data_9GRS
# 
_entry.id   9GRS 
# 
_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   9GRS         pdb_00009grs 10.2210/pdb9grs/pdb 
WWPDB D_1292141067 ?            ?                   
# 
_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                        9GRS 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-12 
_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 
'Paulovcakova, T.' 2 0000-0002-4512-6163 
'Beelen, S.'       3 0009-0004-9687-0891 
'Vantieghem, T.'   4 0000-0002-1452-9584 
'Strelkov, S.V.'   5 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 'DIMETHYL SULFOXIDE'                               78.133    2   ? ? ? ? 
3 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ? ? ? 
4 non-polymer syn 1-bromanyl-4-methylsulfonyl-benzene                235.098   1   ? ? ? ? 
5 water       nat water                                              18.015    192 ? ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                DMS   
3 'SULFATE ION'                       SO4   
4 1-bromanyl-4-methylsulfonyl-benzene A1H6Y 
5 water                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 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 
A1H6Y non-polymer         . 1-bromanyl-4-methylsulfonyl-benzene ? 'C7 H7 Br O2 S'  235.098 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                ? 'C2 H6 O S'      78.133  
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 ?  ?   ?   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        A1H6Y 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6Y 
_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 DMS   1  101 101 DMS   DMS A . 
E 3 SO4   1  102 1   SO4   SO4 A . 
F 3 SO4   1  103 2   SO4   SO4 A . 
G 4 A1H6Y 1  101 101 A1H6Y C8  B . 
H 3 SO4   1  102 3   SO4   SO4 B . 
I 3 SO4   1  103 4   SO4   SO4 B . 
J 3 SO4   1  104 6   SO4   SO4 B . 
K 2 DMS   1  601 601 DMS   DMS C . 
L 3 SO4   1  602 5   SO4   SO4 C . 
M 5 HOH   1  201 73  HOH   HOH A . 
M 5 HOH   2  202 273 HOH   HOH A . 
M 5 HOH   3  203 89  HOH   HOH A . 
M 5 HOH   4  204 132 HOH   HOH A . 
M 5 HOH   5  205 8   HOH   HOH A . 
M 5 HOH   6  206 277 HOH   HOH A . 
M 5 HOH   7  207 99  HOH   HOH A . 
M 5 HOH   8  208 28  HOH   HOH A . 
M 5 HOH   9  209 27  HOH   HOH A . 
M 5 HOH   10 210 109 HOH   HOH A . 
M 5 HOH   11 211 90  HOH   HOH A . 
M 5 HOH   12 212 40  HOH   HOH A . 
M 5 HOH   13 213 103 HOH   HOH A . 
M 5 HOH   14 214 275 HOH   HOH A . 
M 5 HOH   15 215 91  HOH   HOH A . 
M 5 HOH   16 216 33  HOH   HOH A . 
M 5 HOH   17 217 101 HOH   HOH A . 
M 5 HOH   18 218 56  HOH   HOH A . 
M 5 HOH   19 219 7   HOH   HOH A . 
M 5 HOH   20 220 34  HOH   HOH A . 
M 5 HOH   21 221 22  HOH   HOH A . 
M 5 HOH   22 222 42  HOH   HOH A . 
M 5 HOH   23 223 2   HOH   HOH A . 
M 5 HOH   24 224 23  HOH   HOH A . 
M 5 HOH   25 225 148 HOH   HOH A . 
M 5 HOH   26 226 61  HOH   HOH A . 
M 5 HOH   27 227 84  HOH   HOH A . 
M 5 HOH   28 228 236 HOH   HOH A . 
M 5 HOH   29 229 176 HOH   HOH A . 
M 5 HOH   30 230 12  HOH   HOH A . 
M 5 HOH   31 231 20  HOH   HOH A . 
M 5 HOH   32 232 37  HOH   HOH A . 
M 5 HOH   33 233 1   HOH   HOH A . 
M 5 HOH   34 234 38  HOH   HOH A . 
M 5 HOH   35 235 29  HOH   HOH A . 
M 5 HOH   36 236 218 HOH   HOH A . 
M 5 HOH   37 237 3   HOH   HOH A . 
M 5 HOH   38 238 245 HOH   HOH A . 
M 5 HOH   39 239 95  HOH   HOH A . 
M 5 HOH   40 240 178 HOH   HOH A . 
M 5 HOH   41 241 83  HOH   HOH A . 
M 5 HOH   42 242 80  HOH   HOH A . 
M 5 HOH   43 243 59  HOH   HOH A . 
M 5 HOH   44 244 113 HOH   HOH A . 
M 5 HOH   45 245 214 HOH   HOH A . 
M 5 HOH   46 246 241 HOH   HOH A . 
M 5 HOH   47 247 11  HOH   HOH A . 
M 5 HOH   48 248 110 HOH   HOH A . 
M 5 HOH   49 249 30  HOH   HOH A . 
M 5 HOH   50 250 181 HOH   HOH A . 
M 5 HOH   51 251 21  HOH   HOH A . 
M 5 HOH   52 252 32  HOH   HOH A . 
M 5 HOH   53 253 14  HOH   HOH A . 
M 5 HOH   54 254 150 HOH   HOH A . 
M 5 HOH   55 255 152 HOH   HOH A . 
M 5 HOH   56 256 16  HOH   HOH A . 
M 5 HOH   57 257 179 HOH   HOH A . 
M 5 HOH   58 258 47  HOH   HOH A . 
M 5 HOH   59 259 18  HOH   HOH A . 
M 5 HOH   60 260 269 HOH   HOH A . 
M 5 HOH   61 261 81  HOH   HOH A . 
M 5 HOH   62 262 9   HOH   HOH A . 
M 5 HOH   63 263 19  HOH   HOH A . 
M 5 HOH   64 264 118 HOH   HOH A . 
M 5 HOH   65 265 263 HOH   HOH A . 
M 5 HOH   66 266 231 HOH   HOH A . 
M 5 HOH   67 267 270 HOH   HOH A . 
M 5 HOH   68 268 65  HOH   HOH A . 
M 5 HOH   69 269 136 HOH   HOH A . 
M 5 HOH   70 270 155 HOH   HOH A . 
M 5 HOH   71 271 75  HOH   HOH A . 
M 5 HOH   72 272 31  HOH   HOH A . 
M 5 HOH   73 273 200 HOH   HOH A . 
M 5 HOH   74 274 86  HOH   HOH A . 
M 5 HOH   75 275 52  HOH   HOH A . 
M 5 HOH   76 276 204 HOH   HOH A . 
M 5 HOH   77 277 264 HOH   HOH A . 
M 5 HOH   78 278 112 HOH   HOH A . 
M 5 HOH   79 279 149 HOH   HOH A . 
M 5 HOH   80 280 58  HOH   HOH A . 
M 5 HOH   81 281 243 HOH   HOH A . 
M 5 HOH   82 282 168 HOH   HOH A . 
M 5 HOH   83 283 147 HOH   HOH A . 
M 5 HOH   84 284 35  HOH   HOH A . 
M 5 HOH   85 285 244 HOH   HOH A . 
M 5 HOH   86 286 163 HOH   HOH A . 
N 5 HOH   1  201 262 HOH   HOH B . 
N 5 HOH   2  202 46  HOH   HOH B . 
N 5 HOH   3  203 232 HOH   HOH B . 
N 5 HOH   4  204 219 HOH   HOH B . 
N 5 HOH   5  205 226 HOH   HOH B . 
N 5 HOH   6  206 165 HOH   HOH B . 
N 5 HOH   7  207 71  HOH   HOH B . 
N 5 HOH   8  208 17  HOH   HOH B . 
N 5 HOH   9  209 222 HOH   HOH B . 
N 5 HOH   10 210 280 HOH   HOH B . 
N 5 HOH   11 211 260 HOH   HOH B . 
N 5 HOH   12 212 93  HOH   HOH B . 
N 5 HOH   13 213 6   HOH   HOH B . 
N 5 HOH   14 214 189 HOH   HOH B . 
N 5 HOH   15 215 185 HOH   HOH B . 
N 5 HOH   16 216 197 HOH   HOH B . 
N 5 HOH   17 217 172 HOH   HOH B . 
N 5 HOH   18 218 72  HOH   HOH B . 
N 5 HOH   19 219 76  HOH   HOH B . 
N 5 HOH   20 220 10  HOH   HOH B . 
N 5 HOH   21 221 102 HOH   HOH B . 
N 5 HOH   22 222 224 HOH   HOH B . 
N 5 HOH   23 223 100 HOH   HOH B . 
N 5 HOH   24 224 116 HOH   HOH B . 
N 5 HOH   25 225 138 HOH   HOH B . 
N 5 HOH   26 226 128 HOH   HOH B . 
N 5 HOH   27 227 24  HOH   HOH B . 
N 5 HOH   28 228 195 HOH   HOH B . 
N 5 HOH   29 229 133 HOH   HOH B . 
N 5 HOH   30 230 162 HOH   HOH B . 
N 5 HOH   31 231 69  HOH   HOH B . 
N 5 HOH   32 232 279 HOH   HOH B . 
N 5 HOH   33 233 74  HOH   HOH B . 
N 5 HOH   34 234 60  HOH   HOH B . 
N 5 HOH   35 235 25  HOH   HOH B . 
N 5 HOH   36 236 36  HOH   HOH B . 
N 5 HOH   37 237 5   HOH   HOH B . 
N 5 HOH   38 238 62  HOH   HOH B . 
N 5 HOH   39 239 55  HOH   HOH B . 
N 5 HOH   40 240 105 HOH   HOH B . 
N 5 HOH   41 241 278 HOH   HOH B . 
N 5 HOH   42 242 122 HOH   HOH B . 
N 5 HOH   43 243 125 HOH   HOH B . 
N 5 HOH   44 244 13  HOH   HOH B . 
N 5 HOH   45 245 146 HOH   HOH B . 
N 5 HOH   46 246 271 HOH   HOH B . 
N 5 HOH   47 247 141 HOH   HOH B . 
N 5 HOH   48 248 124 HOH   HOH B . 
N 5 HOH   49 249 213 HOH   HOH B . 
N 5 HOH   50 250 78  HOH   HOH B . 
N 5 HOH   51 251 108 HOH   HOH B . 
N 5 HOH   52 252 53  HOH   HOH B . 
N 5 HOH   53 253 44  HOH   HOH B . 
N 5 HOH   54 254 154 HOH   HOH B . 
N 5 HOH   55 255 183 HOH   HOH B . 
N 5 HOH   56 256 134 HOH   HOH B . 
N 5 HOH   57 257 174 HOH   HOH B . 
N 5 HOH   58 258 274 HOH   HOH B . 
N 5 HOH   59 259 82  HOH   HOH B . 
N 5 HOH   60 260 96  HOH   HOH B . 
N 5 HOH   61 261 272 HOH   HOH B . 
N 5 HOH   62 262 201 HOH   HOH B . 
N 5 HOH   63 263 111 HOH   HOH B . 
N 5 HOH   64 264 257 HOH   HOH B . 
O 5 HOH   1  701 106 HOH   HOH C . 
O 5 HOH   2  702 216 HOH   HOH C . 
O 5 HOH   3  703 51  HOH   HOH C . 
O 5 HOH   4  704 92  HOH   HOH C . 
O 5 HOH   5  705 159 HOH   HOH C . 
O 5 HOH   6  706 127 HOH   HOH C . 
O 5 HOH   7  707 15  HOH   HOH C . 
O 5 HOH   8  708 209 HOH   HOH C . 
O 5 HOH   9  709 126 HOH   HOH C . 
O 5 HOH   10 710 94  HOH   HOH C . 
O 5 HOH   11 711 151 HOH   HOH C . 
O 5 HOH   12 712 225 HOH   HOH C . 
O 5 HOH   13 713 142 HOH   HOH C . 
O 5 HOH   14 714 135 HOH   HOH C . 
O 5 HOH   15 715 167 HOH   HOH C . 
O 5 HOH   16 716 140 HOH   HOH C . 
O 5 HOH   17 717 48  HOH   HOH C . 
O 5 HOH   18 718 26  HOH   HOH C . 
O 5 HOH   19 719 4   HOH   HOH C . 
O 5 HOH   20 720 104 HOH   HOH C . 
O 5 HOH   21 721 117 HOH   HOH C . 
O 5 HOH   22 722 45  HOH   HOH C . 
O 5 HOH   23 723 39  HOH   HOH C . 
O 5 HOH   24 724 49  HOH   HOH C . 
O 5 HOH   25 725 130 HOH   HOH C . 
O 5 HOH   26 726 43  HOH   HOH C . 
O 5 HOH   27 727 54  HOH   HOH C . 
O 5 HOH   28 728 276 HOH   HOH C . 
O 5 HOH   29 729 63  HOH   HOH C . 
O 5 HOH   30 730 187 HOH   HOH C . 
O 5 HOH   31 731 123 HOH   HOH C . 
O 5 HOH   32 732 186 HOH   HOH C . 
O 5 HOH   33 733 57  HOH   HOH C . 
O 5 HOH   34 734 68  HOH   HOH C . 
O 5 HOH   35 735 268 HOH   HOH C . 
O 5 HOH   36 736 242 HOH   HOH C . 
O 5 HOH   37 737 173 HOH   HOH C . 
O 5 HOH   38 738 139 HOH   HOH C . 
O 5 HOH   39 739 205 HOH   HOH C . 
O 5 HOH   40 740 107 HOH   HOH C . 
O 5 HOH   41 741 193 HOH   HOH C . 
O 5 HOH   42 742 248 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 GLN 85 ? CG  ? B GLN 86 CG  
9  1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
10 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
11 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
12 1 Y 1 C ASP 66 ? CG  ? C ASP 67 CG  
13 1 Y 1 C ASP 66 ? OD1 ? C ASP 67 OD1 
14 1 Y 1 C ASP 66 ? OD2 ? C ASP 67 OD2 
15 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
16 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
17 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
18 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21.1_5286: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GRS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.688 
_cell.length_a_esd                 ? 
_cell.length_b                     41.940 
_cell.length_b_esd                 ? 
_cell.length_c                     157.744 
_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                         9GRS 
_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                   9GRS 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.66 
_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         2019-12-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.91165 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91165 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GRS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               78.87 
_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                                     34050 
_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                                13.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.77 
_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                                0.075 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       456937 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.072 
_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                                    1.66 
_reflns_shell.d_res_low                                     1.74 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           67899 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4910 
_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                               13.8 
_reflns_shell.pdbx_chi_squared                              0.54 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.2 
_reflns_shell.pdbx_Rrim_I_all                               2.216 
_reflns_shell.pdbx_Rpim_I_all                               0.593 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.632 
_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                                  2.134 
_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                                 9GRS 
_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                            1.66 
_refine.ls_d_res_low                             78.87 
_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                     33973 
_refine.ls_number_reflns_R_free                  1698 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2228 
_refine.ls_R_factor_R_free                       0.2572 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2211 
_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                          1.35 
_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                 26.56 
_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                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2222 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             192 
_refine_hist.number_atoms_total               2463 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        78.87 
# 
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  ? 2358 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.608  ? 3201 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.762 ? 864  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 287  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 420  ? 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' 1.66 1.70  . . 133 2650 100.00 . . . . 0.4198 . . . . . . . . . . . 0.4485 
'X-RAY DIFFRACTION' 1.70 1.76  . . 166 2629 100.00 . . . . 0.3519 . . . . . . . . . . . 0.3821 
'X-RAY DIFFRACTION' 1.76 1.82  . . 144 2639 100.00 . . . . 0.2940 . . . . . . . . . . . 0.3570 
'X-RAY DIFFRACTION' 1.82 1.89  . . 137 2652 100.00 . . . . 0.2520 . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 1.89 1.98  . . 139 2654 100.00 . . . . 0.2438 . . . . . . . . . . . 0.2750 
'X-RAY DIFFRACTION' 1.98 2.09  . . 136 2663 100.00 . . . . 0.2456 . . . . . . . . . . . 0.2708 
'X-RAY DIFFRACTION' 2.09 2.22  . . 161 2647 100.00 . . . . 0.2369 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 2.22 2.39  . . 137 2658 100.00 . . . . 0.2220 . . . . . . . . . . . 0.2814 
'X-RAY DIFFRACTION' 2.39 2.63  . . 139 2709 100.00 . . . . 0.2290 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 2.63 3.01  . . 108 2748 100.00 . . . . 0.2274 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 3.01 3.79  . . 148 2740 100.00 . . . . 0.2077 . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 3.79 78.87 . . 150 2886 100.00 . . . . 0.1969 . . . . . . . . . . . 0.2476 
# 
_struct.entry_id                     9GRS 
_struct.title                        'Crystal structure of HRP-2 PWWP domain in complex with compound 8' 
_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        9GRS 
_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 4 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GRS A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 9GRS B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 9GRS 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 9GRS GLY A 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 1 
2 9GRS GLY B 1 ? UNP Q7Z4V5 ? ? 'expression tag' 0 2 
3 9GRS 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,M   
2 1 B,G,H,I,J,N 
3 1 C,K,L,O     
# 
_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 TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
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                   9GRS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 B ASN 38 ? ? O B HOH 201 ? ? 2.11 
2 1 OD2 B ASP 62 ? ? O B HOH 202 ? ? 2.11 
3 1 NZ  B LYS 34 ? ? O B HOH 203 ? ? 2.13 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ASN 
_pdbx_validate_symm_contact.auth_seq_id_1     72 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     203 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.18 
# 
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 ? ? -152.78 65.01 
2 1 ASN B 87 ? ? -155.49 67.79 
3 1 ASN C 87 ? ? -154.51 67.23 
# 
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 A SER 93 ? A SER 94 
3 1 Y 1 B GLY 0  ? B GLY 1  
4 1 Y 1 C GLY 0  ? C GLY 1  
5 1 Y 1 C MET 1  ? C MET 2  
6 1 Y 1 C PRO 2  ? C PRO 3  
7 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 
A1H6Y C4   C  Y N 1   
A1H6Y C5   C  Y N 2   
A1H6Y C6   C  Y N 3   
A1H6Y C7   C  Y N 4   
A1H6Y C3   C  Y N 5   
A1H6Y C1   C  N N 6   
A1H6Y S1   S  N N 7   
A1H6Y O1   O  N N 8   
A1H6Y O2   O  N N 9   
A1H6Y C2   C  Y N 10  
A1H6Y BR1  BR N N 11  
A1H6Y H1   H  N N 12  
A1H6Y H2   H  N N 13  
A1H6Y H3   H  N N 14  
A1H6Y H4   H  N N 15  
A1H6Y H5   H  N N 16  
A1H6Y H6   H  N N 17  
A1H6Y H7   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 
DMS   S    S  N N 106 
DMS   O    O  N N 107 
DMS   C1   C  N N 108 
DMS   C2   C  N N 109 
DMS   H11  H  N N 110 
DMS   H12  H  N N 111 
DMS   H13  H  N N 112 
DMS   H21  H  N N 113 
DMS   H22  H  N N 114 
DMS   H23  H  N N 115 
GLN   N    N  N N 116 
GLN   CA   C  N S 117 
GLN   C    C  N N 118 
GLN   O    O  N N 119 
GLN   CB   C  N N 120 
GLN   CG   C  N N 121 
GLN   CD   C  N N 122 
GLN   OE1  O  N N 123 
GLN   NE2  N  N N 124 
GLN   OXT  O  N N 125 
GLN   H    H  N N 126 
GLN   H2   H  N N 127 
GLN   HA   H  N N 128 
GLN   HB2  H  N N 129 
GLN   HB3  H  N N 130 
GLN   HG2  H  N N 131 
GLN   HG3  H  N N 132 
GLN   HE21 H  N N 133 
GLN   HE22 H  N N 134 
GLN   HXT  H  N N 135 
GLU   N    N  N N 136 
GLU   CA   C  N S 137 
GLU   C    C  N N 138 
GLU   O    O  N N 139 
GLU   CB   C  N N 140 
GLU   CG   C  N N 141 
GLU   CD   C  N N 142 
GLU   OE1  O  N N 143 
GLU   OE2  O  N N 144 
GLU   OXT  O  N N 145 
GLU   H    H  N N 146 
GLU   H2   H  N N 147 
GLU   HA   H  N N 148 
GLU   HB2  H  N N 149 
GLU   HB3  H  N N 150 
GLU   HG2  H  N N 151 
GLU   HG3  H  N N 152 
GLU   HE2  H  N N 153 
GLU   HXT  H  N N 154 
GLY   N    N  N N 155 
GLY   CA   C  N N 156 
GLY   C    C  N N 157 
GLY   O    O  N N 158 
GLY   OXT  O  N N 159 
GLY   H    H  N N 160 
GLY   H2   H  N N 161 
GLY   HA2  H  N N 162 
GLY   HA3  H  N N 163 
GLY   HXT  H  N N 164 
HIS   N    N  N N 165 
HIS   CA   C  N S 166 
HIS   C    C  N N 167 
HIS   O    O  N N 168 
HIS   CB   C  N N 169 
HIS   CG   C  Y N 170 
HIS   ND1  N  Y N 171 
HIS   CD2  C  Y N 172 
HIS   CE1  C  Y N 173 
HIS   NE2  N  Y N 174 
HIS   OXT  O  N N 175 
HIS   H    H  N N 176 
HIS   H2   H  N N 177 
HIS   HA   H  N N 178 
HIS   HB2  H  N N 179 
HIS   HB3  H  N N 180 
HIS   HD1  H  N N 181 
HIS   HD2  H  N N 182 
HIS   HE1  H  N N 183 
HIS   HE2  H  N N 184 
HIS   HXT  H  N N 185 
HOH   O    O  N N 186 
HOH   H1   H  N N 187 
HOH   H2   H  N N 188 
ILE   N    N  N N 189 
ILE   CA   C  N S 190 
ILE   C    C  N N 191 
ILE   O    O  N N 192 
ILE   CB   C  N S 193 
ILE   CG1  C  N N 194 
ILE   CG2  C  N N 195 
ILE   CD1  C  N N 196 
ILE   OXT  O  N N 197 
ILE   H    H  N N 198 
ILE   H2   H  N N 199 
ILE   HA   H  N N 200 
ILE   HB   H  N N 201 
ILE   HG12 H  N N 202 
ILE   HG13 H  N N 203 
ILE   HG21 H  N N 204 
ILE   HG22 H  N N 205 
ILE   HG23 H  N N 206 
ILE   HD11 H  N N 207 
ILE   HD12 H  N N 208 
ILE   HD13 H  N N 209 
ILE   HXT  H  N N 210 
LEU   N    N  N N 211 
LEU   CA   C  N S 212 
LEU   C    C  N N 213 
LEU   O    O  N N 214 
LEU   CB   C  N N 215 
LEU   CG   C  N N 216 
LEU   CD1  C  N N 217 
LEU   CD2  C  N N 218 
LEU   OXT  O  N N 219 
LEU   H    H  N N 220 
LEU   H2   H  N N 221 
LEU   HA   H  N N 222 
LEU   HB2  H  N N 223 
LEU   HB3  H  N N 224 
LEU   HG   H  N N 225 
LEU   HD11 H  N N 226 
LEU   HD12 H  N N 227 
LEU   HD13 H  N N 228 
LEU   HD21 H  N N 229 
LEU   HD22 H  N N 230 
LEU   HD23 H  N N 231 
LEU   HXT  H  N N 232 
LYS   N    N  N N 233 
LYS   CA   C  N S 234 
LYS   C    C  N N 235 
LYS   O    O  N N 236 
LYS   CB   C  N N 237 
LYS   CG   C  N N 238 
LYS   CD   C  N N 239 
LYS   CE   C  N N 240 
LYS   NZ   N  N N 241 
LYS   OXT  O  N N 242 
LYS   H    H  N N 243 
LYS   H2   H  N N 244 
LYS   HA   H  N N 245 
LYS   HB2  H  N N 246 
LYS   HB3  H  N N 247 
LYS   HG2  H  N N 248 
LYS   HG3  H  N N 249 
LYS   HD2  H  N N 250 
LYS   HD3  H  N N 251 
LYS   HE2  H  N N 252 
LYS   HE3  H  N N 253 
LYS   HZ1  H  N N 254 
LYS   HZ2  H  N N 255 
LYS   HZ3  H  N N 256 
LYS   HXT  H  N N 257 
MET   N    N  N N 258 
MET   CA   C  N S 259 
MET   C    C  N N 260 
MET   O    O  N N 261 
MET   CB   C  N N 262 
MET   CG   C  N N 263 
MET   SD   S  N N 264 
MET   CE   C  N N 265 
MET   OXT  O  N N 266 
MET   H    H  N N 267 
MET   H2   H  N N 268 
MET   HA   H  N N 269 
MET   HB2  H  N N 270 
MET   HB3  H  N N 271 
MET   HG2  H  N N 272 
MET   HG3  H  N N 273 
MET   HE1  H  N N 274 
MET   HE2  H  N N 275 
MET   HE3  H  N N 276 
MET   HXT  H  N N 277 
PHE   N    N  N N 278 
PHE   CA   C  N S 279 
PHE   C    C  N N 280 
PHE   O    O  N N 281 
PHE   CB   C  N N 282 
PHE   CG   C  Y N 283 
PHE   CD1  C  Y N 284 
PHE   CD2  C  Y N 285 
PHE   CE1  C  Y N 286 
PHE   CE2  C  Y N 287 
PHE   CZ   C  Y N 288 
PHE   OXT  O  N N 289 
PHE   H    H  N N 290 
PHE   H2   H  N N 291 
PHE   HA   H  N N 292 
PHE   HB2  H  N N 293 
PHE   HB3  H  N N 294 
PHE   HD1  H  N N 295 
PHE   HD2  H  N N 296 
PHE   HE1  H  N N 297 
PHE   HE2  H  N N 298 
PHE   HZ   H  N N 299 
PHE   HXT  H  N N 300 
PRO   N    N  N N 301 
PRO   CA   C  N S 302 
PRO   C    C  N N 303 
PRO   O    O  N N 304 
PRO   CB   C  N N 305 
PRO   CG   C  N N 306 
PRO   CD   C  N N 307 
PRO   OXT  O  N N 308 
PRO   H    H  N N 309 
PRO   HA   H  N N 310 
PRO   HB2  H  N N 311 
PRO   HB3  H  N N 312 
PRO   HG2  H  N N 313 
PRO   HG3  H  N N 314 
PRO   HD2  H  N N 315 
PRO   HD3  H  N N 316 
PRO   HXT  H  N N 317 
SER   N    N  N N 318 
SER   CA   C  N S 319 
SER   C    C  N N 320 
SER   O    O  N N 321 
SER   CB   C  N N 322 
SER   OG   O  N N 323 
SER   OXT  O  N N 324 
SER   H    H  N N 325 
SER   H2   H  N N 326 
SER   HA   H  N N 327 
SER   HB2  H  N N 328 
SER   HB3  H  N N 329 
SER   HG   H  N N 330 
SER   HXT  H  N N 331 
SO4   S    S  N N 332 
SO4   O1   O  N N 333 
SO4   O2   O  N N 334 
SO4   O3   O  N N 335 
SO4   O4   O  N N 336 
THR   N    N  N N 337 
THR   CA   C  N S 338 
THR   C    C  N N 339 
THR   O    O  N N 340 
THR   CB   C  N R 341 
THR   OG1  O  N N 342 
THR   CG2  C  N N 343 
THR   OXT  O  N N 344 
THR   H    H  N N 345 
THR   H2   H  N N 346 
THR   HA   H  N N 347 
THR   HB   H  N N 348 
THR   HG1  H  N N 349 
THR   HG21 H  N N 350 
THR   HG22 H  N N 351 
THR   HG23 H  N N 352 
THR   HXT  H  N N 353 
TRP   N    N  N N 354 
TRP   CA   C  N S 355 
TRP   C    C  N N 356 
TRP   O    O  N N 357 
TRP   CB   C  N N 358 
TRP   CG   C  Y N 359 
TRP   CD1  C  Y N 360 
TRP   CD2  C  Y N 361 
TRP   NE1  N  Y N 362 
TRP   CE2  C  Y N 363 
TRP   CE3  C  Y N 364 
TRP   CZ2  C  Y N 365 
TRP   CZ3  C  Y N 366 
TRP   CH2  C  Y N 367 
TRP   OXT  O  N N 368 
TRP   H    H  N N 369 
TRP   H2   H  N N 370 
TRP   HA   H  N N 371 
TRP   HB2  H  N N 372 
TRP   HB3  H  N N 373 
TRP   HD1  H  N N 374 
TRP   HE1  H  N N 375 
TRP   HE3  H  N N 376 
TRP   HZ2  H  N N 377 
TRP   HZ3  H  N N 378 
TRP   HH2  H  N N 379 
TRP   HXT  H  N N 380 
TYR   N    N  N N 381 
TYR   CA   C  N S 382 
TYR   C    C  N N 383 
TYR   O    O  N N 384 
TYR   CB   C  N N 385 
TYR   CG   C  Y N 386 
TYR   CD1  C  Y N 387 
TYR   CD2  C  Y N 388 
TYR   CE1  C  Y N 389 
TYR   CE2  C  Y N 390 
TYR   CZ   C  Y N 391 
TYR   OH   O  N N 392 
TYR   OXT  O  N N 393 
TYR   H    H  N N 394 
TYR   H2   H  N N 395 
TYR   HA   H  N N 396 
TYR   HB2  H  N N 397 
TYR   HB3  H  N N 398 
TYR   HD1  H  N N 399 
TYR   HD2  H  N N 400 
TYR   HE1  H  N N 401 
TYR   HE2  H  N N 402 
TYR   HH   H  N N 403 
TYR   HXT  H  N N 404 
VAL   N    N  N N 405 
VAL   CA   C  N S 406 
VAL   C    C  N N 407 
VAL   O    O  N N 408 
VAL   CB   C  N N 409 
VAL   CG1  C  N N 410 
VAL   CG2  C  N N 411 
VAL   OXT  O  N N 412 
VAL   H    H  N N 413 
VAL   H2   H  N N 414 
VAL   HA   H  N N 415 
VAL   HB   H  N N 416 
VAL   HG11 H  N N 417 
VAL   HG12 H  N N 418 
VAL   HG13 H  N N 419 
VAL   HG21 H  N N 420 
VAL   HG22 H  N N 421 
VAL   HG23 H  N N 422 
VAL   HXT  H  N N 423 
# 
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 
A1H6Y O2  S1   doub N N 1   
A1H6Y O1  S1   doub N N 2   
A1H6Y S1  C1   sing N N 3   
A1H6Y S1  C2   sing N N 4   
A1H6Y C2  C3   doub Y N 5   
A1H6Y C2  C7   sing Y N 6   
A1H6Y C3  C4   sing Y N 7   
A1H6Y C7  C6   doub Y N 8   
A1H6Y C4  C5   doub Y N 9   
A1H6Y C6  C5   sing Y N 10  
A1H6Y C5  BR1  sing N N 11  
A1H6Y C4  H1   sing N N 12  
A1H6Y C6  H2   sing N N 13  
A1H6Y C7  H3   sing N N 14  
A1H6Y C3  H4   sing N N 15  
A1H6Y C1  H5   sing N N 16  
A1H6Y C1  H6   sing N N 17  
A1H6Y C1  H7   sing N N 18  
ALA   N   CA   sing N N 19  
ALA   N   H    sing N N 20  
ALA   N   H2   sing N N 21  
ALA   CA  C    sing N N 22  
ALA   CA  CB   sing N N 23  
ALA   CA  HA   sing N N 24  
ALA   C   O    doub N N 25  
ALA   C   OXT  sing N N 26  
ALA   CB  HB1  sing N N 27  
ALA   CB  HB2  sing N N 28  
ALA   CB  HB3  sing N N 29  
ALA   OXT HXT  sing N N 30  
ARG   N   CA   sing N N 31  
ARG   N   H    sing N N 32  
ARG   N   H2   sing N N 33  
ARG   CA  C    sing N N 34  
ARG   CA  CB   sing N N 35  
ARG   CA  HA   sing N N 36  
ARG   C   O    doub N N 37  
ARG   C   OXT  sing N N 38  
ARG   CB  CG   sing N N 39  
ARG   CB  HB2  sing N N 40  
ARG   CB  HB3  sing N N 41  
ARG   CG  CD   sing N N 42  
ARG   CG  HG2  sing N N 43  
ARG   CG  HG3  sing N N 44  
ARG   CD  NE   sing N N 45  
ARG   CD  HD2  sing N N 46  
ARG   CD  HD3  sing N N 47  
ARG   NE  CZ   sing N N 48  
ARG   NE  HE   sing N N 49  
ARG   CZ  NH1  sing N N 50  
ARG   CZ  NH2  doub N N 51  
ARG   NH1 HH11 sing N N 52  
ARG   NH1 HH12 sing N N 53  
ARG   NH2 HH21 sing N N 54  
ARG   NH2 HH22 sing N N 55  
ARG   OXT HXT  sing N N 56  
ASN   N   CA   sing N N 57  
ASN   N   H    sing N N 58  
ASN   N   H2   sing N N 59  
ASN   CA  C    sing N N 60  
ASN   CA  CB   sing N N 61  
ASN   CA  HA   sing N N 62  
ASN   C   O    doub N N 63  
ASN   C   OXT  sing N N 64  
ASN   CB  CG   sing N N 65  
ASN   CB  HB2  sing N N 66  
ASN   CB  HB3  sing N N 67  
ASN   CG  OD1  doub N N 68  
ASN   CG  ND2  sing N N 69  
ASN   ND2 HD21 sing N N 70  
ASN   ND2 HD22 sing N N 71  
ASN   OXT HXT  sing N N 72  
ASP   N   CA   sing N N 73  
ASP   N   H    sing N N 74  
ASP   N   H2   sing N N 75  
ASP   CA  C    sing N N 76  
ASP   CA  CB   sing N N 77  
ASP   CA  HA   sing N N 78  
ASP   C   O    doub N N 79  
ASP   C   OXT  sing N N 80  
ASP   CB  CG   sing N N 81  
ASP   CB  HB2  sing N N 82  
ASP   CB  HB3  sing N N 83  
ASP   CG  OD1  doub N N 84  
ASP   CG  OD2  sing N N 85  
ASP   OD2 HD2  sing N N 86  
ASP   OXT HXT  sing N N 87  
CYS   N   CA   sing N N 88  
CYS   N   H    sing N N 89  
CYS   N   H2   sing N N 90  
CYS   CA  C    sing N N 91  
CYS   CA  CB   sing N N 92  
CYS   CA  HA   sing N N 93  
CYS   C   O    doub N N 94  
CYS   C   OXT  sing N N 95  
CYS   CB  SG   sing N N 96  
CYS   CB  HB2  sing N N 97  
CYS   CB  HB3  sing N N 98  
CYS   SG  HG   sing N N 99  
CYS   OXT HXT  sing N N 100 
DMS   S   O    doub N N 101 
DMS   S   C1   sing N N 102 
DMS   S   C2   sing N N 103 
DMS   C1  H11  sing N N 104 
DMS   C1  H12  sing N N 105 
DMS   C1  H13  sing N N 106 
DMS   C2  H21  sing N N 107 
DMS   C2  H22  sing N N 108 
DMS   C2  H23  sing N N 109 
GLN   N   CA   sing N N 110 
GLN   N   H    sing N N 111 
GLN   N   H2   sing N N 112 
GLN   CA  C    sing N N 113 
GLN   CA  CB   sing N N 114 
GLN   CA  HA   sing N N 115 
GLN   C   O    doub N N 116 
GLN   C   OXT  sing N N 117 
GLN   CB  CG   sing N N 118 
GLN   CB  HB2  sing N N 119 
GLN   CB  HB3  sing N N 120 
GLN   CG  CD   sing N N 121 
GLN   CG  HG2  sing N N 122 
GLN   CG  HG3  sing N N 123 
GLN   CD  OE1  doub N N 124 
GLN   CD  NE2  sing N N 125 
GLN   NE2 HE21 sing N N 126 
GLN   NE2 HE22 sing N N 127 
GLN   OXT HXT  sing N N 128 
GLU   N   CA   sing N N 129 
GLU   N   H    sing N N 130 
GLU   N   H2   sing N N 131 
GLU   CA  C    sing N N 132 
GLU   CA  CB   sing N N 133 
GLU   CA  HA   sing N N 134 
GLU   C   O    doub N N 135 
GLU   C   OXT  sing N N 136 
GLU   CB  CG   sing N N 137 
GLU   CB  HB2  sing N N 138 
GLU   CB  HB3  sing N N 139 
GLU   CG  CD   sing N N 140 
GLU   CG  HG2  sing N N 141 
GLU   CG  HG3  sing N N 142 
GLU   CD  OE1  doub N N 143 
GLU   CD  OE2  sing N N 144 
GLU   OE2 HE2  sing N N 145 
GLU   OXT HXT  sing N N 146 
GLY   N   CA   sing N N 147 
GLY   N   H    sing N N 148 
GLY   N   H2   sing N N 149 
GLY   CA  C    sing N N 150 
GLY   CA  HA2  sing N N 151 
GLY   CA  HA3  sing N N 152 
GLY   C   O    doub N N 153 
GLY   C   OXT  sing N N 154 
GLY   OXT HXT  sing N N 155 
HIS   N   CA   sing N N 156 
HIS   N   H    sing N N 157 
HIS   N   H2   sing N N 158 
HIS   CA  C    sing N N 159 
HIS   CA  CB   sing N N 160 
HIS   CA  HA   sing N N 161 
HIS   C   O    doub N N 162 
HIS   C   OXT  sing N N 163 
HIS   CB  CG   sing N N 164 
HIS   CB  HB2  sing N N 165 
HIS   CB  HB3  sing N N 166 
HIS   CG  ND1  sing Y N 167 
HIS   CG  CD2  doub Y N 168 
HIS   ND1 CE1  doub Y N 169 
HIS   ND1 HD1  sing N N 170 
HIS   CD2 NE2  sing Y N 171 
HIS   CD2 HD2  sing N N 172 
HIS   CE1 NE2  sing Y N 173 
HIS   CE1 HE1  sing N N 174 
HIS   NE2 HE2  sing N N 175 
HIS   OXT HXT  sing N N 176 
HOH   O   H1   sing N N 177 
HOH   O   H2   sing N N 178 
ILE   N   CA   sing N N 179 
ILE   N   H    sing N N 180 
ILE   N   H2   sing N N 181 
ILE   CA  C    sing N N 182 
ILE   CA  CB   sing N N 183 
ILE   CA  HA   sing N N 184 
ILE   C   O    doub N N 185 
ILE   C   OXT  sing N N 186 
ILE   CB  CG1  sing N N 187 
ILE   CB  CG2  sing N N 188 
ILE   CB  HB   sing N N 189 
ILE   CG1 CD1  sing N N 190 
ILE   CG1 HG12 sing N N 191 
ILE   CG1 HG13 sing N N 192 
ILE   CG2 HG21 sing N N 193 
ILE   CG2 HG22 sing N N 194 
ILE   CG2 HG23 sing N N 195 
ILE   CD1 HD11 sing N N 196 
ILE   CD1 HD12 sing N N 197 
ILE   CD1 HD13 sing N N 198 
ILE   OXT HXT  sing N N 199 
LEU   N   CA   sing N N 200 
LEU   N   H    sing N N 201 
LEU   N   H2   sing N N 202 
LEU   CA  C    sing N N 203 
LEU   CA  CB   sing N N 204 
LEU   CA  HA   sing N N 205 
LEU   C   O    doub N N 206 
LEU   C   OXT  sing N N 207 
LEU   CB  CG   sing N N 208 
LEU   CB  HB2  sing N N 209 
LEU   CB  HB3  sing N N 210 
LEU   CG  CD1  sing N N 211 
LEU   CG  CD2  sing N N 212 
LEU   CG  HG   sing N N 213 
LEU   CD1 HD11 sing N N 214 
LEU   CD1 HD12 sing N N 215 
LEU   CD1 HD13 sing N N 216 
LEU   CD2 HD21 sing N N 217 
LEU   CD2 HD22 sing N N 218 
LEU   CD2 HD23 sing N N 219 
LEU   OXT HXT  sing N N 220 
LYS   N   CA   sing N N 221 
LYS   N   H    sing N N 222 
LYS   N   H2   sing N N 223 
LYS   CA  C    sing N N 224 
LYS   CA  CB   sing N N 225 
LYS   CA  HA   sing N N 226 
LYS   C   O    doub N N 227 
LYS   C   OXT  sing N N 228 
LYS   CB  CG   sing N N 229 
LYS   CB  HB2  sing N N 230 
LYS   CB  HB3  sing N N 231 
LYS   CG  CD   sing N N 232 
LYS   CG  HG2  sing N N 233 
LYS   CG  HG3  sing N N 234 
LYS   CD  CE   sing N N 235 
LYS   CD  HD2  sing N N 236 
LYS   CD  HD3  sing N N 237 
LYS   CE  NZ   sing N N 238 
LYS   CE  HE2  sing N N 239 
LYS   CE  HE3  sing N N 240 
LYS   NZ  HZ1  sing N N 241 
LYS   NZ  HZ2  sing N N 242 
LYS   NZ  HZ3  sing N N 243 
LYS   OXT HXT  sing N N 244 
MET   N   CA   sing N N 245 
MET   N   H    sing N N 246 
MET   N   H2   sing N N 247 
MET   CA  C    sing N N 248 
MET   CA  CB   sing N N 249 
MET   CA  HA   sing N N 250 
MET   C   O    doub N N 251 
MET   C   OXT  sing N N 252 
MET   CB  CG   sing N N 253 
MET   CB  HB2  sing N N 254 
MET   CB  HB3  sing N N 255 
MET   CG  SD   sing N N 256 
MET   CG  HG2  sing N N 257 
MET   CG  HG3  sing N N 258 
MET   SD  CE   sing N N 259 
MET   CE  HE1  sing N N 260 
MET   CE  HE2  sing N N 261 
MET   CE  HE3  sing N N 262 
MET   OXT HXT  sing N N 263 
PHE   N   CA   sing N N 264 
PHE   N   H    sing N N 265 
PHE   N   H2   sing N N 266 
PHE   CA  C    sing N N 267 
PHE   CA  CB   sing N N 268 
PHE   CA  HA   sing N N 269 
PHE   C   O    doub N N 270 
PHE   C   OXT  sing N N 271 
PHE   CB  CG   sing N N 272 
PHE   CB  HB2  sing N N 273 
PHE   CB  HB3  sing N N 274 
PHE   CG  CD1  doub Y N 275 
PHE   CG  CD2  sing Y N 276 
PHE   CD1 CE1  sing Y N 277 
PHE   CD1 HD1  sing N N 278 
PHE   CD2 CE2  doub Y N 279 
PHE   CD2 HD2  sing N N 280 
PHE   CE1 CZ   doub Y N 281 
PHE   CE1 HE1  sing N N 282 
PHE   CE2 CZ   sing Y N 283 
PHE   CE2 HE2  sing N N 284 
PHE   CZ  HZ   sing N N 285 
PHE   OXT HXT  sing N N 286 
PRO   N   CA   sing N N 287 
PRO   N   CD   sing N N 288 
PRO   N   H    sing N N 289 
PRO   CA  C    sing N N 290 
PRO   CA  CB   sing N N 291 
PRO   CA  HA   sing N N 292 
PRO   C   O    doub N N 293 
PRO   C   OXT  sing N N 294 
PRO   CB  CG   sing N N 295 
PRO   CB  HB2  sing N N 296 
PRO   CB  HB3  sing N N 297 
PRO   CG  CD   sing N N 298 
PRO   CG  HG2  sing N N 299 
PRO   CG  HG3  sing N N 300 
PRO   CD  HD2  sing N N 301 
PRO   CD  HD3  sing N N 302 
PRO   OXT HXT  sing N N 303 
SER   N   CA   sing N N 304 
SER   N   H    sing N N 305 
SER   N   H2   sing N N 306 
SER   CA  C    sing N N 307 
SER   CA  CB   sing N N 308 
SER   CA  HA   sing N N 309 
SER   C   O    doub N N 310 
SER   C   OXT  sing N N 311 
SER   CB  OG   sing N N 312 
SER   CB  HB2  sing N N 313 
SER   CB  HB3  sing N N 314 
SER   OG  HG   sing N N 315 
SER   OXT HXT  sing N N 316 
SO4   S   O1   doub N N 317 
SO4   S   O2   doub N N 318 
SO4   S   O3   sing N N 319 
SO4   S   O4   sing N N 320 
THR   N   CA   sing N N 321 
THR   N   H    sing N N 322 
THR   N   H2   sing N N 323 
THR   CA  C    sing N N 324 
THR   CA  CB   sing N N 325 
THR   CA  HA   sing N N 326 
THR   C   O    doub N N 327 
THR   C   OXT  sing N N 328 
THR   CB  OG1  sing N N 329 
THR   CB  CG2  sing N N 330 
THR   CB  HB   sing N N 331 
THR   OG1 HG1  sing N N 332 
THR   CG2 HG21 sing N N 333 
THR   CG2 HG22 sing N N 334 
THR   CG2 HG23 sing N N 335 
THR   OXT HXT  sing N N 336 
TRP   N   CA   sing N N 337 
TRP   N   H    sing N N 338 
TRP   N   H2   sing N N 339 
TRP   CA  C    sing N N 340 
TRP   CA  CB   sing N N 341 
TRP   CA  HA   sing N N 342 
TRP   C   O    doub N N 343 
TRP   C   OXT  sing N N 344 
TRP   CB  CG   sing N N 345 
TRP   CB  HB2  sing N N 346 
TRP   CB  HB3  sing N N 347 
TRP   CG  CD1  doub Y N 348 
TRP   CG  CD2  sing Y N 349 
TRP   CD1 NE1  sing Y N 350 
TRP   CD1 HD1  sing N N 351 
TRP   CD2 CE2  doub Y N 352 
TRP   CD2 CE3  sing Y N 353 
TRP   NE1 CE2  sing Y N 354 
TRP   NE1 HE1  sing N N 355 
TRP   CE2 CZ2  sing Y N 356 
TRP   CE3 CZ3  doub Y N 357 
TRP   CE3 HE3  sing N N 358 
TRP   CZ2 CH2  doub Y N 359 
TRP   CZ2 HZ2  sing N N 360 
TRP   CZ3 CH2  sing Y N 361 
TRP   CZ3 HZ3  sing N N 362 
TRP   CH2 HH2  sing N N 363 
TRP   OXT HXT  sing N N 364 
TYR   N   CA   sing N N 365 
TYR   N   H    sing N N 366 
TYR   N   H2   sing N N 367 
TYR   CA  C    sing N N 368 
TYR   CA  CB   sing N N 369 
TYR   CA  HA   sing N N 370 
TYR   C   O    doub N N 371 
TYR   C   OXT  sing N N 372 
TYR   CB  CG   sing N N 373 
TYR   CB  HB2  sing N N 374 
TYR   CB  HB3  sing N N 375 
TYR   CG  CD1  doub Y N 376 
TYR   CG  CD2  sing Y N 377 
TYR   CD1 CE1  sing Y N 378 
TYR   CD1 HD1  sing N N 379 
TYR   CD2 CE2  doub Y N 380 
TYR   CD2 HD2  sing N N 381 
TYR   CE1 CZ   doub Y N 382 
TYR   CE1 HE1  sing N N 383 
TYR   CE2 CZ   sing Y N 384 
TYR   CE2 HE2  sing N N 385 
TYR   CZ  OH   sing N N 386 
TYR   OH  HH   sing N N 387 
TYR   OXT HXT  sing N N 388 
VAL   N   CA   sing N N 389 
VAL   N   H    sing N N 390 
VAL   N   H2   sing N N 391 
VAL   CA  C    sing N N 392 
VAL   CA  CB   sing N N 393 
VAL   CA  HA   sing N N 394 
VAL   C   O    doub N N 395 
VAL   C   OXT  sing N N 396 
VAL   CB  CG1  sing N N 397 
VAL   CB  CG2  sing N N 398 
VAL   CB  HB   sing N N 399 
VAL   CG1 HG11 sing N N 400 
VAL   CG1 HG12 sing N N 401 
VAL   CG1 HG13 sing N N 402 
VAL   CG2 HG21 sing N N 403 
VAL   CG2 HG22 sing N N 404 
VAL   CG2 HG23 sing N N 405 
VAL   OXT HXT  sing N N 406 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3QBY 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GRS 
_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]   0.023988 
_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]   0.023844 
_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]   0.006339 
_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  ? 0.427   4.574   2.519   1.00 47.54  ? 1   MET   A N   1 
ATOM   2    C  CA  . MET   A 1 2  ? -0.612  3.869   1.778   1.00 44.74  ? 1   MET   A CA  1 
ATOM   3    C  C   . MET   A 1 2  ? -0.008  2.800   0.872   1.00 41.96  ? 1   MET   A C   1 
ATOM   4    O  O   . MET   A 1 2  ? 1.099   2.966   0.361   1.00 50.05  ? 1   MET   A O   1 
ATOM   5    C  CB  . MET   A 1 2  ? -1.453  4.854   0.961   1.00 49.32  ? 1   MET   A CB  1 
ATOM   6    C  CG  . MET   A 1 2  ? -2.415  5.701   1.790   1.00 58.91  ? 1   MET   A CG  1 
ATOM   7    S  SD  . MET   A 1 2  ? -3.940  4.843   2.253   1.00 72.39  ? 1   MET   A SD  1 
ATOM   8    C  CE  . MET   A 1 2  ? -3.487  4.084   3.812   1.00 54.57  ? 1   MET   A CE  1 
ATOM   9    N  N   . PRO   A 1 3  ? -0.733  1.699   0.687   1.00 43.54  ? 2   PRO   A N   1 
ATOM   10   C  CA  . PRO   A 1 3  ? -0.170  0.560   -0.045  1.00 33.52  ? 2   PRO   A CA  1 
ATOM   11   C  C   . PRO   A 1 3  ? 0.031   0.844   -1.524  1.00 31.95  ? 2   PRO   A C   1 
ATOM   12   O  O   . PRO   A 1 3  ? -0.703  1.614   -2.148  1.00 34.51  ? 2   PRO   A O   1 
ATOM   13   C  CB  . PRO   A 1 3  ? -1.214  -0.544  0.162   1.00 38.08  ? 2   PRO   A CB  1 
ATOM   14   C  CG  . PRO   A 1 3  ? -1.921  -0.154  1.424   1.00 45.49  ? 2   PRO   A CG  1 
ATOM   15   C  CD  . PRO   A 1 3  ? -1.984  1.343   1.375   1.00 47.71  ? 2   PRO   A CD  1 
ATOM   16   N  N   . HIS   A 1 4  ? 1.045   0.190   -2.080  1.00 35.51  ? 3   HIS   A N   1 
ATOM   17   C  CA  . HIS   A 1 4  ? 1.336   0.214   -3.503  1.00 36.56  ? 3   HIS   A CA  1 
ATOM   18   C  C   . HIS   A 1 4  ? 0.895   -1.097  -4.141  1.00 36.20  ? 3   HIS   A C   1 
ATOM   19   O  O   . HIS   A 1 4  ? 0.466   -2.036  -3.466  1.00 32.32  ? 3   HIS   A O   1 
ATOM   20   C  CB  . HIS   A 1 4  ? 2.834   0.439   -3.749  1.00 39.74  ? 3   HIS   A CB  1 
ATOM   21   C  CG  . HIS   A 1 4  ? 3.348   1.746   -3.233  1.00 43.85  ? 3   HIS   A CG  1 
ATOM   22   N  ND1 . HIS   A 1 4  ? 3.093   2.198   -1.956  1.00 56.86  ? 3   HIS   A ND1 1 
ATOM   23   C  CD2 . HIS   A 1 4  ? 4.114   2.695   -3.822  1.00 59.23  ? 3   HIS   A CD2 1 
ATOM   24   C  CE1 . HIS   A 1 4  ? 3.673   3.372   -1.783  1.00 54.31  ? 3   HIS   A CE1 1 
ATOM   25   N  NE2 . HIS   A 1 4  ? 4.299   3.696   -2.900  1.00 51.46  ? 3   HIS   A NE2 1 
ATOM   26   N  N   . ALA   A 1 5  ? 1.010   -1.153  -5.463  1.00 35.70  ? 4   ALA   A N   1 
ATOM   27   C  CA  . ALA   A 1 5  ? 0.786   -2.409  -6.155  1.00 32.94  ? 4   ALA   A CA  1 
ATOM   28   C  C   . ALA   A 1 5  ? 1.914   -3.387  -5.836  1.00 31.31  ? 4   ALA   A C   1 
ATOM   29   O  O   . ALA   A 1 5  ? 3.022   -2.997  -5.458  1.00 32.65  ? 4   ALA   A O   1 
ATOM   30   C  CB  . ALA   A 1 5  ? 0.684   -2.185  -7.663  1.00 43.55  ? 4   ALA   A CB  1 
ATOM   31   N  N   . PHE   A 1 6  ? 1.615   -4.676  -5.977  1.00 28.98  ? 5   PHE   A N   1 
ATOM   32   C  CA  . PHE   A 1 6  ? 2.631   -5.694  -5.743  1.00 31.24  ? 5   PHE   A CA  1 
ATOM   33   C  C   . PHE   A 1 6  ? 3.749   -5.584  -6.774  1.00 32.47  ? 5   PHE   A C   1 
ATOM   34   O  O   . PHE   A 1 6  ? 3.533   -5.197  -7.925  1.00 30.32  ? 5   PHE   A O   1 
ATOM   35   C  CB  . PHE   A 1 6  ? 2.015   -7.092  -5.784  1.00 28.28  ? 5   PHE   A CB  1 
ATOM   36   C  CG  . PHE   A 1 6  ? 1.277   -7.464  -4.530  1.00 29.43  ? 5   PHE   A CG  1 
ATOM   37   C  CD1 . PHE   A 1 6  ? 1.968   -7.698  -3.349  1.00 28.39  ? 5   PHE   A CD1 1 
ATOM   38   C  CD2 . PHE   A 1 6  ? -0.105  -7.583  -4.528  1.00 29.04  ? 5   PHE   A CD2 1 
ATOM   39   C  CE1 . PHE   A 1 6  ? 1.300   -8.039  -2.184  1.00 26.68  ? 5   PHE   A CE1 1 
ATOM   40   C  CE2 . PHE   A 1 6  ? -0.780  -7.928  -3.364  1.00 25.19  ? 5   PHE   A CE2 1 
ATOM   41   C  CZ  . PHE   A 1 6  ? -0.079  -8.155  -2.194  1.00 23.28  ? 5   PHE   A CZ  1 
ATOM   42   N  N   . LYS   A 1 7  ? 4.955   -5.932  -6.348  1.00 28.25  ? 6   LYS   A N   1 
ATOM   43   C  CA  . LYS   A 1 7  ? 6.138   -5.848  -7.187  1.00 25.95  ? 6   LYS   A CA  1 
ATOM   44   C  C   . LYS   A 1 7  ? 7.029   -7.045  -6.903  1.00 24.91  ? 6   LYS   A C   1 
ATOM   45   O  O   . LYS   A 1 7  ? 6.941   -7.651  -5.829  1.00 24.91  ? 6   LYS   A O   1 
ATOM   46   C  CB  . LYS   A 1 7  ? 6.908   -4.546  -6.929  1.00 28.04  ? 6   LYS   A CB  1 
ATOM   47   C  CG  . LYS   A 1 7  ? 7.432   -4.414  -5.510  1.00 29.29  ? 6   LYS   A CG  1 
ATOM   48   C  CD  . LYS   A 1 7  ? 8.132   -3.080  -5.304  1.00 33.58  ? 6   LYS   A CD  1 
ATOM   49   C  CE  . LYS   A 1 7  ? 8.753   -2.984  -3.920  1.00 35.52  ? 6   LYS   A CE  1 
ATOM   50   N  NZ  . LYS   A 1 7  ? 7.734   -3.146  -2.851  1.00 36.63  ? 6   LYS   A NZ  1 
ATOM   51   N  N   . PRO   A 1 8  ? 7.888   -7.419  -7.848  1.00 25.08  ? 7   PRO   A N   1 
ATOM   52   C  CA  . PRO   A 1 8  ? 8.815   -8.529  -7.606  1.00 24.77  ? 7   PRO   A CA  1 
ATOM   53   C  C   . PRO   A 1 8  ? 9.627   -8.305  -6.338  1.00 24.52  ? 7   PRO   A C   1 
ATOM   54   O  O   . PRO   A 1 8  ? 10.111  -7.201  -6.074  1.00 26.84  ? 7   PRO   A O   1 
ATOM   55   C  CB  . PRO   A 1 8  ? 9.701   -8.525  -8.857  1.00 27.60  ? 7   PRO   A CB  1 
ATOM   56   C  CG  . PRO   A 1 8  ? 8.832   -7.943  -9.915  1.00 34.64  ? 7   PRO   A CG  1 
ATOM   57   C  CD  . PRO   A 1 8  ? 7.983   -6.911  -9.230  1.00 28.00  ? 7   PRO   A CD  1 
ATOM   58   N  N   . GLY   A 1 9  ? 9.763   -9.369  -5.544  1.00 22.64  ? 8   GLY   A N   1 
ATOM   59   C  CA  . GLY   A 1 9  ? 10.452  -9.330  -4.277  1.00 20.61  ? 8   GLY   A CA  1 
ATOM   60   C  C   . GLY   A 1 9  ? 9.548   -9.185  -3.068  1.00 23.57  ? 8   GLY   A C   1 
ATOM   61   O  O   . GLY   A 1 9  ? 9.987   -9.470  -1.950  1.00 23.04  ? 8   GLY   A O   1 
ATOM   62   N  N   . ASP   A 1 10 ? 8.303   -8.745  -3.259  1.00 20.03  ? 9   ASP   A N   1 
ATOM   63   C  CA  . ASP   A 1 10 ? 7.382   -8.635  -2.135  1.00 20.85  ? 9   ASP   A CA  1 
ATOM   64   C  C   . ASP   A 1 10 ? 7.142   -10.004 -1.514  1.00 20.79  ? 9   ASP   A C   1 
ATOM   65   O  O   . ASP   A 1 10 ? 6.983   -11.004 -2.219  1.00 21.56  ? 9   ASP   A O   1 
ATOM   66   C  CB  . ASP   A 1 10 ? 6.046   -8.036  -2.580  1.00 21.90  ? 9   ASP   A CB  1 
ATOM   67   C  CG  . ASP   A 1 10 ? 6.128   -6.549  -2.836  1.00 29.10  ? 9   ASP   A CG  1 
ATOM   68   O  OD1 . ASP   A 1 10 ? 7.093   -5.908  -2.366  1.00 26.20  ? 9   ASP   A OD1 1 
ATOM   69   O  OD2 . ASP   A 1 10 ? 5.208   -6.021  -3.494  1.00 28.29  ? 9   ASP   A OD2 1 
ATOM   70   N  N   . LEU   A 1 11 ? 7.092   -10.042 -0.185  1.00 19.59  ? 10  LEU   A N   1 
ATOM   71   C  CA  . LEU   A 1 11 ? 6.909   -11.287 0.549   1.00 18.40  ? 10  LEU   A CA  1 
ATOM   72   C  C   . LEU   A 1 11 ? 5.461   -11.392 1.003   1.00 21.75  ? 10  LEU   A C   1 
ATOM   73   O  O   . LEU   A 1 11 ? 4.890   -10.416 1.507   1.00 22.74  ? 10  LEU   A O   1 
ATOM   74   C  CB  . LEU   A 1 11 ? 7.856   -11.355 1.745   1.00 21.09  ? 10  LEU   A CB  1 
ATOM   75   C  CG  . LEU   A 1 11 ? 9.323   -11.133 1.356   1.00 18.67  ? 10  LEU   A CG  1 
ATOM   76   C  CD1 . LEU   A 1 11 ? 10.215  -11.251 2.580   1.00 22.00  ? 10  LEU   A CD1 1 
ATOM   77   C  CD2 . LEU   A 1 11 ? 9.731   -12.123 0.269   1.00 20.81  ? 10  LEU   A CD2 1 
ATOM   78   N  N   . VAL   A 1 12 ? 4.865   -12.569 0.809   1.00 20.57  ? 11  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 12 ? 3.437   -12.765 1.013   1.00 21.29  ? 11  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 12 ? 3.189   -14.135 1.629   1.00 21.70  ? 11  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 12 ? 4.058   -15.008 1.656   1.00 20.38  ? 11  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 12 ? 2.632   -12.645 -0.301  1.00 17.94  ? 11  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 12 ? 2.810   -11.275 -0.933  1.00 21.22  ? 11  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 12 ? 3.034   -13.754 -1.291  1.00 20.98  ? 11  VAL   A CG2 1 
ATOM   85   N  N   . PHE   A 1 13 ? 1.971   -14.311 2.129   1.00 21.52  ? 12  PHE   A N   1 
ATOM   86   C  CA  . PHE   A 1 13 ? 1.348   -15.624 2.177   1.00 20.22  ? 12  PHE   A CA  1 
ATOM   87   C  C   . PHE   A 1 13 ? 0.390   -15.704 0.998   1.00 20.78  ? 12  PHE   A C   1 
ATOM   88   O  O   . PHE   A 1 13 ? -0.419  -14.794 0.794   1.00 22.46  ? 12  PHE   A O   1 
ATOM   89   C  CB  . PHE   A 1 13 ? 0.604   -15.862 3.494   1.00 23.66  ? 12  PHE   A CB  1 
ATOM   90   C  CG  . PHE   A 1 13 ? 1.507   -15.966 4.683   1.00 21.77  ? 12  PHE   A CG  1 
ATOM   91   C  CD1 . PHE   A 1 13 ? 2.082   -17.175 5.028   1.00 21.12  ? 12  PHE   A CD1 1 
ATOM   92   C  CD2 . PHE   A 1 13 ? 1.789   -14.849 5.451   1.00 25.78  ? 12  PHE   A CD2 1 
ATOM   93   C  CE1 . PHE   A 1 13 ? 2.927   -17.272 6.133   1.00 24.70  ? 12  PHE   A CE1 1 
ATOM   94   C  CE2 . PHE   A 1 13 ? 2.625   -14.938 6.554   1.00 27.05  ? 12  PHE   A CE2 1 
ATOM   95   C  CZ  . PHE   A 1 13 ? 3.197   -16.155 6.895   1.00 29.27  ? 12  PHE   A CZ  1 
ATOM   96   N  N   . ALA   A 1 14 ? 0.496   -16.775 0.214   1.00 21.42  ? 13  ALA   A N   1 
ATOM   97   C  CA  . ALA   A 1 14 ? -0.326  -16.961 -0.975  1.00 22.40  ? 13  ALA   A CA  1 
ATOM   98   C  C   . ALA   A 1 14 ? -1.293  -18.108 -0.725  1.00 23.21  ? 13  ALA   A C   1 
ATOM   99   O  O   . ALA   A 1 14 ? -0.895  -19.153 -0.202  1.00 23.59  ? 13  ALA   A O   1 
ATOM   100  C  CB  . ALA   A 1 14 ? 0.542   -17.247 -2.205  1.00 22.44  ? 13  ALA   A CB  1 
ATOM   101  N  N   . LYS   A 1 15 ? -2.558  -17.914 -1.091  1.00 22.92  ? 14  LYS   A N   1 
ATOM   102  C  CA  . LYS   A 1 15 ? -3.610  -18.878 -0.787  1.00 26.03  ? 14  LYS   A CA  1 
ATOM   103  C  C   . LYS   A 1 15 ? -4.011  -19.615 -2.057  1.00 29.51  ? 14  LYS   A C   1 
ATOM   104  O  O   . LYS   A 1 15 ? -4.402  -18.987 -3.046  1.00 33.26  ? 14  LYS   A O   1 
ATOM   105  C  CB  . LYS   A 1 15 ? -4.820  -18.183 -0.159  1.00 24.94  ? 14  LYS   A CB  1 
ATOM   106  C  CG  . LYS   A 1 15 ? -5.897  -19.140 0.340   1.00 31.42  ? 14  LYS   A CG  1 
ATOM   107  C  CD  . LYS   A 1 15 ? -5.354  -20.039 1.439   1.00 31.43  ? 14  LYS   A CD  1 
ATOM   108  C  CE  . LYS   A 1 15 ? -6.434  -20.942 2.020   1.00 37.05  ? 14  LYS   A CE  1 
ATOM   109  N  NZ  . LYS   A 1 15 ? -6.863  -21.984 1.048   1.00 36.56  ? 14  LYS   A NZ  1 
ATOM   110  N  N   . MET   A 1 16 ? -3.911  -20.944 -2.022  1.00 27.46  ? 15  MET   A N   1 
ATOM   111  C  CA  . MET   A 1 16 ? -4.370  -21.815 -3.091  1.00 30.77  ? 15  MET   A CA  1 
ATOM   112  C  C   . MET   A 1 16 ? -5.452  -22.736 -2.545  1.00 40.64  ? 15  MET   A C   1 
ATOM   113  O  O   . MET   A 1 16 ? -5.433  -23.104 -1.366  1.00 31.83  ? 15  MET   A O   1 
ATOM   114  C  CB  . MET   A 1 16 ? -3.219  -22.653 -3.660  1.00 33.64  ? 15  MET   A CB  1 
ATOM   115  C  CG  . MET   A 1 16 ? -2.015  -21.839 -4.090  1.00 41.13  ? 15  MET   A CG  1 
ATOM   116  S  SD  . MET   A 1 16 ? -1.896  -21.724 -5.876  1.00 40.09  ? 15  MET   A SD  1 
ATOM   117  C  CE  . MET   A 1 16 ? -1.176  -23.309 -6.284  1.00 55.97  ? 15  MET   A CE  1 
ATOM   118  N  N   . LYS   A 1 17 ? -6.396  -23.099 -3.411  1.00 41.98  ? 16  LYS   A N   1 
ATOM   119  C  CA  . LYS   A 1 17 ? -7.444  -24.040 -3.034  1.00 41.51  ? 16  LYS   A CA  1 
ATOM   120  C  C   . LYS   A 1 17 ? -6.826  -25.317 -2.484  1.00 29.26  ? 16  LYS   A C   1 
ATOM   121  O  O   . LYS   A 1 17 ? -5.901  -25.877 -3.078  1.00 35.11  ? 16  LYS   A O   1 
ATOM   122  C  CB  . LYS   A 1 17 ? -8.323  -24.357 -4.247  1.00 51.33  ? 16  LYS   A CB  1 
ATOM   123  C  CG  . LYS   A 1 17 ? -9.596  -25.127 -3.932  1.00 55.97  ? 16  LYS   A CG  1 
ATOM   124  C  CD  . LYS   A 1 17 ? -10.744 -24.188 -3.588  1.00 63.03  ? 16  LYS   A CD  1 
ATOM   125  C  CE  . LYS   A 1 17 ? -12.031 -24.959 -3.319  1.00 70.51  ? 16  LYS   A CE  1 
ATOM   126  N  NZ  . LYS   A 1 17 ? -12.461 -25.767 -4.496  1.00 60.68  ? 16  LYS   A NZ  1 
ATOM   127  N  N   . GLY   A 1 18 ? -7.321  -25.759 -1.328  1.00 35.09  ? 17  GLY   A N   1 
ATOM   128  C  CA  . GLY   A 1 18 ? -6.849  -26.974 -0.698  1.00 36.09  ? 17  GLY   A CA  1 
ATOM   129  C  C   . GLY   A 1 18 ? -5.530  -26.867 0.036   1.00 40.72  ? 17  GLY   A C   1 
ATOM   130  O  O   . GLY   A 1 18 ? -5.054  -27.880 0.563   1.00 39.59  ? 17  GLY   A O   1 
ATOM   131  N  N   . TYR   A 1 19 ? -4.923  -25.684 0.087   1.00 38.76  ? 18  TYR   A N   1 
ATOM   132  C  CA  . TYR   A 1 19 ? -3.658  -25.469 0.768   1.00 30.67  ? 18  TYR   A CA  1 
ATOM   133  C  C   . TYR   A 1 19 ? -3.814  -24.374 1.810   1.00 28.44  ? 18  TYR   A C   1 
ATOM   134  O  O   . TYR   A 1 19 ? -4.587  -23.436 1.614   1.00 29.45  ? 18  TYR   A O   1 
ATOM   135  C  CB  . TYR   A 1 19 ? -2.552  -25.060 -0.215  1.00 33.34  ? 18  TYR   A CB  1 
ATOM   136  C  CG  . TYR   A 1 19 ? -2.064  -26.145 -1.155  1.00 30.63  ? 18  TYR   A CG  1 
ATOM   137  C  CD1 . TYR   A 1 19 ? -1.174  -27.118 -0.718  1.00 41.51  ? 18  TYR   A CD1 1 
ATOM   138  C  CD2 . TYR   A 1 19 ? -2.460  -26.169 -2.482  1.00 39.98  ? 18  TYR   A CD2 1 
ATOM   139  C  CE1 . TYR   A 1 19 ? -0.711  -28.100 -1.575  1.00 41.94  ? 18  TYR   A CE1 1 
ATOM   140  C  CE2 . TYR   A 1 19 ? -2.002  -27.146 -3.349  1.00 40.68  ? 18  TYR   A CE2 1 
ATOM   141  C  CZ  . TYR   A 1 19 ? -1.127  -28.109 -2.891  1.00 51.71  ? 18  TYR   A CZ  1 
ATOM   142  O  OH  . TYR   A 1 19 ? -0.669  -29.082 -3.749  1.00 55.87  ? 18  TYR   A OH  1 
ATOM   143  N  N   . PRO   A 1 20 ? -3.087  -24.460 2.920   1.00 29.07  ? 19  PRO   A N   1 
ATOM   144  C  CA  . PRO   A 1 20 ? -3.049  -23.335 3.858   1.00 32.18  ? 19  PRO   A CA  1 
ATOM   145  C  C   . PRO   A 1 20 ? -2.331  -22.150 3.232   1.00 29.08  ? 19  PRO   A C   1 
ATOM   146  O  O   . PRO   A 1 20 ? -1.580  -22.293 2.265   1.00 25.90  ? 19  PRO   A O   1 
ATOM   147  C  CB  . PRO   A 1 20 ? -2.262  -23.890 5.048   1.00 31.22  ? 19  PRO   A CB  1 
ATOM   148  C  CG  . PRO   A 1 20 ? -1.379  -24.936 4.441   1.00 30.72  ? 19  PRO   A CG  1 
ATOM   149  C  CD  . PRO   A 1 20 ? -2.194  -25.556 3.335   1.00 34.74  ? 19  PRO   A CD  1 
ATOM   150  N  N   . HIS   A 1 21 ? -2.585  -20.968 3.790   1.00 24.89  ? 20  HIS   A N   1 
ATOM   151  C  CA  . HIS   A 1 21 ? -1.854  -19.775 3.376   1.00 25.45  ? 20  HIS   A CA  1 
ATOM   152  C  C   . HIS   A 1 21 ? -0.358  -20.036 3.479   1.00 27.71  ? 20  HIS   A C   1 
ATOM   153  O  O   . HIS   A 1 21 ? 0.144   -20.395 4.547   1.00 26.89  ? 20  HIS   A O   1 
ATOM   154  C  CB  . HIS   A 1 21 ? -2.259  -18.579 4.238   1.00 27.45  ? 20  HIS   A CB  1 
ATOM   155  C  CG  . HIS   A 1 21 ? -3.706  -18.205 4.116   1.00 29.25  ? 20  HIS   A CG  1 
ATOM   156  N  ND1 . HIS   A 1 21 ? -4.715  -18.919 4.729   1.00 30.76  ? 20  HIS   A ND1 1 
ATOM   157  C  CD2 . HIS   A 1 21 ? -4.311  -17.186 3.460   1.00 34.27  ? 20  HIS   A CD2 1 
ATOM   158  C  CE1 . HIS   A 1 21 ? -5.879  -18.357 4.452   1.00 29.76  ? 20  HIS   A CE1 1 
ATOM   159  N  NE2 . HIS   A 1 21 ? -5.662  -17.305 3.683   1.00 34.54  ? 20  HIS   A NE2 1 
ATOM   160  N  N   . TRP   A 1 22 ? 0.351   -19.862 2.362   1.00 25.20  ? 21  TRP   A N   1 
ATOM   161  C  CA  . TRP   A 1 22 ? 1.672   -20.441 2.181   1.00 21.06  ? 21  TRP   A CA  1 
ATOM   162  C  C   . TRP   A 1 22 ? 2.723   -19.352 1.998   1.00 20.97  ? 21  TRP   A C   1 
ATOM   163  O  O   . TRP   A 1 22 ? 2.525   -18.438 1.183   1.00 21.12  ? 21  TRP   A O   1 
ATOM   164  C  CB  . TRP   A 1 22 ? 1.673   -21.374 0.956   1.00 23.00  ? 21  TRP   A CB  1 
ATOM   165  C  CG  . TRP   A 1 22 ? 2.742   -22.417 0.973   1.00 22.33  ? 21  TRP   A CG  1 
ATOM   166  C  CD1 . TRP   A 1 22 ? 4.068   -22.244 0.700   1.00 22.74  ? 21  TRP   A CD1 1 
ATOM   167  C  CD2 . TRP   A 1 22 ? 2.569   -23.813 1.261   1.00 26.94  ? 21  TRP   A CD2 1 
ATOM   168  N  NE1 . TRP   A 1 22 ? 4.735   -23.448 0.809   1.00 23.19  ? 21  TRP   A NE1 1 
ATOM   169  C  CE2 . TRP   A 1 22 ? 3.834   -24.424 1.152   1.00 25.76  ? 21  TRP   A CE2 1 
ATOM   170  C  CE3 . TRP   A 1 22 ? 1.465   -24.602 1.603   1.00 31.00  ? 21  TRP   A CE3 1 
ATOM   171  C  CZ2 . TRP   A 1 22 ? 4.027   -25.788 1.375   1.00 30.28  ? 21  TRP   A CZ2 1 
ATOM   172  C  CZ3 . TRP   A 1 22 ? 1.660   -25.959 1.824   1.00 28.69  ? 21  TRP   A CZ3 1 
ATOM   173  C  CH2 . TRP   A 1 22 ? 2.930   -26.535 1.709   1.00 26.21  ? 21  TRP   A CH2 1 
ATOM   174  N  N   . PRO   A 1 23 ? 3.851   -19.421 2.705   1.00 21.54  ? 22  PRO   A N   1 
ATOM   175  C  CA  . PRO   A 1 23 ? 4.903   -18.411 2.516   1.00 20.70  ? 22  PRO   A CA  1 
ATOM   176  C  C   . PRO   A 1 23 ? 5.414   -18.412 1.081   1.00 19.32  ? 22  PRO   A C   1 
ATOM   177  O  O   . PRO   A 1 23 ? 5.757   -19.456 0.524   1.00 21.29  ? 22  PRO   A O   1 
ATOM   178  C  CB  . PRO   A 1 23 ? 5.990   -18.842 3.508   1.00 18.86  ? 22  PRO   A CB  1 
ATOM   179  C  CG  . PRO   A 1 23 ? 5.782   -20.327 3.665   1.00 21.92  ? 22  PRO   A CG  1 
ATOM   180  C  CD  . PRO   A 1 23 ? 4.279   -20.498 3.617   1.00 24.91  ? 22  PRO   A CD  1 
ATOM   181  N  N   . ALA   A 1 24 ? 5.476   -17.227 0.484   1.00 18.74  ? 23  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 24 ? 5.804   -17.121 -0.932  1.00 18.56  ? 23  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 24 ? 6.348   -15.727 -1.215  1.00 18.52  ? 23  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 24 ? 6.367   -14.858 -0.345  1.00 19.21  ? 23  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 24 ? 4.579   -17.429 -1.798  1.00 20.59  ? 23  ALA   A CB  1 
ATOM   186  N  N   . ARG   A 1 25 ? 6.803   -15.528 -2.451  1.00 21.53  ? 24  ARG   A N   1 
ATOM   187  C  CA  . ARG   A 1 25 ? 7.255   -14.215 -2.885  1.00 22.11  ? 24  ARG   A CA  1 
ATOM   188  C  C   . ARG   A 1 25 ? 6.762   -13.956 -4.298  1.00 20.85  ? 24  ARG   A C   1 
ATOM   189  O  O   . ARG   A 1 25 ? 6.488   -14.882 -5.066  1.00 20.70  ? 24  ARG   A O   1 
ATOM   190  C  CB  . ARG   A 1 25 ? 8.785   -14.085 -2.836  1.00 21.27  ? 24  ARG   A CB  1 
ATOM   191  C  CG  . ARG   A 1 25 ? 9.493   -14.922 -3.890  1.00 22.90  ? 24  ARG   A CG  1 
ATOM   192  C  CD  . ARG   A 1 25 ? 11.009  -14.877 -3.734  1.00 21.61  ? 24  ARG   A CD  1 
ATOM   193  N  NE  . ARG   A 1 25 ? 11.659  -15.564 -4.848  1.00 24.59  ? 24  ARG   A NE  1 
ATOM   194  C  CZ  . ARG   A 1 25 ? 12.904  -16.021 -4.824  1.00 25.55  ? 24  ARG   A CZ  1 
ATOM   195  N  NH1 . ARG   A 1 25 ? 13.666  -15.886 -3.755  1.00 25.66  ? 24  ARG   A NH1 1 
ATOM   196  N  NH2 . ARG   A 1 25 ? 13.394  -16.632 -5.900  1.00 30.80  ? 24  ARG   A NH2 1 
ATOM   197  N  N   . ILE   A 1 26 ? 6.635   -12.673 -4.629  1.00 18.81  ? 25  ILE   A N   1 
ATOM   198  C  CA  . ILE   A 1 26 ? 6.447   -12.274 -6.020  1.00 19.05  ? 25  ILE   A CA  1 
ATOM   199  C  C   . ILE   A 1 26 ? 7.772   -12.459 -6.740  1.00 23.72  ? 25  ILE   A C   1 
ATOM   200  O  O   . ILE   A 1 26 ? 8.783   -11.842 -6.381  1.00 23.52  ? 25  ILE   A O   1 
ATOM   201  C  CB  . ILE   A 1 26 ? 5.975   -10.819 -6.118  1.00 20.35  ? 25  ILE   A CB  1 
ATOM   202  C  CG1 . ILE   A 1 26 ? 4.855   -10.534 -5.111  1.00 29.08  ? 25  ILE   A CG1 1 
ATOM   203  C  CG2 . ILE   A 1 26 ? 5.546   -10.490 -7.557  1.00 23.90  ? 25  ILE   A CG2 1 
ATOM   204  C  CD1 . ILE   A 1 26 ? 3.493   -10.968 -5.557  1.00 36.54  ? 25  ILE   A CD1 1 
ATOM   205  N  N   . ASP   A 1 27 ? 7.784   -13.327 -7.740  1.00 24.31  ? 26  ASP   A N   1 
ATOM   206  C  CA  . ASP   A 1 27 ? 9.008   -13.566 -8.478  1.00 26.37  ? 26  ASP   A CA  1 
ATOM   207  C  C   . ASP   A 1 27 ? 9.191   -12.516 -9.564  1.00 29.40  ? 26  ASP   A C   1 
ATOM   208  O  O   . ASP   A 1 27 ? 8.256   -11.820 -9.968  1.00 27.28  ? 26  ASP   A O   1 
ATOM   209  C  CB  . ASP   A 1 27 ? 9.005   -14.964 -9.094  1.00 29.21  ? 26  ASP   A CB  1 
ATOM   210  C  CG  . ASP   A 1 27 ? 10.112  -15.836 -8.549  1.00 26.26  ? 26  ASP   A CG  1 
ATOM   211  O  OD1 . ASP   A 1 27 ? 10.811  -15.397 -7.610  1.00 30.48  ? 26  ASP   A OD1 1 
ATOM   212  O  OD2 . ASP   A 1 27 ? 10.289  -16.958 -9.062  1.00 29.89  ? 26  ASP   A OD2 1 
ATOM   213  N  N   . ASP   A 1 28 ? 10.424  -12.398 -10.027 1.00 29.58  ? 27  ASP   A N   1 
ATOM   214  C  CA  . ASP   A 1 28 ? 10.638  -11.686 -11.268 1.00 32.51  ? 27  ASP   A CA  1 
ATOM   215  C  C   . ASP   A 1 28 ? 10.432  -12.650 -12.429 1.00 30.90  ? 27  ASP   A C   1 
ATOM   216  O  O   . ASP   A 1 28 ? 10.287  -13.861 -12.251 1.00 34.41  ? 27  ASP   A O   1 
ATOM   217  C  CB  . ASP   A 1 28 ? 12.037  -11.075 -11.320 1.00 41.76  ? 27  ASP   A CB  1 
ATOM   218  C  CG  . ASP   A 1 28 ? 12.018  -9.626  -11.751 1.00 54.39  ? 27  ASP   A CG  1 
ATOM   219  O  OD1 . ASP   A 1 28 ? 12.693  -8.807  -11.097 1.00 60.21  ? 27  ASP   A OD1 1 
ATOM   220  O  OD2 . ASP   A 1 28 ? 11.314  -9.301  -12.731 1.00 54.42  ? 27  ASP   A OD2 1 
ATOM   221  N  N   . ILE   A 1 29 ? 10.414  -12.098 -13.633 1.00 36.46  ? 28  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 29 ? 10.337  -12.889 -14.852 1.00 38.96  ? 28  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 29 ? 11.669  -12.734 -15.564 1.00 34.53  ? 28  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 29 ? 12.039  -11.623 -15.957 1.00 35.94  ? 28  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 29 ? 9.168   -12.444 -15.742 1.00 34.34  ? 28  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 29 ? 7.855   -12.560 -14.967 1.00 36.54  ? 28  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 29 ? 9.117   -13.281 -17.017 1.00 38.47  ? 28  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 29 ? 6.860   -11.479 -15.296 1.00 36.30  ? 28  ILE   A CD1 1 
ATOM   229  N  N   . ALA   A 1 30 ? 12.401  -13.835 -15.698 1.00 40.57  ? 29  ALA   A N   1 
ATOM   230  C  CA  . ALA   A 1 30 ? 13.676  -13.795 -16.397 1.00 37.90  ? 29  ALA   A CA  1 
ATOM   231  C  C   . ALA   A 1 30 ? 13.468  -13.475 -17.871 1.00 37.87  ? 29  ALA   A C   1 
ATOM   232  O  O   . ALA   A 1 30 ? 12.412  -13.750 -18.448 1.00 32.85  ? 29  ALA   A O   1 
ATOM   233  C  CB  . ALA   A 1 30 ? 14.412  -15.125 -16.252 1.00 36.03  ? 29  ALA   A CB  1 
ATOM   234  N  N   . ASP   A 1 31 ? 14.491  -12.876 -18.476 1.00 30.75  ? 30  ASP   A N   1 
ATOM   235  C  CA  . ASP   A 1 31 ? 14.481  -12.665 -19.915 1.00 34.41  ? 30  ASP   A CA  1 
ATOM   236  C  C   . ASP   A 1 31 ? 14.213  -13.982 -20.630 1.00 27.10  ? 30  ASP   A C   1 
ATOM   237  O  O   . ASP   A 1 31 ? 14.803  -15.015 -20.300 1.00 36.05  ? 30  ASP   A O   1 
ATOM   238  C  CB  . ASP   A 1 31 ? 15.816  -12.072 -20.371 1.00 35.03  ? 30  ASP   A CB  1 
ATOM   239  C  CG  . ASP   A 1 31 ? 15.903  -10.575 -20.137 1.00 33.24  ? 30  ASP   A CG  1 
ATOM   240  O  OD1 . ASP   A 1 31 ? 14.847  -9.918  -20.018 1.00 35.58  ? 30  ASP   A OD1 1 
ATOM   241  O  OD2 . ASP   A 1 31 ? 17.034  -10.048 -20.090 1.00 39.69  ? 30  ASP   A OD2 1 
ATOM   242  N  N   . GLY   A 1 32 ? 13.296  -13.946 -21.594 1.00 32.30  ? 31  GLY   A N   1 
ATOM   243  C  CA  . GLY   A 1 32 ? 12.965  -15.119 -22.374 1.00 29.10  ? 31  GLY   A CA  1 
ATOM   244  C  C   . GLY   A 1 32 ? 12.126  -16.160 -21.669 1.00 38.85  ? 31  GLY   A C   1 
ATOM   245  O  O   . GLY   A 1 32 ? 11.900  -17.232 -22.243 1.00 32.25  ? 31  GLY   A O   1 
ATOM   246  N  N   . ALA   A 1 33 ? 11.657  -15.890 -20.457 1.00 32.94  ? 32  ALA   A N   1 
ATOM   247  C  CA  . ALA   A 1 33 ? 10.857  -16.846 -19.704 1.00 33.17  ? 32  ALA   A CA  1 
ATOM   248  C  C   . ALA   A 1 33 ? 9.369   -16.601 -19.927 1.00 32.66  ? 32  ALA   A C   1 
ATOM   249  O  O   . ALA   A 1 33 ? 8.948   -15.521 -20.342 1.00 29.99  ? 32  ALA   A O   1 
ATOM   250  C  CB  . ALA   A 1 33 ? 11.186  -16.763 -18.210 1.00 37.78  ? 32  ALA   A CB  1 
ATOM   251  N  N   . VAL   A 1 34 ? 8.568   -17.631 -19.636 1.00 35.06  ? 33  VAL   A N   1 
ATOM   252  C  CA  . VAL   A 1 34 ? 7.124   -17.523 -19.812 1.00 31.32  ? 33  VAL   A CA  1 
ATOM   253  C  C   . VAL   A 1 34 ? 6.562   -16.489 -18.849 1.00 29.84  ? 33  VAL   A C   1 
ATOM   254  O  O   . VAL   A 1 34 ? 6.863   -16.500 -17.648 1.00 36.99  ? 33  VAL   A O   1 
ATOM   255  C  CB  . VAL   A 1 34 ? 6.463   -18.894 -19.614 1.00 32.98  ? 33  VAL   A CB  1 
ATOM   256  C  CG1 . VAL   A 1 34 ? 4.947   -18.762 -19.618 1.00 36.79  ? 33  VAL   A CG1 1 
ATOM   257  C  CG2 . VAL   A 1 34 ? 6.916   -19.855 -20.700 1.00 36.43  ? 33  VAL   A CG2 1 
ATOM   258  N  N   . LYS   A 1 35 ? 5.731   -15.573 -19.383 1.00 32.16  ? 34  LYS   A N   1 
ATOM   259  C  CA  . LYS   A 1 35 ? 5.052   -14.486 -18.697 1.00 33.63  ? 34  LYS   A CA  1 
ATOM   260  C  C   . LYS   A 1 35 ? 3.702   -14.944 -18.152 1.00 38.65  ? 34  LYS   A C   1 
ATOM   261  O  O   . LYS   A 1 35 ? 3.081   -15.863 -18.697 1.00 33.08  ? 34  LYS   A O   1 
ATOM   262  C  CB  . LYS   A 1 35 ? 4.850   -13.308 -19.645 1.00 38.72  ? 34  LYS   A CB  1 
ATOM   263  C  CG  . LYS   A 1 35 ? 6.136   -12.580 -20.003 1.00 37.41  ? 34  LYS   A CG  1 
ATOM   264  C  CD  . LYS   A 1 35 ? 5.869   -11.399 -20.917 1.00 44.29  ? 34  LYS   A CD  1 
ATOM   265  C  CE  . LYS   A 1 35 ? 5.374   -11.851 -22.282 1.00 43.05  ? 34  LYS   A CE  1 
ATOM   266  N  NZ  . LYS   A 1 35 ? 5.231   -10.705 -23.219 1.00 48.11  ? 34  LYS   A NZ  1 
ATOM   267  N  N   . PRO   A 1 36 ? 3.233   -14.328 -17.070 1.00 35.73  ? 35  PRO   A N   1 
ATOM   268  C  CA  . PRO   A 1 36 ? 1.946   -14.717 -16.493 1.00 36.03  ? 35  PRO   A CA  1 
ATOM   269  C  C   . PRO   A 1 36 ? 0.790   -14.144 -17.293 1.00 38.36  ? 35  PRO   A C   1 
ATOM   270  O  O   . PRO   A 1 36 ? 0.977   -13.220 -18.100 1.00 35.07  ? 35  PRO   A O   1 
ATOM   271  C  CB  . PRO   A 1 36 ? 2.001   -14.108 -15.084 1.00 32.53  ? 35  PRO   A CB  1 
ATOM   272  C  CG  . PRO   A 1 36 ? 2.862   -12.905 -15.249 1.00 44.37  ? 35  PRO   A CG  1 
ATOM   273  C  CD  . PRO   A 1 36 ? 3.905   -13.290 -16.268 1.00 38.12  ? 35  PRO   A CD  1 
ATOM   274  N  N   . PRO   A 1 37 ? -0.417  -14.670 -17.101 1.00 37.31  ? 36  PRO   A N   1 
ATOM   275  C  CA  . PRO   A 1 37 ? -1.607  -14.065 -17.713 1.00 39.14  ? 36  PRO   A CA  1 
ATOM   276  C  C   . PRO   A 1 37 ? -1.799  -12.640 -17.228 1.00 43.78  ? 36  PRO   A C   1 
ATOM   277  O  O   . PRO   A 1 37 ? -1.183  -12.229 -16.232 1.00 35.79  ? 36  PRO   A O   1 
ATOM   278  C  CB  . PRO   A 1 37 ? -2.749  -14.975 -17.233 1.00 36.27  ? 36  PRO   A CB  1 
ATOM   279  C  CG  . PRO   A 1 37 ? -2.095  -16.279 -16.928 1.00 39.21  ? 36  PRO   A CG  1 
ATOM   280  C  CD  . PRO   A 1 37 ? -0.735  -15.927 -16.400 1.00 35.47  ? 36  PRO   A CD  1 
ATOM   281  N  N   . PRO   A 1 38 ? -2.639  -11.851 -17.903 1.00 41.74  ? 37  PRO   A N   1 
ATOM   282  C  CA  . PRO   A 1 38 ? -2.883  -10.479 -17.444 1.00 45.05  ? 37  PRO   A CA  1 
ATOM   283  C  C   . PRO   A 1 38 ? -3.469  -10.458 -16.040 1.00 37.07  ? 37  PRO   A C   1 
ATOM   284  O  O   . PRO   A 1 38 ? -4.220  -11.351 -15.643 1.00 48.81  ? 37  PRO   A O   1 
ATOM   285  C  CB  . PRO   A 1 38 ? -3.880  -9.929  -18.473 1.00 48.29  ? 37  PRO   A CB  1 
ATOM   286  C  CG  . PRO   A 1 38 ? -3.675  -10.771 -19.682 1.00 41.60  ? 37  PRO   A CG  1 
ATOM   287  C  CD  . PRO   A 1 38 ? -3.330  -12.137 -19.173 1.00 50.60  ? 37  PRO   A CD  1 
ATOM   288  N  N   . ASN   A 1 39 ? -3.094  -9.425  -15.282 1.00 37.03  ? 38  ASN   A N   1 
ATOM   289  C  CA  . ASN   A 1 39 ? -3.521  -9.222  -13.897 1.00 42.54  ? 38  ASN   A CA  1 
ATOM   290  C  C   . ASN   A 1 39 ? -3.095  -10.361 -12.974 1.00 40.59  ? 38  ASN   A C   1 
ATOM   291  O  O   . ASN   A 1 39 ? -3.622  -10.493 -11.866 1.00 39.99  ? 38  ASN   A O   1 
ATOM   292  C  CB  . ASN   A 1 39 ? -5.037  -9.009  -13.799 1.00 51.84  ? 38  ASN   A CB  1 
ATOM   293  C  CG  . ASN   A 1 39 ? -5.466  -7.639  -14.288 1.00 59.29  ? 38  ASN   A CG  1 
ATOM   294  O  OD1 . ASN   A 1 39 ? -4.646  -6.729  -14.410 1.00 61.58  ? 38  ASN   A OD1 1 
ATOM   295  N  ND2 . ASN   A 1 39 ? -6.756  -7.484  -14.562 1.00 56.11  ? 38  ASN   A ND2 1 
ATOM   296  N  N   . LYS   A 1 40 ? -2.150  -11.193 -13.404 1.00 37.00  ? 39  LYS   A N   1 
ATOM   297  C  CA  . LYS   A 1 40 ? -1.593  -12.242 -12.564 1.00 29.18  ? 39  LYS   A CA  1 
ATOM   298  C  C   . LYS   A 1 40 ? -0.119  -11.967 -12.299 1.00 27.27  ? 39  LYS   A C   1 
ATOM   299  O  O   . LYS   A 1 40 ? 0.554   -11.258 -13.055 1.00 29.73  ? 39  LYS   A O   1 
ATOM   300  C  CB  . LYS   A 1 40 ? -1.758  -13.624 -13.202 1.00 34.04  ? 39  LYS   A CB  1 
ATOM   301  C  CG  . LYS   A 1 40 ? -3.199  -14.046 -13.447 1.00 41.76  ? 39  LYS   A CG  1 
ATOM   302  C  CD  . LYS   A 1 40 ? -4.041  -13.926 -12.186 1.00 33.99  ? 39  LYS   A CD  1 
ATOM   303  C  CE  . LYS   A 1 40 ? -5.495  -14.314 -12.444 1.00 37.84  ? 39  LYS   A CE  1 
ATOM   304  N  NZ  . LYS   A 1 40 ? -5.662  -15.773 -12.694 1.00 47.01  ? 39  LYS   A NZ  1 
ATOM   305  N  N   . TYR   A 1 41 ? 0.368   -12.529 -11.198 1.00 24.32  ? 40  TYR   A N   1 
ATOM   306  C  CA  . TYR   A 1 41 ? 1.754   -12.427 -10.783 1.00 23.36  ? 40  TYR   A CA  1 
ATOM   307  C  C   . TYR   A 1 41 ? 2.373   -13.814 -10.699 1.00 24.73  ? 40  TYR   A C   1 
ATOM   308  O  O   . TYR   A 1 41 ? 1.689   -14.784 -10.358 1.00 24.28  ? 40  TYR   A O   1 
ATOM   309  C  CB  . TYR   A 1 41 ? 1.882   -11.739 -9.414  1.00 22.26  ? 40  TYR   A CB  1 
ATOM   310  C  CG  . TYR   A 1 41 ? 1.404   -10.310 -9.409  1.00 22.24  ? 40  TYR   A CG  1 
ATOM   311  C  CD1 . TYR   A 1 41 ? 0.055   -10.012 -9.246  1.00 30.24  ? 40  TYR   A CD1 1 
ATOM   312  C  CD2 . TYR   A 1 41 ? 2.292   -9.258  -9.575  1.00 29.23  ? 40  TYR   A CD2 1 
ATOM   313  C  CE1 . TYR   A 1 41 ? -0.392  -8.703  -9.250  1.00 33.38  ? 40  TYR   A CE1 1 
ATOM   314  C  CE2 . TYR   A 1 41 ? 1.852   -7.944  -9.575  1.00 26.60  ? 40  TYR   A CE2 1 
ATOM   315  C  CZ  . TYR   A 1 41 ? 0.511   -7.675  -9.414  1.00 32.43  ? 40  TYR   A CZ  1 
ATOM   316  O  OH  . TYR   A 1 41 ? 0.071   -6.372  -9.419  1.00 35.91  ? 40  TYR   A OH  1 
ATOM   317  N  N   . PRO   A 1 42 ? 3.667   -13.946 -10.997 1.00 22.82  ? 41  PRO   A N   1 
ATOM   318  C  CA  . PRO   A 1 42 ? 4.342   -15.230 -10.757 1.00 19.73  ? 41  PRO   A CA  1 
ATOM   319  C  C   . PRO   A 1 42 ? 4.655   -15.364 -9.274  1.00 22.86  ? 41  PRO   A C   1 
ATOM   320  O  O   . PRO   A 1 42 ? 5.389   -14.550 -8.707  1.00 23.85  ? 41  PRO   A O   1 
ATOM   321  C  CB  . PRO   A 1 42 ? 5.617   -15.123 -11.600 1.00 24.48  ? 41  PRO   A CB  1 
ATOM   322  C  CG  . PRO   A 1 42 ? 5.902   -13.662 -11.660 1.00 25.89  ? 41  PRO   A CG  1 
ATOM   323  C  CD  . PRO   A 1 42 ? 4.577   -12.934 -11.563 1.00 26.63  ? 41  PRO   A CD  1 
ATOM   324  N  N   . ILE   A 1 43 ? 4.073   -16.377 -8.638  1.00 20.93  ? 42  ILE   A N   1 
ATOM   325  C  CA  . ILE   A 1 43 ? 4.200   -16.572 -7.198  1.00 20.16  ? 42  ILE   A CA  1 
ATOM   326  C  C   . ILE   A 1 43 ? 5.106   -17.770 -6.962  1.00 24.67  ? 42  ILE   A C   1 
ATOM   327  O  O   . ILE   A 1 43 ? 4.757   -18.905 -7.316  1.00 25.85  ? 42  ILE   A O   1 
ATOM   328  C  CB  . ILE   A 1 43 ? 2.834   -16.771 -6.522  1.00 20.74  ? 42  ILE   A CB  1 
ATOM   329  C  CG1 . ILE   A 1 43 ? 1.911   -15.595 -6.830  1.00 21.91  ? 42  ILE   A CG1 1 
ATOM   330  C  CG2 . ILE   A 1 43 ? 2.999   -16.940 -5.012  1.00 22.07  ? 42  ILE   A CG2 1 
ATOM   331  C  CD1 . ILE   A 1 43 ? 2.479   -14.245 -6.431  1.00 23.41  ? 42  ILE   A CD1 1 
ATOM   332  N  N   . PHE   A 1 44 ? 6.263   -17.522 -6.357  1.00 19.74  ? 43  PHE   A N   1 
ATOM   333  C  CA  . PHE   A 1 44 ? 7.199   -18.580 -5.996  1.00 20.32  ? 43  PHE   A CA  1 
ATOM   334  C  C   . PHE   A 1 44 ? 6.920   -19.014 -4.562  1.00 23.12  ? 43  PHE   A C   1 
ATOM   335  O  O   . PHE   A 1 44 ? 7.013   -18.203 -3.639  1.00 21.09  ? 43  PHE   A O   1 
ATOM   336  C  CB  . PHE   A 1 44 ? 8.642   -18.094 -6.140  1.00 20.84  ? 43  PHE   A CB  1 
ATOM   337  C  CG  . PHE   A 1 44 ? 9.673   -19.110 -5.730  1.00 22.35  ? 43  PHE   A CG  1 
ATOM   338  C  CD1 . PHE   A 1 44 ? 10.107  -20.074 -6.625  1.00 28.62  ? 43  PHE   A CD1 1 
ATOM   339  C  CD2 . PHE   A 1 44 ? 10.212  -19.093 -4.451  1.00 25.86  ? 43  PHE   A CD2 1 
ATOM   340  C  CE1 . PHE   A 1 44 ? 11.056  -21.011 -6.248  1.00 29.04  ? 43  PHE   A CE1 1 
ATOM   341  C  CE2 . PHE   A 1 44 ? 11.162  -20.021 -4.068  1.00 26.01  ? 43  PHE   A CE2 1 
ATOM   342  C  CZ  . PHE   A 1 44 ? 11.584  -20.986 -4.973  1.00 28.38  ? 43  PHE   A CZ  1 
ATOM   343  N  N   . PHE   A 1 45 ? 6.577   -20.285 -4.374  1.00 22.97  ? 44  PHE   A N   1 
ATOM   344  C  CA  . PHE   A 1 45 ? 6.229   -20.798 -3.055  1.00 21.28  ? 44  PHE   A CA  1 
ATOM   345  C  C   . PHE   A 1 45 ? 7.483   -21.339 -2.386  1.00 26.26  ? 44  PHE   A C   1 
ATOM   346  O  O   . PHE   A 1 45 ? 8.157   -22.214 -2.941  1.00 23.66  ? 44  PHE   A O   1 
ATOM   347  C  CB  . PHE   A 1 45 ? 5.160   -21.887 -3.169  1.00 25.09  ? 44  PHE   A CB  1 
ATOM   348  C  CG  . PHE   A 1 45 ? 3.817   -21.367 -3.556  1.00 21.29  ? 44  PHE   A CG  1 
ATOM   349  C  CD1 . PHE   A 1 45 ? 3.506   -21.128 -4.883  1.00 25.87  ? 44  PHE   A CD1 1 
ATOM   350  C  CD2 . PHE   A 1 45 ? 2.866   -21.090 -2.592  1.00 24.43  ? 44  PHE   A CD2 1 
ATOM   351  C  CE1 . PHE   A 1 45 ? 2.263   -20.635 -5.240  1.00 28.82  ? 44  PHE   A CE1 1 
ATOM   352  C  CE2 . PHE   A 1 45 ? 1.625   -20.598 -2.942  1.00 25.90  ? 44  PHE   A CE2 1 
ATOM   353  C  CZ  . PHE   A 1 45 ? 1.323   -20.371 -4.264  1.00 26.31  ? 44  PHE   A CZ  1 
ATOM   354  N  N   . PHE   A 1 46 ? 7.805   -20.806 -1.208  1.00 24.87  ? 45  PHE   A N   1 
ATOM   355  C  CA  . PHE   A 1 46 ? 8.963   -21.297 -0.480  1.00 22.13  ? 45  PHE   A CA  1 
ATOM   356  C  C   . PHE   A 1 46 ? 8.715   -22.732 -0.029  1.00 23.79  ? 45  PHE   A C   1 
ATOM   357  O  O   . PHE   A 1 46 ? 7.573   -23.178 0.115   1.00 26.07  ? 45  PHE   A O   1 
ATOM   358  C  CB  . PHE   A 1 46 ? 9.276   -20.397 0.721   1.00 18.69  ? 45  PHE   A CB  1 
ATOM   359  C  CG  . PHE   A 1 46 ? 9.718   -19.001 0.339   1.00 21.09  ? 45  PHE   A CG  1 
ATOM   360  C  CD1 . PHE   A 1 46 ? 10.930  -18.801 -0.297  1.00 21.91  ? 45  PHE   A CD1 1 
ATOM   361  C  CD2 . PHE   A 1 46 ? 8.934   -17.898 0.637   1.00 21.10  ? 45  PHE   A CD2 1 
ATOM   362  C  CE1 . PHE   A 1 46 ? 11.353  -17.533 -0.647  1.00 22.34  ? 45  PHE   A CE1 1 
ATOM   363  C  CE2 . PHE   A 1 46 ? 9.349   -16.623 0.293   1.00 20.79  ? 45  PHE   A CE2 1 
ATOM   364  C  CZ  . PHE   A 1 46 ? 10.562  -16.440 -0.353  1.00 22.13  ? 45  PHE   A CZ  1 
ATOM   365  N  N   . GLY   A 1 47 ? 9.805   -23.468 0.162   1.00 25.28  ? 46  GLY   A N   1 
ATOM   366  C  CA  . GLY   A 1 47 ? 9.701   -24.862 0.554   1.00 24.77  ? 46  GLY   A CA  1 
ATOM   367  C  C   . GLY   A 1 47 ? 9.492   -25.794 -0.622  1.00 34.68  ? 46  GLY   A C   1 
ATOM   368  O  O   . GLY   A 1 47 ? 10.388  -26.570 -0.968  1.00 34.86  ? 46  GLY   A O   1 
ATOM   369  N  N   . THR   A 1 48 ? 8.315   -25.728 -1.252  1.00 30.16  ? 47  THR   A N   1 
ATOM   370  C  CA  . THR   A 1 48 ? 8.071   -26.561 -2.428  1.00 36.28  ? 47  THR   A CA  1 
ATOM   371  C  C   . THR   A 1 48 ? 8.825   -26.046 -3.645  1.00 35.03  ? 47  THR   A C   1 
ATOM   372  O  O   . THR   A 1 48 ? 9.132   -26.827 -4.557  1.00 31.64  ? 47  THR   A O   1 
ATOM   373  C  CB  . THR   A 1 48 ? 6.576   -26.632 -2.744  1.00 32.03  ? 47  THR   A CB  1 
ATOM   374  O  OG1 . THR   A 1 48 ? 6.106   -25.333 -3.133  1.00 33.72  ? 47  THR   A OG1 1 
ATOM   375  C  CG2 . THR   A 1 48 ? 5.794   -27.111 -1.540  1.00 31.91  ? 47  THR   A CG2 1 
ATOM   376  N  N   . HIS   A 1 49 ? 9.117   -24.743 -3.681  1.00 31.12  ? 48  HIS   A N   1 
ATOM   377  C  CA  . HIS   A 1 49 ? 9.829   -24.088 -4.777  1.00 26.72  ? 48  HIS   A CA  1 
ATOM   378  C  C   . HIS   A 1 49 ? 9.057   -24.152 -6.090  1.00 26.11  ? 48  HIS   A C   1 
ATOM   379  O  O   . HIS   A 1 49 ? 9.651   -24.067 -7.168  1.00 31.49  ? 48  HIS   A O   1 
ATOM   380  C  CB  . HIS   A 1 49 ? 11.238  -24.666 -4.950  1.00 33.31  ? 48  HIS   A CB  1 
ATOM   381  C  CG  . HIS   A 1 49 ? 12.029  -24.700 -3.680  1.00 32.15  ? 48  HIS   A CG  1 
ATOM   382  N  ND1 . HIS   A 1 49 ? 12.811  -25.775 -3.317  1.00 34.44  ? 48  HIS   A ND1 1 
ATOM   383  C  CD2 . HIS   A 1 49 ? 12.143  -23.796 -2.677  1.00 25.74  ? 48  HIS   A CD2 1 
ATOM   384  C  CE1 . HIS   A 1 49 ? 13.378  -25.530 -2.149  1.00 35.93  ? 48  HIS   A CE1 1 
ATOM   385  N  NE2 . HIS   A 1 49 ? 12.987  -24.336 -1.738  1.00 31.83  ? 48  HIS   A NE2 1 
ATOM   386  N  N   . GLU   A 1 50 ? 7.737   -24.266 -6.017  1.00 28.03  ? 49  GLU   A N   1 
ATOM   387  C  CA  . GLU   A 1 50 ? 6.888   -24.266 -7.197  1.00 30.60  ? 49  GLU   A CA  1 
ATOM   388  C  C   . GLU   A 1 50 ? 6.374   -22.859 -7.495  1.00 24.93  ? 49  GLU   A C   1 
ATOM   389  O  O   . GLU   A 1 50 ? 6.311   -21.990 -6.621  1.00 27.22  ? 49  GLU   A O   1 
ATOM   390  C  CB  . GLU   A 1 50 ? 5.716   -25.230 -7.009  1.00 34.73  ? 49  GLU   A CB  1 
ATOM   391  C  CG  . GLU   A 1 50 ? 6.148   -26.690 -6.934  1.00 40.33  ? 49  GLU   A CG  1 
ATOM   392  C  CD  . GLU   A 1 50 ? 5.120   -27.580 -6.262  1.00 57.18  ? 49  GLU   A CD  1 
ATOM   393  O  OE1 . GLU   A 1 50 ? 3.925   -27.213 -6.249  1.00 63.85  ? 49  GLU   A OE1 1 
ATOM   394  O  OE2 . GLU   A 1 50 ? 5.511   -28.646 -5.738  1.00 62.02  ? 49  GLU   A OE2 1 
ATOM   395  N  N   . THR   A 1 51 ? 6.013   -22.639 -8.757  1.00 29.01  ? 50  THR   A N   1 
ATOM   396  C  CA  . THR   A 1 51 ? 5.499   -21.354 -9.211  1.00 23.90  ? 50  THR   A CA  1 
ATOM   397  C  C   . THR   A 1 51 ? 4.068   -21.522 -9.699  1.00 31.45  ? 50  THR   A C   1 
ATOM   398  O  O   . THR   A 1 51 ? 3.771   -22.452 -10.455 1.00 29.54  ? 50  THR   A O   1 
ATOM   399  C  CB  . THR   A 1 51 ? 6.366   -20.768 -10.332 1.00 32.63  ? 50  THR   A CB  1 
ATOM   400  O  OG1 . THR   A 1 51 ? 7.686   -20.513 -9.837  1.00 30.77  ? 50  THR   A OG1 1 
ATOM   401  C  CG2 . THR   A 1 51 ? 5.768   -19.465 -10.842 1.00 28.54  ? 50  THR   A CG2 1 
ATOM   402  N  N   . ALA   A 1 52 ? 3.186   -20.629 -9.258  1.00 26.46  ? 51  ALA   A N   1 
ATOM   403  C  CA  . ALA   A 1 52 ? 1.837   -20.524 -9.790  1.00 26.31  ? 51  ALA   A CA  1 
ATOM   404  C  C   . ALA   A 1 52 ? 1.536   -19.062 -10.085 1.00 26.99  ? 51  ALA   A C   1 
ATOM   405  O  O   . ALA   A 1 52 ? 2.180   -18.156 -9.551  1.00 27.83  ? 51  ALA   A O   1 
ATOM   406  C  CB  . ALA   A 1 52 ? 0.793   -21.100 -8.823  1.00 26.39  ? 51  ALA   A CB  1 
ATOM   407  N  N   . PHE   A 1 53 ? 0.554   -18.836 -10.959 1.00 25.83  ? 52  PHE   A N   1 
ATOM   408  C  CA  . PHE   A 1 53 ? 0.156   -17.493 -11.367 1.00 26.89  ? 52  PHE   A CA  1 
ATOM   409  C  C   . PHE   A 1 53 ? -1.100  -17.111 -10.596 1.00 32.39  ? 52  PHE   A C   1 
ATOM   410  O  O   . PHE   A 1 53 ? -2.139  -17.764 -10.736 1.00 34.54  ? 52  PHE   A O   1 
ATOM   411  C  CB  . PHE   A 1 53 ? -0.090  -17.428 -12.875 1.00 29.82  ? 52  PHE   A CB  1 
ATOM   412  C  CG  . PHE   A 1 53 ? 1.134   -17.704 -13.700 1.00 30.22  ? 52  PHE   A CG  1 
ATOM   413  C  CD1 . PHE   A 1 53 ? 2.333   -17.074 -13.411 1.00 32.20  ? 52  PHE   A CD1 1 
ATOM   414  C  CD2 . PHE   A 1 53 ? 1.091   -18.603 -14.753 1.00 37.55  ? 52  PHE   A CD2 1 
ATOM   415  C  CE1 . PHE   A 1 53 ? 3.467   -17.321 -14.163 1.00 40.59  ? 52  PHE   A CE1 1 
ATOM   416  C  CE2 . PHE   A 1 53 ? 2.223   -18.859 -15.510 1.00 39.39  ? 52  PHE   A CE2 1 
ATOM   417  C  CZ  . PHE   A 1 53 ? 3.412   -18.218 -15.215 1.00 37.89  ? 52  PHE   A CZ  1 
ATOM   418  N  N   . LEU   A 1 54 ? -1.001  -16.064 -9.778  1.00 26.88  ? 53  LEU   A N   1 
ATOM   419  C  CA  . LEU   A 1 54 ? -2.073  -15.691 -8.867  1.00 25.40  ? 53  LEU   A CA  1 
ATOM   420  C  C   . LEU   A 1 54 ? -2.377  -14.206 -8.971  1.00 25.11  ? 53  LEU   A C   1 
ATOM   421  O  O   . LEU   A 1 54 ? -1.521  -13.396 -9.336  1.00 25.93  ? 53  LEU   A O   1 
ATOM   422  C  CB  . LEU   A 1 54 ? -1.720  -16.026 -7.404  1.00 22.54  ? 53  LEU   A CB  1 
ATOM   423  C  CG  . LEU   A 1 54 ? -1.516  -17.504 -7.058  1.00 26.18  ? 53  LEU   A CG  1 
ATOM   424  C  CD1 . LEU   A 1 54 ? -1.263  -17.660 -5.569  1.00 27.92  ? 53  LEU   A CD1 1 
ATOM   425  C  CD2 . LEU   A 1 54 ? -2.721  -18.321 -7.496  1.00 39.81  ? 53  LEU   A CD2 1 
ATOM   426  N  N   . GLY   A 1 55 ? -3.614  -13.857 -8.635  1.00 24.61  ? 54  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55 ? -4.013  -12.474 -8.552  1.00 24.45  ? 54  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55 ? -3.973  -11.981 -7.117  1.00 23.08  ? 54  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55 ? -3.861  -12.766 -6.173  1.00 24.01  ? 54  GLY   A O   1 
ATOM   430  N  N   . PRO   A 1 56 ? -4.072  -10.662 -6.931  1.00 24.43  ? 55  PRO   A N   1 
ATOM   431  C  CA  . PRO   A 1 56 ? -3.970  -10.088 -5.577  1.00 19.88  ? 55  PRO   A CA  1 
ATOM   432  C  C   . PRO   A 1 56 ? -4.989  -10.619 -4.581  1.00 24.07  ? 55  PRO   A C   1 
ATOM   433  O  O   . PRO   A 1 56 ? -4.736  -10.550 -3.372  1.00 22.45  ? 55  PRO   A O   1 
ATOM   434  C  CB  . PRO   A 1 56 ? -4.168  -8.586  -5.828  1.00 25.46  ? 55  PRO   A CB  1 
ATOM   435  C  CG  . PRO   A 1 56 ? -3.649  -8.385  -7.202  1.00 29.35  ? 55  PRO   A CG  1 
ATOM   436  C  CD  . PRO   A 1 56 ? -4.034  -9.620  -7.972  1.00 28.37  ? 55  PRO   A CD  1 
ATOM   437  N  N   . LYS   A 1 57 ? -6.124  -11.160 -5.035  1.00 25.42  ? 56  LYS   A N   1 
ATOM   438  C  CA  . LYS   A 1 57 ? -7.115  -11.661 -4.087  1.00 24.17  ? 56  LYS   A CA  1 
ATOM   439  C  C   . LYS   A 1 57 ? -6.567  -12.791 -3.232  1.00 25.30  ? 56  LYS   A C   1 
ATOM   440  O  O   . LYS   A 1 57 ? -7.091  -13.045 -2.144  1.00 24.91  ? 56  LYS   A O   1 
ATOM   441  C  CB  . LYS   A 1 57 ? -8.370  -12.142 -4.822  1.00 28.73  ? 56  LYS   A CB  1 
ATOM   442  C  CG  . LYS   A 1 57 ? -8.167  -13.421 -5.619  1.00 30.92  ? 56  LYS   A CG  1 
ATOM   443  C  CD  . LYS   A 1 57 ? -9.461  -13.874 -6.284  1.00 34.81  ? 56  LYS   A CD  1 
ATOM   444  C  CE  . LYS   A 1 57 ? -9.299  -15.238 -6.939  1.00 37.93  ? 56  LYS   A CE  1 
ATOM   445  N  NZ  . LYS   A 1 57 ? -9.134  -16.324 -5.931  1.00 47.62  ? 56  LYS   A NZ  1 
ATOM   446  N  N   . ASP   A 1 58 ? -5.515  -13.467 -3.689  1.00 22.07  ? 57  ASP   A N   1 
ATOM   447  C  CA  . ASP   A 1 58 ? -4.944  -14.586 -2.958  1.00 26.19  ? 57  ASP   A CA  1 
ATOM   448  C  C   . ASP   A 1 58 ? -3.607  -14.250 -2.311  1.00 22.51  ? 57  ASP   A C   1 
ATOM   449  O  O   . ASP   A 1 58 ? -2.911  -15.161 -1.847  1.00 24.99  ? 57  ASP   A O   1 
ATOM   450  C  CB  . ASP   A 1 58 ? -4.801  -15.788 -3.891  1.00 31.15  ? 57  ASP   A CB  1 
ATOM   451  C  CG  . ASP   A 1 58 ? -6.148  -16.333 -4.334  1.00 31.40  ? 57  ASP   A CG  1 
ATOM   452  O  OD1 . ASP   A 1 58 ? -7.065  -16.385 -3.490  1.00 36.30  ? 57  ASP   A OD1 1 
ATOM   453  O  OD2 . ASP   A 1 58 ? -6.288  -16.704 -5.515  1.00 33.21  ? 57  ASP   A OD2 1 
ATOM   454  N  N   . LEU   A 1 59 ? -3.238  -12.972 -2.259  1.00 22.19  ? 58  LEU   A N   1 
ATOM   455  C  CA  . LEU   A 1 59 ? -1.931  -12.538 -1.769  1.00 21.44  ? 58  LEU   A CA  1 
ATOM   456  C  C   . LEU   A 1 59 ? -2.113  -11.694 -0.515  1.00 20.41  ? 58  LEU   A C   1 
ATOM   457  O  O   . LEU   A 1 59 ? -2.781  -10.657 -0.552  1.00 23.43  ? 58  LEU   A O   1 
ATOM   458  C  CB  . LEU   A 1 59 ? -1.181  -11.747 -2.848  1.00 20.95  ? 58  LEU   A CB  1 
ATOM   459  C  CG  . LEU   A 1 59 ? -1.023  -12.460 -4.187  1.00 20.76  ? 58  LEU   A CG  1 
ATOM   460  C  CD1 . LEU   A 1 59 ? -0.300  -11.562 -5.187  1.00 22.02  ? 58  LEU   A CD1 1 
ATOM   461  C  CD2 . LEU   A 1 59 ? -0.293  -13.794 -4.026  1.00 22.89  ? 58  LEU   A CD2 1 
ATOM   462  N  N   . PHE   A 1 60 ? -1.508  -12.134 0.587   1.00 20.41  ? 59  PHE   A N   1 
ATOM   463  C  CA  . PHE   A 1 60 ? -1.567  -11.476 1.884   1.00 19.04  ? 59  PHE   A CA  1 
ATOM   464  C  C   . PHE   A 1 60 ? -0.170  -11.030 2.294   1.00 20.72  ? 59  PHE   A C   1 
ATOM   465  O  O   . PHE   A 1 60 ? 0.775   -11.809 2.168   1.00 25.79  ? 59  PHE   A O   1 
ATOM   466  C  CB  . PHE   A 1 60 ? -2.136  -12.427 2.952   1.00 22.10  ? 59  PHE   A CB  1 
ATOM   467  C  CG  . PHE   A 1 60 ? -3.536  -12.903 2.656   1.00 25.19  ? 59  PHE   A CG  1 
ATOM   468  C  CD1 . PHE   A 1 60 ? -3.767  -13.856 1.670   1.00 27.07  ? 59  PHE   A CD1 1 
ATOM   469  C  CD2 . PHE   A 1 60 ? -4.613  -12.412 3.377   1.00 26.71  ? 59  PHE   A CD2 1 
ATOM   470  C  CE1 . PHE   A 1 60 ? -5.050  -14.301 1.395   1.00 26.77  ? 59  PHE   A CE1 1 
ATOM   471  C  CE2 . PHE   A 1 60 ? -5.899  -12.855 3.109   1.00 25.67  ? 59  PHE   A CE2 1 
ATOM   472  C  CZ  . PHE   A 1 60 ? -6.116  -13.799 2.119   1.00 22.36  ? 59  PHE   A CZ  1 
ATOM   473  N  N   . PRO   A 1 61 ? -0.001  -9.809  2.794   1.00 23.93  ? 60  PRO   A N   1 
ATOM   474  C  CA  . PRO   A 1 61 ? 1.350   -9.347  3.150   1.00 26.36  ? 60  PRO   A CA  1 
ATOM   475  C  C   . PRO   A 1 61 ? 1.957   -10.192 4.262   1.00 24.58  ? 60  PRO   A C   1 
ATOM   476  O  O   . PRO   A 1 61 ? 1.307   -10.487 5.268   1.00 27.84  ? 60  PRO   A O   1 
ATOM   477  C  CB  . PRO   A 1 61 ? 1.126   -7.898  3.594   1.00 31.21  ? 60  PRO   A CB  1 
ATOM   478  C  CG  . PRO   A 1 61 ? -0.315  -7.837  3.977   1.00 37.00  ? 60  PRO   A CG  1 
ATOM   479  C  CD  . PRO   A 1 61 ? -1.028  -8.788  3.066   1.00 27.97  ? 60  PRO   A CD  1 
ATOM   480  N  N   . TYR   A 1 62 ? 3.218   -10.590 4.066   1.00 23.24  ? 61  TYR   A N   1 
ATOM   481  C  CA  . TYR   A 1 62 ? 3.870   -11.489 5.013   1.00 25.01  ? 61  TYR   A CA  1 
ATOM   482  C  C   . TYR   A 1 62 ? 4.001   -10.848 6.389   1.00 23.83  ? 61  TYR   A C   1 
ATOM   483  O  O   . TYR   A 1 62 ? 3.672   -11.466 7.405   1.00 27.33  ? 61  TYR   A O   1 
ATOM   484  C  CB  . TYR   A 1 62 ? 5.244   -11.903 4.483   1.00 24.39  ? 61  TYR   A CB  1 
ATOM   485  C  CG  . TYR   A 1 62 ? 6.092   -12.632 5.503   1.00 22.69  ? 61  TYR   A CG  1 
ATOM   486  C  CD1 . TYR   A 1 62 ? 5.798   -13.940 5.872   1.00 22.92  ? 61  TYR   A CD1 1 
ATOM   487  C  CD2 . TYR   A 1 62 ? 7.185   -12.011 6.096   1.00 30.65  ? 61  TYR   A CD2 1 
ATOM   488  C  CE1 . TYR   A 1 62 ? 6.565   -14.607 6.804   1.00 26.75  ? 61  TYR   A CE1 1 
ATOM   489  C  CE2 . TYR   A 1 62 ? 7.958   -12.676 7.028   1.00 30.97  ? 61  TYR   A CE2 1 
ATOM   490  C  CZ  . TYR   A 1 62 ? 7.644   -13.970 7.378   1.00 32.88  ? 61  TYR   A CZ  1 
ATOM   491  O  OH  . TYR   A 1 62 ? 8.412   -14.633 8.309   1.00 30.32  ? 61  TYR   A OH  1 
ATOM   492  N  N   . ASP   A 1 63 ? 4.471   -9.603  6.439   1.00 28.10  ? 62  ASP   A N   1 
ATOM   493  C  CA  . ASP   A 1 63 ? 4.724   -8.971  7.730   1.00 36.30  ? 62  ASP   A CA  1 
ATOM   494  C  C   . ASP   A 1 63 ? 3.431   -8.758  8.508   1.00 41.53  ? 62  ASP   A C   1 
ATOM   495  O  O   . ASP   A 1 63 ? 3.380   -9.013  9.718   1.00 40.62  ? 62  ASP   A O   1 
ATOM   496  C  CB  . ASP   A 1 63 ? 5.474   -7.654  7.531   1.00 31.25  ? 62  ASP   A CB  1 
ATOM   497  C  CG  . ASP   A 1 63 ? 4.692   -6.638  6.710   1.00 48.10  ? 62  ASP   A CG  1 
ATOM   498  O  OD1 . ASP   A 1 63 ? 5.142   -5.476  6.636   1.00 46.50  ? 62  ASP   A OD1 1 
ATOM   499  O  OD2 . ASP   A 1 63 ? 3.630   -6.985  6.150   1.00 42.89  ? 62  ASP   A OD2 1 
ATOM   500  N  N   . LYS   A 1 64 ? 2.372   -8.314  7.826   1.00 37.96  ? 63  LYS   A N   1 
ATOM   501  C  CA  . LYS   A 1 64 ? 1.094   -8.076  8.493   1.00 36.64  ? 63  LYS   A CA  1 
ATOM   502  C  C   . LYS   A 1 64 ? 0.498   -9.368  9.034   1.00 34.73  ? 63  LYS   A C   1 
ATOM   503  O  O   . LYS   A 1 64 ? -0.109  -9.378  10.112  1.00 34.42  ? 63  LYS   A O   1 
ATOM   504  C  CB  . LYS   A 1 64 ? 0.123   -7.405  7.517   1.00 40.10  ? 63  LYS   A CB  1 
ATOM   505  C  CG  . LYS   A 1 64 ? -1.351  -7.376  7.946   1.00 41.62  ? 63  LYS   A CG  1 
ATOM   506  C  CD  . LYS   A 1 64 ? -2.245  -7.013  6.755   1.00 42.75  ? 63  LYS   A CD  1 
ATOM   507  C  CE  . LYS   A 1 64 ? -3.418  -6.116  7.136   1.00 47.77  ? 63  LYS   A CE  1 
ATOM   508  N  NZ  . LYS   A 1 64 ? -4.507  -6.834  7.849   1.00 51.86  ? 63  LYS   A NZ  1 
ATOM   509  N  N   . CYS   A 1 65 ? 0.671   -10.474 8.313   1.00 27.54  ? 64  CYS   A N   1 
ATOM   510  C  CA  . CYS   A 1 65 ? -0.111  -11.676 8.570   1.00 26.59  ? 64  CYS   A CA  1 
ATOM   511  C  C   . CYS   A 1 65 ? 0.702   -12.845 9.121   1.00 28.38  ? 64  CYS   A C   1 
ATOM   512  O  O   . CYS   A 1 65 ? 0.159   -13.946 9.249   1.00 32.33  ? 64  CYS   A O   1 
ATOM   513  C  CB  . CYS   A 1 65 ? -0.829  -12.108 7.288   1.00 33.65  ? 64  CYS   A CB  1 
ATOM   514  S  SG  . CYS   A 1 65 ? -2.006  -10.890 6.655   1.00 38.20  ? 64  CYS   A SG  1 
ATOM   515  N  N   . LYS   A 1 66 ? 1.980   -12.645 9.463   1.00 29.88  ? 65  LYS   A N   1 
ATOM   516  C  CA  . LYS   A 1 66 ? 2.790   -13.789 9.883   1.00 33.17  ? 65  LYS   A CA  1 
ATOM   517  C  C   . LYS   A 1 66 ? 2.381   -14.310 11.255  1.00 34.76  ? 65  LYS   A C   1 
ATOM   518  O  O   . LYS   A 1 66 ? 2.543   -15.505 11.533  1.00 33.13  ? 65  LYS   A O   1 
ATOM   519  C  CB  . LYS   A 1 66 ? 4.279   -13.441 9.869   1.00 32.59  ? 65  LYS   A CB  1 
ATOM   520  C  CG  . LYS   A 1 66 ? 4.682   -12.240 10.695  1.00 35.72  ? 65  LYS   A CG  1 
ATOM   521  C  CD  . LYS   A 1 66 ? 6.183   -12.022 10.575  1.00 47.80  ? 65  LYS   A CD  1 
ATOM   522  C  CE  . LYS   A 1 66 ? 6.627   -10.715 11.208  1.00 46.88  ? 65  LYS   A CE  1 
ATOM   523  N  NZ  . LYS   A 1 66 ? 8.083   -10.491 10.987  1.00 52.51  ? 65  LYS   A NZ  1 
ATOM   524  N  N   . ASP   A 1 67 ? 1.851   -13.444 12.123  1.00 34.80  ? 66  ASP   A N   1 
ATOM   525  C  CA  . ASP   A 1 67 ? 1.342   -13.928 13.402  1.00 44.01  ? 66  ASP   A CA  1 
ATOM   526  C  C   . ASP   A 1 67 ? 0.202   -14.913 13.205  1.00 34.99  ? 66  ASP   A C   1 
ATOM   527  O  O   . ASP   A 1 67 ? 0.057   -15.863 13.983  1.00 43.86  ? 66  ASP   A O   1 
ATOM   528  C  CB  . ASP   A 1 67 ? 0.878   -12.758 14.272  1.00 50.66  ? 66  ASP   A CB  1 
ATOM   529  C  CG  . ASP   A 1 67 ? 2.030   -11.918 14.784  1.00 60.73  ? 66  ASP   A CG  1 
ATOM   530  O  OD1 . ASP   A 1 67 ? 3.175   -12.417 14.787  1.00 57.03  ? 66  ASP   A OD1 1 
ATOM   531  O  OD2 . ASP   A 1 67 ? 1.788   -10.762 15.192  1.00 68.37  ? 66  ASP   A OD2 1 
ATOM   532  N  N   . LYS   A 1 68 ? -0.607  -14.714 12.164  1.00 34.11  ? 67  LYS   A N   1 
ATOM   533  C  CA  . LYS   A 1 68 ? -1.755  -15.569 11.903  1.00 32.63  ? 67  LYS   A CA  1 
ATOM   534  C  C   . LYS   A 1 68 ? -1.399  -16.799 11.076  1.00 40.07  ? 67  LYS   A C   1 
ATOM   535  O  O   . LYS   A 1 68 ? -1.906  -17.893 11.347  1.00 38.16  ? 67  LYS   A O   1 
ATOM   536  C  CB  . LYS   A 1 68 ? -2.847  -14.767 11.193  1.00 36.36  ? 67  LYS   A CB  1 
ATOM   537  C  CG  . LYS   A 1 68 ? -4.004  -15.610 10.705  1.00 39.50  ? 67  LYS   A CG  1 
ATOM   538  C  CD  . LYS   A 1 68 ? -4.999  -14.779 9.923   1.00 49.70  ? 67  LYS   A CD  1 
ATOM   539  C  CE  . LYS   A 1 68 ? -6.276  -14.591 10.709  1.00 57.40  ? 67  LYS   A CE  1 
ATOM   540  N  NZ  . LYS   A 1 68 ? -7.330  -13.934 9.887   1.00 58.92  ? 67  LYS   A NZ  1 
ATOM   541  N  N   . TYR   A 1 69 ? -0.526  -16.647 10.079  1.00 33.09  ? 68  TYR   A N   1 
ATOM   542  C  CA  . TYR   A 1 69 ? -0.269  -17.696 9.102   1.00 29.46  ? 68  TYR   A CA  1 
ATOM   543  C  C   . TYR   A 1 69 ? 1.091   -18.364 9.247   1.00 32.54  ? 68  TYR   A C   1 
ATOM   544  O  O   . TYR   A 1 69 ? 1.294   -19.438 8.671   1.00 35.09  ? 68  TYR   A O   1 
ATOM   545  C  CB  . TYR   A 1 69 ? -0.387  -17.125 7.680   1.00 30.84  ? 68  TYR   A CB  1 
ATOM   546  C  CG  . TYR   A 1 69 ? -1.773  -16.657 7.304   1.00 28.24  ? 68  TYR   A CG  1 
ATOM   547  C  CD1 . TYR   A 1 69 ? -2.899  -17.368 7.700   1.00 33.51  ? 68  TYR   A CD1 1 
ATOM   548  C  CD2 . TYR   A 1 69 ? -1.956  -15.508 6.546   1.00 29.46  ? 68  TYR   A CD2 1 
ATOM   549  C  CE1 . TYR   A 1 69 ? -4.168  -16.946 7.351   1.00 33.60  ? 68  TYR   A CE1 1 
ATOM   550  C  CE2 . TYR   A 1 69 ? -3.220  -15.076 6.195   1.00 30.46  ? 68  TYR   A CE2 1 
ATOM   551  C  CZ  . TYR   A 1 69 ? -4.322  -15.799 6.599   1.00 31.86  ? 68  TYR   A CZ  1 
ATOM   552  O  OH  . TYR   A 1 69 ? -5.582  -15.373 6.250   1.00 33.96  ? 68  TYR   A OH  1 
ATOM   553  N  N   . GLY   A 1 70 ? 2.023   -17.766 9.984   1.00 31.76  ? 69  GLY   A N   1 
ATOM   554  C  CA  . GLY   A 1 70 ? 3.378   -18.278 10.046  1.00 33.30  ? 69  GLY   A CA  1 
ATOM   555  C  C   . GLY   A 1 70 ? 3.634   -19.257 11.173  1.00 31.85  ? 69  GLY   A C   1 
ATOM   556  O  O   . GLY   A 1 70 ? 4.611   -19.117 11.914  1.00 40.27  ? 69  GLY   A O   1 
ATOM   557  N  N   . LYS   A 1 71 ? 2.761   -20.243 11.315  1.00 35.75  ? 70  LYS   A N   1 
ATOM   558  C  CA  . LYS   A 1 71 ? 2.927   -21.323 12.271  1.00 42.36  ? 70  LYS   A CA  1 
ATOM   559  C  C   . LYS   A 1 71 ? 3.270   -22.611 11.535  1.00 31.73  ? 70  LYS   A C   1 
ATOM   560  O  O   . LYS   A 1 71 ? 2.917   -22.767 10.362  1.00 37.60  ? 70  LYS   A O   1 
ATOM   561  C  CB  . LYS   A 1 71 ? 1.652   -21.537 13.096  1.00 37.65  ? 70  LYS   A CB  1 
ATOM   562  C  CG  . LYS   A 1 71 ? 1.282   -20.370 13.992  1.00 44.84  ? 70  LYS   A CG  1 
ATOM   563  C  CD  . LYS   A 1 71 ? -0.204  -20.059 13.897  1.00 61.20  ? 70  LYS   A CD  1 
ATOM   564  C  CE  . LYS   A 1 71 ? -0.678  -19.261 15.099  1.00 57.10  ? 70  LYS   A CE  1 
ATOM   565  N  NZ  . LYS   A 1 71 ? -1.960  -18.554 14.823  1.00 58.14  ? 70  LYS   A NZ  1 
ATOM   566  N  N   . PRO   A 1 72 ? 3.964   -23.549 12.182  1.00 36.14  ? 71  PRO   A N   1 
ATOM   567  C  CA  . PRO   A 1 72 ? 4.271   -24.819 11.515  1.00 32.83  ? 71  PRO   A CA  1 
ATOM   568  C  C   . PRO   A 1 72 ? 3.011   -25.536 11.048  1.00 38.63  ? 71  PRO   A C   1 
ATOM   569  O  O   . PRO   A 1 72 ? 1.941   -25.427 11.649  1.00 43.15  ? 71  PRO   A O   1 
ATOM   570  C  CB  . PRO   A 1 72 ? 5.002   -25.620 12.599  1.00 40.09  ? 71  PRO   A CB  1 
ATOM   571  C  CG  . PRO   A 1 72 ? 5.643   -24.578 13.444  1.00 39.04  ? 71  PRO   A CG  1 
ATOM   572  C  CD  . PRO   A 1 72 ? 4.661   -23.429 13.475  1.00 36.80  ? 71  PRO   A CD  1 
ATOM   573  N  N   . ASN   A 1 73 ? 3.156   -26.273 9.951   1.00 34.64  ? 72  ASN   A N   1 
ATOM   574  C  CA  . ASN   A 1 73 ? 2.051   -26.966 9.309   1.00 40.51  ? 72  ASN   A CA  1 
ATOM   575  C  C   . ASN   A 1 73 ? 2.542   -28.330 8.850   1.00 47.77  ? 72  ASN   A C   1 
ATOM   576  O  O   . ASN   A 1 73 ? 3.718   -28.502 8.518   1.00 46.84  ? 72  ASN   A O   1 
ATOM   577  C  CB  . ASN   A 1 73 ? 1.503   -26.155 8.119   1.00 43.37  ? 72  ASN   A CB  1 
ATOM   578  C  CG  . ASN   A 1 73 ? 0.160   -26.656 7.633   1.00 44.67  ? 72  ASN   A CG  1 
ATOM   579  O  OD1 . ASN   A 1 73 ? 0.083   -27.635 6.896   1.00 49.58  ? 72  ASN   A OD1 1 
ATOM   580  N  ND2 . ASN   A 1 73 ? -0.908  -25.976 8.035   1.00 50.97  ? 72  ASN   A ND2 1 
ATOM   581  N  N   . LYS   A 1 74 ? 1.631   -29.304 8.834   1.00 46.67  ? 73  LYS   A N   1 
ATOM   582  C  CA  . LYS   A 1 74 ? 2.020   -30.668 8.497   1.00 45.28  ? 73  LYS   A CA  1 
ATOM   583  C  C   . LYS   A 1 74 ? 2.286   -30.857 7.008   1.00 47.80  ? 73  LYS   A C   1 
ATOM   584  O  O   . LYS   A 1 74 ? 2.901   -31.858 6.626   1.00 45.08  ? 73  LYS   A O   1 
ATOM   585  C  CB  . LYS   A 1 74 ? 0.938   -31.648 8.954   1.00 43.13  ? 73  LYS   A CB  1 
ATOM   586  N  N   . ARG   A 1 75 ? 1.849   -29.925 6.165   1.00 37.52  ? 74  ARG   A N   1 
ATOM   587  C  CA  . ARG   A 1 75 ? 1.947   -30.120 4.726   1.00 42.12  ? 74  ARG   A CA  1 
ATOM   588  C  C   . ARG   A 1 75 ? 3.401   -30.113 4.262   1.00 43.14  ? 74  ARG   A C   1 
ATOM   589  O  O   . ARG   A 1 75 ? 4.251   -29.398 4.801   1.00 37.99  ? 74  ARG   A O   1 
ATOM   590  C  CB  . ARG   A 1 75 ? 1.151   -29.047 3.983   1.00 42.79  ? 74  ARG   A CB  1 
ATOM   591  C  CG  . ARG   A 1 75 ? -0.352  -29.157 4.181   1.00 44.24  ? 74  ARG   A CG  1 
ATOM   592  C  CD  . ARG   A 1 75 ? -0.895  -30.483 3.663   1.00 40.14  ? 74  ARG   A CD  1 
ATOM   593  N  NE  . ARG   A 1 75 ? -1.144  -30.462 2.226   1.00 51.89  ? 74  ARG   A NE  1 
ATOM   594  C  CZ  . ARG   A 1 75 ? -2.203  -29.899 1.658   1.00 48.56  ? 74  ARG   A CZ  1 
ATOM   595  N  NH1 . ARG   A 1 75 ? -3.112  -29.256 2.375   1.00 43.02  ? 74  ARG   A NH1 1 
ATOM   596  N  NH2 . ARG   A 1 75 ? -2.353  -29.983 0.340   1.00 52.78  ? 74  ARG   A NH2 1 
ATOM   597  N  N   . LYS   A 1 76 ? 3.669   -30.925 3.242   1.00 31.80  ? 75  LYS   A N   1 
ATOM   598  C  CA  . LYS   A 1 76 ? 5.022   -31.125 2.743   1.00 36.97  ? 75  LYS   A CA  1 
ATOM   599  C  C   . LYS   A 1 76 ? 5.629   -29.811 2.266   1.00 33.61  ? 75  LYS   A C   1 
ATOM   600  O  O   . LYS   A 1 76 ? 5.050   -29.111 1.433   1.00 32.75  ? 75  LYS   A O   1 
ATOM   601  C  CB  . LYS   A 1 76 ? 4.994   -32.139 1.601   1.00 48.50  ? 75  LYS   A CB  1 
ATOM   602  C  CG  . LYS   A 1 76 ? 6.347   -32.551 1.057   1.00 42.60  ? 75  LYS   A CG  1 
ATOM   603  C  CD  . LYS   A 1 76 ? 6.165   -33.356 -0.227  1.00 55.54  ? 75  LYS   A CD  1 
ATOM   604  C  CE  . LYS   A 1 76 ? 7.390   -34.193 -0.554  1.00 62.00  ? 75  LYS   A CE  1 
ATOM   605  N  NZ  . LYS   A 1 76 ? 8.611   -33.362 -0.713  1.00 61.97  ? 75  LYS   A NZ  1 
ATOM   606  N  N   . GLY   A 1 77 ? 6.806   -29.482 2.796   1.00 34.66  ? 76  GLY   A N   1 
ATOM   607  C  CA  . GLY   A 1 77 ? 7.528   -28.301 2.378   1.00 32.09  ? 76  GLY   A CA  1 
ATOM   608  C  C   . GLY   A 1 77 ? 7.191   -27.035 3.133   1.00 27.49  ? 76  GLY   A C   1 
ATOM   609  O  O   . GLY   A 1 77 ? 7.910   -26.039 2.986   1.00 27.76  ? 76  GLY   A O   1 
ATOM   610  N  N   . PHE   A 1 78 ? 6.137   -27.040 3.951   1.00 30.18  ? 77  PHE   A N   1 
ATOM   611  C  CA  . PHE   A 1 78 ? 5.687   -25.801 4.579   1.00 29.74  ? 77  PHE   A CA  1 
ATOM   612  C  C   . PHE   A 1 78 ? 6.720   -25.263 5.562   1.00 34.81  ? 77  PHE   A C   1 
ATOM   613  O  O   . PHE   A 1 78 ? 7.033   -24.067 5.558   1.00 27.48  ? 77  PHE   A O   1 
ATOM   614  C  CB  . PHE   A 1 78 ? 4.346   -26.025 5.279   1.00 28.71  ? 77  PHE   A CB  1 
ATOM   615  C  CG  . PHE   A 1 78 ? 3.663   -24.751 5.693   1.00 31.94  ? 77  PHE   A CG  1 
ATOM   616  C  CD1 . PHE   A 1 78 ? 3.962   -24.142 6.904   1.00 32.40  ? 77  PHE   A CD1 1 
ATOM   617  C  CD2 . PHE   A 1 78 ? 2.725   -24.156 4.865   1.00 28.13  ? 77  PHE   A CD2 1 
ATOM   618  C  CE1 . PHE   A 1 78 ? 3.335   -22.969 7.282   1.00 33.56  ? 77  PHE   A CE1 1 
ATOM   619  C  CE2 . PHE   A 1 78 ? 2.097   -22.981 5.238   1.00 28.14  ? 77  PHE   A CE2 1 
ATOM   620  C  CZ  . PHE   A 1 78 ? 2.402   -22.386 6.446   1.00 27.82  ? 77  PHE   A CZ  1 
ATOM   621  N  N   . ASN   A 1 79 ? 7.253   -26.131 6.424   1.00 30.15  ? 78  ASN   A N   1 
ATOM   622  C  CA  . ASN   A 1 79 ? 8.165   -25.662 7.460   1.00 25.04  ? 78  ASN   A CA  1 
ATOM   623  C  C   . ASN   A 1 79 ? 9.518   -25.267 6.885   1.00 24.04  ? 78  ASN   A C   1 
ATOM   624  O  O   . ASN   A 1 79 ? 10.155  -24.334 7.394   1.00 26.96  ? 78  ASN   A O   1 
ATOM   625  C  CB  . ASN   A 1 79 ? 8.313   -26.734 8.539   1.00 27.04  ? 78  ASN   A CB  1 
ATOM   626  C  CG  . ASN   A 1 79 ? 7.013   -26.992 9.267   1.00 33.46  ? 78  ASN   A CG  1 
ATOM   627  O  OD1 . ASN   A 1 79 ? 6.135   -26.129 9.304   1.00 28.55  ? 78  ASN   A OD1 1 
ATOM   628  N  ND2 . ASN   A 1 79 ? 6.876   -28.180 9.847   1.00 34.61  ? 78  ASN   A ND2 1 
ATOM   629  N  N   . GLU   A 1 80 ? 9.974   -25.951 5.834   1.00 24.33  ? 79  GLU   A N   1 
ATOM   630  C  CA  . GLU   A 1 80 ? 11.123  -25.447 5.097   1.00 26.96  ? 79  GLU   A CA  1 
ATOM   631  C  C   . GLU   A 1 80 ? 10.817  -24.073 4.523   1.00 26.29  ? 79  GLU   A C   1 
ATOM   632  O  O   . GLU   A 1 80 ? 11.655  -23.166 4.582   1.00 25.60  ? 79  GLU   A O   1 
ATOM   633  C  CB  . GLU   A 1 80 ? 11.524  -26.417 3.985   1.00 32.23  ? 79  GLU   A CB  1 
ATOM   634  C  CG  . GLU   A 1 80 ? 12.722  -25.949 3.163   1.00 27.82  ? 79  GLU   A CG  1 
ATOM   635  C  CD  . GLU   A 1 80 ? 13.174  -26.978 2.148   1.00 43.35  ? 79  GLU   A CD  1 
ATOM   636  O  OE1 . GLU   A 1 80 ? 12.434  -27.959 1.924   1.00 43.02  ? 79  GLU   A OE1 1 
ATOM   637  O  OE2 . GLU   A 1 80 ? 14.272  -26.807 1.578   1.00 41.40  ? 79  GLU   A OE2 1 
ATOM   638  N  N   . GLY   A 1 81 ? 9.601   -23.891 4.003   1.00 28.35  ? 80  GLY   A N   1 
ATOM   639  C  CA  . GLY   A 1 81 ? 9.227   -22.594 3.454   1.00 23.90  ? 80  GLY   A CA  1 
ATOM   640  C  C   . GLY   A 1 81 ? 9.205   -21.492 4.496   1.00 23.19  ? 80  GLY   A C   1 
ATOM   641  O  O   . GLY   A 1 81 ? 9.574   -20.348 4.211   1.00 24.73  ? 80  GLY   A O   1 
ATOM   642  N  N   . LEU   A 1 82 ? 8.753   -21.810 5.712   1.00 24.13  ? 81  LEU   A N   1 
ATOM   643  C  CA  . LEU   A 1 82 ? 8.804   -20.825 6.786   1.00 21.22  ? 81  LEU   A CA  1 
ATOM   644  C  C   . LEU   A 1 82 ? 10.238  -20.390 7.064   1.00 24.18  ? 81  LEU   A C   1 
ATOM   645  O  O   . LEU   A 1 82 ? 10.501  -19.204 7.286   1.00 24.64  ? 81  LEU   A O   1 
ATOM   646  C  CB  . LEU   A 1 82 ? 8.161   -21.388 8.056   1.00 24.15  ? 81  LEU   A CB  1 
ATOM   647  C  CG  . LEU   A 1 82 ? 6.646   -21.591 8.104   1.00 27.05  ? 81  LEU   A CG  1 
ATOM   648  C  CD1 . LEU   A 1 82 ? 6.247   -22.155 9.464   1.00 28.10  ? 81  LEU   A CD1 1 
ATOM   649  C  CD2 . LEU   A 1 82 ? 5.900   -20.293 7.831   1.00 28.44  ? 81  LEU   A CD2 1 
ATOM   650  N  N   . TRP   A 1 83 ? 11.184  -21.337 7.048   1.00 26.25  ? 82  TRP   A N   1 
ATOM   651  C  CA  . TRP   A 1 83 ? 12.581  -20.968 7.248   1.00 27.33  ? 82  TRP   A CA  1 
ATOM   652  C  C   . TRP   A 1 83 ? 13.069  -20.059 6.131   1.00 22.97  ? 82  TRP   A C   1 
ATOM   653  O  O   . TRP   A 1 83 ? 13.783  -19.082 6.381   1.00 26.13  ? 82  TRP   A O   1 
ATOM   654  C  CB  . TRP   A 1 83 ? 13.470  -22.213 7.328   1.00 25.45  ? 82  TRP   A CB  1 
ATOM   655  C  CG  . TRP   A 1 83 ? 14.920  -21.853 7.545   1.00 27.89  ? 82  TRP   A CG  1 
ATOM   656  C  CD1 . TRP   A 1 83 ? 15.560  -21.736 8.740   1.00 26.94  ? 82  TRP   A CD1 1 
ATOM   657  C  CD2 . TRP   A 1 83 ? 15.896  -21.539 6.534   1.00 26.15  ? 82  TRP   A CD2 1 
ATOM   658  N  NE1 . TRP   A 1 83 ? 16.873  -21.379 8.542   1.00 33.94  ? 82  TRP   A NE1 1 
ATOM   659  C  CE2 . TRP   A 1 83 ? 17.104  -21.253 7.198   1.00 30.46  ? 82  TRP   A CE2 1 
ATOM   660  C  CE3 . TRP   A 1 83 ? 15.862  -21.475 5.136   1.00 30.34  ? 82  TRP   A CE3 1 
ATOM   661  C  CZ2 . TRP   A 1 83 ? 18.270  -20.911 6.515   1.00 36.62  ? 82  TRP   A CZ2 1 
ATOM   662  C  CZ3 . TRP   A 1 83 ? 17.022  -21.139 4.458   1.00 29.77  ? 82  TRP   A CZ3 1 
ATOM   663  C  CH2 . TRP   A 1 83 ? 18.209  -20.859 5.149   1.00 32.05  ? 82  TRP   A CH2 1 
ATOM   664  N  N   . GLU   A 1 84 ? 12.702  -20.376 4.888   1.00 23.28  ? 83  GLU   A N   1 
ATOM   665  C  CA  . GLU   A 1 84 ? 13.202  -19.615 3.747   1.00 22.91  ? 83  GLU   A CA  1 
ATOM   666  C  C   . GLU   A 1 84 ? 12.700  -18.179 3.773   1.00 27.68  ? 83  GLU   A C   1 
ATOM   667  O  O   . GLU   A 1 84 ? 13.477  -17.237 3.580   1.00 22.09  ? 83  GLU   A O   1 
ATOM   668  C  CB  . GLU   A 1 84 ? 12.803  -20.308 2.445   1.00 24.63  ? 83  GLU   A CB  1 
ATOM   669  C  CG  . GLU   A 1 84 ? 13.486  -21.664 2.263   1.00 27.12  ? 83  GLU   A CG  1 
ATOM   670  C  CD  . GLU   A 1 84 ? 13.044  -22.386 1.004   1.00 34.51  ? 83  GLU   A CD  1 
ATOM   671  O  OE1 . GLU   A 1 84 ? 12.059  -21.942 0.381   1.00 27.97  ? 83  GLU   A OE1 1 
ATOM   672  O  OE2 . GLU   A 1 84 ? 13.678  -23.398 0.631   1.00 29.78  ? 83  GLU   A OE2 1 
ATOM   673  N  N   . ILE   A 1 85 ? 11.402  -17.983 4.018   1.00 19.53  ? 84  ILE   A N   1 
ATOM   674  C  CA  . ILE   A 1 85 ? 10.867  -16.623 3.961   1.00 21.94  ? 84  ILE   A CA  1 
ATOM   675  C  C   . ILE   A 1 85 ? 11.445  -15.758 5.077   1.00 26.84  ? 84  ILE   A C   1 
ATOM   676  O  O   . ILE   A 1 85 ? 11.570  -14.534 4.926   1.00 24.01  ? 84  ILE   A O   1 
ATOM   677  C  CB  . ILE   A 1 85 ? 9.325   -16.644 3.997   1.00 21.06  ? 84  ILE   A CB  1 
ATOM   678  C  CG1 . ILE   A 1 85 ? 8.774   -15.268 3.617   1.00 23.63  ? 84  ILE   A CG1 1 
ATOM   679  C  CG2 . ILE   A 1 85 ? 8.795   -17.084 5.373   1.00 20.89  ? 84  ILE   A CG2 1 
ATOM   680  C  CD1 . ILE   A 1 85 ? 7.358   -15.311 3.103   1.00 19.17  ? 84  ILE   A CD1 1 
ATOM   681  N  N   . GLN   A 1 86 ? 11.821  -16.371 6.201   1.00 22.87  ? 85  GLN   A N   1 
ATOM   682  C  CA  . GLN   A 1 86 ? 12.345  -15.604 7.324   1.00 24.85  ? 85  GLN   A CA  1 
ATOM   683  C  C   . GLN   A 1 86 ? 13.840  -15.342 7.184   1.00 26.51  ? 85  GLN   A C   1 
ATOM   684  O  O   . GLN   A 1 86 ? 14.319  -14.271 7.574   1.00 29.48  ? 85  GLN   A O   1 
ATOM   685  C  CB  . GLN   A 1 86 ? 12.052  -16.342 8.637   1.00 29.81  ? 85  GLN   A CB  1 
ATOM   686  C  CG  . GLN   A 1 86 ? 12.384  -15.551 9.898   1.00 30.91  ? 85  GLN   A CG  1 
ATOM   687  C  CD  . GLN   A 1 86 ? 11.847  -16.199 11.169  1.00 45.28  ? 85  GLN   A CD  1 
ATOM   688  O  OE1 . GLN   A 1 86 ? 11.619  -17.407 11.219  1.00 40.32  ? 85  GLN   A OE1 1 
ATOM   689  N  NE2 . GLN   A 1 86 ? 11.636  -15.388 12.202  1.00 46.55  ? 85  GLN   A NE2 1 
ATOM   690  N  N   . ASN   A 1 87 ? 14.588  -16.296 6.626   1.00 23.01  ? 86  ASN   A N   1 
ATOM   691  C  CA  . ASN   A 1 87 ? 16.044  -16.265 6.700   1.00 26.53  ? 86  ASN   A CA  1 
ATOM   692  C  C   . ASN   A 1 87 ? 16.756  -16.017 5.379   1.00 25.59  ? 86  ASN   A C   1 
ATOM   693  O  O   . ASN   A 1 87 ? 17.874  -15.503 5.402   1.00 27.88  ? 86  ASN   A O   1 
ATOM   694  C  CB  . ASN   A 1 87 ? 16.564  -17.572 7.309   1.00 25.51  ? 86  ASN   A CB  1 
ATOM   695  C  CG  . ASN   A 1 87 ? 16.177  -17.712 8.760   1.00 31.12  ? 86  ASN   A CG  1 
ATOM   696  O  OD1 . ASN   A 1 87 ? 16.665  -16.974 9.615   1.00 38.66  ? 86  ASN   A OD1 1 
ATOM   697  N  ND2 . ASN   A 1 87 ? 15.261  -18.631 9.044   1.00 28.97  ? 86  ASN   A ND2 1 
ATOM   698  N  N   . ASN   A 1 88 ? 16.168  -16.380 4.231   1.00 22.49  ? 87  ASN   A N   1 
ATOM   699  C  CA  . ASN   A 1 88 ? 16.779  -16.000 2.959   1.00 23.34  ? 87  ASN   A CA  1 
ATOM   700  C  C   . ASN   A 1 88 ? 15.710  -15.890 1.875   1.00 23.47  ? 87  ASN   A C   1 
ATOM   701  O  O   . ASN   A 1 88 ? 15.717  -16.647 0.893   1.00 25.37  ? 87  ASN   A O   1 
ATOM   702  C  CB  . ASN   A 1 88 ? 17.872  -16.990 2.550   1.00 27.49  ? 87  ASN   A CB  1 
ATOM   703  C  CG  . ASN   A 1 88 ? 18.991  -16.321 1.754   1.00 28.65  ? 87  ASN   A CG  1 
ATOM   704  O  OD1 . ASN   A 1 88 ? 18.761  -15.349 1.028   1.00 23.88  ? 87  ASN   A OD1 1 
ATOM   705  N  ND2 . ASN   A 1 88 ? 20.206  -16.837 1.888   1.00 30.43  ? 87  ASN   A ND2 1 
ATOM   706  N  N   . PRO   A 1 89 ? 14.787  -14.936 2.011   1.00 23.86  ? 88  PRO   A N   1 
ATOM   707  C  CA  . PRO   A 1 89 ? 13.640  -14.893 1.095   1.00 22.17  ? 88  PRO   A CA  1 
ATOM   708  C  C   . PRO   A 1 89 ? 13.985  -14.484 -0.325  1.00 26.32  ? 88  PRO   A C   1 
ATOM   709  O  O   . PRO   A 1 89 ? 13.178  -14.744 -1.222  1.00 22.08  ? 88  PRO   A O   1 
ATOM   710  C  CB  . PRO   A 1 89 ? 12.709  -13.867 1.753   1.00 19.89  ? 88  PRO   A CB  1 
ATOM   711  C  CG  . PRO   A 1 89 ? 13.636  -12.979 2.541   1.00 21.89  ? 88  PRO   A CG  1 
ATOM   712  C  CD  . PRO   A 1 89 ? 14.715  -13.892 3.046   1.00 21.68  ? 88  PRO   A CD  1 
ATOM   713  N  N   . HIS   A 1 90 ? 15.132  -13.845 -0.571  1.00 21.27  ? 89  HIS   A N   1 
ATOM   714  C  CA  . HIS   A 1 90 ? 15.462  -13.380 -1.912  1.00 18.92  ? 89  HIS   A CA  1 
ATOM   715  C  C   . HIS   A 1 90 ? 16.554  -14.212 -2.581  1.00 21.34  ? 89  HIS   A C   1 
ATOM   716  O  O   . HIS   A 1 90 ? 17.100  -13.806 -3.613  1.00 22.42  ? 89  HIS   A O   1 
ATOM   717  C  CB  . HIS   A 1 90 ? 15.856  -11.904 -1.865  1.00 21.98  ? 89  HIS   A CB  1 
ATOM   718  C  CG  . HIS   A 1 90 ? 14.819  -11.033 -1.225  1.00 22.40  ? 89  HIS   A CG  1 
ATOM   719  N  ND1 . HIS   A 1 90 ? 13.559  -10.865 -1.760  1.00 21.90  ? 89  HIS   A ND1 1 
ATOM   720  C  CD2 . HIS   A 1 90 ? 14.847  -10.296 -0.091  1.00 23.51  ? 89  HIS   A CD2 1 
ATOM   721  C  CE1 . HIS   A 1 90 ? 12.859  -10.054 -0.986  1.00 20.93  ? 89  HIS   A CE1 1 
ATOM   722  N  NE2 . HIS   A 1 90 ? 13.618  -9.693  0.032   1.00 22.68  ? 89  HIS   A NE2 1 
ATOM   723  N  N   . ALA   A 1 91 ? 16.859  -15.385 -2.035  1.00 26.56  ? 90  ALA   A N   1 
ATOM   724  C  CA  . ALA   A 1 91 ? 17.933  -16.191 -2.589  1.00 26.22  ? 90  ALA   A CA  1 
ATOM   725  C  C   . ALA   A 1 91 ? 17.504  -16.852 -3.902  1.00 30.39  ? 90  ALA   A C   1 
ATOM   726  O  O   . ALA   A 1 91 ? 16.323  -16.903 -4.255  1.00 26.37  ? 90  ALA   A O   1 
ATOM   727  C  CB  . ALA   A 1 91 ? 18.369  -17.257 -1.584  1.00 26.29  ? 90  ALA   A CB  1 
ATOM   728  N  N   . SER   A 1 92 ? 18.496  -17.368 -4.631  1.00 36.37  ? 91  SER   A N   1 
ATOM   729  C  CA  . SER   A 1 92 ? 18.232  -18.205 -5.796  1.00 37.46  ? 91  SER   A CA  1 
ATOM   730  C  C   . SER   A 1 92 ? 17.923  -19.621 -5.336  1.00 40.48  ? 91  SER   A C   1 
ATOM   731  O  O   . SER   A 1 92 ? 18.718  -20.229 -4.614  1.00 39.95  ? 91  SER   A O   1 
ATOM   732  C  CB  . SER   A 1 92 ? 19.432  -18.230 -6.743  1.00 44.46  ? 91  SER   A CB  1 
ATOM   733  O  OG  . SER   A 1 92 ? 19.768  -16.939 -7.206  1.00 50.71  ? 91  SER   A OG  1 
ATOM   734  N  N   . TYR   A 1 93 ? 16.773  -20.144 -5.751  1.00 38.33  ? 92  TYR   A N   1 
ATOM   735  C  CA  . TYR   A 1 93 ? 16.382  -21.495 -5.369  1.00 41.32  ? 92  TYR   A CA  1 
ATOM   736  C  C   . TYR   A 1 93 ? 16.304  -22.406 -6.588  1.00 41.51  ? 92  TYR   A C   1 
ATOM   737  O  O   . TYR   A 1 93 ? 16.048  -23.603 -6.465  1.00 61.20  ? 92  TYR   A O   1 
ATOM   738  C  CB  . TYR   A 1 93 ? 15.042  -21.480 -4.629  1.00 44.42  ? 92  TYR   A CB  1 
ATOM   739  C  CG  . TYR   A 1 93 ? 15.129  -20.928 -3.225  1.00 37.78  ? 92  TYR   A CG  1 
ATOM   740  C  CD1 . TYR   A 1 93 ? 15.450  -21.750 -2.156  1.00 41.39  ? 92  TYR   A CD1 1 
ATOM   741  C  CD2 . TYR   A 1 93 ? 14.897  -19.581 -2.970  1.00 36.84  ? 92  TYR   A CD2 1 
ATOM   742  C  CE1 . TYR   A 1 93 ? 15.536  -21.251 -0.870  1.00 40.56  ? 92  TYR   A CE1 1 
ATOM   743  C  CE2 . TYR   A 1 93 ? 14.981  -19.074 -1.684  1.00 32.66  ? 92  TYR   A CE2 1 
ATOM   744  C  CZ  . TYR   A 1 93 ? 15.300  -19.912 -0.640  1.00 32.64  ? 92  TYR   A CZ  1 
ATOM   745  O  OH  . TYR   A 1 93 ? 15.390  -19.419 0.642   1.00 37.02  ? 92  TYR   A OH  1 
ATOM   746  N  N   . MET   B 1 2  ? 38.473  -10.496 -41.779 1.00 73.53  ? 1   MET   B N   1 
ATOM   747  C  CA  . MET   B 1 2  ? 38.101  -11.526 -42.742 1.00 71.25  ? 1   MET   B CA  1 
ATOM   748  C  C   . MET   B 1 2  ? 36.600  -11.624 -42.915 1.00 61.94  ? 1   MET   B C   1 
ATOM   749  O  O   . MET   B 1 2  ? 35.873  -11.782 -41.935 1.00 65.71  ? 1   MET   B O   1 
ATOM   750  C  CB  . MET   B 1 2  ? 38.644  -12.886 -42.313 1.00 74.90  ? 1   MET   B CB  1 
ATOM   751  C  CG  . MET   B 1 2  ? 40.139  -12.934 -42.293 1.00 85.71  ? 1   MET   B CG  1 
ATOM   752  S  SD  . MET   B 1 2  ? 40.774  -11.944 -43.649 1.00 95.59  ? 1   MET   B SD  1 
ATOM   753  C  CE  . MET   B 1 2  ? 42.471  -12.471 -43.627 1.00 79.69  ? 1   MET   B CE  1 
ATOM   754  N  N   . PRO   B 1 3  ? 36.132  -11.532 -44.158 1.00 50.38  ? 2   PRO   B N   1 
ATOM   755  C  CA  . PRO   B 1 3  ? 34.713  -11.796 -44.421 1.00 43.45  ? 2   PRO   B CA  1 
ATOM   756  C  C   . PRO   B 1 3  ? 34.366  -13.233 -44.066 1.00 55.45  ? 2   PRO   B C   1 
ATOM   757  O  O   . PRO   B 1 3  ? 34.999  -14.180 -44.539 1.00 49.11  ? 2   PRO   B O   1 
ATOM   758  C  CB  . PRO   B 1 3  ? 34.572  -11.532 -45.925 1.00 48.25  ? 2   PRO   B CB  1 
ATOM   759  C  CG  . PRO   B 1 3  ? 35.734  -10.668 -46.277 1.00 42.16  ? 2   PRO   B CG  1 
ATOM   760  C  CD  . PRO   B 1 3  ? 36.848  -11.090 -45.366 1.00 43.00  ? 2   PRO   B CD  1 
ATOM   761  N  N   . HIS   B 1 4  ? 33.367  -13.388 -43.211 1.00 49.39  ? 3   HIS   B N   1 
ATOM   762  C  CA  . HIS   B 1 4  ? 32.861  -14.693 -42.825 1.00 53.36  ? 3   HIS   B CA  1 
ATOM   763  C  C   . HIS   B 1 4  ? 31.475  -14.892 -43.428 1.00 54.06  ? 3   HIS   B C   1 
ATOM   764  O  O   . HIS   B 1 4  ? 30.918  -13.995 -44.069 1.00 47.31  ? 3   HIS   B O   1 
ATOM   765  C  CB  . HIS   B 1 4  ? 32.842  -14.830 -41.301 1.00 49.51  ? 3   HIS   B CB  1 
ATOM   766  C  CG  . HIS   B 1 4  ? 34.200  -14.759 -40.671 1.00 56.78  ? 3   HIS   B CG  1 
ATOM   767  N  ND1 . HIS   B 1 4  ? 35.249  -15.562 -41.068 1.00 64.03  ? 3   HIS   B ND1 1 
ATOM   768  C  CD2 . HIS   B 1 4  ? 34.679  -13.987 -39.666 1.00 63.31  ? 3   HIS   B CD2 1 
ATOM   769  C  CE1 . HIS   B 1 4  ? 36.316  -15.284 -40.339 1.00 65.12  ? 3   HIS   B CE1 1 
ATOM   770  N  NE2 . HIS   B 1 4  ? 35.996  -14.332 -39.481 1.00 64.27  ? 3   HIS   B NE2 1 
ATOM   771  N  N   . ALA   B 1 5  ? 30.928  -16.096 -43.234 1.00 42.57  ? 4   ALA   B N   1 
ATOM   772  C  CA  . ALA   B 1 5  ? 29.578  -16.376 -43.713 1.00 44.60  ? 4   ALA   B CA  1 
ATOM   773  C  C   . ALA   B 1 5  ? 28.581  -15.390 -43.126 1.00 35.97  ? 4   ALA   B C   1 
ATOM   774  O  O   . ALA   B 1 5  ? 27.657  -14.941 -43.815 1.00 39.69  ? 4   ALA   B O   1 
ATOM   775  C  CB  . ALA   B 1 5  ? 29.180  -17.808 -43.361 1.00 34.06  ? 4   ALA   B CB  1 
ATOM   776  N  N   . PHE   B 1 6  ? 28.755  -15.048 -41.854 1.00 43.91  ? 5   PHE   B N   1 
ATOM   777  C  CA  . PHE   B 1 6  ? 27.967  -14.028 -41.181 1.00 39.23  ? 5   PHE   B CA  1 
ATOM   778  C  C   . PHE   B 1 6  ? 28.831  -12.797 -40.962 1.00 41.28  ? 5   PHE   B C   1 
ATOM   779  O  O   . PHE   B 1 6  ? 29.971  -12.908 -40.495 1.00 49.35  ? 5   PHE   B O   1 
ATOM   780  C  CB  . PHE   B 1 6  ? 27.435  -14.537 -39.841 1.00 34.73  ? 5   PHE   B CB  1 
ATOM   781  C  CG  . PHE   B 1 6  ? 26.459  -15.671 -39.967 1.00 33.26  ? 5   PHE   B CG  1 
ATOM   782  C  CD1 . PHE   B 1 6  ? 25.097  -15.427 -39.997 1.00 35.57  ? 5   PHE   B CD1 1 
ATOM   783  C  CD2 . PHE   B 1 6  ? 26.903  -16.977 -40.051 1.00 40.48  ? 5   PHE   B CD2 1 
ATOM   784  C  CE1 . PHE   B 1 6  ? 24.193  -16.467 -40.109 1.00 37.91  ? 5   PHE   B CE1 1 
ATOM   785  C  CE2 . PHE   B 1 6  ? 26.004  -18.019 -40.166 1.00 30.66  ? 5   PHE   B CE2 1 
ATOM   786  C  CZ  . PHE   B 1 6  ? 24.651  -17.765 -40.192 1.00 30.42  ? 5   PHE   B CZ  1 
ATOM   787  N  N   . LYS   B 1 7  ? 28.290  -11.633 -41.293 1.00 35.60  ? 6   LYS   B N   1 
ATOM   788  C  CA  . LYS   B 1 7  ? 28.970  -10.368 -41.084 1.00 37.42  ? 6   LYS   B CA  1 
ATOM   789  C  C   . LYS   B 1 7  ? 28.184  -9.510  -40.103 1.00 39.39  ? 6   LYS   B C   1 
ATOM   790  O  O   . LYS   B 1 7  ? 26.963  -9.662  -39.972 1.00 30.62  ? 6   LYS   B O   1 
ATOM   791  C  CB  . LYS   B 1 7  ? 29.149  -9.615  -42.410 1.00 42.09  ? 6   LYS   B CB  1 
ATOM   792  C  CG  . LYS   B 1 7  ? 27.861  -9.330  -43.164 1.00 43.37  ? 6   LYS   B CG  1 
ATOM   793  C  CD  . LYS   B 1 7  ? 28.168  -8.750  -44.538 1.00 41.89  ? 6   LYS   B CD  1 
ATOM   794  C  CE  . LYS   B 1 7  ? 26.897  -8.485  -45.317 1.00 48.15  ? 6   LYS   B CE  1 
ATOM   795  N  NZ  . LYS   B 1 7  ? 26.088  -9.726  -45.435 1.00 40.11  ? 6   LYS   B NZ  1 
ATOM   796  N  N   . PRO   B 1 8  ? 28.855  -8.607  -39.390 1.00 41.23  ? 7   PRO   B N   1 
ATOM   797  C  CA  . PRO   B 1 8  ? 28.153  -7.733  -38.441 1.00 32.70  ? 7   PRO   B CA  1 
ATOM   798  C  C   . PRO   B 1 8  ? 26.994  -6.996  -39.095 1.00 36.00  ? 7   PRO   B C   1 
ATOM   799  O  O   . PRO   B 1 8  ? 27.127  -6.423  -40.179 1.00 35.60  ? 7   PRO   B O   1 
ATOM   800  C  CB  . PRO   B 1 8  ? 29.250  -6.771  -37.979 1.00 40.89  ? 7   PRO   B CB  1 
ATOM   801  C  CG  . PRO   B 1 8  ? 30.509  -7.559  -38.112 1.00 48.57  ? 7   PRO   B CG  1 
ATOM   802  C  CD  . PRO   B 1 8  ? 30.317  -8.444  -39.316 1.00 41.25  ? 7   PRO   B CD  1 
ATOM   803  N  N   . GLY   B 1 9  ? 25.844  -7.015  -38.423 1.00 29.89  ? 8   GLY   B N   1 
ATOM   804  C  CA  . GLY   B 1 9  ? 24.625  -6.452  -38.957 1.00 28.44  ? 8   GLY   B CA  1 
ATOM   805  C  C   . GLY   B 1 9  ? 23.696  -7.455  -39.604 1.00 28.84  ? 8   GLY   B C   1 
ATOM   806  O  O   . GLY   B 1 9  ? 22.550  -7.106  -39.904 1.00 31.29  ? 8   GLY   B O   1 
ATOM   807  N  N   . ASP   B 1 10 ? 24.154  -8.684  -39.837 1.00 28.98  ? 9   ASP   B N   1 
ATOM   808  C  CA  . ASP   B 1 10 ? 23.258  -9.705  -40.355 1.00 28.82  ? 9   ASP   B CA  1 
ATOM   809  C  C   . ASP   B 1 10 ? 22.149  -9.985  -39.348 1.00 23.11  ? 9   ASP   B C   1 
ATOM   810  O  O   . ASP   B 1 10 ? 22.385  -10.059 -38.141 1.00 25.81  ? 9   ASP   B O   1 
ATOM   811  C  CB  . ASP   B 1 10 ? 24.028  -10.988 -40.669 1.00 26.90  ? 9   ASP   B CB  1 
ATOM   812  C  CG  . ASP   B 1 10 ? 24.739  -10.930 -42.008 1.00 39.47  ? 9   ASP   B CG  1 
ATOM   813  O  OD1 . ASP   B 1 10 ? 24.389  -10.059 -42.830 1.00 41.77  ? 9   ASP   B OD1 1 
ATOM   814  O  OD2 . ASP   B 1 10 ? 25.636  -11.767 -42.245 1.00 38.11  ? 9   ASP   B OD2 1 
ATOM   815  N  N   . LEU   B 1 11 ? 20.932  -10.125 -39.854 1.00 25.23  ? 10  LEU   B N   1 
ATOM   816  C  CA  . LEU   B 1 11 ? 19.759  -10.362 -39.026 1.00 24.28  ? 10  LEU   B CA  1 
ATOM   817  C  C   . LEU   B 1 11 ? 19.408  -11.842 -39.065 1.00 24.55  ? 10  LEU   B C   1 
ATOM   818  O  O   . LEU   B 1 11 ? 19.332  -12.441 -40.145 1.00 24.39  ? 10  LEU   B O   1 
ATOM   819  C  CB  . LEU   B 1 11 ? 18.583  -9.514  -39.505 1.00 25.37  ? 10  LEU   B CB  1 
ATOM   820  C  CG  . LEU   B 1 11 ? 18.910  -8.018  -39.545 1.00 29.04  ? 10  LEU   B CG  1 
ATOM   821  C  CD1 . LEU   B 1 11 ? 17.702  -7.204  -39.975 1.00 27.07  ? 10  LEU   B CD1 1 
ATOM   822  C  CD2 . LEU   B 1 11 ? 19.431  -7.555  -38.192 1.00 25.37  ? 10  LEU   B CD2 1 
ATOM   823  N  N   . VAL   B 1 12 ? 19.191  -12.428 -37.888 1.00 22.02  ? 11  VAL   B N   1 
ATOM   824  C  CA  . VAL   B 1 12 ? 19.026  -13.872 -37.761 1.00 22.84  ? 11  VAL   B CA  1 
ATOM   825  C  C   . VAL   B 1 12 ? 17.953  -14.185 -36.729 1.00 26.52  ? 11  VAL   B C   1 
ATOM   826  O  O   . VAL   B 1 12 ? 17.492  -13.322 -35.983 1.00 25.38  ? 11  VAL   B O   1 
ATOM   827  C  CB  . VAL   B 1 12 ? 20.340  -14.577 -37.360 1.00 21.80  ? 11  VAL   B CB  1 
ATOM   828  C  CG1 . VAL   B 1 12 ? 21.412  -14.383 -38.429 1.00 24.79  ? 11  VAL   B CG1 1 
ATOM   829  C  CG2 . VAL   B 1 12 ? 20.814  -14.088 -35.988 1.00 24.27  ? 11  VAL   B CG2 1 
ATOM   830  N  N   . PHE   B 1 13 ? 17.554  -15.449 -36.702 1.00 22.22  ? 12  PHE   B N   1 
ATOM   831  C  CA  . PHE   B 1 13 ? 16.971  -16.043 -35.511 1.00 21.54  ? 12  PHE   B CA  1 
ATOM   832  C  C   . PHE   B 1 13 ? 18.063  -16.874 -34.864 1.00 22.98  ? 12  PHE   B C   1 
ATOM   833  O  O   . PHE   B 1 13 ? 18.729  -17.657 -35.548 1.00 23.24  ? 12  PHE   B O   1 
ATOM   834  C  CB  . PHE   B 1 13 ? 15.752  -16.907 -35.840 1.00 23.62  ? 12  PHE   B CB  1 
ATOM   835  C  CG  . PHE   B 1 13 ? 14.540  -16.113 -36.238 1.00 23.95  ? 12  PHE   B CG  1 
ATOM   836  C  CD1 . PHE   B 1 13 ? 13.684  -15.603 -35.275 1.00 24.22  ? 12  PHE   B CD1 1 
ATOM   837  C  CD2 . PHE   B 1 13 ? 14.260  -15.875 -37.570 1.00 26.98  ? 12  PHE   B CD2 1 
ATOM   838  C  CE1 . PHE   B 1 13 ? 12.564  -14.866 -35.638 1.00 25.02  ? 12  PHE   B CE1 1 
ATOM   839  C  CE2 . PHE   B 1 13 ? 13.145  -15.138 -37.940 1.00 30.32  ? 12  PHE   B CE2 1 
ATOM   840  C  CZ  . PHE   B 1 13 ? 12.296  -14.635 -36.974 1.00 28.39  ? 12  PHE   B CZ  1 
ATOM   841  N  N   . ALA   B 1 14 ? 18.279  -16.669 -33.567 1.00 22.40  ? 13  ALA   B N   1 
ATOM   842  C  CA  . ALA   B 1 14 ? 19.308  -17.377 -32.821 1.00 24.31  ? 13  ALA   B CA  1 
ATOM   843  C  C   . ALA   B 1 14 ? 18.635  -18.362 -31.878 1.00 25.07  ? 13  ALA   B C   1 
ATOM   844  O  O   . ALA   B 1 14 ? 17.679  -18.002 -31.184 1.00 24.21  ? 13  ALA   B O   1 
ATOM   845  C  CB  . ALA   B 1 14 ? 20.192  -16.405 -32.037 1.00 23.47  ? 13  ALA   B CB  1 
ATOM   846  N  N   . LYS   B 1 15 ? 19.116  -19.600 -31.871 1.00 23.79  ? 14  LYS   B N   1 
ATOM   847  C  CA  . LYS   B 1 15 ? 18.501  -20.667 -31.092 1.00 25.23  ? 14  LYS   B CA  1 
ATOM   848  C  C   . LYS   B 1 15 ? 19.380  -21.021 -29.903 1.00 28.74  ? 14  LYS   B C   1 
ATOM   849  O  O   . LYS   B 1 15 ? 20.559  -21.349 -30.072 1.00 32.13  ? 14  LYS   B O   1 
ATOM   850  C  CB  . LYS   B 1 15 ? 18.266  -21.908 -31.951 1.00 25.04  ? 14  LYS   B CB  1 
ATOM   851  C  CG  . LYS   B 1 15 ? 17.515  -23.022 -31.221 1.00 28.87  ? 14  LYS   B CG  1 
ATOM   852  C  CD  . LYS   B 1 15 ? 16.090  -22.595 -30.896 1.00 26.79  ? 14  LYS   B CD  1 
ATOM   853  C  CE  . LYS   B 1 15 ? 15.295  -23.739 -30.267 1.00 30.18  ? 14  LYS   B CE  1 
ATOM   854  N  NZ  . LYS   B 1 15 ? 15.801  -24.056 -28.901 1.00 25.68  ? 14  LYS   B NZ  1 
ATOM   855  N  N   . MET   B 1 16 ? 18.798  -20.960 -28.707 1.00 32.11  ? 15  MET   B N   1 
ATOM   856  C  CA  . MET   B 1 16 ? 19.438  -21.410 -27.483 1.00 29.94  ? 15  MET   B CA  1 
ATOM   857  C  C   . MET   B 1 16 ? 18.547  -22.446 -26.811 1.00 33.41  ? 15  MET   B C   1 
ATOM   858  O  O   . MET   B 1 16 ? 17.317  -22.372 -26.902 1.00 30.96  ? 15  MET   B O   1 
ATOM   859  C  CB  . MET   B 1 16 ? 19.704  -20.241 -26.532 1.00 35.51  ? 15  MET   B CB  1 
ATOM   860  C  CG  . MET   B 1 16 ? 20.589  -19.166 -27.130 1.00 38.16  ? 15  MET   B CG  1 
ATOM   861  S  SD  . MET   B 1 16 ? 21.424  -18.211 -25.866 1.00 46.87  ? 15  MET   B SD  1 
ATOM   862  C  CE  . MET   B 1 16 ? 22.032  -19.526 -24.809 1.00 46.89  ? 15  MET   B CE  1 
ATOM   863  N  N   . LYS   B 1 17 ? 19.172  -23.423 -26.161 1.00 36.71  ? 16  LYS   B N   1 
ATOM   864  C  CA  . LYS   B 1 17 ? 18.410  -24.475 -25.499 1.00 40.92  ? 16  LYS   B CA  1 
ATOM   865  C  C   . LYS   B 1 17 ? 17.483  -23.864 -24.457 1.00 26.55  ? 16  LYS   B C   1 
ATOM   866  O  O   . LYS   B 1 17 ? 17.898  -23.020 -23.660 1.00 29.66  ? 16  LYS   B O   1 
ATOM   867  C  CB  . LYS   B 1 17 ? 19.357  -25.483 -24.850 1.00 44.04  ? 16  LYS   B CB  1 
ATOM   868  C  CG  . LYS   B 1 17 ? 18.929  -26.934 -25.000 1.00 62.15  ? 16  LYS   B CG  1 
ATOM   869  C  CD  . LYS   B 1 17 ? 20.096  -27.868 -24.720 1.00 59.93  ? 16  LYS   B CD  1 
ATOM   870  C  CE  . LYS   B 1 17 ? 21.321  -27.476 -25.543 1.00 74.29  ? 16  LYS   B CE  1 
ATOM   871  N  NZ  . LYS   B 1 17 ? 21.106  -27.653 -27.009 1.00 70.72  ? 16  LYS   B NZ  1 
ATOM   872  N  N   . GLY   B 1 18 ? 16.212  -24.273 -24.488 1.00 35.91  ? 17  GLY   B N   1 
ATOM   873  C  CA  . GLY   B 1 18 ? 15.217  -23.751 -23.577 1.00 39.86  ? 17  GLY   B CA  1 
ATOM   874  C  C   . GLY   B 1 18 ? 14.455  -22.539 -24.070 1.00 38.12  ? 17  GLY   B C   1 
ATOM   875  O  O   . GLY   B 1 18 ? 13.511  -22.109 -23.395 1.00 34.96  ? 17  GLY   B O   1 
ATOM   876  N  N   . TYR   B 1 19 ? 14.826  -21.980 -25.220 1.00 31.83  ? 18  TYR   B N   1 
ATOM   877  C  CA  . TYR   B 1 19 ? 14.195  -20.793 -25.772 1.00 28.45  ? 18  TYR   B CA  1 
ATOM   878  C  C   . TYR   B 1 19 ? 13.796  -21.036 -27.219 1.00 28.33  ? 18  TYR   B C   1 
ATOM   879  O  O   . TYR   B 1 19 ? 14.458  -21.801 -27.928 1.00 29.30  ? 18  TYR   B O   1 
ATOM   880  C  CB  . TYR   B 1 19 ? 15.142  -19.584 -25.719 1.00 31.63  ? 18  TYR   B CB  1 
ATOM   881  C  CG  . TYR   B 1 19 ? 15.669  -19.259 -24.341 1.00 32.19  ? 18  TYR   B CG  1 
ATOM   882  C  CD1 . TYR   B 1 19 ? 14.969  -18.415 -23.494 1.00 30.23  ? 18  TYR   B CD1 1 
ATOM   883  C  CD2 . TYR   B 1 19 ? 16.871  -19.790 -23.895 1.00 36.45  ? 18  TYR   B CD2 1 
ATOM   884  C  CE1 . TYR   B 1 19 ? 15.450  -18.110 -22.233 1.00 32.08  ? 18  TYR   B CE1 1 
ATOM   885  C  CE2 . TYR   B 1 19 ? 17.360  -19.492 -22.638 1.00 43.76  ? 18  TYR   B CE2 1 
ATOM   886  C  CZ  . TYR   B 1 19 ? 16.645  -18.652 -21.811 1.00 38.68  ? 18  TYR   B CZ  1 
ATOM   887  O  OH  . TYR   B 1 19 ? 17.124  -18.350 -20.558 1.00 41.83  ? 18  TYR   B OH  1 
ATOM   888  N  N   . PRO   B 1 20 ? 12.727  -20.398 -27.689 1.00 25.49  ? 19  PRO   B N   1 
ATOM   889  C  CA  . PRO   B 1 20 ? 12.409  -20.468 -29.115 1.00 23.48  ? 19  PRO   B CA  1 
ATOM   890  C  C   . PRO   B 1 20 ? 13.435  -19.691 -29.919 1.00 26.71  ? 19  PRO   B C   1 
ATOM   891  O  O   . PRO   B 1 20 ? 14.141  -18.827 -29.392 1.00 26.17  ? 19  PRO   B O   1 
ATOM   892  C  CB  . PRO   B 1 20 ? 11.030  -19.815 -29.209 1.00 25.27  ? 19  PRO   B CB  1 
ATOM   893  C  CG  . PRO   B 1 20 ? 11.012  -18.837 -28.054 1.00 29.45  ? 19  PRO   B CG  1 
ATOM   894  C  CD  . PRO   B 1 20 ? 11.799  -19.518 -26.953 1.00 31.29  ? 19  PRO   B CD  1 
ATOM   895  N  N   . HIS   B 1 21 ? 13.513  -20.022 -31.211 1.00 26.89  ? 20  HIS   B N   1 
ATOM   896  C  CA  . HIS   B 1 21 ? 14.333  -19.251 -32.139 1.00 26.26  ? 20  HIS   B CA  1 
ATOM   897  C  C   . HIS   B 1 21 ? 14.032  -17.768 -31.970 1.00 19.13  ? 20  HIS   B C   1 
ATOM   898  O  O   . HIS   B 1 21 ? 12.875  -17.346 -32.037 1.00 22.44  ? 20  HIS   B O   1 
ATOM   899  C  CB  . HIS   B 1 21 ? 14.068  -19.696 -33.581 1.00 23.99  ? 20  HIS   B CB  1 
ATOM   900  C  CG  . HIS   B 1 21 ? 14.307  -21.157 -33.816 1.00 25.96  ? 20  HIS   B CG  1 
ATOM   901  N  ND1 . HIS   B 1 21 ? 13.409  -22.129 -33.425 1.00 28.48  ? 20  HIS   B ND1 1 
ATOM   902  C  CD2 . HIS   B 1 21 ? 15.338  -21.812 -34.402 1.00 28.16  ? 20  HIS   B CD2 1 
ATOM   903  C  CE1 . HIS   B 1 21 ? 13.880  -23.319 -33.757 1.00 31.32  ? 20  HIS   B CE1 1 
ATOM   904  N  NE2 . HIS   B 1 21 ? 15.049  -23.156 -34.348 1.00 29.44  ? 20  HIS   B NE2 1 
ATOM   905  N  N   . TRP   B 1 22 ? 15.080  -16.981 -31.740 1.00 23.15  ? 21  TRP   B N   1 
ATOM   906  C  CA  . TRP   B 1 22 ? 14.910  -15.649 -31.181 1.00 22.76  ? 21  TRP   B CA  1 
ATOM   907  C  C   . TRP   B 1 22 ? 15.448  -14.587 -32.128 1.00 23.19  ? 21  TRP   B C   1 
ATOM   908  O  O   . TRP   B 1 22 ? 16.584  -14.715 -32.602 1.00 22.94  ? 21  TRP   B O   1 
ATOM   909  C  CB  . TRP   B 1 22 ? 15.629  -15.545 -29.832 1.00 26.48  ? 21  TRP   B CB  1 
ATOM   910  C  CG  . TRP   B 1 22 ? 15.093  -14.442 -28.978 1.00 24.84  ? 21  TRP   B CG  1 
ATOM   911  C  CD1 . TRP   B 1 22 ? 15.368  -13.101 -29.083 1.00 28.74  ? 21  TRP   B CD1 1 
ATOM   912  C  CD2 . TRP   B 1 22 ? 14.174  -14.579 -27.893 1.00 22.28  ? 21  TRP   B CD2 1 
ATOM   913  N  NE1 . TRP   B 1 22 ? 14.673  -12.403 -28.123 1.00 24.60  ? 21  TRP   B NE1 1 
ATOM   914  C  CE2 . TRP   B 1 22 ? 13.935  -13.289 -27.379 1.00 23.20  ? 21  TRP   B CE2 1 
ATOM   915  C  CE3 . TRP   B 1 22 ? 13.529  -15.671 -27.304 1.00 30.03  ? 21  TRP   B CE3 1 
ATOM   916  C  CZ2 . TRP   B 1 22 ? 13.079  -13.062 -26.304 1.00 26.39  ? 21  TRP   B CZ2 1 
ATOM   917  C  CZ3 . TRP   B 1 22 ? 12.684  -15.444 -26.237 1.00 28.55  ? 21  TRP   B CZ3 1 
ATOM   918  C  CH2 . TRP   B 1 22 ? 12.464  -14.151 -25.748 1.00 28.74  ? 21  TRP   B CH2 1 
ATOM   919  N  N   . PRO   B 1 23 ? 14.688  -13.526 -32.405 1.00 22.68  ? 22  PRO   B N   1 
ATOM   920  C  CA  . PRO   B 1 23 ? 15.186  -12.468 -33.299 1.00 20.28  ? 22  PRO   B CA  1 
ATOM   921  C  C   . PRO   B 1 23 ? 16.461  -11.847 -32.750 1.00 24.06  ? 22  PRO   B C   1 
ATOM   922  O  O   . PRO   B 1 23 ? 16.536  -11.468 -31.579 1.00 25.21  ? 22  PRO   B O   1 
ATOM   923  C  CB  . PRO   B 1 23 ? 14.029  -11.460 -33.337 1.00 21.25  ? 22  PRO   B CB  1 
ATOM   924  C  CG  . PRO   B 1 23 ? 13.260  -11.710 -32.043 1.00 27.68  ? 22  PRO   B CG  1 
ATOM   925  C  CD  . PRO   B 1 23 ? 13.354  -13.209 -31.864 1.00 22.24  ? 22  PRO   B CD  1 
ATOM   926  N  N   . ALA   B 1 24 ? 17.472  -11.743 -33.608 1.00 21.96  ? 23  ALA   B N   1 
ATOM   927  C  CA  . ALA   B 1 24 ? 18.791  -11.350 -33.138 1.00 21.31  ? 23  ALA   B CA  1 
ATOM   928  C  C   . ALA   B 1 24 ? 19.594  -10.785 -34.302 1.00 19.66  ? 23  ALA   B C   1 
ATOM   929  O  O   . ALA   B 1 24 ? 19.143  -10.765 -35.450 1.00 22.67  ? 23  ALA   B O   1 
ATOM   930  C  CB  . ALA   B 1 24 ? 19.519  -12.530 -32.483 1.00 23.86  ? 23  ALA   B CB  1 
ATOM   931  N  N   . ARG   B 1 25 ? 20.790  -10.305 -33.979 1.00 25.09  ? 24  ARG   B N   1 
ATOM   932  C  CA  . ARG   B 1 25 ? 21.697  -9.788  -34.989 1.00 23.87  ? 24  ARG   B CA  1 
ATOM   933  C  C   . ARG   B 1 25 ? 23.113  -10.232 -34.662 1.00 21.70  ? 24  ARG   B C   1 
ATOM   934  O  O   . ARG   B 1 25 ? 23.453  -10.493 -33.504 1.00 27.02  ? 24  ARG   B O   1 
ATOM   935  C  CB  . ARG   B 1 25 ? 21.636  -8.254  -35.083 1.00 22.65  ? 24  ARG   B CB  1 
ATOM   936  C  CG  . ARG   B 1 25 ? 22.286  -7.553  -33.906 1.00 22.99  ? 24  ARG   B CG  1 
ATOM   937  C  CD  . ARG   B 1 25 ? 22.033  -6.049  -33.942 1.00 23.48  ? 24  ARG   B CD  1 
ATOM   938  N  NE  . ARG   B 1 25 ? 22.727  -5.367  -32.859 1.00 27.46  ? 24  ARG   B NE  1 
ATOM   939  C  CZ  . ARG   B 1 25 ? 22.451  -4.135  -32.453 1.00 29.56  ? 24  ARG   B CZ  1 
ATOM   940  N  NH1 . ARG   B 1 25 ? 21.476  -3.431  -33.001 1.00 30.27  ? 24  ARG   B NH1 1 
ATOM   941  N  NH2 . ARG   B 1 25 ? 23.172  -3.598  -31.474 1.00 29.66  ? 24  ARG   B NH2 1 
ATOM   942  N  N   . ILE   B 1 26 ? 23.930  -10.338 -35.705 1.00 26.83  ? 25  ILE   B N   1 
ATOM   943  C  CA  . ILE   B 1 26 ? 25.363  -10.537 -35.540 1.00 22.91  ? 25  ILE   B CA  1 
ATOM   944  C  C   . ILE   B 1 26 ? 25.962  -9.197  -35.146 1.00 33.32  ? 25  ILE   B C   1 
ATOM   945  O  O   . ILE   B 1 26 ? 25.814  -8.209  -35.871 1.00 30.28  ? 25  ILE   B O   1 
ATOM   946  C  CB  . ILE   B 1 26 ? 26.008  -11.059 -36.832 1.00 28.82  ? 25  ILE   B CB  1 
ATOM   947  C  CG1 . ILE   B 1 26 ? 25.237  -12.258 -37.384 1.00 32.69  ? 25  ILE   B CG1 1 
ATOM   948  C  CG2 . ILE   B 1 26 ? 27.477  -11.394 -36.590 1.00 31.56  ? 25  ILE   B CG2 1 
ATOM   949  C  CD1 . ILE   B 1 26 ? 25.291  -13.482 -36.506 1.00 32.28  ? 25  ILE   B CD1 1 
ATOM   950  N  N   . ASP   B 1 27 ? 26.629  -9.157  -34.001 1.00 29.30  ? 26  ASP   B N   1 
ATOM   951  C  CA  . ASP   B 1 27 ? 27.282  -7.935  -33.567 1.00 32.56  ? 26  ASP   B CA  1 
ATOM   952  C  C   . ASP   B 1 27 ? 28.706  -7.878  -34.102 1.00 35.34  ? 26  ASP   B C   1 
ATOM   953  O  O   . ASP   B 1 27 ? 29.283  -8.881  -34.529 1.00 38.48  ? 26  ASP   B O   1 
ATOM   954  C  CB  . ASP   B 1 27 ? 27.297  -7.826  -32.041 1.00 36.75  ? 26  ASP   B CB  1 
ATOM   955  C  CG  . ASP   B 1 27 ? 26.126  -7.031  -31.501 1.00 35.26  ? 26  ASP   B CG  1 
ATOM   956  O  OD1 . ASP   B 1 27 ? 25.350  -6.487  -32.318 1.00 35.79  ? 26  ASP   B OD1 1 
ATOM   957  O  OD2 . ASP   B 1 27 ? 25.983  -6.947  -30.260 1.00 35.65  ? 26  ASP   B OD2 1 
ATOM   958  N  N   . ASP   B 1 28 ? 29.267  -6.676  -34.088 1.00 42.09  ? 27  ASP   B N   1 
ATOM   959  C  CA  . ASP   B 1 28 ? 30.680  -6.544  -34.378 1.00 47.33  ? 27  ASP   B CA  1 
ATOM   960  C  C   . ASP   B 1 28 ? 31.488  -6.797  -33.111 1.00 53.25  ? 27  ASP   B C   1 
ATOM   961  O  O   . ASP   B 1 28 ? 30.994  -6.665  -31.987 1.00 51.67  ? 27  ASP   B O   1 
ATOM   962  C  CB  . ASP   B 1 28 ? 30.997  -5.159  -34.942 1.00 57.90  ? 27  ASP   B CB  1 
ATOM   963  C  CG  . ASP   B 1 28 ? 32.294  -5.134  -35.732 1.00 59.95  ? 27  ASP   B CG  1 
ATOM   964  O  OD1 . ASP   B 1 28 ? 33.296  -5.721  -35.271 1.00 69.76  ? 27  ASP   B OD1 1 
ATOM   965  O  OD2 . ASP   B 1 28 ? 32.308  -4.536  -36.826 1.00 57.23  ? 27  ASP   B OD2 1 
ATOM   966  N  N   . ILE   B 1 29 ? 32.743  -7.186  -33.306 1.00 57.25  ? 28  ILE   B N   1 
ATOM   967  C  CA  . ILE   B 1 29 ? 33.686  -7.340  -32.208 1.00 59.57  ? 28  ILE   B CA  1 
ATOM   968  C  C   . ILE   B 1 29 ? 34.306  -5.966  -31.983 1.00 72.11  ? 28  ILE   B C   1 
ATOM   969  O  O   . ILE   B 1 29 ? 35.136  -5.510  -32.772 1.00 76.86  ? 28  ILE   B O   1 
ATOM   970  C  CB  . ILE   B 1 29 ? 34.741  -8.403  -32.508 1.00 61.64  ? 28  ILE   B CB  1 
ATOM   971  C  CG1 . ILE   B 1 29 ? 34.068  -9.738  -32.831 1.00 64.86  ? 28  ILE   B CG1 1 
ATOM   972  C  CG2 . ILE   B 1 29 ? 35.693  -8.551  -31.330 1.00 71.00  ? 28  ILE   B CG2 1 
ATOM   973  C  CD1 . ILE   B 1 29 ? 35.015  -10.784 -33.364 1.00 71.08  ? 28  ILE   B CD1 1 
ATOM   974  N  N   . ALA   B 1 30 ? 33.878  -5.292  -30.917 1.00 69.65  ? 29  ALA   B N   1 
ATOM   975  C  CA  . ALA   B 1 30 ? 34.420  -3.979  -30.600 1.00 76.76  ? 29  ALA   B CA  1 
ATOM   976  C  C   . ALA   B 1 30 ? 35.932  -4.063  -30.444 1.00 77.98  ? 29  ALA   B C   1 
ATOM   977  O  O   . ALA   B 1 30 ? 36.463  -5.036  -29.903 1.00 79.19  ? 29  ALA   B O   1 
ATOM   978  C  CB  . ALA   B 1 30 ? 33.782  -3.431  -29.323 1.00 64.88  ? 29  ALA   B CB  1 
ATOM   979  N  N   . ASP   B 1 31 ? 36.627  -3.047  -30.950 1.00 81.33  ? 30  ASP   B N   1 
ATOM   980  C  CA  . ASP   B 1 31 ? 38.082  -3.044  -30.896 1.00 77.69  ? 30  ASP   B CA  1 
ATOM   981  C  C   . ASP   B 1 31 ? 38.560  -3.057  -29.450 1.00 74.44  ? 30  ASP   B C   1 
ATOM   982  O  O   . ASP   B 1 31 ? 38.124  -2.245  -28.629 1.00 68.12  ? 30  ASP   B O   1 
ATOM   983  C  CB  . ASP   B 1 31 ? 38.635  -1.830  -31.639 1.00 75.70  ? 30  ASP   B CB  1 
ATOM   984  C  CG  . ASP   B 1 31 ? 38.779  -2.079  -33.129 1.00 83.61  ? 30  ASP   B CG  1 
ATOM   985  O  OD1 . ASP   B 1 31 ? 39.581  -2.958  -33.509 1.00 85.90  ? 30  ASP   B OD1 1 
ATOM   986  O  OD2 . ASP   B 1 31 ? 38.078  -1.412  -33.918 1.00 80.14  ? 30  ASP   B OD2 1 
ATOM   987  N  N   . GLY   B 1 32 ? 39.446  -4.000  -29.139 1.00 78.68  ? 31  GLY   B N   1 
ATOM   988  C  CA  . GLY   B 1 32 ? 39.946  -4.166  -27.792 1.00 74.46  ? 31  GLY   B CA  1 
ATOM   989  C  C   . GLY   B 1 32 ? 39.088  -5.020  -26.888 1.00 74.64  ? 31  GLY   B C   1 
ATOM   990  O  O   . GLY   B 1 32 ? 39.383  -5.112  -25.690 1.00 71.85  ? 31  GLY   B O   1 
ATOM   991  N  N   . ALA   B 1 33 ? 38.047  -5.656  -27.415 1.00 78.61  ? 32  ALA   B N   1 
ATOM   992  C  CA  . ALA   B 1 33 ? 37.110  -6.422  -26.608 1.00 75.83  ? 32  ALA   B CA  1 
ATOM   993  C  C   . ALA   B 1 33 ? 37.418  -7.915  -26.673 1.00 81.40  ? 32  ALA   B C   1 
ATOM   994  O  O   . ALA   B 1 33 ? 38.256  -8.378  -27.451 1.00 74.26  ? 32  ALA   B O   1 
ATOM   995  C  CB  . ALA   B 1 33 ? 35.670  -6.157  -27.057 1.00 68.73  ? 32  ALA   B CB  1 
ATOM   996  N  N   . VAL   B 1 34 ? 36.710  -8.670  -25.827 1.00 84.90  ? 33  VAL   B N   1 
ATOM   997  C  CA  . VAL   B 1 34 ? 36.894  -10.114 -25.765 1.00 79.83  ? 33  VAL   B CA  1 
ATOM   998  C  C   . VAL   B 1 34 ? 36.506  -10.742 -27.094 1.00 75.53  ? 33  VAL   B C   1 
ATOM   999  O  O   . VAL   B 1 34 ? 35.495  -10.378 -27.708 1.00 78.27  ? 33  VAL   B O   1 
ATOM   1000 C  CB  . VAL   B 1 34 ? 36.068  -10.705 -24.609 1.00 80.34  ? 33  VAL   B CB  1 
ATOM   1001 C  CG1 . VAL   B 1 34 ? 36.156  -12.226 -24.602 1.00 76.47  ? 33  VAL   B CG1 1 
ATOM   1002 C  CG2 . VAL   B 1 34 ? 36.535  -10.135 -23.281 1.00 75.80  ? 33  VAL   B CG2 1 
ATOM   1003 N  N   . LYS   B 1 35 ? 37.323  -11.691 -27.553 1.00 77.13  ? 34  LYS   B N   1 
ATOM   1004 C  CA  . LYS   B 1 35 ? 36.944  -12.342 -28.796 1.00 71.11  ? 34  LYS   B CA  1 
ATOM   1005 C  C   . LYS   B 1 35 ? 36.061  -13.552 -28.516 1.00 61.91  ? 34  LYS   B C   1 
ATOM   1006 O  O   . LYS   B 1 35 ? 36.193  -14.197 -27.471 1.00 62.42  ? 34  LYS   B O   1 
ATOM   1007 C  CB  . LYS   B 1 35 ? 38.181  -12.794 -29.563 1.00 65.32  ? 34  LYS   B CB  1 
ATOM   1008 C  CG  . LYS   B 1 35 ? 39.348  -11.833 -29.502 1.00 77.34  ? 34  LYS   B CG  1 
ATOM   1009 C  CD  . LYS   B 1 35 ? 40.660  -12.593 -29.601 1.00 82.70  ? 34  LYS   B CD  1 
ATOM   1010 C  CE  . LYS   B 1 35 ? 41.832  -11.729 -29.182 1.00 79.00  ? 34  LYS   B CE  1 
ATOM   1011 N  NZ  . LYS   B 1 35 ? 42.982  -12.568 -28.749 1.00 70.86  ? 34  LYS   B NZ  1 
ATOM   1012 N  N   . PRO   B 1 36 ? 35.161  -13.880 -29.436 1.00 66.95  ? 35  PRO   B N   1 
ATOM   1013 C  CA  . PRO   B 1 36 ? 34.358  -15.096 -29.290 1.00 53.84  ? 35  PRO   B CA  1 
ATOM   1014 C  C   . PRO   B 1 36 ? 35.232  -16.333 -29.379 1.00 50.62  ? 35  PRO   B C   1 
ATOM   1015 O  O   . PRO   B 1 36 ? 36.327  -16.291 -29.961 1.00 53.19  ? 35  PRO   B O   1 
ATOM   1016 C  CB  . PRO   B 1 36 ? 33.384  -15.020 -30.475 1.00 48.88  ? 35  PRO   B CB  1 
ATOM   1017 C  CG  . PRO   B 1 36 ? 34.047  -14.108 -31.460 1.00 61.39  ? 35  PRO   B CG  1 
ATOM   1018 C  CD  . PRO   B 1 36 ? 34.789  -13.108 -30.633 1.00 56.05  ? 35  PRO   B CD  1 
ATOM   1019 N  N   . PRO   B 1 37 ? 34.788  -17.452 -28.814 1.00 49.53  ? 36  PRO   B N   1 
ATOM   1020 C  CA  . PRO   B 1 37 ? 35.492  -18.718 -29.024 1.00 48.91  ? 36  PRO   B CA  1 
ATOM   1021 C  C   . PRO   B 1 37 ? 35.542  -19.049 -30.503 1.00 56.23  ? 36  PRO   B C   1 
ATOM   1022 O  O   . PRO   B 1 37 ? 34.734  -18.526 -31.286 1.00 52.06  ? 36  PRO   B O   1 
ATOM   1023 C  CB  . PRO   B 1 37 ? 34.636  -19.733 -28.249 1.00 50.65  ? 36  PRO   B CB  1 
ATOM   1024 C  CG  . PRO   B 1 37 ? 33.877  -18.913 -27.252 1.00 44.62  ? 36  PRO   B CG  1 
ATOM   1025 C  CD  . PRO   B 1 37 ? 33.620  -17.603 -27.929 1.00 55.54  ? 36  PRO   B CD  1 
ATOM   1026 N  N   . PRO   B 1 38 ? 36.477  -19.897 -30.932 1.00 52.62  ? 37  PRO   B N   1 
ATOM   1027 C  CA  . PRO   B 1 38 ? 36.562  -20.221 -32.360 1.00 58.70  ? 37  PRO   B CA  1 
ATOM   1028 C  C   . PRO   B 1 38 ? 35.256  -20.815 -32.863 1.00 51.98  ? 37  PRO   B C   1 
ATOM   1029 O  O   . PRO   B 1 38 ? 34.562  -21.533 -32.138 1.00 49.05  ? 37  PRO   B O   1 
ATOM   1030 C  CB  . PRO   B 1 38 ? 37.712  -21.233 -32.430 1.00 62.14  ? 37  PRO   B CB  1 
ATOM   1031 C  CG  . PRO   B 1 38 ? 37.812  -21.795 -31.050 1.00 57.14  ? 37  PRO   B CG  1 
ATOM   1032 C  CD  . PRO   B 1 38 ? 37.450  -20.664 -30.135 1.00 60.39  ? 37  PRO   B CD  1 
ATOM   1033 N  N   . ASN   B 1 39 ? 34.913  -20.473 -34.104 1.00 51.61  ? 38  ASN   B N   1 
ATOM   1034 C  CA  . ASN   B 1 39 ? 33.736  -20.909 -34.854 1.00 48.90  ? 38  ASN   B CA  1 
ATOM   1035 C  C   . ASN   B 1 39 ? 32.467  -20.165 -34.439 1.00 50.86  ? 38  ASN   B C   1 
ATOM   1036 O  O   . ASN   B 1 39 ? 31.404  -20.446 -35.003 1.00 45.37  ? 38  ASN   B O   1 
ATOM   1037 C  CB  . ASN   B 1 39 ? 33.482  -22.423 -34.732 1.00 56.83  ? 38  ASN   B CB  1 
ATOM   1038 C  CG  . ASN   B 1 39 ? 32.850  -23.014 -35.973 1.00 69.70  ? 38  ASN   B CG  1 
ATOM   1039 O  OD1 . ASN   B 1 39 ? 32.368  -22.293 -36.842 1.00 64.86  ? 38  ASN   B OD1 1 
ATOM   1040 N  ND2 . ASN   B 1 39 ? 32.848  -24.340 -36.060 1.00 74.43  ? 38  ASN   B ND2 1 
ATOM   1041 N  N   . LYS   B 1 40 ? 32.531  -19.225 -33.497 1.00 45.20  ? 39  LYS   B N   1 
ATOM   1042 C  CA  . LYS   B 1 40 ? 31.334  -18.609 -32.944 1.00 41.91  ? 39  LYS   B CA  1 
ATOM   1043 C  C   . LYS   B 1 40 ? 31.323  -17.104 -33.192 1.00 38.63  ? 39  LYS   B C   1 
ATOM   1044 O  O   . LYS   B 1 40 ? 32.350  -16.492 -33.500 1.00 41.72  ? 39  LYS   B O   1 
ATOM   1045 C  CB  . LYS   B 1 40 ? 31.215  -18.908 -31.444 1.00 43.14  ? 39  LYS   B CB  1 
ATOM   1046 C  CG  . LYS   B 1 40 ? 30.958  -20.384 -31.160 1.00 39.14  ? 39  LYS   B CG  1 
ATOM   1047 C  CD  . LYS   B 1 40 ? 31.271  -20.760 -29.724 1.00 51.42  ? 39  LYS   B CD  1 
ATOM   1048 C  CE  . LYS   B 1 40 ? 31.096  -22.256 -29.498 1.00 53.60  ? 39  LYS   B CE  1 
ATOM   1049 N  NZ  . LYS   B 1 40 ? 29.674  -22.682 -29.612 1.00 54.77  ? 39  LYS   B NZ  1 
ATOM   1050 N  N   . TYR   B 1 41 ? 30.136  -16.519 -33.058 1.00 33.07  ? 40  TYR   B N   1 
ATOM   1051 C  CA  . TYR   B 1 41 ? 29.864  -15.121 -33.349 1.00 30.25  ? 40  TYR   B CA  1 
ATOM   1052 C  C   . TYR   B 1 41 ? 29.237  -14.446 -32.141 1.00 36.27  ? 40  TYR   B C   1 
ATOM   1053 O  O   . TYR   B 1 41 ? 28.504  -15.084 -31.378 1.00 30.17  ? 40  TYR   B O   1 
ATOM   1054 C  CB  . TYR   B 1 41 ? 28.905  -14.972 -34.539 1.00 31.16  ? 40  TYR   B CB  1 
ATOM   1055 C  CG  . TYR   B 1 41 ? 29.441  -15.462 -35.857 1.00 35.86  ? 40  TYR   B CG  1 
ATOM   1056 C  CD1 . TYR   B 1 41 ? 29.222  -16.763 -36.274 1.00 32.73  ? 40  TYR   B CD1 1 
ATOM   1057 C  CD2 . TYR   B 1 41 ? 30.148  -14.613 -36.698 1.00 34.56  ? 40  TYR   B CD2 1 
ATOM   1058 C  CE1 . TYR   B 1 41 ? 29.705  -17.214 -37.490 1.00 33.06  ? 40  TYR   B CE1 1 
ATOM   1059 C  CE2 . TYR   B 1 41 ? 30.635  -15.053 -37.910 1.00 39.56  ? 40  TYR   B CE2 1 
ATOM   1060 C  CZ  . TYR   B 1 41 ? 30.411  -16.354 -38.303 1.00 35.40  ? 40  TYR   B CZ  1 
ATOM   1061 O  OH  . TYR   B 1 41 ? 30.893  -16.798 -39.513 1.00 38.64  ? 40  TYR   B OH  1 
ATOM   1062 N  N   . PRO   B 1 42 ? 29.489  -13.149 -31.953 1.00 37.75  ? 41  PRO   B N   1 
ATOM   1063 C  CA  . PRO   B 1 42 ? 28.779  -12.403 -30.905 1.00 31.27  ? 41  PRO   B CA  1 
ATOM   1064 C  C   . PRO   B 1 42 ? 27.359  -12.097 -31.356 1.00 30.84  ? 41  PRO   B C   1 
ATOM   1065 O  O   . PRO   B 1 42 ? 27.146  -11.493 -32.412 1.00 27.66  ? 41  PRO   B O   1 
ATOM   1066 C  CB  . PRO   B 1 42 ? 29.618  -11.131 -30.745 1.00 31.24  ? 41  PRO   B CB  1 
ATOM   1067 C  CG  . PRO   B 1 42 ? 30.239  -10.930 -32.080 1.00 30.74  ? 41  PRO   B CG  1 
ATOM   1068 C  CD  . PRO   B 1 42 ? 30.434  -12.297 -32.699 1.00 34.38  ? 41  PRO   B CD  1 
ATOM   1069 N  N   . ILE   B 1 43 ? 26.385  -12.545 -30.566 1.00 29.48  ? 42  ILE   B N   1 
ATOM   1070 C  CA  . ILE   B 1 43 ? 24.970  -12.398 -30.887 1.00 24.40  ? 42  ILE   B CA  1 
ATOM   1071 C  C   . ILE   B 1 43 ? 24.355  -11.373 -29.943 1.00 28.91  ? 42  ILE   B C   1 
ATOM   1072 O  O   . ILE   B 1 43 ? 24.659  -11.356 -28.745 1.00 32.47  ? 42  ILE   B O   1 
ATOM   1073 C  CB  . ILE   B 1 43 ? 24.231  -13.748 -30.789 1.00 22.38  ? 42  ILE   B CB  1 
ATOM   1074 C  CG1 . ILE   B 1 43 ? 24.963  -14.822 -31.600 1.00 26.23  ? 42  ILE   B CG1 1 
ATOM   1075 C  CG2 . ILE   B 1 43 ? 22.793  -13.598 -31.250 1.00 28.43  ? 42  ILE   B CG2 1 
ATOM   1076 C  CD1 . ILE   B 1 43 ? 25.194  -14.464 -33.045 1.00 27.67  ? 42  ILE   B CD1 1 
ATOM   1077 N  N   . PHE   B 1 44 ? 23.505  -10.509 -30.489 1.00 25.85  ? 43  PHE   B N   1 
ATOM   1078 C  CA  . PHE   B 1 44 ? 22.694  -9.582  -29.709 1.00 27.98  ? 43  PHE   B CA  1 
ATOM   1079 C  C   . PHE   B 1 44 ? 21.236  -9.976  -29.891 1.00 26.07  ? 43  PHE   B C   1 
ATOM   1080 O  O   . PHE   B 1 44 ? 20.738  -10.017 -31.020 1.00 22.78  ? 43  PHE   B O   1 
ATOM   1081 C  CB  . PHE   B 1 44 ? 22.932  -8.135  -30.149 1.00 26.35  ? 43  PHE   B CB  1 
ATOM   1082 C  CG  . PHE   B 1 44 ? 22.011  -7.135  -29.500 1.00 26.25  ? 43  PHE   B CG  1 
ATOM   1083 C  CD1 . PHE   B 1 44 ? 22.339  -6.560  -28.282 1.00 30.63  ? 43  PHE   B CD1 1 
ATOM   1084 C  CD2 . PHE   B 1 44 ? 20.828  -6.760  -30.117 1.00 25.46  ? 43  PHE   B CD2 1 
ATOM   1085 C  CE1 . PHE   B 1 44 ? 21.499  -5.629  -27.681 1.00 28.30  ? 43  PHE   B CE1 1 
ATOM   1086 C  CE2 . PHE   B 1 44 ? 19.983  -5.831  -29.523 1.00 25.98  ? 43  PHE   B CE2 1 
ATOM   1087 C  CZ  . PHE   B 1 44 ? 20.322  -5.267  -28.304 1.00 25.60  ? 43  PHE   B CZ  1 
ATOM   1088 N  N   . PHE   B 1 45 ? 20.558  -10.278 -28.787 1.00 25.39  ? 44  PHE   B N   1 
ATOM   1089 C  CA  . PHE   B 1 45 ? 19.169  -10.716 -28.826 1.00 26.03  ? 44  PHE   B CA  1 
ATOM   1090 C  C   . PHE   B 1 45 ? 18.253  -9.507  -28.691 1.00 24.55  ? 44  PHE   B C   1 
ATOM   1091 O  O   . PHE   B 1 45 ? 18.332  -8.768  -27.703 1.00 26.52  ? 44  PHE   B O   1 
ATOM   1092 C  CB  . PHE   B 1 45 ? 18.896  -11.738 -27.720 1.00 26.83  ? 44  PHE   B CB  1 
ATOM   1093 C  CG  . PHE   B 1 45 ? 19.638  -13.036 -27.901 1.00 25.46  ? 44  PHE   B CG  1 
ATOM   1094 C  CD1 . PHE   B 1 45 ? 20.974  -13.145 -27.545 1.00 29.96  ? 44  PHE   B CD1 1 
ATOM   1095 C  CD2 . PHE   B 1 45 ? 19.000  -14.146 -28.431 1.00 29.81  ? 44  PHE   B CD2 1 
ATOM   1096 C  CE1 . PHE   B 1 45 ? 21.664  -14.336 -27.716 1.00 27.91  ? 44  PHE   B CE1 1 
ATOM   1097 C  CE2 . PHE   B 1 45 ? 19.680  -15.343 -28.605 1.00 27.22  ? 44  PHE   B CE2 1 
ATOM   1098 C  CZ  . PHE   B 1 45 ? 21.012  -15.439 -28.247 1.00 28.42  ? 44  PHE   B CZ  1 
ATOM   1099 N  N   . PHE   B 1 46 ? 17.383  -9.309  -29.675 1.00 23.09  ? 45  PHE   B N   1 
ATOM   1100 C  CA  . PHE   B 1 46 ? 16.456  -8.191  -29.620 1.00 24.49  ? 45  PHE   B CA  1 
ATOM   1101 C  C   . PHE   B 1 46 ? 15.420  -8.408  -28.520 1.00 29.73  ? 45  PHE   B C   1 
ATOM   1102 O  O   . PHE   B 1 46 ? 15.140  -9.536  -28.099 1.00 27.07  ? 45  PHE   B O   1 
ATOM   1103 C  CB  . PHE   B 1 46 ? 15.762  -7.998  -30.969 1.00 25.16  ? 45  PHE   B CB  1 
ATOM   1104 C  CG  . PHE   B 1 46 ? 16.673  -7.498  -32.054 1.00 24.57  ? 45  PHE   B CG  1 
ATOM   1105 C  CD1 . PHE   B 1 46 ? 17.178  -6.205  -32.014 1.00 23.84  ? 45  PHE   B CD1 1 
ATOM   1106 C  CD2 . PHE   B 1 46 ? 17.014  -8.314  -33.118 1.00 27.30  ? 45  PHE   B CD2 1 
ATOM   1107 C  CE1 . PHE   B 1 46 ? 18.018  -5.738  -33.018 1.00 25.07  ? 45  PHE   B CE1 1 
ATOM   1108 C  CE2 . PHE   B 1 46 ? 17.850  -7.858  -34.128 1.00 28.73  ? 45  PHE   B CE2 1 
ATOM   1109 C  CZ  . PHE   B 1 46 ? 18.352  -6.567  -34.082 1.00 24.83  ? 45  PHE   B CZ  1 
ATOM   1110 N  N   . GLY   B 1 47 ? 14.859  -7.301  -28.039 1.00 28.01  ? 46  GLY   B N   1 
ATOM   1111 C  CA  . GLY   B 1 47 ? 13.871  -7.362  -26.978 1.00 27.03  ? 46  GLY   B CA  1 
ATOM   1112 C  C   . GLY   B 1 47 ? 14.485  -7.510  -25.601 1.00 30.23  ? 46  GLY   B C   1 
ATOM   1113 O  O   . GLY   B 1 47 ? 14.287  -6.654  -24.733 1.00 34.35  ? 46  GLY   B O   1 
ATOM   1114 N  N   . THR   B 1 48 ? 15.230  -8.593  -25.385 1.00 28.33  ? 47  THR   B N   1 
ATOM   1115 C  CA  . THR   B 1 48 ? 15.919  -8.784  -24.114 1.00 31.00  ? 47  THR   B CA  1 
ATOM   1116 C  C   . THR   B 1 48 ? 17.219  -7.998  -24.050 1.00 36.10  ? 47  THR   B C   1 
ATOM   1117 O  O   . THR   B 1 48 ? 17.688  -7.671  -22.953 1.00 31.14  ? 47  THR   B O   1 
ATOM   1118 C  CB  . THR   B 1 48 ? 16.227  -10.265 -23.882 1.00 31.84  ? 47  THR   B CB  1 
ATOM   1119 O  OG1 . THR   B 1 48 ? 17.153  -10.725 -24.879 1.00 30.30  ? 47  THR   B OG1 1 
ATOM   1120 C  CG2 . THR   B 1 48 ? 14.953  -11.094 -23.938 1.00 29.95  ? 47  THR   B CG2 1 
ATOM   1121 N  N   . HIS   B 1 49 ? 17.813  -7.704  -25.207 1.00 30.74  ? 48  HIS   B N   1 
ATOM   1122 C  CA  . HIS   B 1 49 ? 19.120  -7.060  -25.317 1.00 33.66  ? 48  HIS   B CA  1 
ATOM   1123 C  C   . HIS   B 1 49 ? 20.219  -7.876  -24.651 1.00 29.31  ? 48  HIS   B C   1 
ATOM   1124 O  O   . HIS   B 1 49 ? 21.275  -7.336  -24.306 1.00 35.68  ? 48  HIS   B O   1 
ATOM   1125 C  CB  . HIS   B 1 49 ? 19.092  -5.635  -24.754 1.00 29.58  ? 48  HIS   B CB  1 
ATOM   1126 C  CG  . HIS   B 1 49 ? 17.840  -4.891  -25.085 1.00 31.04  ? 48  HIS   B CG  1 
ATOM   1127 N  ND1 . HIS   B 1 49 ? 17.338  -4.813  -26.366 1.00 31.64  ? 48  HIS   B ND1 1 
ATOM   1128 C  CD2 . HIS   B 1 49 ? 16.976  -4.206  -24.299 1.00 36.64  ? 48  HIS   B CD2 1 
ATOM   1129 C  CE1 . HIS   B 1 49 ? 16.224  -4.104  -26.355 1.00 31.28  ? 48  HIS   B CE1 1 
ATOM   1130 N  NE2 . HIS   B 1 49 ? 15.982  -3.723  -25.113 1.00 42.77  ? 48  HIS   B NE2 1 
ATOM   1131 N  N   . GLU   B 1 50 ? 19.989  -9.176  -24.472 1.00 30.44  ? 49  GLU   B N   1 
ATOM   1132 C  CA  . GLU   B 1 50 ? 21.028  -10.070 -23.991 1.00 28.48  ? 49  GLU   B CA  1 
ATOM   1133 C  C   . GLU   B 1 50 ? 22.047  -10.336 -25.095 1.00 34.13  ? 49  GLU   B C   1 
ATOM   1134 O  O   . GLU   B 1 50 ? 21.808  -10.076 -26.276 1.00 32.13  ? 49  GLU   B O   1 
ATOM   1135 C  CB  . GLU   B 1 50 ? 20.424  -11.392 -23.517 1.00 38.30  ? 49  GLU   B CB  1 
ATOM   1136 C  CG  . GLU   B 1 50 ? 19.412  -11.254 -22.394 1.00 41.76  ? 49  GLU   B CG  1 
ATOM   1137 C  CD  . GLU   B 1 50 ? 19.864  -11.930 -21.117 1.00 53.19  ? 49  GLU   B CD  1 
ATOM   1138 O  OE1 . GLU   B 1 50 ? 20.976  -12.498 -21.104 1.00 53.70  ? 49  GLU   B OE1 1 
ATOM   1139 O  OE2 . GLU   B 1 50 ? 19.105  -11.894 -20.127 1.00 45.64  ? 49  GLU   B OE2 1 
ATOM   1140 N  N   . THR   B 1 51 ? 23.198  -10.869 -24.695 1.00 31.57  ? 50  THR   B N   1 
ATOM   1141 C  CA  . THR   B 1 51 ? 24.254  -11.227 -25.628 1.00 34.95  ? 50  THR   B CA  1 
ATOM   1142 C  C   . THR   B 1 51 ? 24.748  -12.634 -25.326 1.00 38.28  ? 50  THR   B C   1 
ATOM   1143 O  O   . THR   B 1 51 ? 24.675  -13.106 -24.187 1.00 35.92  ? 50  THR   B O   1 
ATOM   1144 C  CB  . THR   B 1 51 ? 25.434  -10.247 -25.566 1.00 43.10  ? 50  THR   B CB  1 
ATOM   1145 O  OG1 . THR   B 1 51 ? 25.935  -10.186 -24.226 1.00 40.83  ? 50  THR   B OG1 1 
ATOM   1146 C  CG2 . THR   B 1 51 ? 25.003  -8.854  -26.010 1.00 30.86  ? 50  THR   B CG2 1 
ATOM   1147 N  N   . ALA   B 1 52 ? 25.252  -13.298 -26.362 1.00 33.09  ? 51  ALA   B N   1 
ATOM   1148 C  CA  . ALA   B 1 52 ? 25.843  -14.622 -26.217 1.00 32.10  ? 51  ALA   B CA  1 
ATOM   1149 C  C   . ALA   B 1 52 ? 26.704  -14.908 -27.437 1.00 33.08  ? 51  ALA   B C   1 
ATOM   1150 O  O   . ALA   B 1 52 ? 26.632  -14.213 -28.452 1.00 30.38  ? 51  ALA   B O   1 
ATOM   1151 C  CB  . ALA   B 1 52 ? 24.772  -15.706 -26.047 1.00 32.14  ? 51  ALA   B CB  1 
ATOM   1152 N  N   . PHE   B 1 53 ? 27.521  -15.953 -27.322 1.00 30.94  ? 52  PHE   B N   1 
ATOM   1153 C  CA  . PHE   B 1 53 ? 28.330  -16.451 -28.428 1.00 35.83  ? 52  PHE   B CA  1 
ATOM   1154 C  C   . PHE   B 1 53 ? 27.685  -17.723 -28.963 1.00 36.57  ? 52  PHE   B C   1 
ATOM   1155 O  O   . PHE   B 1 53 ? 27.481  -18.682 -28.210 1.00 34.52  ? 52  PHE   B O   1 
ATOM   1156 C  CB  . PHE   B 1 53 ? 29.767  -16.732 -27.987 1.00 37.81  ? 52  PHE   B CB  1 
ATOM   1157 C  CG  . PHE   B 1 53 ? 30.509  -15.518 -27.500 1.00 41.19  ? 52  PHE   B CG  1 
ATOM   1158 C  CD1 . PHE   B 1 53 ? 30.790  -14.468 -28.358 1.00 41.06  ? 52  PHE   B CD1 1 
ATOM   1159 C  CD2 . PHE   B 1 53 ? 30.946  -15.440 -26.189 1.00 46.53  ? 52  PHE   B CD2 1 
ATOM   1160 C  CE1 . PHE   B 1 53 ? 31.482  -13.355 -27.913 1.00 40.27  ? 52  PHE   B CE1 1 
ATOM   1161 C  CE2 . PHE   B 1 53 ? 31.636  -14.330 -25.737 1.00 44.33  ? 52  PHE   B CE2 1 
ATOM   1162 C  CZ  . PHE   B 1 53 ? 31.904  -13.287 -26.602 1.00 48.80  ? 52  PHE   B CZ  1 
ATOM   1163 N  N   . LEU   B 1 54 ? 27.366  -17.733 -30.255 1.00 30.99  ? 53  LEU   B N   1 
ATOM   1164 C  CA  . LEU   B 1 54 ? 26.728  -18.881 -30.879 1.00 27.99  ? 53  LEU   B CA  1 
ATOM   1165 C  C   . LEU   B 1 54 ? 27.438  -19.234 -32.176 1.00 30.16  ? 53  LEU   B C   1 
ATOM   1166 O  O   . LEU   B 1 54 ? 28.042  -18.375 -32.827 1.00 30.16  ? 53  LEU   B O   1 
ATOM   1167 C  CB  . LEU   B 1 54 ? 25.239  -18.622 -31.163 1.00 31.53  ? 53  LEU   B CB  1 
ATOM   1168 C  CG  . LEU   B 1 54 ? 24.302  -18.606 -29.952 1.00 29.35  ? 53  LEU   B CG  1 
ATOM   1169 C  CD1 . LEU   B 1 54 ? 22.873  -18.348 -30.393 1.00 28.53  ? 53  LEU   B CD1 1 
ATOM   1170 C  CD2 . LEU   B 1 54 ? 24.407  -19.916 -29.190 1.00 42.11  ? 53  LEU   B CD2 1 
ATOM   1171 N  N   . GLY   B 1 55 ? 27.354  -20.512 -32.544 1.00 31.18  ? 54  GLY   B N   1 
ATOM   1172 C  CA  . GLY   B 1 55 ? 27.891  -20.985 -33.797 1.00 28.81  ? 54  GLY   B CA  1 
ATOM   1173 C  C   . GLY   B 1 55 ? 26.831  -21.072 -34.877 1.00 30.04  ? 54  GLY   B C   1 
ATOM   1174 O  O   . GLY   B 1 55 ? 25.629  -20.997 -34.603 1.00 25.84  ? 54  GLY   B O   1 
ATOM   1175 N  N   . PRO   B 1 56 ? 27.266  -21.242 -36.131 1.00 30.58  ? 55  PRO   B N   1 
ATOM   1176 C  CA  . PRO   B 1 56 ? 26.322  -21.241 -37.266 1.00 27.90  ? 55  PRO   B CA  1 
ATOM   1177 C  C   . PRO   B 1 56 ? 25.180  -22.239 -37.158 1.00 26.82  ? 55  PRO   B C   1 
ATOM   1178 O  O   . PRO   B 1 56 ? 24.105  -21.992 -37.722 1.00 27.03  ? 55  PRO   B O   1 
ATOM   1179 C  CB  . PRO   B 1 56 ? 27.228  -21.569 -38.460 1.00 30.68  ? 55  PRO   B CB  1 
ATOM   1180 C  CG  . PRO   B 1 56 ? 28.567  -21.053 -38.058 1.00 38.53  ? 55  PRO   B CG  1 
ATOM   1181 C  CD  . PRO   B 1 56 ? 28.668  -21.298 -36.577 1.00 31.11  ? 55  PRO   B CD  1 
ATOM   1182 N  N   . LYS   B 1 57 ? 25.370  -23.361 -36.460 1.00 30.80  ? 56  LYS   B N   1 
ATOM   1183 C  CA  . LYS   B 1 57 ? 24.299  -24.345 -36.360 1.00 25.04  ? 56  LYS   B CA  1 
ATOM   1184 C  C   . LYS   B 1 57 ? 23.067  -23.783 -35.664 1.00 30.02  ? 56  LYS   B C   1 
ATOM   1185 O  O   . LYS   B 1 57 ? 21.964  -24.307 -35.855 1.00 28.36  ? 56  LYS   B O   1 
ATOM   1186 C  CB  . LYS   B 1 57 ? 24.789  -25.595 -35.619 1.00 28.30  ? 56  LYS   B CB  1 
ATOM   1187 C  CG  . LYS   B 1 57 ? 24.933  -25.417 -34.114 1.00 31.64  ? 56  LYS   B CG  1 
ATOM   1188 C  CD  . LYS   B 1 57 ? 25.318  -26.727 -33.440 1.00 39.32  ? 56  LYS   B CD  1 
ATOM   1189 C  CE  . LYS   B 1 57 ? 25.362  -26.583 -31.926 1.00 35.62  ? 56  LYS   B CE  1 
ATOM   1190 N  NZ  . LYS   B 1 57 ? 24.010  -26.346 -31.340 1.00 42.51  ? 56  LYS   B NZ  1 
ATOM   1191 N  N   . ASP   B 1 58 ? 23.229  -22.724 -34.874 1.00 29.09  ? 57  ASP   B N   1 
ATOM   1192 C  CA  . ASP   B 1 58 ? 22.135  -22.117 -34.132 1.00 26.26  ? 57  ASP   B CA  1 
ATOM   1193 C  C   . ASP   B 1 58 ? 21.703  -20.780 -34.719 1.00 24.77  ? 57  ASP   B C   1 
ATOM   1194 O  O   . ASP   B 1 58 ? 20.923  -20.061 -34.088 1.00 23.35  ? 57  ASP   B O   1 
ATOM   1195 C  CB  . ASP   B 1 58 ? 22.534  -21.944 -32.667 1.00 28.03  ? 57  ASP   B CB  1 
ATOM   1196 C  CG  . ASP   B 1 58 ? 22.707  -23.274 -31.946 1.00 31.28  ? 57  ASP   B CG  1 
ATOM   1197 O  OD1 . ASP   B 1 58 ? 21.832  -24.151 -32.093 1.00 34.56  ? 57  ASP   B OD1 1 
ATOM   1198 O  OD2 . ASP   B 1 58 ? 23.720  -23.441 -31.238 1.00 33.78  ? 57  ASP   B OD2 1 
ATOM   1199 N  N   . LEU   B 1 59 ? 22.176  -20.436 -35.915 1.00 24.06  ? 58  LEU   B N   1 
ATOM   1200 C  CA  . LEU   B 1 59 ? 21.888  -19.147 -36.535 1.00 23.02  ? 58  LEU   B CA  1 
ATOM   1201 C  C   . LEU   B 1 59 ? 21.126  -19.376 -37.829 1.00 24.58  ? 58  LEU   B C   1 
ATOM   1202 O  O   . LEU   B 1 59 ? 21.604  -20.096 -38.714 1.00 30.81  ? 58  LEU   B O   1 
ATOM   1203 C  CB  . LEU   B 1 59 ? 23.179  -18.368 -36.796 1.00 25.44  ? 58  LEU   B CB  1 
ATOM   1204 C  CG  . LEU   B 1 59 ? 24.009  -18.081 -35.546 1.00 26.22  ? 58  LEU   B CG  1 
ATOM   1205 C  CD1 . LEU   B 1 59 ? 25.319  -17.412 -35.927 1.00 28.57  ? 58  LEU   B CD1 1 
ATOM   1206 C  CD2 . LEU   B 1 59 ? 23.226  -17.227 -34.555 1.00 26.21  ? 58  LEU   B CD2 1 
ATOM   1207 N  N   . PHE   B 1 60 ? 19.947  -18.757 -37.938 1.00 21.91  ? 59  PHE   B N   1 
ATOM   1208 C  CA  . PHE   B 1 60 ? 19.034  -18.903 -39.059 1.00 20.90  ? 59  PHE   B CA  1 
ATOM   1209 C  C   . PHE   B 1 60 ? 18.758  -17.542 -39.689 1.00 23.51  ? 59  PHE   B C   1 
ATOM   1210 O  O   . PHE   B 1 60 ? 18.495  -16.578 -38.969 1.00 25.34  ? 59  PHE   B O   1 
ATOM   1211 C  CB  . PHE   B 1 60 ? 17.702  -19.532 -38.603 1.00 22.97  ? 59  PHE   B CB  1 
ATOM   1212 C  CG  . PHE   B 1 60 ? 17.845  -20.903 -37.990 1.00 25.26  ? 59  PHE   B CG  1 
ATOM   1213 C  CD1 . PHE   B 1 60 ? 18.313  -21.052 -36.692 1.00 25.04  ? 59  PHE   B CD1 1 
ATOM   1214 C  CD2 . PHE   B 1 60 ? 17.490  -22.038 -38.706 1.00 31.00  ? 59  PHE   B CD2 1 
ATOM   1215 C  CE1 . PHE   B 1 60 ? 18.442  -22.313 -36.124 1.00 29.13  ? 59  PHE   B CE1 1 
ATOM   1216 C  CE2 . PHE   B 1 60 ? 17.612  -23.299 -38.140 1.00 29.83  ? 59  PHE   B CE2 1 
ATOM   1217 C  CZ  . PHE   B 1 60 ? 18.090  -23.432 -36.850 1.00 29.71  ? 59  PHE   B CZ  1 
ATOM   1218 N  N   . PRO   B 1 61 ? 18.793  -17.427 -41.013 1.00 24.48  ? 60  PRO   B N   1 
ATOM   1219 C  CA  . PRO   B 1 61 ? 18.574  -16.110 -41.636 1.00 23.11  ? 60  PRO   B CA  1 
ATOM   1220 C  C   . PRO   B 1 61 ? 17.178  -15.567 -41.348 1.00 27.49  ? 60  PRO   B C   1 
ATOM   1221 O  O   . PRO   B 1 61 ? 16.178  -16.275 -41.467 1.00 27.66  ? 60  PRO   B O   1 
ATOM   1222 C  CB  . PRO   B 1 61 ? 18.786  -16.383 -43.128 1.00 26.61  ? 60  PRO   B CB  1 
ATOM   1223 C  CG  . PRO   B 1 61 ? 18.609  -17.871 -43.282 1.00 37.08  ? 60  PRO   B CG  1 
ATOM   1224 C  CD  . PRO   B 1 61 ? 19.080  -18.479 -42.004 1.00 28.67  ? 60  PRO   B CD  1 
ATOM   1225 N  N   . TYR   B 1 62 ? 17.116  -14.285 -40.974 1.00 25.15  ? 61  TYR   B N   1 
ATOM   1226 C  CA  . TYR   B 1 62 ? 15.848  -13.709 -40.535 1.00 26.61  ? 61  TYR   B CA  1 
ATOM   1227 C  C   . TYR   B 1 62 ? 14.827  -13.672 -41.664 1.00 28.60  ? 61  TYR   B C   1 
ATOM   1228 O  O   . TYR   B 1 62 ? 13.703  -14.159 -41.511 1.00 32.97  ? 61  TYR   B O   1 
ATOM   1229 C  CB  . TYR   B 1 62 ? 16.069  -12.305 -39.973 1.00 24.06  ? 61  TYR   B CB  1 
ATOM   1230 C  CG  . TYR   B 1 62 ? 14.784  -11.540 -39.751 1.00 28.68  ? 61  TYR   B CG  1 
ATOM   1231 C  CD1 . TYR   B 1 62 ? 13.925  -11.877 -38.712 1.00 30.42  ? 61  TYR   B CD1 1 
ATOM   1232 C  CD2 . TYR   B 1 62 ? 14.427  -10.486 -40.583 1.00 32.16  ? 61  TYR   B CD2 1 
ATOM   1233 C  CE1 . TYR   B 1 62 ? 12.747  -11.187 -38.506 1.00 32.95  ? 61  TYR   B CE1 1 
ATOM   1234 C  CE2 . TYR   B 1 62 ? 13.250  -9.787  -40.384 1.00 33.73  ? 61  TYR   B CE2 1 
ATOM   1235 C  CZ  . TYR   B 1 62 ? 12.416  -10.142 -39.345 1.00 36.29  ? 61  TYR   B CZ  1 
ATOM   1236 O  OH  . TYR   B 1 62 ? 11.245  -9.452  -39.143 1.00 39.71  ? 61  TYR   B OH  1 
ATOM   1237 N  N   . ASP   B 1 63 ? 15.196  -13.086 -42.805 1.00 34.53  ? 62  ASP   B N   1 
ATOM   1238 C  CA  . ASP   B 1 63 ? 14.239  -12.935 -43.898 1.00 36.40  ? 62  ASP   B CA  1 
ATOM   1239 C  C   . ASP   B 1 63 ? 13.780  -14.286 -44.429 1.00 36.29  ? 62  ASP   B C   1 
ATOM   1240 O  O   . ASP   B 1 63 ? 12.596  -14.469 -44.735 1.00 39.02  ? 62  ASP   B O   1 
ATOM   1241 C  CB  . ASP   B 1 63 ? 14.850  -12.100 -45.022 1.00 38.65  ? 62  ASP   B CB  1 
ATOM   1242 C  CG  . ASP   B 1 63 ? 14.826  -10.616 -44.720 1.00 53.73  ? 62  ASP   B CG  1 
ATOM   1243 O  OD1 . ASP   B 1 63 ? 13.733  -10.015 -44.769 1.00 57.75  ? 62  ASP   B OD1 1 
ATOM   1244 O  OD2 . ASP   B 1 63 ? 15.898  -10.054 -44.418 1.00 66.09  ? 62  ASP   B OD2 1 
ATOM   1245 N  N   . LYS   B 1 64 ? 14.699  -15.249 -44.536 1.00 33.31  ? 63  LYS   B N   1 
ATOM   1246 C  CA  . LYS   B 1 64 ? 14.341  -16.562 -45.065 1.00 36.35  ? 63  LYS   B CA  1 
ATOM   1247 C  C   . LYS   B 1 64 ? 13.352  -17.286 -44.158 1.00 33.80  ? 63  LYS   B C   1 
ATOM   1248 O  O   . LYS   B 1 64 ? 12.436  -17.961 -44.642 1.00 37.66  ? 63  LYS   B O   1 
ATOM   1249 C  CB  . LYS   B 1 64 ? 15.599  -17.411 -45.257 1.00 37.97  ? 63  LYS   B CB  1 
ATOM   1250 C  CG  . LYS   B 1 64 ? 15.334  -18.859 -45.691 1.00 41.24  ? 63  LYS   B CG  1 
ATOM   1251 C  CD  . LYS   B 1 64 ? 16.600  -19.702 -45.571 1.00 42.70  ? 63  LYS   B CD  1 
ATOM   1252 C  CE  . LYS   B 1 64 ? 16.452  -21.075 -46.217 1.00 40.82  ? 63  LYS   B CE  1 
ATOM   1253 N  NZ  . LYS   B 1 64 ? 15.448  -21.934 -45.535 1.00 45.29  ? 63  LYS   B NZ  1 
ATOM   1254 N  N   . CYS   B 1 65 ? 13.512  -17.155 -42.840 1.00 30.63  ? 64  CYS   B N   1 
ATOM   1255 C  CA  . CYS   B 1 65 ? 12.819  -18.025 -41.895 1.00 31.08  ? 64  CYS   B CA  1 
ATOM   1256 C  C   . CYS   B 1 65 ? 11.859  -17.288 -40.968 1.00 30.28  ? 64  CYS   B C   1 
ATOM   1257 O  O   . CYS   B 1 65 ? 11.395  -17.881 -39.985 1.00 34.89  ? 64  CYS   B O   1 
ATOM   1258 C  CB  . CYS   B 1 65 ? 13.846  -18.803 -41.066 1.00 27.22  ? 64  CYS   B CB  1 
ATOM   1259 S  SG  . CYS   B 1 65 ? 14.926  -19.865 -42.057 1.00 36.89  ? 64  CYS   B SG  1 
ATOM   1260 N  N   . LYS   B 1 66 ? 11.534  -16.022 -41.247 1.00 33.28  ? 65  LYS   B N   1 
ATOM   1261 C  CA  . LYS   B 1 66 ? 10.653  -15.294 -40.338 1.00 37.26  ? 65  LYS   B CA  1 
ATOM   1262 C  C   . LYS   B 1 66 ? 9.213   -15.782 -40.428 1.00 39.33  ? 65  LYS   B C   1 
ATOM   1263 O  O   . LYS   B 1 66 ? 8.463   -15.669 -39.452 1.00 41.87  ? 65  LYS   B O   1 
ATOM   1264 C  CB  . LYS   B 1 66 ? 10.718  -13.791 -40.608 1.00 31.88  ? 65  LYS   B CB  1 
ATOM   1265 C  CG  . LYS   B 1 66 ? 10.227  -13.363 -41.977 1.00 31.71  ? 65  LYS   B CG  1 
ATOM   1266 C  CD  . LYS   B 1 66 ? 10.470  -11.878 -42.179 1.00 48.87  ? 65  LYS   B CD  1 
ATOM   1267 C  CE  . LYS   B 1 66 ? 10.063  -11.431 -43.569 1.00 49.77  ? 65  LYS   B CE  1 
ATOM   1268 N  NZ  . LYS   B 1 66 ? 10.688  -10.125 -43.911 1.00 52.83  ? 65  LYS   B NZ  1 
ATOM   1269 N  N   . ASP   B 1 67 ? 8.804   -16.317 -41.582 1.00 35.50  ? 66  ASP   B N   1 
ATOM   1270 C  CA  . ASP   B 1 67 ? 7.471   -16.898 -41.687 1.00 39.70  ? 66  ASP   B CA  1 
ATOM   1271 C  C   . ASP   B 1 67 ? 7.297   -18.059 -40.717 1.00 40.22  ? 66  ASP   B C   1 
ATOM   1272 O  O   . ASP   B 1 67 ? 6.181   -18.320 -40.254 1.00 49.89  ? 66  ASP   B O   1 
ATOM   1273 C  CB  . ASP   B 1 67 ? 7.208   -17.358 -43.122 1.00 47.34  ? 66  ASP   B CB  1 
ATOM   1274 N  N   . LYS   B 1 68 ? 8.383   -18.756 -40.391 1.00 36.54  ? 67  LYS   B N   1 
ATOM   1275 C  CA  . LYS   B 1 68 ? 8.322   -19.894 -39.483 1.00 36.42  ? 67  LYS   B CA  1 
ATOM   1276 C  C   . LYS   B 1 68 ? 8.572   -19.492 -38.031 1.00 36.97  ? 67  LYS   B C   1 
ATOM   1277 O  O   . LYS   B 1 68 ? 7.819   -19.887 -37.138 1.00 36.91  ? 67  LYS   B O   1 
ATOM   1278 C  CB  . LYS   B 1 68 ? 9.336   -20.958 -39.919 1.00 41.09  ? 67  LYS   B CB  1 
ATOM   1279 C  CG  . LYS   B 1 68 ? 9.255   -22.248 -39.126 1.00 47.52  ? 67  LYS   B CG  1 
ATOM   1280 C  CD  . LYS   B 1 68 ? 10.148  -23.326 -39.714 1.00 56.66  ? 67  LYS   B CD  1 
ATOM   1281 C  CE  . LYS   B 1 68 ? 9.910   -24.658 -39.019 1.00 52.03  ? 67  LYS   B CE  1 
ATOM   1282 N  NZ  . LYS   B 1 68 ? 11.161  -25.246 -38.465 1.00 55.59  ? 67  LYS   B NZ  1 
ATOM   1283 N  N   . TYR   B 1 69 ? 9.617   -18.702 -37.779 1.00 29.46  ? 68  TYR   B N   1 
ATOM   1284 C  CA  . TYR   B 1 69 ? 10.059  -18.410 -36.422 1.00 25.86  ? 68  TYR   B CA  1 
ATOM   1285 C  C   . TYR   B 1 69 ? 9.538   -17.087 -35.880 1.00 30.25  ? 68  TYR   B C   1 
ATOM   1286 O  O   . TYR   B 1 69 ? 9.727   -16.813 -34.690 1.00 30.03  ? 68  TYR   B O   1 
ATOM   1287 C  CB  . TYR   B 1 69 ? 11.591  -18.400 -36.359 1.00 26.79  ? 68  TYR   B CB  1 
ATOM   1288 C  CG  . TYR   B 1 69 ? 12.236  -19.709 -36.751 1.00 26.12  ? 68  TYR   B CG  1 
ATOM   1289 C  CD1 . TYR   B 1 69 ? 11.750  -20.915 -36.265 1.00 31.95  ? 68  TYR   B CD1 1 
ATOM   1290 C  CD2 . TYR   B 1 69 ? 13.328  -19.739 -37.607 1.00 27.06  ? 68  TYR   B CD2 1 
ATOM   1291 C  CE1 . TYR   B 1 69 ? 12.336  -22.112 -36.618 1.00 29.27  ? 68  TYR   B CE1 1 
ATOM   1292 C  CE2 . TYR   B 1 69 ? 13.921  -20.935 -37.968 1.00 32.27  ? 68  TYR   B CE2 1 
ATOM   1293 C  CZ  . TYR   B 1 69 ? 13.420  -22.118 -37.471 1.00 36.91  ? 68  TYR   B CZ  1 
ATOM   1294 O  OH  . TYR   B 1 69 ? 14.007  -23.312 -37.826 1.00 31.55  ? 68  TYR   B OH  1 
ATOM   1295 N  N   . GLY   B 1 70 ? 8.894   -16.267 -36.708 1.00 34.54  ? 69  GLY   B N   1 
ATOM   1296 C  CA  . GLY   B 1 70 ? 8.529   -14.925 -36.293 1.00 42.52  ? 69  GLY   B CA  1 
ATOM   1297 C  C   . GLY   B 1 70 ? 7.111   -14.755 -35.785 1.00 43.79  ? 69  GLY   B C   1 
ATOM   1298 O  O   . GLY   B 1 70 ? 6.535   -13.669 -35.900 1.00 49.59  ? 69  GLY   B O   1 
ATOM   1299 N  N   . LYS   B 1 71 ? 6.537   -15.813 -35.225 1.00 42.85  ? 70  LYS   B N   1 
ATOM   1300 C  CA  . LYS   B 1 71 ? 5.208   -15.618 -34.661 1.00 42.96  ? 70  LYS   B CA  1 
ATOM   1301 C  C   . LYS   B 1 71 ? 5.315   -15.230 -33.191 1.00 43.14  ? 70  LYS   B C   1 
ATOM   1302 O  O   . LYS   B 1 71 ? 6.199   -15.723 -32.483 1.00 45.58  ? 70  LYS   B O   1 
ATOM   1303 C  CB  . LYS   B 1 71 ? 4.368   -16.886 -34.798 1.00 40.39  ? 70  LYS   B CB  1 
ATOM   1304 C  CG  . LYS   B 1 71 ? 3.832   -17.105 -36.206 1.00 60.69  ? 70  LYS   B CG  1 
ATOM   1305 C  CD  . LYS   B 1 71 ? 3.451   -18.556 -36.467 1.00 65.99  ? 70  LYS   B CD  1 
ATOM   1306 C  CE  . LYS   B 1 71 ? 2.192   -18.965 -35.719 1.00 72.13  ? 70  LYS   B CE  1 
ATOM   1307 N  NZ  . LYS   B 1 71 ? 1.751   -20.335 -36.113 1.00 73.26  ? 70  LYS   B NZ  1 
ATOM   1308 N  N   . PRO   B 1 72 ? 4.439   -14.343 -32.719 1.00 46.67  ? 71  PRO   B N   1 
ATOM   1309 C  CA  . PRO   B 1 72 ? 4.501   -13.929 -31.315 1.00 45.83  ? 71  PRO   B CA  1 
ATOM   1310 C  C   . PRO   B 1 72 ? 4.314   -15.111 -30.376 1.00 46.66  ? 71  PRO   B C   1 
ATOM   1311 O  O   . PRO   B 1 72 ? 3.716   -16.134 -30.722 1.00 44.46  ? 71  PRO   B O   1 
ATOM   1312 C  CB  . PRO   B 1 72 ? 3.347   -12.927 -31.185 1.00 50.25  ? 71  PRO   B CB  1 
ATOM   1313 C  CG  . PRO   B 1 72 ? 3.079   -12.463 -32.567 1.00 57.73  ? 71  PRO   B CG  1 
ATOM   1314 C  CD  . PRO   B 1 72 ? 3.380   -13.634 -33.457 1.00 46.78  ? 71  PRO   B CD  1 
ATOM   1315 N  N   . ASN   B 1 73 ? 4.846   -14.961 -29.170 1.00 44.76  ? 72  ASN   B N   1 
ATOM   1316 C  CA  . ASN   B 1 73 ? 4.649   -15.971 -28.145 1.00 42.92  ? 72  ASN   B CA  1 
ATOM   1317 C  C   . ASN   B 1 73 ? 4.596   -15.284 -26.784 1.00 42.92  ? 72  ASN   B C   1 
ATOM   1318 O  O   . ASN   B 1 73 ? 4.448   -14.060 -26.692 1.00 46.59  ? 72  ASN   B O   1 
ATOM   1319 C  CB  . ASN   B 1 73 ? 5.737   -17.058 -28.232 1.00 46.95  ? 72  ASN   B CB  1 
ATOM   1320 C  CG  . ASN   B 1 73 ? 7.143   -16.524 -27.980 1.00 40.39  ? 72  ASN   B CG  1 
ATOM   1321 O  OD1 . ASN   B 1 73 ? 7.376   -15.725 -27.076 1.00 35.95  ? 72  ASN   B OD1 1 
ATOM   1322 N  ND2 . ASN   B 1 73 ? 8.095   -16.983 -28.788 1.00 34.76  ? 72  ASN   B ND2 1 
ATOM   1323 N  N   . LYS   B 1 74 ? 4.753   -16.082 -25.732 1.00 43.20  ? 73  LYS   B N   1 
ATOM   1324 C  CA  . LYS   B 1 74 ? 4.554   -15.680 -24.349 1.00 44.83  ? 73  LYS   B CA  1 
ATOM   1325 C  C   . LYS   B 1 74 ? 5.862   -15.471 -23.602 1.00 51.55  ? 73  LYS   B C   1 
ATOM   1326 O  O   . LYS   B 1 74 ? 5.840   -15.216 -22.392 1.00 38.83  ? 73  LYS   B O   1 
ATOM   1327 C  CB  . LYS   B 1 74 ? 3.714   -16.740 -23.620 1.00 50.46  ? 73  LYS   B CB  1 
ATOM   1328 C  CG  . LYS   B 1 74 ? 4.427   -18.088 -23.407 1.00 49.26  ? 73  LYS   B CG  1 
ATOM   1329 C  CD  . LYS   B 1 74 ? 4.613   -18.872 -24.719 1.00 57.18  ? 73  LYS   B CD  1 
ATOM   1330 C  CE  . LYS   B 1 74 ? 5.511   -20.076 -24.556 1.00 51.78  ? 73  LYS   B CE  1 
ATOM   1331 N  NZ  . LYS   B 1 74 ? 6.071   -20.488 -25.874 1.00 64.35  ? 73  LYS   B NZ  1 
ATOM   1332 N  N   . ARG   B 1 75 ? 6.996   -15.584 -24.289 1.00 33.59  ? 74  ARG   B N   1 
ATOM   1333 C  CA  . ARG   B 1 75 ? 8.289   -15.407 -23.650 1.00 32.37  ? 74  ARG   B CA  1 
ATOM   1334 C  C   . ARG   B 1 75 ? 8.592   -13.925 -23.479 1.00 38.55  ? 74  ARG   B C   1 
ATOM   1335 O  O   . ARG   B 1 75 ? 8.331   -13.111 -24.372 1.00 31.37  ? 74  ARG   B O   1 
ATOM   1336 C  CB  . ARG   B 1 75 ? 9.393   -16.086 -24.464 1.00 27.75  ? 74  ARG   B CB  1 
ATOM   1337 C  CG  . ARG   B 1 75 ? 9.199   -17.585 -24.688 1.00 29.32  ? 74  ARG   B CG  1 
ATOM   1338 C  CD  . ARG   B 1 75 ? 9.106   -18.345 -23.375 1.00 37.49  ? 74  ARG   B CD  1 
ATOM   1339 N  NE  . ARG   B 1 75 ? 9.264   -19.782 -23.569 1.00 31.60  ? 74  ARG   B NE  1 
ATOM   1340 C  CZ  . ARG   B 1 75 ? 10.411  -20.437 -23.440 1.00 31.85  ? 74  ARG   B CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 75 ? 11.525  -19.820 -23.083 1.00 33.50  ? 74  ARG   B NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 75 ? 10.440  -21.745 -23.673 1.00 35.26  ? 74  ARG   B NH2 1 
ATOM   1343 N  N   . LYS   B 1 76 ? 9.137   -13.577 -22.316 1.00 31.31  ? 75  LYS   B N   1 
ATOM   1344 C  CA  . LYS   B 1 76 ? 9.408   -12.181 -22.004 1.00 28.86  ? 75  LYS   B CA  1 
ATOM   1345 C  C   . LYS   B 1 76 ? 10.460  -11.609 -22.945 1.00 30.69  ? 75  LYS   B C   1 
ATOM   1346 O  O   . LYS   B 1 76 ? 11.551  -12.168 -23.091 1.00 30.00  ? 75  LYS   B O   1 
ATOM   1347 C  CB  . LYS   B 1 76 ? 9.875   -12.051 -20.556 1.00 30.29  ? 75  LYS   B CB  1 
ATOM   1348 C  CG  . LYS   B 1 76 ? 10.283  -10.639 -20.175 1.00 30.68  ? 75  LYS   B CG  1 
ATOM   1349 C  CD  . LYS   B 1 76 ? 10.874  -10.595 -18.778 1.00 39.56  ? 75  LYS   B CD  1 
ATOM   1350 C  CE  . LYS   B 1 76 ? 11.224  -9.173  -18.369 1.00 33.51  ? 75  LYS   B CE  1 
ATOM   1351 N  NZ  . LYS   B 1 76 ? 11.692  -9.110  -16.953 1.00 42.80  ? 75  LYS   B NZ  1 
ATOM   1352 N  N   . GLY   B 1 77 ? 10.134  -10.476 -23.568 1.00 32.23  ? 76  GLY   B N   1 
ATOM   1353 C  CA  . GLY   B 1 77 ? 11.027  -9.810  -24.489 1.00 34.25  ? 76  GLY   B CA  1 
ATOM   1354 C  C   . GLY   B 1 77 ? 10.865  -10.205 -25.941 1.00 32.77  ? 76  GLY   B C   1 
ATOM   1355 O  O   . GLY   B 1 77 ? 11.462  -9.562  -26.812 1.00 27.38  ? 76  GLY   B O   1 
ATOM   1356 N  N   . PHE   B 1 78 ? 10.063  -11.226 -26.241 1.00 35.24  ? 77  PHE   B N   1 
ATOM   1357 C  CA  . PHE   B 1 78 ? 10.027  -11.743 -27.605 1.00 30.04  ? 77  PHE   B CA  1 
ATOM   1358 C  C   . PHE   B 1 78 ? 9.291   -10.797 -28.545 1.00 31.78  ? 77  PHE   B C   1 
ATOM   1359 O  O   . PHE   B 1 78 ? 9.772   -10.505 -29.647 1.00 30.98  ? 77  PHE   B O   1 
ATOM   1360 C  CB  . PHE   B 1 78 ? 9.384   -13.127 -27.627 1.00 24.82  ? 77  PHE   B CB  1 
ATOM   1361 C  CG  . PHE   B 1 78 ? 9.538   -13.828 -28.939 1.00 26.45  ? 77  PHE   B CG  1 
ATOM   1362 C  CD1 . PHE   B 1 78 ? 10.667  -14.589 -29.199 1.00 27.89  ? 77  PHE   B CD1 1 
ATOM   1363 C  CD2 . PHE   B 1 78 ? 8.573   -13.707 -29.924 1.00 28.62  ? 77  PHE   B CD2 1 
ATOM   1364 C  CE1 . PHE   B 1 78 ? 10.819  -15.235 -30.419 1.00 27.42  ? 77  PHE   B CE1 1 
ATOM   1365 C  CE2 . PHE   B 1 78 ? 8.723   -14.350 -31.144 1.00 32.55  ? 77  PHE   B CE2 1 
ATOM   1366 C  CZ  . PHE   B 1 78 ? 9.847   -15.110 -31.386 1.00 26.02  ? 77  PHE   B CZ  1 
ATOM   1367 N  N   . ASN   B 1 79 ? 8.112   -10.318 -28.141 1.00 29.66  ? 78  ASN   B N   1 
ATOM   1368 C  CA  . ASN   B 1 79 ? 7.346   -9.444  -29.024 1.00 31.68  ? 78  ASN   B CA  1 
ATOM   1369 C  C   . ASN   B 1 79 ? 8.045   -8.103  -29.212 1.00 31.72  ? 78  ASN   B C   1 
ATOM   1370 O  O   . ASN   B 1 79 ? 8.009   -7.528  -30.305 1.00 32.06  ? 78  ASN   B O   1 
ATOM   1371 C  CB  . ASN   B 1 79 ? 5.930   -9.252  -28.486 1.00 36.12  ? 78  ASN   B CB  1 
ATOM   1372 C  CG  . ASN   B 1 79 ? 5.115   -10.529 -28.535 1.00 50.37  ? 78  ASN   B CG  1 
ATOM   1373 O  OD1 . ASN   B 1 79 ? 5.483   -11.488 -29.215 1.00 46.38  ? 78  ASN   B OD1 1 
ATOM   1374 N  ND2 . ASN   B 1 79 ? 4.001   -10.548 -27.815 1.00 52.95  ? 78  ASN   B ND2 1 
ATOM   1375 N  N   . GLU   B 1 80 ? 8.696   -7.596  -28.164 1.00 31.68  ? 79  GLU   B N   1 
ATOM   1376 C  CA  . GLU   B 1 80 ? 9.523   -6.405  -28.335 1.00 36.79  ? 79  GLU   B CA  1 
ATOM   1377 C  C   . GLU   B 1 80 ? 10.700  -6.679  -29.261 1.00 30.76  ? 79  GLU   B C   1 
ATOM   1378 O  O   . GLU   B 1 80 ? 11.112  -5.794  -30.021 1.00 28.01  ? 79  GLU   B O   1 
ATOM   1379 C  CB  . GLU   B 1 80 ? 10.015  -5.899  -26.981 1.00 37.78  ? 79  GLU   B CB  1 
ATOM   1380 C  CG  . GLU   B 1 80 ? 9.079   -4.892  -26.336 1.00 61.15  ? 79  GLU   B CG  1 
ATOM   1381 C  CD  . GLU   B 1 80 ? 8.870   -3.659  -27.202 1.00 69.45  ? 79  GLU   B CD  1 
ATOM   1382 O  OE1 . GLU   B 1 80 ? 9.866   -2.975  -27.521 1.00 71.72  ? 79  GLU   B OE1 1 
ATOM   1383 O  OE2 . GLU   B 1 80 ? 7.711   -3.380  -27.577 1.00 71.56  ? 79  GLU   B OE2 1 
ATOM   1384 N  N   . GLY   B 1 81 ? 11.245  -7.896  -29.217 1.00 25.89  ? 80  GLY   B N   1 
ATOM   1385 C  CA  . GLY   B 1 81 ? 12.315  -8.248  -30.133 1.00 29.32  ? 80  GLY   B CA  1 
ATOM   1386 C  C   . GLY   B 1 81 ? 11.845  -8.298  -31.573 1.00 27.41  ? 80  GLY   B C   1 
ATOM   1387 O  O   . GLY   B 1 81 ? 12.558  -7.868  -32.485 1.00 27.77  ? 80  GLY   B O   1 
ATOM   1388 N  N   . LEU   B 1 82 ? 10.637  -8.822  -31.798 1.00 26.23  ? 81  LEU   B N   1 
ATOM   1389 C  CA  . LEU   B 1 82 ? 10.066  -8.802  -33.140 1.00 29.59  ? 81  LEU   B CA  1 
ATOM   1390 C  C   . LEU   B 1 82 ? 9.904   -7.374  -33.643 1.00 32.30  ? 81  LEU   B C   1 
ATOM   1391 O  O   . LEU   B 1 82 ? 10.156  -7.089  -34.819 1.00 33.03  ? 81  LEU   B O   1 
ATOM   1392 C  CB  . LEU   B 1 82 ? 8.723   -9.530  -33.159 1.00 31.64  ? 81  LEU   B CB  1 
ATOM   1393 C  CG  . LEU   B 1 82 ? 8.779   -11.043 -32.968 1.00 28.98  ? 81  LEU   B CG  1 
ATOM   1394 C  CD1 . LEU   B 1 82 ? 7.384   -11.642 -33.058 1.00 35.11  ? 81  LEU   B CD1 1 
ATOM   1395 C  CD2 . LEU   B 1 82 ? 9.707   -11.667 -34.000 1.00 31.57  ? 81  LEU   B CD2 1 
ATOM   1396 N  N   . TRP   B 1 83 ? 9.488   -6.460  -32.766 1.00 26.80  ? 82  TRP   B N   1 
ATOM   1397 C  CA  . TRP   B 1 83 ? 9.369   -5.063  -33.168 1.00 27.53  ? 82  TRP   B CA  1 
ATOM   1398 C  C   . TRP   B 1 83 ? 10.728  -4.483  -33.533 1.00 28.02  ? 82  TRP   B C   1 
ATOM   1399 O  O   . TRP   B 1 83 ? 10.868  -3.796  -34.550 1.00 31.07  ? 82  TRP   B O   1 
ATOM   1400 C  CB  . TRP   B 1 83 ? 8.727   -4.239  -32.054 1.00 32.89  ? 82  TRP   B CB  1 
ATOM   1401 C  CG  . TRP   B 1 83 ? 8.440   -2.837  -32.486 1.00 33.02  ? 82  TRP   B CG  1 
ATOM   1402 C  CD1 . TRP   B 1 83 ? 7.262   -2.363  -32.983 1.00 44.04  ? 82  TRP   B CD1 1 
ATOM   1403 C  CD2 . TRP   B 1 83 ? 9.354   -1.732  -32.493 1.00 38.58  ? 82  TRP   B CD2 1 
ATOM   1404 N  NE1 . TRP   B 1 83 ? 7.381   -1.028  -33.286 1.00 44.85  ? 82  TRP   B NE1 1 
ATOM   1405 C  CE2 . TRP   B 1 83 ? 8.655   -0.617  -32.995 1.00 35.01  ? 82  TRP   B CE2 1 
ATOM   1406 C  CE3 . TRP   B 1 83 ? 10.693  -1.575  -32.116 1.00 33.69  ? 82  TRP   B CE3 1 
ATOM   1407 C  CZ2 . TRP   B 1 83 ? 9.248   0.637   -33.133 1.00 45.16  ? 82  TRP   B CZ2 1 
ATOM   1408 C  CZ3 . TRP   B 1 83 ? 11.281  -0.327  -32.254 1.00 38.91  ? 82  TRP   B CZ3 1 
ATOM   1409 C  CH2 . TRP   B 1 83 ? 10.557  0.761   -32.757 1.00 45.98  ? 82  TRP   B CH2 1 
ATOM   1410 N  N   . GLU   B 1 84 ? 11.746  -4.761  -32.717 1.00 24.41  ? 83  GLU   B N   1 
ATOM   1411 C  CA  . GLU   B 1 84 ? 13.063  -4.165  -32.926 1.00 27.02  ? 83  GLU   B CA  1 
ATOM   1412 C  C   . GLU   B 1 84 ? 13.702  -4.644  -34.223 1.00 30.00  ? 83  GLU   B C   1 
ATOM   1413 O  O   . GLU   B 1 84 ? 14.260  -3.843  -34.982 1.00 29.29  ? 83  GLU   B O   1 
ATOM   1414 C  CB  . GLU   B 1 84 ? 13.967  -4.481  -31.739 1.00 24.72  ? 83  GLU   B CB  1 
ATOM   1415 C  CG  . GLU   B 1 84 ? 13.570  -3.736  -30.474 1.00 27.27  ? 83  GLU   B CG  1 
ATOM   1416 C  CD  . GLU   B 1 84 ? 14.396  -4.118  -29.268 1.00 30.58  ? 83  GLU   B CD  1 
ATOM   1417 O  OE1 . GLU   B 1 84 ? 15.283  -4.992  -29.383 1.00 29.33  ? 83  GLU   B OE1 1 
ATOM   1418 O  OE2 . GLU   B 1 84 ? 14.149  -3.531  -28.194 1.00 33.72  ? 83  GLU   B OE2 1 
ATOM   1419 N  N   . ILE   B 1 85 ? 13.644  -5.951  -34.493 1.00 27.44  ? 84  ILE   B N   1 
ATOM   1420 C  CA  . ILE   B 1 85 ? 14.340  -6.459  -35.675 1.00 26.40  ? 84  ILE   B CA  1 
ATOM   1421 C  C   . ILE   B 1 85 ? 13.688  -5.938  -36.951 1.00 26.19  ? 84  ILE   B C   1 
ATOM   1422 O  O   . ILE   B 1 85 ? 14.353  -5.805  -37.985 1.00 29.69  ? 84  ILE   B O   1 
ATOM   1423 C  CB  . ILE   B 1 85 ? 14.403  -8.000  -35.655 1.00 27.01  ? 84  ILE   B CB  1 
ATOM   1424 C  CG1 . ILE   B 1 85 ? 15.397  -8.511  -36.706 1.00 24.33  ? 84  ILE   B CG1 1 
ATOM   1425 C  CG2 . ILE   B 1 85 ? 13.021  -8.613  -35.887 1.00 25.35  ? 84  ILE   B CG2 1 
ATOM   1426 C  CD1 . ILE   B 1 85 ? 15.809  -9.963  -36.492 1.00 25.26  ? 84  ILE   B CD1 1 
ATOM   1427 N  N   . GLN   B 1 86 ? 12.396  -5.613  -36.904 1.00 27.63  ? 85  GLN   B N   1 
ATOM   1428 C  CA  . GLN   B 1 86 ? 11.698  -5.117  -38.083 1.00 35.25  ? 85  GLN   B CA  1 
ATOM   1429 C  C   . GLN   B 1 86 ? 11.796  -3.605  -38.237 1.00 34.43  ? 85  GLN   B C   1 
ATOM   1430 O  O   . GLN   B 1 86 ? 11.817  -3.107  -39.369 1.00 34.26  ? 85  GLN   B O   1 
ATOM   1431 C  CB  . GLN   B 1 86 ? 10.223  -5.528  -38.031 1.00 38.35  ? 85  GLN   B CB  1 
ATOM   1432 N  N   . ASN   B 1 87 ? 11.873  -2.864  -37.134 1.00 29.95  ? 86  ASN   B N   1 
ATOM   1433 C  CA  . ASN   B 1 87 ? 11.770  -1.410  -37.184 1.00 33.51  ? 86  ASN   B CA  1 
ATOM   1434 C  C   . ASN   B 1 87 ? 13.084  -0.678  -36.968 1.00 31.12  ? 86  ASN   B C   1 
ATOM   1435 O  O   . ASN   B 1 87 ? 13.258  0.411   -37.517 1.00 33.07  ? 86  ASN   B O   1 
ATOM   1436 C  CB  . ASN   B 1 87 ? 10.748  -0.917  -36.151 1.00 32.00  ? 86  ASN   B CB  1 
ATOM   1437 C  CG  . ASN   B 1 87 ? 9.323   -1.266  -36.536 1.00 42.35  ? 86  ASN   B CG  1 
ATOM   1438 O  OD1 . ASN   B 1 87 ? 8.687   -0.553  -37.314 1.00 48.93  ? 86  ASN   B OD1 1 
ATOM   1439 N  ND2 . ASN   B 1 87 ? 8.815   -2.368  -35.996 1.00 38.18  ? 86  ASN   B ND2 1 
ATOM   1440 N  N   . ASN   B 1 88 ? 14.007  -1.228  -36.186 1.00 26.54  ? 87  ASN   B N   1 
ATOM   1441 C  CA  . ASN   B 1 88 ? 15.307  -0.585  -36.019 1.00 26.53  ? 87  ASN   B CA  1 
ATOM   1442 C  C   . ASN   B 1 88 ? 16.351  -1.620  -35.623 1.00 26.10  ? 87  ASN   B C   1 
ATOM   1443 O  O   . ASN   B 1 88 ? 16.868  -1.588  -34.498 1.00 27.62  ? 87  ASN   B O   1 
ATOM   1444 C  CB  . ASN   B 1 88 ? 15.238  0.533   -34.974 1.00 29.63  ? 87  ASN   B CB  1 
ATOM   1445 C  CG  . ASN   B 1 88 ? 16.259  1.628   -35.226 1.00 31.44  ? 87  ASN   B CG  1 
ATOM   1446 O  OD1 . ASN   B 1 88 ? 17.305  1.396   -35.833 1.00 33.86  ? 87  ASN   B OD1 1 
ATOM   1447 N  ND2 . ASN   B 1 88 ? 15.955  2.835   -34.765 1.00 37.37  ? 87  ASN   B ND2 1 
ATOM   1448 N  N   . PRO   B 1 89 ? 16.695  -2.545  -36.525 1.00 29.27  ? 88  PRO   B N   1 
ATOM   1449 C  CA  . PRO   B 1 89 ? 17.591  -3.647  -36.142 1.00 26.22  ? 88  PRO   B CA  1 
ATOM   1450 C  C   . PRO   B 1 89 ? 19.029  -3.226  -35.890 1.00 24.61  ? 88  PRO   B C   1 
ATOM   1451 O  O   . PRO   B 1 89 ? 19.759  -3.967  -35.225 1.00 25.27  ? 88  PRO   B O   1 
ATOM   1452 C  CB  . PRO   B 1 89 ? 17.497  -4.607  -37.337 1.00 25.48  ? 88  PRO   B CB  1 
ATOM   1453 C  CG  . PRO   B 1 89 ? 17.127  -3.732  -38.496 1.00 23.98  ? 88  PRO   B CG  1 
ATOM   1454 C  CD  . PRO   B 1 89 ? 16.236  -2.659  -37.923 1.00 28.56  ? 88  PRO   B CD  1 
ATOM   1455 N  N   . HIS   B 1 90 ? 19.472  -2.077  -36.398 1.00 24.03  ? 89  HIS   B N   1 
ATOM   1456 C  CA  . HIS   B 1 90 ? 20.875  -1.701  -36.281 1.00 23.16  ? 89  HIS   B CA  1 
ATOM   1457 C  C   . HIS   B 1 90 ? 21.113  -0.612  -35.243 1.00 30.38  ? 89  HIS   B C   1 
ATOM   1458 O  O   . HIS   B 1 90 ? 22.242  -0.125  -35.118 1.00 26.32  ? 89  HIS   B O   1 
ATOM   1459 C  CB  . HIS   B 1 90 ? 21.412  -1.274  -37.651 1.00 25.60  ? 89  HIS   B CB  1 
ATOM   1460 C  CG  . HIS   B 1 90 ? 21.237  -2.323  -38.706 1.00 29.59  ? 89  HIS   B CG  1 
ATOM   1461 N  ND1 . HIS   B 1 90 ? 21.832  -3.564  -38.625 1.00 28.47  ? 89  HIS   B ND1 1 
ATOM   1462 C  CD2 . HIS   B 1 90 ? 20.517  -2.326  -39.853 1.00 26.77  ? 89  HIS   B CD2 1 
ATOM   1463 C  CE1 . HIS   B 1 90 ? 21.493  -4.283  -39.679 1.00 26.64  ? 89  HIS   B CE1 1 
ATOM   1464 N  NE2 . HIS   B 1 90 ? 20.694  -3.557  -40.439 1.00 25.60  ? 89  HIS   B NE2 1 
ATOM   1465 N  N   . ALA   B 1 91 ? 20.092  -0.252  -34.473 1.00 27.57  ? 90  ALA   B N   1 
ATOM   1466 C  CA  . ALA   B 1 91 ? 20.232  0.807   -33.486 1.00 27.76  ? 90  ALA   B CA  1 
ATOM   1467 C  C   . ALA   B 1 91 ? 21.154  0.386   -32.343 1.00 35.23  ? 90  ALA   B C   1 
ATOM   1468 O  O   . ALA   B 1 91 ? 21.428  -0.799  -32.119 1.00 33.93  ? 90  ALA   B O   1 
ATOM   1469 C  CB  . ALA   B 1 91 ? 18.865  1.202   -32.926 1.00 31.30  ? 90  ALA   B CB  1 
ATOM   1470 N  N   . SER   B 1 92 ? 21.647  1.388   -31.621 1.00 37.25  ? 91  SER   B N   1 
ATOM   1471 C  CA  . SER   B 1 92 ? 22.328  1.154   -30.356 1.00 38.90  ? 91  SER   B CA  1 
ATOM   1472 C  C   . SER   B 1 92 ? 21.281  0.959   -29.267 1.00 43.66  ? 91  SER   B C   1 
ATOM   1473 O  O   . SER   B 1 92 ? 20.427  1.826   -29.059 1.00 39.49  ? 91  SER   B O   1 
ATOM   1474 C  CB  . SER   B 1 92 ? 23.250  2.323   -30.016 1.00 47.85  ? 91  SER   B CB  1 
ATOM   1475 O  OG  . SER   B 1 92 ? 23.627  2.283   -28.653 1.00 51.96  ? 91  SER   B OG  1 
ATOM   1476 N  N   . TYR   B 1 93 ? 21.334  -0.180  -28.580 1.00 40.18  ? 92  TYR   B N   1 
ATOM   1477 C  CA  . TYR   B 1 93 ? 20.374  -0.474  -27.528 1.00 41.72  ? 92  TYR   B CA  1 
ATOM   1478 C  C   . TYR   B 1 93 ? 20.971  -0.409  -26.131 1.00 55.60  ? 92  TYR   B C   1 
ATOM   1479 O  O   . TYR   B 1 93 ? 20.223  -0.511  -25.152 1.00 61.58  ? 92  TYR   B O   1 
ATOM   1480 C  CB  . TYR   B 1 93 ? 19.732  -1.849  -27.765 1.00 39.66  ? 92  TYR   B CB  1 
ATOM   1481 C  CG  . TYR   B 1 93 ? 18.728  -1.821  -28.894 1.00 31.34  ? 92  TYR   B CG  1 
ATOM   1482 C  CD1 . TYR   B 1 93 ? 17.441  -1.348  -28.686 1.00 35.30  ? 92  TYR   B CD1 1 
ATOM   1483 C  CD2 . TYR   B 1 93 ? 19.073  -2.245  -30.175 1.00 29.45  ? 92  TYR   B CD2 1 
ATOM   1484 C  CE1 . TYR   B 1 93 ? 16.520  -1.304  -29.715 1.00 35.32  ? 92  TYR   B CE1 1 
ATOM   1485 C  CE2 . TYR   B 1 93 ? 18.155  -2.205  -31.211 1.00 28.69  ? 92  TYR   B CE2 1 
ATOM   1486 C  CZ  . TYR   B 1 93 ? 16.881  -1.735  -30.975 1.00 29.37  ? 92  TYR   B CZ  1 
ATOM   1487 O  OH  . TYR   B 1 93 ? 15.957  -1.691  -31.994 1.00 34.77  ? 92  TYR   B OH  1 
ATOM   1488 N  N   . SER   B 1 94 ? 22.281  -0.230  -26.011 1.00 59.09  ? 93  SER   B N   1 
ATOM   1489 C  CA  . SER   B 1 94 ? 22.894  0.054   -24.724 1.00 64.53  ? 93  SER   B CA  1 
ATOM   1490 C  C   . SER   B 1 94 ? 22.775  1.546   -24.432 1.00 76.81  ? 93  SER   B C   1 
ATOM   1491 O  O   . SER   B 1 94 ? 21.855  1.988   -23.742 1.00 73.84  ? 93  SER   B O   1 
ATOM   1492 C  CB  . SER   B 1 94 ? 24.359  -0.383  -24.710 1.00 71.59  ? 93  SER   B CB  1 
ATOM   1493 O  OG  . SER   B 1 94 ? 25.102  0.293   -25.711 1.00 71.68  ? 93  SER   B OG  1 
ATOM   1494 O  OXT . SER   B 1 94 ? 23.588  2.347   -24.897 1.00 74.32  ? 93  SER   B OXT 1 
ATOM   1495 N  N   . HIS   C 1 4  ? 32.604  -23.262 27.468  1.00 84.35  ? 3   HIS   C N   1 
ATOM   1496 C  CA  . HIS   C 1 4  ? 31.574  -22.660 28.308  1.00 75.49  ? 3   HIS   C CA  1 
ATOM   1497 C  C   . HIS   C 1 4  ? 30.505  -23.673 28.700  1.00 75.73  ? 3   HIS   C C   1 
ATOM   1498 O  O   . HIS   C 1 4  ? 29.816  -24.226 27.842  1.00 78.60  ? 3   HIS   C O   1 
ATOM   1499 C  CB  . HIS   C 1 4  ? 30.925  -21.474 27.593  1.00 85.71  ? 3   HIS   C CB  1 
ATOM   1500 C  CG  . HIS   C 1 4  ? 29.596  -21.082 28.161  1.00 89.05  ? 3   HIS   C CG  1 
ATOM   1501 N  ND1 . HIS   C 1 4  ? 28.401  -21.515 27.626  1.00 95.56  ? 3   HIS   C ND1 1 
ATOM   1502 C  CD2 . HIS   C 1 4  ? 29.272  -20.301 29.219  1.00 84.60  ? 3   HIS   C CD2 1 
ATOM   1503 C  CE1 . HIS   C 1 4  ? 27.400  -21.016 28.328  1.00 92.73  ? 3   HIS   C CE1 1 
ATOM   1504 N  NE2 . HIS   C 1 4  ? 27.901  -20.276 29.301  1.00 84.65  ? 3   HIS   C NE2 1 
ATOM   1505 N  N   . ALA   C 1 5  ? 30.370  -23.910 30.002  1.00 61.78  ? 4   ALA   C N   1 
ATOM   1506 C  CA  . ALA   C 1 5  ? 29.336  -24.810 30.494  1.00 67.60  ? 4   ALA   C CA  1 
ATOM   1507 C  C   . ALA   C 1 5  ? 27.972  -24.137 30.402  1.00 54.04  ? 4   ALA   C C   1 
ATOM   1508 O  O   . ALA   C 1 5  ? 27.798  -22.996 30.840  1.00 59.11  ? 4   ALA   C O   1 
ATOM   1509 C  CB  . ALA   C 1 5  ? 29.632  -25.226 31.935  1.00 50.97  ? 4   ALA   C CB  1 
ATOM   1510 N  N   . PHE   C 1 6  ? 27.006  -24.845 29.829  1.00 55.01  ? 5   PHE   C N   1 
ATOM   1511 C  CA  . PHE   C 1 6  ? 25.679  -24.302 29.594  1.00 56.45  ? 5   PHE   C CA  1 
ATOM   1512 C  C   . PHE   C 1 6  ? 24.812  -24.436 30.846  1.00 58.93  ? 5   PHE   C C   1 
ATOM   1513 O  O   . PHE   C 1 6  ? 25.156  -25.133 31.804  1.00 56.25  ? 5   PHE   C O   1 
ATOM   1514 C  CB  . PHE   C 1 6  ? 25.023  -25.006 28.404  1.00 53.76  ? 5   PHE   C CB  1 
ATOM   1515 C  CG  . PHE   C 1 6  ? 25.829  -24.931 27.132  1.00 55.14  ? 5   PHE   C CG  1 
ATOM   1516 C  CD1 . PHE   C 1 6  ? 25.634  -23.898 26.230  1.00 61.15  ? 5   PHE   C CD1 1 
ATOM   1517 C  CD2 . PHE   C 1 6  ? 26.781  -25.895 26.840  1.00 49.00  ? 5   PHE   C CD2 1 
ATOM   1518 C  CE1 . PHE   C 1 6  ? 26.374  -23.827 25.060  1.00 54.57  ? 5   PHE   C CE1 1 
ATOM   1519 C  CE2 . PHE   C 1 6  ? 27.524  -25.830 25.673  1.00 44.34  ? 5   PHE   C CE2 1 
ATOM   1520 C  CZ  . PHE   C 1 6  ? 27.320  -24.796 24.782  1.00 37.90  ? 5   PHE   C CZ  1 
ATOM   1521 N  N   . LYS   C 1 7  ? 23.674  -23.754 30.824  1.00 55.98  ? 6   LYS   C N   1 
ATOM   1522 C  CA  . LYS   C 1 7  ? 22.704  -23.744 31.906  1.00 55.87  ? 6   LYS   C CA  1 
ATOM   1523 C  C   . LYS   C 1 7  ? 21.328  -24.057 31.340  1.00 50.23  ? 6   LYS   C C   1 
ATOM   1524 O  O   . LYS   C 1 7  ? 21.083  -23.853 30.147  1.00 41.13  ? 6   LYS   C O   1 
ATOM   1525 C  CB  . LYS   C 1 7  ? 22.683  -22.381 32.617  1.00 52.45  ? 6   LYS   C CB  1 
ATOM   1526 C  CG  . LYS   C 1 7  ? 21.997  -21.278 31.824  1.00 63.70  ? 6   LYS   C CG  1 
ATOM   1527 C  CD  . LYS   C 1 7  ? 22.401  -19.900 32.329  1.00 67.85  ? 6   LYS   C CD  1 
ATOM   1528 C  CE  . LYS   C 1 7  ? 21.678  -18.787 31.577  1.00 67.08  ? 6   LYS   C CE  1 
ATOM   1529 N  NZ  . LYS   C 1 7  ? 22.012  -18.751 30.123  1.00 66.54  ? 6   LYS   C NZ  1 
ATOM   1530 N  N   . PRO   C 1 8  ? 20.401  -24.576 32.172  1.00 53.47  ? 7   PRO   C N   1 
ATOM   1531 C  CA  . PRO   C 1 8  ? 19.054  -24.897 31.671  1.00 52.89  ? 7   PRO   C CA  1 
ATOM   1532 C  C   . PRO   C 1 8  ? 18.380  -23.737 30.953  1.00 55.34  ? 7   PRO   C C   1 
ATOM   1533 O  O   . PRO   C 1 8  ? 18.225  -22.652 31.522  1.00 54.64  ? 7   PRO   C O   1 
ATOM   1534 C  CB  . PRO   C 1 8  ? 18.292  -25.276 32.948  1.00 52.24  ? 7   PRO   C CB  1 
ATOM   1535 C  CG  . PRO   C 1 8  ? 19.342  -25.805 33.855  1.00 52.91  ? 7   PRO   C CG  1 
ATOM   1536 C  CD  . PRO   C 1 8  ? 20.574  -24.987 33.578  1.00 47.97  ? 7   PRO   C CD  1 
ATOM   1537 N  N   . GLY   C 1 9  ? 17.985  -23.953 29.698  1.00 57.30  ? 8   GLY   C N   1 
ATOM   1538 C  CA  . GLY   C 1 9  ? 17.351  -22.938 28.882  1.00 54.52  ? 8   GLY   C CA  1 
ATOM   1539 C  C   . GLY   C 1 9  ? 18.188  -22.456 27.715  1.00 47.59  ? 8   GLY   C C   1 
ATOM   1540 O  O   . GLY   C 1 9  ? 17.627  -21.910 26.757  1.00 50.53  ? 8   GLY   C O   1 
ATOM   1541 N  N   . ASP   C 1 10 ? 19.507  -22.637 27.767  1.00 44.99  ? 9   ASP   C N   1 
ATOM   1542 C  CA  . ASP   C 1 10 ? 20.369  -22.179 26.685  1.00 33.65  ? 9   ASP   C CA  1 
ATOM   1543 C  C   . ASP   C 1 10 ? 20.058  -22.932 25.398  1.00 45.41  ? 9   ASP   C C   1 
ATOM   1544 O  O   . ASP   C 1 10 ? 19.757  -24.128 25.418  1.00 44.64  ? 9   ASP   C O   1 
ATOM   1545 C  CB  . ASP   C 1 10 ? 21.840  -22.373 27.056  1.00 45.73  ? 9   ASP   C CB  1 
ATOM   1546 C  CG  . ASP   C 1 10 ? 22.229  -21.631 28.317  1.00 60.09  ? 9   ASP   C CG  1 
ATOM   1547 O  OD1 . ASP   C 1 10 ? 21.514  -20.678 28.693  1.00 61.09  ? 9   ASP   C OD1 1 
ATOM   1548 O  OD2 . ASP   C 1 10 ? 23.256  -22.001 28.929  1.00 43.78  ? 9   ASP   C OD2 1 
ATOM   1549 N  N   . LEU   C 1 11 ? 20.139  -22.226 24.275  1.00 39.69  ? 10  LEU   C N   1 
ATOM   1550 C  CA  . LEU   C 1 11 ? 19.843  -22.792 22.965  1.00 44.97  ? 10  LEU   C CA  1 
ATOM   1551 C  C   . LEU   C 1 11 ? 21.133  -23.193 22.264  1.00 48.54  ? 10  LEU   C C   1 
ATOM   1552 O  O   . LEU   C 1 11 ? 22.117  -22.447 22.277  1.00 42.09  ? 10  LEU   C O   1 
ATOM   1553 C  CB  . LEU   C 1 11 ? 19.075  -21.789 22.104  1.00 38.65  ? 10  LEU   C CB  1 
ATOM   1554 C  CG  . LEU   C 1 11 ? 17.915  -21.082 22.802  1.00 40.50  ? 10  LEU   C CG  1 
ATOM   1555 C  CD1 . LEU   C 1 11 ? 17.273  -20.095 21.846  1.00 46.86  ? 10  LEU   C CD1 1 
ATOM   1556 C  CD2 . LEU   C 1 11 ? 16.894  -22.086 23.324  1.00 40.32  ? 10  LEU   C CD2 1 
ATOM   1557 N  N   . VAL   C 1 12 ? 21.125  -24.376 21.645  1.00 37.68  ? 11  VAL   C N   1 
ATOM   1558 C  CA  . VAL   C 1 12 ? 22.319  -24.957 21.044  1.00 38.74  ? 11  VAL   C CA  1 
ATOM   1559 C  C   . VAL   C 1 12 ? 21.942  -25.706 19.772  1.00 37.80  ? 11  VAL   C C   1 
ATOM   1560 O  O   . VAL   C 1 12 ? 20.768  -25.933 19.474  1.00 36.55  ? 11  VAL   C O   1 
ATOM   1561 C  CB  . VAL   C 1 12 ? 23.048  -25.927 22.004  1.00 37.61  ? 11  VAL   C CB  1 
ATOM   1562 C  CG1 . VAL   C 1 12 ? 23.572  -25.203 23.238  1.00 44.21  ? 11  VAL   C CG1 1 
ATOM   1563 C  CG2 . VAL   C 1 12 ? 22.121  -27.069 22.395  1.00 37.36  ? 11  VAL   C CG2 1 
ATOM   1564 N  N   . PHE   C 1 13 ? 22.971  -26.086 19.019  1.00 32.62  ? 12  PHE   C N   1 
ATOM   1565 C  CA  . PHE   C 1 13 ? 22.898  -27.211 18.098  1.00 29.40  ? 12  PHE   C CA  1 
ATOM   1566 C  C   . PHE   C 1 13 ? 23.564  -28.405 18.769  1.00 33.22  ? 12  PHE   C C   1 
ATOM   1567 O  O   . PHE   C 1 13 ? 24.709  -28.305 19.222  1.00 36.32  ? 12  PHE   C O   1 
ATOM   1568 C  CB  . PHE   C 1 13 ? 23.584  -26.904 16.765  1.00 31.93  ? 12  PHE   C CB  1 
ATOM   1569 C  CG  . PHE   C 1 13 ? 22.840  -25.919 15.911  1.00 34.05  ? 12  PHE   C CG  1 
ATOM   1570 C  CD1 . PHE   C 1 13 ? 21.805  -26.337 15.091  1.00 32.43  ? 12  PHE   C CD1 1 
ATOM   1571 C  CD2 . PHE   C 1 13 ? 23.182  -24.579 15.919  1.00 42.89  ? 12  PHE   C CD2 1 
ATOM   1572 C  CE1 . PHE   C 1 13 ? 21.120  -25.436 14.300  1.00 34.12  ? 12  PHE   C CE1 1 
ATOM   1573 C  CE2 . PHE   C 1 13 ? 22.498  -23.674 15.133  1.00 42.46  ? 12  PHE   C CE2 1 
ATOM   1574 C  CZ  . PHE   C 1 13 ? 21.466  -24.104 14.322  1.00 37.48  ? 12  PHE   C CZ  1 
ATOM   1575 N  N   . ALA   C 1 14 ? 22.847  -29.525 18.840  1.00 27.55  ? 13  ALA   C N   1 
ATOM   1576 C  CA  . ALA   C 1 14 ? 23.318  -30.720 19.527  1.00 26.86  ? 13  ALA   C CA  1 
ATOM   1577 C  C   . ALA   C 1 14 ? 23.539  -31.822 18.502  1.00 30.92  ? 13  ALA   C C   1 
ATOM   1578 O  O   . ALA   C 1 14 ? 22.659  -32.087 17.680  1.00 25.79  ? 13  ALA   C O   1 
ATOM   1579 C  CB  . ALA   C 1 14 ? 22.315  -31.174 20.591  1.00 28.35  ? 13  ALA   C CB  1 
ATOM   1580 N  N   . LYS   C 1 15 ? 24.711  -32.461 18.554  1.00 26.64  ? 14  LYS   C N   1 
ATOM   1581 C  CA  . LYS   C 1 15 ? 25.101  -33.482 17.585  1.00 28.97  ? 14  LYS   C CA  1 
ATOM   1582 C  C   . LYS   C 1 15 ? 25.055  -34.850 18.254  1.00 32.78  ? 14  LYS   C C   1 
ATOM   1583 O  O   . LYS   C 1 15 ? 25.838  -35.130 19.167  1.00 32.05  ? 14  LYS   C O   1 
ATOM   1584 C  CB  . LYS   C 1 15 ? 26.492  -33.197 17.023  1.00 34.43  ? 14  LYS   C CB  1 
ATOM   1585 C  CG  . LYS   C 1 15 ? 26.963  -34.210 15.995  1.00 35.15  ? 14  LYS   C CG  1 
ATOM   1586 C  CD  . LYS   C 1 15 ? 26.181  -34.091 14.695  1.00 30.28  ? 14  LYS   C CD  1 
ATOM   1587 C  CE  . LYS   C 1 15 ? 26.675  -35.100 13.664  1.00 33.53  ? 14  LYS   C CE  1 
ATOM   1588 N  NZ  . LYS   C 1 15 ? 26.227  -36.484 13.987  1.00 35.84  ? 14  LYS   C NZ  1 
ATOM   1589 N  N   . MET   C 1 16 ? 24.133  -35.693 17.802  1.00 26.20  ? 15  MET   C N   1 
ATOM   1590 C  CA  . MET   C 1 16 ? 24.074  -37.088 18.197  1.00 27.41  ? 15  MET   C CA  1 
ATOM   1591 C  C   . MET   C 1 16 ? 24.541  -37.953 17.036  1.00 32.46  ? 15  MET   C C   1 
ATOM   1592 O  O   . MET   C 1 16 ? 24.390  -37.584 15.870  1.00 28.22  ? 15  MET   C O   1 
ATOM   1593 C  CB  . MET   C 1 16 ? 22.657  -37.504 18.598  1.00 32.42  ? 15  MET   C CB  1 
ATOM   1594 C  CG  . MET   C 1 16 ? 22.134  -36.876 19.873  1.00 49.84  ? 15  MET   C CG  1 
ATOM   1595 S  SD  . MET   C 1 16 ? 20.828  -37.890 20.596  1.00 57.69  ? 15  MET   C SD  1 
ATOM   1596 C  CE  . MET   C 1 16 ? 21.730  -39.399 20.940  1.00 53.08  ? 15  MET   C CE  1 
ATOM   1597 N  N   . LYS   C 1 17 ? 25.111  -39.108 17.363  1.00 32.10  ? 16  LYS   C N   1 
ATOM   1598 C  CA  . LYS   C 1 17 ? 25.471  -40.061 16.325  1.00 32.01  ? 16  LYS   C CA  1 
ATOM   1599 C  C   . LYS   C 1 17 ? 24.222  -40.477 15.560  1.00 26.17  ? 16  LYS   C C   1 
ATOM   1600 O  O   . LYS   C 1 17 ? 23.209  -40.850 16.160  1.00 30.54  ? 16  LYS   C O   1 
ATOM   1601 C  CB  . LYS   C 1 17 ? 26.152  -41.282 16.947  1.00 32.11  ? 16  LYS   C CB  1 
ATOM   1602 C  CG  . LYS   C 1 17 ? 26.803  -42.221 15.940  1.00 32.36  ? 16  LYS   C CG  1 
ATOM   1603 C  CD  . LYS   C 1 17 ? 28.057  -41.613 15.334  1.00 39.31  ? 16  LYS   C CD  1 
ATOM   1604 C  CE  . LYS   C 1 17 ? 28.666  -42.539 14.290  1.00 48.26  ? 16  LYS   C CE  1 
ATOM   1605 N  NZ  . LYS   C 1 17 ? 29.843  -41.921 13.617  1.00 43.21  ? 16  LYS   C NZ  1 
ATOM   1606 N  N   . GLY   C 1 18 ? 24.292  -40.393 14.234  1.00 30.76  ? 17  GLY   C N   1 
ATOM   1607 C  CA  . GLY   C 1 18 ? 23.188  -40.761 13.372  1.00 27.54  ? 17  GLY   C CA  1 
ATOM   1608 C  C   . GLY   C 1 18 ? 22.270  -39.625 12.968  1.00 30.44  ? 17  GLY   C C   1 
ATOM   1609 O  O   . GLY   C 1 18 ? 21.287  -39.872 12.255  1.00 30.46  ? 17  GLY   C O   1 
ATOM   1610 N  N   . TYR   C 1 19 ? 22.553  -38.397 13.393  1.00 29.49  ? 18  TYR   C N   1 
ATOM   1611 C  CA  . TYR   C 1 19 ? 21.705  -37.247 13.109  1.00 29.03  ? 18  TYR   C CA  1 
ATOM   1612 C  C   . TYR   C 1 19 ? 22.565  -36.035 12.796  1.00 28.94  ? 18  TYR   C C   1 
ATOM   1613 O  O   . TYR   C 1 19 ? 23.700  -35.936 13.276  1.00 28.31  ? 18  TYR   C O   1 
ATOM   1614 C  CB  . TYR   C 1 19 ? 20.787  -36.924 14.299  1.00 27.29  ? 18  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   C 1 19 ? 19.876  -38.067 14.677  1.00 31.09  ? 18  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   C 1 19 ? 18.651  -38.235 14.050  1.00 34.29  ? 18  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   C 1 19 ? 20.245  -38.983 15.655  1.00 36.18  ? 18  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   C 1 19 ? 17.815  -39.279 14.386  1.00 37.78  ? 18  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   C 1 19 ? 19.415  -40.031 15.999  1.00 36.20  ? 18  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   C 1 19 ? 18.199  -40.172 15.362  1.00 41.97  ? 18  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   C 1 19 ? 17.365  -41.212 15.697  1.00 48.79  ? 18  TYR   C OH  1 
ATOM   1622 N  N   . PRO   C 1 20 ? 22.053  -35.098 12.001  1.00 29.26  ? 19  PRO   C N   1 
ATOM   1623 C  CA  . PRO   C 1 20 ? 22.781  -33.849 11.773  1.00 29.92  ? 19  PRO   C CA  1 
ATOM   1624 C  C   . PRO   C 1 20 ? 22.709  -32.955 13.000  1.00 31.37  ? 19  PRO   C C   1 
ATOM   1625 O  O   . PRO   C 1 20 ? 21.948  -33.191 13.941  1.00 27.29  ? 19  PRO   C O   1 
ATOM   1626 C  CB  . PRO   C 1 20 ? 22.049  -33.225 10.583  1.00 39.11  ? 19  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   C 1 20 ? 20.652  -33.726 10.727  1.00 30.56  ? 19  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   C 1 20 ? 20.772  -35.129 11.275  1.00 28.86  ? 19  PRO   C CD  1 
ATOM   1629 N  N   . HIS   C 1 21 ? 23.524  -31.908 12.984  1.00 28.91  ? 20  HIS   C N   1 
ATOM   1630 C  CA  . HIS   C 1 21 ? 23.488  -30.946 14.075  1.00 26.54  ? 20  HIS   C CA  1 
ATOM   1631 C  C   . HIS   C 1 21 ? 22.079  -30.391 14.210  1.00 27.07  ? 20  HIS   C C   1 
ATOM   1632 O  O   . HIS   C 1 21 ? 21.515  -29.863 13.245  1.00 30.77  ? 20  HIS   C O   1 
ATOM   1633 C  CB  . HIS   C 1 21 ? 24.499  -29.831 13.830  1.00 35.41  ? 20  HIS   C CB  1 
ATOM   1634 C  CG  . HIS   C 1 21 ? 25.920  -30.300 13.832  1.00 37.24  ? 20  HIS   C CG  1 
ATOM   1635 N  ND1 . HIS   C 1 21 ? 26.452  -31.069 12.818  1.00 41.91  ? 20  HIS   C ND1 1 
ATOM   1636 C  CD2 . HIS   C 1 21 ? 26.918  -30.118 14.730  1.00 45.28  ? 20  HIS   C CD2 1 
ATOM   1637 C  CE1 . HIS   C 1 21 ? 27.717  -31.334 13.089  1.00 39.63  ? 20  HIS   C CE1 1 
ATOM   1638 N  NE2 . HIS   C 1 21 ? 28.025  -30.771 14.243  1.00 40.36  ? 20  HIS   C NE2 1 
ATOM   1639 N  N   . TRP   C 1 22 ? 21.506  -30.531 15.404  1.00 25.55  ? 21  TRP   C N   1 
ATOM   1640 C  CA  . TRP   C 1 22 ? 20.077  -30.367 15.606  1.00 28.19  ? 21  TRP   C CA  1 
ATOM   1641 C  C   . TRP   C 1 22 ? 19.783  -29.188 16.523  1.00 26.87  ? 21  TRP   C C   1 
ATOM   1642 O  O   . TRP   C 1 22 ? 20.408  -29.065 17.587  1.00 28.30  ? 21  TRP   C O   1 
ATOM   1643 C  CB  . TRP   C 1 22 ? 19.482  -31.647 16.211  1.00 24.06  ? 21  TRP   C CB  1 
ATOM   1644 C  CG  . TRP   C 1 22 ? 18.044  -31.844 15.906  1.00 26.14  ? 21  TRP   C CG  1 
ATOM   1645 C  CD1 . TRP   C 1 22 ? 16.980  -31.234 16.508  1.00 27.71  ? 21  TRP   C CD1 1 
ATOM   1646 C  CD2 . TRP   C 1 22 ? 17.498  -32.722 14.919  1.00 27.41  ? 21  TRP   C CD2 1 
ATOM   1647 N  NE1 . TRP   C 1 22 ? 15.805  -31.680 15.951  1.00 27.55  ? 21  TRP   C NE1 1 
ATOM   1648 C  CE2 . TRP   C 1 22 ? 16.097  -32.594 14.974  1.00 32.81  ? 21  TRP   C CE2 1 
ATOM   1649 C  CE3 . TRP   C 1 22 ? 18.060  -33.609 13.996  1.00 23.92  ? 21  TRP   C CE3 1 
ATOM   1650 C  CZ2 . TRP   C 1 22 ? 15.250  -33.318 14.137  1.00 31.55  ? 21  TRP   C CZ2 1 
ATOM   1651 C  CZ3 . TRP   C 1 22 ? 17.218  -34.321 13.166  1.00 32.69  ? 21  TRP   C CZ3 1 
ATOM   1652 C  CH2 . TRP   C 1 22 ? 15.829  -34.172 13.244  1.00 27.85  ? 21  TRP   C CH2 1 
ATOM   1653 N  N   . PRO   C 1 23 ? 18.837  -28.318 16.170  1.00 29.94  ? 22  PRO   C N   1 
ATOM   1654 C  CA  . PRO   C 1 23 ? 18.437  -27.250 17.097  1.00 31.80  ? 22  PRO   C CA  1 
ATOM   1655 C  C   . PRO   C 1 23 ? 17.885  -27.836 18.391  1.00 26.70  ? 22  PRO   C C   1 
ATOM   1656 O  O   . PRO   C 1 23 ? 17.021  -28.715 18.380  1.00 25.87  ? 22  PRO   C O   1 
ATOM   1657 C  CB  . PRO   C 1 23 ? 17.364  -26.481 16.312  1.00 27.88  ? 22  PRO   C CB  1 
ATOM   1658 C  CG  . PRO   C 1 23 ? 16.862  -27.465 15.291  1.00 25.45  ? 22  PRO   C CG  1 
ATOM   1659 C  CD  . PRO   C 1 23 ? 18.052  -28.298 14.924  1.00 27.83  ? 22  PRO   C CD  1 
ATOM   1660 N  N   . ALA   C 1 24 ? 18.399  -27.350 19.517  1.00 29.54  ? 23  ALA   C N   1 
ATOM   1661 C  CA  . ALA   C 1 24 ? 18.066  -27.956 20.798  1.00 33.78  ? 23  ALA   C CA  1 
ATOM   1662 C  C   . ALA   C 1 24 ? 18.286  -26.936 21.904  1.00 39.47  ? 23  ALA   C C   1 
ATOM   1663 O  O   . ALA   C 1 24 ? 18.774  -25.828 21.669  1.00 33.57  ? 23  ALA   C O   1 
ATOM   1664 C  CB  . ALA   C 1 24 ? 18.898  -29.216 21.051  1.00 31.63  ? 23  ALA   C CB  1 
ATOM   1665 N  N   . ARG   C 1 25 ? 17.918  -27.336 23.122  1.00 39.71  ? 24  ARG   C N   1 
ATOM   1666 C  CA  . ARG   C 1 25 ? 18.102  -26.506 24.302  1.00 39.12  ? 24  ARG   C CA  1 
ATOM   1667 C  C   . ARG   C 1 25 ? 18.490  -27.380 25.486  1.00 33.82  ? 24  ARG   C C   1 
ATOM   1668 O  O   . ARG   C 1 25 ? 18.250  -28.591 25.503  1.00 34.02  ? 24  ARG   C O   1 
ATOM   1669 C  CB  . ARG   C 1 25 ? 16.838  -25.707 24.644  1.00 37.93  ? 24  ARG   C CB  1 
ATOM   1670 C  CG  . ARG   C 1 25 ? 15.729  -26.541 25.252  1.00 42.62  ? 24  ARG   C CG  1 
ATOM   1671 C  CD  . ARG   C 1 25 ? 14.593  -25.653 25.721  1.00 52.83  ? 24  ARG   C CD  1 
ATOM   1672 N  NE  . ARG   C 1 25 ? 13.430  -26.425 26.139  1.00 45.54  ? 24  ARG   C NE  1 
ATOM   1673 C  CZ  . ARG   C 1 25 ? 12.177  -26.016 25.998  1.00 61.10  ? 24  ARG   C CZ  1 
ATOM   1674 N  NH1 . ARG   C 1 25 ? 11.890  -24.856 25.430  1.00 51.97  ? 24  ARG   C NH1 1 
ATOM   1675 N  NH2 . ARG   C 1 25 ? 11.187  -26.796 26.424  1.00 59.02  ? 24  ARG   C NH2 1 
ATOM   1676 N  N   . ILE   C 1 26 ? 19.096  -26.739 26.479  1.00 39.02  ? 25  ILE   C N   1 
ATOM   1677 C  CA  . ILE   C 1 26 ? 19.466  -27.399 27.726  1.00 40.47  ? 25  ILE   C CA  1 
ATOM   1678 C  C   . ILE   C 1 26 ? 18.247  -27.482 28.633  1.00 46.78  ? 25  ILE   C C   1 
ATOM   1679 O  O   . ILE   C 1 26 ? 17.485  -26.516 28.766  1.00 44.33  ? 25  ILE   C O   1 
ATOM   1680 C  CB  . ILE   C 1 26 ? 20.616  -26.641 28.412  1.00 42.92  ? 25  ILE   C CB  1 
ATOM   1681 C  CG1 . ILE   C 1 26 ? 21.761  -26.401 27.428  1.00 37.05  ? 25  ILE   C CG1 1 
ATOM   1682 C  CG2 . ILE   C 1 26 ? 21.104  -27.401 29.637  1.00 47.33  ? 25  ILE   C CG2 1 
ATOM   1683 C  CD1 . ILE   C 1 26 ? 22.445  -27.669 26.957  1.00 46.50  ? 25  ILE   C CD1 1 
ATOM   1684 N  N   . ASP   C 1 27 ? 18.056  -28.635 29.262  1.00 46.41  ? 26  ASP   C N   1 
ATOM   1685 C  CA  . ASP   C 1 27 ? 16.960  -28.846 30.194  1.00 55.19  ? 26  ASP   C CA  1 
ATOM   1686 C  C   . ASP   C 1 27 ? 17.484  -28.875 31.627  1.00 58.79  ? 26  ASP   C C   1 
ATOM   1687 O  O   . ASP   C 1 27 ? 18.690  -28.802 31.884  1.00 63.17  ? 26  ASP   C O   1 
ATOM   1688 C  CB  . ASP   C 1 27 ? 16.201  -30.131 29.856  1.00 48.97  ? 26  ASP   C CB  1 
ATOM   1689 C  CG  . ASP   C 1 27 ? 14.960  -29.872 29.023  1.00 56.89  ? 26  ASP   C CG  1 
ATOM   1690 O  OD1 . ASP   C 1 27 ? 14.878  -28.798 28.391  1.00 54.87  ? 26  ASP   C OD1 1 
ATOM   1691 O  OD2 . ASP   C 1 27 ? 14.059  -30.738 29.010  1.00 62.27  ? 26  ASP   C OD2 1 
ATOM   1692 N  N   . ASP   C 1 28 ? 16.547  -28.983 32.566  1.00 71.70  ? 27  ASP   C N   1 
ATOM   1693 C  CA  . ASP   C 1 28 ? 16.827  -28.980 33.998  1.00 78.45  ? 27  ASP   C CA  1 
ATOM   1694 C  C   . ASP   C 1 28 ? 16.289  -30.284 34.574  1.00 86.90  ? 27  ASP   C C   1 
ATOM   1695 O  O   . ASP   C 1 28 ? 15.070  -30.483 34.625  1.00 88.84  ? 27  ASP   C O   1 
ATOM   1696 C  CB  . ASP   C 1 28 ? 16.182  -27.762 34.667  1.00 83.82  ? 27  ASP   C CB  1 
ATOM   1697 C  CG  . ASP   C 1 28 ? 16.754  -27.459 36.048  1.00 89.78  ? 27  ASP   C CG  1 
ATOM   1698 O  OD1 . ASP   C 1 28 ? 17.577  -28.244 36.558  1.00 87.73  ? 27  ASP   C OD1 1 
ATOM   1699 O  OD2 . ASP   C 1 28 ? 16.372  -26.418 36.626  1.00 77.06  ? 27  ASP   C OD2 1 
ATOM   1700 N  N   . ILE   C 1 29 ? 17.186  -31.184 34.987  1.00 86.83  ? 28  ILE   C N   1 
ATOM   1701 C  CA  . ILE   C 1 29 ? 16.737  -32.425 35.607  1.00 90.01  ? 28  ILE   C CA  1 
ATOM   1702 C  C   . ILE   C 1 29 ? 16.062  -32.102 36.931  1.00 93.91  ? 28  ILE   C C   1 
ATOM   1703 O  O   . ILE   C 1 29 ? 16.548  -31.275 37.714  1.00 93.66  ? 28  ILE   C O   1 
ATOM   1704 C  CB  . ILE   C 1 29 ? 17.893  -33.418 35.821  1.00 92.03  ? 28  ILE   C CB  1 
ATOM   1705 C  CG1 . ILE   C 1 29 ? 19.210  -32.871 35.281  1.00 88.06  ? 28  ILE   C CG1 1 
ATOM   1706 C  CG2 . ILE   C 1 29 ? 17.565  -34.772 35.196  1.00 88.13  ? 28  ILE   C CG2 1 
ATOM   1707 C  CD1 . ILE   C 1 29 ? 20.368  -33.110 36.212  1.00 94.01  ? 28  ILE   C CD1 1 
ATOM   1708 N  N   . ALA   C 1 30 ? 14.929  -32.751 37.184  1.00 99.42  ? 29  ALA   C N   1 
ATOM   1709 C  CA  . ALA   C 1 30 ? 14.262  -32.604 38.467  1.00 98.15  ? 29  ALA   C CA  1 
ATOM   1710 C  C   . ALA   C 1 30 ? 15.142  -33.153 39.583  1.00 98.20  ? 29  ALA   C C   1 
ATOM   1711 O  O   . ALA   C 1 30 ? 15.901  -34.108 39.394  1.00 90.73  ? 29  ALA   C O   1 
ATOM   1712 C  CB  . ALA   C 1 30 ? 12.914  -33.325 38.457  1.00 83.37  ? 29  ALA   C CB  1 
ATOM   1713 N  N   . ASP   C 1 31 ? 15.038  -32.529 40.759  1.00 97.47  ? 30  ASP   C N   1 
ATOM   1714 C  CA  . ASP   C 1 31 ? 15.836  -32.968 41.900  1.00 94.89  ? 30  ASP   C CA  1 
ATOM   1715 C  C   . ASP   C 1 31 ? 15.523  -34.410 42.281  1.00 93.68  ? 30  ASP   C C   1 
ATOM   1716 O  O   . ASP   C 1 31 ? 16.407  -35.130 42.760  1.00 94.91  ? 30  ASP   C O   1 
ATOM   1717 C  CB  . ASP   C 1 31 ? 15.606  -32.035 43.088  1.00 77.61  ? 30  ASP   C CB  1 
ATOM   1718 C  CG  . ASP   C 1 31 ? 16.731  -32.091 44.100  1.00 84.91  ? 30  ASP   C CG  1 
ATOM   1719 O  OD1 . ASP   C 1 31 ? 17.870  -31.725 43.742  1.00 89.49  ? 30  ASP   C OD1 1 
ATOM   1720 O  OD2 . ASP   C 1 31 ? 16.478  -32.495 45.254  1.00 83.05  ? 30  ASP   C OD2 1 
ATOM   1721 N  N   . GLY   C 1 32 ? 14.278  -34.849 42.075  1.00 84.23  ? 31  GLY   C N   1 
ATOM   1722 C  CA  . GLY   C 1 32 ? 13.930  -36.229 42.360  1.00 76.72  ? 31  GLY   C CA  1 
ATOM   1723 C  C   . GLY   C 1 32 ? 14.275  -37.186 41.242  1.00 85.76  ? 31  GLY   C C   1 
ATOM   1724 O  O   . GLY   C 1 32 ? 14.446  -38.385 41.485  1.00 74.48  ? 31  GLY   C O   1 
ATOM   1725 N  N   . ALA   C 1 33 ? 14.384  -36.681 40.016  1.00 94.74  ? 32  ALA   C N   1 
ATOM   1726 C  CA  . ALA   C 1 33 ? 14.721  -37.526 38.884  1.00 93.03  ? 32  ALA   C CA  1 
ATOM   1727 C  C   . ALA   C 1 33 ? 16.177  -37.975 38.966  1.00 96.79  ? 32  ALA   C C   1 
ATOM   1728 O  O   . ALA   C 1 33 ? 17.000  -37.391 39.676  1.00 99.05  ? 32  ALA   C O   1 
ATOM   1729 C  CB  . ALA   C 1 33 ? 14.468  -36.788 37.570  1.00 91.82  ? 32  ALA   C CB  1 
ATOM   1730 N  N   . VAL   C 1 34 ? 16.487  -39.042 38.229  1.00 96.90  ? 33  VAL   C N   1 
ATOM   1731 C  CA  . VAL   C 1 34 ? 17.846  -39.564 38.226  1.00 99.84  ? 33  VAL   C CA  1 
ATOM   1732 C  C   . VAL   C 1 34 ? 18.754  -38.613 37.452  1.00 97.60  ? 33  VAL   C C   1 
ATOM   1733 O  O   . VAL   C 1 34 ? 18.334  -37.947 36.495  1.00 91.37  ? 33  VAL   C O   1 
ATOM   1734 C  CB  . VAL   C 1 34 ? 17.887  -40.990 37.643  1.00 94.02  ? 33  VAL   C CB  1 
ATOM   1735 C  CG1 . VAL   C 1 34 ? 17.649  -40.973 36.138  1.00 89.06  ? 33  VAL   C CG1 1 
ATOM   1736 C  CG2 . VAL   C 1 34 ? 19.204  -41.673 37.985  1.00 88.94  ? 33  VAL   C CG2 1 
ATOM   1737 N  N   . LYS   C 1 35 ? 20.007  -38.535 37.884  1.00 96.89  ? 34  LYS   C N   1 
ATOM   1738 C  CA  . LYS   C 1 35 ? 20.963  -37.596 37.325  1.00 91.37  ? 34  LYS   C CA  1 
ATOM   1739 C  C   . LYS   C 1 35 ? 21.598  -38.155 36.053  1.00 77.06  ? 34  LYS   C C   1 
ATOM   1740 O  O   . LYS   C 1 35 ? 21.562  -39.364 35.808  1.00 78.52  ? 34  LYS   C O   1 
ATOM   1741 C  CB  . LYS   C 1 35 ? 22.031  -37.272 38.367  1.00 91.77  ? 34  LYS   C CB  1 
ATOM   1742 C  CG  . LYS   C 1 35 ? 21.499  -36.498 39.563  1.00 101.99 ? 34  LYS   C CG  1 
ATOM   1743 C  CD  . LYS   C 1 35 ? 22.507  -35.472 40.052  1.00 105.99 ? 34  LYS   C CD  1 
ATOM   1744 C  CE  . LYS   C 1 35 ? 22.776  -34.416 38.990  1.00 103.69 ? 34  LYS   C CE  1 
ATOM   1745 N  NZ  . LYS   C 1 35 ? 23.782  -33.415 39.442  1.00 106.48 ? 34  LYS   C NZ  1 
ATOM   1746 N  N   . PRO   C 1 36 ? 22.179  -37.294 35.220  1.00 67.30  ? 35  PRO   C N   1 
ATOM   1747 C  CA  . PRO   C 1 36 ? 22.790  -37.765 33.976  1.00 64.93  ? 35  PRO   C CA  1 
ATOM   1748 C  C   . PRO   C 1 36 ? 24.028  -38.592 34.264  1.00 69.12  ? 35  PRO   C C   1 
ATOM   1749 O  O   . PRO   C 1 36 ? 24.498  -38.644 35.411  1.00 60.40  ? 35  PRO   C O   1 
ATOM   1750 C  CB  . PRO   C 1 36 ? 23.161  -36.462 33.244  1.00 59.01  ? 35  PRO   C CB  1 
ATOM   1751 C  CG  . PRO   C 1 36 ? 22.435  -35.373 33.958  1.00 61.91  ? 35  PRO   C CG  1 
ATOM   1752 C  CD  . PRO   C 1 36 ? 22.315  -35.836 35.365  1.00 77.35  ? 35  PRO   C CD  1 
ATOM   1753 N  N   . PRO   C 1 37 ? 24.585  -39.256 33.256  1.00 59.28  ? 36  PRO   C N   1 
ATOM   1754 C  CA  . PRO   C 1 37 ? 25.951  -39.757 33.374  1.00 53.78  ? 36  PRO   C CA  1 
ATOM   1755 C  C   . PRO   C 1 37 ? 26.898  -38.610 33.677  1.00 55.41  ? 36  PRO   C C   1 
ATOM   1756 O  O   . PRO   C 1 37 ? 26.567  -37.442 33.417  1.00 47.68  ? 36  PRO   C O   1 
ATOM   1757 C  CB  . PRO   C 1 37 ? 26.228  -40.366 31.991  1.00 56.46  ? 36  PRO   C CB  1 
ATOM   1758 C  CG  . PRO   C 1 37 ? 24.881  -40.725 31.468  1.00 56.86  ? 36  PRO   C CG  1 
ATOM   1759 C  CD  . PRO   C 1 37 ? 23.949  -39.668 31.991  1.00 54.09  ? 36  PRO   C CD  1 
ATOM   1760 N  N   . PRO   C 1 38 ? 28.067  -38.893 34.247  1.00 52.30  ? 37  PRO   C N   1 
ATOM   1761 C  CA  . PRO   C 1 38 ? 29.010  -37.815 34.569  1.00 44.54  ? 37  PRO   C CA  1 
ATOM   1762 C  C   . PRO   C 1 38 ? 29.315  -36.945 33.358  1.00 47.12  ? 37  PRO   C C   1 
ATOM   1763 O  O   . PRO   C 1 38 ? 29.550  -37.443 32.255  1.00 45.42  ? 37  PRO   C O   1 
ATOM   1764 C  CB  . PRO   C 1 38 ? 30.252  -38.572 35.050  1.00 47.76  ? 37  PRO   C CB  1 
ATOM   1765 C  CG  . PRO   C 1 38 ? 29.710  -39.849 35.600  1.00 51.27  ? 37  PRO   C CG  1 
ATOM   1766 C  CD  . PRO   C 1 38 ? 28.538  -40.204 34.728  1.00 49.11  ? 37  PRO   C CD  1 
ATOM   1767 N  N   . ASN   C 1 39 ? 29.271  -35.627 33.571  1.00 44.77  ? 38  ASN   C N   1 
ATOM   1768 C  CA  . ASN   C 1 39 ? 29.653  -34.626 32.578  1.00 47.30  ? 38  ASN   C CA  1 
ATOM   1769 C  C   . ASN   C 1 39 ? 28.708  -34.600 31.377  1.00 41.34  ? 38  ASN   C C   1 
ATOM   1770 O  O   . ASN   C 1 39 ? 29.116  -34.241 30.270  1.00 46.02  ? 38  ASN   C O   1 
ATOM   1771 C  CB  . ASN   C 1 39 ? 31.098  -34.833 32.110  1.00 38.28  ? 38  ASN   C CB  1 
ATOM   1772 C  CG  . ASN   C 1 39 ? 31.729  -33.562 31.577  1.00 41.11  ? 38  ASN   C CG  1 
ATOM   1773 O  OD1 . ASN   C 1 39 ? 31.316  -32.456 31.924  1.00 50.01  ? 38  ASN   C OD1 1 
ATOM   1774 N  ND2 . ASN   C 1 39 ? 32.741  -33.715 30.729  1.00 43.29  ? 38  ASN   C ND2 1 
ATOM   1775 N  N   . LYS   C 1 40 ? 27.441  -34.963 31.575  1.00 37.66  ? 39  LYS   C N   1 
ATOM   1776 C  CA  . LYS   C 1 40 ? 26.447  -34.936 30.512  1.00 34.47  ? 39  LYS   C CA  1 
ATOM   1777 C  C   . LYS   C 1 40 ? 25.330  -33.960 30.853  1.00 37.61  ? 39  LYS   C C   1 
ATOM   1778 O  O   . LYS   C 1 40 ? 24.956  -33.799 32.019  1.00 38.94  ? 39  LYS   C O   1 
ATOM   1779 C  CB  . LYS   C 1 40 ? 25.850  -36.328 30.263  1.00 36.12  ? 39  LYS   C CB  1 
ATOM   1780 C  CG  . LYS   C 1 40 ? 26.872  -37.378 29.881  1.00 42.29  ? 39  LYS   C CG  1 
ATOM   1781 C  CD  . LYS   C 1 40 ? 27.616  -36.999 28.612  1.00 40.67  ? 39  LYS   C CD  1 
ATOM   1782 C  CE  . LYS   C 1 40 ? 28.577  -38.103 28.192  1.00 45.74  ? 39  LYS   C CE  1 
ATOM   1783 N  NZ  . LYS   C 1 40 ? 29.278  -37.776 26.921  1.00 49.13  ? 39  LYS   C NZ  1 
ATOM   1784 N  N   . TYR   C 1 41 ? 24.796  -33.310 29.816  1.00 37.72  ? 40  TYR   C N   1 
ATOM   1785 C  CA  . TYR   C 1 41 ? 23.679  -32.374 29.855  1.00 39.76  ? 40  TYR   C CA  1 
ATOM   1786 C  C   . TYR   C 1 41 ? 22.386  -33.053 29.430  1.00 44.08  ? 40  TYR   C C   1 
ATOM   1787 O  O   . TYR   C 1 41 ? 22.392  -33.883 28.513  1.00 38.49  ? 40  TYR   C O   1 
ATOM   1788 C  CB  . TYR   C 1 41 ? 23.922  -31.189 28.922  1.00 33.70  ? 40  TYR   C CB  1 
ATOM   1789 C  CG  . TYR   C 1 41 ? 25.059  -30.278 29.304  1.00 31.85  ? 40  TYR   C CG  1 
ATOM   1790 C  CD1 . TYR   C 1 41 ? 26.342  -30.499 28.821  1.00 47.45  ? 40  TYR   C CD1 1 
ATOM   1791 C  CD2 . TYR   C 1 41 ? 24.847  -29.181 30.131  1.00 45.72  ? 40  TYR   C CD2 1 
ATOM   1792 C  CE1 . TYR   C 1 41 ? 27.386  -29.662 29.159  1.00 38.94  ? 40  TYR   C CE1 1 
ATOM   1793 C  CE2 . TYR   C 1 41 ? 25.885  -28.338 30.475  1.00 46.23  ? 40  TYR   C CE2 1 
ATOM   1794 C  CZ  . TYR   C 1 41 ? 27.151  -28.584 29.986  1.00 51.37  ? 40  TYR   C CZ  1 
ATOM   1795 O  OH  . TYR   C 1 41 ? 28.191  -27.753 30.323  1.00 50.52  ? 40  TYR   C OH  1 
ATOM   1796 N  N   . PRO   C 1 42 ? 21.261  -32.700 30.053  1.00 40.60  ? 41  PRO   C N   1 
ATOM   1797 C  CA  . PRO   C 1 42 ? 19.959  -33.121 29.519  1.00 40.67  ? 41  PRO   C CA  1 
ATOM   1798 C  C   . PRO   C 1 42 ? 19.581  -32.219 28.353  1.00 42.25  ? 41  PRO   C C   1 
ATOM   1799 O  O   . PRO   C 1 42 ? 19.526  -30.996 28.496  1.00 38.09  ? 41  PRO   C O   1 
ATOM   1800 C  CB  . PRO   C 1 42 ? 19.010  -32.942 30.710  1.00 40.17  ? 41  PRO   C CB  1 
ATOM   1801 C  CG  . PRO   C 1 42 ? 19.705  -31.973 31.642  1.00 41.63  ? 41  PRO   C CG  1 
ATOM   1802 C  CD  . PRO   C 1 42 ? 21.121  -31.754 31.174  1.00 48.96  ? 41  PRO   C CD  1 
ATOM   1803 N  N   . ILE   C 1 43 ? 19.339  -32.823 27.194  1.00 35.44  ? 42  ILE   C N   1 
ATOM   1804 C  CA  . ILE   C 1 43 ? 19.082  -32.088 25.960  1.00 33.12  ? 42  ILE   C CA  1 
ATOM   1805 C  C   . ILE   C 1 43 ? 17.632  -32.297 25.556  1.00 36.35  ? 42  ILE   C C   1 
ATOM   1806 O  O   . ILE   C 1 43 ? 17.126  -33.425 25.582  1.00 37.68  ? 42  ILE   C O   1 
ATOM   1807 C  CB  . ILE   C 1 43 ? 20.033  -32.529 24.834  1.00 34.33  ? 42  ILE   C CB  1 
ATOM   1808 C  CG1 . ILE   C 1 43 ? 21.488  -32.358 25.269  1.00 38.06  ? 42  ILE   C CG1 1 
ATOM   1809 C  CG2 . ILE   C 1 43 ? 19.770  -31.725 23.566  1.00 35.30  ? 42  ILE   C CG2 1 
ATOM   1810 C  CD1 . ILE   C 1 43 ? 21.873  -30.928 25.552  1.00 39.84  ? 42  ILE   C CD1 1 
ATOM   1811 N  N   . PHE   C 1 44 ? 16.966  -31.207 25.188  1.00 34.50  ? 43  PHE   C N   1 
ATOM   1812 C  CA  . PHE   C 1 44 ? 15.647  -31.244 24.572  1.00 36.20  ? 43  PHE   C CA  1 
ATOM   1813 C  C   . PHE   C 1 44 ? 15.812  -30.830 23.117  1.00 27.86  ? 43  PHE   C C   1 
ATOM   1814 O  O   . PHE   C 1 44 ? 16.317  -29.739 22.838  1.00 32.95  ? 43  PHE   C O   1 
ATOM   1815 C  CB  . PHE   C 1 44 ? 14.674  -30.314 25.300  1.00 43.56  ? 43  PHE   C CB  1 
ATOM   1816 C  CG  . PHE   C 1 44 ? 13.283  -30.310 24.725  1.00 35.70  ? 43  PHE   C CG  1 
ATOM   1817 C  CD1 . PHE   C 1 44 ? 12.386  -31.317 25.043  1.00 39.02  ? 43  PHE   C CD1 1 
ATOM   1818 C  CD2 . PHE   C 1 44 ? 12.870  -29.292 23.877  1.00 46.02  ? 43  PHE   C CD2 1 
ATOM   1819 C  CE1 . PHE   C 1 44 ? 11.104  -31.317 24.523  1.00 43.99  ? 43  PHE   C CE1 1 
ATOM   1820 C  CE2 . PHE   C 1 44 ? 11.588  -29.284 23.352  1.00 45.78  ? 43  PHE   C CE2 1 
ATOM   1821 C  CZ  . PHE   C 1 44 ? 10.703  -30.301 23.678  1.00 48.12  ? 43  PHE   C CZ  1 
ATOM   1822 N  N   . PHE   C 1 45 ? 15.416  -31.707 22.198  1.00 33.56  ? 44  PHE   C N   1 
ATOM   1823 C  CA  . PHE   C 1 45 ? 15.558  -31.445 20.772  1.00 34.22  ? 44  PHE   C CA  1 
ATOM   1824 C  C   . PHE   C 1 45 ? 14.290  -30.773 20.261  1.00 35.13  ? 44  PHE   C C   1 
ATOM   1825 O  O   . PHE   C 1 45 ? 13.196  -31.335 20.380  1.00 33.77  ? 44  PHE   C O   1 
ATOM   1826 C  CB  . PHE   C 1 45 ? 15.830  -32.738 20.003  1.00 30.48  ? 44  PHE   C CB  1 
ATOM   1827 C  CG  . PHE   C 1 45 ? 17.158  -33.360 20.322  1.00 37.20  ? 44  PHE   C CG  1 
ATOM   1828 C  CD1 . PHE   C 1 45 ? 18.287  -33.026 19.591  1.00 31.62  ? 44  PHE   C CD1 1 
ATOM   1829 C  CD2 . PHE   C 1 45 ? 17.280  -34.272 21.357  1.00 35.02  ? 44  PHE   C CD2 1 
ATOM   1830 C  CE1 . PHE   C 1 45 ? 19.515  -33.595 19.885  1.00 33.64  ? 44  PHE   C CE1 1 
ATOM   1831 C  CE2 . PHE   C 1 45 ? 18.505  -34.842 21.657  1.00 42.39  ? 44  PHE   C CE2 1 
ATOM   1832 C  CZ  . PHE   C 1 45 ? 19.622  -34.501 20.920  1.00 32.38  ? 44  PHE   C CZ  1 
ATOM   1833 N  N   . PHE   C 1 46 ? 14.434  -29.572 19.702  1.00 36.27  ? 45  PHE   C N   1 
ATOM   1834 C  CA  . PHE   C 1 46 ? 13.297  -28.914 19.073  1.00 32.40  ? 45  PHE   C CA  1 
ATOM   1835 C  C   . PHE   C 1 46 ? 12.778  -29.753 17.910  1.00 30.57  ? 45  PHE   C C   1 
ATOM   1836 O  O   . PHE   C 1 46 ? 13.518  -30.518 17.284  1.00 29.79  ? 45  PHE   C O   1 
ATOM   1837 C  CB  . PHE   C 1 46 ? 13.683  -27.520 18.578  1.00 31.89  ? 45  PHE   C CB  1 
ATOM   1838 C  CG  . PHE   C 1 46 ? 13.916  -26.521 19.678  1.00 29.62  ? 45  PHE   C CG  1 
ATOM   1839 C  CD1 . PHE   C 1 46 ? 12.876  -26.119 20.501  1.00 35.20  ? 45  PHE   C CD1 1 
ATOM   1840 C  CD2 . PHE   C 1 46 ? 15.169  -25.964 19.870  1.00 30.25  ? 45  PHE   C CD2 1 
ATOM   1841 C  CE1 . PHE   C 1 46 ? 13.086  -25.193 21.507  1.00 36.41  ? 45  PHE   C CE1 1 
ATOM   1842 C  CE2 . PHE   C 1 46 ? 15.386  -25.037 20.876  1.00 34.47  ? 45  PHE   C CE2 1 
ATOM   1843 C  CZ  . PHE   C 1 46 ? 14.342  -24.651 21.694  1.00 38.30  ? 45  PHE   C CZ  1 
ATOM   1844 N  N   . GLY   C 1 47 ? 11.488  -29.606 17.621  1.00 36.29  ? 46  GLY   C N   1 
ATOM   1845 C  CA  . GLY   C 1 47 ? 10.886  -30.328 16.518  1.00 38.84  ? 46  GLY   C CA  1 
ATOM   1846 C  C   . GLY   C 1 47 ? 10.427  -31.726 16.880  1.00 44.70  ? 46  GLY   C C   1 
ATOM   1847 O  O   . GLY   C 1 47 ? 9.224   -31.994 16.929  1.00 47.86  ? 46  GLY   C O   1 
ATOM   1848 N  N   . THR   C 1 48 ? 11.378  -32.632 17.126  1.00 38.96  ? 47  THR   C N   1 
ATOM   1849 C  CA  . THR   C 1 48 ? 11.010  -33.983 17.536  1.00 36.43  ? 47  THR   C CA  1 
ATOM   1850 C  C   . THR   C 1 48 ? 10.538  -34.023 18.983  1.00 37.21  ? 47  THR   C C   1 
ATOM   1851 O  O   . THR   C 1 48 ? 9.774   -34.920 19.357  1.00 46.46  ? 47  THR   C O   1 
ATOM   1852 C  CB  . THR   C 1 48 ? 12.189  -34.938 17.355  1.00 37.82  ? 47  THR   C CB  1 
ATOM   1853 O  OG1 . THR   C 1 48 ? 13.253  -34.557 18.237  1.00 41.93  ? 47  THR   C OG1 1 
ATOM   1854 C  CG2 . THR   C 1 48 ? 12.683  -34.916 15.919  1.00 37.95  ? 47  THR   C CG2 1 
ATOM   1855 N  N   . HIS   C 1 49 ? 10.985  -33.071 19.804  1.00 38.55  ? 48  HIS   C N   1 
ATOM   1856 C  CA  . HIS   C 1 49 ? 10.662  -32.998 21.228  1.00 45.41  ? 48  HIS   C CA  1 
ATOM   1857 C  C   . HIS   C 1 49 ? 11.151  -34.221 21.999  1.00 47.96  ? 48  HIS   C C   1 
ATOM   1858 O  O   . HIS   C 1 49 ? 10.623  -34.536 23.072  1.00 46.88  ? 48  HIS   C O   1 
ATOM   1859 C  CB  . HIS   C 1 49 ? 9.160   -32.787 21.449  1.00 49.84  ? 48  HIS   C CB  1 
ATOM   1860 C  CG  . HIS   C 1 49 ? 8.631   -31.535 20.822  1.00 54.57  ? 48  HIS   C CG  1 
ATOM   1861 N  ND1 . HIS   C 1 49 ? 7.342   -31.425 20.347  1.00 55.00  ? 48  HIS   C ND1 1 
ATOM   1862 C  CD2 . HIS   C 1 49 ? 9.221   -30.338 20.590  1.00 49.21  ? 48  HIS   C CD2 1 
ATOM   1863 C  CE1 . HIS   C 1 49 ? 7.160   -30.215 19.850  1.00 65.21  ? 48  HIS   C CE1 1 
ATOM   1864 N  NE2 . HIS   C 1 49 ? 8.284   -29.535 19.985  1.00 55.83  ? 48  HIS   C NE2 1 
ATOM   1865 N  N   . GLU   C 1 50 ? 12.153  -34.919 21.470  1.00 38.57  ? 49  GLU   C N   1 
ATOM   1866 C  CA  . GLU   C 1 50 ? 12.789  -36.009 22.193  1.00 35.49  ? 49  GLU   C CA  1 
ATOM   1867 C  C   . GLU   C 1 50 ? 13.800  -35.449 23.192  1.00 37.79  ? 49  GLU   C C   1 
ATOM   1868 O  O   . GLU   C 1 50 ? 14.128  -34.261 23.187  1.00 41.76  ? 49  GLU   C O   1 
ATOM   1869 C  CB  . GLU   C 1 50 ? 13.481  -36.969 21.225  1.00 42.06  ? 49  GLU   C CB  1 
ATOM   1870 C  CG  . GLU   C 1 50 ? 12.672  -37.307 19.981  1.00 51.47  ? 49  GLU   C CG  1 
ATOM   1871 C  CD  . GLU   C 1 50 ? 11.790  -38.526 20.156  1.00 59.62  ? 49  GLU   C CD  1 
ATOM   1872 O  OE1 . GLU   C 1 50 ? 12.067  -39.554 19.503  1.00 68.72  ? 49  GLU   C OE1 1 
ATOM   1873 O  OE2 . GLU   C 1 50 ? 10.823  -38.460 20.944  1.00 68.37  ? 49  GLU   C OE2 1 
ATOM   1874 N  N   . THR   C 1 51 ? 14.299  -36.322 24.065  1.00 44.36  ? 50  THR   C N   1 
ATOM   1875 C  CA  . THR   C 1 51 ? 15.318  -35.949 25.035  1.00 38.68  ? 50  THR   C CA  1 
ATOM   1876 C  C   . THR   C 1 51 ? 16.473  -36.940 24.972  1.00 34.21  ? 50  THR   C C   1 
ATOM   1877 O  O   . THR   C 1 51 ? 16.325  -38.072 24.504  1.00 38.76  ? 50  THR   C O   1 
ATOM   1878 C  CB  . THR   C 1 51 ? 14.764  -35.893 26.465  1.00 44.96  ? 50  THR   C CB  1 
ATOM   1879 O  OG1 . THR   C 1 51 ? 13.976  -37.062 26.720  1.00 43.72  ? 50  THR   C OG1 1 
ATOM   1880 C  CG2 . THR   C 1 51 ? 13.911  -34.648 26.665  1.00 47.97  ? 50  THR   C CG2 1 
ATOM   1881 N  N   . ALA   C 1 52 ? 17.630  -36.492 25.449  1.00 34.94  ? 51  ALA   C N   1 
ATOM   1882 C  CA  . ALA   C 1 52 ? 18.840  -37.305 25.460  1.00 38.49  ? 51  ALA   C CA  1 
ATOM   1883 C  C   . ALA   C 1 52 ? 19.870  -36.625 26.352  1.00 42.94  ? 51  ALA   C C   1 
ATOM   1884 O  O   . ALA   C 1 52 ? 19.715  -35.465 26.741  1.00 38.23  ? 51  ALA   C O   1 
ATOM   1885 C  CB  . ALA   C 1 52 ? 19.399  -37.511 24.049  1.00 41.97  ? 51  ALA   C CB  1 
ATOM   1886 N  N   . PHE   C 1 53 ? 20.928  -37.366 26.669  1.00 42.19  ? 52  PHE   C N   1 
ATOM   1887 C  CA  . PHE   C 1 53 ? 22.054  -36.855 27.438  1.00 36.53  ? 52  PHE   C CA  1 
ATOM   1888 C  C   . PHE   C 1 53 ? 23.267  -36.736 26.528  1.00 43.31  ? 52  PHE   C C   1 
ATOM   1889 O  O   . PHE   C 1 53 ? 23.646  -37.706 25.865  1.00 41.55  ? 52  PHE   C O   1 
ATOM   1890 C  CB  . PHE   C 1 53 ? 22.374  -37.763 28.631  1.00 40.17  ? 52  PHE   C CB  1 
ATOM   1891 C  CG  . PHE   C 1 53 ? 21.394  -37.645 29.761  1.00 44.93  ? 52  PHE   C CG  1 
ATOM   1892 C  CD1 . PHE   C 1 53 ? 20.696  -38.753 30.210  1.00 53.07  ? 52  PHE   C CD1 1 
ATOM   1893 C  CD2 . PHE   C 1 53 ? 21.160  -36.420 30.364  1.00 45.76  ? 52  PHE   C CD2 1 
ATOM   1894 C  CE1 . PHE   C 1 53 ? 19.788  -38.641 31.250  1.00 64.60  ? 52  PHE   C CE1 1 
ATOM   1895 C  CE2 . PHE   C 1 53 ? 20.251  -36.302 31.401  1.00 48.90  ? 52  PHE   C CE2 1 
ATOM   1896 C  CZ  . PHE   C 1 53 ? 19.568  -37.412 31.845  1.00 48.81  ? 52  PHE   C CZ  1 
ATOM   1897 N  N   . LEU   C 1 54 ? 23.873  -35.552 26.500  1.00 35.92  ? 53  LEU   C N   1 
ATOM   1898 C  CA  . LEU   C 1 54 ? 25.011  -35.290 25.633  1.00 36.14  ? 53  LEU   C CA  1 
ATOM   1899 C  C   . LEU   C 1 54 ? 26.076  -34.526 26.402  1.00 34.15  ? 53  LEU   C C   1 
ATOM   1900 O  O   . LEU   C 1 54 ? 25.776  -33.788 27.345  1.00 37.90  ? 53  LEU   C O   1 
ATOM   1901 C  CB  . LEU   C 1 54 ? 24.608  -34.496 24.381  1.00 33.27  ? 53  LEU   C CB  1 
ATOM   1902 C  CG  . LEU   C 1 54 ? 23.804  -35.241 23.315  1.00 41.46  ? 53  LEU   C CG  1 
ATOM   1903 C  CD1 . LEU   C 1 54 ? 23.512  -34.326 22.136  1.00 32.62  ? 53  LEU   C CD1 1 
ATOM   1904 C  CD2 . LEU   C 1 54 ? 24.549  -36.484 22.857  1.00 39.35  ? 53  LEU   C CD2 1 
ATOM   1905 N  N   . GLY   C 1 55 ? 27.326  -34.710 25.984  1.00 37.37  ? 54  GLY   C N   1 
ATOM   1906 C  CA  . GLY   C 1 55 ? 28.446  -34.036 26.596  1.00 37.30  ? 54  GLY   C CA  1 
ATOM   1907 C  C   . GLY   C 1 55 ? 28.832  -32.775 25.851  1.00 45.62  ? 54  GLY   C C   1 
ATOM   1908 O  O   . GLY   C 1 55 ? 28.349  -32.502 24.746  1.00 40.24  ? 54  GLY   C O   1 
ATOM   1909 N  N   . PRO   C 1 56 ? 29.725  -31.980 26.451  1.00 44.80  ? 55  PRO   C N   1 
ATOM   1910 C  CA  . PRO   C 1 56 ? 30.108  -30.700 25.830  1.00 39.53  ? 55  PRO   C CA  1 
ATOM   1911 C  C   . PRO   C 1 56 ? 30.671  -30.840 24.428  1.00 40.50  ? 55  PRO   C C   1 
ATOM   1912 O  O   . PRO   C 1 56 ? 30.512  -29.923 23.614  1.00 43.78  ? 55  PRO   C O   1 
ATOM   1913 C  CB  . PRO   C 1 56 ? 31.160  -30.141 26.800  1.00 55.12  ? 55  PRO   C CB  1 
ATOM   1914 C  CG  . PRO   C 1 56 ? 30.891  -30.823 28.097  1.00 44.15  ? 55  PRO   C CG  1 
ATOM   1915 C  CD  . PRO   C 1 56 ? 30.390  -32.191 27.747  1.00 40.34  ? 55  PRO   C CD  1 
ATOM   1916 N  N   . LYS   C 1 57 ? 31.325  -31.964 24.123  1.00 46.52  ? 56  LYS   C N   1 
ATOM   1917 C  CA  . LYS   C 1 57 ? 31.874  -32.183 22.788  1.00 45.13  ? 56  LYS   C CA  1 
ATOM   1918 C  C   . LYS   C 1 57 ? 30.799  -32.086 21.709  1.00 46.82  ? 56  LYS   C C   1 
ATOM   1919 O  O   . LYS   C 1 57 ? 31.095  -31.714 20.567  1.00 45.08  ? 56  LYS   C O   1 
ATOM   1920 C  CB  . LYS   C 1 57 ? 32.569  -33.549 22.747  1.00 51.05  ? 56  LYS   C CB  1 
ATOM   1921 C  CG  . LYS   C 1 57 ? 32.856  -34.101 21.358  1.00 60.94  ? 56  LYS   C CG  1 
ATOM   1922 C  CD  . LYS   C 1 57 ? 31.922  -35.253 21.010  1.00 59.31  ? 56  LYS   C CD  1 
ATOM   1923 C  CE  . LYS   C 1 57 ? 32.189  -36.475 21.877  1.00 71.08  ? 56  LYS   C CE  1 
ATOM   1924 N  NZ  . LYS   C 1 57 ? 31.304  -37.616 21.510  1.00 61.00  ? 56  LYS   C NZ  1 
ATOM   1925 N  N   . ASP   C 1 58 ? 29.550  -32.385 22.057  1.00 42.84  ? 57  ASP   C N   1 
ATOM   1926 C  CA  . ASP   C 1 58 ? 28.467  -32.502 21.093  1.00 42.16  ? 57  ASP   C CA  1 
ATOM   1927 C  C   . ASP   C 1 58 ? 27.588  -31.259 21.013  1.00 43.97  ? 57  ASP   C C   1 
ATOM   1928 O  O   . ASP   C 1 58 ? 26.540  -31.305 20.362  1.00 36.82  ? 57  ASP   C O   1 
ATOM   1929 C  CB  . ASP   C 1 58 ? 27.602  -33.716 21.435  1.00 39.78  ? 57  ASP   C CB  1 
ATOM   1930 C  CG  . ASP   C 1 58 ? 28.338  -35.026 21.251  1.00 51.10  ? 57  ASP   C CG  1 
ATOM   1931 O  OD1 . ASP   C 1 58 ? 28.887  -35.248 20.153  1.00 55.28  ? 57  ASP   C OD1 1 
ATOM   1932 O  OD2 . ASP   C 1 58 ? 28.369  -35.831 22.205  1.00 56.29  ? 57  ASP   C OD2 1 
ATOM   1933 N  N   . LEU   C 1 59 ? 27.979  -30.155 21.649  1.00 39.23  ? 58  LEU   C N   1 
ATOM   1934 C  CA  . LEU   C 1 59 ? 27.113  -28.992 21.786  1.00 44.65  ? 58  LEU   C CA  1 
ATOM   1935 C  C   . LEU   C 1 59 ? 27.762  -27.752 21.184  1.00 48.09  ? 58  LEU   C C   1 
ATOM   1936 O  O   . LEU   C 1 59 ? 28.975  -27.548 21.305  1.00 47.15  ? 58  LEU   C O   1 
ATOM   1937 C  CB  . LEU   C 1 59 ? 26.769  -28.739 23.255  1.00 34.96  ? 58  LEU   C CB  1 
ATOM   1938 C  CG  . LEU   C 1 59 ? 26.080  -29.902 23.967  1.00 33.62  ? 58  LEU   C CG  1 
ATOM   1939 C  CD1 . LEU   C 1 59 ? 25.840  -29.570 25.432  1.00 39.89  ? 58  LEU   C CD1 1 
ATOM   1940 C  CD2 . LEU   C 1 59 ? 24.774  -30.257 23.270  1.00 34.31  ? 58  LEU   C CD2 1 
ATOM   1941 N  N   . PHE   C 1 60 ? 26.934  -26.920 20.543  1.00 47.46  ? 59  PHE   C N   1 
ATOM   1942 C  CA  . PHE   C 1 60 ? 27.357  -25.703 19.856  1.00 43.67  ? 59  PHE   C CA  1 
ATOM   1943 C  C   . PHE   C 1 60 ? 26.333  -24.599 20.095  1.00 48.42  ? 59  PHE   C C   1 
ATOM   1944 O  O   . PHE   C 1 60 ? 25.154  -24.776 19.769  1.00 48.42  ? 59  PHE   C O   1 
ATOM   1945 C  CB  . PHE   C 1 60 ? 27.518  -25.957 18.355  1.00 43.83  ? 59  PHE   C CB  1 
ATOM   1946 C  CG  . PHE   C 1 60 ? 28.427  -27.107 18.025  1.00 48.08  ? 59  PHE   C CG  1 
ATOM   1947 C  CD1 . PHE   C 1 60 ? 27.938  -28.404 17.971  1.00 42.95  ? 59  PHE   C CD1 1 
ATOM   1948 C  CD2 . PHE   C 1 60 ? 29.770  -26.891 17.759  1.00 43.66  ? 59  PHE   C CD2 1 
ATOM   1949 C  CE1 . PHE   C 1 60 ? 28.772  -29.464 17.669  1.00 41.20  ? 59  PHE   C CE1 1 
ATOM   1950 C  CE2 . PHE   C 1 60 ? 30.609  -27.946 17.452  1.00 49.59  ? 59  PHE   C CE2 1 
ATOM   1951 C  CZ  . PHE   C 1 60 ? 30.110  -29.234 17.407  1.00 55.80  ? 59  PHE   C CZ  1 
ATOM   1952 N  N   . PRO   C 1 61 ? 26.737  -23.450 20.641  1.00 44.92  ? 60  PRO   C N   1 
ATOM   1953 C  CA  . PRO   C 1 61 ? 25.754  -22.408 20.973  1.00 38.34  ? 60  PRO   C CA  1 
ATOM   1954 C  C   . PRO   C 1 61 ? 25.003  -21.927 19.737  1.00 43.62  ? 60  PRO   C C   1 
ATOM   1955 O  O   . PRO   C 1 61 ? 25.570  -21.799 18.650  1.00 45.36  ? 60  PRO   C O   1 
ATOM   1956 C  CB  . PRO   C 1 61 ? 26.610  -21.294 21.589  1.00 46.21  ? 60  PRO   C CB  1 
ATOM   1957 C  CG  . PRO   C 1 61 ? 27.987  -21.531 21.059  1.00 47.92  ? 60  PRO   C CG  1 
ATOM   1958 C  CD  . PRO   C 1 61 ? 28.117  -23.021 20.922  1.00 52.67  ? 60  PRO   C CD  1 
ATOM   1959 N  N   . TYR   C 1 62 ? 23.707  -21.663 19.919  1.00 47.13  ? 61  TYR   C N   1 
ATOM   1960 C  CA  . TYR   C 1 62 ? 22.825  -21.411 18.783  1.00 39.68  ? 61  TYR   C CA  1 
ATOM   1961 C  C   . TYR   C 1 62 ? 23.206  -20.130 18.048  1.00 50.57  ? 61  TYR   C C   1 
ATOM   1962 O  O   . TYR   C 1 62 ? 23.446  -20.143 16.835  1.00 51.42  ? 61  TYR   C O   1 
ATOM   1963 C  CB  . TYR   C 1 62 ? 21.370  -21.353 19.254  1.00 39.71  ? 61  TYR   C CB  1 
ATOM   1964 C  CG  . TYR   C 1 62 ? 20.395  -21.017 18.148  1.00 47.11  ? 61  TYR   C CG  1 
ATOM   1965 C  CD1 . TYR   C 1 62 ? 20.431  -21.699 16.939  1.00 40.89  ? 61  TYR   C CD1 1 
ATOM   1966 C  CD2 . TYR   C 1 62 ? 19.441  -20.022 18.311  1.00 51.18  ? 61  TYR   C CD2 1 
ATOM   1967 C  CE1 . TYR   C 1 62 ? 19.548  -21.397 15.921  1.00 50.69  ? 61  TYR   C CE1 1 
ATOM   1968 C  CE2 . TYR   C 1 62 ? 18.551  -19.712 17.296  1.00 48.95  ? 61  TYR   C CE2 1 
ATOM   1969 C  CZ  . TYR   C 1 62 ? 18.610  -20.402 16.104  1.00 47.28  ? 61  TYR   C CZ  1 
ATOM   1970 O  OH  . TYR   C 1 62 ? 17.728  -20.099 15.092  1.00 52.42  ? 61  TYR   C OH  1 
ATOM   1971 N  N   . ASP   C 1 63 ? 23.266  -19.008 18.770  1.00 49.28  ? 62  ASP   C N   1 
ATOM   1972 C  CA  . ASP   C 1 63 ? 23.478  -17.720 18.114  1.00 51.21  ? 62  ASP   C CA  1 
ATOM   1973 C  C   . ASP   C 1 63 ? 24.866  -17.611 17.492  1.00 51.15  ? 62  ASP   C C   1 
ATOM   1974 O  O   . ASP   C 1 63 ? 25.044  -16.888 16.505  1.00 58.79  ? 62  ASP   C O   1 
ATOM   1975 C  CB  . ASP   C 1 63 ? 23.243  -16.581 19.106  1.00 54.02  ? 62  ASP   C CB  1 
ATOM   1976 C  CG  . ASP   C 1 63 ? 21.768  -16.297 19.325  1.00 66.30  ? 62  ASP   C CG  1 
ATOM   1977 O  OD1 . ASP   C 1 63 ? 21.074  -15.960 18.341  1.00 71.03  ? 62  ASP   C OD1 1 
ATOM   1978 O  OD2 . ASP   C 1 63 ? 21.298  -16.424 20.475  1.00 67.99  ? 62  ASP   C OD2 1 
ATOM   1979 N  N   . LYS   C 1 64 ? 25.854  -18.317 18.043  1.00 49.46  ? 63  LYS   C N   1 
ATOM   1980 C  CA  . LYS   C 1 64 ? 27.195  -18.285 17.467  1.00 49.07  ? 63  LYS   C CA  1 
ATOM   1981 C  C   . LYS   C 1 64 ? 27.312  -19.141 16.213  1.00 51.19  ? 63  LYS   C C   1 
ATOM   1982 O  O   . LYS   C 1 64 ? 28.051  -18.781 15.290  1.00 43.43  ? 63  LYS   C O   1 
ATOM   1983 C  CB  . LYS   C 1 64 ? 28.226  -18.738 18.501  1.00 51.38  ? 63  LYS   C CB  1 
ATOM   1984 C  CG  . LYS   C 1 64 ? 28.787  -17.600 19.336  1.00 60.78  ? 63  LYS   C CG  1 
ATOM   1985 C  CD  . LYS   C 1 64 ? 29.590  -18.105 20.520  1.00 67.84  ? 63  LYS   C CD  1 
ATOM   1986 C  CE  . LYS   C 1 64 ? 29.720  -17.019 21.579  1.00 75.63  ? 63  LYS   C CE  1 
ATOM   1987 N  NZ  . LYS   C 1 64 ? 28.553  -17.002 22.509  1.00 73.95  ? 63  LYS   C NZ  1 
ATOM   1988 N  N   . CYS   C 1 65 ? 26.591  -20.258 16.150  1.00 46.50  ? 64  CYS   C N   1 
ATOM   1989 C  CA  . CYS   C 1 65 ? 26.790  -21.246 15.100  1.00 38.09  ? 64  CYS   C CA  1 
ATOM   1990 C  C   . CYS   C 1 65 ? 25.602  -21.397 14.161  1.00 42.09  ? 64  CYS   C C   1 
ATOM   1991 O  O   . CYS   C 1 65 ? 25.667  -22.221 13.241  1.00 41.02  ? 64  CYS   C O   1 
ATOM   1992 C  CB  . CYS   C 1 65 ? 27.127  -22.604 15.725  1.00 43.18  ? 64  CYS   C CB  1 
ATOM   1993 S  SG  . CYS   C 1 65 ? 28.614  -22.579 16.762  1.00 56.57  ? 64  CYS   C SG  1 
ATOM   1994 N  N   . LYS   C 1 66 ? 24.527  -20.626 14.359  1.00 38.05  ? 65  LYS   C N   1 
ATOM   1995 C  CA  . LYS   C 1 66 ? 23.351  -20.739 13.499  1.00 42.01  ? 65  LYS   C CA  1 
ATOM   1996 C  C   . LYS   C 1 66 ? 23.703  -20.575 12.027  1.00 42.96  ? 65  LYS   C C   1 
ATOM   1997 O  O   . LYS   C 1 66 ? 23.059  -21.178 11.161  1.00 37.21  ? 65  LYS   C O   1 
ATOM   1998 C  CB  . LYS   C 1 66 ? 22.301  -19.698 13.900  1.00 44.13  ? 65  LYS   C CB  1 
ATOM   1999 C  CG  . LYS   C 1 66 ? 22.740  -18.261 13.641  1.00 43.54  ? 65  LYS   C CG  1 
ATOM   2000 C  CD  . LYS   C 1 66 ? 21.720  -17.233 14.109  1.00 67.32  ? 65  LYS   C CD  1 
ATOM   2001 C  CE  . LYS   C 1 66 ? 22.101  -15.842 13.607  1.00 65.37  ? 65  LYS   C CE  1 
ATOM   2002 N  NZ  . LYS   C 1 66 ? 21.207  -14.771 14.130  1.00 74.90  ? 65  LYS   C NZ  1 
ATOM   2003 N  N   . ASP   C 1 67 ? 24.728  -19.774 11.724  1.00 55.33  ? 66  ASP   C N   1 
ATOM   2004 C  CA  . ASP   C 1 67 ? 25.055  -19.478 10.334  1.00 47.32  ? 66  ASP   C CA  1 
ATOM   2005 C  C   . ASP   C 1 67 ? 25.497  -20.724 9.579   1.00 43.62  ? 66  ASP   C C   1 
ATOM   2006 O  O   . ASP   C 1 67 ? 25.276  -20.824 8.367   1.00 40.83  ? 66  ASP   C O   1 
ATOM   2007 C  CB  . ASP   C 1 67 ? 26.138  -18.401 10.272  1.00 37.50  ? 66  ASP   C CB  1 
ATOM   2008 N  N   . LYS   C 1 68 ? 26.112  -21.686 10.267  1.00 44.61  ? 67  LYS   C N   1 
ATOM   2009 C  CA  . LYS   C 1 68 ? 26.577  -22.894 9.596   1.00 47.92  ? 67  LYS   C CA  1 
ATOM   2010 C  C   . LYS   C 1 68 ? 25.660  -24.095 9.790   1.00 49.63  ? 67  LYS   C C   1 
ATOM   2011 O  O   . LYS   C 1 68 ? 25.576  -24.938 8.892   1.00 39.98  ? 67  LYS   C O   1 
ATOM   2012 C  CB  . LYS   C 1 68 ? 27.999  -23.254 10.053  1.00 60.77  ? 67  LYS   C CB  1 
ATOM   2013 C  CG  . LYS   C 1 68 ? 28.233  -23.315 11.556  1.00 61.59  ? 67  LYS   C CG  1 
ATOM   2014 C  CD  . LYS   C 1 68 ? 29.710  -23.602 11.833  1.00 60.06  ? 67  LYS   C CD  1 
ATOM   2015 C  CE  . LYS   C 1 68 ? 30.003  -23.801 13.313  1.00 68.08  ? 67  LYS   C CE  1 
ATOM   2016 N  NZ  . LYS   C 1 68 ? 29.871  -22.542 14.095  1.00 66.69  ? 67  LYS   C NZ  1 
ATOM   2017 N  N   . TYR   C 1 69 ? 24.958  -24.197 10.919  1.00 41.60  ? 68  TYR   C N   1 
ATOM   2018 C  CA  . TYR   C 1 69 ? 24.076  -25.337 11.142  1.00 41.49  ? 68  TYR   C CA  1 
ATOM   2019 C  C   . TYR   C 1 69 ? 22.597  -25.007 10.994  1.00 43.76  ? 68  TYR   C C   1 
ATOM   2020 O  O   . TYR   C 1 69 ? 21.791  -25.929 10.822  1.00 40.17  ? 68  TYR   C O   1 
ATOM   2021 C  CB  . TYR   C 1 69 ? 24.315  -25.936 12.533  1.00 40.91  ? 68  TYR   C CB  1 
ATOM   2022 C  CG  . TYR   C 1 69 ? 25.727  -26.435 12.748  1.00 39.18  ? 68  TYR   C CG  1 
ATOM   2023 C  CD1 . TYR   C 1 69 ? 26.273  -27.408 11.922  1.00 45.33  ? 68  TYR   C CD1 1 
ATOM   2024 C  CD2 . TYR   C 1 69 ? 26.506  -25.941 13.782  1.00 48.81  ? 68  TYR   C CD2 1 
ATOM   2025 C  CE1 . TYR   C 1 69 ? 27.562  -27.870 12.118  1.00 45.57  ? 68  TYR   C CE1 1 
ATOM   2026 C  CE2 . TYR   C 1 69 ? 27.792  -26.397 13.988  1.00 49.63  ? 68  TYR   C CE2 1 
ATOM   2027 C  CZ  . TYR   C 1 69 ? 28.316  -27.359 13.152  1.00 48.31  ? 68  TYR   C CZ  1 
ATOM   2028 O  OH  . TYR   C 1 69 ? 29.598  -27.813 13.355  1.00 63.40  ? 68  TYR   C OH  1 
ATOM   2029 N  N   . GLY   C 1 70 ? 22.219  -23.731 11.060  1.00 37.31  ? 69  GLY   C N   1 
ATOM   2030 C  CA  . GLY   C 1 70 ? 20.828  -23.356 10.888  1.00 41.55  ? 69  GLY   C CA  1 
ATOM   2031 C  C   . GLY   C 1 70 ? 20.408  -23.335 9.433   1.00 43.49  ? 69  GLY   C C   1 
ATOM   2032 O  O   . GLY   C 1 70 ? 20.231  -22.265 8.844   1.00 49.43  ? 69  GLY   C O   1 
ATOM   2033 N  N   . LYS   C 1 71 ? 20.256  -24.519 8.843   1.00 36.86  ? 70  LYS   C N   1 
ATOM   2034 C  CA  . LYS   C 1 71 ? 19.875  -24.690 7.449   1.00 47.85  ? 70  LYS   C CA  1 
ATOM   2035 C  C   . LYS   C 1 71 ? 18.894  -25.851 7.368   1.00 43.90  ? 70  LYS   C C   1 
ATOM   2036 O  O   . LYS   C 1 71 ? 19.060  -26.851 8.082   1.00 49.02  ? 70  LYS   C O   1 
ATOM   2037 C  CB  . LYS   C 1 71 ? 21.100  -24.961 6.561   1.00 43.89  ? 70  LYS   C CB  1 
ATOM   2038 C  CG  . LYS   C 1 71 ? 20.794  -25.556 5.193   1.00 48.20  ? 70  LYS   C CG  1 
ATOM   2039 C  CD  . LYS   C 1 71 ? 21.993  -25.428 4.264   1.00 53.03  ? 70  LYS   C CD  1 
ATOM   2040 C  CE  . LYS   C 1 71 ? 22.386  -26.769 3.657   1.00 57.18  ? 70  LYS   C CE  1 
ATOM   2041 N  NZ  . LYS   C 1 71 ? 21.313  -27.346 2.797   1.00 51.45  ? 70  LYS   C NZ  1 
ATOM   2042 N  N   . PRO   C 1 72 ? 17.856  -25.744 6.537   1.00 35.79  ? 71  PRO   C N   1 
ATOM   2043 C  CA  . PRO   C 1 72 ? 16.867  -26.823 6.464   1.00 26.70  ? 71  PRO   C CA  1 
ATOM   2044 C  C   . PRO   C 1 72 ? 17.475  -28.130 5.982   1.00 35.50  ? 71  PRO   C C   1 
ATOM   2045 O  O   . PRO   C 1 72 ? 18.491  -28.157 5.284   1.00 39.90  ? 71  PRO   C O   1 
ATOM   2046 C  CB  . PRO   C 1 72 ? 15.836  -26.296 5.458   1.00 36.87  ? 71  PRO   C CB  1 
ATOM   2047 C  CG  . PRO   C 1 72 ? 15.979  -24.830 5.508   1.00 30.92  ? 71  PRO   C CG  1 
ATOM   2048 C  CD  . PRO   C 1 72 ? 17.436  -24.563 5.762   1.00 36.46  ? 71  PRO   C CD  1 
ATOM   2049 N  N   . ASN   C 1 73 ? 16.830  -29.223 6.377   1.00 37.79  ? 72  ASN   C N   1 
ATOM   2050 C  CA  . ASN   C 1 73 ? 17.069  -30.534 5.791   1.00 46.28  ? 72  ASN   C CA  1 
ATOM   2051 C  C   . ASN   C 1 73 ? 15.811  -31.359 6.015   1.00 37.82  ? 72  ASN   C C   1 
ATOM   2052 O  O   . ASN   C 1 73 ? 14.890  -30.944 6.723   1.00 40.21  ? 72  ASN   C O   1 
ATOM   2053 C  CB  . ASN   C 1 73 ? 18.314  -31.214 6.374   1.00 47.54  ? 72  ASN   C CB  1 
ATOM   2054 C  CG  . ASN   C 1 73 ? 18.109  -31.693 7.791   1.00 40.04  ? 72  ASN   C CG  1 
ATOM   2055 O  OD1 . ASN   C 1 73 ? 17.382  -32.651 8.031   1.00 44.39  ? 72  ASN   C OD1 1 
ATOM   2056 N  ND2 . ASN   C 1 73 ? 18.762  -31.037 8.737   1.00 50.72  ? 72  ASN   C ND2 1 
ATOM   2057 N  N   . LYS   C 1 74 ? 15.786  -32.540 5.409   1.00 38.14  ? 73  LYS   C N   1 
ATOM   2058 C  CA  . LYS   C 1 74 ? 14.558  -33.316 5.301   1.00 36.28  ? 73  LYS   C CA  1 
ATOM   2059 C  C   . LYS   C 1 74 ? 14.340  -34.291 6.450   1.00 43.31  ? 73  LYS   C C   1 
ATOM   2060 O  O   . LYS   C 1 74 ? 13.312  -34.975 6.464   1.00 48.24  ? 73  LYS   C O   1 
ATOM   2061 C  CB  . LYS   C 1 74 ? 14.544  -34.082 3.973   1.00 37.52  ? 73  LYS   C CB  1 
ATOM   2062 N  N   . ARG   C 1 75 ? 15.264  -34.377 7.406   1.00 40.09  ? 74  ARG   C N   1 
ATOM   2063 C  CA  . ARG   C 1 75 ? 15.089  -35.304 8.516   1.00 33.30  ? 74  ARG   C CA  1 
ATOM   2064 C  C   . ARG   C 1 75 ? 13.847  -34.935 9.322   1.00 40.76  ? 74  ARG   C C   1 
ATOM   2065 O  O   . ARG   C 1 75 ? 13.541  -33.754 9.518   1.00 36.57  ? 74  ARG   C O   1 
ATOM   2066 C  CB  . ARG   C 1 75 ? 16.336  -35.308 9.406   1.00 36.61  ? 74  ARG   C CB  1 
ATOM   2067 C  CG  . ARG   C 1 75 ? 17.636  -35.588 8.654   1.00 43.96  ? 74  ARG   C CG  1 
ATOM   2068 C  CD  . ARG   C 1 75 ? 17.723  -37.021 8.166   1.00 49.93  ? 74  ARG   C CD  1 
ATOM   2069 N  NE  . ARG   C 1 75 ? 18.043  -37.931 9.255   1.00 50.92  ? 74  ARG   C NE  1 
ATOM   2070 C  CZ  . ARG   C 1 75 ? 19.275  -38.260 9.617   1.00 46.52  ? 74  ARG   C CZ  1 
ATOM   2071 N  NH1 . ARG   C 1 75 ? 20.334  -37.791 8.977   1.00 39.50  ? 74  ARG   C NH1 1 
ATOM   2072 N  NH2 . ARG   C 1 75 ? 19.448  -39.077 10.649  1.00 36.02  ? 74  ARG   C NH2 1 
ATOM   2073 N  N   . LYS   C 1 76 ? 13.125  -35.960 9.777   1.00 38.36  ? 75  LYS   C N   1 
ATOM   2074 C  CA  . LYS   C 1 76 ? 11.823  -35.759 10.408  1.00 47.75  ? 75  LYS   C CA  1 
ATOM   2075 C  C   . LYS   C 1 76 ? 11.920  -34.824 11.607  1.00 46.74  ? 75  LYS   C C   1 
ATOM   2076 O  O   . LYS   C 1 76 ? 12.731  -35.036 12.514  1.00 38.33  ? 75  LYS   C O   1 
ATOM   2077 C  CB  . LYS   C 1 76 ? 11.237  -37.104 10.845  1.00 48.08  ? 75  LYS   C CB  1 
ATOM   2078 C  CG  . LYS   C 1 76 ? 10.060  -36.994 11.810  1.00 61.66  ? 75  LYS   C CG  1 
ATOM   2079 C  CD  . LYS   C 1 76 ? 8.735   -36.851 11.077  1.00 68.30  ? 75  LYS   C CD  1 
ATOM   2080 C  CE  . LYS   C 1 76 ? 7.599   -36.500 12.029  1.00 64.95  ? 75  LYS   C CE  1 
ATOM   2081 N  NZ  . LYS   C 1 76 ? 7.594   -35.050 12.384  1.00 62.58  ? 75  LYS   C NZ  1 
ATOM   2082 N  N   . GLY   C 1 77 ? 11.078  -33.787 11.607  1.00 43.53  ? 76  GLY   C N   1 
ATOM   2083 C  CA  . GLY   C 1 77 ? 10.991  -32.847 12.702  1.00 36.04  ? 76  GLY   C CA  1 
ATOM   2084 C  C   . GLY   C 1 77 ? 12.018  -31.737 12.686  1.00 30.92  ? 76  GLY   C C   1 
ATOM   2085 O  O   . GLY   C 1 77 ? 11.940  -30.835 13.529  1.00 32.74  ? 76  GLY   C O   1 
ATOM   2086 N  N   . PHE   C 1 78 ? 12.968  -31.765 11.751  1.00 27.49  ? 77  PHE   C N   1 
ATOM   2087 C  CA  . PHE   C 1 78 ? 14.077  -30.818 11.794  1.00 29.11  ? 77  PHE   C CA  1 
ATOM   2088 C  C   . PHE   C 1 78 ? 13.607  -29.400 11.500  1.00 30.06  ? 77  PHE   C C   1 
ATOM   2089 O  O   . PHE   C 1 78 ? 13.957  -28.456 12.220  1.00 26.13  ? 77  PHE   C O   1 
ATOM   2090 C  CB  . PHE   C 1 78 ? 15.165  -31.232 10.804  1.00 33.05  ? 77  PHE   C CB  1 
ATOM   2091 C  CG  . PHE   C 1 78 ? 16.460  -30.490 10.985  1.00 30.50  ? 77  PHE   C CG  1 
ATOM   2092 C  CD1 . PHE   C 1 78 ? 16.654  -29.246 10.407  1.00 28.07  ? 77  PHE   C CD1 1 
ATOM   2093 C  CD2 . PHE   C 1 78 ? 17.479  -31.034 11.742  1.00 24.72  ? 77  PHE   C CD2 1 
ATOM   2094 C  CE1 . PHE   C 1 78 ? 17.842  -28.558 10.584  1.00 32.59  ? 77  PHE   C CE1 1 
ATOM   2095 C  CE2 . PHE   C 1 78 ? 18.668  -30.356 11.924  1.00 28.16  ? 77  PHE   C CE2 1 
ATOM   2096 C  CZ  . PHE   C 1 78 ? 18.853  -29.116 11.343  1.00 34.96  ? 77  PHE   C CZ  1 
ATOM   2097 N  N   . ASN   C 1 79 ? 12.827  -29.227 10.432  1.00 29.80  ? 78  ASN   C N   1 
ATOM   2098 C  CA  . ASN   C 1 79 ? 12.453  -27.877 10.027  1.00 27.80  ? 78  ASN   C CA  1 
ATOM   2099 C  C   . ASN   C 1 79 ? 11.462  -27.248 10.995  1.00 28.41  ? 78  ASN   C C   1 
ATOM   2100 O  O   . ASN   C 1 79 ? 11.501  -26.031 11.212  1.00 28.30  ? 78  ASN   C O   1 
ATOM   2101 C  CB  . ASN   C 1 79 ? 11.897  -27.893 8.603   1.00 30.48  ? 78  ASN   C CB  1 
ATOM   2102 C  CG  . ASN   C 1 79 ? 12.942  -28.298 7.583   1.00 35.92  ? 78  ASN   C CG  1 
ATOM   2103 O  OD1 . ASN   C 1 79 ? 14.134  -28.047 7.767   1.00 31.87  ? 78  ASN   C OD1 1 
ATOM   2104 N  ND2 . ASN   C 1 79 ? 12.502  -28.932 6.503   1.00 30.85  ? 78  ASN   C ND2 1 
ATOM   2105 N  N   . GLU   C 1 80 ? 10.572  -28.044 11.592  1.00 30.46  ? 79  GLU   C N   1 
ATOM   2106 C  CA  . GLU   C 1 80 ? 9.760   -27.514 12.682  1.00 32.30  ? 79  GLU   C CA  1 
ATOM   2107 C  C   . GLU   C 1 80 ? 10.635  -27.115 13.864  1.00 34.14  ? 79  GLU   C C   1 
ATOM   2108 O  O   . GLU   C 1 80 ? 10.361  -26.117 14.540  1.00 32.20  ? 79  GLU   C O   1 
ATOM   2109 C  CB  . GLU   C 1 80 ? 8.703   -28.533 13.110  1.00 41.08  ? 79  GLU   C CB  1 
ATOM   2110 C  CG  . GLU   C 1 80 ? 7.742   -28.011 14.165  1.00 38.10  ? 79  GLU   C CG  1 
ATOM   2111 C  CD  . GLU   C 1 80 ? 6.472   -28.834 14.268  1.00 43.57  ? 79  GLU   C CD  1 
ATOM   2112 O  OE1 . GLU   C 1 80 ? 6.365   -29.866 13.574  1.00 51.25  ? 79  GLU   C OE1 1 
ATOM   2113 O  OE2 . GLU   C 1 80 ? 5.576   -28.442 15.044  1.00 42.68  ? 79  GLU   C OE2 1 
ATOM   2114 N  N   . GLY   C 1 81 ? 11.701  -27.874 14.123  1.00 32.97  ? 80  GLY   C N   1 
ATOM   2115 C  CA  . GLY   C 1 81 ? 12.627  -27.486 15.175  1.00 29.07  ? 80  GLY   C CA  1 
ATOM   2116 C  C   . GLY   C 1 81 ? 13.350  -26.188 14.868  1.00 29.19  ? 80  GLY   C C   1 
ATOM   2117 O  O   . GLY   C 1 81 ? 13.603  -25.381 15.766  1.00 32.27  ? 80  GLY   C O   1 
ATOM   2118 N  N   . LEU   C 1 82 ? 13.703  -25.973 13.597  1.00 29.42  ? 81  LEU   C N   1 
ATOM   2119 C  CA  . LEU   C 1 82 ? 14.306  -24.703 13.208  1.00 27.16  ? 81  LEU   C CA  1 
ATOM   2120 C  C   . LEU   C 1 82 ? 13.357  -23.542 13.465  1.00 28.50  ? 81  LEU   C C   1 
ATOM   2121 O  O   . LEU   C 1 82 ? 13.791  -22.448 13.840  1.00 29.95  ? 81  LEU   C O   1 
ATOM   2122 C  CB  . LEU   C 1 82 ? 14.716  -24.731 11.735  1.00 28.58  ? 81  LEU   C CB  1 
ATOM   2123 C  CG  . LEU   C 1 82 ? 15.971  -25.518 11.348  1.00 27.00  ? 81  LEU   C CG  1 
ATOM   2124 C  CD1 . LEU   C 1 82 ? 16.225  -25.390 9.853   1.00 30.21  ? 81  LEU   C CD1 1 
ATOM   2125 C  CD2 . LEU   C 1 82 ? 17.178  -25.040 12.140  1.00 28.43  ? 81  LEU   C CD2 1 
ATOM   2126 N  N   . TRP   C 1 83 ? 12.055  -23.758 13.265  1.00 29.24  ? 82  TRP   C N   1 
ATOM   2127 C  CA  . TRP   C 1 83 ? 11.094  -22.698 13.549  1.00 33.78  ? 82  TRP   C CA  1 
ATOM   2128 C  C   . TRP   C 1 83 ? 11.003  -22.420 15.045  1.00 34.32  ? 82  TRP   C C   1 
ATOM   2129 O  O   . TRP   C 1 83 ? 10.904  -21.260 15.462  1.00 34.40  ? 82  TRP   C O   1 
ATOM   2130 C  CB  . TRP   C 1 83 ? 9.719   -23.065 12.990  1.00 30.89  ? 82  TRP   C CB  1 
ATOM   2131 C  CG  . TRP   C 1 83 ? 8.717   -21.956 13.130  1.00 34.79  ? 82  TRP   C CG  1 
ATOM   2132 C  CD1 . TRP   C 1 83 ? 8.460   -20.966 12.226  1.00 33.70  ? 82  TRP   C CD1 1 
ATOM   2133 C  CD2 . TRP   C 1 83 ? 7.849   -21.716 14.247  1.00 39.64  ? 82  TRP   C CD2 1 
ATOM   2134 N  NE1 . TRP   C 1 83 ? 7.482   -20.127 12.708  1.00 34.80  ? 82  TRP   C NE1 1 
ATOM   2135 C  CE2 . TRP   C 1 83 ? 7.090   -20.566 13.946  1.00 36.41  ? 82  TRP   C CE2 1 
ATOM   2136 C  CE3 . TRP   C 1 83 ? 7.637   -22.363 15.468  1.00 35.72  ? 82  TRP   C CE3 1 
ATOM   2137 C  CZ2 . TRP   C 1 83 ? 6.138   -20.049 14.823  1.00 46.93  ? 82  TRP   C CZ2 1 
ATOM   2138 C  CZ3 . TRP   C 1 83 ? 6.689   -21.846 16.339  1.00 44.60  ? 82  TRP   C CZ3 1 
ATOM   2139 C  CH2 . TRP   C 1 83 ? 5.952   -20.702 16.011  1.00 41.15  ? 82  TRP   C CH2 1 
ATOM   2140 N  N   . GLU   C 1 84 ? 11.041  -23.472 15.867  1.00 30.20  ? 83  GLU   C N   1 
ATOM   2141 C  CA  . GLU   C 1 84 ? 10.893  -23.297 17.308  1.00 32.61  ? 83  GLU   C CA  1 
ATOM   2142 C  C   . GLU   C 1 84 ? 12.080  -22.554 17.907  1.00 40.04  ? 83  GLU   C C   1 
ATOM   2143 O  O   . GLU   C 1 84 ? 11.900  -21.639 18.718  1.00 38.47  ? 83  GLU   C O   1 
ATOM   2144 C  CB  . GLU   C 1 84 ? 10.717  -24.657 17.987  1.00 36.85  ? 83  GLU   C CB  1 
ATOM   2145 C  CG  . GLU   C 1 84 ? 9.422   -25.367 17.627  1.00 38.13  ? 83  GLU   C CG  1 
ATOM   2146 C  CD  . GLU   C 1 84 ? 9.339   -26.766 18.208  1.00 47.24  ? 83  GLU   C CD  1 
ATOM   2147 O  OE1 . GLU   C 1 84 ? 10.377  -27.279 18.677  1.00 44.42  ? 83  GLU   C OE1 1 
ATOM   2148 O  OE2 . GLU   C 1 84 ? 8.238   -27.356 18.193  1.00 48.33  ? 83  GLU   C OE2 1 
ATOM   2149 N  N   . ILE   C 1 85 ? 13.302  -22.921 17.514  1.00 37.14  ? 84  ILE   C N   1 
ATOM   2150 C  CA  . ILE   C 1 85 ? 14.473  -22.326 18.149  1.00 39.97  ? 84  ILE   C CA  1 
ATOM   2151 C  C   . ILE   C 1 85 ? 14.590  -20.847 17.804  1.00 43.02  ? 84  ILE   C C   1 
ATOM   2152 O  O   . ILE   C 1 85 ? 15.168  -20.067 18.570  1.00 41.82  ? 84  ILE   C O   1 
ATOM   2153 C  CB  . ILE   C 1 85 ? 15.746  -23.103 17.767  1.00 41.18  ? 84  ILE   C CB  1 
ATOM   2154 C  CG1 . ILE   C 1 85 ? 16.898  -22.744 18.711  1.00 37.01  ? 84  ILE   C CG1 1 
ATOM   2155 C  CG2 . ILE   C 1 85 ? 16.137  -22.841 16.319  1.00 35.99  ? 84  ILE   C CG2 1 
ATOM   2156 C  CD1 . ILE   C 1 85 ? 18.071  -23.697 18.624  1.00 33.86  ? 84  ILE   C CD1 1 
ATOM   2157 N  N   . GLN   C 1 86 ? 14.032  -20.429 16.668  1.00 32.20  ? 85  GLN   C N   1 
ATOM   2158 C  CA  . GLN   C 1 86 ? 14.101  -19.034 16.255  1.00 38.26  ? 85  GLN   C CA  1 
ATOM   2159 C  C   . GLN   C 1 86 ? 12.899  -18.221 16.717  1.00 41.33  ? 85  GLN   C C   1 
ATOM   2160 O  O   . GLN   C 1 86 ? 13.032  -17.014 16.951  1.00 37.46  ? 85  GLN   C O   1 
ATOM   2161 C  CB  . GLN   C 1 86 ? 14.226  -18.949 14.731  1.00 35.55  ? 85  GLN   C CB  1 
ATOM   2162 C  CG  . GLN   C 1 86 ? 14.453  -17.542 14.193  1.00 32.26  ? 85  GLN   C CG  1 
ATOM   2163 C  CD  . GLN   C 1 86 ? 14.762  -17.531 12.709  1.00 38.67  ? 85  GLN   C CD  1 
ATOM   2164 O  OE1 . GLN   C 1 86 ? 14.643  -18.553 12.031  1.00 37.26  ? 85  GLN   C OE1 1 
ATOM   2165 N  NE2 . GLN   C 1 86 ? 15.166  -16.371 12.196  1.00 38.83  ? 85  GLN   C NE2 1 
ATOM   2166 N  N   . ASN   C 1 87 ? 11.736  -18.854 16.871  1.00 32.54  ? 86  ASN   C N   1 
ATOM   2167 C  CA  . ASN   C 1 87 ? 10.496  -18.135 17.118  1.00 45.32  ? 86  ASN   C CA  1 
ATOM   2168 C  C   . ASN   C 1 87 ? 9.830   -18.444 18.451  1.00 42.24  ? 86  ASN   C C   1 
ATOM   2169 O  O   . ASN   C 1 87 ? 9.067   -17.602 18.937  1.00 43.19  ? 86  ASN   C O   1 
ATOM   2170 C  CB  . ASN   C 1 87 ? 9.490   -18.408 15.989  1.00 40.44  ? 86  ASN   C CB  1 
ATOM   2171 C  CG  . ASN   C 1 87 ? 9.959   -17.864 14.658  1.00 43.37  ? 86  ASN   C CG  1 
ATOM   2172 O  OD1 . ASN   C 1 87 ? 9.951   -16.654 14.435  1.00 45.89  ? 86  ASN   C OD1 1 
ATOM   2173 N  ND2 . ASN   C 1 87 ? 10.385  -18.754 13.770  1.00 34.69  ? 86  ASN   C ND2 1 
ATOM   2174 N  N   . ASN   C 1 88 ? 10.074  -19.608 19.050  1.00 43.04  ? 87  ASN   C N   1 
ATOM   2175 C  CA  . ASN   C 1 88 ? 9.465   -19.887 20.348  1.00 34.70  ? 87  ASN   C CA  1 
ATOM   2176 C  C   . ASN   C 1 88 ? 10.294  -20.897 21.138  1.00 46.85  ? 87  ASN   C C   1 
ATOM   2177 O  O   . ASN   C 1 88 ? 9.841   -22.023 21.380  1.00 47.02  ? 87  ASN   C O   1 
ATOM   2178 C  CB  . ASN   C 1 88 ? 8.037   -20.398 20.167  1.00 46.63  ? 87  ASN   C CB  1 
ATOM   2179 C  CG  . ASN   C 1 88 ? 7.248   -20.384 21.463  1.00 49.43  ? 87  ASN   C CG  1 
ATOM   2180 O  OD1 . ASN   C 1 88 ? 7.654   -19.751 22.438  1.00 53.85  ? 87  ASN   C OD1 1 
ATOM   2181 N  ND2 . ASN   C 1 88 ? 6.123   -21.090 21.485  1.00 57.54  ? 87  ASN   C ND2 1 
ATOM   2182 N  N   . PRO   C 1 89 ? 11.505  -20.537 21.568  1.00 39.81  ? 88  PRO   C N   1 
ATOM   2183 C  CA  . PRO   C 1 89 ? 12.427  -21.547 22.097  1.00 47.28  ? 88  PRO   C CA  1 
ATOM   2184 C  C   . PRO   C 1 89 ? 12.234  -21.900 23.563  1.00 53.00  ? 88  PRO   C C   1 
ATOM   2185 O  O   . PRO   C 1 89 ? 13.042  -22.669 24.092  1.00 51.35  ? 88  PRO   C O   1 
ATOM   2186 C  CB  . PRO   C 1 89 ? 13.795  -20.895 21.874  1.00 43.37  ? 88  PRO   C CB  1 
ATOM   2187 C  CG  . PRO   C 1 89 ? 13.523  -19.441 22.013  1.00 55.71  ? 88  PRO   C CG  1 
ATOM   2188 C  CD  . PRO   C 1 89 ? 12.148  -19.216 21.441  1.00 38.54  ? 88  PRO   C CD  1 
ATOM   2189 N  N   . HIS   C 1 90 ? 11.205  -21.383 24.245  1.00 54.70  ? 89  HIS   C N   1 
ATOM   2190 C  CA  . HIS   C 1 90 ? 11.048  -21.643 25.673  1.00 51.33  ? 89  HIS   C CA  1 
ATOM   2191 C  C   . HIS   C 1 90 ? 9.627   -22.058 26.037  1.00 54.26  ? 89  HIS   C C   1 
ATOM   2192 O  O   . HIS   C 1 90 ? 9.216   -21.896 27.192  1.00 59.71  ? 89  HIS   C O   1 
ATOM   2193 C  CB  . HIS   C 1 90 ? 11.474  -20.424 26.493  1.00 41.86  ? 89  HIS   C CB  1 
ATOM   2194 C  CG  . HIS   C 1 90 ? 12.909  -20.040 26.301  1.00 42.89  ? 89  HIS   C CG  1 
ATOM   2195 N  ND1 . HIS   C 1 90 ? 13.293  -18.852 25.717  1.00 57.89  ? 89  HIS   C ND1 1 
ATOM   2196 C  CD2 . HIS   C 1 90 ? 14.055  -20.694 26.608  1.00 47.52  ? 89  HIS   C CD2 1 
ATOM   2197 C  CE1 . HIS   C 1 90 ? 14.612  -18.787 25.679  1.00 48.27  ? 89  HIS   C CE1 1 
ATOM   2198 N  NE2 . HIS   C 1 90 ? 15.099  -19.893 26.213  1.00 49.23  ? 89  HIS   C NE2 1 
ATOM   2199 N  N   . ALA   C 1 91 ? 8.866   -22.585 25.083  1.00 54.83  ? 90  ALA   C N   1 
ATOM   2200 C  CA  . ALA   C 1 91 ? 7.564   -23.141 25.403  1.00 68.53  ? 90  ALA   C CA  1 
ATOM   2201 C  C   . ALA   C 1 91 ? 7.724   -24.518 26.047  1.00 73.49  ? 90  ALA   C C   1 
ATOM   2202 O  O   . ALA   C 1 91 ? 8.801   -25.120 26.039  1.00 75.60  ? 90  ALA   C O   1 
ATOM   2203 C  CB  . ALA   C 1 91 ? 6.691   -23.226 24.152  1.00 68.26  ? 90  ALA   C CB  1 
ATOM   2204 N  N   . SER   C 1 92 ? 6.626   -25.019 26.617  1.00 68.75  ? 91  SER   C N   1 
ATOM   2205 C  CA  . SER   C 1 92 ? 6.680   -26.302 27.312  1.00 78.76  ? 91  SER   C CA  1 
ATOM   2206 C  C   . SER   C 1 92 ? 6.763   -27.466 26.331  1.00 73.85  ? 91  SER   C C   1 
ATOM   2207 O  O   . SER   C 1 92 ? 7.481   -28.442 26.581  1.00 74.75  ? 91  SER   C O   1 
ATOM   2208 C  CB  . SER   C 1 92 ? 5.465   -26.455 28.227  1.00 76.18  ? 91  SER   C CB  1 
ATOM   2209 O  OG  . SER   C 1 92 ? 5.488   -25.496 29.269  1.00 73.77  ? 91  SER   C OG  1 
ATOM   2210 N  N   . TYR   C 1 93 ? 6.038   -27.379 25.218  1.00 74.18  ? 92  TYR   C N   1 
ATOM   2211 C  CA  . TYR   C 1 93 ? 5.994   -28.437 24.207  1.00 75.24  ? 92  TYR   C CA  1 
ATOM   2212 C  C   . TYR   C 1 93 ? 5.631   -29.791 24.810  1.00 78.49  ? 92  TYR   C C   1 
ATOM   2213 O  O   . TYR   C 1 93 ? 6.427   -30.730 24.775  1.00 75.58  ? 92  TYR   C O   1 
ATOM   2214 C  CB  . TYR   C 1 93 ? 7.333   -28.537 23.468  1.00 71.05  ? 92  TYR   C CB  1 
ATOM   2215 C  CG  . TYR   C 1 93 ? 7.713   -27.282 22.716  1.00 66.54  ? 92  TYR   C CG  1 
ATOM   2216 C  CD1 . TYR   C 1 93 ? 7.073   -26.939 21.532  1.00 57.31  ? 92  TYR   C CD1 1 
ATOM   2217 C  CD2 . TYR   C 1 93 ? 8.714   -26.443 23.188  1.00 60.81  ? 92  TYR   C CD2 1 
ATOM   2218 C  CE1 . TYR   C 1 93 ? 7.417   -25.793 20.840  1.00 57.43  ? 92  TYR   C CE1 1 
ATOM   2219 C  CE2 . TYR   C 1 93 ? 9.065   -25.295 22.502  1.00 60.88  ? 92  TYR   C CE2 1 
ATOM   2220 C  CZ  . TYR   C 1 93 ? 8.413   -24.975 21.329  1.00 55.61  ? 92  TYR   C CZ  1 
ATOM   2221 O  OH  . TYR   C 1 93 ? 8.759   -23.833 20.642  1.00 55.88  ? 92  TYR   C OH  1 
HETATM 2222 S  S   . DMS   D 2 .  ? 2.503   -24.754 -2.809  1.00 56.34  ? 101 DMS   A S   1 
HETATM 2223 O  O   . DMS   D 2 .  ? 3.776   -25.152 -3.521  1.00 45.07  ? 101 DMS   A O   1 
HETATM 2224 C  C1  . DMS   D 2 .  ? 2.107   -26.115 -1.697  1.00 51.98  ? 101 DMS   A C1  1 
HETATM 2225 C  C2  . DMS   D 2 .  ? 1.154   -25.028 -3.981  1.00 54.30  ? 101 DMS   A C2  1 
HETATM 2226 S  S   . SO4   E 3 .  ? 8.594   -29.569 5.719   0.68 36.02  ? 102 SO4   A S   1 
HETATM 2227 O  O1  . SO4   E 3 .  ? 8.193   -30.703 4.823   0.68 31.77  ? 102 SO4   A O1  1 
HETATM 2228 O  O2  . SO4   E 3 .  ? 9.292   -28.522 4.913   0.68 33.19  ? 102 SO4   A O2  1 
HETATM 2229 O  O3  . SO4   E 3 .  ? 7.369   -28.990 6.365   0.68 36.10  ? 102 SO4   A O3  1 
HETATM 2230 O  O4  . SO4   E 3 .  ? 9.532   -30.074 6.771   0.68 36.61  ? 102 SO4   A O4  1 
HETATM 2231 S  S   . SO4   F 3 .  ? 1.160   -33.607 1.610   1.00 66.68  ? 103 SO4   A S   1 
HETATM 2232 O  O1  . SO4   F 3 .  ? 2.157   -34.162 0.642   1.00 47.51  ? 103 SO4   A O1  1 
HETATM 2233 O  O2  . SO4   F 3 .  ? 1.567   -32.221 2.007   1.00 47.26  ? 103 SO4   A O2  1 
HETATM 2234 O  O3  . SO4   F 3 .  ? -0.193  -33.566 0.964   1.00 69.24  ? 103 SO4   A O3  1 
HETATM 2235 O  O4  . SO4   F 3 .  ? 1.108   -34.479 2.829   1.00 67.42  ? 103 SO4   A O4  1 
HETATM 2236 C  C4  . A1H6Y G 4 .  ? 21.007  -15.075 -23.959 0.81 40.63  ? 101 A1H6Y B C4  1 
HETATM 2237 C  C5  . A1H6Y G 4 .  ? 21.056  -15.426 -22.626 0.81 54.08  ? 101 A1H6Y B C5  1 
HETATM 2238 C  C6  . A1H6Y G 4 .  ? 19.914  -15.507 -21.857 0.81 46.09  ? 101 A1H6Y B C6  1 
HETATM 2239 C  C7  . A1H6Y G 4 .  ? 18.688  -15.231 -22.435 0.81 41.24  ? 101 A1H6Y B C7  1 
HETATM 2240 C  C3  . A1H6Y G 4 .  ? 19.784  -14.798 -24.541 0.81 40.24  ? 101 A1H6Y B C3  1 
HETATM 2241 C  C1  . A1H6Y G 4 .  ? 16.768  -15.889 -25.576 0.81 37.13  ? 101 A1H6Y B C1  1 
HETATM 2242 S  S1  . A1H6Y G 4 .  ? 17.068  -14.525 -24.516 0.81 35.26  ? 101 A1H6Y B S1  1 
HETATM 2243 O  O1  . A1H6Y G 4 .  ? 16.073  -14.520 -23.482 0.81 38.48  ? 101 A1H6Y B O1  1 
HETATM 2244 O  O2  . A1H6Y G 4 .  ? 17.210  -13.344 -25.321 0.81 34.41  ? 101 A1H6Y B O2  1 
HETATM 2245 C  C2  . A1H6Y G 4 .  ? 18.634  -14.878 -23.774 0.81 34.14  ? 101 A1H6Y B C2  1 
HETATM 2246 BR BR1 . A1H6Y G 4 .  ? 22.737  -15.807 -21.830 0.81 133.05 ? 101 A1H6Y B BR1 1 
HETATM 2247 S  S   . SO4   H 3 .  ? 7.257   -8.435  -24.590 1.00 57.29  ? 102 SO4   B S   1 
HETATM 2248 O  O1  . SO4   H 3 .  ? 8.409   -8.377  -25.547 1.00 41.17  ? 102 SO4   B O1  1 
HETATM 2249 O  O2  . SO4   H 3 .  ? 6.134   -9.201  -25.218 1.00 49.23  ? 102 SO4   B O2  1 
HETATM 2250 O  O3  . SO4   H 3 .  ? 7.681   -9.112  -23.318 1.00 45.11  ? 102 SO4   B O3  1 
HETATM 2251 O  O4  . SO4   H 3 .  ? 6.805   -7.039  -24.286 1.00 67.82  ? 102 SO4   B O4  1 
HETATM 2252 S  S   . SO4   I 3 .  ? 14.473  -26.674 -26.540 0.77 53.21  ? 103 SO4   B S   1 
HETATM 2253 O  O1  . SO4   I 3 .  ? 15.928  -26.323 -26.536 0.77 47.61  ? 103 SO4   B O1  1 
HETATM 2254 O  O2  . SO4   I 3 .  ? 13.834  -26.172 -27.797 0.77 55.12  ? 103 SO4   B O2  1 
HETATM 2255 O  O3  . SO4   I 3 .  ? 14.331  -28.165 -26.464 0.77 68.48  ? 103 SO4   B O3  1 
HETATM 2256 O  O4  . SO4   I 3 .  ? 13.802  -26.055 -25.351 0.77 52.80  ? 103 SO4   B O4  1 
HETATM 2257 S  S   . SO4   J 3 .  ? 7.010   -23.362 -24.191 1.00 73.15  ? 104 SO4   B S   1 
HETATM 2258 O  O1  . SO4   J 3 .  ? 8.073   -24.174 -23.519 1.00 67.78  ? 104 SO4   B O1  1 
HETATM 2259 O  O2  . SO4   J 3 .  ? 6.274   -24.212 -25.182 1.00 67.32  ? 104 SO4   B O2  1 
HETATM 2260 O  O3  . SO4   J 3 .  ? 6.050   -22.855 -23.157 1.00 63.28  ? 104 SO4   B O3  1 
HETATM 2261 O  O4  . SO4   J 3 .  ? 7.664   -22.219 -24.908 1.00 67.42  ? 104 SO4   B O4  1 
HETATM 2262 S  S   . DMS   K 2 .  ? 16.548  -35.675 17.400  1.00 44.78  ? 601 DMS   C S   1 
HETATM 2263 O  O   . DMS   K 2 .  ? 15.456  -35.932 18.410  1.00 48.43  ? 601 DMS   C O   1 
HETATM 2264 C  C1  . DMS   K 2 .  ? 16.133  -36.649 15.944  1.00 46.81  ? 601 DMS   C C1  1 
HETATM 2265 C  C2  . DMS   K 2 .  ? 17.987  -36.631 17.921  1.00 53.80  ? 601 DMS   C C2  1 
HETATM 2266 S  S   . SO4   L 3 .  ? 14.831  -39.425 10.762  1.00 80.05  ? 602 SO4   C S   1 
HETATM 2267 O  O1  . SO4   L 3 .  ? 14.247  -40.252 9.658   1.00 83.75  ? 602 SO4   C O1  1 
HETATM 2268 O  O2  . SO4   L 3 .  ? 15.481  -38.211 10.180  1.00 69.91  ? 602 SO4   C O2  1 
HETATM 2269 O  O3  . SO4   L 3 .  ? 13.739  -39.008 11.701  1.00 69.80  ? 602 SO4   C O3  1 
HETATM 2270 O  O4  . SO4   L 3 .  ? 15.854  -40.228 11.507  1.00 80.94  ? 602 SO4   C O4  1 
HETATM 2271 O  O   . HOH   M 5 .  ? -0.165  -33.632 4.692   1.00 49.26  ? 201 HOH   A O   1 
HETATM 2272 O  O   . HOH   M 5 .  ? 16.362  -16.476 -19.157 1.00 49.08  ? 202 HOH   A O   1 
HETATM 2273 O  O   . HOH   M 5 .  ? 9.333   -22.412 -9.459  1.00 33.13  ? 203 HOH   A O   1 
HETATM 2274 O  O   . HOH   M 5 .  ? -7.625  -16.840 6.808   1.00 51.75  ? 204 HOH   A O   1 
HETATM 2275 O  O   . HOH   M 5 .  ? 19.870  -15.700 7.041   1.00 30.53  ? 205 HOH   A O   1 
HETATM 2276 O  O   . HOH   M 5 .  ? -4.361  -20.969 6.305   1.00 41.07  ? 206 HOH   A O   1 
HETATM 2277 O  O   . HOH   M 5 .  ? 13.016  -12.051 8.030   1.00 43.01  ? 207 HOH   A O   1 
HETATM 2278 O  O   . HOH   M 5 .  ? 4.421   -3.531  -3.219  1.00 35.65  ? 208 HOH   A O   1 
HETATM 2279 O  O   . HOH   M 5 .  ? 1.843   -4.503  -9.983  1.00 40.84  ? 209 HOH   A O   1 
HETATM 2280 O  O   . HOH   M 5 .  ? 15.052  -18.796 -7.244  1.00 44.61  ? 210 HOH   A O   1 
HETATM 2281 O  O   . HOH   M 5 .  ? 15.782  -24.572 1.731   1.00 34.81  ? 211 HOH   A O   1 
HETATM 2282 O  O   . HOH   M 5 .  ? 6.776   -18.066 10.807  1.00 44.42  ? 212 HOH   A O   1 
HETATM 2283 O  O   . HOH   M 5 .  ? 1.130   -17.656 -18.684 1.00 47.11  ? 213 HOH   A O   1 
HETATM 2284 O  O   . HOH   M 5 .  ? -4.893  -25.447 -5.522  1.00 44.78  ? 214 HOH   A O   1 
HETATM 2285 O  O   . HOH   M 5 .  ? 7.215   -10.372 -11.993 1.00 33.02  ? 215 HOH   A O   1 
HETATM 2286 O  O   . HOH   M 5 .  ? 12.506  -18.286 -8.277  1.00 39.79  ? 216 HOH   A O   1 
HETATM 2287 O  O   . HOH   M 5 .  ? 10.718  -5.016  -7.558  1.00 37.26  ? 217 HOH   A O   1 
HETATM 2288 O  O   . HOH   M 5 .  ? 8.894   -18.007 -11.146 1.00 37.03  ? 218 HOH   A O   1 
HETATM 2289 O  O   . HOH   M 5 .  ? -0.624  -20.876 7.120   1.00 29.52  ? 219 HOH   A O   1 
HETATM 2290 O  O   . HOH   M 5 .  ? 9.680   -5.836  -1.502  1.00 37.17  ? 220 HOH   A O   1 
HETATM 2291 O  O   . HOH   M 5 .  ? 8.750   -8.966  -13.639 1.00 39.05  ? 221 HOH   A O   1 
HETATM 2292 O  O   . HOH   M 5 .  ? -6.131  -11.388 -11.165 1.00 40.47  ? 222 HOH   A O   1 
HETATM 2293 O  O   . HOH   M 5 .  ? -1.779  -21.768 -0.436  1.00 29.08  ? 223 HOH   A O   1 
HETATM 2294 O  O   . HOH   M 5 .  ? 11.656  -11.973 5.958   1.00 33.28  ? 224 HOH   A O   1 
HETATM 2295 O  O   . HOH   M 5 .  ? 0.592   -10.175 -15.681 1.00 48.78  ? 225 HOH   A O   1 
HETATM 2296 O  O   . HOH   M 5 .  ? -5.642  -19.394 -5.735  1.00 40.72  ? 226 HOH   A O   1 
HETATM 2297 O  O   . HOH   M 5 .  ? 3.644   -16.802 13.748  1.00 53.26  ? 227 HOH   A O   1 
HETATM 2298 O  O   . HOH   M 5 .  ? 8.693   -17.774 -15.965 1.00 53.95  ? 228 HOH   A O   1 
HETATM 2299 O  O   . HOH   M 5 .  ? 2.109   -1.738  -0.358  1.00 45.34  ? 229 HOH   A O   1 
HETATM 2300 O  O   . HOH   M 5 .  ? -5.708  -15.697 -8.060  1.00 31.60  ? 230 HOH   A O   1 
HETATM 2301 O  O   . HOH   M 5 .  ? 8.077   -7.796  1.212   1.00 33.89  ? 231 HOH   A O   1 
HETATM 2302 O  O   . HOH   M 5 .  ? 4.627   -7.656  0.971   1.00 34.45  ? 232 HOH   A O   1 
HETATM 2303 O  O   . HOH   M 5 .  ? 17.253  -12.970 1.239   1.00 24.67  ? 233 HOH   A O   1 
HETATM 2304 O  O   . HOH   M 5 .  ? -8.370  -21.104 -1.178  1.00 37.26  ? 234 HOH   A O   1 
HETATM 2305 O  O   . HOH   M 5 .  ? 11.567  -12.366 -6.183  1.00 34.94  ? 235 HOH   A O   1 
HETATM 2306 O  O   . HOH   M 5 .  ? 10.350  -12.957 9.535   1.00 50.97  ? 236 HOH   A O   1 
HETATM 2307 O  O   . HOH   M 5 .  ? 13.191  -11.922 -4.371  1.00 26.30  ? 237 HOH   A O   1 
HETATM 2308 O  O   . HOH   M 5 .  ? 9.812   -30.375 9.591   1.00 41.48  ? 238 HOH   A O   1 
HETATM 2309 O  O   . HOH   M 5 .  ? -2.693  3.667   -2.098  1.00 43.55  ? 239 HOH   A O   1 
HETATM 2310 O  O   . HOH   M 5 .  ? 12.756  -13.754 -8.929  1.00 51.82  ? 240 HOH   A O   1 
HETATM 2311 O  O   . HOH   M 5 .  ? -0.973  -11.527 11.827  1.00 38.03  ? 241 HOH   A O   1 
HETATM 2312 O  O   . HOH   M 5 .  ? 16.855  -12.289 -16.930 1.00 47.70  ? 242 HOH   A O   1 
HETATM 2313 O  O   . HOH   M 5 .  ? 8.153   -17.465 8.864   1.00 42.51  ? 243 HOH   A O   1 
HETATM 2314 O  O   . HOH   M 5 .  ? 11.310  -6.021  -3.694  1.00 38.68  ? 244 HOH   A O   1 
HETATM 2315 O  O   . HOH   M 5 .  ? 6.499   -24.781 -10.683 1.00 33.87  ? 245 HOH   A O   1 
HETATM 2316 O  O   . HOH   M 5 .  ? 0.166   -22.800 9.376   1.00 43.92  ? 246 HOH   A O   1 
HETATM 2317 O  O   . HOH   M 5 .  ? 2.431   -25.019 -9.958  1.00 30.92  ? 247 HOH   A O   1 
HETATM 2318 O  O   . HOH   M 5 .  ? 15.749  -12.039 -5.533  1.00 46.30  ? 248 HOH   A O   1 
HETATM 2319 O  O   . HOH   M 5 .  ? 11.512  -16.492 -14.775 1.00 41.55  ? 249 HOH   A O   1 
HETATM 2320 O  O   . HOH   M 5 .  ? 23.038  -16.726 1.050   1.00 48.10  ? 250 HOH   A O   1 
HETATM 2321 O  O   . HOH   M 5 .  ? 8.788   -16.249 -13.155 1.00 34.32  ? 251 HOH   A O   1 
HETATM 2322 O  O   . HOH   M 5 .  ? -7.921  -15.605 -0.757  1.00 38.33  ? 252 HOH   A O   1 
HETATM 2323 O  O   . HOH   M 5 .  ? 5.648   -8.294  4.046   1.00 35.53  ? 253 HOH   A O   1 
HETATM 2324 O  O   . HOH   M 5 .  ? -5.390  -17.363 -10.185 1.00 55.50  ? 254 HOH   A O   1 
HETATM 2325 O  O   . HOH   M 5 .  ? 6.828   -5.875  0.621   1.00 41.61  ? 255 HOH   A O   1 
HETATM 2326 O  O   . HOH   M 5 .  ? -7.133  -11.200 -7.879  1.00 34.18  ? 256 HOH   A O   1 
HETATM 2327 O  O   . HOH   M 5 .  ? 12.619  -15.745 -11.847 1.00 50.70  ? 257 HOH   A O   1 
HETATM 2328 O  O   . HOH   M 5 .  ? 9.631   -20.166 -18.341 1.00 48.53  ? 258 HOH   A O   1 
HETATM 2329 O  O   . HOH   M 5 .  ? 2.053   -10.373 12.107  1.00 42.13  ? 259 HOH   A O   1 
HETATM 2330 O  O   . HOH   M 5 .  ? -5.748  -12.388 6.956   1.00 46.37  ? 260 HOH   A O   1 
HETATM 2331 O  O   . HOH   M 5 .  ? -8.012  -16.529 1.812   1.00 44.70  ? 261 HOH   A O   1 
HETATM 2332 O  O   . HOH   M 5 .  ? 11.115  -7.836  0.437   1.00 27.60  ? 262 HOH   A O   1 
HETATM 2333 O  O   . HOH   M 5 .  ? 21.167  -16.741 -3.131  1.00 32.64  ? 263 HOH   A O   1 
HETATM 2334 O  O   . HOH   M 5 .  ? -8.022  -19.353 -3.157  1.00 48.51  ? 264 HOH   A O   1 
HETATM 2335 O  O   . HOH   M 5 .  ? -0.636  -20.729 10.797  1.00 59.02  ? 265 HOH   A O   1 
HETATM 2336 O  O   . HOH   M 5 .  ? -3.814  -8.025  10.795  1.00 57.19  ? 266 HOH   A O   1 
HETATM 2337 O  O   . HOH   M 5 .  ? -0.520  -27.552 11.442  1.00 58.43  ? 267 HOH   A O   1 
HETATM 2338 O  O   . HOH   M 5 .  ? 10.220  -27.578 -7.538  1.00 46.04  ? 268 HOH   A O   1 
HETATM 2339 O  O   . HOH   M 5 .  ? 7.939   -30.178 -0.940  1.00 55.58  ? 269 HOH   A O   1 
HETATM 2340 O  O   . HOH   M 5 .  ? -1.911  -6.777  11.272  1.00 55.62  ? 270 HOH   A O   1 
HETATM 2341 O  O   . HOH   M 5 .  ? -10.668 -16.317 -2.895  1.00 49.61  ? 271 HOH   A O   1 
HETATM 2342 O  O   . HOH   M 5 .  ? -6.073  -26.310 3.470   1.00 45.22  ? 272 HOH   A O   1 
HETATM 2343 O  O   . HOH   M 5 .  ? -4.535  -19.891 9.888   1.00 44.85  ? 273 HOH   A O   1 
HETATM 2344 O  O   . HOH   M 5 .  ? -7.184  -13.855 -9.243  1.00 42.05  ? 274 HOH   A O   1 
HETATM 2345 O  O   . HOH   M 5 .  ? 12.021  -21.193 10.578  1.00 34.67  ? 275 HOH   A O   1 
HETATM 2346 O  O   . HOH   M 5 .  ? -7.737  -11.236 7.448   1.00 43.84  ? 276 HOH   A O   1 
HETATM 2347 O  O   . HOH   M 5 .  ? -9.364  -19.035 1.541   1.00 52.53  ? 277 HOH   A O   1 
HETATM 2348 O  O   . HOH   M 5 .  ? 5.018   -6.841  -11.264 1.00 41.34  ? 278 HOH   A O   1 
HETATM 2349 O  O   . HOH   M 5 .  ? 11.681  -20.877 -9.949  1.00 44.08  ? 279 HOH   A O   1 
HETATM 2350 O  O   . HOH   M 5 .  ? 5.068   -9.382  -11.393 1.00 47.08  ? 280 HOH   A O   1 
HETATM 2351 O  O   . HOH   M 5 .  ? -6.184  -22.736 5.968   1.00 47.64  ? 281 HOH   A O   1 
HETATM 2352 O  O   . HOH   M 5 .  ? -6.682  -19.133 8.618   1.00 55.63  ? 282 HOH   A O   1 
HETATM 2353 O  O   . HOH   M 5 .  ? -9.728  -15.032 -10.264 1.00 58.06  ? 283 HOH   A O   1 
HETATM 2354 O  O   . HOH   M 5 .  ? 8.361   -8.092  4.507   1.00 35.53  ? 284 HOH   A O   1 
HETATM 2355 O  O   . HOH   M 5 .  ? 12.849  -18.552 -15.298 1.00 47.76  ? 285 HOH   A O   1 
HETATM 2356 O  O   . HOH   M 5 .  ? 9.600   -3.184  -9.303  1.00 44.13  ? 286 HOH   A O   1 
HETATM 2357 O  O   . HOH   N 5 .  ? 31.831  -20.711 -38.132 1.00 47.32  ? 201 HOH   B O   1 
HETATM 2358 O  O   . HOH   N 5 .  ? 17.442  -8.983  -43.455 1.00 40.21  ? 202 HOH   B O   1 
HETATM 2359 O  O   . HOH   N 5 .  ? 44.289  -12.979 -27.117 1.00 67.95  ? 203 HOH   B O   1 
HETATM 2360 O  O   . HOH   N 5 .  ? 13.101  -25.735 -37.188 1.00 38.95  ? 204 HOH   B O   1 
HETATM 2361 O  O   . HOH   N 5 .  ? 4.005   -22.491 -22.005 1.00 54.77  ? 205 HOH   B O   1 
HETATM 2362 O  O   . HOH   N 5 .  ? 20.899  -25.181 -30.155 1.00 52.30  ? 206 HOH   B O   1 
HETATM 2363 O  O   . HOH   N 5 .  ? 30.548  -19.117 -40.175 1.00 37.58  ? 207 HOH   B O   1 
HETATM 2364 O  O   . HOH   N 5 .  ? 26.057  -22.641 -30.957 1.00 35.39  ? 208 HOH   B O   1 
HETATM 2365 O  O   . HOH   N 5 .  ? 24.288  -1.321  -35.954 1.00 40.55  ? 209 HOH   B O   1 
HETATM 2366 O  O   . HOH   N 5 .  ? 27.769  -7.902  -28.748 1.00 47.99  ? 210 HOH   B O   1 
HETATM 2367 O  O   . HOH   N 5 .  ? 34.298  -22.950 -29.917 1.00 51.02  ? 211 HOH   B O   1 
HETATM 2368 O  O   . HOH   N 5 .  ? 6.423   -12.042 -25.870 1.00 45.09  ? 212 HOH   B O   1 
HETATM 2369 O  O   . HOH   N 5 .  ? 10.424  -18.426 -32.699 1.00 27.83  ? 213 HOH   B O   1 
HETATM 2370 O  O   . HOH   N 5 .  ? 12.686  -4.246  -41.628 1.00 45.46  ? 214 HOH   B O   1 
HETATM 2371 O  O   . HOH   N 5 .  ? 31.377  -11.644 -38.569 1.00 48.42  ? 215 HOH   B O   1 
HETATM 2372 O  O   . HOH   N 5 .  ? 17.531  -0.313  -25.100 1.00 52.47  ? 216 HOH   B O   1 
HETATM 2373 O  O   . HOH   N 5 .  ? 23.247  -5.507  -24.550 1.00 39.96  ? 217 HOH   B O   1 
HETATM 2374 O  O   . HOH   N 5 .  ? 8.364   -21.042 -27.250 1.00 42.94  ? 218 HOH   B O   1 
HETATM 2375 O  O   . HOH   N 5 .  ? 14.681  -23.445 -40.467 1.00 39.90  ? 219 HOH   B O   1 
HETATM 2376 O  O   . HOH   N 5 .  ? 16.984  -18.923 -28.596 1.00 27.92  ? 220 HOH   B O   1 
HETATM 2377 O  O   . HOH   N 5 .  ? 24.897  -4.550  -29.525 1.00 38.28  ? 221 HOH   B O   1 
HETATM 2378 O  O   . HOH   N 5 .  ? 12.828  -21.349 -46.248 1.00 46.44  ? 222 HOH   B O   1 
HETATM 2379 O  O   . HOH   N 5 .  ? 20.064  -25.356 -34.098 1.00 39.05  ? 223 HOH   B O   1 
HETATM 2380 O  O   . HOH   N 5 .  ? 31.194  -10.428 -35.882 1.00 51.73  ? 224 HOH   B O   1 
HETATM 2381 O  O   . HOH   N 5 .  ? 22.760  -22.982 -28.637 1.00 39.70  ? 225 HOH   B O   1 
HETATM 2382 O  O   . HOH   N 5 .  ? 26.048  -3.918  -33.248 1.00 45.23  ? 226 HOH   B O   1 
HETATM 2383 O  O   . HOH   N 5 .  ? 14.339  -5.966  -40.804 1.00 35.08  ? 227 HOH   B O   1 
HETATM 2384 O  O   . HOH   N 5 .  ? 27.167  -10.074 -28.538 1.00 45.17  ? 228 HOH   B O   1 
HETATM 2385 O  O   . HOH   N 5 .  ? 16.637  -25.504 -34.492 1.00 41.34  ? 229 HOH   B O   1 
HETATM 2386 O  O   . HOH   N 5 .  ? 23.496  -1.996  -28.893 1.00 40.28  ? 230 HOH   B O   1 
HETATM 2387 O  O   . HOH   N 5 .  ? 10.033  -16.212 -44.157 1.00 51.29  ? 231 HOH   B O   1 
HETATM 2388 O  O   . HOH   N 5 .  ? 17.263  -14.121 -45.196 1.00 48.00  ? 232 HOH   B O   1 
HETATM 2389 O  O   . HOH   N 5 .  ? 23.478  -11.175 -21.671 1.00 45.10  ? 233 HOH   B O   1 
HETATM 2390 O  O   . HOH   N 5 .  ? 8.911   -8.763  -16.223 1.00 39.31  ? 234 HOH   B O   1 
HETATM 2391 O  O   . HOH   N 5 .  ? 23.677  -3.858  -36.411 1.00 29.69  ? 235 HOH   B O   1 
HETATM 2392 O  O   . HOH   N 5 .  ? 21.209  -6.053  -42.254 1.00 34.44  ? 236 HOH   B O   1 
HETATM 2393 O  O   . HOH   N 5 .  ? 18.193  -0.117  -38.149 1.00 29.48  ? 237 HOH   B O   1 
HETATM 2394 O  O   . HOH   N 5 .  ? 20.746  -9.730  -42.728 1.00 39.75  ? 238 HOH   B O   1 
HETATM 2395 O  O   . HOH   N 5 .  ? 25.225  -5.365  -35.436 1.00 40.86  ? 239 HOH   B O   1 
HETATM 2396 O  O   . HOH   N 5 .  ? 8.122   -18.418 -31.352 1.00 40.79  ? 240 HOH   B O   1 
HETATM 2397 O  O   . HOH   N 5 .  ? 15.119  -7.824  -42.661 1.00 43.76  ? 241 HOH   B O   1 
HETATM 2398 O  O   . HOH   N 5 .  ? 27.764  -17.181 -24.651 1.00 42.04  ? 242 HOH   B O   1 
HETATM 2399 O  O   . HOH   N 5 .  ? 18.235  -25.711 -29.122 1.00 39.98  ? 243 HOH   B O   1 
HETATM 2400 O  O   . HOH   N 5 .  ? 10.639  -21.428 -32.628 1.00 34.85  ? 244 HOH   B O   1 
HETATM 2401 O  O   . HOH   N 5 .  ? 21.148  -13.457 -42.271 1.00 42.75  ? 245 HOH   B O   1 
HETATM 2402 O  O   . HOH   N 5 .  ? 3.098   -8.695  -25.670 1.00 60.80  ? 246 HOH   B O   1 
HETATM 2403 O  O   . HOH   N 5 .  ? 17.858  -11.649 -42.845 1.00 37.06  ? 247 HOH   B O   1 
HETATM 2404 O  O   . HOH   N 5 .  ? 32.542  -18.408 -42.257 1.00 44.54  ? 248 HOH   B O   1 
HETATM 2405 O  O   . HOH   N 5 .  ? 21.889  -27.711 -32.953 1.00 49.63  ? 249 HOH   B O   1 
HETATM 2406 O  O   . HOH   N 5 .  ? 7.833   -8.133  -20.441 1.00 47.77  ? 250 HOH   B O   1 
HETATM 2407 O  O   . HOH   N 5 .  ? 27.884  -24.416 -35.062 1.00 37.62  ? 251 HOH   B O   1 
HETATM 2408 O  O   . HOH   N 5 .  ? 20.727  4.180   -32.563 1.00 37.50  ? 252 HOH   B O   1 
HETATM 2409 O  O   . HOH   N 5 .  ? 24.894  -6.342  -42.509 1.00 38.51  ? 253 HOH   B O   1 
HETATM 2410 O  O   . HOH   N 5 .  ? 27.969  -24.288 -31.878 1.00 47.00  ? 254 HOH   B O   1 
HETATM 2411 O  O   . HOH   N 5 .  ? 8.604   -27.333 -37.843 1.00 54.36  ? 255 HOH   B O   1 
HETATM 2412 O  O   . HOH   N 5 .  ? 18.638  5.058   -34.259 1.00 51.80  ? 256 HOH   B O   1 
HETATM 2413 O  O   . HOH   N 5 .  ? 15.772  -26.257 -21.383 1.00 54.24  ? 257 HOH   B O   1 
HETATM 2414 O  O   . HOH   N 5 .  ? 12.947  -20.193 -19.664 1.00 52.00  ? 258 HOH   B O   1 
HETATM 2415 O  O   . HOH   N 5 .  ? 18.023  -3.587  -21.519 1.00 48.72  ? 259 HOH   B O   1 
HETATM 2416 O  O   . HOH   N 5 .  ? 7.626   -21.220 -29.699 1.00 37.30  ? 260 HOH   B O   1 
HETATM 2417 O  O   . HOH   N 5 .  ? 19.349  -7.780  -43.620 1.00 40.25  ? 261 HOH   B O   1 
HETATM 2418 O  O   . HOH   N 5 .  ? 24.976  -4.857  -26.713 1.00 51.67  ? 262 HOH   B O   1 
HETATM 2419 O  O   . HOH   N 5 .  ? 7.487   -9.815  -18.331 1.00 45.71  ? 263 HOH   B O   1 
HETATM 2420 O  O   . HOH   N 5 .  ? 18.802  -15.267 -46.500 1.00 49.78  ? 264 HOH   B O   1 
HETATM 2421 O  O   . HOH   O 5 .  ? 25.384  -31.260 10.604  1.00 40.73  ? 701 HOH   C O   1 
HETATM 2422 O  O   . HOH   O 5 .  ? 14.033  -37.388 13.560  1.00 50.09  ? 702 HOH   C O   1 
HETATM 2423 O  O   . HOH   O 5 .  ? 27.869  -37.028 18.709  1.00 43.78  ? 703 HOH   C O   1 
HETATM 2424 O  O   . HOH   O 5 .  ? 15.059  -21.142 12.059  1.00 38.65  ? 704 HOH   C O   1 
HETATM 2425 O  O   . HOH   O 5 .  ? 31.670  -43.206 12.317  1.00 43.64  ? 705 HOH   C O   1 
HETATM 2426 O  O   . HOH   O 5 .  ? 20.724  -28.854 8.285   1.00 44.07  ? 706 HOH   C O   1 
HETATM 2427 O  O   . HOH   O 5 .  ? 19.720  -41.960 12.155  1.00 35.33  ? 707 HOH   C O   1 
HETATM 2428 O  O   . HOH   O 5 .  ? 31.898  -29.964 32.489  1.00 53.83  ? 708 HOH   C O   1 
HETATM 2429 O  O   . HOH   O 5 .  ? 4.618   -29.253 11.698  1.00 44.54  ? 709 HOH   C O   1 
HETATM 2430 O  O   . HOH   O 5 .  ? 12.425  -31.555 8.576   1.00 40.19  ? 710 HOH   C O   1 
HETATM 2431 O  O   . HOH   O 5 .  ? 25.770  -19.850 5.950   1.00 38.73  ? 711 HOH   C O   1 
HETATM 2432 O  O   . HOH   O 5 .  ? 25.833  -17.503 14.034  1.00 51.16  ? 712 HOH   C O   1 
HETATM 2433 O  O   . HOH   O 5 .  ? 22.853  -41.747 18.651  1.00 41.44  ? 713 HOH   C O   1 
HETATM 2434 O  O   . HOH   O 5 .  ? 13.392  -29.650 4.087   1.00 48.17  ? 714 HOH   C O   1 
HETATM 2435 O  O   . HOH   O 5 .  ? 23.389  -20.854 24.044  1.00 45.86  ? 715 HOH   C O   1 
HETATM 2436 O  O   . HOH   O 5 .  ? 18.580  -27.130 2.710   1.00 46.83  ? 716 HOH   C O   1 
HETATM 2437 O  O   . HOH   O 5 .  ? 29.960  -39.979 31.277  1.00 37.18  ? 717 HOH   C O   1 
HETATM 2438 O  O   . HOH   O 5 .  ? 11.206  -23.658 9.851   1.00 31.74  ? 718 HOH   C O   1 
HETATM 2439 O  O   . HOH   O 5 .  ? 21.966  -34.483 16.373  1.00 28.62  ? 719 HOH   C O   1 
HETATM 2440 O  O   . HOH   O 5 .  ? 18.681  -43.471 14.726  1.00 49.35  ? 720 HOH   C O   1 
HETATM 2441 O  O   . HOH   O 5 .  ? 17.793  -21.352 12.589  1.00 48.19  ? 721 HOH   C O   1 
HETATM 2442 O  O   . HOH   O 5 .  ? 22.200  -28.739 10.771  1.00 38.65  ? 722 HOH   C O   1 
HETATM 2443 O  O   . HOH   O 5 .  ? 19.031  -20.462 10.640  1.00 44.83  ? 723 HOH   C O   1 
HETATM 2444 O  O   . HOH   O 5 .  ? 27.950  -37.664 15.930  1.00 47.05  ? 724 HOH   C O   1 
HETATM 2445 O  O   . HOH   O 5 .  ? 15.636  -42.294 8.217   1.00 56.86  ? 725 HOH   C O   1 
HETATM 2446 O  O   . HOH   O 5 .  ? 20.707  -40.180 26.053  1.00 47.66  ? 726 HOH   C O   1 
HETATM 2447 O  O   . HOH   O 5 .  ? 22.929  -18.858 21.710  1.00 53.11  ? 727 HOH   C O   1 
HETATM 2448 O  O   . HOH   O 5 .  ? 21.545  -35.839 7.103   1.00 60.89  ? 728 HOH   C O   1 
HETATM 2449 O  O   . HOH   O 5 .  ? 26.082  -39.467 20.146  1.00 41.25  ? 729 HOH   C O   1 
HETATM 2450 O  O   . HOH   O 5 .  ? 2.612   -28.001 14.957  1.00 52.73  ? 730 HOH   C O   1 
HETATM 2451 O  O   . HOH   O 5 .  ? 18.150  -17.119 15.332  1.00 62.92  ? 731 HOH   C O   1 
HETATM 2452 O  O   . HOH   O 5 .  ? 21.176  -29.547 5.211   1.00 58.87  ? 732 HOH   C O   1 
HETATM 2453 O  O   . HOH   O 5 .  ? 31.466  -39.904 27.096  1.00 42.92  ? 733 HOH   C O   1 
HETATM 2454 O  O   . HOH   O 5 .  ? 25.245  -18.119 21.136  1.00 49.32  ? 734 HOH   C O   1 
HETATM 2455 O  O   . HOH   O 5 .  ? 26.390  -35.888 36.176  1.00 60.84  ? 735 HOH   C O   1 
HETATM 2456 O  O   . HOH   O 5 .  ? 29.364  -39.018 12.159  1.00 48.53  ? 736 HOH   C O   1 
HETATM 2457 O  O   . HOH   O 5 .  ? 16.977  -39.086 21.327  1.00 55.31  ? 737 HOH   C O   1 
HETATM 2458 O  O   . HOH   O 5 .  ? 16.496  -13.608 10.731  1.00 50.39  ? 738 HOH   C O   1 
HETATM 2459 O  O   . HOH   O 5 .  ? 29.407  -40.219 19.200  1.00 50.93  ? 739 HOH   C O   1 
HETATM 2460 O  O   . HOH   O 5 .  ? 32.103  -39.211 29.764  1.00 45.46  ? 740 HOH   C O   1 
HETATM 2461 O  O   . HOH   O 5 .  ? 24.431  -29.217 9.366   1.00 50.05  ? 741 HOH   C O   1 
HETATM 2462 O  O   . HOH   O 5 .  ? 28.241  -14.711 12.972  1.00 50.67  ? 742 HOH   C O   1 
# 
