? 19.855  -38.558 31.422  1.00 43.89 ? 52  PHE   C CE1  1 
ATOM   1899 C  CE2  . PHE   C 1 53 ? 19.867  -36.169 31.381  1.00 42.67 ? 52  PHE   C CE2  1 
ATOM   1900 C  CZ   . PHE   C 1 53 ? 19.406  -37.350 31.922  1.00 40.22 ? 52  PHE   C CZ   1 
ATOM   1901 N  N    . LEU   C 1 54 ? 23.689  -35.241 26.600  1.00 28.54 ? 53  LEU   C N    1 
ATOM   1902 C  CA   . LEU   C 1 54 ? 24.807  -34.969 25.709  1.00 36.12 ? 53  LEU   C CA   1 
ATOM   1903 C  C    . LEU   C 1 54 ? 25.908  -34.231 26.455  1.00 33.48 ? 53  LEU   C C    1 
ATOM   1904 O  O    . LEU   C 1 54 ? 25.643  -33.422 27.346  1.00 36.85 ? 53  LEU   C O    1 
ATOM   1905 C  CB   . LEU   C 1 54 ? 24.375  -34.139 24.493  1.00 35.12 ? 53  LEU   C CB   1 
ATOM   1906 C  CG   . LEU   C 1 54 ? 23.893  -34.929 23.283  1.00 44.04 ? 53  LEU   C CG   1 
ATOM   1907 C  CD1  . LEU   C 1 54 ? 23.429  -33.991 22.179  1.00 31.97 ? 53  LEU   C CD1  1 
ATOM   1908 C  CD2  . LEU   C 1 54 ? 25.005  -35.848 22.788  1.00 42.26 ? 53  LEU   C CD2  1 
ATOM   1909 N  N    . GLY   C 1 55 ? 27.150  -34.513 26.069  1.00 34.19 ? 54  GLY   C N    1 
ATOM   1910 C  CA   . GLY   C 1 55 ? 28.294  -33.820 26.609  1.00 36.16 ? 54  GLY   C CA   1 
ATOM   1911 C  C    . GLY   C 1 55 ? 28.588  -32.550 25.837  1.00 39.87 ? 54  GLY   C C    1 
ATOM   1912 O  O    . GLY   C 1 55 ? 28.100  -32.348 24.719  1.00 36.71 ? 54  GLY   C O    1 
ATOM   1913 N  N    . PRO   C 1 56 ? 29.402  -31.667 26.422  1.00 37.46 ? 55  PRO   C N    1 
ATOM   1914 C  CA   . PRO   C 1 56 ? 29.656  -30.365 25.781  1.00 43.56 ? 55  PRO   C CA   1 
ATOM   1915 C  C    . PRO   C 1 56 ? 30.305  -30.468 24.412  1.00 36.06 ? 55  PRO   C C    1 
ATOM   1916 O  O    . PRO   C 1 56 ? 30.146  -29.547 23.602  1.00 44.53 ? 55  PRO   C O    1 
ATOM   1917 C  CB   . PRO   C 1 56 ? 30.570  -29.649 26.787  1.00 45.92 ? 55  PRO   C CB   1 
ATOM   1918 C  CG   . PRO   C 1 56 ? 31.169  -30.747 27.615  1.00 38.25 ? 55  PRO   C CG   1 
ATOM   1919 C  CD   . PRO   C 1 56 ? 30.110  -31.801 27.706  1.00 36.13 ? 55  PRO   C CD   1 
ATOM   1920 N  N    . LYS   C 1 57 ? 31.015  -31.559 24.117  1.00 43.29 ? 56  LYS   C N    1 
ATOM   1921 C  CA   . LYS   C 1 57 ? 31.599  -31.724 22.791  1.00 44.52 ? 56  LYS   C CA   1 
ATOM   1922 C  C    . LYS   C 1 57 ? 30.541  -31.755 21.696  1.00 44.31 ? 56  LYS   C C    1 
ATOM   1923 O  O    . LYS   C 1 57 ? 30.859  -31.485 20.533  1.00 41.56 ? 56  LYS   C O    1 
ATOM   1924 C  CB   . LYS   C 1 57 ? 32.435  -33.004 22.734  1.00 45.99 ? 56  LYS   C CB   1 
ATOM   1925 N  N    . ASP   C 1 58 ? 29.292  -32.061 22.044  1.00 36.89 ? 57  ASP   C N    1 
ATOM   1926 C  CA   . ASP   C 1 58 ? 28.208  -32.185 21.079  1.00 36.66 ? 57  ASP   C CA   1 
ATOM   1927 C  C    . ASP   C 1 58 ? 27.233  -31.013 21.124  1.00 32.63 ? 57  ASP   C C    1 
ATOM   1928 O  O    . ASP   C 1 58 ? 26.137  -31.114 20.565  1.00 34.46 ? 57  ASP   C O    1 
ATOM   1929 C  CB   . ASP   C 1 58 ? 27.457  -33.497 21.312  1.00 39.74 ? 57  ASP   C CB   1 
ATOM   1930 C  CG   . ASP   C 1 58 ? 28.348  -34.715 21.152  1.00 49.12 ? 57  ASP   C CG   1 
ATOM   1931 O  OD1  . ASP   C 1 58 ? 29.131  -34.758 20.178  1.00 47.45 ? 57  ASP   C OD1  1 
ATOM   1932 O  OD2  . ASP   C 1 58 ? 28.266  -35.628 22.002  1.00 46.37 ? 57  ASP   C OD2  1 
ATOM   1933 N  N    . LEU   C 1 59 ? 27.601  -29.903 21.761  1.00 34.92 ? 58  LEU   C N    1 
ATOM   1934 C  CA   . LEU   C 1 59 ? 26.697  -28.776 21.953  1.00 31.80 ? 58  LEU   C CA   1 
ATOM   1935 C  C    . LEU   C 1 59 ? 27.317  -27.511 21.378  1.00 41.12 ? 58  LEU   C C    1 
ATOM   1936 O  O    . LEU   C 1 59 ? 28.496  -27.228 21.614  1.00 40.32 ? 58  LEU   C O    1 
ATOM   1937 C  CB   . LEU   C 1 59 ? 26.374  -28.584 23.434  1.00 31.98 ? 58  LEU   C CB   1 
ATOM   1938 C  CG   . LEU   C 1 59 ? 25.705  -29.792 24.089  1.00 34.36 ? 58  LEU   C CG   1 
ATOM   1939 C  CD1  . LEU   C 1 59 ? 25.416  -29.510 25.549  1.00 32.42 ? 58  LEU   C CD1  1 
ATOM   1940 C  CD2  . LEU   C 1 59 ? 24.431  -30.157 23.345  1.00 26.32 ? 58  LEU   C CD2  1 
ATOM   1941 N  N    . PHE   C 1 60 ? 26.515  -26.746 20.640  1.00 36.48 ? 59  PHE   C N    1 
ATOM   1942 C  CA   . PHE   C 1 60 ? 26.987  -25.563 19.922  1.00 36.24 ? 59  PHE   C CA   1 
ATOM   1943 C  C    . PHE   C 1 60 ? 26.015  -24.420 20.178  1.00 34.13 ? 59  PHE   C C    1 
ATOM   1944 O  O    . PHE   C 1 60 ? 24.804  -24.576 19.927  1.00 38.22 ? 59  PHE   C O    1 
ATOM   1945 C  CB   . PHE   C 1 60 ? 27.115  -25.862 18.427  1.00 42.08 ? 59  PHE   C CB   1 
ATOM   1946 C  CG   . PHE   C 1 60 ? 28.017  -27.024 18.117  1.00 39.96 ? 59  PHE   C CG   1 
ATOM   1947 C  CD1  . PHE   C 1 60 ? 27.538  -28.325 18.156  1.00 40.48 ? 59  PHE   C CD1  1 
ATOM   1948 C  CD2  . PHE   C 1 60 ? 29.347  -26.818 17.795  1.00 44.57 ? 59  PHE   C CD2  1 
ATOM   1949 C  CE1  . PHE   C 1 60 ? 28.367  -29.392 17.881  1.00 35.16 ? 59  PHE   C CE1  1 
ATOM   1950 C  CE2  . PHE   C 1 60 ? 30.180  -27.882 17.516  1.00 43.25 ? 59  PHE   C CE2  1 
ATOM   1951 C  CZ   . PHE   C 1 60 ? 29.689  -29.170 17.560  1.00 46.32 ? 59  PHE   C CZ   1 
ATOM   1952 N  N    . PRO   C 1 61 ? 26.476  -23.273 20.675  1.00 39.76 ? 60  PRO   C N    1 
ATOM   1953 C  CA   . PRO   C 1 61 ? 25.547  -22.176 20.980  1.00 38.78 ? 60  PRO   C CA   1 
ATOM   1954 C  C    . PRO   C 1 61 ? 24.772  -21.740 19.743  1.00 33.14 ? 60  PRO   C C    1 
ATOM   1955 O  O    . PRO   C 1 61 ? 25.320  -21.650 18.642  1.00 39.12 ? 60  PRO   C O    1 
ATOM   1956 C  CB   . PRO   C 1 61 ? 26.469  -21.063 21.494  1.00 42.47 ? 60  PRO   C CB   1 
ATOM   1957 C  CG   . PRO   C 1 61 ? 27.701  -21.771 21.951  1.00 39.53 ? 60  PRO   C CG   1 
ATOM   1958 C  CD   . PRO   C 1 61 ? 27.864  -22.942 21.034  1.00 45.41 ? 60  PRO   C CD   1 
ATOM   1959 N  N    . TYR   C 1 62 ? 23.476  -21.478 19.939  1.00 39.08 ? 61  TYR   C N    1 
ATOM   1960 C  CA   . TYR   C 1 62 ? 22.581  -21.227 18.811  1.00 37.54 ? 61  TYR   C CA   1 
ATOM   1961 C  C    . TYR   C 1 62 ? 22.971  -19.961 18.057  1.00 41.42 ? 61  TYR   C C    1 
ATOM   1962 O  O    . TYR   C 1 62 ? 23.190  -19.994 16.841  1.00 43.51 ? 61  TYR   C O    1 
ATOM   1963 C  CB   . TYR   C 1 62 ? 21.135  -21.137 19.301  1.00 40.17 ? 61  TYR   C CB   1 
ATOM   1964 C  CG   . TYR   C 1 62 ? 20.145  -20.741 18.227  1.00 41.45 ? 61  TYR   C CG   1 
ATOM   1965 C  CD1  . TYR   C 1 62 ? 19.965  -21.528 17.097  1.00 35.74 ? 61  TYR   C CD1  1 
ATOM   1966 C  CD2  . TYR   C 1 62 ? 19.381  -19.585 18.349  1.00 40.09 ? 61  TYR   C CD2  1 
ATOM   1967 C  CE1  . TYR   C 1 62 ? 19.061  -21.174 16.111  1.00 43.52 ? 61  TYR   C CE1  1 
ATOM   1968 C  CE2  . TYR   C 1 62 ? 18.473  -19.222 17.371  1.00 47.09 ? 61  TYR   C CE2  1 
ATOM   1969 C  CZ   . TYR   C 1 62 ? 18.317  -20.019 16.254  1.00 44.10 ? 61  TYR   C CZ   1 
ATOM   1970 O  OH   . TYR   C 1 62 ? 17.415  -19.659 15.278  1.00 41.59 ? 61  TYR   C OH   1 
ATOM   1971 N  N    . ASP   C 1 63 ? 23.061  -18.831 18.763  1.00 44.58 ? 62  ASP   C N    1 
ATOM   1972 C  CA   . ASP   C 1 63 ? 23.347  -17.568 18.089  1.00 51.33 ? 62  ASP   C CA   1 
ATOM   1973 C  C    . ASP   C 1 63 ? 24.711  -17.580 17.413  1.00 42.43 ? 62  ASP   C C    1 
ATOM   1974 O  O    . ASP   C 1 63 ? 24.884  -16.962 16.355  1.00 54.87 ? 62  ASP   C O    1 
ATOM   1975 C  CB   . ASP   C 1 63 ? 23.255  -16.410 19.083  1.00 51.86 ? 62  ASP   C CB   1 
ATOM   1976 C  CG   . ASP   C 1 63 ? 21.828  -15.941 19.301  1.00 61.36 ? 62  ASP   C CG   1 
ATOM   1977 O  OD1  . ASP   C 1 63 ? 21.629  -14.746 19.602  1.00 68.38 ? 62  ASP   C OD1  1 
ATOM   1978 O  OD2  . ASP   C 1 63 ? 20.902  -16.766 19.153  1.00 64.50 ? 62  ASP   C OD2  1 
ATOM   1979 N  N    . LYS   C 1 64 ? 25.688  -18.278 17.995  1.00 39.76 ? 63  LYS   C N    1 
ATOM   1980 C  CA   . LYS   C 1 64 ? 27.024  -18.286 17.409  1.00 40.07 ? 63  LYS   C CA   1 
ATOM   1981 C  C    . LYS   C 1 64 ? 27.101  -19.163 16.166  1.00 47.68 ? 63  LYS   C C    1 
ATOM   1982 O  O    . LYS   C 1 64 ? 27.849  -18.844 15.233  1.00 41.55 ? 63  LYS   C O    1 
ATOM   1983 C  CB   . LYS   C 1 64 ? 28.049  -18.756 18.442  1.00 37.18 ? 63  LYS   C CB   1 
ATOM   1984 N  N    . CYS   C 1 65 ? 26.340  -20.260 16.127  1.00 39.59 ? 64  CYS   C N    1 
ATOM   1985 C  CA   . CYS   C 1 65 ? 26.485  -21.267 15.085  1.00 36.08 ? 64  CYS   C CA   1 
ATOM   1986 C  C    . CYS   C 1 65 ? 25.280  -21.378 14.158  1.00 38.10 ? 64  CYS   C C    1 
ATOM   1987 O  O    . CYS   C 1 65 ? 25.284  -22.242 13.274  1.00 36.91 ? 64  CYS   C O    1 
ATOM   1988 C  CB   . CYS   C 1 65 ? 26.765  -22.636 15.719  1.00 41.30 ? 64  CYS   C CB   1 
ATOM   1989 S  SG   . CYS   C 1 65 ? 28.268  -22.705 16.719  1.00 44.63 ? 64  CYS   C SG   1 
ATOM   1990 N  N    . LYS   C 1 66 ? 24.255  -20.535 14.327  1.00 38.60 ? 65  LYS   C N    1 
ATOM   1991 C  CA   . LYS   C 1 66 ? 23.056  -20.667 13.502  1.00 33.69 ? 65  LYS   C CA   1 
ATOM   1992 C  C    . LYS   C 1 66 ? 23.358  -20.450 12.025  1.00 37.09 ? 65  LYS   C C    1 
ATOM   1993 O  O    . LYS   C 1 66 ? 22.713  -21.060 11.167  1.00 40.69 ? 65  LYS   C O    1 
ATOM   1994 C  CB   . LYS   C 1 66 ? 21.972  -19.692 13.966  1.00 39.90 ? 65  LYS   C CB   1 
ATOM   1995 C  CG   . LYS   C 1 66 ? 22.350  -18.234 13.815  1.00 41.22 ? 65  LYS   C CG   1 
ATOM   1996 C  CD   . LYS   C 1 66 ? 21.149  -17.318 13.976  1.00 55.49 ? 65  LYS   C CD   1 
ATOM   1997 C  CE   . LYS   C 1 66 ? 20.703  -17.226 15.424  1.00 58.27 ? 65  LYS   C CE   1 
ATOM   1998 N  NZ   . LYS   C 1 66 ? 19.940  -15.968 15.669  1.00 58.60 ? 65  LYS   C NZ   1 
ATOM   1999 N  N    . ASP   C 1 67 ? 24.336  -19.600 11.705  1.00 41.61 ? 66  ASP   C N    1 
ATOM   2000 C  CA   . ASP   C 1 67 ? 24.679  -19.390 10.303  1.00 39.35 ? 66  ASP   C CA   1 
ATOM   2001 C  C    . ASP   C 1 67 ? 25.224  -20.656 9.659   1.00 46.57 ? 66  ASP   C C    1 
ATOM   2002 O  O    . ASP   C 1 67 ? 25.132  -20.808 8.435   1.00 39.92 ? 66  ASP   C O    1 
ATOM   2003 C  CB   . ASP   C 1 67 ? 25.691  -18.248 10.169  1.00 43.68 ? 66  ASP   C CB   1 
ATOM   2004 C  CG   . ASP   C 1 67 ? 27.062  -18.613 10.703  1.00 51.11 ? 66  ASP   C CG   1 
ATOM   2005 O  OD1  . ASP   C 1 67 ? 27.140  -19.329 11.725  1.00 55.82 ? 66  ASP   C OD1  1 
ATOM   2006 O  OD2  . ASP   C 1 67 ? 28.066  -18.182 10.097  1.00 58.68 ? 66  ASP   C OD2  1 
ATOM   2007 N  N    . LYS   C 1 68 ? 25.766  -21.577 10.456  1.00 38.02 ? 67  LYS   C N    1 
ATOM   2008 C  CA   . LYS   C 1 68 ? 26.310  -22.830 9.953   1.00 43.08 ? 67  LYS   C CA   1 
ATOM   2009 C  C    . LYS   C 1 68 ? 25.317  -23.982 10.024  1.00 37.99 ? 67  LYS   C C    1 
ATOM   2010 O  O    . LYS   C 1 68 ? 25.176  -24.729 9.052   1.00 35.12 ? 67  LYS   C O    1 
ATOM   2011 C  CB   . LYS   C 1 68 ? 27.580  -23.199 10.729  1.00 43.73 ? 67  LYS   C CB   1 
ATOM   2012 C  CG   . LYS   C 1 68 ? 28.405  -24.303 10.090  1.00 53.69 ? 67  LYS   C CG   1 
ATOM   2013 C  CD   . LYS   C 1 68 ? 29.757  -24.441 10.777  1.00 46.58 ? 67  LYS   C CD   1 
ATOM   2014 C  CE   . LYS   C 1 68 ? 30.601  -25.528 10.127  1.00 67.50 ? 67  LYS   C CE   1 
ATOM   2015 N  NZ   . LYS   C 1 68 ? 31.915  -25.690 10.810  1.00 58.91 ? 67  LYS   C NZ   1 
ATOM   2016 N  N    . TYR   C 1 69 ? 24.616  -24.140 11.150  1.00 35.82 ? 68  TYR   C N    1 
ATOM   2017 C  CA   . TYR   C 1 69 ? 23.711  -25.265 11.345  1.00 34.35 ? 68  TYR   C CA   1 
ATOM   2018 C  C    . TYR   C 1 69 ? 22.239  -24.902 11.188  1.00 33.89 ? 68  TYR   C C    1 
ATOM   2019 O  O    . TYR   C 1 69 ? 21.414  -25.804 11.007  1.00 35.50 ? 68  TYR   C O    1 
ATOM   2020 C  CB   . TYR   C 1 69 ? 23.929  -25.879 12.733  1.00 30.74 ? 68  TYR   C CB   1 
ATOM   2021 C  CG   . TYR   C 1 69 ? 25.350  -26.332 12.973  1.00 27.02 ? 68  TYR   C CG   1 
ATOM   2022 C  CD1  . TYR   C 1 69 ? 26.019  -27.108 12.039  1.00 34.84 ? 68  TYR   C CD1  1 
ATOM   2023 C  CD2  . TYR   C 1 69 ? 26.025  -25.970 14.130  1.00 36.33 ? 68  TYR   C CD2  1 
ATOM   2024 C  CE1  . TYR   C 1 69 ? 27.318  -27.524 12.254  1.00 37.41 ? 68  TYR   C CE1  1 
ATOM   2025 C  CE2  . TYR   C 1 69 ? 27.323  -26.377 14.353  1.00 38.40 ? 68  TYR   C CE2  1 
ATOM   2026 C  CZ   . TYR   C 1 69 ? 27.965  -27.154 13.412  1.00 43.52 ? 68  TYR   C CZ   1 
ATOM   2027 O  OH   . TYR   C 1 69 ? 29.260  -27.560 13.635  1.00 51.31 ? 68  TYR   C OH   1 
ATOM   2028 N  N    . GLY   C 1 70 ? 21.892  -23.619 11.253  1.00 31.14 ? 69  GLY   C N    1 
ATOM   2029 C  CA   . GLY   C 1 70 ? 20.510  -23.210 11.107  1.00 29.53 ? 69  GLY   C CA   1 
ATOM   2030 C  C    . GLY   C 1 70 ? 20.093  -23.115 9.655   1.00 31.29 ? 69  GLY   C C    1 
ATOM   2031 O  O    . GLY   C 1 70 ? 19.952  -22.017 9.110   1.00 33.35 ? 69  GLY   C O    1 
ATOM   2032 N  N    . LYS   C 1 71 ? 19.917  -24.266 9.018   1.00 28.06 ? 70  LYS   C N    1 
ATOM   2033 C  CA   . LYS   C 1 71 ? 19.472  -24.380 7.638   1.00 32.98 ? 70  LYS   C CA   1 
ATOM   2034 C  C    . LYS   C 1 71 ? 18.520  -25.561 7.559   1.00 33.55 ? 70  LYS   C C    1 
ATOM   2035 O  O    . LYS   C 1 71 ? 18.638  -26.505 8.350   1.00 36.46 ? 70  LYS   C O    1 
ATOM   2036 C  CB   . LYS   C 1 71 ? 20.648  -24.597 6.673   1.00 38.30 ? 70  LYS   C CB   1 
ATOM   2037 C  CG   . LYS   C 1 71 ? 21.259  -25.981 6.786   1.00 43.03 ? 70  LYS   C CG   1 
ATOM   2038 C  CD   . LYS   C 1 71 ? 22.677  -26.035 6.252   1.00 47.14 ? 70  LYS   C CD   1 
ATOM   2039 C  CE   . LYS   C 1 71 ? 23.448  -27.189 6.881   1.00 45.05 ? 70  LYS   C CE   1 
ATOM   2040 N  NZ   . LYS   C 1 71 ? 24.067  -26.790 8.181   1.00 44.79 ? 70  LYS   C NZ   1 
ATOM   2041 N  N    . PRO   C 1 72 ? 17.562  -25.534 6.633   1.00 27.66 ? 71  PRO   C N    1 
ATOM   2042 C  CA   . PRO   C 1 72 ? 16.563  -26.606 6.587   1.00 22.72 ? 71  PRO   C CA   1 
ATOM   2043 C  C    . PRO   C 1 72 ? 17.184  -27.971 6.328   1.00 32.70 ? 71  PRO   C C    1 
ATOM   2044 O  O    . PRO   C 1 72 ? 18.193  -28.107 5.634   1.00 29.21 ? 71  PRO   C O    1 
ATOM   2045 C  CB   . PRO   C 1 72 ? 15.643  -26.183 5.437   1.00 29.16 ? 71  PRO   C CB   1 
ATOM   2046 C  CG   . PRO   C 1 72 ? 15.749  -24.700 5.425   1.00 27.85 ? 71  PRO   C CG   1 
ATOM   2047 C  CD   . PRO   C 1 72 ? 17.194  -24.411 5.754   1.00 29.74 ? 71  PRO   C CD   1 
ATOM   2048 N  N    . ASN   C 1 73 ? 16.561  -28.985 6.919   1.00 33.96 ? 72  ASN   C N    1 
ATOM   2049 C  CA   . ASN   C 1 73 ? 16.953  -30.374 6.756   1.00 34.61 ? 72  ASN   C CA   1 
ATOM   2050 C  C    . ASN   C 1 73 ? 15.681  -31.188 6.592   1.00 28.58 ? 72  ASN   C C    1 
ATOM   2051 O  O    . ASN   C 1 73 ? 14.646  -30.867 7.182   1.00 32.78 ? 72  ASN   C O    1 
ATOM   2052 C  CB   . ASN   C 1 73 ? 17.774  -30.883 7.956   1.00 32.72 ? 72  ASN   C CB   1 
ATOM   2053 C  CG   . ASN   C 1 73 ? 18.363  -32.264 7.721   1.00 38.14 ? 72  ASN   C CG   1 
ATOM   2054 O  OD1  . ASN   C 1 73 ? 17.643  -33.260 7.686   1.00 34.92 ? 72  ASN   C OD1  1 
ATOM   2055 N  ND2  . ASN   C 1 73 ? 19.683  -32.328 7.563   1.00 40.69 ? 72  ASN   C ND2  1 
ATOM   2056 N  N    . LYS   C 1 74 ? 15.765  -32.246 5.790   1.00 34.28 ? 73  LYS   C N    1 
ATOM   2057 C  CA   . LYS   C 1 74 ? 14.593  -33.053 5.479   1.00 32.21 ? 73  LYS   C CA   1 
ATOM   2058 C  C    . LYS   C 1 74 ? 14.195  -34.005 6.599   1.00 33.47 ? 73  LYS   C C    1 
ATOM   2059 O  O    . LYS   C 1 74 ? 13.079  -34.537 6.561   1.00 34.30 ? 73  LYS   C O    1 
ATOM   2060 C  CB   . LYS   C 1 74 ? 14.843  -33.847 4.198   1.00 33.48 ? 73  LYS   C CB   1 
ATOM   2061 C  CG   . LYS   C 1 74 ? 15.050  -32.970 2.979   1.00 37.35 ? 73  LYS   C CG   1 
ATOM   2062 C  CD   . LYS   C 1 74 ? 13.939  -31.942 2.890   1.00 39.53 ? 73  LYS   C CD   1 
ATOM   2063 C  CE   . LYS   C 1 74 ? 13.808  -31.357 1.497   1.00 57.20 ? 73  LYS   C CE   1 
ATOM   2064 N  NZ   . LYS   C 1 74 ? 12.549  -30.565 1.387   1.00 49.75 ? 73  LYS   C NZ   1 
ATOM   2065 N  N    . ARG   C 1 75 ? 15.067  -34.230 7.581   1.00 29.50 ? 74  ARG   C N    1 
ATOM   2066 C  CA   . ARG   C 1 75 ? 14.775  -35.172 8.655   1.00 27.27 ? 74  ARG   C CA   1 
ATOM   2067 C  C    . ARG   C 1 75 ? 13.496  -34.773 9.384   1.00 34.37 ? 74  ARG   C C    1 
ATOM   2068 O  O    . ARG   C 1 75 ? 13.238  -33.589 9.619   1.00 29.17 ? 74  ARG   C O    1 
ATOM   2069 C  CB   . ARG   C 1 75 ? 15.953  -35.233 9.634   1.00 28.64 ? 74  ARG   C CB   1 
ATOM   2070 C  CG   . ARG   C 1 75 ? 16.038  -36.517 10.456  1.00 36.82 ? 74  ARG   C CG   1 
ATOM   2071 C  CD   . ARG   C 1 75 ? 16.551  -37.686 9.613   1.00 31.68 ? 74  ARG   C CD   1 
ATOM   2072 N  NE   . ARG   C 1 75 ? 17.880  -37.443 9.064   1.00 32.39 ? 74  ARG   C NE   1 
ATOM   2073 C  CZ   . ARG   C 1 75 ? 19.011  -37.898 9.592   1.00 33.94 ? 74  ARG   C CZ   1 
ATOM   2074 N  NH1  . ARG   C 1 75 ? 19.012  -38.628 10.699  1.00 32.54 ? 74  ARG   C NH1  1 
ATOM   2075 N  NH2  . ARG   C 1 75 ? 20.173  -37.620 8.985   1.00 36.59 ? 74  ARG   C NH2  1 
ATOM   2076 N  N    . LYS   C 1 76 ? 12.688  -35.775 9.730   1.00 27.99 ? 75  LYS   C N    1 
ATOM   2077 C  CA   . LYS   C 1 76 ? 11.385  -35.527 10.336  1.00 34.24 ? 75  LYS   C CA   1 
ATOM   2078 C  C    . LYS   C 1 76 ? 11.502  -34.623 11.556  1.00 33.98 ? 75  LYS   C C    1 
ATOM   2079 O  O    . LYS   C 1 76 ? 12.349  -34.834 12.429  1.00 29.15 ? 75  LYS   C O    1 
ATOM   2080 C  CB   . LYS   C 1 76 ? 10.730  -36.852 10.729  1.00 35.91 ? 75  LYS   C CB   1 
ATOM   2081 C  CG   . LYS   C 1 76 ? 9.334   -36.706 11.319  1.00 46.39 ? 75  LYS   C CG   1 
ATOM   2082 C  CD   . LYS   C 1 76 ? 8.894   -37.990 12.013  1.00 53.27 ? 75  LYS   C CD   1 
ATOM   2083 C  CE   . LYS   C 1 76 ? 7.374   -38.097 12.104  1.00 58.94 ? 75  LYS   C CE   1 
ATOM   2084 N  NZ   . LYS   C 1 76 ? 6.829   -37.693 13.430  1.00 60.78 ? 75  LYS   C NZ   1 
ATOM   2085 N  N    . GLY   C 1 77 ? 10.649  -33.600 11.601  1.00 36.33 ? 76  GLY   C N    1 
ATOM   2086 C  CA   . GLY   C 1 77 ? 10.611  -32.683 12.717  1.00 31.09 ? 76  GLY   C CA   1 
ATOM   2087 C  C    . GLY   C 1 77 ? 11.652  -31.586 12.698  1.00 26.41 ? 76  GLY   C C    1 
ATOM   2088 O  O    . GLY   C 1 77 ? 11.551  -30.650 13.498  1.00 28.30 ? 76  GLY   C O    1 
ATOM   2089 N  N    . PHE   C 1 78 ? 12.644  -31.653 11.808  1.00 24.08 ? 77  PHE   C N    1 
ATOM   2090 C  CA   . PHE   C 1 78 ? 13.751  -30.705 11.874  1.00 21.20 ? 77  PHE   C CA   1 
ATOM   2091 C  C    . PHE   C 1 78 ? 13.284  -29.278 11.599  1.00 27.84 ? 77  PHE   C C    1 
ATOM   2092 O  O    . PHE   C 1 78 ? 13.600  -28.354 12.355  1.00 26.11 ? 77  PHE   C O    1 
ATOM   2093 C  CB   . PHE   C 1 78 ? 14.849  -31.111 10.893  1.00 26.56 ? 77  PHE   C CB   1 
ATOM   2094 C  CG   . PHE   C 1 78 ? 16.140  -30.366 11.083  1.00 25.02 ? 77  PHE   C CG   1 
ATOM   2095 C  CD1  . PHE   C 1 78 ? 16.318  -29.101 10.540  1.00 22.76 ? 77  PHE   C CD1  1 
ATOM   2096 C  CD2  . PHE   C 1 78 ? 17.180  -30.936 11.803  1.00 26.28 ? 77  PHE   C CD2  1 
ATOM   2097 C  CE1  . PHE   C 1 78 ? 17.510  -28.417 10.718  1.00 28.03 ? 77  PHE   C CE1  1 
ATOM   2098 C  CE2  . PHE   C 1 78 ? 18.370  -30.260 11.982  1.00 25.92 ? 77  PHE   C CE2  1 
ATOM   2099 C  CZ   . PHE   C 1 78 ? 18.537  -28.997 11.439  1.00 27.26 ? 77  PHE   C CZ   1 
ATOM   2100 N  N    . ASN   C 1 79 ? 12.540  -29.077 10.511  1.00 27.12 ? 78  ASN   C N    1 
ATOM   2101 C  CA   . ASN   C 1 79 ? 12.185  -27.717 10.124  1.00 25.94 ? 78  ASN   C CA   1 
ATOM   2102 C  C    . ASN   C 1 79 ? 11.163  -27.105 11.072  1.00 24.44 ? 78  ASN   C C    1 
ATOM   2103 O  O    . ASN   C 1 79 ? 11.185  -25.890 11.300  1.00 24.84 ? 78  ASN   C O    1 
ATOM   2104 C  CB   . ASN   C 1 79 ? 11.693  -27.710 8.679   1.00 26.93 ? 78  ASN   C CB   1 
ATOM   2105 C  CG   . ASN   C 1 79 ? 12.784  -28.108 7.708   1.00 28.05 ? 78  ASN   C CG   1 
ATOM   2106 O  OD1  . ASN   C 1 79 ? 13.959  -27.847 7.957   1.00 27.62 ? 78  ASN   C OD1  1 
ATOM   2107 N  ND2  . ASN   C 1 79 ? 12.408  -28.740 6.602   1.00 30.87 ? 78  ASN   C ND2  1 
ATOM   2108 N  N    . GLU   C 1 80 ? 10.272  -27.915 11.646  1.00 24.90 ? 79  GLU   C N    1 
ATOM   2109 C  CA   . GLU   C 1 80 ? 9.458   -27.411 12.746  1.00 26.78 ? 79  GLU   C CA   1 
ATOM   2110 C  C    . GLU   C 1 80 ? 10.338  -26.996 13.918  1.00 30.99 ? 79  GLU   C C    1 
ATOM   2111 O  O    . GLU   C 1 80 ? 10.072  -25.985 14.578  1.00 29.88 ? 79  GLU   C O    1 
ATOM   2112 C  CB   . GLU   C 1 80 ? 8.432   -28.458 13.182  1.00 32.87 ? 79  GLU   C CB   1 
ATOM   2113 C  CG   . GLU   C 1 80 ? 7.556   -28.000 14.340  1.00 33.48 ? 79  GLU   C CG   1 
ATOM   2114 C  CD   . GLU   C 1 80 ? 6.269   -28.786 14.448  1.00 49.27 ? 79  GLU   C CD   1 
ATOM   2115 O  OE1  . GLU   C 1 80 ? 6.219   -29.916 13.919  1.00 49.69 ? 79  GLU   C OE1  1 
ATOM   2116 O  OE2  . GLU   C 1 80 ? 5.306   -28.268 15.054  1.00 44.05 ? 79  GLU   C OE2  1 
ATOM   2117 N  N    . GLY   C 1 81 ? 11.416  -27.746 14.163  1.00 27.92 ? 80  GLY   C N    1 
ATOM   2118 C  CA   . GLY   C 1 81 ? 12.348  -27.368 15.214  1.00 26.83 ? 80  GLY   C CA   1 
ATOM   2119 C  C    . GLY   C 1 81 ? 13.039  -26.044 14.950  1.00 25.42 ? 80  GLY   C C    1 
ATOM   2120 O  O    . GLY   C 1 81 ? 13.257  -25.254 15.873  1.00 26.60 ? 80  GLY   C O    1 
ATOM   2121 N  N    . LEU   C 1 82 ? 13.410  -25.789 13.690  1.00 25.03 ? 81  LEU   C N    1 
ATOM   2122 C  CA   . LEU   C 1 82 ? 14.000  -24.499 13.342  1.00 27.55 ? 81  LEU   C CA   1 
ATOM   2123 C  C    . LEU   C 1 82 ? 13.025  -23.361 13.611  1.00 24.47 ? 81  LEU   C C    1 
ATOM   2124 O  O    . LEU   C 1 82 ? 13.424  -22.287 14.076  1.00 25.47 ? 81  LEU   C O    1 
ATOM   2125 C  CB   . LEU   C 1 82 ? 14.435  -24.490 11.874  1.00 24.95 ? 81  LEU   C CB   1 
ATOM   2126 C  CG   . LEU   C 1 82 ? 15.665  -25.316 11.487  1.00 27.35 ? 81  LEU   C CG   1 
ATOM   2127 C  CD1  . LEU   C 1 82 ? 15.922  -25.208 9.999   1.00 25.89 ? 81  LEU   C CD1  1 
ATOM   2128 C  CD2  . LEU   C 1 82 ? 16.886  -24.855 12.251  1.00 27.36 ? 81  LEU   C CD2  1 
ATOM   2129 N  N    . TRP   C 1 83 ? 11.739  -23.577 13.328  1.00 26.01 ? 82  TRP   C N    1 
ATOM   2130 C  CA   . TRP   C 1 83 ? 10.755  -22.544 13.628  1.00 31.21 ? 82  TRP   C CA   1 
ATOM   2131 C  C    . TRP   C 1 83 ? 10.654  -22.305 15.127  1.00 26.81 ? 82  TRP   C C    1 
ATOM   2132 O  O    . TRP   C 1 83 ? 10.542  -21.158 15.574  1.00 30.53 ? 82  TRP   C O    1 
ATOM   2133 C  CB   . TRP   C 1 83 ? 9.387   -22.919 13.064  1.00 31.12 ? 82  TRP   C CB   1 
ATOM   2134 C  CG   . TRP   C 1 83 ? 8.401   -21.790 13.185  1.00 30.25 ? 82  TRP   C CG   1 
ATOM   2135 C  CD1  . TRP   C 1 83 ? 8.169   -20.805 12.268  1.00 34.82 ? 82  TRP   C CD1  1 
ATOM   2136 C  CD2  . TRP   C 1 83 ? 7.533   -21.516 14.293  1.00 35.67 ? 82  TRP   C CD2  1 
ATOM   2137 N  NE1  . TRP   C 1 83 ? 7.207   -19.943 12.731  1.00 32.64 ? 82  TRP   C NE1  1 
ATOM   2138 C  CE2  . TRP   C 1 83 ? 6.801   -20.355 13.973  1.00 31.44 ? 82  TRP   C CE2  1 
ATOM   2139 C  CE3  . TRP   C 1 83 ? 7.304   -22.139 15.525  1.00 40.46 ? 82  TRP   C CE3  1 
ATOM   2140 C  CZ2  . TRP   C 1 83 ? 5.854   -19.808 14.835  1.00 36.58 ? 82  TRP   C CZ2  1 
ATOM   2141 C  CZ3  . TRP   C 1 83 ? 6.359   -21.594 16.380  1.00 36.36 ? 82  TRP   C CZ3  1 
ATOM   2142 C  CH2  . TRP   C 1 83 ? 5.648   -20.439 16.030  1.00 38.85 ? 82  TRP   C CH2  1 
ATOM   2143 N  N    . GLU   C 1 84 ? 10.704  -23.377 15.919  1.00 27.20 ? 83  GLU   C N    1 
ATOM   2144 C  CA   . GLU   C 1 84 ? 10.540  -23.242 17.363  1.00 29.02 ? 83  GLU   C CA   1 
ATOM   2145 C  C    . GLU   C 1 84 ? 11.710  -22.497 17.992  1.00 30.41 ? 83  GLU   C C    1 
ATOM   2146 O  O    . GLU   C 1 84 ? 11.509  -21.621 18.841  1.00 31.30 ? 83  GLU   C O    1 
ATOM   2147 C  CB   . GLU   C 1 84 ? 10.373  -24.622 17.998  1.00 27.71 ? 83  GLU   C CB   1 
ATOM   2148 C  CG   . GLU   C 1 84 ? 9.115   -25.333 17.543  1.00 33.54 ? 83  GLU   C CG   1 
ATOM   2149 C  CD   . GLU   C 1 84 ? 8.960   -26.712 18.143  1.00 37.00 ? 83  GLU   C CD   1 
ATOM   2150 O  OE1  . GLU   C 1 84 ? 9.950   -27.258 18.673  1.00 34.53 ? 83  GLU   C OE1  1 
ATOM   2151 O  OE2  . GLU   C 1 84 ? 7.837   -27.250 18.080  1.00 39.34 ? 83  GLU   C OE2  1 
ATOM   2152 N  N    . ILE   C 1 85 ? 12.941  -22.811 17.579  1.00 26.89 ? 84  ILE   C N    1 
ATOM   2153 C  CA   . ILE   C 1 85 ? 14.094  -22.205 18.233  1.00 31.47 ? 84  ILE   C CA   1 
ATOM   2154 C  C    . ILE   C 1 85 ? 14.226  -20.727 17.890  1.00 33.98 ? 84  ILE   C C    1 
ATOM   2155 O  O    . ILE   C 1 85 ? 14.832  -19.966 18.654  1.00 29.53 ? 84  ILE   C O    1 
ATOM   2156 C  CB   . ILE   C 1 85 ? 15.383  -22.969 17.877  1.00 30.38 ? 84  ILE   C CB   1 
ATOM   2157 C  CG1  . ILE   C 1 85 ? 16.511  -22.593 18.842  1.00 28.59 ? 84  ILE   C CG1  1 
ATOM   2158 C  CG2  . ILE   C 1 85 ? 15.792  -22.704 16.430  1.00 32.09 ? 84  ILE   C CG2  1 
ATOM   2159 C  CD1  . ILE   C 1 85 ? 17.701  -23.535 18.786  1.00 30.78 ? 84  ILE   C CD1  1 
ATOM   2160 N  N    . GLN   C 1 86 ? 13.662  -20.294 16.766  1.00 29.74 ? 85  GLN   C N    1 
ATOM   2161 C  CA   . GLN   C 1 86 ? 13.739  -18.895 16.373  1.00 27.72 ? 85  GLN   C CA   1 
ATOM   2162 C  C    . GLN   C 1 86 ? 12.537  -18.090 16.840  1.00 28.96 ? 85  GLN   C C    1 
ATOM   2163 O  O    . GLN   C 1 86 ? 12.676  -16.895 17.130  1.00 38.83 ? 85  GLN   C O    1 
ATOM   2164 C  CB   . GLN   C 1 86 ? 13.869  -18.791 14.848  1.00 30.01 ? 85  GLN   C CB   1 
ATOM   2165 C  CG   . GLN   C 1 86 ? 14.049  -17.371 14.324  1.00 32.52 ? 85  GLN   C CG   1 
ATOM   2166 C  CD   . GLN   C 1 86 ? 14.343  -17.339 12.835  1.00 34.68 ? 85  GLN   C CD   1 
ATOM   2167 O  OE1  . GLN   C 1 86 ? 14.205  -18.348 12.141  1.00 38.01 ? 85  GLN   C OE1  1 
ATOM   2168 N  NE2  . GLN   C 1 86 ? 14.759  -16.182 12.338  1.00 39.12 ? 85  GLN   C NE2  1 
ATOM   2169 N  N    . ASN   C 1 87 ? 11.364  -18.716 16.944  1.00 30.76 ? 86  ASN   C N    1 
ATOM   2170 C  CA   . ASN   C 1 87 ? 10.128  -17.991 17.213  1.00 38.83 ? 86  ASN   C CA   1 
ATOM   2171 C  C    . ASN   C 1 87 ? 9.486   -18.321 18.552  1.00 33.77 ? 86  ASN   C C    1 
ATOM   2172 O  O    . ASN   C 1 87 ? 8.761   -17.483 19.089  1.00 39.23 ? 86  ASN   C O    1 
ATOM   2173 C  CB   . ASN   C 1 87 ? 9.111   -18.254 16.097  1.00 35.63 ? 86  ASN   C CB   1 
ATOM   2174 C  CG   . ASN   C 1 87 ? 9.614   -17.805 14.739  1.00 36.46 ? 86  ASN   C CG   1 
ATOM   2175 O  OD1  . ASN   C 1 87 ? 10.133  -18.604 13.958  1.00 34.89 ? 86  ASN   C OD1  1 
ATOM   2176 N  ND2  . ASN   C 1 87 ? 9.476   -16.515 14.456  1.00 35.92 ? 86  ASN   C ND2  1 
ATOM   2177 N  N    . ASN   C 1 88 ? 9.719   -19.510 19.105  1.00 36.57 ? 87  ASN   C N    1 
ATOM   2178 C  CA   . ASN   C 1 88 ? 9.085   -19.867 20.370  1.00 30.66 ? 87  ASN   C CA   1 
ATOM   2179 C  C    . ASN   C 1 88 ? 9.981   -20.803 21.173  1.00 37.27 ? 87  ASN   C C    1 
ATOM   2180 O  O    . ASN   C 1 88 ? 9.571   -21.926 21.497  1.00 35.51 ? 87  ASN   C O    1 
ATOM   2181 C  CB   . ASN   C 1 88 ? 7.726   -20.519 20.109  1.00 37.91 ? 87  ASN   C CB   1 
ATOM   2182 C  CG   . ASN   C 1 88 ? 6.820   -20.479 21.322  1.00 44.84 ? 87  ASN   C CG   1 
ATOM   2183 O  OD1  . ASN   C 1 88 ? 7.103   -19.784 22.297  1.00 49.33 ? 87  ASN   C OD1  1 
ATOM   2184 N  ND2  . ASN   C 1 88 ? 5.717   -21.217 21.262  1.00 47.74 ? 87  ASN   C ND2  1 
ATOM   2185 N  N    . PRO   C 1 89 ? 11.201  -20.379 21.523  1.00 32.78 ? 88  PRO   C N    1 
ATOM   2186 C  CA   . PRO   C 1 89 ? 12.183  -21.336 22.055  1.00 31.88 ? 88  PRO   C CA   1 
ATOM   2187 C  C    . PRO   C 1 89 ? 11.949  -21.759 23.494  1.00 44.75 ? 88  PRO   C C    1 
ATOM   2188 O  O    . PRO   C 1 89 ? 12.416  -22.838 23.881  1.00 36.40 ? 88  PRO   C O    1 
ATOM   2189 C  CB   . PRO   C 1 89 ? 13.509  -20.580 21.923  1.00 30.14 ? 88  PRO   C CB   1 
ATOM   2190 C  CG   . PRO   C 1 89 ? 13.119  -19.146 22.049  1.00 37.59 ? 88  PRO   C CG   1 
ATOM   2191 C  CD   . PRO   C 1 89 ? 11.758  -19.019 21.415  1.00 36.55 ? 88  PRO   C CD   1 
ATOM   2192 N  N    . HIS   C 1 90 ? 11.255  -20.959 24.300  1.00 42.77 ? 89  HIS   C N    1 
ATOM   2193 C  CA   . HIS   C 1 90 ? 11.081  -21.258 25.715  1.00 47.34 ? 89  HIS   C CA   1 
ATOM   2194 C  C    . HIS   C 1 90 ? 9.631   -21.571 26.071  1.00 48.86 ? 89  HIS   C C    1 
ATOM   2195 O  O    . HIS   C 1 90 ? 9.177   -21.261 27.174  1.00 63.00 ? 89  HIS   C O    1 
ATOM   2196 C  CB   . HIS   C 1 90 ? 11.605  -20.106 26.567  1.00 43.92 ? 89  HIS   C CB   1 
ATOM   2197 C  CG   . HIS   C 1 90 ? 13.049  -19.800 26.335  1.00 41.04 ? 89  HIS   C CG   1 
ATOM   2198 N  ND1  . HIS   C 1 90 ? 13.476  -18.643 25.722  1.00 39.98 ? 89  HIS   C ND1  1 
ATOM   2199 C  CD2  . HIS   C 1 90 ? 14.167  -20.508 26.621  1.00 44.70 ? 89  HIS   C CD2  1 
ATOM   2200 C  CE1  . HIS   C 1 90 ? 14.794  -18.645 25.648  1.00 37.86 ? 89  HIS   C CE1  1 
ATOM   2201 N  NE2  . HIS   C 1 90 ? 15.239  -19.766 26.187  1.00 49.40 ? 89  HIS   C NE2  1 
ATOM   2202 N  N    . ALA   C 1 91 ? 8.898   -22.191 25.152  1.00 45.31 ? 90  ALA   C N    1 
ATOM   2203 C  CA   . ALA   C 1 91 ? 7.555   -22.672 25.444  1.00 58.87 ? 90  ALA   C CA   1 
ATOM   2204 C  C    . ALA   C 1 91 ? 7.658   -23.979 26.229  1.00 66.57 ? 90  ALA   C C    1 
ATOM   2205 O  O    . ALA   C 1 91 ? 8.727   -24.353 26.722  1.00 67.89 ? 90  ALA   C O    1 
ATOM   2206 C  CB   . ALA   C 1 91 ? 6.755   -22.830 24.155  1.00 55.93 ? 90  ALA   C CB   1 
ATOM   2207 N  N    . SER   C 1 92 ? 6.542   -24.698 26.355  1.00 62.87 ? 91  SER   C N    1 
ATOM   2208 C  CA   . SER   C 1 92 ? 6.517   -25.960 27.086  1.00 61.43 ? 91  SER   C CA   1 
ATOM   2209 C  C    . SER   C 1 92 ? 6.424   -27.186 26.192  1.00 69.31 ? 91  SER   C C    1 
ATOM   2210 O  O    . SER   C 1 92 ? 6.999   -28.222 26.535  1.00 70.99 ? 91  SER   C O    1 
ATOM   2211 C  CB   . SER   C 1 92 ? 5.349   -25.979 28.080  1.00 63.52 ? 91  SER   C CB   1 
ATOM   2212 O  OG   . SER   C 1 92 ? 5.550   -25.031 29.114  1.00 63.96 ? 91  SER   C OG   1 
ATOM   2213 N  N    . TYR   C 1 93 ? 5.717   -27.093 25.068  1.00 68.89 ? 92  TYR   C N    1 
ATOM   2214 C  CA   . TYR   C 1 93 ? 5.616   -28.180 24.093  1.00 70.47 ? 92  TYR   C CA   1 
ATOM   2215 C  C    . TYR   C 1 93 ? 5.197   -29.506 24.724  1.00 72.03 ? 92  TYR   C C    1 
ATOM   2216 O  O    . TYR   C 1 93 ? 4.208   -29.570 25.454  1.00 78.22 ? 92  TYR   C O    1 
ATOM   2217 C  CB   . TYR   C 1 93 ? 6.944   -28.347 23.352  1.00 65.14 ? 92  TYR   C CB   1 
ATOM   2218 C  CG   . TYR   C 1 93 ? 7.350   -27.109 22.590  1.00 59.75 ? 92  TYR   C CG   1 
ATOM   2219 C  CD1  . TYR   C 1 93 ? 6.713   -26.765 21.405  1.00 55.55 ? 92  TYR   C CD1  1 
ATOM   2220 C  CD2  . TYR   C 1 93 ? 8.359   -26.277 23.058  1.00 54.63 ? 92  TYR   C CD2  1 
ATOM   2221 C  CE1  . TYR   C 1 93 ? 7.070   -25.631 20.705  1.00 55.23 ? 92  TYR   C CE1  1 
ATOM   2222 C  CE2  . TYR   C 1 93 ? 8.726   -25.139 22.359  1.00 54.46 ? 92  TYR   C CE2  1 
ATOM   2223 C  CZ   . TYR   C 1 93 ? 8.076   -24.823 21.185  1.00 47.50 ? 92  TYR   C CZ   1 
ATOM   2224 O  OH   . TYR   C 1 93 ? 8.429   -23.695 20.482  1.00 53.55 ? 92  TYR   C OH   1 
HETATM 2225 C  C01  . A1D73 D 2 .  ? 0.390   -26.068 -5.545  0.50 45.95 ? 101 A1D73 A C01  1 
HETATM 2226 C  C02  . A1D73 D 2 .  ? -0.156  -26.195 -6.809  0.50 45.37 ? 101 A1D73 A C02  1 
HETATM 2227 C  C04  . A1D73 D 2 .  ? 1.123   -24.502 -7.630  0.50 41.70 ? 101 A1D73 A C04  1 
HETATM 2228 C  C05  . A1D73 D 2 .  ? 1.730   -24.295 -6.405  0.50 35.96 ? 101 A1D73 A C05  1 
HETATM 2229 C  C06  . A1D73 D 2 .  ? 1.360   -25.097 -5.329  0.50 35.16 ? 101 A1D73 A C06  1 
HETATM 2230 C  C07  . A1D73 D 2 .  ? 2.053   -24.985 -4.024  0.50 37.07 ? 101 A1D73 A C07  1 
HETATM 2231 C  C08  . A1D73 D 2 .  ? 1.669   -24.518 -2.752  0.50 35.93 ? 101 A1D73 A C08  1 
HETATM 2232 C  C09  . A1D73 D 2 .  ? 2.794   -24.653 -1.945  0.50 26.98 ? 101 A1D73 A C09  1 
HETATM 2233 N  N03  . A1D73 D 2 .  ? 0.190   -25.433 -7.853  0.50 47.12 ? 101 A1D73 A N03  1 
HETATM 2234 N  N10  . A1D73 D 2 .  ? 3.821   -25.160 -2.616  0.50 34.78 ? 101 A1D73 A N10  1 
HETATM 2235 N  N11  . A1D73 D 2 .  ? 3.348   -25.357 -3.883  0.50 33.20 ? 101 A1D73 A N11  1 
HETATM 2236 BR BR12 . A1D73 D 2 .  ? -0.008  -23.829 -2.285  0.50 50.62 ? 101 A1D73 A BR12 1 
HETATM 2237 S  S    . SO4   E 3 .  ? 1.303   -33.784 1.971   0.76 50.31 ? 102 SO4   A S    1 
HETATM 2238 O  O1   . SO4   E 3 .  ? 1.678   -34.273 0.606   0.76 54.29 ? 102 SO4   A O1   1 
HETATM 2239 O  O2   . SO4   E 3 .  ? 1.480   -32.298 2.044   0.76 40.81 ? 102 SO4   A O2   1 
HETATM 2240 O  O3   . SO4   E 3 .  ? -0.133  -34.120 2.242   0.76 58.97 ? 102 SO4   A O3   1 
HETATM 2241 O  O4   . SO4   E 3 .  ? 2.172   -34.445 2.999   0.76 51.18 ? 102 SO4   A O4   1 
HETATM 2242 S  S    . SO4   F 3 .  ? -9.567  -25.092 1.516   0.68 55.22 ? 103 SO4   A S    1 
HETATM 2243 O  O1   . SO4   F 3 .  ? -9.586  -24.773 0.052   0.68 36.71 ? 103 SO4   A O1   1 
HETATM 2244 O  O2   . SO4   F 3 .  ? -9.513  -23.819 2.305   0.68 50.12 ? 103 SO4   A O2   1 
HETATM 2245 O  O3   . SO4   F 3 .  ? -10.807 -25.852 1.876   0.68 51.75 ? 103 SO4   A O3   1 
HETATM 2246 O  O4   . SO4   F 3 .  ? -8.362  -25.924 1.835   0.68 49.00 ? 103 SO4   A O4   1 
HETATM 2247 C  C01  . A1D73 G 2 .  ? 18.915  -17.702 -23.395 0.57 37.46 ? 101 A1D73 B C01  1 
HETATM 2248 C  C02  . A1D73 G 2 .  ? 19.727  -18.498 -22.611 0.57 39.29 ? 101 A1D73 B C02  1 
HETATM 2249 C  C04  . A1D73 G 2 .  ? 21.133  -16.767 -22.150 0.57 47.43 ? 101 A1D73 B C04  1 
HETATM 2250 C  C05  . A1D73 G 2 .  ? 20.387  -15.890 -22.913 0.57 46.04 ? 101 A1D73 B C05  1 
HETATM 2251 C  C06  . A1D73 G 2 .  ? 19.247  -16.362 -23.552 0.57 43.30 ? 101 A1D73 B C06  1 
HETATM 2252 C  C07  . A1D73 G 2 .  ? 18.370  -15.444 -24.305 0.57 35.36 ? 101 A1D73 B C07  1 
HETATM 2253 C  C08  . A1D73 G 2 .  ? 17.531  -15.596 -25.426 0.57 25.61 ? 101 A1D73 B C08  1 
HETATM 2254 C  C09  . A1D73 G 2 .  ? 16.954  -14.345 -25.628 0.57 26.05 ? 101 A1D73 B C09  1 
HETATM 2255 N  N03  . A1D73 G 2 .  ? 20.824  -18.057 -21.989 0.57 46.60 ? 101 A1D73 B N03  1 
HETATM 2256 N  N10  . A1D73 G 2 .  ? 17.372  -13.458 -24.731 0.57 30.19 ? 101 A1D73 B N10  1 
HETATM 2257 N  N11  . A1D73 G 2 .  ? 18.237  -14.151 -23.931 0.57 27.37 ? 101 A1D73 B N11  1 
HETATM 2258 BR BR12 . A1D73 G 2 .  ? 17.279  -17.170 -26.426 0.57 32.73 ? 101 A1D73 B BR12 1 
HETATM 2259 S  S    . SO4   H 3 .  ? 7.435   -8.457  -24.232 0.82 48.81 ? 102 SO4   B S    1 
HETATM 2260 O  O1   . SO4   H 3 .  ? 8.506   -8.602  -25.269 0.82 37.88 ? 102 SO4   B O1   1 
HETATM 2261 O  O2   . SO4   H 3 .  ? 6.119   -8.855  -24.825 0.82 41.05 ? 102 SO4   B O2   1 
HETATM 2262 O  O3   . SO4   H 3 .  ? 7.737   -9.324  -23.047 0.82 34.08 ? 102 SO4   B O3   1 
HETATM 2263 O  O4   . SO4   H 3 .  ? 7.380   -7.020  -23.806 0.82 49.53 ? 102 SO4   B O4   1 
HETATM 2264 S  S    . SO4   I 3 .  ? 14.207  -26.919 -26.340 0.74 48.86 ? 103 SO4   B S    1 
HETATM 2265 O  O1   . SO4   I 3 .  ? 15.705  -26.945 -26.335 0.74 42.10 ? 103 SO4   B O1   1 
HETATM 2266 O  O2   . SO4   I 3 .  ? 13.678  -28.161 -26.988 0.74 59.17 ? 103 SO4   B O2   1 
HETATM 2267 O  O3   . SO4   I 3 .  ? 13.709  -26.852 -24.928 0.74 50.73 ? 103 SO4   B O3   1 
HETATM 2268 O  O4   . SO4   I 3 .  ? 13.732  -25.718 -27.098 0.74 51.18 ? 103 SO4   B O4   1 
HETATM 2269 C  C01  . A1D73 J 2 .  ? 17.038  -38.384 20.367  0.94 34.75 ? 101 A1D73 C C01  1 
HETATM 2270 C  C02  . A1D73 J 2 .  ? 17.663  -39.503 20.883  0.94 37.46 ? 101 A1D73 C C02  1 
HETATM 2271 C  C04  . A1D73 J 2 .  ? 19.000  -39.707 19.050  0.94 35.66 ? 101 A1D73 C C04  1 
HETATM 2272 C  C05  . A1D73 J 2 .  ? 18.437  -38.598 18.449  0.94 32.94 ? 101 A1D73 C C05  1 
HETATM 2273 C  C06  . A1D73 J 2 .  ? 17.430  -37.916 19.119  0.94 30.10 ? 101 A1D73 C C06  1 
HETATM 2274 C  C07  . A1D73 J 2 .  ? 16.770  -36.748 18.507  0.94 29.22 ? 101 A1D73 C C07  1 
HETATM 2275 C  C08  . A1D73 J 2 .  ? 17.237  -35.673 17.741  0.94 30.17 ? 101 A1D73 C C08  1 
HETATM 2276 C  C09  . A1D73 J 2 .  ? 16.115  -34.896 17.466  0.94 29.15 ? 101 A1D73 C C09  1 
HETATM 2277 N  N03  . A1D73 J 2 .  ? 18.633  -40.170 20.250  0.94 29.15 ? 101 A1D73 C N03  1 
HETATM 2278 N  N10  . A1D73 J 2 .  ? 15.014  -35.414 18.004  0.94 25.86 ? 101 A1D73 C N10  1 
HETATM 2279 N  N11  . A1D73 J 2 .  ? 15.438  -36.547 18.636  0.94 34.30 ? 101 A1D73 C N11  1 
HETATM 2280 BR BR12 . A1D73 J 2 .  ? 19.020  -35.368 17.220  0.94 28.93 ? 101 A1D73 C BR12 1 
HETATM 2281 S  S    . SO4   K 3 .  ? 27.742  -39.589 24.022  0.61 51.78 ? 102 SO4   C S    1 
HETATM 2282 O  O1   . SO4   K 3 .  ? 29.109  -38.989 24.144  0.61 43.63 ? 102 SO4   C O1   1 
HETATM 2283 O  O2   . SO4   K 3 .  ? 27.260  -39.460 22.610  0.61 53.85 ? 102 SO4   C O2   1 
HETATM 2284 O  O3   . SO4   K 3 .  ? 27.803  -41.040 24.396  0.61 50.58 ? 102 SO4   C O3   1 
HETATM 2285 O  O4   . SO4   K 3 .  ? 26.797  -38.869 24.936  0.61 46.48 ? 102 SO4   C O4   1 
HETATM 2286 O  O    . HOH   L 4 .  ? -2.609  -30.568 -4.233  1.00 39.36 ? 201 HOH   A O    1 
HETATM 2287 O  O    . HOH   L 4 .  ? -5.749  -13.190 -16.320 1.00 44.25 ? 202 HOH   A O    1 
HETATM 2288 O  O    . HOH   L 4 .  ? -0.312  -33.688 4.542   1.00 48.16 ? 203 HOH   A O    1 
HETATM 2289 O  O    . HOH   L 4 .  ? -4.076  -28.562 4.996   1.00 49.89 ? 204 HOH   A O    1 
HETATM 2290 O  O    . HOH   L 4 .  ? 10.750  -29.675 3.232   1.00 37.10 ? 205 HOH   A O    1 
HETATM 2291 O  O    . HOH   L 4 .  ? -0.592  -31.606 0.578   1.00 54.18 ? 206 HOH   A O    1 
HETATM 2292 O  O    . HOH   L 4 .  ? 1.433   -32.011 -0.418  1.00 46.20 ? 207 HOH   A O    1 
HETATM 2293 O  O    . HOH   L 4 .  ? 5.672   -28.775 6.913   1.00 35.53 ? 208 HOH   A O    1 
HETATM 2294 O  O    . HOH   L 4 .  ? 9.285   -22.508 -9.389  1.00 34.82 ? 209 HOH   A O    1 
HETATM 2295 O  O    . HOH   L 4 .  ? 15.503  -24.462 1.873   1.00 32.95 ? 210 HOH   A O    1 
HETATM 2296 O  O    . HOH   L 4 .  ? -0.814  -29.231 9.691   1.00 49.34 ? 211 HOH   A O    1 
HETATM 2297 O  O    . HOH   L 4 .  ? 4.203   -3.565  -3.178  1.00 33.02 ? 212 HOH   A O    1 
HETATM 2298 O  O    . HOH   L 4 .  ? 6.562   -18.071 10.938  1.00 39.01 ? 213 HOH   A O    1 
HETATM 2299 O  O    . HOH   L 4 .  ? 4.254   -7.857  1.343   1.00 38.50 ? 214 HOH   A O    1 
HETATM 2300 O  O    . HOH   L 4 .  ? -8.695  -18.712 -3.076  1.00 41.84 ? 215 HOH   A O    1 
HETATM 2301 O  O    . HOH   L 4 .  ? 10.444  -5.138  -7.597  1.00 31.67 ? 216 HOH   A O    1 
HETATM 2302 O  O    . HOH   L 4 .  ? -0.989  -20.929 6.932   1.00 28.92 ? 217 HOH   A O    1 
HETATM 2303 O  O    . HOH   L 4 .  ? -6.265  -11.160 -11.127 1.00 38.91 ? 218 HOH   A O    1 
HETATM 2304 O  O    . HOH   L 4 .  ? -11.254 -22.925 -0.841  1.00 50.73 ? 219 HOH   A O    1 
HETATM 2305 O  O    . HOH   L 4 .  ? 2.562   -25.165 -10.170 1.00 32.31 ? 220 HOH   A O    1 
HETATM 2306 O  O    . HOH   L 4 .  ? 3.177   -29.483 -0.404  1.00 42.69 ? 221 HOH   A O    1 
HETATM 2307 O  O    . HOH   L 4 .  ? -9.671  -18.714 -7.315  1.00 50.57 ? 222 HOH   A O    1 
HETATM 2308 O  O    . HOH   L 4 .  ? 11.263  -11.987 5.989   1.00 33.27 ? 223 HOH   A O    1 
HETATM 2309 O  O    . HOH   L 4 .  ? 19.523  -15.631 7.331   1.00 31.06 ? 224 HOH   A O    1 
HETATM 2310 O  O    . HOH   L 4 .  ? 7.002   -10.485 -11.935 1.00 37.40 ? 225 HOH   A O    1 
HETATM 2311 O  O    . HOH   L 4 .  ? 9.786   -12.987 9.606   1.00 44.22 ? 226 HOH   A O    1 
HETATM 2312 O  O    . HOH   L 4 .  ? -4.589  -20.984 6.186   1.00 36.04 ? 227 HOH   A O    1 
HETATM 2313 O  O    . HOH   L 4 .  ? 0.886   -17.411 -19.020 1.00 43.58 ? 228 HOH   A O    1 
HETATM 2314 O  O    . HOH   L 4 .  ? 8.606   -17.957 -11.134 1.00 35.66 ? 229 HOH   A O    1 
HETATM 2315 O  O    . HOH   L 4 .  ? 14.740  -18.545 -7.142  1.00 40.15 ? 230 HOH   A O    1 
HETATM 2316 O  O    . HOH   L 4 .  ? 16.938  -12.897 1.405   1.00 21.37 ? 231 HOH   A O    1 
HETATM 2317 O  O    . HOH   L 4 .  ? 15.457  -27.801 -0.211  1.00 51.42 ? 232 HOH   A O    1 
HETATM 2318 O  O    . HOH   L 4 .  ? -7.992  -16.637 1.738   1.00 39.69 ? 233 HOH   A O    1 
HETATM 2319 O  O    . HOH   L 4 .  ? -1.914  -21.899 -0.478  1.00 23.65 ? 234 HOH   A O    1 
HETATM 2320 O  O    . HOH   L 4 .  ? -5.934  -19.628 -5.536  1.00 34.66 ? 235 HOH   A O    1 
HETATM 2321 O  O    . HOH   L 4 .  ? -5.861  -15.687 -7.924  1.00 29.90 ? 236 HOH   A O    1 
HETATM 2322 O  O    . HOH   L 4 .  ? -1.409  -7.405  11.614  1.00 42.27 ? 237 HOH   A O    1 
HETATM 2323 O  O    . HOH   L 4 .  ? 9.343   -5.926  -1.443  1.00 37.42 ? 238 HOH   A O    1 
HETATM 2324 O  O    . HOH   L 4 .  ? -4.767  -25.726 -5.689  1.00 32.15 ? 239 HOH   A O    1 
HETATM 2325 O  O    . HOH   L 4 .  ? 1.543   0.683   -7.460  1.00 41.05 ? 240 HOH   A O    1 
HETATM 2326 O  O    . HOH   L 4 .  ? 8.280   -17.760 -15.440 1.00 39.19 ? 241 HOH   A O    1 
HETATM 2327 O  O    . HOH   L 4 .  ? -2.693  3.565   -2.198  1.00 41.83 ? 242 HOH   A O    1 
HETATM 2328 O  O    . HOH   L 4 .  ? 2.009   -2.020  -0.708  1.00 44.72 ? 243 HOH   A O    1 
HETATM 2329 O  O    . HOH   L 4 .  ? -0.035  -22.689 9.397   1.00 38.34 ? 244 HOH   A O    1 
HETATM 2330 O  O    . HOH   L 4 .  ? 7.460   -7.721  1.298   1.00 29.13 ? 245 HOH   A O    1 
HETATM 2331 O  O    . HOH   L 4 .  ? 12.560  -13.728 -8.405  1.00 43.05 ? 246 HOH   A O    1 
HETATM 2332 O  O    . HOH   L 4 .  ? 0.710   -10.240 -15.661 1.00 42.96 ? 247 HOH   A O    1 
HETATM 2333 O  O    . HOH   L 4 .  ? 11.387  -16.437 -14.484 1.00 40.88 ? 248 HOH   A O    1 
HETATM 2334 O  O    . HOH   L 4 .  ? -0.950  -20.489 11.248  1.00 47.86 ? 249 HOH   A O    1 
HETATM 2335 O  O    . HOH   L 4 .  ? 5.242   -8.159  4.119   1.00 35.36 ? 250 HOH   A O    1 
HETATM 2336 O  O    . HOH   L 4 .  ? 11.345  -12.232 -6.071  1.00 32.75 ? 251 HOH   A O    1 
HETATM 2337 O  O    . HOH   L 4 .  ? 1.589   -4.498  -10.252 1.00 32.28 ? 252 HOH   A O    1 
HETATM 2338 O  O    . HOH   L 4 .  ? -8.675  -21.237 -1.511  1.00 37.94 ? 253 HOH   A O    1 
HETATM 2339 O  O    . HOH   L 4 .  ? 1.553   -10.477 11.971  1.00 35.19 ? 254 HOH   A O    1 
HETATM 2340 O  O    . HOH   L 4 .  ? -6.081  -26.730 3.453   1.00 46.80 ? 255 HOH   A O    1 
HETATM 2341 O  O    . HOH   L 4 .  ? 14.224  -29.143 4.353   1.00 34.94 ? 256 HOH   A O    1 
HETATM 2342 O  O    . HOH   L 4 .  ? 8.891   -28.623 5.583   1.00 39.00 ? 257 HOH   A O    1 
HETATM 2343 O  O    . HOH   L 4 .  ? -8.175  -15.719 -0.853  1.00 34.24 ? 258 HOH   A O    1 
HETATM 2344 O  O    . HOH   L 4 .  ? -8.785  -16.084 -12.000 1.00 51.19 ? 259 HOH   A O    1 
HETATM 2345 O  O    . HOH   L 4 .  ? 12.482  -18.305 -8.302  1.00 35.29 ? 260 HOH   A O    1 
HETATM 2346 O  O    . HOH   L 4 .  ? 22.459  -16.729 0.510   1.00 48.78 ? 261 HOH   A O    1 
HETATM 2347 O  O    . HOH   L 4 .  ? -11.061 -16.033 -3.350  1.00 48.91 ? 262 HOH   A O    1 
HETATM 2348 O  O    . HOH   L 4 .  ? 16.828  -12.607 -16.560 1.00 41.50 ? 263 HOH   A O    1 
HETATM 2349 O  O    . HOH   L 4 .  ? 12.940  -11.900 -4.434  1.00 27.63 ? 264 HOH   A O    1 
HETATM 2350 O  O    . HOH   L 4 .  ? 12.982  -28.357 -4.588  1.00 49.25 ? 265 HOH   A O    1 
HETATM 2351 O  O    . HOH   L 4 .  ? 9.511   -20.339 -18.174 1.00 46.23 ? 266 HOH   A O    1 
HETATM 2352 O  O    . HOH   L 4 .  ? 6.275   -5.365  0.524   1.00 45.66 ? 267 HOH   A O    1 
HETATM 2353 O  O    . HOH   L 4 .  ? 8.078   -17.532 9.073   1.00 40.08 ? 268 HOH   A O    1 
HETATM 2354 O  O    . HOH   L 4 .  ? 10.867  -7.807  0.449   1.00 26.37 ? 269 HOH   A O    1 
HETATM 2355 O  O    . HOH   L 4 .  ? 8.099   -31.789 4.432   1.00 43.06 ? 270 HOH   A O    1 
HETATM 2356 O  O    . HOH   L 4 .  ? 15.389  -11.701 -5.500  1.00 42.13 ? 271 HOH   A O    1 
HETATM 2357 O  O    . HOH   L 4 .  ? 10.861  -5.972  -3.275  1.00 42.83 ? 272 HOH   A O    1 
HETATM 2358 O  O    . HOH   L 4 .  ? -7.417  -11.552 -8.064  1.00 30.33 ? 273 HOH   A O    1 
HETATM 2359 O  O    . HOH   L 4 .  ? 8.670   -16.453 -13.165 1.00 38.09 ? 274 HOH   A O    1 
HETATM 2360 O  O    . HOH   L 4 .  ? 20.928  -16.757 -3.100  1.00 35.07 ? 275 HOH   A O    1 
HETATM 2361 O  O    . HOH   L 4 .  ? 8.934   -9.208  -13.542 1.00 42.44 ? 276 HOH   A O    1 
HETATM 2362 O  O    . HOH   L 4 .  ? 3.144   -9.738  -13.143 1.00 37.66 ? 277 HOH   A O    1 
HETATM 2363 O  O    . HOH   L 4 .  ? -5.757  -17.806 -10.030 1.00 43.88 ? 278 HOH   A O    1 
HETATM 2364 O  O    . HOH   L 4 .  ? 16.137  -13.690 10.689  1.00 41.70 ? 279 HOH   A O    1 
HETATM 2365 O  O    . HOH   L 4 .  ? 10.622  -27.127 -8.003  1.00 52.50 ? 280 HOH   A O    1 
HETATM 2366 O  O    . HOH   L 4 .  ? -5.788  -23.646 -6.845  1.00 30.45 ? 281 HOH   A O    1 
HETATM 2367 O  O    . HOH   L 4 .  ? -0.682  -7.870  -13.077 1.00 45.10 ? 282 HOH   A O    1 
HETATM 2368 O  O    . HOH   L 4 .  ? 4.900   -6.858  -11.035 1.00 41.11 ? 283 HOH   A O    1 
HETATM 2369 O  O    . HOH   L 4 .  ? -7.576  -13.981 -9.312  1.00 39.53 ? 284 HOH   A O    1 
HETATM 2370 O  O    . HOH   L 4 .  ? 4.790   -29.081 -9.550  1.00 45.54 ? 285 HOH   A O    1 
HETATM 2371 O  O    . HOH   L 4 .  ? 0.163   -16.449 -21.041 1.00 48.84 ? 286 HOH   A O    1 
HETATM 2372 O  O    . HOH   L 4 .  ? 3.088   -5.324  -11.942 1.00 36.24 ? 287 HOH   A O    1 
HETATM 2373 O  O    . HOH   L 4 .  ? 8.712   -28.557 -7.992  1.00 54.44 ? 288 HOH   A O    1 
HETATM 2374 O  O    . HOH   L 4 .  ? 4.968   -9.564  -11.310 1.00 47.04 ? 289 HOH   A O    1 
HETATM 2375 O  O    . HOH   L 4 .  ? -6.561  -22.582 5.809   1.00 53.64 ? 290 HOH   A O    1 
HETATM 2376 O  O    . HOH   L 4 .  ? 5.680   -3.225  1.225   1.00 48.54 ? 291 HOH   A O    1 
HETATM 2377 O  O    . HOH   L 4 .  ? 7.969   -8.201  4.699   1.00 35.48 ? 292 HOH   A O    1 
HETATM 2378 O  O    . HOH   L 4 .  ? 2.666   -5.974  0.512   1.00 42.89 ? 293 HOH   A O    1 
HETATM 2379 O  O    . HOH   L 4 .  ? -9.822  -14.985 -10.143 1.00 44.36 ? 294 HOH   A O    1 
HETATM 2380 O  O    . HOH   L 4 .  ? -5.432  -20.709 -8.166  1.00 46.23 ? 295 HOH   A O    1 
HETATM 2381 O  O    . HOH   M 4 .  ? 19.734  -22.418 -23.238 1.00 46.58 ? 201 HOH   B O    1 
HETATM 2382 O  O    . HOH   M 4 .  ? 30.684  -8.170  -29.625 1.00 46.17 ? 202 HOH   B O    1 
HETATM 2383 O  O    . HOH   M 4 .  ? 15.189  -17.604 -18.920 1.00 39.16 ? 203 HOH   B O    1 
HETATM 2384 O  O    . HOH   M 4 .  ? 27.633  -8.494  -28.619 1.00 44.54 ? 204 HOH   B O    1 
HETATM 2385 O  O    . HOH   M 4 .  ? 25.148  -5.021  -29.442 1.00 34.58 ? 205 HOH   B O    1 
HETATM 2386 O  O    . HOH   M 4 .  ? 6.660   -12.345 -25.683 1.00 36.14 ? 206 HOH   B O    1 
HETATM 2387 O  O    . HOH   M 4 .  ? 11.403  -28.699 -25.973 1.00 49.79 ? 207 HOH   B O    1 
HETATM 2388 O  O    . HOH   M 4 .  ? 13.337  -4.421  -41.223 1.00 51.11 ? 208 HOH   B O    1 
HETATM 2389 O  O    . HOH   M 4 .  ? 16.728  -19.265 -28.568 1.00 24.42 ? 209 HOH   B O    1 
HETATM 2390 O  O    . HOH   M 4 .  ? 26.225  -22.992 -30.898 1.00 32.39 ? 210 HOH   B O    1 
HETATM 2391 O  O    . HOH   M 4 .  ? 6.113   -7.568  -31.824 1.00 50.93 ? 211 HOH   B O    1 
HETATM 2392 O  O    . HOH   M 4 .  ? 30.374  -19.634 -40.060 1.00 35.02 ? 212 HOH   B O    1 
HETATM 2393 O  O    . HOH   M 4 .  ? 12.743  -25.988 -37.081 1.00 46.34 ? 213 HOH   B O    1 
HETATM 2394 O  O    . HOH   M 4 .  ? 12.727  -22.611 -20.651 1.00 47.51 ? 214 HOH   B O    1 
HETATM 2395 O  O    . HOH   M 4 .  ? 17.823  -3.504  -21.924 1.00 48.44 ? 215 HOH   B O    1 
HETATM 2396 O  O    . HOH   M 4 .  ? 20.785  -13.112 -42.390 1.00 37.57 ? 216 HOH   B O    1 
HETATM 2397 O  O    . HOH   M 4 .  ? 23.192  -2.201  -28.765 1.00 36.26 ? 217 HOH   B O    1 
HETATM 2398 O  O    . HOH   M 4 .  ? 32.230  -18.658 -42.287 1.00 41.46 ? 218 HOH   B O    1 
HETATM 2399 O  O    . HOH   M 4 .  ? 10.481  -18.686 -32.520 1.00 25.65 ? 219 HOH   B O    1 
HETATM 2400 O  O    . HOH   M 4 .  ? 3.992   -19.067 -30.338 1.00 46.70 ? 220 HOH   B O    1 
HETATM 2401 O  O    . HOH   M 4 .  ? 7.562   -8.204  -20.529 1.00 41.21 ? 221 HOH   B O    1 
HETATM 2402 O  O    . HOH   M 4 .  ? 18.154  -0.456  -38.049 1.00 25.41 ? 222 HOH   B O    1 
HETATM 2403 O  O    . HOH   M 4 .  ? 8.927   -8.602  -16.038 1.00 40.51 ? 223 HOH   B O    1 
HETATM 2404 O  O    . HOH   M 4 .  ? 10.767  -21.634 -32.476 1.00 37.55 ? 224 HOH   B O    1 
HETATM 2405 O  O    . HOH   M 4 .  ? 19.921  -25.593 -33.945 1.00 33.74 ? 225 HOH   B O    1 
HETATM 2406 O  O    . HOH   M 4 .  ? 12.801  -26.410 -29.644 1.00 52.79 ? 226 HOH   B O    1 
HETATM 2407 O  O    . HOH   M 4 .  ? 17.338  -0.417  -24.695 1.00 50.81 ? 227 HOH   B O    1 
HETATM 2408 O  O    . HOH   M 4 .  ? 7.554   -12.438 -38.436 1.00 47.51 ? 228 HOH   B O    1 
HETATM 2409 O  O    . HOH   M 4 .  ? 14.396  -23.818 -40.283 1.00 42.70 ? 229 HOH   B O    1 
HETATM 2410 O  O    . HOH   M 4 .  ? 14.302  -6.353  -40.752 1.00 41.86 ? 230 HOH   B O    1 
HETATM 2411 O  O    . HOH   M 4 .  ? 16.182  -25.987 -34.303 1.00 41.98 ? 231 HOH   B O    1 
HETATM 2412 O  O    . HOH   M 4 .  ? 2.205   -13.072 -27.430 1.00 47.22 ? 232 HOH   B O    1 
HETATM 2413 O  O    . HOH   M 4 .  ? 34.581  -23.320 -29.774 1.00 55.16 ? 233 HOH   B O    1 
HETATM 2414 O  O    . HOH   M 4 .  ? 27.705  -17.499 -24.707 1.00 39.79 ? 234 HOH   B O    1 
HETATM 2415 O  O    . HOH   M 4 .  ? 26.328  -4.379  -33.178 1.00 42.98 ? 235 HOH   B O    1 
HETATM 2416 O  O    . HOH   M 4 .  ? 20.393  -9.803  -42.608 1.00 38.00 ? 236 HOH   B O    1 
HETATM 2417 O  O    . HOH   M 4 .  ? 7.837   -5.006  -21.758 1.00 51.35 ? 237 HOH   B O    1 
HETATM 2418 O  O    . HOH   M 4 .  ? 25.232  -5.645  -35.497 1.00 42.90 ? 238 HOH   B O    1 
HETATM 2419 O  O    . HOH   M 4 .  ? 22.644  -23.124 -28.497 1.00 34.71 ? 239 HOH   B O    1 
HETATM 2420 O  O    . HOH   M 4 .  ? 21.216  -6.470  -42.234 1.00 33.68 ? 240 HOH   B O    1 
HETATM 2421 O  O    . HOH   M 4 .  ? 23.618  -10.915 -21.713 1.00 42.37 ? 241 HOH   B O    1 
HETATM 2422 O  O    . HOH   M 4 .  ? 7.914   -18.353 -31.383 1.00 36.89 ? 242 HOH   B O    1 
HETATM 2423 O  O    . HOH   M 4 .  ? 24.966  -6.800  -42.274 1.00 49.72 ? 243 HOH   B O    1 
HETATM 2424 O  O    . HOH   M 4 .  ? 18.097  -26.075 -28.981 1.00 35.77 ? 244 HOH   B O    1 
HETATM 2425 O  O    . HOH   M 4 .  ? 20.660  3.837   -32.578 1.00 37.73 ? 245 HOH   B O    1 
HETATM 2426 O  O    . HOH   M 4 .  ? 24.029  -4.005  -36.611 1.00 35.83 ? 246 HOH   B O    1 
HETATM 2427 O  O    . HOH   M 4 .  ? 18.097  4.588   -34.126 1.00 45.14 ? 247 HOH   B O    1 
HETATM 2428 O  O    . HOH   M 4 .  ? 31.712  -20.709 -38.060 1.00 47.33 ? 248 HOH   B O    1 
HETATM 2429 O  O    . HOH   M 4 .  ? 8.194   -27.893 -38.108 1.00 57.66 ? 249 HOH   B O    1 
HETATM 2430 O  O    . HOH   M 4 .  ? 17.293  -9.492  -43.351 1.00 41.53 ? 250 HOH   B O    1 
HETATM 2431 O  O    . HOH   M 4 .  ? 27.858  -24.836 -34.923 1.00 35.93 ? 251 HOH   B O    1 
HETATM 2432 O  O    . HOH   M 4 .  ? 15.036  -8.084  -42.455 1.00 45.70 ? 252 HOH   B O    1 
HETATM 2433 O  O    . HOH   M 4 .  ? 18.096  -15.563 -45.621 1.00 41.88 ? 253 HOH   B O    1 
HETATM 2434 O  O    . HOH   M 4 .  ? 23.526  -14.630 -43.085 1.00 48.79 ? 254 HOH   B O    1 
HETATM 2435 O  O    . HOH   M 4 .  ? 25.103  -1.636  -37.095 1.00 41.49 ? 255 HOH   B O    1 
HETATM 2436 O  O    . HOH   M 4 .  ? 12.814  -19.967 -19.249 1.00 46.91 ? 256 HOH   B O    1 
HETATM 2437 O  O    . HOH   M 4 .  ? 30.165  -24.136 -33.443 1.00 46.38 ? 257 HOH   B O    1 
HETATM 2438 O  O    . HOH   M 4 .  ? 27.929  -24.886 -32.029 1.00 45.31 ? 258 HOH   B O    1 
HETATM 2439 O  O    . HOH   M 4 .  ? 7.132   -9.767  -18.167 1.00 40.65 ? 259 HOH   B O    1 
HETATM 2440 O  O    . HOH   N 4 .  ? 26.571  -42.671 25.257  1.00 42.86 ? 201 HOH   C O    1 
HETATM 2441 O  O    . HOH   N 4 .  ? 33.541  -23.834 25.907  1.00 55.37 ? 202 HOH   C O    1 
HETATM 2442 O  O    . HOH   N 4 .  ? 27.816  -36.735 24.491  1.00 40.79 ? 203 HOH   C O    1 
HETATM 2443 O  O    . HOH   N 4 .  ? 5.704   -26.403 16.602  1.00 45.51 ? 204 HOH   C O    1 
HETATM 2444 O  O    . HOH   N 4 .  ? 25.624  -19.701 6.271   1.00 36.29 ? 205 HOH   C O    1 
HETATM 2445 O  O    . HOH   N 4 .  ? 18.720  -20.396 10.597  1.00 38.00 ? 206 HOH   C O    1 
HETATM 2446 O  O    . HOH   N 4 .  ? 8.941   -18.963 23.829  1.00 42.35 ? 207 HOH   C O    1 
HETATM 2447 O  O    . HOH   N 4 .  ? 31.342  -43.133 12.130  1.00 40.35 ? 208 HOH   C O    1 
HETATM 2448 O  O    . HOH   N 4 .  ? 15.670  -17.635 19.451  1.00 41.26 ? 209 HOH   C O    1 
HETATM 2449 O  O    . HOH   N 4 .  ? 17.309  -17.076 14.979  1.00 47.24 ? 210 HOH   C O    1 
HETATM 2450 O  O    . HOH   N 4 .  ? 24.860  -31.295 10.765  1.00 33.88 ? 211 HOH   C O    1 
HETATM 2451 O  O    . HOH   N 4 .  ? 19.125  -26.793 3.572   1.00 41.58 ? 212 HOH   C O    1 
HETATM 2452 O  O    . HOH   N 4 .  ? 19.648  -41.655 12.096  1.00 30.92 ? 213 HOH   C O    1 
HETATM 2453 O  O    . HOH   N 4 .  ? 17.712  -35.725 6.765   1.00 43.30 ? 214 HOH   C O    1 
HETATM 2454 O  O    . HOH   N 4 .  ? 15.162  -40.554 15.840  1.00 59.83 ? 215 HOH   C O    1 
HETATM 2455 O  O    . HOH   N 4 .  ? 25.477  -17.425 13.812  1.00 43.15 ? 216 HOH   C O    1 
HETATM 2456 O  O    . HOH   N 4 .  ? 28.069  -37.160 15.625  1.00 42.86 ? 217 HOH   C O    1 
HETATM 2457 O  O    . HOH   N 4 .  ? 7.551   -17.158 22.170  1.00 54.65 ? 218 HOH   C O    1 
HETATM 2458 O  O    . HOH   N 4 .  ? 10.967  -23.604 9.940   1.00 28.62 ? 219 HOH   C O    1 
HETATM 2459 O  O    . HOH   N 4 .  ? 21.821  -34.309 16.351  1.00 24.39 ? 220 HOH   C O    1 
HETATM 2460 O  O    . HOH   N 4 .  ? 24.028  -29.131 9.511   1.00 42.72 ? 221 HOH   C O    1 
HETATM 2461 O  O    . HOH   N 4 .  ? 12.334  -31.300 8.495   1.00 32.13 ? 222 HOH   C O    1 
HETATM 2462 O  O    . HOH   N 4 .  ? 27.947  -33.947 35.540  1.00 49.65 ? 223 HOH   C O    1 
HETATM 2463 O  O    . HOH   N 4 .  ? 23.468  -20.864 23.953  1.00 40.42 ? 224 HOH   C O    1 
HETATM 2464 O  O    . HOH   N 4 .  ? 21.947  -28.576 11.029  1.00 29.20 ? 225 HOH   C O    1 
HETATM 2465 O  O    . HOH   N 4 .  ? 30.029  -39.603 31.125  1.00 38.81 ? 226 HOH   C O    1 
HETATM 2466 O  O    . HOH   N 4 .  ? 15.115  -21.094 12.236  1.00 34.77 ? 227 HOH   C O    1 
HETATM 2467 O  O    . HOH   N 4 .  ? 19.928  -42.277 21.500  1.00 40.76 ? 228 HOH   C O    1 
HETATM 2468 O  O    . HOH   N 4 .  ? 22.467  -41.248 18.436  1.00 38.28 ? 229 HOH   C O    1 
HETATM 2469 O  O    . HOH   N 4 .  ? 13.157  -37.313 13.404  1.00 37.90 ? 230 HOH   C O    1 
HETATM 2470 O  O    . HOH   N 4 .  ? 17.264  -21.161 12.928  1.00 40.19 ? 231 HOH   C O    1 
HETATM 2471 O  O    . HOH   N 4 .  ? 9.303   -30.313 10.587  1.00 37.84 ? 232 HOH   C O    1 
HETATM 2472 O  O    . HOH   N 4 .  ? 4.473   -28.956 11.927  1.00 46.06 ? 233 HOH   C O    1 
HETATM 2473 O  O    . HOH   N 4 .  ? 9.370   -32.887 9.147   1.00 38.37 ? 234 HOH   C O    1 
HETATM 2474 O  O    . HOH   N 4 .  ? 16.019  -33.375 28.619  1.00 48.16 ? 235 HOH   C O    1 
HETATM 2475 O  O    . HOH   N 4 .  ? 25.349  -39.524 19.989  1.00 35.53 ? 236 HOH   C O    1 
HETATM 2476 O  O    . HOH   N 4 .  ? 25.808  -34.292 34.622  1.00 44.65 ? 237 HOH   C O    1 
HETATM 2477 O  O    . HOH   N 4 .  ? 27.886  -37.011 18.876  1.00 44.21 ? 238 HOH   C O    1 
HETATM 2478 O  O    . HOH   N 4 .  ? 20.713  -39.897 26.070  1.00 40.82 ? 239 HOH   C O    1 
HETATM 2479 O  O    . HOH   N 4 .  ? 22.903  -18.387 21.638  1.00 44.89 ? 240 HOH   C O    1 
HETATM 2480 O  O    . HOH   N 4 .  ? 20.253  -19.045 24.621  1.00 42.73 ? 241 HOH   C O    1 
HETATM 2481 O  O    . HOH   N 4 .  ? 30.080  -32.744 17.958  1.00 40.14 ? 242 HOH   C O    1 
HETATM 2482 O  O    . HOH   N 4 .  ? 20.640  -28.706 8.495   1.00 35.99 ? 243 HOH   C O    1 
HETATM 2483 O  O    . HOH   N 4 .  ? 13.022  -38.527 8.635   1.00 34.90 ? 244 HOH   C O    1 
HETATM 2484 O  O    . HOH   N 4 .  ? 29.014  -41.485 27.086  1.00 45.51 ? 245 HOH   C O    1 
HETATM 2485 O  O    . HOH   N 4 .  ? 31.963  -26.302 14.311  1.00 51.89 ? 246 HOH   C O    1 
HETATM 2486 O  O    . HOH   N 4 .  ? 31.360  -39.544 26.908  1.00 43.86 ? 247 HOH   C O    1 
HETATM 2487 O  O    . HOH   N 4 .  ? 32.001  -38.725 29.202  1.00 47.16 ? 248 HOH   C O    1 
HETATM 2488 O  O    . HOH   N 4 .  ? 25.114  -18.055 21.133  1.00 48.26 ? 249 HOH   C O    1 
HETATM 2489 O  O    . HOH   N 4 .  ? 15.863  -38.402 29.076  1.00 50.66 ? 250 HOH   C O    1 
HETATM 2490 O  O    . HOH   N 4 .  ? 19.522  -43.490 17.677  1.00 44.49 ? 251 HOH   C O    1 
HETATM 2491 O  O    . HOH   N 4 .  ? 14.517  -41.601 19.295  1.00 59.25 ? 252 HOH   C O    1 
HETATM 2492 O  O    . HOH   N 4 .  ? 11.876  -20.946 10.794  1.00 31.76 ? 253 HOH   C O    1 
HETATM 2493 O  O    . HOH   N 4 .  ? 13.760  -39.273 11.128  1.00 46.70 ? 254 HOH   C O    1 
HETATM 2494 O  O    . HOH   N 4 .  ? 28.465  -41.424 29.508  1.00 37.09 ? 255 HOH   C O    1 
HETATM 2495 O  O    . HOH   N 4 .  ? 3.824   -24.799 16.926  1.00 52.92 ? 256 HOH   C O    1 
HETATM 2496 O  O    . HOH   N 4 .  ? 33.310  -44.136 15.049  1.00 42.56 ? 257 HOH   C O    1 
# 
